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***    ***

elNémo ID: 21042314182030268

Job options:

ID        	=	 21042314182030268
JOBID     	=	 
USERID    	=	 unknown
PRIVAT    	=	 0

NMODES    	=	 5
DQMIN     	=	 -100
DQMAX     	=	 100
DQSTEP    	=	 20
DOGRAPHS  	=	 on

DOPROJMODS	=	 on
DORMSD    	=	 on

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


data_1LIO
# 
_entry.id   1LIO 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.286 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   1LIO         
RCSB  RCSB015971   
WWPDB D_1000015971 
# 
_pdbx_database_PDB_obs_spr.id               SPRSDE 
_pdbx_database_PDB_obs_spr.pdb_id           1LIO 
_pdbx_database_PDB_obs_spr.replace_pdb_id   1DH2 
_pdbx_database_PDB_obs_spr.date             2002-06-12 
_pdbx_database_PDB_obs_spr.details          ? 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.details 
_pdbx_database_related.content_type 
PDB 1LII 'STRUCTURE OF T. GONDII ADENOSINE KINASE BOUND TO ADENOSINE 2 AND AMP-PCP'                unspecified 
PDB 1LIJ 'STRUCTURE OF T. GONDII ADENOSINE KINASE BOUND TO PRODRUG 2 7-IODOTUBERCIDIN AND AMP-PCP' unspecified 
PDB 1LIK 'STRUCTURE OF T. GONDII ADENOSINE KINASE BOUND TO ADENOSINE'                              unspecified 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        1LIO 
_pdbx_database_status.recvd_initial_deposition_date   2002-04-17 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        . 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Schumacher, M.A.' 1 
'Scott, D.M.'      2 
'Mathews, I.I.'    3 
'Ealick, S.E.'     4 
'Brennan, R.G.'    5 
# 
_citation.id                        primary 
_citation.title                     
'Crystal structures of Toxoplasma gondii adenosine kinase reveal a novel catalytic mechanism and prodrug binding.' 
_citation.journal_abbrev            J.Mol.Biol. 
_citation.journal_volume            298 
_citation.page_first                875 
_citation.page_last                 893 
_citation.year                      2000 
_citation.journal_id_ASTM           JMOBAK 
_citation.country                   UK 
_citation.journal_id_ISSN           0022-2836 
_citation.journal_id_CSD            0070 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   10801355 
_citation.pdbx_database_id_DOI      10.1006/jmbi.2000.3753 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Schumacher, M.A.' 1 
primary 'Scott, D.M.'      2 
primary 'Mathews, I.I.'    3 
primary 'Ealick, S.E.'     4 
primary 'Roos, D.S.'       5 
primary 'Ullman, B.'       6 
primary 'Brennan, R.G.'    7 
# 
_cell.entry_id           1LIO 
_cell.length_a           47.100 
_cell.length_b           68.000 
_cell.length_c           56.800 
_cell.angle_alpha        90.00 
_cell.angle_beta         100.80 
_cell.angle_gamma        90.00 
_cell.Z_PDB              2 
_cell.pdbx_unique_axis   ? 
_cell.length_a_esd       ? 
_cell.length_b_esd       ? 
_cell.length_c_esd       ? 
_cell.angle_alpha_esd    ? 
_cell.angle_beta_esd     ? 
_cell.angle_gamma_esd    ? 
# 
_symmetry.entry_id                         1LIO 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
# 
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 'adenosine kinase' 38364.730 1   2.7.1.20 ? ? ? 
2 water   nat water              18.015    179 ?        ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
;AK, Adenosine 5'-phosphotransferase
;
# 
_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       
;MAVDSSNSATGPMRVFAIGNPILDLVAEVPSSFLDEFFLKRGDATLATPEQMRIYSTLDQFNPTSLPGGSALNSVRVVQK
LLRKPGSAGYMGAIGDDPRGQVLKELCDKEGLATRFMVAPGQSTGTCAVLINEKERTLCTHLGACGSFRIPEDWTTFASG
ALIFYATAYTLTATPKNALEVAGYAHGIPNAIFTLNLSAPFCVELYKDAMQSLLLHTNILFGNEEEFAHLAKVHNLVAAD
KTALSTANKEHAVEVCTGALRLLTAGQNTGATKLVVMTRGHNPVIAAEQTADGTVVVHEVGVPVVAAEKIVDTNGAGDAF
VGGFLYGLSQGKTVKQCIMCGNACAQDVIQHVGFSLSFTSLPC
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MAVDSSNSATGPMRVFAIGNPILDLVAEVPSSFLDEFFLKRGDATLATPEQMRIYSTLDQFNPTSLPGGSALNSVRVVQK
LLRKPGSAGYMGAIGDDPRGQVLKELCDKEGLATRFMVAPGQSTGTCAVLINEKERTLCTHLGACGSFRIPEDWTTFASG
ALIFYATAYTLTATPKNALEVAGYAHGIPNAIFTLNLSAPFCVELYKDAMQSLLLHTNILFGNEEEFAHLAKVHNLVAAD
KTALSTANKEHAVEVCTGALRLLTAGQNTGATKLVVMTRGHNPVIAAEQTADGTVVVHEVGVPVVAAEKIVDTNGAGDAF
VGGFLYGLSQGKTVKQCIMCGNACAQDVIQHVGFSLSFTSLPC
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
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   ALA n 
1 3   VAL n 
1 4   ASP n 
1 5   SER n 
1 6   SER n 
1 7   ASN n 
1 8   SER n 
1 9   ALA n 
1 10  THR n 
1 11  GLY n 
1 12  PRO n 
1 13  MET n 
1 14  ARG n 
1 15  VAL n 
1 16  PHE n 
1 17  ALA n 
1 18  ILE n 
1 19  GLY n 
1 20  ASN n 
1 21  PRO n 
1 22  ILE n 
1 23  LEU n 
1 24  ASP n 
1 25  LEU n 
1 26  VAL n 
1 27  ALA n 
1 28  GLU n 
1 29  VAL n 
1 30  PRO n 
1 31  SER n 
1 32  SER n 
1 33  PHE n 
1 34  LEU n 
1 35  ASP n 
1 36  GLU n 
1 37  PHE n 
1 38  PHE n 
1 39  LEU n 
1 40  LYS n 
1 41  ARG n 
1 42  GLY n 
1 43  ASP n 
1 44  ALA n 
1 45  THR n 
1 46  LEU n 
1 47  ALA n 
1 48  THR n 
1 49  PRO n 
1 50  GLU n 
1 51  GLN n 
1 52  MET n 
1 53  ARG n 
1 54  ILE n 
1 55  TYR n 
1 56  SER n 
1 57  THR n 
1 58  LEU n 
1 59  ASP n 
1 60  GLN n 
1 61  PHE n 
1 62  ASN n 
1 63  PRO n 
1 64  THR n 
1 65  SER n 
1 66  LEU n 
1 67  PRO n 
1 68  GLY n 
1 69  GLY n 
1 70  SER n 
1 71  ALA n 
1 72  LEU n 
1 73  ASN n 
1 74  SER n 
1 75  VAL n 
1 76  ARG n 
1 77  VAL n 
1 78  VAL n 
1 79  GLN n 
1 80  LYS n 
1 81  LEU n 
1 82  LEU n 
1 83  ARG n 
1 84  LYS n 
1 85  PRO n 
1 86  GLY n 
1 87  SER n 
1 88  ALA n 
1 89  GLY n 
1 90  TYR n 
1 91  MET n 
1 92  GLY n 
1 93  ALA n 
1 94  ILE n 
1 95  GLY n 
1 96  ASP n 
1 97  ASP n 
1 98  PRO n 
1 99  ARG n 
1 100 GLY n 
1 101 GLN n 
1 102 VAL n 
1 103 LEU n 
1 104 LYS n 
1 105 GLU n 
1 106 LEU n 
1 107 CYS n 
1 108 ASP n 
1 109 LYS n 
1 110 GLU n 
1 111 GLY n 
1 112 LEU n 
1 113 ALA n 
1 114 THR n 
1 115 ARG n 
1 116 PHE n 
1 117 MET n 
1 118 VAL n 
1 119 ALA n 
1 120 PRO n 
1 121 GLY n 
1 122 GLN n 
1 123 SER n 
1 124 THR n 
1 125 GLY n 
1 126 THR n 
1 127 CYS n 
1 128 ALA n 
1 129 VAL n 
1 130 LEU n 
1 131 ILE n 
1 132 ASN n 
1 133 GLU n 
1 134 LYS n 
1 135 GLU n 
1 136 ARG n 
1 137 THR n 
1 138 LEU n 
1 139 CYS n 
1 140 THR n 
1 141 HIS n 
1 142 LEU n 
1 143 GLY n 
1 144 ALA n 
1 145 CYS n 
1 146 GLY n 
1 147 SER n 
1 148 PHE n 
1 149 ARG n 
1 150 ILE n 
1 151 PRO n 
1 152 GLU n 
1 153 ASP n 
1 154 TRP n 
1 155 THR n 
1 156 THR n 
1 157 PHE n 
1 158 ALA n 
1 159 SER n 
1 160 GLY n 
1 161 ALA n 
1 162 LEU n 
1 163 ILE n 
1 164 PHE n 
1 165 TYR n 
1 166 ALA n 
1 167 THR n 
1 168 ALA n 
1 169 TYR n 
1 170 THR n 
1 171 LEU n 
1 172 THR n 
1 173 ALA n 
1 174 THR n 
1 175 PRO n 
1 176 LYS n 
1 177 ASN n 
1 178 ALA n 
1 179 LEU n 
1 180 GLU n 
1 181 VAL n 
1 182 ALA n 
1 183 GLY n 
1 184 TYR n 
1 185 ALA n 
1 186 HIS n 
1 187 GLY n 
1 188 ILE n 
1 189 PRO n 
1 190 ASN n 
1 191 ALA n 
1 192 ILE n 
1 193 PHE n 
1 194 THR n 
1 195 LEU n 
1 196 ASN n 
1 197 LEU n 
1 198 SER n 
1 199 ALA n 
1 200 PRO n 
1 201 PHE n 
1 202 CYS n 
1 203 VAL n 
1 204 GLU n 
1 205 LEU n 
1 206 TYR n 
1 207 LYS n 
1 208 ASP n 
1 209 ALA n 
1 210 MET n 
1 211 GLN n 
1 212 SER n 
1 213 LEU n 
1 214 LEU n 
1 215 LEU n 
1 216 HIS n 
1 217 THR n 
1 218 ASN n 
1 219 ILE n 
1 220 LEU n 
1 221 PHE n 
1 222 GLY n 
1 223 ASN n 
1 224 GLU n 
1 225 GLU n 
1 226 GLU n 
1 227 PHE n 
1 228 ALA n 
1 229 HIS n 
1 230 LEU n 
1 231 ALA n 
1 232 LYS n 
1 233 VAL n 
1 234 HIS n 
1 235 ASN n 
1 236 LEU n 
1 237 VAL n 
1 238 ALA n 
1 239 ALA n 
1 240 ASP n 
1 241 LYS n 
1 242 THR n 
1 243 ALA n 
1 244 LEU n 
1 245 SER n 
1 246 THR n 
1 247 ALA n 
1 248 ASN n 
1 249 LYS n 
1 250 GLU n 
1 251 HIS n 
1 252 ALA n 
1 253 VAL n 
1 254 GLU n 
1 255 VAL n 
1 256 CYS n 
1 257 THR n 
1 258 GLY n 
1 259 ALA n 
1 260 LEU n 
1 261 ARG n 
1 262 LEU n 
1 263 LEU n 
1 264 THR n 
1 265 ALA n 
1 266 GLY n 
1 267 GLN n 
1 268 ASN n 
1 269 THR n 
1 270 GLY n 
1 271 ALA n 
1 272 THR n 
1 273 LYS n 
1 274 LEU n 
1 275 VAL n 
1 276 VAL n 
1 277 MET n 
1 278 THR n 
1 279 ARG n 
1 280 GLY n 
1 281 HIS n 
1 282 ASN n 
1 283 PRO n 
1 284 VAL n 
1 285 ILE n 
1 286 ALA n 
1 287 ALA n 
1 288 GLU n 
1 289 GLN n 
1 290 THR n 
1 291 ALA n 
1 292 ASP n 
1 293 GLY n 
1 294 THR n 
1 295 VAL n 
1 296 VAL n 
1 297 VAL n 
1 298 HIS n 
1 299 GLU n 
1 300 VAL n 
1 301 GLY n 
1 302 VAL n 
1 303 PRO n 
1 304 VAL n 
1 305 VAL n 
1 306 ALA n 
1 307 ALA n 
1 308 GLU n 
1 309 LYS n 
1 310 ILE n 
1 311 VAL n 
1 312 ASP n 
1 313 THR n 
1 314 ASN n 
1 315 GLY n 
1 316 ALA n 
1 317 GLY n 
1 318 ASP n 
1 319 ALA n 
1 320 PHE n 
1 321 VAL n 
1 322 GLY n 
1 323 GLY n 
1 324 PHE n 
1 325 LEU n 
1 326 TYR n 
1 327 GLY n 
1 328 LEU n 
1 329 SER n 
1 330 GLN n 
1 331 GLY n 
1 332 LYS n 
1 333 THR n 
1 334 VAL n 
1 335 LYS n 
1 336 GLN n 
1 337 CYS n 
1 338 ILE n 
1 339 MET n 
1 340 CYS n 
1 341 GLY n 
1 342 ASN n 
1 343 ALA n 
1 344 CYS n 
1 345 ALA n 
1 346 GLN n 
1 347 ASP n 
1 348 VAL n 
1 349 ILE n 
1 350 GLN n 
1 351 HIS n 
1 352 VAL n 
1 353 GLY n 
1 354 PHE n 
1 355 SER n 
1 356 LEU n 
1 357 SER n 
1 358 PHE n 
1 359 THR n 
1 360 SER n 
1 361 LEU n 
1 362 PRO n 
1 363 CYS 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                      ? 
_entity_src_gen.pdbx_beg_seq_num                   ? 
_entity_src_gen.pdbx_end_seq_num                   ? 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     Toxoplasma 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_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      'Toxoplasma gondii' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     5811 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     Escherichia 
_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          PLASMID 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       PBACE 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    ADK_TOXGO 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MAVDSSNSATGPMRVFAIGNPILDLVAEVPSSFLDEFFLKRGDATLATPEQMRIYSTLDQFNPTSLPGGSALNSVRVVQK
LLRKPGSAGYMGAIGDDPRGQVLKELCDKEGLATRFMVAPGQSTGVCAVLINEKERTLCTHLGACGSFRLPEDWTTFASG
ALIFYATAYTLTATPKNALEVAGYAHGIPNAIFTLNLSAPFCVELYKDAMQSLLLHTNILFGNEEEFAHLAKVHNLVAAE
KTALSTANKEHAVEVCTGALRLLTAGQNTGATKLVVMTRGHNPVIAAEQTADGTVVVHEVGVPVVAAEKIVDTNGAGDAF
VGGFLYALSQGKTVKQCIMCGNACAQDVIQHVGFSLSFTSLPC
;
_struct_ref.pdbx_align_begin           1 
_struct_ref.pdbx_db_accession          Q9TVW2 
_struct_ref.pdbx_db_isoform            ? 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              1LIO 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 363 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q9TVW2 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  363 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       363 
# 
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 1LIO THR A 126 ? UNP Q9TVW2 VAL 126 CONFLICT 126 1 
1 1LIO ILE A 150 ? UNP Q9TVW2 LEU 150 CONFLICT 150 2 
1 1LIO ASP A 240 ? UNP Q9TVW2 GLU 240 CONFLICT 240 3 
1 1LIO GLY A 327 ? UNP Q9TVW2 ALA 327 CONFLICT 327 4 
# 
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 
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 
# 
_exptl.entry_id          1LIO 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.33 
_exptl_crystal.density_percent_sol   47.16 
_exptl_crystal.description           ? 
_exptl_crystal.F_000                 ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          ? 
_exptl_crystal_grow.temp            ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              7.50 
_exptl_crystal_grow.pdbx_details    'pH 7.50' 
_exptl_crystal_grow.pdbx_pH_range   . 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           298.0 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               'IMAGE PLATE' 
_diffrn_detector.type                   'RIGAKU RAXIS IV' 
_diffrn_detector.pdbx_collection_date   1998-11-10 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.5418 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      'ROTATING ANODE' 
_diffrn_source.type                        'RIGAKU RU300' 
_diffrn_source.pdbx_synchrotron_site       ? 
_diffrn_source.pdbx_synchrotron_beamline   ? 
_diffrn_source.pdbx_wavelength             1.5418 
_diffrn_source.pdbx_wavelength_list        ? 
# 
_reflns.entry_id                     1LIO 
_reflns.observed_criterion_sigma_I   1.000 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             10.000 
_reflns.d_resolution_high            2.500 
_reflns.number_obs                   28789 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         95.0 
_reflns.pdbx_Rmerge_I_obs            0.0990000 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        10.0000 
_reflns.B_iso_Wilson_estimate        25.000 
_reflns.pdbx_redundancy              2.000 
_reflns.R_free_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.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.pdbx_chi_squared             ? 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
# 
_reflns_shell.d_res_high             2.50 
_reflns_shell.d_res_low              2.70 
_reflns_shell.percent_possible_all   85.0 
_reflns_shell.Rmerge_I_obs           0.2300000 
_reflns_shell.pdbx_Rsym_value        ? 
_reflns_shell.meanI_over_sigI_obs    ? 
_reflns_shell.pdbx_redundancy        2.00 
_reflns_shell.percent_possible_obs   ? 
_reflns_shell.number_unique_all      ? 
_reflns_shell.number_measured_all    ? 
_reflns_shell.number_measured_obs    ? 
_reflns_shell.number_unique_obs      ? 
_reflns_shell.pdbx_chi_squared       ? 
_reflns_shell.pdbx_diffrn_id         ? 
_reflns_shell.pdbx_ordinal           1 
# 
_refine.entry_id                                 1LIO 
_refine.ls_number_reflns_obs                     12000 
_refine.ls_number_reflns_all                     12312 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.000 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_d_res_low                             10.0 
_refine.ls_d_res_high                            2.50 
_refine.ls_percent_reflns_obs                    99.0 
_refine.ls_R_factor_obs                          0.2000000 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.1980000 
_refine.ls_R_factor_R_free                       0.2600000 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_number_reflns_R_free                  1000 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.B_iso_mean                               ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_ls_cross_valid_method               ? 
_refine.details                                  ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_B                             ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.B_iso_min                                ? 
_refine.B_iso_max                                ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_SU_ML                            ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_overall_phase_error                 ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        2420 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_refine_hist.number_atoms_solvent             179 
_refine_hist.number_atoms_total               2599 
_refine_hist.d_res_high                       2.50 
_refine_hist.d_res_low                        10.0 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
t_bond_d    0.011 ? ? ? 'X-RAY DIFFRACTION' ? 
t_angle_deg 1.903 ? ? ? 'X-RAY DIFFRACTION' ? 
# 
_struct.entry_id                  1LIO 
_struct.title                     'STRUCTURE OF APO T. GONDII ADENOSINE KINASE' 
_struct.pdbx_descriptor           'adenosine kinase (E.C.2.7.1.20)' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        1LIO 
_struct_keywords.pdbx_keywords   TRANSFERASE 
_struct_keywords.text            'ALPHA-BETA STRUCTURE, TRANSFERASE' 
# 
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 ? 
# 
_struct_biol.id                    1 
_struct_biol.pdbx_parent_biol_id   ? 
_struct_biol.details               ? 
# 
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  1  PRO A 30  ? PHE A 37  ? PRO A 30  PHE A 37  1 ? 8  
HELX_P HELX_P2  2  THR A 48  ? MET A 52  ? THR A 48  MET A 52  5 ? 5  
HELX_P HELX_P3  3  ARG A 53  ? LEU A 58  ? ARG A 53  LEU A 58  1 ? 6  
HELX_P HELX_P4  4  SER A 70  ? ARG A 83  ? SER A 70  ARG A 83  1 ? 14 
HELX_P HELX_P5  5  ASP A 97  ? GLU A 110 ? ASP A 97  GLU A 110 1 ? 14 
HELX_P HELX_P6  6  ASP A 153 ? ALA A 158 ? ASP A 153 ALA A 158 1 ? 6  
HELX_P HELX_P7  7  TYR A 169 ? ALA A 173 ? TYR A 169 ALA A 173 5 ? 5  
HELX_P HELX_P8  8  LYS A 176 ? VAL A 181 ? LYS A 176 VAL A 181 1 ? 6  
HELX_P HELX_P9  9  ALA A 199 ? LEU A 205 ? ALA A 199 LEU A 205 1 ? 7  
HELX_P HELX_P10 10 TYR A 206 ? ASP A 208 ? TYR A 206 ASP A 208 5 ? 3  
HELX_P HELX_P11 11 ALA A 209 ? HIS A 216 ? ALA A 209 HIS A 216 1 ? 8  
HELX_P HELX_P12 12 GLU A 224 ? LYS A 232 ? GLU A 224 LYS A 232 1 ? 9  
HELX_P HELX_P13 13 ASP A 240 ? GLU A 250 ? ASP A 240 GLU A 250 1 ? 11 
HELX_P HELX_P14 14 ALA A 316 ? GLY A 327 ? ALA A 316 GLY A 327 1 ? 12 
HELX_P HELX_P15 15 THR A 333 ? GLN A 346 ? THR A 333 GLN A 346 1 ? 14 
# 
_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          ILE 
_struct_mon_prot_cis.label_seq_id           188 
_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           ILE 
_struct_mon_prot_cis.auth_seq_id            188 
_struct_mon_prot_cis.auth_asym_id           A 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    189 
_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    PRO 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     189 
_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       -0.23 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A ? 6 ? 
B ? 5 ? 
C ? 2 ? 
D ? 2 ? 
E ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
A 1 2 ? parallel      
A 2 3 ? parallel      
A 3 4 ? parallel      
A 4 5 ? parallel      
A 5 6 ? parallel      
B 1 2 ? parallel      
B 2 3 ? anti-parallel 
B 3 4 ? parallel      
B 4 5 ? anti-parallel 
C 1 2 ? parallel      
D 1 2 ? anti-parallel 
E 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
A 1 GLY A 89  ? MET A 91  ? GLY A 89  MET A 91  
A 2 PHE A 16  ? ILE A 18  ? PHE A 16  ILE A 18  
A 3 ILE A 163 ? THR A 167 ? ILE A 163 THR A 167 
A 4 ILE A 192 ? ASN A 196 ? ILE A 192 ASN A 196 
A 5 ILE A 219 ? ASN A 223 ? ILE A 219 ASN A 223 
A 6 VAL A 276 ? THR A 278 ? VAL A 276 THR A 278 
B 1 ALA A 44  ? LEU A 46  ? ALA A 44  LEU A 46  
B 2 THR A 137 ? THR A 140 ? THR A 137 THR A 140 
B 3 THR A 126 ? LEU A 130 ? THR A 126 LEU A 130 
B 4 ILE A 22  ? ASP A 24  ? ILE A 22  ASP A 24  
B 5 PRO A 67  ? GLY A 68  ? PRO A 67  GLY A 68  
C 1 ILE A 94  ? GLY A 95  ? ILE A 94  GLY A 95  
C 2 VAL A 118 ? ALA A 119 ? VAL A 118 ALA A 119 
D 1 VAL A 284 ? ILE A 285 ? VAL A 284 ILE A 285 
D 2 GLU A 299 ? VAL A 300 ? GLU A 299 VAL A 300 
E 1 GLN A 289 ? THR A 290 ? GLN A 289 THR A 290 
E 2 THR A 294 ? VAL A 295 ? THR A 294 VAL A 295 
# 
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 
A 1 2 O MET A 91  ? O MET A 91  N ALA A 17  ? N ALA A 17  
A 2 3 N PHE A 16  ? N PHE A 16  O ILE A 163 ? O ILE A 163 
A 3 4 N PHE A 164 ? N PHE A 164 O ILE A 192 ? O ILE A 192 
A 4 5 N LEU A 195 ? N LEU A 195 O ILE A 219 ? O ILE A 219 
A 5 6 N GLY A 222 ? N GLY A 222 O THR A 278 ? O THR A 278 
B 1 2 N THR A 45  ? N THR A 45  O THR A 140 ? O THR A 140 
B 2 3 O CYS A 139 ? O CYS A 139 N ALA A 128 ? N ALA A 128 
B 3 4 O CYS A 127 ? O CYS A 127 N LEU A 23  ? N LEU A 23  
B 4 5 N ILE A 22  ? N ILE A 22  O GLY A 68  ? O GLY A 68  
C 1 2 N ILE A 94  ? N ILE A 94  O ALA A 119 ? O ALA A 119 
D 1 2 N VAL A 284 ? N VAL A 284 O VAL A 300 ? O VAL A 300 
E 1 2 N THR A 290 ? N THR A 290 O THR A 294 ? O THR A 294 
# 
_database_PDB_matrix.entry_id          1LIO 
_database_PDB_matrix.origx[1][1]       1.000000 
_database_PDB_matrix.origx[1][2]       0.000000 
_database_PDB_matrix.origx[1][3]       0.000000 
_database_PDB_matrix.origx[2][1]       0.000000 
_database_PDB_matrix.origx[2][2]       1.000000 
_database_PDB_matrix.origx[2][3]       0.000000 
_database_PDB_matrix.origx[3][1]       0.000000 
_database_PDB_matrix.origx[3][2]       0.000000 
_database_PDB_matrix.origx[3][3]       1.000000 
_database_PDB_matrix.origx_vector[1]   0.00000 
_database_PDB_matrix.origx_vector[2]   0.00000 
_database_PDB_matrix.origx_vector[3]   0.00000 
# 
_atom_sites.entry_id                    1LIO 
_atom_sites.fract_transf_matrix[1][1]   0.021231 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.004050 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.014706 
_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]   0.017923 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . PRO A 1 12  ? 41.165 2.681  43.382 1.00 53.74  ? 12  PRO A N   1 
ATOM   2    C CA  . PRO A 1 12  ? 41.760 3.915  43.846 1.00 50.30  ? 12  PRO A CA  1 
ATOM   3    C C   . PRO A 1 12  ? 41.669 4.894  42.676 1.00 56.42  ? 12  PRO A C   1 
ATOM   4    O O   . PRO A 1 12  ? 40.559 5.278  42.286 1.00 64.77  ? 12  PRO A O   1 
ATOM   5    C CB  . PRO A 1 12  ? 43.191 3.556  44.236 1.00 49.80  ? 12  PRO A CB  1 
ATOM   6    C CG  . PRO A 1 12  ? 43.168 2.096  44.486 1.00 56.43  ? 12  PRO A CG  1 
ATOM   7    C CD  . PRO A 1 12  ? 42.213 1.617  43.444 1.00 53.18  ? 12  PRO A CD  1 
ATOM   8    N N   . MET A 1 13  ? 42.810 5.291  42.116 1.00 30.31  ? 13  MET A N   1 
ATOM   9    C CA  . MET A 1 13  ? 42.799 6.226  41.004 1.00 26.72  ? 13  MET A CA  1 
ATOM   10   C C   . MET A 1 13  ? 41.899 5.687  39.909 1.00 41.10  ? 13  MET A C   1 
ATOM   11   O O   . MET A 1 13  ? 42.116 4.561  39.432 1.00 44.75  ? 13  MET A O   1 
ATOM   12   C CB  . MET A 1 13  ? 44.134 6.560  40.448 1.00 28.58  ? 13  MET A CB  1 
ATOM   13   C CG  . MET A 1 13  ? 44.067 7.319  39.143 1.00 34.10  ? 13  MET A CG  1 
ATOM   14   S SD  . MET A 1 13  ? 44.233 9.124  39.412 1.00 35.13  ? 13  MET A SD  1 
ATOM   15   C CE  . MET A 1 13  ? 45.390 9.134  40.807 1.00 29.52  ? 13  MET A CE  1 
ATOM   16   N N   . ARG A 1 14  ? 40.893 6.500  39.548 1.00 36.69  ? 14  ARG A N   1 
ATOM   17   C CA  . ARG A 1 14  ? 39.925 6.150  38.518 1.00 36.24  ? 14  ARG A CA  1 
ATOM   18   C C   . ARG A 1 14  ? 39.285 7.391  37.885 1.00 35.71  ? 14  ARG A C   1 
ATOM   19   O O   . ARG A 1 14  ? 38.252 7.306  37.206 1.00 32.54  ? 14  ARG A O   1 
ATOM   20   C CB  . ARG A 1 14  ? 38.822 5.230  39.058 1.00 50.95  ? 14  ARG A CB  1 
ATOM   21   C CG  . ARG A 1 14  ? 39.375 4.108  39.836 1.00 66.86  ? 14  ARG A CG  1 
ATOM   22   C CD  . ARG A 1 14  ? 38.416 3.225  40.326 1.00 71.60  ? 14  ARG A CD  1 
ATOM   23   N NE  . ARG A 1 14  ? 37.614 2.417  39.431 1.00 58.29  ? 14  ARG A NE  1 
ATOM   24   C CZ  . ARG A 1 14  ? 36.408 2.795  39.079 1.00 96.62  ? 14  ARG A CZ  1 
ATOM   25   N NH1 . ARG A 1 14  ? 35.899 3.930  39.540 1.00 95.70  ? 14  ARG A NH1 1 
ATOM   26   N NH2 . ARG A 1 14  ? 35.697 2.041  38.280 1.00 91.45  ? 14  ARG A NH2 1 
ATOM   27   N N   . VAL A 1 15  ? 39.896 8.531  38.117 1.00 31.22  ? 15  VAL A N   1 
ATOM   28   C CA  . VAL A 1 15  ? 39.449 9.826  37.593 1.00 28.67  ? 15  VAL A CA  1 
ATOM   29   C C   . VAL A 1 15  ? 40.658 10.755 37.638 1.00 33.18  ? 15  VAL A C   1 
ATOM   30   O O   . VAL A 1 15  ? 41.321 10.858 38.666 1.00 38.92  ? 15  VAL A O   1 
ATOM   31   C CB  . VAL A 1 15  ? 38.154 10.389 38.260 1.00 29.81  ? 15  VAL A CB  1 
ATOM   32   C CG1 . VAL A 1 15  ? 37.990 11.873 37.954 1.00 27.57  ? 15  VAL A CG1 1 
ATOM   33   C CG2 . VAL A 1 15  ? 36.897 9.683  37.782 1.00 29.83  ? 15  VAL A CG2 1 
ATOM   34   N N   . PHE A 1 16  ? 40.989 11.427 36.556 1.00 28.00  ? 16  PHE A N   1 
ATOM   35   C CA  . PHE A 1 16  ? 42.155 12.328 36.583 1.00 30.00  ? 16  PHE A CA  1 
ATOM   36   C C   . PHE A 1 16  ? 41.764 13.732 36.135 1.00 35.65  ? 16  PHE A C   1 
ATOM   37   O O   . PHE A 1 16  ? 41.213 13.921 35.051 1.00 37.92  ? 16  PHE A O   1 
ATOM   38   C CB  . PHE A 1 16  ? 43.226 11.800 35.629 1.00 26.36  ? 16  PHE A CB  1 
ATOM   39   C CG  . PHE A 1 16  ? 44.462 12.530 35.696 1.00 21.53  ? 16  PHE A CG  1 
ATOM   40   C CD1 . PHE A 1 16  ? 45.435 12.148 36.535 1.00 21.33  ? 16  PHE A CD1 1 
ATOM   41   C CD2 . PHE A 1 16  ? 44.625 13.626 34.869 1.00 25.35  ? 16  PHE A CD2 1 
ATOM   42   C CE1 . PHE A 1 16  ? 46.595 12.879 36.572 1.00 25.47  ? 16  PHE A CE1 1 
ATOM   43   C CE2 . PHE A 1 16  ? 45.764 14.349 34.883 1.00 25.18  ? 16  PHE A CE2 1 
ATOM   44   C CZ  . PHE A 1 16  ? 46.757 13.985 35.733 1.00 23.34  ? 16  PHE A CZ  1 
ATOM   45   N N   . ALA A 1 17  ? 42.049 14.715 36.962 1.00 36.45  ? 17  ALA A N   1 
ATOM   46   C CA  . ALA A 1 17  ? 41.711 16.101 36.642 1.00 39.01  ? 17  ALA A CA  1 
ATOM   47   C C   . ALA A 1 17  ? 42.932 17.012 36.477 1.00 38.83  ? 17  ALA A C   1 
ATOM   48   O O   . ALA A 1 17  ? 43.964 16.945 37.187 1.00 25.58  ? 17  ALA A O   1 
ATOM   49   C CB  . ALA A 1 17  ? 40.615 16.682 37.563 1.00 41.02  ? 17  ALA A CB  1 
ATOM   50   N N   . ILE A 1 18  ? 42.786 17.889 35.502 1.00 31.81  ? 18  ILE A N   1 
ATOM   51   C CA  . ILE A 1 18  ? 43.828 18.828 35.194 1.00 24.42  ? 18  ILE A CA  1 
ATOM   52   C C   . ILE A 1 18  ? 43.229 20.209 35.057 1.00 28.37  ? 18  ILE A C   1 
ATOM   53   O O   . ILE A 1 18  ? 42.308 20.452 34.260 1.00 25.10  ? 18  ILE A O   1 
ATOM   54   C CB  . ILE A 1 18  ? 44.603 18.244 33.941 1.00 21.64  ? 18  ILE A CB  1 
ATOM   55   C CG1 . ILE A 1 18  ? 46.113 18.260 34.032 1.00 12.16  ? 18  ILE A CG1 1 
ATOM   56   C CG2 . ILE A 1 18  ? 44.059 18.928 32.680 1.00 32.54  ? 18  ILE A CG2 1 
ATOM   57   C CD1 . ILE A 1 18  ? 46.813 17.075 34.552 1.00 21.56  ? 18  ILE A CD1 1 
ATOM   58   N N   . GLY A 1 19  ? 43.772 21.098 35.876 1.00 23.05  ? 19  GLY A N   1 
ATOM   59   C CA  . GLY A 1 19  ? 43.349 22.482 35.922 1.00 20.28  ? 19  GLY A CA  1 
ATOM   60   C C   . GLY A 1 19  ? 44.243 23.344 36.837 1.00 38.92  ? 19  GLY A C   1 
ATOM   61   O O   . GLY A 1 19  ? 45.363 22.993 37.226 1.00 34.74  ? 19  GLY A O   1 
ATOM   62   N N   . ASN A 1 20  ? 43.721 24.521 37.142 1.00 53.07  ? 20  ASN A N   1 
ATOM   63   C CA  . ASN A 1 20  ? 44.398 25.510 37.980 1.00 57.79  ? 20  ASN A CA  1 
ATOM   64   C C   . ASN A 1 20  ? 44.036 25.348 39.452 1.00 69.71  ? 20  ASN A C   1 
ATOM   65   O O   . ASN A 1 20  ? 42.893 25.622 39.858 1.00 71.74  ? 20  ASN A O   1 
ATOM   66   C CB  . ASN A 1 20  ? 43.883 26.866 37.513 1.00 45.06  ? 20  ASN A CB  1 
ATOM   67   C CG  . ASN A 1 20  ? 43.372 26.843 36.071 1.00 64.68  ? 20  ASN A CG  1 
ATOM   68   O OD1 . ASN A 1 20  ? 42.674 25.908 35.681 1.00 77.00  ? 20  ASN A OD1 1 
ATOM   69   N ND2 . ASN A 1 20  ? 43.681 27.825 35.246 1.00 46.12  ? 20  ASN A ND2 1 
ATOM   70   N N   . PRO A 1 21  ? 44.959 24.906 40.296 1.00 63.73  ? 21  PRO A N   1 
ATOM   71   C CA  . PRO A 1 21  ? 44.690 24.753 41.715 1.00 65.01  ? 21  PRO A CA  1 
ATOM   72   C C   . PRO A 1 21  ? 44.441 26.089 42.338 1.00 69.38  ? 21  PRO A C   1 
ATOM   73   O O   . PRO A 1 21  ? 45.407 26.892 42.481 1.00 76.26  ? 21  PRO A O   1 
ATOM   74   C CB  . PRO A 1 21  ? 45.967 24.181 42.271 1.00 64.65  ? 21  PRO A CB  1 
ATOM   75   C CG  . PRO A 1 21  ? 46.960 24.073 41.124 1.00 68.32  ? 21  PRO A CG  1 
ATOM   76   C CD  . PRO A 1 21  ? 46.306 24.542 39.866 1.00 61.54  ? 21  PRO A CD  1 
ATOM   77   N N   . ILE A 1 22  ? 43.233 26.365 42.715 1.00 52.57  ? 22  ILE A N   1 
ATOM   78   C CA  . ILE A 1 22  ? 42.946 27.660 43.332 1.00 48.45  ? 22  ILE A CA  1 
ATOM   79   C C   . ILE A 1 22  ? 42.361 27.404 44.738 1.00 62.49  ? 22  ILE A C   1 
ATOM   80   O O   . ILE A 1 22  ? 41.665 26.404 44.970 1.00 67.99  ? 22  ILE A O   1 
ATOM   81   C CB  . ILE A 1 22  ? 42.012 28.438 42.393 1.00 48.54  ? 22  ILE A CB  1 
ATOM   82   C CG1 . ILE A 1 22  ? 41.591 29.805 42.926 1.00 55.52  ? 22  ILE A CG1 1 
ATOM   83   C CG2 . ILE A 1 22  ? 40.718 27.701 42.079 1.00 47.32  ? 22  ILE A CG2 1 
ATOM   84   C CD1 . ILE A 1 22  ? 40.329 30.342 42.237 1.00 42.33  ? 22  ILE A CD1 1 
ATOM   85   N N   . LEU A 1 23  ? 42.695 28.332 45.618 1.00 43.94  ? 23  LEU A N   1 
ATOM   86   C CA  . LEU A 1 23  ? 42.314 28.314 47.045 1.00 33.03  ? 23  LEU A CA  1 
ATOM   87   C C   . LEU A 1 23  ? 41.206 29.344 47.314 1.00 41.17  ? 23  LEU A C   1 
ATOM   88   O O   . LEU A 1 23  ? 41.130 30.389 46.656 1.00 38.44  ? 23  LEU A O   1 
ATOM   89   C CB  . LEU A 1 23  ? 43.584 28.659 47.849 1.00 31.07  ? 23  LEU A CB  1 
ATOM   90   C CG  . LEU A 1 23  ? 43.407 28.697 49.362 1.00 32.82  ? 23  LEU A CG  1 
ATOM   91   C CD1 . LEU A 1 23  ? 42.245 27.846 49.856 1.00 29.86  ? 23  LEU A CD1 1 
ATOM   92   C CD2 . LEU A 1 23  ? 44.647 28.189 50.114 1.00 30.07  ? 23  LEU A CD2 1 
ATOM   93   N N   . ASP A 1 24  ? 40.369 29.020 48.286 1.00 37.36  ? 24  ASP A N   1 
ATOM   94   C CA  . ASP A 1 24  ? 39.246 29.888 48.687 1.00 28.42  ? 24  ASP A CA  1 
ATOM   95   C C   . ASP A 1 24  ? 39.458 30.335 50.138 1.00 43.00  ? 24  ASP A C   1 
ATOM   96   O O   . ASP A 1 24  ? 39.982 29.576 50.967 1.00 44.39  ? 24  ASP A O   1 
ATOM   97   C CB  . ASP A 1 24  ? 37.946 29.122 48.523 1.00 24.57  ? 24  ASP A CB  1 
ATOM   98   C CG  . ASP A 1 24  ? 37.754 28.659 47.076 1.00 27.34  ? 24  ASP A CG  1 
ATOM   99   O OD1 . ASP A 1 24  ? 38.440 29.213 46.129 1.00 16.52  ? 24  ASP A OD1 1 
ATOM   100  O OD2 . ASP A 1 24  ? 36.918 27.722 46.802 1.00 29.00  ? 24  ASP A OD2 1 
ATOM   101  N N   . LEU A 1 25  ? 39.036 31.567 50.388 1.00 39.24  ? 25  LEU A N   1 
ATOM   102  C CA  . LEU A 1 25  ? 39.195 32.222 51.700 1.00 34.56  ? 25  LEU A CA  1 
ATOM   103  C C   . LEU A 1 25  ? 37.874 32.724 52.300 1.00 49.20  ? 25  LEU A C   1 
ATOM   104  O O   . LEU A 1 25  ? 37.804 33.833 52.846 1.00 58.02  ? 25  LEU A O   1 
ATOM   105  C CB  . LEU A 1 25  ? 40.089 33.459 51.541 1.00 33.74  ? 25  LEU A CB  1 
ATOM   106  C CG  . LEU A 1 25  ? 41.463 33.324 52.184 1.00 38.62  ? 25  LEU A CG  1 
ATOM   107  C CD1 . LEU A 1 25  ? 41.751 31.914 52.690 1.00 45.53  ? 25  LEU A CD1 1 
ATOM   108  C CD2 . LEU A 1 25  ? 42.605 33.665 51.222 1.00 5.00   ? 25  LEU A CD2 1 
ATOM   109  N N   . VAL A 1 26  ? 36.825 31.934 52.215 1.00 45.62  ? 26  VAL A N   1 
ATOM   110  C CA  . VAL A 1 26  ? 35.526 32.363 52.775 1.00 45.88  ? 26  VAL A CA  1 
ATOM   111  C C   . VAL A 1 26  ? 35.750 32.967 54.165 1.00 44.90  ? 26  VAL A C   1 
ATOM   112  O O   . VAL A 1 26  ? 36.508 32.425 54.984 1.00 39.42  ? 26  VAL A O   1 
ATOM   113  C CB  . VAL A 1 26  ? 34.555 31.189 52.898 1.00 52.88  ? 26  VAL A CB  1 
ATOM   114  C CG1 . VAL A 1 26  ? 34.786 30.108 51.845 1.00 53.14  ? 26  VAL A CG1 1 
ATOM   115  C CG2 . VAL A 1 26  ? 34.642 30.480 54.251 1.00 52.28  ? 26  VAL A CG2 1 
ATOM   116  N N   . ALA A 1 27  ? 35.081 34.081 54.387 1.00 44.15  ? 27  ALA A N   1 
ATOM   117  C CA  . ALA A 1 27  ? 35.165 34.813 55.654 1.00 47.59  ? 27  ALA A CA  1 
ATOM   118  C C   . ALA A 1 27  ? 33.800 35.387 56.034 1.00 50.47  ? 27  ALA A C   1 
ATOM   119  O O   . ALA A 1 27  ? 32.829 34.647 56.235 1.00 47.80  ? 27  ALA A O   1 
ATOM   120  C CB  . ALA A 1 27  ? 36.161 35.972 55.526 1.00 49.81  ? 27  ALA A CB  1 
ATOM   121  N N   . GLU A 1 28  ? 33.809 36.680 56.110 1.00 50.48  ? 28  GLU A N   1 
ATOM   122  C CA  . GLU A 1 28  ? 32.660 37.510 56.464 1.00 51.81  ? 28  GLU A CA  1 
ATOM   123  C C   . GLU A 1 28  ? 33.236 38.760 57.052 1.00 50.59  ? 28  GLU A C   1 
ATOM   124  O O   . GLU A 1 28  ? 33.680 38.774 58.213 1.00 46.56  ? 28  GLU A O   1 
ATOM   125  C CB  . GLU A 1 28  ? 31.760 36.789 57.443 1.00 55.11  ? 28  GLU A CB  1 
ATOM   126  C CG  . GLU A 1 28  ? 31.749 37.421 58.820 1.00 49.15  ? 28  GLU A CG  1 
ATOM   127  C CD  . GLU A 1 28  ? 31.896 36.383 59.912 1.00 77.40  ? 28  GLU A CD  1 
ATOM   128  O OE1 . GLU A 1 28  ? 33.007 36.282 60.551 1.00 35.10  ? 28  GLU A OE1 1 
ATOM   129  O OE2 . GLU A 1 28  ? 30.909 35.604 60.190 1.00 98.03  ? 28  GLU A OE2 1 
ATOM   130  N N   . VAL A 1 29  ? 33.194 39.715 56.209 1.00 60.24  ? 29  VAL A N   1 
ATOM   131  C CA  . VAL A 1 29  ? 33.745 41.007 56.429 1.00 60.26  ? 29  VAL A CA  1 
ATOM   132  C C   . VAL A 1 29  ? 32.667 42.073 56.558 1.00 60.31  ? 29  VAL A C   1 
ATOM   133  O O   . VAL A 1 29  ? 31.663 42.064 55.828 1.00 62.38  ? 29  VAL A O   1 
ATOM   134  C CB  . VAL A 1 29  ? 34.608 41.275 55.197 1.00 58.45  ? 29  VAL A CB  1 
ATOM   135  C CG1 . VAL A 1 29  ? 34.086 42.423 54.338 1.00 53.85  ? 29  VAL A CG1 1 
ATOM   136  C CG2 . VAL A 1 29  ? 36.052 41.610 55.533 1.00 56.03  ? 29  VAL A CG2 1 
ATOM   137  N N   . PRO A 1 30  ? 32.799 43.043 57.486 1.00 52.58  ? 30  PRO A N   1 
ATOM   138  C CA  . PRO A 1 30  ? 31.827 44.098 57.576 1.00 49.01  ? 30  PRO A CA  1 
ATOM   139  C C   . PRO A 1 30  ? 31.833 44.790 56.232 1.00 47.14  ? 30  PRO A C   1 
ATOM   140  O O   . PRO A 1 30  ? 32.837 44.640 55.470 1.00 54.77  ? 30  PRO A O   1 
ATOM   141  C CB  . PRO A 1 30  ? 32.333 44.964 58.714 1.00 47.96  ? 30  PRO A CB  1 
ATOM   142  C CG  . PRO A 1 30  ? 33.617 44.332 59.240 1.00 58.81  ? 30  PRO A CG  1 
ATOM   143  C CD  . PRO A 1 30  ? 33.905 43.097 58.444 1.00 55.44  ? 30  PRO A CD  1 
ATOM   144  N N   . SER A 1 31  ? 30.774 45.505 55.948 1.00 26.28  ? 31  SER A N   1 
ATOM   145  C CA  . SER A 1 31  ? 30.625 46.221 54.661 1.00 25.28  ? 31  SER A CA  1 
ATOM   146  C C   . SER A 1 31  ? 31.916 46.972 54.272 1.00 40.98  ? 31  SER A C   1 
ATOM   147  O O   . SER A 1 31  ? 32.422 46.836 53.146 1.00 35.15  ? 31  SER A O   1 
ATOM   148  C CB  . SER A 1 31  ? 29.493 47.242 54.753 1.00 28.34  ? 31  SER A CB  1 
ATOM   149  O OG  . SER A 1 31  ? 28.245 46.575 54.856 1.00 52.09  ? 31  SER A OG  1 
ATOM   150  N N   . SER A 1 32  ? 32.405 47.745 55.227 1.00 46.73  ? 32  SER A N   1 
ATOM   151  C CA  . SER A 1 32  ? 33.616 48.575 55.058 1.00 42.73  ? 32  SER A CA  1 
ATOM   152  C C   . SER A 1 32  ? 34.780 47.767 54.468 1.00 40.54  ? 32  SER A C   1 
ATOM   153  O O   . SER A 1 32  ? 35.326 48.104 53.407 1.00 45.54  ? 32  SER A O   1 
ATOM   154  C CB  . SER A 1 32  ? 34.067 49.153 56.398 1.00 45.27  ? 32  SER A CB  1 
ATOM   155  O OG  . SER A 1 32  ? 34.058 48.146 57.390 1.00 43.54  ? 32  SER A OG  1 
ATOM   156  N N   . PHE A 1 33  ? 35.178 46.695 55.151 1.00 44.64  ? 33  PHE A N   1 
ATOM   157  C CA  . PHE A 1 33  ? 36.292 45.887 54.639 1.00 49.23  ? 33  PHE A CA  1 
ATOM   158  C C   . PHE A 1 33  ? 36.156 45.731 53.156 1.00 62.80  ? 33  PHE A C   1 
ATOM   159  O O   . PHE A 1 33  ? 37.132 45.898 52.411 1.00 64.63  ? 33  PHE A O   1 
ATOM   160  C CB  . PHE A 1 33  ? 36.351 44.469 55.182 1.00 48.17  ? 33  PHE A CB  1 
ATOM   161  C CG  . PHE A 1 33  ? 37.403 43.679 54.389 1.00 46.61  ? 33  PHE A CG  1 
ATOM   162  C CD1 . PHE A 1 33  ? 38.726 43.656 54.834 1.00 42.71  ? 33  PHE A CD1 1 
ATOM   163  C CD2 . PHE A 1 33  ? 37.051 42.995 53.210 1.00 40.06  ? 33  PHE A CD2 1 
ATOM   164  C CE1 . PHE A 1 33  ? 39.699 42.965 54.110 1.00 42.04  ? 33  PHE A CE1 1 
ATOM   165  C CE2 . PHE A 1 33  ? 38.029 42.306 52.483 1.00 32.78  ? 33  PHE A CE2 1 
ATOM   166  C CZ  . PHE A 1 33  ? 39.353 42.292 52.933 1.00 31.49  ? 33  PHE A CZ  1 
ATOM   167  N N   . LEU A 1 34  ? 34.937 45.415 52.828 1.00 58.29  ? 34  LEU A N   1 
ATOM   168  C CA  . LEU A 1 34  ? 34.493 45.188 51.474 1.00 55.84  ? 34  LEU A CA  1 
ATOM   169  C C   . LEU A 1 34  ? 34.692 46.442 50.621 1.00 55.44  ? 34  LEU A C   1 
ATOM   170  O O   . LEU A 1 34  ? 35.273 46.386 49.532 1.00 64.28  ? 34  LEU A O   1 
ATOM   171  C CB  . LEU A 1 34  ? 33.009 44.823 51.498 1.00 56.38  ? 34  LEU A CB  1 
ATOM   172  C CG  . LEU A 1 34  ? 32.371 44.821 50.116 1.00 62.93  ? 34  LEU A CG  1 
ATOM   173  C CD1 . LEU A 1 34  ? 30.988 44.170 50.102 1.00 62.92  ? 34  LEU A CD1 1 
ATOM   174  C CD2 . LEU A 1 34  ? 32.176 46.228 49.551 1.00 57.81  ? 34  LEU A CD2 1 
ATOM   175  N N   . ASP A 1 35  ? 34.206 47.550 51.135 1.00 52.71  ? 35  ASP A N   1 
ATOM   176  C CA  . ASP A 1 35  ? 34.282 48.843 50.433 1.00 57.06  ? 35  ASP A CA  1 
ATOM   177  C C   . ASP A 1 35  ? 35.743 49.357 50.321 1.00 55.79  ? 35  ASP A C   1 
ATOM   178  O O   . ASP A 1 35  ? 36.064 50.183 49.456 1.00 62.23  ? 35  ASP A O   1 
ATOM   179  C CB  . ASP A 1 35  ? 33.453 49.895 51.180 1.00 65.59  ? 35  ASP A CB  1 
ATOM   180  C CG  . ASP A 1 35  ? 32.134 50.236 50.468 1.00 97.08  ? 35  ASP A CG  1 
ATOM   181  O OD1 . ASP A 1 35  ? 31.031 49.676 50.839 1.00 100.00 ? 35  ASP A OD1 1 
ATOM   182  O OD2 . ASP A 1 35  ? 32.126 51.085 49.494 1.00 100.00 ? 35  ASP A OD2 1 
ATOM   183  N N   . GLU A 1 36  ? 36.608 48.855 51.196 1.00 46.96  ? 36  GLU A N   1 
ATOM   184  C CA  . GLU A 1 36  ? 38.046 49.265 51.239 1.00 39.37  ? 36  GLU A CA  1 
ATOM   185  C C   . GLU A 1 36  ? 38.810 48.797 49.997 1.00 34.46  ? 36  GLU A C   1 
ATOM   186  O O   . GLU A 1 36  ? 39.778 49.436 49.558 1.00 27.79  ? 36  GLU A O   1 
ATOM   187  C CB  . GLU A 1 36  ? 38.742 48.656 52.469 1.00 38.41  ? 36  GLU A CB  1 
ATOM   188  C CG  . GLU A 1 36  ? 40.269 48.832 52.455 1.00 58.30  ? 36  GLU A CG  1 
ATOM   189  C CD  . GLU A 1 36  ? 40.739 50.079 53.216 1.00 100.00 ? 36  GLU A CD  1 
ATOM   190  O OE1 . GLU A 1 36  ? 39.884 50.809 53.850 1.00 100.00 ? 36  GLU A OE1 1 
ATOM   191  O OE2 . GLU A 1 36  ? 41.989 50.403 53.221 1.00 100.00 ? 36  GLU A OE2 1 
ATOM   192  N N   . PHE A 1 37  ? 38.345 47.704 49.469 1.00 35.88  ? 37  PHE A N   1 
ATOM   193  C CA  . PHE A 1 37  ? 38.950 47.058 48.309 1.00 34.02  ? 37  PHE A CA  1 
ATOM   194  C C   . PHE A 1 37  ? 38.025 47.152 47.033 1.00 54.05  ? 37  PHE A C   1 
ATOM   195  O O   . PHE A 1 37  ? 38.101 46.285 46.154 1.00 58.50  ? 37  PHE A O   1 
ATOM   196  C CB  . PHE A 1 37  ? 39.154 45.577 48.693 1.00 26.39  ? 37  PHE A CB  1 
ATOM   197  C CG  . PHE A 1 37  ? 40.374 45.342 49.600 1.00 26.73  ? 37  PHE A CG  1 
ATOM   198  C CD1 . PHE A 1 37  ? 40.225 45.023 50.967 1.00 32.21  ? 37  PHE A CD1 1 
ATOM   199  C CD2 . PHE A 1 37  ? 41.650 45.445 49.052 1.00 23.65  ? 37  PHE A CD2 1 
ATOM   200  C CE1 . PHE A 1 37  ? 41.367 44.806 51.765 1.00 21.70  ? 37  PHE A CE1 1 
ATOM   201  C CE2 . PHE A 1 37  ? 42.786 45.227 49.844 1.00 19.83  ? 37  PHE A CE2 1 
ATOM   202  C CZ  . PHE A 1 37  ? 42.646 44.908 51.200 1.00 14.05  ? 37  PHE A CZ  1 
ATOM   203  N N   . PHE A 1 38  ? 37.212 48.249 46.966 1.00 49.71  ? 38  PHE A N   1 
ATOM   204  C CA  . PHE A 1 38  ? 36.103 48.507 45.895 1.00 50.91  ? 38  PHE A CA  1 
ATOM   205  C C   . PHE A 1 38  ? 35.675 47.290 45.115 1.00 71.10  ? 38  PHE A C   1 
ATOM   206  O O   . PHE A 1 38  ? 36.080 47.081 43.953 1.00 78.38  ? 38  PHE A O   1 
ATOM   207  C CB  . PHE A 1 38  ? 36.244 49.512 44.748 1.00 50.20  ? 38  PHE A CB  1 
ATOM   208  C CG  . PHE A 1 38  ? 34.759 49.714 44.208 1.00 43.82  ? 38  PHE A CG  1 
ATOM   209  C CD1 . PHE A 1 38  ? 34.387 49.403 42.878 1.00 37.17  ? 38  PHE A CD1 1 
ATOM   210  C CD2 . PHE A 1 38  ? 33.741 50.191 45.081 1.00 37.23  ? 38  PHE A CD2 1 
ATOM   211  C CE1 . PHE A 1 38  ? 33.034 49.550 42.450 1.00 31.81  ? 38  PHE A CE1 1 
ATOM   212  C CE2 . PHE A 1 38  ? 32.402 50.327 44.653 1.00 35.43  ? 38  PHE A CE2 1 
ATOM   213  C CZ  . PHE A 1 38  ? 32.050 50.005 43.343 1.00 27.27  ? 38  PHE A CZ  1 
ATOM   214  N N   . LEU A 1 39  ? 34.866 46.619 45.856 1.00 68.58  ? 39  LEU A N   1 
ATOM   215  C CA  . LEU A 1 39  ? 34.197 45.408 45.522 1.00 63.29  ? 39  LEU A CA  1 
ATOM   216  C C   . LEU A 1 39  ? 32.793 45.521 45.799 1.00 79.77  ? 39  LEU A C   1 
ATOM   217  O O   . LEU A 1 39  ? 32.390 45.936 46.893 1.00 84.96  ? 39  LEU A O   1 
ATOM   218  C CB  . LEU A 1 39  ? 34.540 44.223 46.457 1.00 60.54  ? 39  LEU A CB  1 
ATOM   219  C CG  . LEU A 1 39  ? 35.925 43.646 46.443 1.00 65.92  ? 39  LEU A CG  1 
ATOM   220  C CD1 . LEU A 1 39  ? 36.238 42.900 47.759 1.00 67.02  ? 39  LEU A CD1 1 
ATOM   221  C CD2 . LEU A 1 39  ? 36.133 42.625 45.337 1.00 69.85  ? 39  LEU A CD2 1 
ATOM   222  N N   . LYS A 1 40  ? 31.943 45.182 44.924 1.00 79.07  ? 40  LYS A N   1 
ATOM   223  C CA  . LYS A 1 40  ? 30.656 45.232 45.445 1.00 78.14  ? 40  LYS A CA  1 
ATOM   224  C C   . LYS A 1 40  ? 29.932 43.979 45.367 1.00 71.56  ? 40  LYS A C   1 
ATOM   225  O O   . LYS A 1 40  ? 30.106 43.194 44.416 1.00 52.35  ? 40  LYS A O   1 
ATOM   226  C CB  . LYS A 1 40  ? 29.679 46.218 44.944 1.00 79.51  ? 40  LYS A CB  1 
ATOM   227  C CG  . LYS A 1 40  ? 28.558 46.344 46.059 1.00 47.02  ? 40  LYS A CG  1 
ATOM   228  C CD  . LYS A 1 40  ? 28.275 47.783 46.514 1.00 61.27  ? 40  LYS A CD  1 
ATOM   229  C CE  . LYS A 1 40  ? 28.478 48.062 48.017 1.00 17.02  ? 40  LYS A CE  1 
ATOM   230  N NZ  . LYS A 1 40  ? 29.859 48.458 48.342 1.00 12.57  ? 40  LYS A NZ  1 
ATOM   231  N N   . ARG A 1 41  ? 29.190 43.976 46.445 1.00 75.81  ? 41  ARG A N   1 
ATOM   232  C CA  . ARG A 1 41  ? 28.290 42.963 46.849 1.00 78.07  ? 41  ARG A CA  1 
ATOM   233  C C   . ARG A 1 41  ? 27.534 42.459 45.659 1.00 90.57  ? 41  ARG A C   1 
ATOM   234  O O   . ARG A 1 41  ? 26.750 43.211 45.037 1.00 93.30  ? 41  ARG A O   1 
ATOM   235  C CB  . ARG A 1 41  ? 27.305 43.536 47.891 1.00 77.72  ? 41  ARG A CB  1 
ATOM   236  C CG  . ARG A 1 41  ? 27.196 42.695 49.193 1.00 93.26  ? 41  ARG A CG  1 
ATOM   237  C CD  . ARG A 1 41  ? 25.998 43.119 50.094 1.00 100.00 ? 41  ARG A CD  1 
ATOM   238  N NE  . ARG A 1 41  ? 26.078 44.527 50.570 1.00 100.00 ? 41  ARG A NE  1 
ATOM   239  C CZ  . ARG A 1 41  ? 26.730 44.918 51.688 1.00 99.12  ? 41  ARG A CZ  1 
ATOM   240  N NH1 . ARG A 1 41  ? 27.369 44.030 52.463 1.00 47.90  ? 41  ARG A NH1 1 
ATOM   241  N NH2 . ARG A 1 41  ? 26.802 46.190 52.117 1.00 72.34  ? 41  ARG A NH2 1 
ATOM   242  N N   . GLY A 1 42  ? 27.816 41.207 45.434 1.00 87.72  ? 42  GLY A N   1 
ATOM   243  C CA  . GLY A 1 42  ? 27.250 40.418 44.377 1.00 83.61  ? 42  GLY A CA  1 
ATOM   244  C C   . GLY A 1 42  ? 28.180 40.479 43.225 1.00 74.12  ? 42  GLY A C   1 
ATOM   245  O O   . GLY A 1 42  ? 27.735 40.658 42.081 1.00 68.42  ? 42  GLY A O   1 
ATOM   246  N N   . ASP A 1 43  ? 29.428 40.318 43.588 1.00 57.82  ? 43  ASP A N   1 
ATOM   247  C CA  . ASP A 1 43  ? 30.520 40.384 42.656 1.00 49.77  ? 43  ASP A CA  1 
ATOM   248  C C   . ASP A 1 43  ? 31.664 39.401 42.978 1.00 50.42  ? 43  ASP A C   1 
ATOM   249  O O   . ASP A 1 43  ? 32.072 39.249 44.140 1.00 49.60  ? 43  ASP A O   1 
ATOM   250  C CB  . ASP A 1 43  ? 31.104 41.783 42.720 1.00 50.55  ? 43  ASP A CB  1 
ATOM   251  C CG  . ASP A 1 43  ? 31.106 42.504 41.395 1.00 46.48  ? 43  ASP A CG  1 
ATOM   252  O OD1 . ASP A 1 43  ? 30.017 42.623 40.725 1.00 34.22  ? 43  ASP A OD1 1 
ATOM   253  O OD2 . ASP A 1 43  ? 32.208 42.996 40.953 1.00 35.45  ? 43  ASP A OD2 1 
ATOM   254  N N   . ALA A 1 44  ? 32.112 38.801 41.899 1.00 43.61  ? 44  ALA A N   1 
ATOM   255  C CA  . ALA A 1 44  ? 33.251 37.867 41.836 1.00 43.50  ? 44  ALA A CA  1 
ATOM   256  C C   . ALA A 1 44  ? 34.057 38.356 40.639 1.00 44.60  ? 44  ALA A C   1 
ATOM   257  O O   . ALA A 1 44  ? 33.586 38.312 39.494 1.00 48.27  ? 44  ALA A O   1 
ATOM   258  C CB  . ALA A 1 44  ? 32.759 36.431 41.646 1.00 45.14  ? 44  ALA A CB  1 
ATOM   259  N N   . THR A 1 45  ? 35.253 38.831 40.890 1.00 23.53  ? 45  THR A N   1 
ATOM   260  C CA  . THR A 1 45  ? 36.057 39.400 39.809 1.00 21.52  ? 45  THR A CA  1 
ATOM   261  C C   . THR A 1 45  ? 37.544 39.192 40.005 1.00 36.31  ? 45  THR A C   1 
ATOM   262  O O   . THR A 1 45  ? 37.998 38.727 41.054 1.00 49.91  ? 45  THR A O   1 
ATOM   263  C CB  . THR A 1 45  ? 35.779 40.905 39.772 1.00 30.85  ? 45  THR A CB  1 
ATOM   264  O OG1 . THR A 1 45  ? 34.769 41.190 38.817 1.00 31.79  ? 45  THR A OG1 1 
ATOM   265  C CG2 . THR A 1 45  ? 37.006 41.736 39.412 1.00 12.68  ? 45  THR A CG2 1 
ATOM   266  N N   . LEU A 1 46  ? 38.271 39.555 38.972 1.00 26.82  ? 46  LEU A N   1 
ATOM   267  C CA  . LEU A 1 46  ? 39.717 39.427 38.971 1.00 24.90  ? 46  LEU A CA  1 
ATOM   268  C C   . LEU A 1 46  ? 40.329 40.600 39.718 1.00 46.33  ? 46  LEU A C   1 
ATOM   269  O O   . LEU A 1 46  ? 40.189 41.764 39.309 1.00 36.07  ? 46  LEU A O   1 
ATOM   270  C CB  . LEU A 1 46  ? 40.219 39.362 37.544 1.00 21.20  ? 46  LEU A CB  1 
ATOM   271  C CG  . LEU A 1 46  ? 40.004 37.965 36.961 1.00 17.27  ? 46  LEU A CG  1 
ATOM   272  C CD1 . LEU A 1 46  ? 38.892 37.919 35.915 1.00 15.43  ? 46  LEU A CD1 1 
ATOM   273  C CD2 . LEU A 1 46  ? 41.247 37.399 36.283 1.00 22.04  ? 46  LEU A CD2 1 
ATOM   274  N N   . ALA A 1 47  ? 40.975 40.208 40.798 1.00 56.39  ? 47  ALA A N   1 
ATOM   275  C CA  . ALA A 1 47  ? 41.656 41.110 41.719 1.00 56.34  ? 47  ALA A CA  1 
ATOM   276  C C   . ALA A 1 47  ? 42.600 42.005 40.960 1.00 49.69  ? 47  ALA A C   1 
ATOM   277  O O   . ALA A 1 47  ? 43.202 41.616 39.958 1.00 44.80  ? 47  ALA A O   1 
ATOM   278  C CB  . ALA A 1 47  ? 42.467 40.292 42.736 1.00 56.94  ? 47  ALA A CB  1 
ATOM   279  N N   . THR A 1 48  ? 42.738 43.233 41.407 1.00 41.05  ? 48  THR A N   1 
ATOM   280  C CA  . THR A 1 48  ? 43.682 44.097 40.731 1.00 37.28  ? 48  THR A CA  1 
ATOM   281  C C   . THR A 1 48  ? 44.830 44.398 41.707 1.00 42.20  ? 48  THR A C   1 
ATOM   282  O O   . THR A 1 48  ? 44.988 43.722 42.739 1.00 34.61  ? 48  THR A O   1 
ATOM   283  C CB  . THR A 1 48  ? 43.034 45.379 40.157 1.00 41.54  ? 48  THR A CB  1 
ATOM   284  O OG1 . THR A 1 48  ? 43.249 46.487 40.997 1.00 53.34  ? 48  THR A OG1 1 
ATOM   285  C CG2 . THR A 1 48  ? 41.521 45.249 39.928 1.00 28.14  ? 48  THR A CG2 1 
ATOM   286  N N   . PRO A 1 49  ? 45.640 45.383 41.431 1.00 45.69  ? 49  PRO A N   1 
ATOM   287  C CA  . PRO A 1 49  ? 46.827 45.678 42.238 1.00 49.50  ? 49  PRO A CA  1 
ATOM   288  C C   . PRO A 1 49  ? 46.556 46.029 43.689 1.00 57.19  ? 49  PRO A C   1 
ATOM   289  O O   . PRO A 1 49  ? 47.353 45.676 44.550 1.00 55.63  ? 49  PRO A O   1 
ATOM   290  C CB  . PRO A 1 49  ? 47.420 46.890 41.555 1.00 53.91  ? 49  PRO A CB  1 
ATOM   291  C CG  . PRO A 1 49  ? 46.527 47.239 40.365 1.00 58.27  ? 49  PRO A CG  1 
ATOM   292  C CD  . PRO A 1 49  ? 45.413 46.261 40.285 1.00 48.91  ? 49  PRO A CD  1 
ATOM   293  N N   . GLU A 1 50  ? 45.449 46.733 43.946 1.00 58.20  ? 50  GLU A N   1 
ATOM   294  C CA  . GLU A 1 50  ? 45.090 47.127 45.307 1.00 58.98  ? 50  GLU A CA  1 
ATOM   295  C C   . GLU A 1 50  ? 44.311 46.030 45.991 1.00 60.64  ? 50  GLU A C   1 
ATOM   296  O O   . GLU A 1 50  ? 44.005 46.136 47.178 1.00 62.79  ? 50  GLU A O   1 
ATOM   297  C CB  . GLU A 1 50  ? 44.097 48.254 45.350 1.00 60.37  ? 50  GLU A CB  1 
ATOM   298  C CG  . GLU A 1 50  ? 42.668 47.817 45.284 1.00 58.32  ? 50  GLU A CG  1 
ATOM   299  C CD  . GLU A 1 50  ? 42.008 48.592 44.163 1.00 51.39  ? 50  GLU A CD  1 
ATOM   300  O OE1 . GLU A 1 50  ? 40.760 48.705 44.092 1.00 53.72  ? 50  GLU A OE1 1 
ATOM   301  O OE2 . GLU A 1 50  ? 42.800 49.051 43.297 1.00 46.22  ? 50  GLU A OE2 1 
ATOM   302  N N   . GLN A 1 51  ? 44.000 44.985 45.249 1.00 57.21  ? 51  GLN A N   1 
ATOM   303  C CA  . GLN A 1 51  ? 43.267 43.898 45.835 1.00 59.30  ? 51  GLN A CA  1 
ATOM   304  C C   . GLN A 1 51  ? 44.183 42.713 46.075 1.00 64.20  ? 51  GLN A C   1 
ATOM   305  O O   . GLN A 1 51  ? 43.723 41.638 46.428 1.00 67.09  ? 51  GLN A O   1 
ATOM   306  C CB  . GLN A 1 51  ? 42.114 43.502 44.949 1.00 58.85  ? 51  GLN A CB  1 
ATOM   307  C CG  . GLN A 1 51  ? 41.049 44.559 44.969 1.00 23.60  ? 51  GLN A CG  1 
ATOM   308  C CD  . GLN A 1 51  ? 40.235 44.543 43.741 1.00 18.84  ? 51  GLN A CD  1 
ATOM   309  O OE1 . GLN A 1 51  ? 40.717 44.074 42.716 1.00 39.26  ? 51  GLN A OE1 1 
ATOM   310  N NE2 . GLN A 1 51  ? 38.970 45.002 43.822 1.00 19.06  ? 51  GLN A NE2 1 
ATOM   311  N N   . MET A 1 52  ? 45.487 42.911 45.897 1.00 52.00  ? 52  MET A N   1 
ATOM   312  C CA  . MET A 1 52  ? 46.427 41.819 46.131 1.00 51.79  ? 52  MET A CA  1 
ATOM   313  C C   . MET A 1 52  ? 46.774 41.712 47.607 1.00 61.38  ? 52  MET A C   1 
ATOM   314  O O   . MET A 1 52  ? 46.845 40.607 48.162 1.00 64.32  ? 52  MET A O   1 
ATOM   315  C CB  . MET A 1 52  ? 47.662 41.887 45.272 1.00 52.87  ? 52  MET A CB  1 
ATOM   316  C CG  . MET A 1 52  ? 48.029 40.556 44.603 1.00 55.17  ? 52  MET A CG  1 
ATOM   317  S SD  . MET A 1 52  ? 47.249 40.328 42.952 1.00 60.93  ? 52  MET A SD  1 
ATOM   318  C CE  . MET A 1 52  ? 48.056 41.621 42.011 1.00 61.28  ? 52  MET A CE  1 
ATOM   319  N N   . ARG A 1 53  ? 46.984 42.875 48.221 1.00 51.16  ? 53  ARG A N   1 
ATOM   320  C CA  . ARG A 1 53  ? 47.332 43.011 49.638 1.00 48.45  ? 53  ARG A CA  1 
ATOM   321  C C   . ARG A 1 53  ? 46.156 42.564 50.510 1.00 41.32  ? 53  ARG A C   1 
ATOM   322  O O   . ARG A 1 53  ? 46.206 42.567 51.739 1.00 42.27  ? 53  ARG A O   1 
ATOM   323  C CB  . ARG A 1 53  ? 47.650 44.542 49.796 1.00 62.62  ? 53  ARG A CB  1 
ATOM   324  C CG  . ARG A 1 53  ? 48.156 45.361 48.468 1.00 62.01  ? 53  ARG A CG  1 
ATOM   325  C CD  . ARG A 1 53  ? 49.504 46.030 48.631 1.00 64.56  ? 53  ARG A CD  1 
ATOM   326  N NE  . ARG A 1 53  ? 49.589 46.857 49.840 1.00 74.15  ? 53  ARG A NE  1 
ATOM   327  C CZ  . ARG A 1 53  ? 50.425 46.659 50.859 1.00 72.70  ? 53  ARG A CZ  1 
ATOM   328  N NH1 . ARG A 1 53  ? 51.255 45.622 50.771 1.00 74.49  ? 53  ARG A NH1 1 
ATOM   329  N NH2 . ARG A 1 53  ? 50.432 47.481 51.952 1.00 13.93  ? 53  ARG A NH2 1 
ATOM   330  N N   . ILE A 1 54  ? 45.101 42.185 49.819 1.00 32.82  ? 54  ILE A N   1 
ATOM   331  C CA  . ILE A 1 54  ? 43.863 41.717 50.436 1.00 29.78  ? 54  ILE A CA  1 
ATOM   332  C C   . ILE A 1 54  ? 44.019 40.296 50.996 1.00 41.66  ? 54  ILE A C   1 
ATOM   333  O O   . ILE A 1 54  ? 43.515 40.015 52.086 1.00 45.85  ? 54  ILE A O   1 
ATOM   334  C CB  . ILE A 1 54  ? 42.730 41.633 49.292 1.00 29.51  ? 54  ILE A CB  1 
ATOM   335  C CG1 . ILE A 1 54  ? 41.287 41.931 49.638 1.00 29.35  ? 54  ILE A CG1 1 
ATOM   336  C CG2 . ILE A 1 54  ? 42.645 40.319 48.598 1.00 24.81  ? 54  ILE A CG2 1 
ATOM   337  C CD1 . ILE A 1 54  ? 40.369 41.574 48.428 1.00 17.54  ? 54  ILE A CD1 1 
ATOM   338  N N   . TYR A 1 55  ? 44.703 39.414 50.252 1.00 40.18  ? 55  TYR A N   1 
ATOM   339  C CA  . TYR A 1 55  ? 44.913 38.032 50.677 1.00 34.78  ? 55  TYR A CA  1 
ATOM   340  C C   . TYR A 1 55  ? 45.477 38.044 52.070 1.00 32.55  ? 55  TYR A C   1 
ATOM   341  O O   . TYR A 1 55  ? 44.990 37.326 52.941 1.00 43.95  ? 55  TYR A O   1 
ATOM   342  C CB  . TYR A 1 55  ? 45.499 37.111 49.605 1.00 30.15  ? 55  TYR A CB  1 
ATOM   343  C CG  . TYR A 1 55  ? 44.480 37.260 48.455 1.00 16.01  ? 55  TYR A CG  1 
ATOM   344  C CD1 . TYR A 1 55  ? 44.711 38.059 47.301 1.00 14.68  ? 55  TYR A CD1 1 
ATOM   345  C CD2 . TYR A 1 55  ? 43.291 36.663 48.550 1.00 10.72  ? 55  TYR A CD2 1 
ATOM   346  C CE1 . TYR A 1 55  ? 43.755 38.174 46.301 1.00 1.00   ? 55  TYR A CE1 1 
ATOM   347  C CE2 . TYR A 1 55  ? 42.341 36.762 47.567 1.00 9.70   ? 55  TYR A CE2 1 
ATOM   348  C CZ  . TYR A 1 55  ? 42.564 37.512 46.475 1.00 22.48  ? 55  TYR A CZ  1 
ATOM   349  O OH  . TYR A 1 55  ? 41.502 37.545 45.553 1.00 21.20  ? 55  TYR A OH  1 
ATOM   350  N N   . SER A 1 56  ? 46.487 38.857 52.266 1.00 25.84  ? 56  SER A N   1 
ATOM   351  C CA  . SER A 1 56  ? 47.077 38.934 53.584 1.00 29.09  ? 56  SER A CA  1 
ATOM   352  C C   . SER A 1 56  ? 45.982 39.335 54.563 1.00 47.78  ? 56  SER A C   1 
ATOM   353  O O   . SER A 1 56  ? 45.838 38.727 55.624 1.00 56.89  ? 56  SER A O   1 
ATOM   354  C CB  . SER A 1 56  ? 48.123 40.009 53.675 1.00 29.18  ? 56  SER A CB  1 
ATOM   355  O OG  . SER A 1 56  ? 49.383 39.458 53.406 1.00 35.19  ? 56  SER A OG  1 
ATOM   356  N N   . THR A 1 57  ? 45.205 40.360 54.192 1.00 42.75  ? 57  THR A N   1 
ATOM   357  C CA  . THR A 1 57  ? 44.112 40.864 55.025 1.00 41.35  ? 57  THR A CA  1 
ATOM   358  C C   . THR A 1 57  ? 43.237 39.725 55.513 1.00 42.45  ? 57  THR A C   1 
ATOM   359  O O   . THR A 1 57  ? 43.313 39.286 56.638 1.00 40.48  ? 57  THR A O   1 
ATOM   360  C CB  . THR A 1 57  ? 43.430 42.140 54.625 1.00 52.77  ? 57  THR A CB  1 
ATOM   361  O OG1 . THR A 1 57  ? 44.243 43.261 55.038 1.00 42.93  ? 57  THR A OG1 1 
ATOM   362  C CG2 . THR A 1 57  ? 42.202 42.159 55.440 1.00 59.05  ? 57  THR A CG2 1 
ATOM   363  N N   . LEU A 1 58  ? 42.379 39.219 54.637 1.00 41.51  ? 58  LEU A N   1 
ATOM   364  C CA  . LEU A 1 58  ? 41.502 38.107 54.976 1.00 35.96  ? 58  LEU A CA  1 
ATOM   365  C C   . LEU A 1 58  ? 42.339 36.874 55.402 1.00 38.91  ? 58  LEU A C   1 
ATOM   366  O O   . LEU A 1 58  ? 41.810 35.799 55.674 1.00 24.09  ? 58  LEU A O   1 
ATOM   367  C CB  . LEU A 1 58  ? 40.784 37.822 53.655 1.00 34.81  ? 58  LEU A CB  1 
ATOM   368  C CG  . LEU A 1 58  ? 39.319 37.469 53.698 1.00 40.00  ? 58  LEU A CG  1 
ATOM   369  C CD1 . LEU A 1 58  ? 38.832 37.092 52.315 1.00 37.02  ? 58  LEU A CD1 1 
ATOM   370  C CD2 . LEU A 1 58  ? 39.125 36.330 54.661 1.00 42.25  ? 58  LEU A CD2 1 
ATOM   371  N N   . ASP A 1 59  ? 43.662 37.005 55.465 1.00 40.94  ? 59  ASP A N   1 
ATOM   372  C CA  . ASP A 1 59  ? 44.482 35.880 55.866 1.00 43.30  ? 59  ASP A CA  1 
ATOM   373  C C   . ASP A 1 59  ? 44.695 35.908 57.373 1.00 58.01  ? 59  ASP A C   1 
ATOM   374  O O   . ASP A 1 59  ? 45.487 35.139 57.917 1.00 58.47  ? 59  ASP A O   1 
ATOM   375  C CB  . ASP A 1 59  ? 45.789 35.647 55.056 1.00 42.05  ? 59  ASP A CB  1 
ATOM   376  C CG  . ASP A 1 59  ? 45.862 34.234 54.389 1.00 51.87  ? 59  ASP A CG  1 
ATOM   377  O OD1 . ASP A 1 59  ? 45.146 33.283 54.815 1.00 46.72  ? 59  ASP A OD1 1 
ATOM   378  O OD2 . ASP A 1 59  ? 46.663 34.025 53.428 1.00 78.22  ? 59  ASP A OD2 1 
ATOM   379  N N   . GLN A 1 60  ? 43.975 36.799 58.051 1.00 64.70  ? 60  GLN A N   1 
ATOM   380  C CA  . GLN A 1 60  ? 44.102 36.916 59.498 1.00 74.58  ? 60  GLN A CA  1 
ATOM   381  C C   . GLN A 1 60  ? 42.770 36.695 60.226 1.00 88.33  ? 60  GLN A C   1 
ATOM   382  O O   . GLN A 1 60  ? 42.731 35.950 61.197 1.00 96.36  ? 60  GLN A O   1 
ATOM   383  C CB  . GLN A 1 60  ? 44.747 38.316 59.735 1.00 79.62  ? 60  GLN A CB  1 
ATOM   384  C CG  . GLN A 1 60  ? 45.374 39.028 58.442 1.00 100.00 ? 60  GLN A CG  1 
ATOM   385  C CD  . GLN A 1 60  ? 45.151 40.597 58.320 1.00 65.02  ? 60  GLN A CD  1 
ATOM   386  O OE1 . GLN A 1 60  ? 44.138 41.087 57.803 1.00 29.07  ? 60  GLN A OE1 1 
ATOM   387  N NE2 . GLN A 1 60  ? 46.086 41.370 58.890 1.00 51.08  ? 60  GLN A NE2 1 
ATOM   388  N N   . PHE A 1 61  ? 41.700 37.342 59.748 1.00 79.72  ? 61  PHE A N   1 
ATOM   389  C CA  . PHE A 1 61  ? 40.324 37.284 60.275 1.00 78.59  ? 61  PHE A CA  1 
ATOM   390  C C   . PHE A 1 61  ? 39.944 36.024 61.069 1.00 85.79  ? 61  PHE A C   1 
ATOM   391  O O   . PHE A 1 61  ? 40.396 35.811 62.183 1.00 81.76  ? 61  PHE A O   1 
ATOM   392  C CB  . PHE A 1 61  ? 39.561 36.964 59.043 1.00 79.74  ? 61  PHE A CB  1 
ATOM   393  C CG  . PHE A 1 61  ? 38.774 38.027 58.588 1.00 79.33  ? 61  PHE A CG  1 
ATOM   394  C CD1 . PHE A 1 61  ? 39.375 39.079 57.945 1.00 80.99  ? 61  PHE A CD1 1 
ATOM   395  C CD2 . PHE A 1 61  ? 37.430 37.992 58.828 1.00 81.11  ? 61  PHE A CD2 1 
ATOM   396  C CE1 . PHE A 1 61  ? 38.597 40.097 57.510 1.00 83.54  ? 61  PHE A CE1 1 
ATOM   397  C CE2 . PHE A 1 61  ? 36.643 39.006 58.402 1.00 85.22  ? 61  PHE A CE2 1 
ATOM   398  C CZ  . PHE A 1 61  ? 37.244 40.069 57.751 1.00 83.24  ? 61  PHE A CZ  1 
ATOM   399  N N   . ASN A 1 62  ? 39.091 35.205 60.430 1.00 90.90  ? 62  ASN A N   1 
ATOM   400  C CA  . ASN A 1 62  ? 38.539 33.913 60.906 1.00 91.63  ? 62  ASN A CA  1 
ATOM   401  C C   . ASN A 1 62  ? 38.019 33.194 59.650 1.00 96.44  ? 62  ASN A C   1 
ATOM   402  O O   . ASN A 1 62  ? 36.911 32.647 59.647 1.00 100.00 ? 62  ASN A O   1 
ATOM   403  C CB  . ASN A 1 62  ? 37.301 34.362 61.783 1.00 84.31  ? 62  ASN A CB  1 
ATOM   404  C CG  . ASN A 1 62  ? 36.748 33.305 62.748 1.00 74.76  ? 62  ASN A CG  1 
ATOM   405  O OD1 . ASN A 1 62  ? 36.744 33.611 63.923 1.00 59.41  ? 62  ASN A OD1 1 
ATOM   406  N ND2 . ASN A 1 62  ? 36.228 32.135 62.294 1.00 42.22  ? 62  ASN A ND2 1 
ATOM   407  N N   . PRO A 1 63  ? 38.837 33.214 58.563 1.00 84.71  ? 63  PRO A N   1 
ATOM   408  C CA  . PRO A 1 63  ? 38.437 32.578 57.297 1.00 82.84  ? 63  PRO A CA  1 
ATOM   409  C C   . PRO A 1 63  ? 38.828 31.115 57.172 1.00 83.58  ? 63  PRO A C   1 
ATOM   410  O O   . PRO A 1 63  ? 40.011 30.789 57.062 1.00 79.68  ? 63  PRO A O   1 
ATOM   411  C CB  . PRO A 1 63  ? 39.390 33.266 56.371 1.00 84.38  ? 63  PRO A CB  1 
ATOM   412  C CG  . PRO A 1 63  ? 40.715 33.476 57.175 1.00 86.46  ? 63  PRO A CG  1 
ATOM   413  C CD  . PRO A 1 63  ? 40.326 33.145 58.611 1.00 81.72  ? 63  PRO A CD  1 
ATOM   414  N N   . THR A 1 64  ? 37.857 30.222 57.179 1.00 80.53  ? 64  THR A N   1 
ATOM   415  C CA  . THR A 1 64  ? 38.170 28.804 57.046 1.00 78.61  ? 64  THR A CA  1 
ATOM   416  C C   . THR A 1 64  ? 38.274 28.487 55.561 1.00 73.65  ? 64  THR A C   1 
ATOM   417  O O   . THR A 1 64  ? 37.289 28.118 54.940 1.00 74.62  ? 64  THR A O   1 
ATOM   418  C CB  . THR A 1 64  ? 37.841 27.718 58.163 1.00 99.72  ? 64  THR A CB  1 
ATOM   419  O OG1 . THR A 1 64  ? 37.876 28.329 59.481 1.00 90.99  ? 64  THR A OG1 1 
ATOM   420  C CG2 . THR A 1 64  ? 38.852 26.528 58.130 1.00 100.00 ? 64  THR A CG2 1 
ATOM   421  N N   . SER A 1 65  ? 39.483 28.677 55.033 1.00 65.03  ? 65  SER A N   1 
ATOM   422  C CA  . SER A 1 65  ? 39.879 28.473 53.650 1.00 63.21  ? 65  SER A CA  1 
ATOM   423  C C   . SER A 1 65  ? 39.955 27.024 53.214 1.00 58.84  ? 65  SER A C   1 
ATOM   424  O O   . SER A 1 65  ? 40.612 26.196 53.862 1.00 52.81  ? 65  SER A O   1 
ATOM   425  C CB  . SER A 1 65  ? 41.307 29.086 53.504 1.00 69.53  ? 65  SER A CB  1 
ATOM   426  O OG  . SER A 1 65  ? 42.245 28.811 54.596 1.00 51.73  ? 65  SER A OG  1 
ATOM   427  N N   . LEU A 1 66  ? 39.281 26.737 52.101 1.00 51.74  ? 66  LEU A N   1 
ATOM   428  C CA  . LEU A 1 66  ? 39.265 25.389 51.563 1.00 51.28  ? 66  LEU A CA  1 
ATOM   429  C C   . LEU A 1 66  ? 39.917 25.377 50.193 1.00 54.92  ? 66  LEU A C   1 
ATOM   430  O O   . LEU A 1 66  ? 40.023 26.418 49.559 1.00 64.52  ? 66  LEU A O   1 
ATOM   431  C CB  . LEU A 1 66  ? 37.811 24.920 51.223 1.00 50.46  ? 66  LEU A CB  1 
ATOM   432  C CG  . LEU A 1 66  ? 36.492 25.607 51.635 1.00 52.98  ? 66  LEU A CG  1 
ATOM   433  C CD1 . LEU A 1 66  ? 36.599 26.460 52.838 1.00 49.93  ? 66  LEU A CD1 1 
ATOM   434  C CD2 . LEU A 1 66  ? 35.843 26.399 50.530 1.00 49.98  ? 66  LEU A CD2 1 
ATOM   435  N N   . PRO A 1 67  ? 40.288 24.204 49.728 1.00 39.03  ? 67  PRO A N   1 
ATOM   436  C CA  . PRO A 1 67  ? 40.899 24.089 48.423 1.00 44.75  ? 67  PRO A CA  1 
ATOM   437  C C   . PRO A 1 67  ? 39.797 23.976 47.323 1.00 60.16  ? 67  PRO A C   1 
ATOM   438  O O   . PRO A 1 67  ? 38.647 23.655 47.612 1.00 67.31  ? 67  PRO A O   1 
ATOM   439  C CB  . PRO A 1 67  ? 41.848 22.926 48.579 1.00 44.82  ? 67  PRO A CB  1 
ATOM   440  C CG  . PRO A 1 67  ? 41.903 22.699 50.076 1.00 45.46  ? 67  PRO A CG  1 
ATOM   441  C CD  . PRO A 1 67  ? 40.570 23.036 50.542 1.00 37.43  ? 67  PRO A CD  1 
ATOM   442  N N   . GLY A 1 68  ? 40.147 24.236 46.053 1.00 52.78  ? 68  GLY A N   1 
ATOM   443  C CA  . GLY A 1 68  ? 39.150 24.151 44.979 1.00 50.58  ? 68  GLY A CA  1 
ATOM   444  C C   . GLY A 1 68  ? 39.398 25.043 43.745 1.00 41.13  ? 68  GLY A C   1 
ATOM   445  O O   . GLY A 1 68  ? 40.466 25.586 43.539 1.00 40.54  ? 68  GLY A O   1 
ATOM   446  N N   . GLY A 1 69  ? 38.382 25.172 42.924 1.00 31.58  ? 69  GLY A N   1 
ATOM   447  C CA  . GLY A 1 69  ? 38.470 25.968 41.720 1.00 37.47  ? 69  GLY A CA  1 
ATOM   448  C C   . GLY A 1 69  ? 37.310 25.619 40.797 1.00 59.22  ? 69  GLY A C   1 
ATOM   449  O O   . GLY A 1 69  ? 36.200 26.171 40.905 1.00 61.71  ? 69  GLY A O   1 
ATOM   450  N N   . SER A 1 70  ? 37.591 24.700 39.890 1.00 58.76  ? 70  SER A N   1 
ATOM   451  C CA  . SER A 1 70  ? 36.617 24.228 38.925 1.00 57.45  ? 70  SER A CA  1 
ATOM   452  C C   . SER A 1 70  ? 36.817 22.744 38.763 1.00 70.09  ? 70  SER A C   1 
ATOM   453  O O   . SER A 1 70  ? 35.912 21.943 39.021 1.00 74.63  ? 70  SER A O   1 
ATOM   454  C CB  . SER A 1 70  ? 36.796 24.842 37.603 1.00 53.04  ? 70  SER A CB  1 
ATOM   455  O OG  . SER A 1 70  ? 35.459 24.797 37.164 1.00 35.53  ? 70  SER A OG  1 
ATOM   456  N N   . ALA A 1 71  ? 38.028 22.399 38.332 1.00 58.88  ? 71  ALA A N   1 
ATOM   457  C CA  . ALA A 1 71  ? 38.385 21.012 38.147 1.00 52.26  ? 71  ALA A CA  1 
ATOM   458  C C   . ALA A 1 71  ? 38.545 20.471 39.555 1.00 46.37  ? 71  ALA A C   1 
ATOM   459  O O   . ALA A 1 71  ? 38.188 19.331 39.817 1.00 42.71  ? 71  ALA A O   1 
ATOM   460  C CB  . ALA A 1 71  ? 39.699 20.842 37.362 1.00 52.48  ? 71  ALA A CB  1 
ATOM   461  N N   . LEU A 1 72  ? 39.084 21.326 40.431 1.00 43.16  ? 72  LEU A N   1 
ATOM   462  C CA  . LEU A 1 72  ? 39.321 21.004 41.837 1.00 36.57  ? 72  LEU A CA  1 
ATOM   463  C C   . LEU A 1 72  ? 38.040 20.683 42.576 1.00 45.61  ? 72  LEU A C   1 
ATOM   464  O O   . LEU A 1 72  ? 37.929 19.620 43.188 1.00 53.50  ? 72  LEU A O   1 
ATOM   465  C CB  . LEU A 1 72  ? 39.983 22.111 42.578 1.00 29.94  ? 72  LEU A CB  1 
ATOM   466  C CG  . LEU A 1 72  ? 40.574 21.278 43.681 1.00 32.50  ? 72  LEU A CG  1 
ATOM   467  C CD1 . LEU A 1 72  ? 40.850 19.842 43.225 1.00 29.22  ? 72  LEU A CD1 1 
ATOM   468  C CD2 . LEU A 1 72  ? 41.862 21.933 44.210 1.00 37.76  ? 72  LEU A CD2 1 
ATOM   469  N N   . ASN A 1 73  ? 37.082 21.604 42.526 1.00 31.52  ? 73  ASN A N   1 
ATOM   470  C CA  . ASN A 1 73  ? 35.841 21.382 43.200 1.00 25.47  ? 73  ASN A CA  1 
ATOM   471  C C   . ASN A 1 73  ? 35.144 20.191 42.603 1.00 43.81  ? 73  ASN A C   1 
ATOM   472  O O   . ASN A 1 73  ? 34.686 19.310 43.337 1.00 51.21  ? 73  ASN A O   1 
ATOM   473  C CB  . ASN A 1 73  ? 35.023 22.545 43.126 1.00 15.76  ? 73  ASN A CB  1 
ATOM   474  C CG  . ASN A 1 73  ? 35.586 23.550 43.909 1.00 44.24  ? 73  ASN A CG  1 
ATOM   475  O OD1 . ASN A 1 73  ? 36.411 23.278 44.771 1.00 39.12  ? 73  ASN A OD1 1 
ATOM   476  N ND2 . ASN A 1 73  ? 35.233 24.755 43.616 1.00 46.78  ? 73  ASN A ND2 1 
ATOM   477  N N   . SER A 1 74  ? 35.073 20.172 41.268 1.00 35.73  ? 74  SER A N   1 
ATOM   478  C CA  . SER A 1 74  ? 34.433 19.078 40.544 1.00 33.90  ? 74  SER A CA  1 
ATOM   479  C C   . SER A 1 74  ? 35.002 17.739 41.054 1.00 28.74  ? 74  SER A C   1 
ATOM   480  O O   . SER A 1 74  ? 34.262 16.805 41.364 1.00 25.01  ? 74  SER A O   1 
ATOM   481  C CB  . SER A 1 74  ? 34.752 19.164 39.073 1.00 42.67  ? 74  SER A CB  1 
ATOM   482  O OG  . SER A 1 74  ? 33.720 19.859 38.390 1.00 50.55  ? 74  SER A OG  1 
ATOM   483  N N   . VAL A 1 75  ? 36.358 17.659 41.134 1.00 25.29  ? 75  VAL A N   1 
ATOM   484  C CA  . VAL A 1 75  ? 37.015 16.403 41.599 1.00 18.87  ? 75  VAL A CA  1 
ATOM   485  C C   . VAL A 1 75  ? 36.507 16.057 43.002 1.00 44.73  ? 75  VAL A C   1 
ATOM   486  O O   . VAL A 1 75  ? 35.941 14.977 43.210 1.00 55.34  ? 75  VAL A O   1 
ATOM   487  C CB  . VAL A 1 75  ? 38.548 16.488 41.631 1.00 22.15  ? 75  VAL A CB  1 
ATOM   488  C CG1 . VAL A 1 75  ? 39.144 15.988 42.949 1.00 25.54  ? 75  VAL A CG1 1 
ATOM   489  C CG2 . VAL A 1 75  ? 39.205 15.624 40.538 1.00 20.39  ? 75  VAL A CG2 1 
ATOM   490  N N   . ARG A 1 76  ? 36.715 16.984 43.937 1.00 40.34  ? 76  ARG A N   1 
ATOM   491  C CA  . ARG A 1 76  ? 36.239 16.820 45.346 1.00 27.80  ? 76  ARG A CA  1 
ATOM   492  C C   . ARG A 1 76  ? 35.142 15.826 45.425 1.00 22.74  ? 76  ARG A C   1 
ATOM   493  O O   . ARG A 1 76  ? 35.283 14.775 46.053 1.00 30.47  ? 76  ARG A O   1 
ATOM   494  C CB  . ARG A 1 76  ? 35.611 18.107 45.885 1.00 19.78  ? 76  ARG A CB  1 
ATOM   495  C CG  . ARG A 1 76  ? 36.607 19.023 46.470 1.00 29.11  ? 76  ARG A CG  1 
ATOM   496  C CD  . ARG A 1 76  ? 37.929 18.791 45.832 1.00 32.43  ? 76  ARG A CD  1 
ATOM   497  N NE  . ARG A 1 76  ? 38.992 19.544 46.421 1.00 35.66  ? 76  ARG A NE  1 
ATOM   498  C CZ  . ARG A 1 76  ? 38.840 20.574 47.238 1.00 51.12  ? 76  ARG A CZ  1 
ATOM   499  N NH1 . ARG A 1 76  ? 37.634 21.008 47.605 1.00 40.12  ? 76  ARG A NH1 1 
ATOM   500  N NH2 . ARG A 1 76  ? 39.877 21.251 47.749 1.00 59.19  ? 76  ARG A NH2 1 
ATOM   501  N N   . VAL A 1 77  ? 34.078 16.256 44.779 1.00 15.43  ? 77  VAL A N   1 
ATOM   502  C CA  . VAL A 1 77  ? 32.852 15.494 44.674 1.00 23.99  ? 77  VAL A CA  1 
ATOM   503  C C   . VAL A 1 77  ? 33.166 14.047 44.501 1.00 33.54  ? 77  VAL A C   1 
ATOM   504  O O   . VAL A 1 77  ? 32.989 13.243 45.419 1.00 34.85  ? 77  VAL A O   1 
ATOM   505  C CB  . VAL A 1 77  ? 32.073 15.898 43.441 1.00 26.19  ? 77  VAL A CB  1 
ATOM   506  C CG1 . VAL A 1 77  ? 30.948 14.900 43.139 1.00 14.22  ? 77  VAL A CG1 1 
ATOM   507  C CG2 . VAL A 1 77  ? 31.420 17.259 43.558 1.00 30.76  ? 77  VAL A CG2 1 
ATOM   508  N N   . VAL A 1 78  ? 33.582 13.848 43.307 1.00 26.46  ? 78  VAL A N   1 
ATOM   509  C CA  . VAL A 1 78  ? 34.022 12.602 42.757 1.00 20.28  ? 78  VAL A CA  1 
ATOM   510  C C   . VAL A 1 78  ? 34.702 11.808 43.862 1.00 29.52  ? 78  VAL A C   1 
ATOM   511  O O   . VAL A 1 78  ? 34.312 10.668 44.179 1.00 29.78  ? 78  VAL A O   1 
ATOM   512  C CB  . VAL A 1 78  ? 35.004 13.059 41.683 1.00 11.37  ? 78  VAL A CB  1 
ATOM   513  C CG1 . VAL A 1 78  ? 36.108 12.081 41.378 1.00 1.00   ? 78  VAL A CG1 1 
ATOM   514  C CG2 . VAL A 1 78  ? 34.324 13.389 40.358 1.00 16.75  ? 78  VAL A CG2 1 
ATOM   515  N N   . GLN A 1 79  ? 35.677 12.514 44.372 1.00 31.52  ? 79  GLN A N   1 
ATOM   516  C CA  . GLN A 1 79  ? 36.570 12.083 45.423 1.00 32.71  ? 79  GLN A CA  1 
ATOM   517  C C   . GLN A 1 79  ? 35.856 11.630 46.687 1.00 56.02  ? 79  GLN A C   1 
ATOM   518  O O   . GLN A 1 79  ? 36.076 10.516 47.180 1.00 53.84  ? 79  GLN A O   1 
ATOM   519  C CB  . GLN A 1 79  ? 37.475 13.212 45.835 1.00 29.41  ? 79  GLN A CB  1 
ATOM   520  C CG  . GLN A 1 79  ? 38.121 12.913 47.164 1.00 77.15  ? 79  GLN A CG  1 
ATOM   521  C CD  . GLN A 1 79  ? 38.575 11.461 47.253 1.00 73.25  ? 79  GLN A CD  1 
ATOM   522  O OE1 . GLN A 1 79  ? 37.996 10.698 48.027 1.00 24.87  ? 79  GLN A OE1 1 
ATOM   523  N NE2 . GLN A 1 79  ? 39.572 11.022 46.511 1.00 22.02  ? 79  GLN A NE2 1 
ATOM   524  N N   . LYS A 1 80  ? 35.024 12.499 47.222 1.00 56.34  ? 80  LYS A N   1 
ATOM   525  C CA  . LYS A 1 80  ? 34.276 12.170 48.439 1.00 50.15  ? 80  LYS A CA  1 
ATOM   526  C C   . LYS A 1 80  ? 33.189 11.175 48.067 1.00 40.22  ? 80  LYS A C   1 
ATOM   527  O O   . LYS A 1 80  ? 32.784 10.325 48.874 1.00 40.18  ? 80  LYS A O   1 
ATOM   528  C CB  . LYS A 1 80  ? 33.658 13.429 49.059 1.00 49.09  ? 80  LYS A CB  1 
ATOM   529  C CG  . LYS A 1 80  ? 34.682 14.264 49.854 1.00 77.56  ? 80  LYS A CG  1 
ATOM   530  C CD  . LYS A 1 80  ? 34.557 14.110 51.379 1.00 80.40  ? 80  LYS A CD  1 
ATOM   531  C CE  . LYS A 1 80  ? 33.685 15.196 52.023 1.00 32.19  ? 80  LYS A CE  1 
ATOM   532  N NZ  . LYS A 1 80  ? 34.220 15.690 53.302 1.00 50.45  ? 80  LYS A NZ  1 
ATOM   533  N N   . LEU A 1 81  ? 32.752 11.303 46.836 1.00 27.10  ? 81  LEU A N   1 
ATOM   534  C CA  . LEU A 1 81  ? 31.722 10.443 46.306 1.00 28.39  ? 81  LEU A CA  1 
ATOM   535  C C   . LEU A 1 81  ? 32.149 9.025  46.399 1.00 31.09  ? 81  LEU A C   1 
ATOM   536  O O   . LEU A 1 81  ? 31.313 8.108  46.463 1.00 21.32  ? 81  LEU A O   1 
ATOM   537  C CB  . LEU A 1 81  ? 31.424 10.771 44.884 1.00 27.59  ? 81  LEU A CB  1 
ATOM   538  C CG  . LEU A 1 81  ? 29.979 11.101 44.811 1.00 27.70  ? 81  LEU A CG  1 
ATOM   539  C CD1 . LEU A 1 81  ? 29.572 12.053 45.948 1.00 30.56  ? 81  LEU A CD1 1 
ATOM   540  C CD2 . LEU A 1 81  ? 29.564 11.744 43.527 1.00 14.23  ? 81  LEU A CD2 1 
ATOM   541  N N   . LEU A 1 82  ? 33.415 8.897  46.414 1.00 29.18  ? 82  LEU A N   1 
ATOM   542  C CA  . LEU A 1 82  ? 34.036 7.638  46.529 1.00 33.70  ? 82  LEU A CA  1 
ATOM   543  C C   . LEU A 1 82  ? 34.095 7.259  48.002 1.00 58.06  ? 82  LEU A C   1 
ATOM   544  O O   . LEU A 1 82  ? 33.251 6.489  48.489 1.00 63.02  ? 82  LEU A O   1 
ATOM   545  C CB  . LEU A 1 82  ? 35.415 7.717  45.955 1.00 32.88  ? 82  LEU A CB  1 
ATOM   546  C CG  . LEU A 1 82  ? 35.834 6.364  45.537 1.00 42.99  ? 82  LEU A CG  1 
ATOM   547  C CD1 . LEU A 1 82  ? 36.546 5.622  46.651 1.00 43.76  ? 82  LEU A CD1 1 
ATOM   548  C CD2 . LEU A 1 82  ? 34.627 5.506  45.146 1.00 57.69  ? 82  LEU A CD2 1 
ATOM   549  N N   . ARG A 1 83  ? 35.098 7.819  48.621 1.00 56.69  ? 83  ARG A N   1 
ATOM   550  C CA  . ARG A 1 83  ? 35.393 7.683  50.053 1.00 56.89  ? 83  ARG A CA  1 
ATOM   551  C C   . ARG A 1 83  ? 36.841 7.204  50.264 1.00 67.36  ? 83  ARG A C   1 
ATOM   552  O O   . ARG A 1 83  ? 37.421 7.420  51.333 1.00 68.24  ? 83  ARG A O   1 
ATOM   553  C CB  . ARG A 1 83  ? 34.374 6.754  50.781 1.00 62.22  ? 83  ARG A CB  1 
ATOM   554  C CG  . ARG A 1 83  ? 32.980 7.461  51.078 1.00 62.83  ? 83  ARG A CG  1 
ATOM   555  C CD  . ARG A 1 83  ? 32.826 8.118  52.502 1.00 30.26  ? 83  ARG A CD  1 
ATOM   556  N NE  . ARG A 1 83  ? 33.860 9.130  52.775 1.00 72.26  ? 83  ARG A NE  1 
ATOM   557  C CZ  . ARG A 1 83  ? 33.673 10.472 52.844 1.00 54.47  ? 83  ARG A CZ  1 
ATOM   558  N NH1 . ARG A 1 83  ? 32.469 11.032 52.682 1.00 8.29   ? 83  ARG A NH1 1 
ATOM   559  N NH2 . ARG A 1 83  ? 34.673 11.349 53.071 1.00 31.96  ? 83  ARG A NH2 1 
ATOM   560  N N   . LYS A 1 84  ? 37.411 6.548  49.251 1.00 63.63  ? 84  LYS A N   1 
ATOM   561  C CA  . LYS A 1 84  ? 38.774 6.034  49.317 1.00 56.21  ? 84  LYS A CA  1 
ATOM   562  C C   . LYS A 1 84  ? 39.866 7.045  48.966 1.00 59.39  ? 84  LYS A C   1 
ATOM   563  O O   . LYS A 1 84  ? 39.599 8.036  48.282 1.00 62.91  ? 84  LYS A O   1 
ATOM   564  C CB  . LYS A 1 84  ? 38.935 4.586  49.095 1.00 48.21  ? 84  LYS A CB  1 
ATOM   565  C CG  . LYS A 1 84  ? 40.322 3.987  49.352 1.00 45.59  ? 84  LYS A CG  1 
ATOM   566  C CD  . LYS A 1 84  ? 41.005 3.787  48.008 1.00 31.88  ? 84  LYS A CD  1 
ATOM   567  C CE  . LYS A 1 84  ? 39.907 3.206  47.169 1.00 51.65  ? 84  LYS A CE  1 
ATOM   568  N NZ  . LYS A 1 84  ? 39.325 2.056  47.928 1.00 66.07  ? 84  LYS A NZ  1 
ATOM   569  N N   . PRO A 1 85  ? 41.100 6.783  49.451 1.00 43.96  ? 85  PRO A N   1 
ATOM   570  C CA  . PRO A 1 85  ? 42.248 7.664  49.213 1.00 41.34  ? 85  PRO A CA  1 
ATOM   571  C C   . PRO A 1 85  ? 43.024 7.389  47.928 1.00 46.38  ? 85  PRO A C   1 
ATOM   572  O O   . PRO A 1 85  ? 43.342 6.256  47.614 1.00 39.63  ? 85  PRO A O   1 
ATOM   573  C CB  . PRO A 1 85  ? 43.052 7.453  50.472 1.00 39.87  ? 85  PRO A CB  1 
ATOM   574  C CG  . PRO A 1 85  ? 42.296 6.456  51.305 1.00 38.03  ? 85  PRO A CG  1 
ATOM   575  C CD  . PRO A 1 85  ? 40.932 6.505  50.894 1.00 34.75  ? 85  PRO A CD  1 
ATOM   576  N N   . GLY A 1 86  ? 43.328 8.482  47.206 1.00 46.54  ? 86  GLY A N   1 
ATOM   577  C CA  . GLY A 1 86  ? 44.062 8.472  45.944 1.00 35.77  ? 86  GLY A CA  1 
ATOM   578  C C   . GLY A 1 86  ? 43.218 7.913  44.822 1.00 34.94  ? 86  GLY A C   1 
ATOM   579  O O   . GLY A 1 86  ? 43.757 7.398  43.833 1.00 33.40  ? 86  GLY A O   1 
ATOM   580  N N   . SER A 1 87  ? 41.897 7.995  44.985 1.00 35.56  ? 87  SER A N   1 
ATOM   581  C CA  . SER A 1 87  ? 40.907 7.503  44.005 1.00 40.19  ? 87  SER A CA  1 
ATOM   582  C C   . SER A 1 87  ? 40.658 8.537  42.904 1.00 35.20  ? 87  SER A C   1 
ATOM   583  O O   . SER A 1 87  ? 39.839 8.350  42.003 1.00 26.08  ? 87  SER A O   1 
ATOM   584  C CB  . SER A 1 87  ? 39.497 7.198  44.740 1.00 40.68  ? 87  SER A CB  1 
ATOM   585  O OG  . SER A 1 87  ? 39.171 5.808  44.814 1.00 27.51  ? 87  SER A OG  1 
ATOM   586  N N   . ALA A 1 88  ? 41.375 9.635  43.025 1.00 34.33  ? 88  ALA A N   1 
ATOM   587  C CA  . ALA A 1 88  ? 41.299 10.749 42.110 1.00 36.28  ? 88  ALA A CA  1 
ATOM   588  C C   . ALA A 1 88  ? 42.572 11.515 42.256 1.00 38.31  ? 88  ALA A C   1 
ATOM   589  O O   . ALA A 1 88  ? 42.994 11.797 43.372 1.00 40.28  ? 88  ALA A O   1 
ATOM   590  C CB  . ALA A 1 88  ? 40.166 11.731 42.455 1.00 38.99  ? 88  ALA A CB  1 
ATOM   591  N N   . GLY A 1 89  ? 43.168 11.828 41.138 1.00 33.12  ? 89  GLY A N   1 
ATOM   592  C CA  . GLY A 1 89  ? 44.401 12.561 41.128 1.00 33.40  ? 89  GLY A CA  1 
ATOM   593  C C   . GLY A 1 89  ? 44.134 13.745 40.281 1.00 38.64  ? 89  GLY A C   1 
ATOM   594  O O   . GLY A 1 89  ? 43.190 13.727 39.487 1.00 33.50  ? 89  GLY A O   1 
ATOM   595  N N   . TYR A 1 90  ? 44.945 14.751 40.448 1.00 40.24  ? 90  TYR A N   1 
ATOM   596  C CA  . TYR A 1 90  ? 44.740 15.938 39.660 1.00 37.90  ? 90  TYR A CA  1 
ATOM   597  C C   . TYR A 1 90  ? 46.045 16.702 39.492 1.00 42.45  ? 90  TYR A C   1 
ATOM   598  O O   . TYR A 1 90  ? 46.847 16.861 40.410 1.00 46.75  ? 90  TYR A O   1 
ATOM   599  C CB  . TYR A 1 90  ? 43.554 16.669 40.357 1.00 36.28  ? 90  TYR A CB  1 
ATOM   600  C CG  . TYR A 1 90  ? 43.291 18.113 40.127 1.00 31.59  ? 90  TYR A CG  1 
ATOM   601  C CD1 . TYR A 1 90  ? 42.247 18.542 39.297 1.00 30.96  ? 90  TYR A CD1 1 
ATOM   602  C CD2 . TYR A 1 90  ? 44.087 19.072 40.751 1.00 32.67  ? 90  TYR A CD2 1 
ATOM   603  C CE1 . TYR A 1 90  ? 42.003 19.914 39.093 1.00 37.91  ? 90  TYR A CE1 1 
ATOM   604  C CE2 . TYR A 1 90  ? 43.872 20.432 40.549 1.00 32.56  ? 90  TYR A CE2 1 
ATOM   605  C CZ  . TYR A 1 90  ? 42.836 20.856 39.733 1.00 42.50  ? 90  TYR A CZ  1 
ATOM   606  O OH  . TYR A 1 90  ? 42.685 22.203 39.605 1.00 40.66  ? 90  TYR A OH  1 
ATOM   607  N N   . MET A 1 91  ? 46.292 17.182 38.308 1.00 35.34  ? 91  MET A N   1 
ATOM   608  C CA  . MET A 1 91  ? 47.530 17.918 38.147 1.00 35.11  ? 91  MET A CA  1 
ATOM   609  C C   . MET A 1 91  ? 47.231 19.401 38.043 1.00 49.57  ? 91  MET A C   1 
ATOM   610  O O   . MET A 1 91  ? 46.250 19.790 37.405 1.00 51.75  ? 91  MET A O   1 
ATOM   611  C CB  . MET A 1 91  ? 48.390 17.281 37.147 1.00 35.49  ? 91  MET A CB  1 
ATOM   612  C CG  . MET A 1 91  ? 49.471 16.566 37.878 1.00 34.07  ? 91  MET A CG  1 
ATOM   613  S SD  . MET A 1 91  ? 50.413 15.842 36.631 1.00 27.07  ? 91  MET A SD  1 
ATOM   614  C CE  . MET A 1 91  ? 51.517 15.078 37.777 1.00 21.29  ? 91  MET A CE  1 
ATOM   615  N N   . GLY A 1 92  ? 48.045 20.231 38.698 1.00 48.94  ? 92  GLY A N   1 
ATOM   616  C CA  . GLY A 1 92  ? 47.798 21.676 38.651 1.00 45.53  ? 92  GLY A CA  1 
ATOM   617  C C   . GLY A 1 92  ? 48.963 22.519 39.144 1.00 50.33  ? 92  GLY A C   1 
ATOM   618  O O   . GLY A 1 92  ? 49.679 22.137 40.072 1.00 46.33  ? 92  GLY A O   1 
ATOM   619  N N   . ALA A 1 93  ? 49.123 23.669 38.516 1.00 50.91  ? 93  ALA A N   1 
ATOM   620  C CA  . ALA A 1 93  ? 50.173 24.609 38.844 1.00 44.66  ? 93  ALA A CA  1 
ATOM   621  C C   . ALA A 1 93  ? 49.957 25.427 40.112 1.00 44.52  ? 93  ALA A C   1 
ATOM   622  O O   . ALA A 1 93  ? 48.939 26.113 40.283 1.00 43.17  ? 93  ALA A O   1 
ATOM   623  C CB  . ALA A 1 93  ? 50.402 25.515 37.647 1.00 45.72  ? 93  ALA A CB  1 
ATOM   624  N N   . ILE A 1 94  ? 50.954 25.327 40.973 1.00 39.63  ? 94  ILE A N   1 
ATOM   625  C CA  . ILE A 1 94  ? 51.030 26.005 42.248 1.00 42.65  ? 94  ILE A CA  1 
ATOM   626  C C   . ILE A 1 94  ? 52.379 26.728 42.264 1.00 45.74  ? 94  ILE A C   1 
ATOM   627  O O   . ILE A 1 94  ? 53.226 26.426 41.445 1.00 44.61  ? 94  ILE A O   1 
ATOM   628  C CB  . ILE A 1 94  ? 50.829 24.979 43.450 1.00 47.39  ? 94  ILE A CB  1 
ATOM   629  C CG1 . ILE A 1 94  ? 52.013 24.087 43.796 1.00 49.12  ? 94  ILE A CG1 1 
ATOM   630  C CG2 . ILE A 1 94  ? 49.625 24.179 43.219 1.00 41.90  ? 94  ILE A CG2 1 
ATOM   631  C CD1 . ILE A 1 94  ? 52.363 24.133 45.250 1.00 32.98  ? 94  ILE A CD1 1 
ATOM   632  N N   . GLY A 1 95  ? 52.611 27.674 43.161 1.00 40.48  ? 95  GLY A N   1 
ATOM   633  C CA  . GLY A 1 95  ? 53.915 28.326 43.142 1.00 44.21  ? 95  GLY A CA  1 
ATOM   634  C C   . GLY A 1 95  ? 54.609 27.964 44.436 1.00 43.37  ? 95  GLY A C   1 
ATOM   635  O O   . GLY A 1 95  ? 53.987 27.331 45.273 1.00 44.57  ? 95  GLY A O   1 
ATOM   636  N N   . ASP A 1 96  ? 55.862 28.337 44.634 1.00 36.59  ? 96  ASP A N   1 
ATOM   637  C CA  . ASP A 1 96  ? 56.491 27.985 45.897 1.00 36.48  ? 96  ASP A CA  1 
ATOM   638  C C   . ASP A 1 96  ? 55.848 28.852 46.992 1.00 38.23  ? 96  ASP A C   1 
ATOM   639  O O   . ASP A 1 96  ? 56.509 29.621 47.702 1.00 21.93  ? 96  ASP A O   1 
ATOM   640  C CB  . ASP A 1 96  ? 58.047 27.859 45.810 1.00 39.21  ? 96  ASP A CB  1 
ATOM   641  C CG  . ASP A 1 96  ? 58.564 26.687 46.654 1.00 49.02  ? 96  ASP A CG  1 
ATOM   642  O OD1 . ASP A 1 96  ? 59.447 25.884 46.247 1.00 48.58  ? 96  ASP A OD1 1 
ATOM   643  O OD2 . ASP A 1 96  ? 58.143 26.584 47.846 1.00 57.07  ? 96  ASP A OD2 1 
ATOM   644  N N   . ASP A 1 97  ? 54.529 28.748 47.142 1.00 42.84  ? 97  ASP A N   1 
ATOM   645  C CA  . ASP A 1 97  ? 53.888 29.568 48.168 1.00 42.41  ? 97  ASP A CA  1 
ATOM   646  C C   . ASP A 1 97  ? 53.056 28.838 49.218 1.00 40.00  ? 97  ASP A C   1 
ATOM   647  O O   . ASP A 1 97  ? 52.335 27.872 48.900 1.00 24.08  ? 97  ASP A O   1 
ATOM   648  C CB  . ASP A 1 97  ? 53.660 31.074 47.814 1.00 45.56  ? 97  ASP A CB  1 
ATOM   649  C CG  . ASP A 1 97  ? 52.199 31.454 47.710 1.00 41.18  ? 97  ASP A CG  1 
ATOM   650  O OD1 . ASP A 1 97  ? 51.946 32.713 47.735 1.00 34.82  ? 97  ASP A OD1 1 
ATOM   651  O OD2 . ASP A 1 97  ? 51.368 30.546 47.525 1.00 48.57  ? 97  ASP A OD2 1 
ATOM   652  N N   . PRO A 1 98  ? 53.187 29.329 50.483 1.00 43.32  ? 98  PRO A N   1 
ATOM   653  C CA  . PRO A 1 98  ? 52.460 28.751 51.615 1.00 43.70  ? 98  PRO A CA  1 
ATOM   654  C C   . PRO A 1 98  ? 50.967 28.663 51.299 1.00 39.68  ? 98  PRO A C   1 
ATOM   655  O O   . PRO A 1 98  ? 50.233 27.936 51.968 1.00 44.58  ? 98  PRO A O   1 
ATOM   656  C CB  . PRO A 1 98  ? 52.853 29.636 52.817 1.00 45.40  ? 98  PRO A CB  1 
ATOM   657  C CG  . PRO A 1 98  ? 54.261 29.979 52.525 1.00 41.48  ? 98  PRO A CG  1 
ATOM   658  C CD  . PRO A 1 98  ? 54.161 30.325 51.036 1.00 39.58  ? 98  PRO A CD  1 
ATOM   659  N N   . ARG A 1 99  ? 50.536 29.403 50.282 1.00 26.12  ? 99  ARG A N   1 
ATOM   660  C CA  . ARG A 1 99  ? 49.139 29.373 49.903 1.00 25.71  ? 99  ARG A CA  1 
ATOM   661  C C   . ARG A 1 99  ? 48.960 28.049 49.212 1.00 31.55  ? 99  ARG A C   1 
ATOM   662  O O   . ARG A 1 99  ? 47.848 27.603 48.974 1.00 37.69  ? 99  ARG A O   1 
ATOM   663  C CB  . ARG A 1 99  ? 48.609 30.552 48.995 1.00 17.06  ? 99  ARG A CB  1 
ATOM   664  C CG  . ARG A 1 99  ? 47.318 31.174 49.766 1.00 44.87  ? 99  ARG A CG  1 
ATOM   665  C CD  . ARG A 1 99  ? 46.570 32.430 49.196 1.00 48.69  ? 99  ARG A CD  1 
ATOM   666  N NE  . ARG A 1 99  ? 46.995 33.717 49.781 1.00 23.28  ? 99  ARG A NE  1 
ATOM   667  C CZ  . ARG A 1 99  ? 48.252 34.146 49.936 1.00 44.83  ? 99  ARG A CZ  1 
ATOM   668  N NH1 . ARG A 1 99  ? 49.270 33.400 49.534 1.00 85.82  ? 99  ARG A NH1 1 
ATOM   669  N NH2 . ARG A 1 99  ? 48.519 35.325 50.483 1.00 12.76  ? 99  ARG A NH2 1 
ATOM   670  N N   . GLY A 1 100 ? 50.088 27.427 48.894 1.00 22.69  ? 100 GLY A N   1 
ATOM   671  C CA  . GLY A 1 100 ? 50.030 26.148 48.236 1.00 26.22  ? 100 GLY A CA  1 
ATOM   672  C C   . GLY A 1 100 ? 50.419 25.077 49.237 1.00 45.09  ? 100 GLY A C   1 
ATOM   673  O O   . GLY A 1 100 ? 49.838 23.996 49.283 1.00 48.15  ? 100 GLY A O   1 
ATOM   674  N N   . GLN A 1 101 ? 51.410 25.406 50.055 1.00 39.02  ? 101 GLN A N   1 
ATOM   675  C CA  . GLN A 1 101 ? 51.899 24.490 51.083 1.00 35.35  ? 101 GLN A CA  1 
ATOM   676  C C   . GLN A 1 101 ? 50.740 23.963 51.914 1.00 43.13  ? 101 GLN A C   1 
ATOM   677  O O   . GLN A 1 101 ? 50.795 22.877 52.491 1.00 46.71  ? 101 GLN A O   1 
ATOM   678  C CB  . GLN A 1 101 ? 52.912 25.160 52.002 1.00 36.87  ? 101 GLN A CB  1 
ATOM   679  C CG  . GLN A 1 101 ? 52.410 25.909 53.267 1.00 62.00  ? 101 GLN A CG  1 
ATOM   680  C CD  . GLN A 1 101 ? 53.181 25.430 54.475 1.00 82.82  ? 101 GLN A CD  1 
ATOM   681  O OE1 . GLN A 1 101 ? 53.604 24.247 54.527 1.00 68.17  ? 101 GLN A OE1 1 
ATOM   682  N NE2 . GLN A 1 101 ? 53.392 26.323 55.446 1.00 69.14  ? 101 GLN A NE2 1 
ATOM   683  N N   . VAL A 1 102 ? 49.691 24.768 51.959 1.00 29.07  ? 102 VAL A N   1 
ATOM   684  C CA  . VAL A 1 102 ? 48.509 24.423 52.691 1.00 22.93  ? 102 VAL A CA  1 
ATOM   685  C C   . VAL A 1 102 ? 47.511 23.909 51.704 1.00 40.70  ? 102 VAL A C   1 
ATOM   686  O O   . VAL A 1 102 ? 46.510 23.285 52.074 1.00 49.45  ? 102 VAL A O   1 
ATOM   687  C CB  . VAL A 1 102 ? 47.962 25.556 53.561 1.00 28.41  ? 102 VAL A CB  1 
ATOM   688  C CG1 . VAL A 1 102 ? 49.152 25.948 54.462 1.00 30.15  ? 102 VAL A CG1 1 
ATOM   689  C CG2 . VAL A 1 102 ? 47.290 26.768 52.827 1.00 26.47  ? 102 VAL A CG2 1 
ATOM   690  N N   . LEU A 1 103 ? 47.808 24.178 50.438 1.00 37.95  ? 103 LEU A N   1 
ATOM   691  C CA  . LEU A 1 103 ? 46.957 23.740 49.337 1.00 33.58  ? 103 LEU A CA  1 
ATOM   692  C C   . LEU A 1 103 ? 47.158 22.243 49.056 1.00 39.54  ? 103 LEU A C   1 
ATOM   693  O O   . LEU A 1 103 ? 46.331 21.566 48.427 1.00 39.46  ? 103 LEU A O   1 
ATOM   694  C CB  . LEU A 1 103 ? 45.896 24.677 48.582 1.00 27.31  ? 103 LEU A CB  1 
ATOM   695  C CG  . LEU A 1 103 ? 45.655 24.569 47.025 1.00 27.12  ? 103 LEU A CG  1 
ATOM   696  C CD1 . LEU A 1 103 ? 46.522 23.516 46.451 1.00 29.32  ? 103 LEU A CD1 1 
ATOM   697  C CD2 . LEU A 1 103 ? 44.262 24.204 46.471 1.00 11.71  ? 103 LEU A CD2 1 
ATOM   698  N N   . LYS A 1 104 ? 48.286 21.720 49.540 1.00 43.08  ? 104 LYS A N   1 
ATOM   699  C CA  . LYS A 1 104 ? 48.591 20.285 49.354 1.00 45.86  ? 104 LYS A CA  1 
ATOM   700  C C   . LYS A 1 104 ? 48.207 19.415 50.567 1.00 58.78  ? 104 LYS A C   1 
ATOM   701  O O   . LYS A 1 104 ? 47.690 18.304 50.411 1.00 62.89  ? 104 LYS A O   1 
ATOM   702  C CB  . LYS A 1 104 ? 49.850 20.034 48.508 1.00 42.51  ? 104 LYS A CB  1 
ATOM   703  C CG  . LYS A 1 104 ? 51.149 20.340 49.211 1.00 17.80  ? 104 LYS A CG  1 
ATOM   704  C CD  . LYS A 1 104 ? 51.570 21.802 49.308 1.00 39.08  ? 104 LYS A CD  1 
ATOM   705  C CE  . LYS A 1 104 ? 53.098 21.917 49.323 1.00 52.18  ? 104 LYS A CE  1 
ATOM   706  N NZ  . LYS A 1 104 ? 53.580 22.992 48.402 1.00 37.89  ? 104 LYS A NZ  1 
ATOM   707  N N   . GLU A 1 105 ? 48.442 19.916 51.790 1.00 50.94  ? 105 GLU A N   1 
ATOM   708  C CA  . GLU A 1 105 ? 48.093 19.157 52.985 1.00 44.60  ? 105 GLU A CA  1 
ATOM   709  C C   . GLU A 1 105 ? 46.567 19.148 53.146 1.00 42.65  ? 105 GLU A C   1 
ATOM   710  O O   . GLU A 1 105 ? 45.983 18.166 53.605 1.00 31.38  ? 105 GLU A O   1 
ATOM   711  C CB  . GLU A 1 105 ? 48.866 19.645 54.231 1.00 45.96  ? 105 GLU A CB  1 
ATOM   712  C CG  . GLU A 1 105 ? 48.357 20.937 54.973 1.00 67.73  ? 105 GLU A CG  1 
ATOM   713  C CD  . GLU A 1 105 ? 49.243 21.413 56.270 1.00 97.67  ? 105 GLU A CD  1 
ATOM   714  O OE1 . GLU A 1 105 ? 48.789 21.225 57.442 1.00 100.00 ? 105 GLU A OE1 1 
ATOM   715  O OE2 . GLU A 1 105 ? 50.371 22.008 56.141 1.00 46.71  ? 105 GLU A OE2 1 
ATOM   716  N N   . LEU A 1 106 ? 45.935 20.243 52.748 1.00 48.17  ? 106 LEU A N   1 
ATOM   717  C CA  . LEU A 1 106 ? 44.491 20.361 52.847 1.00 53.37  ? 106 LEU A CA  1 
ATOM   718  C C   . LEU A 1 106 ? 43.842 19.476 51.780 1.00 53.30  ? 106 LEU A C   1 
ATOM   719  O O   . LEU A 1 106 ? 42.898 18.743 52.051 1.00 55.61  ? 106 LEU A O   1 
ATOM   720  C CB  . LEU A 1 106 ? 43.989 21.843 52.848 1.00 58.43  ? 106 LEU A CB  1 
ATOM   721  C CG  . LEU A 1 106 ? 43.540 22.359 54.229 1.00 68.58  ? 106 LEU A CG  1 
ATOM   722  C CD1 . LEU A 1 106 ? 44.710 22.533 55.212 1.00 69.05  ? 106 LEU A CD1 1 
ATOM   723  C CD2 . LEU A 1 106 ? 42.648 23.635 54.104 1.00 75.26  ? 106 LEU A CD2 1 
ATOM   724  N N   . CYS A 1 107 ? 44.349 19.547 50.561 1.00 49.49  ? 107 CYS A N   1 
ATOM   725  C CA  . CYS A 1 107 ? 43.755 18.712 49.542 1.00 50.17  ? 107 CYS A CA  1 
ATOM   726  C C   . CYS A 1 107 ? 44.006 17.264 49.985 1.00 49.72  ? 107 CYS A C   1 
ATOM   727  O O   . CYS A 1 107 ? 43.249 16.356 49.653 1.00 47.84  ? 107 CYS A O   1 
ATOM   728  C CB  . CYS A 1 107 ? 44.512 18.932 48.210 1.00 49.30  ? 107 CYS A CB  1 
ATOM   729  S SG  . CYS A 1 107 ? 43.803 20.073 46.991 1.00 49.63  ? 107 CYS A SG  1 
ATOM   730  N N   . ASP A 1 108 ? 45.088 17.080 50.738 1.00 39.48  ? 108 ASP A N   1 
ATOM   731  C CA  . ASP A 1 108 ? 45.494 15.777 51.253 1.00 37.08  ? 108 ASP A CA  1 
ATOM   732  C C   . ASP A 1 108 ? 44.442 15.096 52.108 1.00 41.23  ? 108 ASP A C   1 
ATOM   733  O O   . ASP A 1 108 ? 43.927 14.023 51.751 1.00 34.78  ? 108 ASP A O   1 
ATOM   734  C CB  . ASP A 1 108 ? 46.664 15.823 52.185 1.00 38.79  ? 108 ASP A CB  1 
ATOM   735  C CG  . ASP A 1 108 ? 46.684 14.576 53.035 1.00 78.38  ? 108 ASP A CG  1 
ATOM   736  O OD1 . ASP A 1 108 ? 46.222 14.631 54.202 1.00 88.23  ? 108 ASP A OD1 1 
ATOM   737  O OD2 . ASP A 1 108 ? 47.112 13.508 52.523 1.00 87.97  ? 108 ASP A OD2 1 
ATOM   738  N N   . LYS A 1 109 ? 44.147 15.734 53.231 1.00 37.83  ? 109 LYS A N   1 
ATOM   739  C CA  . LYS A 1 109 ? 43.172 15.214 54.164 1.00 34.74  ? 109 LYS A CA  1 
ATOM   740  C C   . LYS A 1 109 ? 41.877 14.788 53.491 1.00 49.41  ? 109 LYS A C   1 
ATOM   741  O O   . LYS A 1 109 ? 41.119 13.985 54.022 1.00 59.42  ? 109 LYS A O   1 
ATOM   742  C CB  . LYS A 1 109 ? 43.013 16.199 55.222 1.00 30.05  ? 109 LYS A CB  1 
ATOM   743  C CG  . LYS A 1 109 ? 44.363 16.861 55.478 1.00 51.49  ? 109 LYS A CG  1 
ATOM   744  C CD  . LYS A 1 109 ? 44.107 18.330 55.663 1.00 75.38  ? 109 LYS A CD  1 
ATOM   745  C CE  . LYS A 1 109 ? 44.994 19.014 56.708 1.00 94.41  ? 109 LYS A CE  1 
ATOM   746  N NZ  . LYS A 1 109 ? 45.537 18.043 57.700 1.00 100.00 ? 109 LYS A NZ  1 
ATOM   747  N N   . GLU A 1 110 ? 41.614 15.310 52.307 1.00 40.15  ? 110 GLU A N   1 
ATOM   748  C CA  . GLU A 1 110 ? 40.389 14.958 51.594 1.00 40.99  ? 110 GLU A CA  1 
ATOM   749  C C   . GLU A 1 110 ? 40.474 13.628 50.840 1.00 33.69  ? 110 GLU A C   1 
ATOM   750  O O   . GLU A 1 110 ? 39.486 13.177 50.242 1.00 22.53  ? 110 GLU A O   1 
ATOM   751  C CB  . GLU A 1 110 ? 40.362 15.986 50.506 1.00 44.45  ? 110 GLU A CB  1 
ATOM   752  C CG  . GLU A 1 110 ? 38.966 16.308 50.071 1.00 70.50  ? 110 GLU A CG  1 
ATOM   753  C CD  . GLU A 1 110 ? 38.645 17.512 50.830 1.00 88.86  ? 110 GLU A CD  1 
ATOM   754  O OE1 . GLU A 1 110 ? 37.630 18.179 50.570 1.00 100.00 ? 110 GLU A OE1 1 
ATOM   755  O OE2 . GLU A 1 110 ? 39.514 17.816 51.685 1.00 66.30  ? 110 GLU A OE2 1 
ATOM   756  N N   . GLY A 1 111 ? 41.639 13.009 50.852 1.00 25.65  ? 111 GLY A N   1 
ATOM   757  C CA  . GLY A 1 111 ? 41.785 11.748 50.148 1.00 25.54  ? 111 GLY A CA  1 
ATOM   758  C C   . GLY A 1 111 ? 41.991 11.984 48.653 1.00 33.32  ? 111 GLY A C   1 
ATOM   759  O O   . GLY A 1 111 ? 41.563 11.190 47.818 1.00 33.85  ? 111 GLY A O   1 
ATOM   760  N N   . LEU A 1 112 ? 42.668 13.077 48.321 1.00 40.15  ? 112 LEU A N   1 
ATOM   761  C CA  . LEU A 1 112 ? 42.961 13.457 46.924 1.00 37.91  ? 112 LEU A CA  1 
ATOM   762  C C   . LEU A 1 112 ? 44.406 13.143 46.512 1.00 36.64  ? 112 LEU A C   1 
ATOM   763  O O   . LEU A 1 112 ? 45.347 13.306 47.310 1.00 23.70  ? 112 LEU A O   1 
ATOM   764  C CB  . LEU A 1 112 ? 42.692 14.947 46.716 1.00 38.92  ? 112 LEU A CB  1 
ATOM   765  C CG  . LEU A 1 112 ? 41.846 15.386 45.527 1.00 49.77  ? 112 LEU A CG  1 
ATOM   766  C CD1 . LEU A 1 112 ? 41.742 14.260 44.513 1.00 54.34  ? 112 LEU A CD1 1 
ATOM   767  C CD2 . LEU A 1 112 ? 40.519 16.020 45.916 1.00 57.29  ? 112 LEU A CD2 1 
ATOM   768  N N   . ALA A 1 113 ? 44.559 12.710 45.264 1.00 41.88  ? 113 ALA A N   1 
ATOM   769  C CA  . ALA A 1 113 ? 45.871 12.358 44.719 1.00 47.38  ? 113 ALA A CA  1 
ATOM   770  C C   . ALA A 1 113 ? 46.407 13.315 43.649 1.00 52.18  ? 113 ALA A C   1 
ATOM   771  O O   . ALA A 1 113 ? 47.116 12.910 42.718 1.00 56.95  ? 113 ALA A O   1 
ATOM   772  C CB  . ALA A 1 113 ? 45.785 10.943 44.118 1.00 49.15  ? 113 ALA A CB  1 
ATOM   773  N N   . THR A 1 114 ? 46.075 14.549 43.810 1.00 45.01  ? 114 THR A N   1 
ATOM   774  C CA  . THR A 1 114 ? 46.526 15.619 42.922 1.00 43.76  ? 114 THR A CA  1 
ATOM   775  C C   . THR A 1 114 ? 48.060 15.769 43.032 1.00 52.87  ? 114 THR A C   1 
ATOM   776  O O   . THR A 1 114 ? 48.638 15.557 44.102 1.00 58.34  ? 114 THR A O   1 
ATOM   777  C CB  . THR A 1 114 ? 45.895 16.893 43.402 1.00 19.66  ? 114 THR A CB  1 
ATOM   778  O OG1 . THR A 1 114 ? 46.534 17.274 44.618 1.00 31.86  ? 114 THR A OG1 1 
ATOM   779  C CG2 . THR A 1 114 ? 44.411 16.734 43.685 1.00 17.94  ? 114 THR A CG2 1 
ATOM   780  N N   . ARG A 1 115 ? 48.675 16.135 41.931 1.00 50.93  ? 115 ARG A N   1 
ATOM   781  C CA  . ARG A 1 115 ? 50.148 16.377 41.842 1.00 46.85  ? 115 ARG A CA  1 
ATOM   782  C C   . ARG A 1 115 ? 50.276 17.830 41.382 1.00 39.96  ? 115 ARG A C   1 
ATOM   783  O O   . ARG A 1 115 ? 49.800 18.200 40.307 1.00 31.43  ? 115 ARG A O   1 
ATOM   784  C CB  . ARG A 1 115 ? 50.746 15.377 40.826 1.00 40.24  ? 115 ARG A CB  1 
ATOM   785  C CG  . ARG A 1 115 ? 52.267 15.197 40.895 1.00 61.60  ? 115 ARG A CG  1 
ATOM   786  C CD  . ARG A 1 115 ? 52.725 13.855 40.293 1.00 67.23  ? 115 ARG A CD  1 
ATOM   787  N NE  . ARG A 1 115 ? 54.191 13.736 40.419 1.00 61.62  ? 115 ARG A NE  1 
ATOM   788  C CZ  . ARG A 1 115 ? 54.878 12.603 40.179 1.00 77.07  ? 115 ARG A CZ  1 
ATOM   789  N NH1 . ARG A 1 115 ? 54.250 11.482 39.790 1.00 57.92  ? 115 ARG A NH1 1 
ATOM   790  N NH2 . ARG A 1 115 ? 56.209 12.490 40.301 1.00 63.22  ? 115 ARG A NH2 1 
ATOM   791  N N   . PHE A 1 116 ? 50.885 18.660 42.178 1.00 46.13  ? 116 PHE A N   1 
ATOM   792  C CA  . PHE A 1 116 ? 50.992 20.088 41.837 1.00 45.62  ? 116 PHE A CA  1 
ATOM   793  C C   . PHE A 1 116 ? 52.319 20.542 41.772 1.00 51.36  ? 116 PHE A C   1 
ATOM   794  O O   . PHE A 1 116 ? 52.958 20.681 42.820 1.00 46.75  ? 116 PHE A O   1 
ATOM   795  C CB  . PHE A 1 116 ? 50.455 21.051 42.885 1.00 37.98  ? 116 PHE A CB  1 
ATOM   796  C CG  . PHE A 1 116 ? 49.034 20.951 43.275 1.00 27.69  ? 116 PHE A CG  1 
ATOM   797  C CD1 . PHE A 1 116 ? 48.752 20.579 44.575 1.00 23.71  ? 116 PHE A CD1 1 
ATOM   798  C CD2 . PHE A 1 116 ? 48.040 21.253 42.359 1.00 18.23  ? 116 PHE A CD2 1 
ATOM   799  C CE1 . PHE A 1 116 ? 47.446 20.495 44.984 1.00 17.43  ? 116 PHE A CE1 1 
ATOM   800  C CE2 . PHE A 1 116 ? 46.718 21.169 42.768 1.00 19.67  ? 116 PHE A CE2 1 
ATOM   801  C CZ  . PHE A 1 116 ? 46.420 20.788 44.084 1.00 20.04  ? 116 PHE A CZ  1 
ATOM   802  N N   . MET A 1 117 ? 52.717 20.779 40.635 1.00 50.65  ? 117 MET A N   1 
ATOM   803  C CA  . MET A 1 117 ? 54.018 21.258 40.468 1.00 57.23  ? 117 MET A CA  1 
ATOM   804  C C   . MET A 1 117 ? 54.056 22.653 41.031 1.00 54.14  ? 117 MET A C   1 
ATOM   805  O O   . MET A 1 117 ? 53.042 23.359 41.089 1.00 55.33  ? 117 MET A O   1 
ATOM   806  C CB  . MET A 1 117 ? 54.350 21.254 38.998 1.00 64.31  ? 117 MET A CB  1 
ATOM   807  C CG  . MET A 1 117 ? 54.122 22.611 38.360 1.00 70.13  ? 117 MET A CG  1 
ATOM   808  S SD  . MET A 1 117 ? 53.616 22.508 36.666 1.00 78.38  ? 117 MET A SD  1 
ATOM   809  C CE  . MET A 1 117 ? 54.611 23.610 35.690 1.00 77.64  ? 117 MET A CE  1 
ATOM   810  N N   . VAL A 1 118 ? 55.225 23.056 41.447 1.00 46.97  ? 118 VAL A N   1 
ATOM   811  C CA  . VAL A 1 118 ? 55.378 24.393 41.992 1.00 41.71  ? 118 VAL A CA  1 
ATOM   812  C C   . VAL A 1 118 ? 56.011 25.321 40.967 1.00 41.74  ? 118 VAL A C   1 
ATOM   813  O O   . VAL A 1 118 ? 56.993 24.964 40.297 1.00 38.62  ? 118 VAL A O   1 
ATOM   814  C CB  . VAL A 1 118 ? 56.235 24.394 43.239 1.00 48.20  ? 118 VAL A CB  1 
ATOM   815  C CG1 . VAL A 1 118 ? 57.208 25.569 43.279 1.00 50.17  ? 118 VAL A CG1 1 
ATOM   816  C CG2 . VAL A 1 118 ? 55.394 24.500 44.515 1.00 48.10  ? 118 VAL A CG2 1 
ATOM   817  N N   . ALA A 1 119 ? 55.397 26.487 40.905 1.00 42.42  ? 119 ALA A N   1 
ATOM   818  C CA  . ALA A 1 119 ? 55.797 27.563 40.007 1.00 40.40  ? 119 ALA A CA  1 
ATOM   819  C C   . ALA A 1 119 ? 56.758 28.508 40.716 1.00 49.28  ? 119 ALA A C   1 
ATOM   820  O O   . ALA A 1 119 ? 56.393 29.273 41.608 1.00 48.66  ? 119 ALA A O   1 
ATOM   821  C CB  . ALA A 1 119 ? 54.568 28.352 39.552 1.00 38.66  ? 119 ALA A CB  1 
ATOM   822  N N   . PRO A 1 120 ? 58.004 28.411 40.291 1.00 46.62  ? 120 PRO A N   1 
ATOM   823  C CA  . PRO A 1 120 ? 59.117 29.156 40.771 1.00 47.44  ? 120 PRO A CA  1 
ATOM   824  C C   . PRO A 1 120 ? 58.748 30.609 40.936 1.00 59.53  ? 120 PRO A C   1 
ATOM   825  O O   . PRO A 1 120 ? 58.265 31.229 39.984 1.00 57.79  ? 120 PRO A O   1 
ATOM   826  C CB  . PRO A 1 120 ? 60.202 28.971 39.681 1.00 50.84  ? 120 PRO A CB  1 
ATOM   827  C CG  . PRO A 1 120 ? 59.629 28.052 38.695 1.00 55.04  ? 120 PRO A CG  1 
ATOM   828  C CD  . PRO A 1 120 ? 58.202 28.223 38.885 1.00 47.29  ? 120 PRO A CD  1 
ATOM   829  N N   . GLY A 1 121 ? 58.957 31.130 42.156 1.00 61.67  ? 121 GLY A N   1 
ATOM   830  C CA  . GLY A 1 121 ? 58.663 32.517 42.529 1.00 63.27  ? 121 GLY A CA  1 
ATOM   831  C C   . GLY A 1 121 ? 57.336 32.980 41.961 1.00 69.15  ? 121 GLY A C   1 
ATOM   832  O O   . GLY A 1 121 ? 57.065 34.173 41.893 1.00 70.66  ? 121 GLY A O   1 
ATOM   833  N N   . GLN A 1 122 ? 56.516 32.045 41.561 1.00 67.68  ? 122 GLN A N   1 
ATOM   834  C CA  . GLN A 1 122 ? 55.244 32.347 40.990 1.00 70.74  ? 122 GLN A CA  1 
ATOM   835  C C   . GLN A 1 122 ? 54.238 32.733 42.035 1.00 81.20  ? 122 GLN A C   1 
ATOM   836  O O   . GLN A 1 122 ? 53.264 33.415 41.729 1.00 83.55  ? 122 GLN A O   1 
ATOM   837  C CB  . GLN A 1 122 ? 54.811 31.121 40.251 1.00 71.74  ? 122 GLN A CB  1 
ATOM   838  C CG  . GLN A 1 122 ? 55.276 31.090 38.862 1.00 65.49  ? 122 GLN A CG  1 
ATOM   839  C CD  . GLN A 1 122 ? 55.295 32.433 38.191 1.00 56.86  ? 122 GLN A CD  1 
ATOM   840  O OE1 . GLN A 1 122 ? 56.412 33.020 38.023 1.00 46.15  ? 122 GLN A OE1 1 
ATOM   841  N NE2 . GLN A 1 122 ? 54.111 32.987 37.831 1.00 22.50  ? 122 GLN A NE2 1 
ATOM   842  N N   . SER A 1 123 ? 54.456 32.286 43.263 1.00 80.69  ? 123 SER A N   1 
ATOM   843  C CA  . SER A 1 123 ? 53.522 32.590 44.331 1.00 83.56  ? 123 SER A CA  1 
ATOM   844  C C   . SER A 1 123 ? 52.252 31.756 44.138 1.00 86.31  ? 123 SER A C   1 
ATOM   845  O O   . SER A 1 123 ? 52.161 31.002 43.180 1.00 87.40  ? 123 SER A O   1 
ATOM   846  C CB  . SER A 1 123 ? 53.281 34.113 44.447 1.00 93.16  ? 123 SER A CB  1 
ATOM   847  O OG  . SER A 1 123 ? 54.434 34.881 44.077 1.00 96.48  ? 123 SER A OG  1 
ATOM   848  N N   . THR A 1 124 ? 51.316 31.871 45.061 1.00 79.95  ? 124 THR A N   1 
ATOM   849  C CA  . THR A 1 124 ? 50.071 31.078 44.945 1.00 76.95  ? 124 THR A CA  1 
ATOM   850  C C   . THR A 1 124 ? 48.900 31.886 44.417 1.00 76.60  ? 124 THR A C   1 
ATOM   851  O O   . THR A 1 124 ? 49.062 32.973 43.859 1.00 71.00  ? 124 THR A O   1 
ATOM   852  C CB  . THR A 1 124 ? 50.001 29.457 44.959 1.00 48.55  ? 124 THR A CB  1 
ATOM   853  O OG1 . THR A 1 124 ? 49.522 28.990 43.711 1.00 48.93  ? 124 THR A OG1 1 
ATOM   854  C CG2 . THR A 1 124 ? 48.920 28.951 45.906 1.00 27.88  ? 124 THR A CG2 1 
ATOM   855  N N   . GLY A 1 125 ? 47.689 31.312 44.556 1.00 74.48  ? 125 GLY A N   1 
ATOM   856  C CA  . GLY A 1 125 ? 46.505 31.923 44.091 1.00 69.54  ? 125 GLY A CA  1 
ATOM   857  C C   . GLY A 1 125 ? 45.225 31.423 44.754 1.00 54.87  ? 125 GLY A C   1 
ATOM   858  O O   . GLY A 1 125 ? 44.984 30.200 44.769 1.00 49.83  ? 125 GLY A O   1 
ATOM   859  N N   . THR A 1 126 ? 44.449 32.341 45.322 1.00 41.54  ? 126 THR A N   1 
ATOM   860  C CA  . THR A 1 126 ? 43.225 32.044 45.983 1.00 42.94  ? 126 THR A CA  1 
ATOM   861  C C   . THR A 1 126 ? 42.084 32.949 45.460 1.00 45.46  ? 126 THR A C   1 
ATOM   862  O O   . THR A 1 126 ? 42.153 33.489 44.371 1.00 46.80  ? 126 THR A O   1 
ATOM   863  C CB  . THR A 1 126 ? 43.492 32.275 47.437 1.00 62.94  ? 126 THR A CB  1 
ATOM   864  O OG1 . THR A 1 126 ? 42.228 32.427 48.118 1.00 82.02  ? 126 THR A OG1 1 
ATOM   865  C CG2 . THR A 1 126 ? 44.386 33.544 47.480 1.00 51.91  ? 126 THR A CG2 1 
ATOM   866  N N   . CYS A 1 127 ? 41.057 33.098 46.268 1.00 32.72  ? 127 CYS A N   1 
ATOM   867  C CA  . CYS A 1 127 ? 39.931 33.915 45.897 1.00 27.20  ? 127 CYS A CA  1 
ATOM   868  C C   . CYS A 1 127 ? 39.228 34.320 47.175 1.00 39.30  ? 127 CYS A C   1 
ATOM   869  O O   . CYS A 1 127 ? 38.449 33.514 47.682 1.00 50.05  ? 127 CYS A O   1 
ATOM   870  C CB  . CYS A 1 127 ? 38.961 33.183 44.986 1.00 20.56  ? 127 CYS A CB  1 
ATOM   871  S SG  . CYS A 1 127 ? 37.167 33.659 45.213 1.00 27.11  ? 127 CYS A SG  1 
ATOM   872  N N   . ALA A 1 128 ? 39.540 35.529 47.666 1.00 28.47  ? 128 ALA A N   1 
ATOM   873  C CA  . ALA A 1 128 ? 38.936 36.023 48.879 1.00 28.27  ? 128 ALA A CA  1 
ATOM   874  C C   . ALA A 1 128 ? 37.460 35.880 48.629 1.00 36.68  ? 128 ALA A C   1 
ATOM   875  O O   . ALA A 1 128 ? 36.953 36.434 47.645 1.00 43.11  ? 128 ALA A O   1 
ATOM   876  C CB  . ALA A 1 128 ? 39.463 37.457 49.253 1.00 30.66  ? 128 ALA A CB  1 
ATOM   877  N N   . VAL A 1 129 ? 36.778 35.121 49.486 1.00 29.90  ? 129 VAL A N   1 
ATOM   878  C CA  . VAL A 1 129 ? 35.351 34.897 49.336 1.00 29.22  ? 129 VAL A CA  1 
ATOM   879  C C   . VAL A 1 129 ? 34.463 35.597 50.369 1.00 32.93  ? 129 VAL A C   1 
ATOM   880  O O   . VAL A 1 129 ? 33.725 34.974 51.127 1.00 45.65  ? 129 VAL A O   1 
ATOM   881  C CB  . VAL A 1 129 ? 35.041 33.484 48.791 1.00 31.88  ? 129 VAL A CB  1 
ATOM   882  C CG1 . VAL A 1 129 ? 36.188 32.514 48.972 1.00 28.89  ? 129 VAL A CG1 1 
ATOM   883  C CG2 . VAL A 1 129 ? 33.545 33.048 48.948 1.00 30.88  ? 129 VAL A CG2 1 
ATOM   884  N N   . LEU A 1 130 ? 34.530 36.916 50.389 1.00 26.01  ? 130 LEU A N   1 
ATOM   885  C CA  . LEU A 1 130 ? 33.746 37.744 51.317 1.00 24.95  ? 130 LEU A CA  1 
ATOM   886  C C   . LEU A 1 130 ? 32.273 37.352 51.306 1.00 28.34  ? 130 LEU A C   1 
ATOM   887  O O   . LEU A 1 130 ? 31.839 36.785 50.325 1.00 30.65  ? 130 LEU A O   1 
ATOM   888  C CB  . LEU A 1 130 ? 33.784 39.183 50.868 1.00 19.93  ? 130 LEU A CB  1 
ATOM   889  C CG  . LEU A 1 130 ? 35.169 39.609 50.954 1.00 19.62  ? 130 LEU A CG  1 
ATOM   890  C CD1 . LEU A 1 130 ? 35.876 38.836 51.975 1.00 18.12  ? 130 LEU A CD1 1 
ATOM   891  C CD2 . LEU A 1 130 ? 35.813 39.436 49.618 1.00 21.17  ? 130 LEU A CD2 1 
ATOM   892  N N   . ILE A 1 131 ? 31.516 37.643 52.364 1.00 26.46  ? 131 ILE A N   1 
ATOM   893  C CA  . ILE A 1 131 ? 30.104 37.265 52.337 1.00 35.30  ? 131 ILE A CA  1 
ATOM   894  C C   . ILE A 1 131 ? 29.183 38.356 52.877 1.00 59.74  ? 131 ILE A C   1 
ATOM   895  O O   . ILE A 1 131 ? 29.371 39.560 52.712 1.00 62.71  ? 131 ILE A O   1 
ATOM   896  C CB  . ILE A 1 131 ? 29.819 35.975 53.214 1.00 39.38  ? 131 ILE A CB  1 
ATOM   897  C CG1 . ILE A 1 131 ? 31.093 35.162 53.256 1.00 43.98  ? 131 ILE A CG1 1 
ATOM   898  C CG2 . ILE A 1 131 ? 28.583 35.186 52.838 1.00 36.46  ? 131 ILE A CG2 1 
ATOM   899  C CD1 . ILE A 1 131 ? 31.084 33.810 53.932 1.00 16.91  ? 131 ILE A CD1 1 
ATOM   900  N N   . ASN A 1 132 ? 28.169 37.855 53.530 1.00 65.10  ? 132 ASN A N   1 
ATOM   901  C CA  . ASN A 1 132 ? 27.092 38.576 54.185 1.00 69.84  ? 132 ASN A CA  1 
ATOM   902  C C   . ASN A 1 132 ? 26.506 37.435 55.001 1.00 87.64  ? 132 ASN A C   1 
ATOM   903  O O   . ASN A 1 132 ? 27.278 36.604 55.465 1.00 88.98  ? 132 ASN A O   1 
ATOM   904  C CB  . ASN A 1 132 ? 26.148 39.371 53.155 1.00 67.83  ? 132 ASN A CB  1 
ATOM   905  C CG  . ASN A 1 132 ? 25.503 40.723 53.708 1.00 70.39  ? 132 ASN A CG  1 
ATOM   906  O OD1 . ASN A 1 132 ? 25.925 41.247 54.749 1.00 90.13  ? 132 ASN A OD1 1 
ATOM   907  N ND2 . ASN A 1 132 ? 24.490 41.267 52.995 1.00 13.48  ? 132 ASN A ND2 1 
ATOM   908  N N   . GLU A 1 133 ? 25.199 37.361 55.186 1.00 90.43  ? 133 GLU A N   1 
ATOM   909  C CA  . GLU A 1 133 ? 24.725 36.237 55.981 1.00 92.43  ? 133 GLU A CA  1 
ATOM   910  C C   . GLU A 1 133 ? 24.719 34.930 55.174 1.00 84.55  ? 133 GLU A C   1 
ATOM   911  O O   . GLU A 1 133 ? 24.392 33.862 55.700 1.00 84.36  ? 133 GLU A O   1 
ATOM   912  C CB  . GLU A 1 133 ? 23.611 36.532 57.018 1.00 95.05  ? 133 GLU A CB  1 
ATOM   913  C CG  . GLU A 1 133 ? 24.085 36.218 58.484 1.00 100.00 ? 133 GLU A CG  1 
ATOM   914  C CD  . GLU A 1 133 ? 23.841 37.403 59.464 1.00 100.00 ? 133 GLU A CD  1 
ATOM   915  O OE1 . GLU A 1 133 ? 22.663 37.786 59.714 1.00 100.00 ? 133 GLU A OE1 1 
ATOM   916  O OE2 . GLU A 1 133 ? 24.881 37.946 59.952 1.00 100.00 ? 133 GLU A OE2 1 
ATOM   917  N N   . LYS A 1 134 ? 25.161 35.053 53.922 1.00 71.54  ? 134 LYS A N   1 
ATOM   918  C CA  . LYS A 1 134 ? 25.224 33.979 52.966 1.00 67.42  ? 134 LYS A CA  1 
ATOM   919  C C   . LYS A 1 134 ? 25.760 34.541 51.681 1.00 66.34  ? 134 LYS A C   1 
ATOM   920  O O   . LYS A 1 134 ? 26.722 33.989 51.105 1.00 69.74  ? 134 LYS A O   1 
ATOM   921  C CB  . LYS A 1 134 ? 23.825 33.423 52.558 1.00 68.77  ? 134 LYS A CB  1 
ATOM   922  C CG  . LYS A 1 134 ? 23.010 32.626 53.584 1.00 20.47  ? 134 LYS A CG  1 
ATOM   923  C CD  . LYS A 1 134 ? 21.931 31.726 53.031 1.00 11.58  ? 134 LYS A CD  1 
ATOM   924  C CE  . LYS A 1 134 ? 20.499 32.311 52.994 1.00 24.97  ? 134 LYS A CE  1 
ATOM   925  N NZ  . LYS A 1 134 ? 20.562 33.726 53.417 1.00 47.52  ? 134 LYS A NZ  1 
ATOM   926  N N   . GLU A 1 135 ? 25.192 35.668 51.250 1.00 60.78  ? 135 GLU A N   1 
ATOM   927  C CA  . GLU A 1 135 ? 25.583 36.422 50.039 1.00 59.34  ? 135 GLU A CA  1 
ATOM   928  C C   . GLU A 1 135 ? 27.073 36.705 49.992 1.00 61.06  ? 135 GLU A C   1 
ATOM   929  O O   . GLU A 1 135 ? 27.548 37.495 50.785 1.00 65.49  ? 135 GLU A O   1 
ATOM   930  C CB  . GLU A 1 135 ? 24.842 37.759 50.106 1.00 59.02  ? 135 GLU A CB  1 
ATOM   931  C CG  . GLU A 1 135 ? 23.525 37.560 50.890 1.00 57.42  ? 135 GLU A CG  1 
ATOM   932  C CD  . GLU A 1 135 ? 23.689 37.713 52.395 1.00 45.17  ? 135 GLU A CD  1 
ATOM   933  O OE1 . GLU A 1 135 ? 24.586 37.077 52.949 1.00 22.33  ? 135 GLU A OE1 1 
ATOM   934  O OE2 . GLU A 1 135 ? 22.993 38.483 53.051 1.00 54.09  ? 135 GLU A OE2 1 
ATOM   935  N N   . ARG A 1 136 ? 27.793 36.054 49.059 1.00 50.04  ? 136 ARG A N   1 
ATOM   936  C CA  . ARG A 1 136 ? 29.243 36.206 48.896 1.00 40.22  ? 136 ARG A CA  1 
ATOM   937  C C   . ARG A 1 136 ? 29.706 37.113 47.754 1.00 41.11  ? 136 ARG A C   1 
ATOM   938  O O   . ARG A 1 136 ? 28.983 37.371 46.794 1.00 40.17  ? 136 ARG A O   1 
ATOM   939  C CB  . ARG A 1 136 ? 29.622 34.836 48.247 1.00 43.31  ? 136 ARG A CB  1 
ATOM   940  C CG  . ARG A 1 136 ? 29.003 33.587 48.955 1.00 43.33  ? 136 ARG A CG  1 
ATOM   941  C CD  . ARG A 1 136 ? 29.354 33.684 50.386 1.00 34.50  ? 136 ARG A CD  1 
ATOM   942  N NE  . ARG A 1 136 ? 29.469 32.520 51.206 1.00 64.16  ? 136 ARG A NE  1 
ATOM   943  C CZ  . ARG A 1 136 ? 30.649 32.038 51.515 1.00 90.69  ? 136 ARG A CZ  1 
ATOM   944  N NH1 . ARG A 1 136 ? 31.700 32.701 51.026 1.00 86.82  ? 136 ARG A NH1 1 
ATOM   945  N NH2 . ARG A 1 136 ? 30.820 30.949 52.266 1.00 82.07  ? 136 ARG A NH2 1 
ATOM   946  N N   . THR A 1 137 ? 30.954 37.585 47.887 1.00 39.28  ? 137 THR A N   1 
ATOM   947  C CA  . THR A 1 137 ? 31.653 38.458 46.936 1.00 35.05  ? 137 THR A CA  1 
ATOM   948  C C   . THR A 1 137 ? 33.040 37.864 46.775 1.00 25.86  ? 137 THR A C   1 
ATOM   949  O O   . THR A 1 137 ? 33.793 37.738 47.729 1.00 26.96  ? 137 THR A O   1 
ATOM   950  C CB  . THR A 1 137 ? 31.530 40.095 47.032 1.00 42.53  ? 137 THR A CB  1 
ATOM   951  O OG1 . THR A 1 137 ? 32.577 40.683 46.225 1.00 39.19  ? 137 THR A OG1 1 
ATOM   952  C CG2 . THR A 1 137 ? 31.457 40.707 48.460 1.00 14.76  ? 137 THR A CG2 1 
ATOM   953  N N   . LEU A 1 138 ? 33.415 37.473 45.589 1.00 24.37  ? 138 LEU A N   1 
ATOM   954  C CA  . LEU A 1 138 ? 34.741 36.899 45.534 1.00 27.96  ? 138 LEU A CA  1 
ATOM   955  C C   . LEU A 1 138 ? 35.782 37.632 44.707 1.00 34.69  ? 138 LEU A C   1 
ATOM   956  O O   . LEU A 1 138 ? 35.512 38.040 43.586 1.00 32.26  ? 138 LEU A O   1 
ATOM   957  C CB  . LEU A 1 138 ? 34.580 35.474 44.858 1.00 28.70  ? 138 LEU A CB  1 
ATOM   958  C CG  . LEU A 1 138 ? 33.429 34.456 45.183 1.00 28.58  ? 138 LEU A CG  1 
ATOM   959  C CD1 . LEU A 1 138 ? 32.503 34.943 46.372 1.00 23.85  ? 138 LEU A CD1 1 
ATOM   960  C CD2 . LEU A 1 138 ? 32.631 34.101 43.865 1.00 21.69  ? 138 LEU A CD2 1 
ATOM   961  N N   . CYS A 1 139 ? 36.975 37.777 45.276 1.00 38.06  ? 139 CYS A N   1 
ATOM   962  C CA  . CYS A 1 139 ? 38.072 38.444 44.580 1.00 43.47  ? 139 CYS A CA  1 
ATOM   963  C C   . CYS A 1 139 ? 39.068 37.338 44.226 1.00 44.12  ? 139 CYS A C   1 
ATOM   964  O O   . CYS A 1 139 ? 39.478 36.594 45.125 1.00 38.74  ? 139 CYS A O   1 
ATOM   965  C CB  . CYS A 1 139 ? 38.672 39.575 45.367 1.00 45.31  ? 139 CYS A CB  1 
ATOM   966  S SG  . CYS A 1 139 ? 39.898 40.519 44.432 1.00 47.64  ? 139 CYS A SG  1 
ATOM   967  N N   . THR A 1 140 ? 39.443 37.204 42.941 1.00 42.51  ? 140 THR A N   1 
ATOM   968  C CA  . THR A 1 140 ? 40.386 36.141 42.576 1.00 47.95  ? 140 THR A CA  1 
ATOM   969  C C   . THR A 1 140 ? 41.658 36.603 41.894 1.00 71.91  ? 140 THR A C   1 
ATOM   970  O O   . THR A 1 140 ? 41.712 37.695 41.346 1.00 79.85  ? 140 THR A O   1 
ATOM   971  C CB  . THR A 1 140 ? 39.895 35.117 41.522 1.00 43.56  ? 140 THR A CB  1 
ATOM   972  O OG1 . THR A 1 140 ? 38.448 34.988 41.490 1.00 47.65  ? 140 THR A OG1 1 
ATOM   973  C CG2 . THR A 1 140 ? 40.565 33.773 41.746 1.00 45.85  ? 140 THR A CG2 1 
ATOM   974  N N   . HIS A 1 141 ? 42.668 35.748 41.932 1.00 71.68  ? 141 HIS A N   1 
ATOM   975  C CA  . HIS A 1 141 ? 43.953 36.038 41.329 1.00 75.04  ? 141 HIS A CA  1 
ATOM   976  C C   . HIS A 1 141 ? 44.425 34.801 40.572 1.00 87.11  ? 141 HIS A C   1 
ATOM   977  O O   . HIS A 1 141 ? 45.217 34.011 41.075 1.00 87.82  ? 141 HIS A O   1 
ATOM   978  C CB  . HIS A 1 141 ? 44.982 36.445 42.416 1.00 76.19  ? 141 HIS A CB  1 
ATOM   979  C CG  . HIS A 1 141 ? 46.347 36.653 41.844 1.00 82.00  ? 141 HIS A CG  1 
ATOM   980  N ND1 . HIS A 1 141 ? 47.370 35.729 41.949 1.00 85.21  ? 141 HIS A ND1 1 
ATOM   981  C CD2 . HIS A 1 141 ? 46.852 37.670 41.135 1.00 85.20  ? 141 HIS A CD2 1 
ATOM   982  C CE1 . HIS A 1 141 ? 48.452 36.172 41.331 1.00 84.37  ? 141 HIS A CE1 1 
ATOM   983  N NE2 . HIS A 1 141 ? 48.157 37.350 40.819 1.00 85.24  ? 141 HIS A NE2 1 
ATOM   984  N N   . LEU A 1 142 ? 43.943 34.612 39.349 1.00 87.60  ? 142 LEU A N   1 
ATOM   985  C CA  . LEU A 1 142 ? 44.336 33.442 38.553 1.00 89.22  ? 142 LEU A CA  1 
ATOM   986  C C   . LEU A 1 142 ? 45.566 33.672 37.684 1.00 89.92  ? 142 LEU A C   1 
ATOM   987  O O   . LEU A 1 142 ? 45.476 34.001 36.498 1.00 96.96  ? 142 LEU A O   1 
ATOM   988  C CB  . LEU A 1 142 ? 43.171 33.127 37.655 1.00 92.14  ? 142 LEU A CB  1 
ATOM   989  C CG  . LEU A 1 142 ? 42.350 31.963 38.155 1.00 99.55  ? 142 LEU A CG  1 
ATOM   990  C CD1 . LEU A 1 142 ? 41.639 31.299 36.992 1.00 100.00 ? 142 LEU A CD1 1 
ATOM   991  C CD2 . LEU A 1 142 ? 43.142 30.967 38.989 1.00 100.00 ? 142 LEU A CD2 1 
ATOM   992  N N   . GLY A 1 143 ? 46.750 33.475 38.234 1.00 74.50  ? 143 GLY A N   1 
ATOM   993  C CA  . GLY A 1 143 ? 47.935 33.682 37.399 1.00 71.29  ? 143 GLY A CA  1 
ATOM   994  C C   . GLY A 1 143 ? 49.159 33.064 38.048 1.00 75.97  ? 143 GLY A C   1 
ATOM   995  O O   . GLY A 1 143 ? 50.197 32.938 37.413 1.00 78.70  ? 143 GLY A O   1 
ATOM   996  N N   . ALA A 1 144 ? 49.078 32.681 39.308 1.00 70.39  ? 144 ALA A N   1 
ATOM   997  C CA  . ALA A 1 144 ? 50.240 32.092 39.934 1.00 70.01  ? 144 ALA A CA  1 
ATOM   998  C C   . ALA A 1 144 ? 49.991 30.567 39.817 1.00 74.28  ? 144 ALA A C   1 
ATOM   999  O O   . ALA A 1 144 ? 50.718 29.752 40.406 1.00 73.97  ? 144 ALA A O   1 
ATOM   1000 C CB  . ALA A 1 144 ? 50.376 32.591 41.397 1.00 70.51  ? 144 ALA A CB  1 
ATOM   1001 N N   . CYS A 1 145 ? 48.935 30.335 39.008 1.00 70.32  ? 145 CYS A N   1 
ATOM   1002 C CA  . CYS A 1 145 ? 48.325 29.019 38.662 1.00 64.19  ? 145 CYS A CA  1 
ATOM   1003 C C   . CYS A 1 145 ? 48.295 28.706 37.162 1.00 70.60  ? 145 CYS A C   1 
ATOM   1004 O O   . CYS A 1 145 ? 47.761 27.665 36.737 1.00 69.63  ? 145 CYS A O   1 
ATOM   1005 C CB  . CYS A 1 145 ? 46.876 29.054 38.983 1.00 58.35  ? 145 CYS A CB  1 
ATOM   1006 S SG  . CYS A 1 145 ? 45.977 29.955 37.584 1.00 56.87  ? 145 CYS A SG  1 
ATOM   1007 N N   . GLY A 1 146 ? 48.831 29.609 36.379 1.00 72.84  ? 146 GLY A N   1 
ATOM   1008 C CA  . GLY A 1 146 ? 48.814 29.471 34.910 1.00 73.25  ? 146 GLY A CA  1 
ATOM   1009 C C   . GLY A 1 146 ? 50.197 29.243 34.349 1.00 72.16  ? 146 GLY A C   1 
ATOM   1010 O O   . GLY A 1 146 ? 50.812 30.147 33.770 1.00 63.21  ? 146 GLY A O   1 
ATOM   1011 N N   . SER A 1 147 ? 50.644 28.048 34.526 1.00 71.90  ? 147 SER A N   1 
ATOM   1012 C CA  . SER A 1 147 ? 51.938 27.643 34.057 1.00 71.19  ? 147 SER A CA  1 
ATOM   1013 C C   . SER A 1 147 ? 52.147 26.217 34.395 1.00 69.96  ? 147 SER A C   1 
ATOM   1014 O O   . SER A 1 147 ? 53.127 25.854 35.066 1.00 76.06  ? 147 SER A O   1 
ATOM   1015 C CB  . SER A 1 147 ? 53.017 28.491 34.690 1.00 77.23  ? 147 SER A CB  1 
ATOM   1016 O OG  . SER A 1 147 ? 53.227 29.651 33.898 1.00 100.00 ? 147 SER A OG  1 
ATOM   1017 N N   . PHE A 1 148 ? 51.208 25.508 33.934 1.00 54.33  ? 148 PHE A N   1 
ATOM   1018 C CA  . PHE A 1 148 ? 51.191 24.123 34.027 1.00 50.84  ? 148 PHE A CA  1 
ATOM   1019 C C   . PHE A 1 148 ? 51.630 23.706 32.679 1.00 64.33  ? 148 PHE A C   1 
ATOM   1020 O O   . PHE A 1 148 ? 51.115 24.197 31.665 1.00 58.27  ? 148 PHE A O   1 
ATOM   1021 C CB  . PHE A 1 148 ? 49.782 23.635 34.368 1.00 47.10  ? 148 PHE A CB  1 
ATOM   1022 C CG  . PHE A 1 148 ? 49.670 22.124 34.689 1.00 41.76  ? 148 PHE A CG  1 
ATOM   1023 C CD1 . PHE A 1 148 ? 50.570 21.500 35.574 1.00 42.79  ? 148 PHE A CD1 1 
ATOM   1024 C CD2 . PHE A 1 148 ? 48.650 21.361 34.098 1.00 34.94  ? 148 PHE A CD2 1 
ATOM   1025 C CE1 . PHE A 1 148 ? 50.435 20.125 35.869 1.00 36.19  ? 148 PHE A CE1 1 
ATOM   1026 C CE2 . PHE A 1 148 ? 48.514 19.996 34.396 1.00 35.22  ? 148 PHE A CE2 1 
ATOM   1027 C CZ  . PHE A 1 148 ? 49.404 19.378 35.281 1.00 34.10  ? 148 PHE A CZ  1 
ATOM   1028 N N   . ARG A 1 149 ? 52.541 22.890 32.710 1.00 70.22  ? 149 ARG A N   1 
ATOM   1029 C CA  . ARG A 1 149 ? 53.095 22.313 31.560 1.00 71.69  ? 149 ARG A CA  1 
ATOM   1030 C C   . ARG A 1 149 ? 53.141 20.919 31.932 1.00 72.06  ? 149 ARG A C   1 
ATOM   1031 O O   . ARG A 1 149 ? 54.057 20.482 32.624 1.00 61.01  ? 149 ARG A O   1 
ATOM   1032 C CB  . ARG A 1 149 ? 54.449 22.925 31.313 1.00 77.30  ? 149 ARG A CB  1 
ATOM   1033 C CG  . ARG A 1 149 ? 54.576 23.518 29.929 1.00 63.09  ? 149 ARG A CG  1 
ATOM   1034 C CD  . ARG A 1 149 ? 55.775 22.973 29.180 1.00 87.19  ? 149 ARG A CD  1 
ATOM   1035 N NE  . ARG A 1 149 ? 57.033 23.570 29.626 1.00 91.94  ? 149 ARG A NE  1 
ATOM   1036 C CZ  . ARG A 1 149 ? 58.092 22.872 30.045 1.00 69.41  ? 149 ARG A CZ  1 
ATOM   1037 N NH1 . ARG A 1 149 ? 58.065 21.534 30.090 1.00 34.54  ? 149 ARG A NH1 1 
ATOM   1038 N NH2 . ARG A 1 149 ? 59.242 23.431 30.443 1.00 55.07  ? 149 ARG A NH2 1 
ATOM   1039 N N   . ILE A 1 150 ? 52.172 20.238 31.505 1.00 78.48  ? 150 ILE A N   1 
ATOM   1040 C CA  . ILE A 1 150 ? 52.072 18.890 31.891 1.00 86.84  ? 150 ILE A CA  1 
ATOM   1041 C C   . ILE A 1 150 ? 53.430 18.218 31.854 1.00 95.11  ? 150 ILE A C   1 
ATOM   1042 O O   . ILE A 1 150 ? 54.131 18.236 30.820 1.00 97.09  ? 150 ILE A O   1 
ATOM   1043 C CB  . ILE A 1 150 ? 51.078 18.157 31.027 1.00 93.40  ? 150 ILE A CB  1 
ATOM   1044 C CG1 . ILE A 1 150 ? 49.978 19.073 30.491 1.00 94.52  ? 150 ILE A CG1 1 
ATOM   1045 C CG2 . ILE A 1 150 ? 50.352 17.052 31.809 1.00 93.01  ? 150 ILE A CG2 1 
ATOM   1046 C CD1 . ILE A 1 150 ? 49.573 18.729 29.059 1.00 50.00  ? 150 ILE A CD1 1 
ATOM   1047 N N   . PRO A 1 151 ? 53.822 17.616 33.007 1.00 58.36  ? 151 PRO A N   1 
ATOM   1048 C CA  . PRO A 1 151 ? 55.055 16.892 33.094 1.00 54.23  ? 151 PRO A CA  1 
ATOM   1049 C C   . PRO A 1 151 ? 54.977 15.813 32.041 1.00 58.31  ? 151 PRO A C   1 
ATOM   1050 O O   . PRO A 1 151 ? 53.845 15.314 31.757 1.00 53.50  ? 151 PRO A O   1 
ATOM   1051 C CB  . PRO A 1 151 ? 55.073 16.368 34.526 1.00 55.49  ? 151 PRO A CB  1 
ATOM   1052 C CG  . PRO A 1 151 ? 53.803 16.855 35.221 1.00 54.92  ? 151 PRO A CG  1 
ATOM   1053 C CD  . PRO A 1 151 ? 53.012 17.662 34.239 1.00 50.15  ? 151 PRO A CD  1 
ATOM   1054 N N   . GLU A 1 152 ? 56.123 15.474 31.479 1.00 57.10  ? 152 GLU A N   1 
ATOM   1055 C CA  . GLU A 1 152 ? 56.205 14.453 30.403 1.00 57.06  ? 152 GLU A CA  1 
ATOM   1056 C C   . GLU A 1 152 ? 55.820 13.046 30.907 1.00 51.35  ? 152 GLU A C   1 
ATOM   1057 O O   . GLU A 1 152 ? 55.433 12.169 30.126 1.00 58.50  ? 152 GLU A O   1 
ATOM   1058 C CB  . GLU A 1 152 ? 57.627 14.369 29.833 1.00 55.39  ? 152 GLU A CB  1 
ATOM   1059 C CG  . GLU A 1 152 ? 57.660 13.902 28.365 1.00 55.73  ? 152 GLU A CG  1 
ATOM   1060 C CD  . GLU A 1 152 ? 58.361 12.549 28.176 1.00 50.00  ? 152 GLU A CD  1 
ATOM   1061 O OE1 . GLU A 1 152 ? 59.266 12.409 27.265 1.00 50.00  ? 152 GLU A OE1 1 
ATOM   1062 O OE2 . GLU A 1 152 ? 58.048 11.548 28.928 1.00 57.10  ? 152 GLU A OE2 1 
ATOM   1063 N N   . ASP A 1 153 ? 55.927 12.842 32.207 1.00 54.38  ? 153 ASP A N   1 
ATOM   1064 C CA  . ASP A 1 153 ? 55.607 11.530 32.821 1.00 59.85  ? 153 ASP A CA  1 
ATOM   1065 C C   . ASP A 1 153 ? 54.249 11.544 33.521 1.00 55.08  ? 153 ASP A C   1 
ATOM   1066 O O   . ASP A 1 153 ? 53.935 10.661 34.327 1.00 59.47  ? 153 ASP A O   1 
ATOM   1067 C CB  . ASP A 1 153 ? 56.644 11.168 33.875 1.00 51.52  ? 153 ASP A CB  1 
ATOM   1068 C CG  . ASP A 1 153 ? 56.648 12.155 35.042 1.00 53.85  ? 153 ASP A CG  1 
ATOM   1069 O OD1 . ASP A 1 153 ? 56.770 11.730 36.252 1.00 50.40  ? 153 ASP A OD1 1 
ATOM   1070 O OD2 . ASP A 1 153 ? 56.534 13.419 34.809 1.00 26.68  ? 153 ASP A OD2 1 
ATOM   1071 N N   . TRP A 1 154 ? 53.459 12.534 33.211 1.00 58.71  ? 154 TRP A N   1 
ATOM   1072 C CA  . TRP A 1 154 ? 52.143 12.677 33.834 1.00 52.51  ? 154 TRP A CA  1 
ATOM   1073 C C   . TRP A 1 154 ? 51.281 11.414 33.609 1.00 56.91  ? 154 TRP A C   1 
ATOM   1074 O O   . TRP A 1 154 ? 50.433 11.058 34.438 1.00 50.00  ? 154 TRP A O   1 
ATOM   1075 C CB  . TRP A 1 154 ? 51.418 13.891 33.265 1.00 53.19  ? 154 TRP A CB  1 
ATOM   1076 C CG  . TRP A 1 154 ? 50.841 13.650 31.886 1.00 55.87  ? 154 TRP A CG  1 
ATOM   1077 C CD1 . TRP A 1 154 ? 51.464 13.815 30.716 1.00 58.36  ? 154 TRP A CD1 1 
ATOM   1078 C CD2 . TRP A 1 154 ? 49.528 13.206 31.633 1.00 56.61  ? 154 TRP A CD2 1 
ATOM   1079 N NE1 . TRP A 1 154 ? 50.526 13.470 29.695 1.00 58.30  ? 154 TRP A NE1 1 
ATOM   1080 C CE2 . TRP A 1 154 ? 49.395 13.117 30.257 1.00 50.00  ? 154 TRP A CE2 1 
ATOM   1081 C CE3 . TRP A 1 154 ? 48.443 12.874 32.450 1.00 58.55  ? 154 TRP A CE3 1 
ATOM   1082 C CZ2 . TRP A 1 154 ? 48.216 12.710 29.629 1.00 50.00  ? 154 TRP A CZ2 1 
ATOM   1083 C CZ3 . TRP A 1 154 ? 47.258 12.463 31.810 1.00 59.65  ? 154 TRP A CZ3 1 
ATOM   1084 C CH2 . TRP A 1 154 ? 47.150 12.386 30.464 1.00 50.00  ? 154 TRP A CH2 1 
ATOM   1085 N N   . THR A 1 155 ? 51.504 10.734 32.490 1.00 59.13  ? 155 THR A N   1 
ATOM   1086 C CA  . THR A 1 155 ? 50.727 9.516  32.168 1.00 56.17  ? 155 THR A CA  1 
ATOM   1087 C C   . THR A 1 155 ? 51.026 8.397  33.182 1.00 52.61  ? 155 THR A C   1 
ATOM   1088 O O   . THR A 1 155 ? 50.192 7.522  33.440 1.00 55.42  ? 155 THR A O   1 
ATOM   1089 C CB  . THR A 1 155 ? 51.044 9.000  30.759 1.00 50.00  ? 155 THR A CB  1 
ATOM   1090 O OG1 . THR A 1 155 ? 52.441 8.931  30.561 1.00 59.98  ? 155 THR A OG1 1 
ATOM   1091 C CG2 . THR A 1 155 ? 50.465 9.895  29.655 1.00 50.00  ? 155 THR A CG2 1 
ATOM   1092 N N   . THR A 1 156 ? 52.217 8.429  33.761 1.00 54.07  ? 156 THR A N   1 
ATOM   1093 C CA  . THR A 1 156 ? 52.604 7.410  34.760 1.00 54.01  ? 156 THR A CA  1 
ATOM   1094 C C   . THR A 1 156 ? 51.876 7.677  36.088 1.00 58.37  ? 156 THR A C   1 
ATOM   1095 O O   . THR A 1 156 ? 51.433 6.743  36.771 1.00 55.11  ? 156 THR A O   1 
ATOM   1096 C CB  . THR A 1 156 ? 54.113 7.428  35.027 1.00 50.31  ? 156 THR A CB  1 
ATOM   1097 O OG1 . THR A 1 156 ? 54.824 7.120  33.839 1.00 50.00  ? 156 THR A OG1 1 
ATOM   1098 C CG2 . THR A 1 156 ? 54.539 6.404  36.089 1.00 54.32  ? 156 THR A CG2 1 
ATOM   1099 N N   . PHE A 1 157 ? 51.777 8.955  36.402 1.00 58.19  ? 157 PHE A N   1 
ATOM   1100 C CA  . PHE A 1 157 ? 51.133 9.448  37.640 1.00 55.60  ? 157 PHE A CA  1 
ATOM   1101 C C   . PHE A 1 157 ? 49.621 9.132  37.654 1.00 57.02  ? 157 PHE A C   1 
ATOM   1102 O O   . PHE A 1 157 ? 49.012 8.958  38.719 1.00 58.40  ? 157 PHE A O   1 
ATOM   1103 C CB  . PHE A 1 157 ? 51.324 10.963 37.735 1.00 53.11  ? 157 PHE A CB  1 
ATOM   1104 C CG  . PHE A 1 157 ? 50.645 11.599 38.948 1.00 57.10  ? 157 PHE A CG  1 
ATOM   1105 C CD1 . PHE A 1 157 ? 49.373 12.166 38.817 1.00 53.72  ? 157 PHE A CD1 1 
ATOM   1106 C CD2 . PHE A 1 157 ? 51.297 11.619 40.188 1.00 51.19  ? 157 PHE A CD2 1 
ATOM   1107 C CE1 . PHE A 1 157 ? 48.752 12.757 39.923 1.00 51.74  ? 157 PHE A CE1 1 
ATOM   1108 C CE2 . PHE A 1 157 ? 50.677 12.211 41.294 1.00 50.87  ? 157 PHE A CE2 1 
ATOM   1109 C CZ  . PHE A 1 157 ? 49.404 12.781 41.161 1.00 59.77  ? 157 PHE A CZ  1 
ATOM   1110 N N   . ALA A 1 158 ? 49.041 9.067  36.464 1.00 53.17  ? 158 ALA A N   1 
ATOM   1111 C CA  . ALA A 1 158 ? 47.596 8.773  36.298 1.00 59.08  ? 158 ALA A CA  1 
ATOM   1112 C C   . ALA A 1 158 ? 47.375 7.304  35.754 1.00 50.30  ? 158 ALA A C   1 
ATOM   1113 O O   . ALA A 1 158 ? 46.218 6.869  35.598 1.00 50.22  ? 158 ALA A O   1 
ATOM   1114 C CB  . ALA A 1 158 ? 46.976 9.771  35.303 1.00 59.28  ? 158 ALA A CB  1 
ATOM   1115 N N   . SER A 1 159 ? 48.539 6.617  35.507 1.00 50.29  ? 159 SER A N   1 
ATOM   1116 C CA  . SER A 1 159 ? 48.698 5.172  34.928 1.00 58.21  ? 159 SER A CA  1 
ATOM   1117 C C   . SER A 1 159 ? 47.689 4.131  35.472 1.00 51.80  ? 159 SER A C   1 
ATOM   1118 O O   . SER A 1 159 ? 47.863 3.561  36.553 1.00 47.84  ? 159 SER A O   1 
ATOM   1119 C CB  . SER A 1 159 ? 50.093 4.606  35.264 1.00 52.82  ? 159 SER A CB  1 
ATOM   1120 O OG  . SER A 1 159 ? 50.275 4.593  36.677 1.00 69.89  ? 159 SER A OG  1 
ATOM   1121 N N   . GLY A 1 160 ? 46.644 3.891  34.700 1.00 34.44  ? 160 GLY A N   1 
ATOM   1122 C CA  . GLY A 1 160 ? 45.584 2.944  35.096 1.00 32.79  ? 160 GLY A CA  1 
ATOM   1123 C C   . GLY A 1 160 ? 44.208 3.628  35.019 1.00 40.36  ? 160 GLY A C   1 
ATOM   1124 O O   . GLY A 1 160 ? 43.186 2.977  34.777 1.00 43.68  ? 160 GLY A O   1 
ATOM   1125 N N   . ALA A 1 161 ? 44.219 4.939  35.227 1.00 28.31  ? 161 ALA A N   1 
ATOM   1126 C CA  . ALA A 1 161 ? 42.988 5.766  35.175 1.00 22.04  ? 161 ALA A CA  1 
ATOM   1127 C C   . ALA A 1 161 ? 42.351 5.656  33.773 1.00 30.48  ? 161 ALA A C   1 
ATOM   1128 O O   . ALA A 1 161 ? 43.055 5.571  32.758 1.00 42.76  ? 161 ALA A O   1 
ATOM   1129 C CB  . ALA A 1 161 ? 43.332 7.231  35.458 1.00 24.64  ? 161 ALA A CB  1 
ATOM   1130 N N   . LEU A 1 162 ? 41.011 5.663  33.747 1.00 29.43  ? 162 LEU A N   1 
ATOM   1131 C CA  . LEU A 1 162 ? 40.240 5.545  32.476 1.00 25.15  ? 162 LEU A CA  1 
ATOM   1132 C C   . LEU A 1 162 ? 39.253 6.748  32.257 1.00 45.82  ? 162 LEU A C   1 
ATOM   1133 O O   . LEU A 1 162 ? 38.627 6.867  31.187 1.00 61.01  ? 162 LEU A O   1 
ATOM   1134 C CB  . LEU A 1 162 ? 39.408 4.246  32.476 1.00 21.80  ? 162 LEU A CB  1 
ATOM   1135 C CG  . LEU A 1 162 ? 40.235 2.980  32.180 1.00 27.26  ? 162 LEU A CG  1 
ATOM   1136 C CD1 . LEU A 1 162 ? 39.410 1.689  32.261 1.00 31.58  ? 162 LEU A CD1 1 
ATOM   1137 C CD2 . LEU A 1 162 ? 40.858 2.979  30.782 1.00 31.50  ? 162 LEU A CD2 1 
ATOM   1138 N N   . ILE A 1 163 ? 39.141 7.617  33.286 1.00 34.86  ? 163 ILE A N   1 
ATOM   1139 C CA  . ILE A 1 163 ? 38.238 8.840  33.274 1.00 38.54  ? 163 ILE A CA  1 
ATOM   1140 C C   . ILE A 1 163 ? 39.056 10.137 33.413 1.00 40.52  ? 163 ILE A C   1 
ATOM   1141 O O   . ILE A 1 163 ? 39.394 10.565 34.526 1.00 37.22  ? 163 ILE A O   1 
ATOM   1142 C CB  . ILE A 1 163 ? 37.260 8.807  34.458 1.00 40.39  ? 163 ILE A CB  1 
ATOM   1143 C CG1 . ILE A 1 163 ? 36.660 7.426  34.706 1.00 34.91  ? 163 ILE A CG1 1 
ATOM   1144 C CG2 . ILE A 1 163 ? 36.067 9.754  34.287 1.00 40.32  ? 163 ILE A CG2 1 
ATOM   1145 C CD1 . ILE A 1 163 ? 35.141 7.395  34.531 1.00 17.19  ? 163 ILE A CD1 1 
ATOM   1146 N N   . PHE A 1 164 ? 39.350 10.735 32.281 1.00 29.13  ? 164 PHE A N   1 
ATOM   1147 C CA  . PHE A 1 164 ? 40.156 11.968 32.217 1.00 27.40  ? 164 PHE A CA  1 
ATOM   1148 C C   . PHE A 1 164 ? 39.273 13.204 32.158 1.00 29.60  ? 164 PHE A C   1 
ATOM   1149 O O   . PHE A 1 164 ? 38.240 13.229 31.495 1.00 30.41  ? 164 PHE A O   1 
ATOM   1150 C CB  . PHE A 1 164 ? 41.014 11.945 30.957 1.00 28.45  ? 164 PHE A CB  1 
ATOM   1151 C CG  . PHE A 1 164 ? 41.999 10.783 30.920 1.00 22.33  ? 164 PHE A CG  1 
ATOM   1152 C CD1 . PHE A 1 164 ? 43.287 10.963 31.420 1.00 17.37  ? 164 PHE A CD1 1 
ATOM   1153 C CD2 . PHE A 1 164 ? 41.614 9.544  30.386 1.00 22.25  ? 164 PHE A CD2 1 
ATOM   1154 C CE1 . PHE A 1 164 ? 44.201 9.911  31.388 1.00 20.67  ? 164 PHE A CE1 1 
ATOM   1155 C CE2 . PHE A 1 164 ? 42.533 8.489  30.353 1.00 26.84  ? 164 PHE A CE2 1 
ATOM   1156 C CZ  . PHE A 1 164 ? 43.826 8.674  30.854 1.00 21.61  ? 164 PHE A CZ  1 
ATOM   1157 N N   . TYR A 1 165 ? 39.684 14.242 32.849 1.00 27.01  ? 165 TYR A N   1 
ATOM   1158 C CA  . TYR A 1 165 ? 38.911 15.485 32.845 1.00 29.19  ? 165 TYR A CA  1 
ATOM   1159 C C   . TYR A 1 165 ? 39.859 16.673 33.068 1.00 35.27  ? 165 TYR A C   1 
ATOM   1160 O O   . TYR A 1 165 ? 41.036 16.496 33.422 1.00 34.66  ? 165 TYR A O   1 
ATOM   1161 C CB  . TYR A 1 165 ? 37.828 15.395 33.934 1.00 30.22  ? 165 TYR A CB  1 
ATOM   1162 C CG  . TYR A 1 165 ? 37.136 16.719 34.266 1.00 35.31  ? 165 TYR A CG  1 
ATOM   1163 C CD1 . TYR A 1 165 ? 36.317 17.375 33.320 1.00 37.10  ? 165 TYR A CD1 1 
ATOM   1164 C CD2 . TYR A 1 165 ? 37.318 17.273 35.528 1.00 33.56  ? 165 TYR A CD2 1 
ATOM   1165 C CE1 . TYR A 1 165 ? 35.699 18.600 33.658 1.00 37.91  ? 165 TYR A CE1 1 
ATOM   1166 C CE2 . TYR A 1 165 ? 36.711 18.490 35.865 1.00 35.72  ? 165 TYR A CE2 1 
ATOM   1167 C CZ  . TYR A 1 165 ? 35.903 19.155 34.933 1.00 49.04  ? 165 TYR A CZ  1 
ATOM   1168 O OH  . TYR A 1 165 ? 35.322 20.339 35.270 1.00 45.75  ? 165 TYR A OH  1 
ATOM   1169 N N   . ALA A 1 166 ? 39.298 17.837 32.834 1.00 40.07  ? 166 ALA A N   1 
ATOM   1170 C CA  . ALA A 1 166 ? 39.991 19.124 32.958 1.00 44.97  ? 166 ALA A CA  1 
ATOM   1171 C C   . ALA A 1 166 ? 39.055 20.225 32.470 1.00 44.13  ? 166 ALA A C   1 
ATOM   1172 O O   . ALA A 1 166 ? 38.240 20.016 31.563 1.00 37.62  ? 166 ALA A O   1 
ATOM   1173 C CB  . ALA A 1 166 ? 41.264 19.114 32.104 1.00 47.17  ? 166 ALA A CB  1 
ATOM   1174 N N   . THR A 1 167 ? 39.186 21.375 33.084 1.00 48.67  ? 167 THR A N   1 
ATOM   1175 C CA  . THR A 1 167 ? 38.355 22.535 32.748 1.00 45.92  ? 167 THR A CA  1 
ATOM   1176 C C   . THR A 1 167 ? 38.996 23.300 31.571 1.00 50.37  ? 167 THR A C   1 
ATOM   1177 O O   . THR A 1 167 ? 40.227 23.430 31.487 1.00 41.17  ? 167 THR A O   1 
ATOM   1178 C CB  . THR A 1 167 ? 38.228 23.430 33.986 1.00 19.39  ? 167 THR A CB  1 
ATOM   1179 O OG1 . THR A 1 167 ? 37.246 24.431 33.767 1.00 36.26  ? 167 THR A OG1 1 
ATOM   1180 C CG2 . THR A 1 167 ? 39.531 24.135 34.358 1.00 10.71  ? 167 THR A CG2 1 
ATOM   1181 N N   . ALA A 1 168 ? 38.119 23.776 30.692 1.00 42.59  ? 168 ALA A N   1 
ATOM   1182 C CA  . ALA A 1 168 ? 38.506 24.531 29.480 1.00 43.12  ? 168 ALA A CA  1 
ATOM   1183 C C   . ALA A 1 168 ? 39.418 25.703 29.846 1.00 47.03  ? 168 ALA A C   1 
ATOM   1184 O O   . ALA A 1 168 ? 40.127 26.257 28.994 1.00 58.02  ? 168 ALA A O   1 
ATOM   1185 C CB  . ALA A 1 168 ? 37.263 25.079 28.780 1.00 45.43  ? 168 ALA A CB  1 
ATOM   1186 N N   . TYR A 1 169 ? 39.368 26.051 31.110 1.00 27.81  ? 169 TYR A N   1 
ATOM   1187 C CA  . TYR A 1 169 ? 40.182 27.137 31.659 1.00 22.36  ? 169 TYR A CA  1 
ATOM   1188 C C   . TYR A 1 169 ? 41.609 26.896 31.313 1.00 32.38  ? 169 TYR A C   1 
ATOM   1189 O O   . TYR A 1 169 ? 42.353 27.841 31.007 1.00 36.46  ? 169 TYR A O   1 
ATOM   1190 C CB  . TYR A 1 169 ? 40.040 27.165 33.158 1.00 23.00  ? 169 TYR A CB  1 
ATOM   1191 C CG  . TYR A 1 169 ? 38.804 27.879 33.534 1.00 29.01  ? 169 TYR A CG  1 
ATOM   1192 C CD1 . TYR A 1 169 ? 37.746 27.171 34.086 1.00 30.65  ? 169 TYR A CD1 1 
ATOM   1193 C CD2 . TYR A 1 169 ? 38.742 29.242 33.308 1.00 18.80  ? 169 TYR A CD2 1 
ATOM   1194 C CE1 . TYR A 1 169 ? 36.582 27.846 34.413 1.00 27.71  ? 169 TYR A CE1 1 
ATOM   1195 C CE2 . TYR A 1 169 ? 37.576 29.922 33.630 1.00 13.57  ? 169 TYR A CE2 1 
ATOM   1196 C CZ  . TYR A 1 169 ? 36.494 29.225 34.181 1.00 36.09  ? 169 TYR A CZ  1 
ATOM   1197 O OH  . TYR A 1 169 ? 35.355 29.889 34.490 1.00 68.69  ? 169 TYR A OH  1 
ATOM   1198 N N   . THR A 1 170 ? 41.887 25.632 31.389 1.00 30.10  ? 170 THR A N   1 
ATOM   1199 C CA  . THR A 1 170 ? 43.181 25.062 31.118 1.00 26.17  ? 170 THR A CA  1 
ATOM   1200 C C   . THR A 1 170 ? 43.829 25.752 29.925 1.00 29.81  ? 170 THR A C   1 
ATOM   1201 O O   . THR A 1 170 ? 45.039 26.006 29.913 1.00 30.16  ? 170 THR A O   1 
ATOM   1202 C CB  . THR A 1 170 ? 43.005 23.580 30.822 1.00 55.42  ? 170 THR A CB  1 
ATOM   1203 O OG1 . THR A 1 170 ? 42.452 22.928 31.960 1.00 47.14  ? 170 THR A OG1 1 
ATOM   1204 C CG2 . THR A 1 170 ? 44.315 22.882 30.482 1.00 70.33  ? 170 THR A CG2 1 
ATOM   1205 N N   . LEU A 1 171 ? 43.020 26.044 28.935 1.00 27.99  ? 171 LEU A N   1 
ATOM   1206 C CA  . LEU A 1 171 ? 43.506 26.706 27.726 1.00 28.23  ? 171 LEU A CA  1 
ATOM   1207 C C   . LEU A 1 171 ? 44.181 28.031 28.078 1.00 30.52  ? 171 LEU A C   1 
ATOM   1208 O O   . LEU A 1 171 ? 45.270 28.341 27.577 1.00 32.96  ? 171 LEU A O   1 
ATOM   1209 C CB  . LEU A 1 171 ? 42.353 27.023 26.770 1.00 25.17  ? 171 LEU A CB  1 
ATOM   1210 C CG  . LEU A 1 171 ? 41.472 25.823 26.451 1.00 23.29  ? 171 LEU A CG  1 
ATOM   1211 C CD1 . LEU A 1 171 ? 40.465 26.106 25.334 1.00 20.71  ? 171 LEU A CD1 1 
ATOM   1212 C CD2 . LEU A 1 171 ? 42.269 24.603 25.996 1.00 25.98  ? 171 LEU A CD2 1 
ATOM   1213 N N   . THR A 1 172 ? 43.495 28.763 28.943 1.00 25.72  ? 172 THR A N   1 
ATOM   1214 C CA  . THR A 1 172 ? 43.920 30.107 29.385 1.00 34.45  ? 172 THR A CA  1 
ATOM   1215 C C   . THR A 1 172 ? 45.456 30.242 29.395 1.00 55.79  ? 172 THR A C   1 
ATOM   1216 O O   . THR A 1 172 ? 46.007 31.305 29.104 1.00 69.31  ? 172 THR A O   1 
ATOM   1217 C CB  . THR A 1 172 ? 43.357 30.439 30.760 1.00 63.29  ? 172 THR A CB  1 
ATOM   1218 O OG1 . THR A 1 172 ? 42.320 31.418 30.616 1.00 49.00  ? 172 THR A OG1 1 
ATOM   1219 C CG2 . THR A 1 172 ? 44.391 31.016 31.713 1.00 75.19  ? 172 THR A CG2 1 
ATOM   1220 N N   . ALA A 1 173 ? 46.168 29.191 29.730 1.00 43.77  ? 173 ALA A N   1 
ATOM   1221 C CA  . ALA A 1 173 ? 47.652 29.250 29.683 1.00 45.48  ? 173 ALA A CA  1 
ATOM   1222 C C   . ALA A 1 173 ? 48.029 28.922 28.233 1.00 56.98  ? 173 ALA A C   1 
ATOM   1223 O O   . ALA A 1 173 ? 48.329 29.829 27.434 1.00 67.35  ? 173 ALA A O   1 
ATOM   1224 C CB  . ALA A 1 173 ? 48.251 28.230 30.653 1.00 44.95  ? 173 ALA A CB  1 
ATOM   1225 N N   . THR A 1 174 ? 47.975 27.627 27.989 1.00 50.70  ? 174 THR A N   1 
ATOM   1226 C CA  . THR A 1 174 ? 48.246 26.993 26.689 1.00 48.64  ? 174 THR A CA  1 
ATOM   1227 C C   . THR A 1 174 ? 47.461 25.741 26.526 1.00 41.31  ? 174 THR A C   1 
ATOM   1228 O O   . THR A 1 174 ? 47.544 24.843 27.364 1.00 37.62  ? 174 THR A O   1 
ATOM   1229 C CB  . THR A 1 174 ? 49.660 26.498 26.523 1.00 41.93  ? 174 THR A CB  1 
ATOM   1230 O OG1 . THR A 1 174 ? 49.632 25.318 25.697 1.00 25.78  ? 174 THR A OG1 1 
ATOM   1231 C CG2 . THR A 1 174 ? 50.306 26.102 27.841 1.00 26.55  ? 174 THR A CG2 1 
ATOM   1232 N N   . PRO A 1 175 ? 46.673 25.612 25.527 1.00 28.89  ? 175 PRO A N   1 
ATOM   1233 C CA  . PRO A 1 175 ? 45.959 24.355 25.281 1.00 26.85  ? 175 PRO A CA  1 
ATOM   1234 C C   . PRO A 1 175 ? 46.832 23.079 25.017 1.00 19.89  ? 175 PRO A C   1 
ATOM   1235 O O   . PRO A 1 175 ? 46.307 22.060 24.462 1.00 21.56  ? 175 PRO A O   1 
ATOM   1236 C CB  . PRO A 1 175 ? 45.129 24.666 24.073 1.00 33.28  ? 175 PRO A CB  1 
ATOM   1237 C CG  . PRO A 1 175 ? 45.392 26.124 23.694 1.00 43.18  ? 175 PRO A CG  1 
ATOM   1238 C CD  . PRO A 1 175 ? 46.420 26.698 24.598 1.00 34.41  ? 175 PRO A CD  1 
ATOM   1239 N N   . LYS A 1 176 ? 48.094 23.050 25.392 1.00 10.00  ? 176 LYS A N   1 
ATOM   1240 C CA  . LYS A 1 176 ? 48.922 21.835 25.159 1.00 13.33  ? 176 LYS A CA  1 
ATOM   1241 C C   . LYS A 1 176 ? 48.403 20.689 26.103 1.00 30.45  ? 176 LYS A C   1 
ATOM   1242 O O   . LYS A 1 176 ? 47.999 19.605 25.640 1.00 29.20  ? 176 LYS A O   1 
ATOM   1243 C CB  . LYS A 1 176 ? 50.398 22.194 25.395 1.00 29.53  ? 176 LYS A CB  1 
ATOM   1244 C CG  . LYS A 1 176 ? 51.026 22.844 24.127 1.00 39.60  ? 176 LYS A CG  1 
ATOM   1245 C CD  . LYS A 1 176 ? 51.642 24.231 24.368 1.00 35.39  ? 176 LYS A CD  1 
ATOM   1246 C CE  . LYS A 1 176 ? 53.093 24.320 23.881 1.00 34.41  ? 176 LYS A CE  1 
ATOM   1247 N NZ  . LYS A 1 176 ? 53.971 25.006 24.841 1.00 8.81   ? 176 LYS A NZ  1 
ATOM   1248 N N   . ASN A 1 177 ? 48.413 20.995 27.370 1.00 38.86  ? 177 ASN A N   1 
ATOM   1249 C CA  . ASN A 1 177 ? 47.958 20.124 28.480 1.00 36.02  ? 177 ASN A CA  1 
ATOM   1250 C C   . ASN A 1 177 ? 46.606 19.410 28.163 1.00 44.16  ? 177 ASN A C   1 
ATOM   1251 O O   . ASN A 1 177 ? 46.558 18.194 27.908 1.00 46.27  ? 177 ASN A O   1 
ATOM   1252 C CB  . ASN A 1 177 ? 47.790 21.027 29.686 1.00 44.45  ? 177 ASN A CB  1 
ATOM   1253 C CG  . ASN A 1 177 ? 49.041 21.885 29.913 1.00 65.31  ? 177 ASN A CG  1 
ATOM   1254 O OD1 . ASN A 1 177 ? 49.198 22.950 29.313 1.00 62.80  ? 177 ASN A OD1 1 
ATOM   1255 N ND2 . ASN A 1 177 ? 49.960 21.466 30.761 1.00 13.87  ? 177 ASN A ND2 1 
ATOM   1256 N N   . ALA A 1 178 ? 45.518 20.179 28.199 1.00 39.37  ? 178 ALA A N   1 
ATOM   1257 C CA  . ALA A 1 178 ? 44.163 19.654 27.903 1.00 36.72  ? 178 ALA A CA  1 
ATOM   1258 C C   . ALA A 1 178 ? 44.139 19.179 26.453 1.00 36.86  ? 178 ALA A C   1 
ATOM   1259 O O   . ALA A 1 178 ? 43.160 18.605 25.989 1.00 32.10  ? 178 ALA A O   1 
ATOM   1260 C CB  . ALA A 1 178 ? 43.117 20.751 28.104 1.00 38.52  ? 178 ALA A CB  1 
ATOM   1261 N N   . LEU A 1 179 ? 45.237 19.435 25.745 1.00 36.06  ? 179 LEU A N   1 
ATOM   1262 C CA  . LEU A 1 179 ? 45.405 19.056 24.365 1.00 30.52  ? 179 LEU A CA  1 
ATOM   1263 C C   . LEU A 1 179 ? 46.056 17.683 24.289 1.00 34.49  ? 179 LEU A C   1 
ATOM   1264 O O   . LEU A 1 179 ? 45.653 16.751 23.567 1.00 32.61  ? 179 LEU A O   1 
ATOM   1265 C CB  . LEU A 1 179 ? 44.472 19.571 23.321 1.00 30.37  ? 179 LEU A CB  1 
ATOM   1266 C CG  . LEU A 1 179 ? 45.244 20.255 22.172 1.00 27.87  ? 179 LEU A CG  1 
ATOM   1267 C CD1 . LEU A 1 179 ? 45.052 21.703 22.186 1.00 25.79  ? 179 LEU A CD1 1 
ATOM   1268 C CD2 . LEU A 1 179 ? 46.743 19.996 22.367 1.00 24.87  ? 179 LEU A CD2 1 
ATOM   1269 N N   . GLU A 1 180 ? 47.099 17.602 25.104 1.00 32.00  ? 180 GLU A N   1 
ATOM   1270 C CA  . GLU A 1 180 ? 47.943 16.441 25.268 1.00 32.13  ? 180 GLU A CA  1 
ATOM   1271 C C   . GLU A 1 180 ? 47.339 15.432 26.244 1.00 33.47  ? 180 GLU A C   1 
ATOM   1272 O O   . GLU A 1 180 ? 47.915 14.381 26.463 1.00 35.91  ? 180 GLU A O   1 
ATOM   1273 C CB  . GLU A 1 180 ? 49.153 17.188 25.822 1.00 32.99  ? 180 GLU A CB  1 
ATOM   1274 C CG  . GLU A 1 180 ? 49.846 16.521 26.919 1.00 53.37  ? 180 GLU A CG  1 
ATOM   1275 C CD  . GLU A 1 180 ? 51.225 16.789 26.664 1.00 40.13  ? 180 GLU A CD  1 
ATOM   1276 O OE1 . GLU A 1 180 ? 52.121 16.061 27.212 1.00 30.62  ? 180 GLU A OE1 1 
ATOM   1277 O OE2 . GLU A 1 180 ? 51.376 17.764 25.891 1.00 35.21  ? 180 GLU A OE2 1 
ATOM   1278 N N   . VAL A 1 181 ? 46.182 15.739 26.833 1.00 27.39  ? 181 VAL A N   1 
ATOM   1279 C CA  . VAL A 1 181 ? 45.557 14.810 27.771 1.00 24.30  ? 181 VAL A CA  1 
ATOM   1280 C C   . VAL A 1 181 ? 44.544 13.916 27.082 1.00 48.60  ? 181 VAL A C   1 
ATOM   1281 O O   . VAL A 1 181 ? 44.417 12.749 27.465 1.00 61.83  ? 181 VAL A O   1 
ATOM   1282 C CB  . VAL A 1 181 ? 44.901 15.418 29.043 1.00 25.54  ? 181 VAL A CB  1 
ATOM   1283 C CG1 . VAL A 1 181 ? 44.240 14.351 29.984 1.00 21.25  ? 181 VAL A CG1 1 
ATOM   1284 C CG2 . VAL A 1 181 ? 45.894 16.227 29.920 1.00 22.01  ? 181 VAL A CG2 1 
ATOM   1285 N N   . ALA A 1 182 ? 43.812 14.441 26.089 1.00 39.61  ? 182 ALA A N   1 
ATOM   1286 C CA  . ALA A 1 182 ? 42.791 13.675 25.342 1.00 38.82  ? 182 ALA A CA  1 
ATOM   1287 C C   . ALA A 1 182 ? 43.376 12.963 24.092 1.00 51.06  ? 182 ALA A C   1 
ATOM   1288 O O   . ALA A 1 182 ? 42.703 12.141 23.433 1.00 45.24  ? 182 ALA A O   1 
ATOM   1289 C CB  . ALA A 1 182 ? 41.608 14.584 24.952 1.00 36.30  ? 182 ALA A CB  1 
ATOM   1290 N N   . GLY A 1 183 ? 44.652 13.309 23.793 1.00 49.87  ? 183 GLY A N   1 
ATOM   1291 C CA  . GLY A 1 183 ? 45.423 12.776 22.677 1.00 48.63  ? 183 GLY A CA  1 
ATOM   1292 C C   . GLY A 1 183 ? 46.056 11.477 23.120 1.00 56.08  ? 183 GLY A C   1 
ATOM   1293 O O   . GLY A 1 183 ? 46.193 10.564 22.320 1.00 59.33  ? 183 GLY A O   1 
ATOM   1294 N N   . TYR A 1 184 ? 46.434 11.409 24.402 1.00 54.01  ? 184 TYR A N   1 
ATOM   1295 C CA  . TYR A 1 184 ? 47.049 10.229 25.014 1.00 57.86  ? 184 TYR A CA  1 
ATOM   1296 C C   . TYR A 1 184 ? 45.851 9.389  25.386 1.00 63.02  ? 184 TYR A C   1 
ATOM   1297 O O   . TYR A 1 184 ? 45.751 8.207  25.062 1.00 59.67  ? 184 TYR A O   1 
ATOM   1298 C CB  . TYR A 1 184 ? 47.765 10.651 26.370 1.00 60.57  ? 184 TYR A CB  1 
ATOM   1299 C CG  . TYR A 1 184 ? 47.993 9.526  27.521 1.00 61.61  ? 184 TYR A CG  1 
ATOM   1300 C CD1 . TYR A 1 184 ? 49.271 9.199  27.932 1.00 61.53  ? 184 TYR A CD1 1 
ATOM   1301 C CD2 . TYR A 1 184 ? 46.960 8.860  28.210 1.00 62.63  ? 184 TYR A CD2 1 
ATOM   1302 C CE1 . TYR A 1 184 ? 49.566 8.295  28.927 1.00 63.45  ? 184 TYR A CE1 1 
ATOM   1303 C CE2 . TYR A 1 184 ? 47.239 7.902  29.234 1.00 63.81  ? 184 TYR A CE2 1 
ATOM   1304 C CZ  . TYR A 1 184 ? 48.568 7.630  29.611 1.00 78.53  ? 184 TYR A CZ  1 
ATOM   1305 O OH  . TYR A 1 184 ? 48.958 6.729  30.588 1.00 87.07  ? 184 TYR A OH  1 
ATOM   1306 N N   . ALA A 1 185 ? 44.938 10.066 26.077 1.00 58.84  ? 185 ALA A N   1 
ATOM   1307 C CA  . ALA A 1 185 ? 43.691 9.487  26.548 1.00 56.17  ? 185 ALA A CA  1 
ATOM   1308 C C   . ALA A 1 185 ? 43.034 8.757  25.403 1.00 42.69  ? 185 ALA A C   1 
ATOM   1309 O O   . ALA A 1 185 ? 42.352 7.766  25.600 1.00 40.49  ? 185 ALA A O   1 
ATOM   1310 C CB  . ALA A 1 185 ? 42.701 10.622 26.937 1.00 55.23  ? 185 ALA A CB  1 
ATOM   1311 N N   . HIS A 1 186 ? 43.245 9.252  24.211 1.00 33.60  ? 186 HIS A N   1 
ATOM   1312 C CA  . HIS A 1 186 ? 42.642 8.618  23.059 1.00 32.98  ? 186 HIS A CA  1 
ATOM   1313 C C   . HIS A 1 186 ? 43.374 7.356  22.671 1.00 32.86  ? 186 HIS A C   1 
ATOM   1314 O O   . HIS A 1 186 ? 42.766 6.447  22.108 1.00 36.37  ? 186 HIS A O   1 
ATOM   1315 C CB  . HIS A 1 186 ? 42.114 9.671  22.052 1.00 34.93  ? 186 HIS A CB  1 
ATOM   1316 C CG  . HIS A 1 186 ? 42.051 9.190  20.665 1.00 38.51  ? 186 HIS A CG  1 
ATOM   1317 N ND1 . HIS A 1 186 ? 40.879 9.002  19.984 1.00 39.86  ? 186 HIS A ND1 1 
ATOM   1318 C CD2 . HIS A 1 186 ? 43.031 8.828  19.815 1.00 43.74  ? 186 HIS A CD2 1 
ATOM   1319 C CE1 . HIS A 1 186 ? 41.137 8.557  18.768 1.00 42.43  ? 186 HIS A CE1 1 
ATOM   1320 N NE2 . HIS A 1 186 ? 42.444 8.441  18.636 1.00 44.51  ? 186 HIS A NE2 1 
ATOM   1321 N N   . GLY A 1 187 ? 44.665 7.317  22.991 1.00 41.73  ? 187 GLY A N   1 
ATOM   1322 C CA  . GLY A 1 187 ? 45.544 6.154  22.698 1.00 49.78  ? 187 GLY A CA  1 
ATOM   1323 C C   . GLY A 1 187 ? 45.034 4.834  23.294 1.00 61.49  ? 187 GLY A C   1 
ATOM   1324 O O   . GLY A 1 187 ? 45.097 3.765  22.683 1.00 57.24  ? 187 GLY A O   1 
ATOM   1325 N N   . ILE A 1 188 ? 44.549 4.926  24.511 1.00 67.75  ? 188 ILE A N   1 
ATOM   1326 C CA  . ILE A 1 188 ? 44.036 3.738  25.135 1.00 75.09  ? 188 ILE A CA  1 
ATOM   1327 C C   . ILE A 1 188 ? 43.840 4.057  26.601 1.00 83.90  ? 188 ILE A C   1 
ATOM   1328 O O   . ILE A 1 188 ? 44.200 5.141  27.051 1.00 77.88  ? 188 ILE A O   1 
ATOM   1329 C CB  . ILE A 1 188 ? 42.594 3.537  24.514 1.00 81.73  ? 188 ILE A CB  1 
ATOM   1330 C CG1 . ILE A 1 188 ? 42.484 2.404  23.477 1.00 85.94  ? 188 ILE A CG1 1 
ATOM   1331 C CG2 . ILE A 1 188 ? 41.674 4.750  24.714 1.00 77.72  ? 188 ILE A CG2 1 
ATOM   1332 C CD1 . ILE A 1 188 ? 41.707 2.850  22.251 1.00 100.00 ? 188 ILE A CD1 1 
ATOM   1333 N N   . PRO A 1 189 ? 43.292 3.146  27.378 1.00 88.25  ? 189 PRO A N   1 
ATOM   1334 C CA  . PRO A 1 189 ? 42.847 1.838  26.938 1.00 88.70  ? 189 PRO A CA  1 
ATOM   1335 C C   . PRO A 1 189 ? 41.340 1.702  26.594 1.00 87.50  ? 189 PRO A C   1 
ATOM   1336 O O   . PRO A 1 189 ? 40.892 0.596  26.341 1.00 88.09  ? 189 PRO A O   1 
ATOM   1337 C CB  . PRO A 1 189 ? 42.861 1.146  28.264 1.00 92.25  ? 189 PRO A CB  1 
ATOM   1338 C CG  . PRO A 1 189 ? 42.357 2.153  29.283 1.00 99.57  ? 189 PRO A CG  1 
ATOM   1339 C CD  . PRO A 1 189 ? 42.594 3.549  28.642 1.00 91.77  ? 189 PRO A CD  1 
ATOM   1340 N N   . ASN A 1 190 ? 40.600 2.806  26.613 1.00 71.73  ? 190 ASN A N   1 
ATOM   1341 C CA  . ASN A 1 190 ? 39.164 2.942  26.347 1.00 60.67  ? 190 ASN A CA  1 
ATOM   1342 C C   . ASN A 1 190 ? 38.628 3.892  27.423 1.00 46.42  ? 190 ASN A C   1 
ATOM   1343 O O   . ASN A 1 190 ? 37.479 3.848  27.843 1.00 25.70  ? 190 ASN A O   1 
ATOM   1344 C CB  . ASN A 1 190 ? 38.331 1.683  26.071 1.00 61.88  ? 190 ASN A CB  1 
ATOM   1345 C CG  . ASN A 1 190 ? 38.266 0.615  27.238 1.00 50.03  ? 190 ASN A CG  1 
ATOM   1346 O OD1 . ASN A 1 190 ? 39.190 0.374  28.020 1.00 51.65  ? 190 ASN A OD1 1 
ATOM   1347 N ND2 . ASN A 1 190 ? 37.177 -0.092 27.226 1.00 12.61  ? 190 ASN A ND2 1 
ATOM   1348 N N   . ALA A 1 191 ? 39.538 4.779  27.845 1.00 54.05  ? 191 ALA A N   1 
ATOM   1349 C CA  . ALA A 1 191 ? 39.271 5.789  28.854 1.00 56.02  ? 191 ALA A CA  1 
ATOM   1350 C C   . ALA A 1 191 ? 38.198 6.742  28.376 1.00 58.74  ? 191 ALA A C   1 
ATOM   1351 O O   . ALA A 1 191 ? 37.462 6.438  27.443 1.00 56.15  ? 191 ALA A O   1 
ATOM   1352 C CB  . ALA A 1 191 ? 40.530 6.556  29.243 1.00 57.24  ? 191 ALA A CB  1 
ATOM   1353 N N   . ILE A 1 192 ? 38.106 7.904  29.022 1.00 61.30  ? 192 ILE A N   1 
ATOM   1354 C CA  . ILE A 1 192 ? 37.120 8.933  28.675 1.00 58.47  ? 192 ILE A CA  1 
ATOM   1355 C C   . ILE A 1 192 ? 37.646 10.363 28.833 1.00 59.28  ? 192 ILE A C   1 
ATOM   1356 O O   . ILE A 1 192 ? 38.354 10.685 29.797 1.00 60.90  ? 192 ILE A O   1 
ATOM   1357 C CB  . ILE A 1 192 ? 35.570 8.689  29.229 1.00 56.66  ? 192 ILE A CB  1 
ATOM   1358 C CG1 . ILE A 1 192 ? 34.515 9.561  28.524 1.00 52.45  ? 192 ILE A CG1 1 
ATOM   1359 C CG2 . ILE A 1 192 ? 35.361 9.029  30.680 1.00 54.12  ? 192 ILE A CG2 1 
ATOM   1360 C CD1 . ILE A 1 192 ? 33.719 8.857  27.471 1.00 43.80  ? 192 ILE A CD1 1 
ATOM   1361 N N   . PHE A 1 193 ? 37.284 11.209 27.858 1.00 45.12  ? 193 PHE A N   1 
ATOM   1362 C CA  . PHE A 1 193 ? 37.686 12.618 27.844 1.00 39.07  ? 193 PHE A CA  1 
ATOM   1363 C C   . PHE A 1 193 ? 36.471 13.504 27.948 1.00 35.53  ? 193 PHE A C   1 
ATOM   1364 O O   . PHE A 1 193 ? 35.565 13.465 27.112 1.00 38.93  ? 193 PHE A O   1 
ATOM   1365 C CB  . PHE A 1 193 ? 38.391 13.241 26.775 1.00 41.10  ? 193 PHE A CB  1 
ATOM   1366 C CG  . PHE A 1 193 ? 39.031 14.481 27.246 1.00 36.83  ? 193 PHE A CG  1 
ATOM   1367 C CD1 . PHE A 1 193 ? 38.721 15.675 26.738 1.00 27.24  ? 193 PHE A CD1 1 
ATOM   1368 C CD2 . PHE A 1 193 ? 39.966 14.398 28.256 1.00 31.48  ? 193 PHE A CD2 1 
ATOM   1369 C CE1 . PHE A 1 193 ? 39.321 16.811 27.169 1.00 21.62  ? 193 PHE A CE1 1 
ATOM   1370 C CE2 . PHE A 1 193 ? 40.607 15.511 28.730 1.00 26.31  ? 193 PHE A CE2 1 
ATOM   1371 C CZ  . PHE A 1 193 ? 40.280 16.722 28.182 1.00 19.48  ? 193 PHE A CZ  1 
ATOM   1372 N N   . THR A 1 194 ? 36.452 14.302 28.987 1.00 34.04  ? 194 THR A N   1 
ATOM   1373 C CA  . THR A 1 194 ? 35.331 15.199 29.222 1.00 28.27  ? 194 THR A CA  1 
ATOM   1374 C C   . THR A 1 194 ? 35.798 16.634 29.315 1.00 25.84  ? 194 THR A C   1 
ATOM   1375 O O   . THR A 1 194 ? 36.765 16.931 30.004 1.00 28.20  ? 194 THR A O   1 
ATOM   1376 C CB  . THR A 1 194 ? 35.014 14.723 30.702 1.00 23.34  ? 194 THR A CB  1 
ATOM   1377 O OG1 . THR A 1 194 ? 36.275 14.486 31.349 1.00 17.92  ? 194 THR A OG1 1 
ATOM   1378 C CG2 . THR A 1 194 ? 34.377 13.347 30.743 1.00 8.68   ? 194 THR A CG2 1 
ATOM   1379 N N   . LEU A 1 195 ? 35.148 17.555 28.638 1.00 28.16  ? 195 LEU A N   1 
ATOM   1380 C CA  . LEU A 1 195 ? 35.640 18.928 28.774 1.00 32.66  ? 195 LEU A CA  1 
ATOM   1381 C C   . LEU A 1 195 ? 34.509 19.830 29.211 1.00 36.65  ? 195 LEU A C   1 
ATOM   1382 O O   . LEU A 1 195 ? 33.368 19.612 28.790 1.00 33.93  ? 195 LEU A O   1 
ATOM   1383 C CB  . LEU A 1 195 ? 36.524 19.486 27.606 1.00 33.97  ? 195 LEU A CB  1 
ATOM   1384 C CG  . LEU A 1 195 ? 36.605 21.044 27.274 1.00 31.72  ? 195 LEU A CG  1 
ATOM   1385 C CD1 . LEU A 1 195 ? 38.048 21.646 27.308 1.00 24.08  ? 195 LEU A CD1 1 
ATOM   1386 C CD2 . LEU A 1 195 ? 35.956 21.319 25.938 1.00 27.01  ? 195 LEU A CD2 1 
ATOM   1387 N N   . ASN A 1 196 ? 34.814 20.833 30.033 1.00 40.86  ? 196 ASN A N   1 
ATOM   1388 C CA  . ASN A 1 196 ? 33.798 21.763 30.505 1.00 42.82  ? 196 ASN A CA  1 
ATOM   1389 C C   . ASN A 1 196 ? 33.965 23.180 29.956 1.00 47.69  ? 196 ASN A C   1 
ATOM   1390 O O   . ASN A 1 196 ? 34.895 23.902 30.336 1.00 50.77  ? 196 ASN A O   1 
ATOM   1391 C CB  . ASN A 1 196 ? 33.387 21.617 31.942 1.00 50.39  ? 196 ASN A CB  1 
ATOM   1392 C CG  . ASN A 1 196 ? 34.207 22.356 32.884 1.00 62.00  ? 196 ASN A CG  1 
ATOM   1393 O OD1 . ASN A 1 196 ? 34.244 21.917 34.023 1.00 50.39  ? 196 ASN A OD1 1 
ATOM   1394 N ND2 . ASN A 1 196 ? 34.799 23.497 32.554 1.00 68.01  ? 196 ASN A ND2 1 
ATOM   1395 N N   . LEU A 1 197 ? 33.034 23.547 29.084 1.00 36.64  ? 197 LEU A N   1 
ATOM   1396 C CA  . LEU A 1 197 ? 32.923 24.828 28.388 1.00 27.64  ? 197 LEU A CA  1 
ATOM   1397 C C   . LEU A 1 197 ? 33.484 26.009 29.154 1.00 33.22  ? 197 LEU A C   1 
ATOM   1398 O O   . LEU A 1 197 ? 33.859 27.015 28.563 1.00 39.34  ? 197 LEU A O   1 
ATOM   1399 C CB  . LEU A 1 197 ? 31.516 25.147 28.011 1.00 23.61  ? 197 LEU A CB  1 
ATOM   1400 C CG  . LEU A 1 197 ? 30.956 24.152 26.970 1.00 27.20  ? 197 LEU A CG  1 
ATOM   1401 C CD1 . LEU A 1 197 ? 31.293 24.558 25.493 1.00 28.47  ? 197 LEU A CD1 1 
ATOM   1402 C CD2 . LEU A 1 197 ? 31.184 22.643 27.225 1.00 22.55  ? 197 LEU A CD2 1 
ATOM   1403 N N   . SER A 1 198 ? 33.537 25.895 30.460 1.00 31.90  ? 198 SER A N   1 
ATOM   1404 C CA  . SER A 1 198 ? 34.049 26.959 31.298 1.00 30.85  ? 198 SER A CA  1 
ATOM   1405 C C   . SER A 1 198 ? 33.347 28.304 31.101 1.00 30.53  ? 198 SER A C   1 
ATOM   1406 O O   . SER A 1 198 ? 32.131 28.383 31.159 1.00 23.78  ? 198 SER A O   1 
ATOM   1407 C CB  . SER A 1 198 ? 35.509 26.922 31.570 1.00 35.25  ? 198 SER A CB  1 
ATOM   1408 O OG  . SER A 1 198 ? 35.790 25.843 32.488 1.00 37.85  ? 198 SER A OG  1 
ATOM   1409 N N   . ALA A 1 199 ? 34.084 29.365 30.854 1.00 31.45  ? 199 ALA A N   1 
ATOM   1410 C CA  . ALA A 1 199 ? 33.452 30.669 30.665 1.00 28.32  ? 199 ALA A CA  1 
ATOM   1411 C C   . ALA A 1 199 ? 33.259 31.036 29.186 1.00 51.27  ? 199 ALA A C   1 
ATOM   1412 O O   . ALA A 1 199 ? 33.615 30.261 28.302 1.00 54.32  ? 199 ALA A O   1 
ATOM   1413 C CB  . ALA A 1 199 ? 34.490 31.696 31.277 1.00 22.24  ? 199 ALA A CB  1 
ATOM   1414 N N   . PRO A 1 200 ? 32.687 32.235 28.939 1.00 51.95  ? 200 PRO A N   1 
ATOM   1415 C CA  . PRO A 1 200 ? 32.447 32.735 27.586 1.00 49.61  ? 200 PRO A CA  1 
ATOM   1416 C C   . PRO A 1 200 ? 33.801 33.026 26.990 1.00 50.13  ? 200 PRO A C   1 
ATOM   1417 O O   . PRO A 1 200 ? 34.029 32.868 25.790 1.00 49.29  ? 200 PRO A O   1 
ATOM   1418 C CB  . PRO A 1 200 ? 31.580 33.964 27.804 1.00 48.58  ? 200 PRO A CB  1 
ATOM   1419 C CG  . PRO A 1 200 ? 30.639 33.378 28.805 1.00 51.06  ? 200 PRO A CG  1 
ATOM   1420 C CD  . PRO A 1 200 ? 31.459 32.476 29.721 1.00 48.00  ? 200 PRO A CD  1 
ATOM   1421 N N   . PHE A 1 201 ? 34.706 33.414 27.861 1.00 51.89  ? 201 PHE A N   1 
ATOM   1422 C CA  . PHE A 1 201 ? 36.052 33.715 27.426 1.00 55.58  ? 201 PHE A CA  1 
ATOM   1423 C C   . PHE A 1 201 ? 36.659 32.453 26.760 1.00 66.25  ? 201 PHE A C   1 
ATOM   1424 O O   . PHE A 1 201 ? 36.989 32.508 25.584 1.00 66.94  ? 201 PHE A O   1 
ATOM   1425 C CB  . PHE A 1 201 ? 36.832 34.359 28.589 1.00 59.33  ? 201 PHE A CB  1 
ATOM   1426 C CG  . PHE A 1 201 ? 37.630 33.415 29.491 1.00 64.51  ? 201 PHE A CG  1 
ATOM   1427 C CD1 . PHE A 1 201 ? 38.868 32.946 29.061 1.00 73.40  ? 201 PHE A CD1 1 
ATOM   1428 C CD2 . PHE A 1 201 ? 37.170 33.022 30.780 1.00 63.55  ? 201 PHE A CD2 1 
ATOM   1429 C CE1 . PHE A 1 201 ? 39.605 32.095 29.888 1.00 75.34  ? 201 PHE A CE1 1 
ATOM   1430 C CE2 . PHE A 1 201 ? 37.901 32.181 31.591 1.00 67.24  ? 201 PHE A CE2 1 
ATOM   1431 C CZ  . PHE A 1 201 ? 39.114 31.725 31.144 1.00 68.93  ? 201 PHE A CZ  1 
ATOM   1432 N N   . CYS A 1 202 ? 36.778 31.334 27.498 1.00 62.49  ? 202 CYS A N   1 
ATOM   1433 C CA  . CYS A 1 202 ? 37.333 30.061 26.983 1.00 59.40  ? 202 CYS A CA  1 
ATOM   1434 C C   . CYS A 1 202 ? 36.789 29.703 25.611 1.00 52.68  ? 202 CYS A C   1 
ATOM   1435 O O   . CYS A 1 202 ? 37.532 29.365 24.667 1.00 38.40  ? 202 CYS A O   1 
ATOM   1436 C CB  . CYS A 1 202 ? 36.768 28.885 27.790 1.00 59.79  ? 202 CYS A CB  1 
ATOM   1437 S SG  . CYS A 1 202 ? 37.621 28.708 29.366 1.00 65.25  ? 202 CYS A SG  1 
ATOM   1438 N N   . VAL A 1 203 ? 35.470 29.799 25.549 1.00 44.97  ? 203 VAL A N   1 
ATOM   1439 C CA  . VAL A 1 203 ? 34.784 29.499 24.348 1.00 43.25  ? 203 VAL A CA  1 
ATOM   1440 C C   . VAL A 1 203 ? 35.121 30.451 23.219 1.00 57.93  ? 203 VAL A C   1 
ATOM   1441 O O   . VAL A 1 203 ? 35.706 30.028 22.226 1.00 57.42  ? 203 VAL A O   1 
ATOM   1442 C CB  . VAL A 1 203 ? 33.358 29.669 24.603 1.00 44.07  ? 203 VAL A CB  1 
ATOM   1443 C CG1 . VAL A 1 203 ? 32.661 29.726 23.270 1.00 44.75  ? 203 VAL A CG1 1 
ATOM   1444 C CG2 . VAL A 1 203 ? 32.987 28.474 25.486 1.00 45.62  ? 203 VAL A CG2 1 
ATOM   1445 N N   . GLU A 1 204 ? 34.761 31.698 23.366 1.00 54.81  ? 204 GLU A N   1 
ATOM   1446 C CA  . GLU A 1 204 ? 34.989 32.754 22.386 1.00 51.93  ? 204 GLU A CA  1 
ATOM   1447 C C   . GLU A 1 204 ? 36.420 33.195 22.263 1.00 48.80  ? 204 GLU A C   1 
ATOM   1448 O O   . GLU A 1 204 ? 36.878 33.518 21.159 1.00 46.00  ? 204 GLU A O   1 
ATOM   1449 C CB  . GLU A 1 204 ? 34.382 34.007 22.904 1.00 53.25  ? 204 GLU A CB  1 
ATOM   1450 C CG  . GLU A 1 204 ? 33.878 34.904 21.832 1.00 59.95  ? 204 GLU A CG  1 
ATOM   1451 C CD  . GLU A 1 204 ? 32.701 35.565 22.428 1.00 77.66  ? 204 GLU A CD  1 
ATOM   1452 O OE1 . GLU A 1 204 ? 31.586 35.389 21.873 1.00 73.40  ? 204 GLU A OE1 1 
ATOM   1453 O OE2 . GLU A 1 204 ? 32.954 36.206 23.499 1.00 63.32  ? 204 GLU A OE2 1 
ATOM   1454 N N   . LEU A 1 205 ? 37.119 33.234 23.388 1.00 47.55  ? 205 LEU A N   1 
ATOM   1455 C CA  . LEU A 1 205 ? 38.498 33.661 23.415 1.00 48.68  ? 205 LEU A CA  1 
ATOM   1456 C C   . LEU A 1 205 ? 39.431 32.475 23.307 1.00 59.96  ? 205 LEU A C   1 
ATOM   1457 O O   . LEU A 1 205 ? 40.524 32.544 23.890 1.00 60.55  ? 205 LEU A O   1 
ATOM   1458 C CB  . LEU A 1 205 ? 38.841 34.612 24.633 1.00 44.66  ? 205 LEU A CB  1 
ATOM   1459 C CG  . LEU A 1 205 ? 37.959 35.872 24.687 1.00 43.30  ? 205 LEU A CG  1 
ATOM   1460 C CD1 . LEU A 1 205 ? 36.505 35.619 25.131 1.00 42.51  ? 205 LEU A CD1 1 
ATOM   1461 C CD2 . LEU A 1 205 ? 38.638 37.082 25.337 1.00 34.64  ? 205 LEU A CD2 1 
ATOM   1462 N N   . TYR A 1 206 ? 38.998 31.391 22.598 1.00 61.22  ? 206 TYR A N   1 
ATOM   1463 C CA  . TYR A 1 206 ? 39.814 30.166 22.419 1.00 63.01  ? 206 TYR A CA  1 
ATOM   1464 C C   . TYR A 1 206 ? 39.728 29.499 21.015 1.00 64.71  ? 206 TYR A C   1 
ATOM   1465 O O   . TYR A 1 206 ? 40.773 29.143 20.468 1.00 65.02  ? 206 TYR A O   1 
ATOM   1466 C CB  . TYR A 1 206 ? 40.213 29.292 23.667 1.00 65.84  ? 206 TYR A CB  1 
ATOM   1467 C CG  . TYR A 1 206 ? 41.607 29.643 24.247 1.00 64.28  ? 206 TYR A CG  1 
ATOM   1468 C CD1 . TYR A 1 206 ? 41.724 30.512 25.323 1.00 65.60  ? 206 TYR A CD1 1 
ATOM   1469 C CD2 . TYR A 1 206 ? 42.761 29.101 23.748 1.00 61.67  ? 206 TYR A CD2 1 
ATOM   1470 C CE1 . TYR A 1 206 ? 42.919 30.892 25.860 1.00 64.04  ? 206 TYR A CE1 1 
ATOM   1471 C CE2 . TYR A 1 206 ? 43.974 29.443 24.293 1.00 63.41  ? 206 TYR A CE2 1 
ATOM   1472 C CZ  . TYR A 1 206 ? 44.058 30.344 25.350 1.00 82.24  ? 206 TYR A CZ  1 
ATOM   1473 O OH  . TYR A 1 206 ? 45.300 30.699 25.904 1.00 96.38  ? 206 TYR A OH  1 
ATOM   1474 N N   . LYS A 1 207 ? 38.522 29.329 20.443 1.00 64.97  ? 207 LYS A N   1 
ATOM   1475 C CA  . LYS A 1 207 ? 38.298 28.718 19.117 1.00 68.96  ? 207 LYS A CA  1 
ATOM   1476 C C   . LYS A 1 207 ? 39.280 27.605 18.699 1.00 81.46  ? 207 LYS A C   1 
ATOM   1477 O O   . LYS A 1 207 ? 39.362 26.575 19.353 1.00 86.69  ? 207 LYS A O   1 
ATOM   1478 C CB  . LYS A 1 207 ? 38.312 29.782 18.005 1.00 66.40  ? 207 LYS A CB  1 
ATOM   1479 C CG  . LYS A 1 207 ? 37.013 29.930 17.204 1.00 64.30  ? 207 LYS A CG  1 
ATOM   1480 C CD  . LYS A 1 207 ? 37.243 29.757 15.712 1.00 72.61  ? 207 LYS A CD  1 
ATOM   1481 C CE  . LYS A 1 207 ? 36.003 29.959 14.828 1.00 77.07  ? 207 LYS A CE  1 
ATOM   1482 N NZ  . LYS A 1 207 ? 35.385 28.629 14.395 1.00 69.75  ? 207 LYS A NZ  1 
ATOM   1483 N N   . ASP A 1 208 ? 40.008 27.848 17.587 1.00 72.40  ? 208 ASP A N   1 
ATOM   1484 C CA  . ASP A 1 208 ? 41.018 26.958 16.953 1.00 69.61  ? 208 ASP A CA  1 
ATOM   1485 C C   . ASP A 1 208 ? 41.565 25.823 17.829 1.00 71.60  ? 208 ASP A C   1 
ATOM   1486 O O   . ASP A 1 208 ? 42.008 24.798 17.314 1.00 78.71  ? 208 ASP A O   1 
ATOM   1487 C CB  . ASP A 1 208 ? 42.188 27.674 16.214 1.00 70.74  ? 208 ASP A CB  1 
ATOM   1488 C CG  . ASP A 1 208 ? 41.766 28.705 15.161 1.00 73.52  ? 208 ASP A CG  1 
ATOM   1489 O OD1 . ASP A 1 208 ? 41.431 29.833 15.540 1.00 75.80  ? 208 ASP A OD1 1 
ATOM   1490 O OD2 . ASP A 1 208 ? 41.846 28.455 13.931 1.00 76.92  ? 208 ASP A OD2 1 
ATOM   1491 N N   . ALA A 1 209 ? 41.544 25.992 19.144 1.00 52.79  ? 209 ALA A N   1 
ATOM   1492 C CA  . ALA A 1 209 ? 42.040 24.950 20.034 1.00 48.72  ? 209 ALA A CA  1 
ATOM   1493 C C   . ALA A 1 209 ? 40.892 23.985 20.325 1.00 57.22  ? 209 ALA A C   1 
ATOM   1494 O O   . ALA A 1 209 ? 41.051 22.771 20.219 1.00 57.00  ? 209 ALA A O   1 
ATOM   1495 C CB  . ALA A 1 209 ? 42.636 25.524 21.331 1.00 46.53  ? 209 ALA A CB  1 
ATOM   1496 N N   . MET A 1 210 ? 39.734 24.537 20.688 1.00 46.98  ? 210 MET A N   1 
ATOM   1497 C CA  . MET A 1 210 ? 38.543 23.755 20.997 1.00 42.74  ? 210 MET A CA  1 
ATOM   1498 C C   . MET A 1 210 ? 38.079 22.900 19.831 1.00 39.71  ? 210 MET A C   1 
ATOM   1499 O O   . MET A 1 210 ? 37.576 21.800 20.028 1.00 34.45  ? 210 MET A O   1 
ATOM   1500 C CB  . MET A 1 210 ? 37.433 24.626 21.588 1.00 44.81  ? 210 MET A CB  1 
ATOM   1501 C CG  . MET A 1 210 ? 37.776 25.095 23.020 1.00 49.72  ? 210 MET A CG  1 
ATOM   1502 S SD  . MET A 1 210 ? 36.493 25.603 24.247 1.00 58.05  ? 210 MET A SD  1 
ATOM   1503 C CE  . MET A 1 210 ? 34.991 25.170 23.378 1.00 56.54  ? 210 MET A CE  1 
ATOM   1504 N N   . GLN A 1 211 ? 38.248 23.389 18.615 1.00 37.17  ? 211 GLN A N   1 
ATOM   1505 C CA  . GLN A 1 211 ? 37.826 22.612 17.455 1.00 42.04  ? 211 GLN A CA  1 
ATOM   1506 C C   . GLN A 1 211 ? 38.483 21.218 17.453 1.00 50.53  ? 211 GLN A C   1 
ATOM   1507 O O   . GLN A 1 211 ? 37.853 20.223 17.089 1.00 54.83  ? 211 GLN A O   1 
ATOM   1508 C CB  . GLN A 1 211 ? 37.560 23.412 16.126 1.00 45.35  ? 211 GLN A CB  1 
ATOM   1509 C CG  . GLN A 1 211 ? 36.028 23.742 15.654 1.00 62.78  ? 211 GLN A CG  1 
ATOM   1510 C CD  . GLN A 1 211 ? 35.223 24.922 16.388 1.00 75.71  ? 211 GLN A CD  1 
ATOM   1511 O OE1 . GLN A 1 211 ? 35.793 25.978 16.782 1.00 51.88  ? 211 GLN A OE1 1 
ATOM   1512 N NE2 . GLN A 1 211 ? 33.891 24.732 16.521 1.00 51.24  ? 211 GLN A NE2 1 
ATOM   1513 N N   . SER A 1 212 ? 39.755 21.150 17.846 1.00 46.99  ? 212 SER A N   1 
ATOM   1514 C CA  . SER A 1 212 ? 40.452 19.868 17.877 1.00 53.50  ? 212 SER A CA  1 
ATOM   1515 C C   . SER A 1 212 ? 40.112 19.135 19.175 1.00 56.08  ? 212 SER A C   1 
ATOM   1516 O O   . SER A 1 212 ? 39.780 17.949 19.158 1.00 53.47  ? 212 SER A O   1 
ATOM   1517 C CB  . SER A 1 212 ? 42.022 19.929 17.985 1.00 64.49  ? 212 SER A CB  1 
ATOM   1518 O OG  . SER A 1 212 ? 42.508 19.163 19.112 1.00 54.65  ? 212 SER A OG  1 
ATOM   1519 N N   . LEU A 1 213 ? 40.209 19.882 20.291 1.00 44.99  ? 213 LEU A N   1 
ATOM   1520 C CA  . LEU A 1 213 ? 39.914 19.396 21.634 1.00 38.24  ? 213 LEU A CA  1 
ATOM   1521 C C   . LEU A 1 213 ? 38.564 18.718 21.544 1.00 43.75  ? 213 LEU A C   1 
ATOM   1522 O O   . LEU A 1 213 ? 38.424 17.543 21.900 1.00 45.16  ? 213 LEU A O   1 
ATOM   1523 C CB  . LEU A 1 213 ? 39.668 20.609 22.588 1.00 32.86  ? 213 LEU A CB  1 
ATOM   1524 C CG  . LEU A 1 213 ? 40.115 20.323 24.025 1.00 31.78  ? 213 LEU A CG  1 
ATOM   1525 C CD1 . LEU A 1 213 ? 41.332 19.378 24.019 1.00 20.12  ? 213 LEU A CD1 1 
ATOM   1526 C CD2 . LEU A 1 213 ? 40.367 21.618 24.802 1.00 40.28  ? 213 LEU A CD2 1 
ATOM   1527 N N   . LEU A 1 214 ? 37.583 19.498 21.033 1.00 28.31  ? 214 LEU A N   1 
ATOM   1528 C CA  . LEU A 1 214 ? 36.189 19.073 20.836 1.00 29.36  ? 214 LEU A CA  1 
ATOM   1529 C C   . LEU A 1 214 ? 36.093 17.640 20.336 1.00 44.69  ? 214 LEU A C   1 
ATOM   1530 O O   . LEU A 1 214 ? 35.431 16.787 20.931 1.00 53.01  ? 214 LEU A O   1 
ATOM   1531 C CB  . LEU A 1 214 ? 35.634 19.863 19.664 1.00 32.51  ? 214 LEU A CB  1 
ATOM   1532 C CG  . LEU A 1 214 ? 34.863 21.168 19.837 1.00 47.65  ? 214 LEU A CG  1 
ATOM   1533 C CD1 . LEU A 1 214 ? 35.024 22.036 21.111 1.00 50.11  ? 214 LEU A CD1 1 
ATOM   1534 C CD2 . LEU A 1 214 ? 35.175 21.989 18.645 1.00 54.73  ? 214 LEU A CD2 1 
ATOM   1535 N N   . LEU A 1 215 ? 36.769 17.379 19.234 1.00 45.40  ? 215 LEU A N   1 
ATOM   1536 C CA  . LEU A 1 215 ? 36.760 16.048 18.655 1.00 44.66  ? 215 LEU A CA  1 
ATOM   1537 C C   . LEU A 1 215 ? 37.395 15.034 19.606 1.00 51.05  ? 215 LEU A C   1 
ATOM   1538 O O   . LEU A 1 215 ? 36.876 13.946 19.799 1.00 51.45  ? 215 LEU A O   1 
ATOM   1539 C CB  . LEU A 1 215 ? 37.074 15.964 17.157 1.00 43.26  ? 215 LEU A CB  1 
ATOM   1540 C CG  . LEU A 1 215 ? 37.982 16.941 16.406 1.00 42.72  ? 215 LEU A CG  1 
ATOM   1541 C CD1 . LEU A 1 215 ? 39.100 16.114 15.673 1.00 41.02  ? 215 LEU A CD1 1 
ATOM   1542 C CD2 . LEU A 1 215 ? 37.120 17.754 15.438 1.00 34.27  ? 215 LEU A CD2 1 
ATOM   1543 N N   . HIS A 1 216 ? 38.511 15.373 20.207 1.00 50.53  ? 216 HIS A N   1 
ATOM   1544 C CA  . HIS A 1 216 ? 39.156 14.451 21.126 1.00 53.17  ? 216 HIS A CA  1 
ATOM   1545 C C   . HIS A 1 216 ? 38.511 14.604 22.506 1.00 42.48  ? 216 HIS A C   1 
ATOM   1546 O O   . HIS A 1 216 ? 39.168 14.575 23.569 1.00 28.87  ? 216 HIS A O   1 
ATOM   1547 C CB  . HIS A 1 216 ? 40.675 14.688 21.059 1.00 59.64  ? 216 HIS A CB  1 
ATOM   1548 C CG  . HIS A 1 216 ? 41.240 14.354 19.711 1.00 67.25  ? 216 HIS A CG  1 
ATOM   1549 N ND1 . HIS A 1 216 ? 42.123 15.182 19.031 1.00 72.02  ? 216 HIS A ND1 1 
ATOM   1550 C CD2 . HIS A 1 216 ? 41.037 13.272 18.916 1.00 70.93  ? 216 HIS A CD2 1 
ATOM   1551 C CE1 . HIS A 1 216 ? 42.439 14.600 17.876 1.00 73.27  ? 216 HIS A CE1 1 
ATOM   1552 N NE2 . HIS A 1 216 ? 41.790 13.447 17.783 1.00 72.76  ? 216 HIS A NE2 1 
ATOM   1553 N N   . THR A 1 217 ? 37.197 14.760 22.460 1.00 39.24  ? 217 THR A N   1 
ATOM   1554 C CA  . THR A 1 217 ? 36.403 14.925 23.658 1.00 40.19  ? 217 THR A CA  1 
ATOM   1555 C C   . THR A 1 217 ? 35.247 13.919 23.683 1.00 44.67  ? 217 THR A C   1 
ATOM   1556 O O   . THR A 1 217 ? 34.422 13.853 22.771 1.00 38.27  ? 217 THR A O   1 
ATOM   1557 C CB  . THR A 1 217 ? 36.104 16.447 24.004 1.00 38.37  ? 217 THR A CB  1 
ATOM   1558 O OG1 . THR A 1 217 ? 36.853 16.925 25.098 1.00 57.33  ? 217 THR A OG1 1 
ATOM   1559 C CG2 . THR A 1 217 ? 34.640 16.715 24.421 1.00 29.60  ? 217 THR A CG2 1 
ATOM   1560 N N   . ASN A 1 218 ? 35.199 13.111 24.726 1.00 41.19  ? 218 ASN A N   1 
ATOM   1561 C CA  . ASN A 1 218 ? 34.143 12.130 24.831 1.00 42.23  ? 218 ASN A CA  1 
ATOM   1562 C C   . ASN A 1 218 ? 32.995 12.719 25.646 1.00 52.40  ? 218 ASN A C   1 
ATOM   1563 O O   . ASN A 1 218 ? 31.819 12.387 25.477 1.00 50.11  ? 218 ASN A O   1 
ATOM   1564 C CB  . ASN A 1 218 ? 34.681 10.953 25.586 1.00 45.12  ? 218 ASN A CB  1 
ATOM   1565 C CG  . ASN A 1 218 ? 35.386 9.960  24.716 1.00 48.66  ? 218 ASN A CG  1 
ATOM   1566 O OD1 . ASN A 1 218 ? 36.592 9.771  24.858 1.00 12.15  ? 218 ASN A OD1 1 
ATOM   1567 N ND2 . ASN A 1 218 ? 34.668 9.338  23.821 1.00 13.17  ? 218 ASN A ND2 1 
ATOM   1568 N N   . ILE A 1 219 ? 33.330 13.614 26.539 1.00 52.92  ? 219 ILE A N   1 
ATOM   1569 C CA  . ILE A 1 219 ? 32.323 14.239 27.373 1.00 52.52  ? 219 ILE A CA  1 
ATOM   1570 C C   . ILE A 1 219 ? 32.399 15.762 27.322 1.00 45.95  ? 219 ILE A C   1 
ATOM   1571 O O   . ILE A 1 219 ? 33.445 16.364 27.558 1.00 40.29  ? 219 ILE A O   1 
ATOM   1572 C CB  . ILE A 1 219 ? 31.795 13.486 28.633 1.00 53.52  ? 219 ILE A CB  1 
ATOM   1573 C CG1 . ILE A 1 219 ? 31.208 12.100 28.203 1.00 47.42  ? 219 ILE A CG1 1 
ATOM   1574 C CG2 . ILE A 1 219 ? 30.813 14.416 29.410 1.00 50.63  ? 219 ILE A CG2 1 
ATOM   1575 C CD1 . ILE A 1 219 ? 29.949 11.678 28.936 1.00 17.67  ? 219 ILE A CD1 1 
ATOM   1576 N N   . LEU A 1 220 ? 31.272 16.349 27.011 1.00 39.83  ? 220 LEU A N   1 
ATOM   1577 C CA  . LEU A 1 220 ? 31.144 17.792 26.931 1.00 38.35  ? 220 LEU A CA  1 
ATOM   1578 C C   . LEU A 1 220 ? 30.225 18.236 28.035 1.00 23.66  ? 220 LEU A C   1 
ATOM   1579 O O   . LEU A 1 220 ? 29.005 17.989 28.010 1.00 15.06  ? 220 LEU A O   1 
ATOM   1580 C CB  . LEU A 1 220 ? 30.495 18.427 25.625 1.00 40.76  ? 220 LEU A CB  1 
ATOM   1581 C CG  . LEU A 1 220 ? 30.802 19.965 25.379 1.00 40.60  ? 220 LEU A CG  1 
ATOM   1582 C CD1 . LEU A 1 220 ? 32.262 20.249 25.380 1.00 37.28  ? 220 LEU A CD1 1 
ATOM   1583 C CD2 . LEU A 1 220 ? 30.327 20.458 24.056 1.00 32.74  ? 220 LEU A CD2 1 
ATOM   1584 N N   . PHE A 1 221 ? 30.841 18.907 28.987 1.00 25.78  ? 221 PHE A N   1 
ATOM   1585 C CA  . PHE A 1 221 ? 30.125 19.440 30.141 1.00 31.03  ? 221 PHE A CA  1 
ATOM   1586 C C   . PHE A 1 221 ? 30.020 20.955 30.086 1.00 43.67  ? 221 PHE A C   1 
ATOM   1587 O O   . PHE A 1 221 ? 31.016 21.626 29.773 1.00 44.08  ? 221 PHE A O   1 
ATOM   1588 C CB  . PHE A 1 221 ? 31.045 19.268 31.323 1.00 33.78  ? 221 PHE A CB  1 
ATOM   1589 C CG  . PHE A 1 221 ? 30.961 17.941 31.999 1.00 37.64  ? 221 PHE A CG  1 
ATOM   1590 C CD1 . PHE A 1 221 ? 32.114 17.107 32.070 1.00 32.70  ? 221 PHE A CD1 1 
ATOM   1591 C CD2 . PHE A 1 221 ? 29.760 17.517 32.588 1.00 33.87  ? 221 PHE A CD2 1 
ATOM   1592 C CE1 . PHE A 1 221 ? 32.032 15.914 32.711 1.00 29.83  ? 221 PHE A CE1 1 
ATOM   1593 C CE2 . PHE A 1 221 ? 29.716 16.334 33.205 1.00 30.67  ? 221 PHE A CE2 1 
ATOM   1594 C CZ  . PHE A 1 221 ? 30.837 15.547 33.263 1.00 26.24  ? 221 PHE A CZ  1 
ATOM   1595 N N   . GLY A 1 222 ? 28.811 21.465 30.401 1.00 51.11  ? 222 GLY A N   1 
ATOM   1596 C CA  . GLY A 1 222 ? 28.544 22.909 30.394 1.00 53.73  ? 222 GLY A CA  1 
ATOM   1597 C C   . GLY A 1 222 ? 27.059 23.270 30.573 1.00 46.41  ? 222 GLY A C   1 
ATOM   1598 O O   . GLY A 1 222 ? 26.190 22.415 30.844 1.00 37.41  ? 222 GLY A O   1 
ATOM   1599 N N   . ASN A 1 223 ? 26.790 24.567 30.398 1.00 40.89  ? 223 ASN A N   1 
ATOM   1600 C CA  . ASN A 1 223 ? 25.463 25.178 30.527 1.00 43.10  ? 223 ASN A CA  1 
ATOM   1601 C C   . ASN A 1 223 ? 24.984 25.854 29.214 1.00 50.75  ? 223 ASN A C   1 
ATOM   1602 O O   . ASN A 1 223 ? 25.660 25.855 28.194 1.00 55.16  ? 223 ASN A O   1 
ATOM   1603 C CB  . ASN A 1 223 ? 25.546 26.226 31.704 1.00 55.80  ? 223 ASN A CB  1 
ATOM   1604 C CG  . ASN A 1 223 ? 25.834 27.685 31.254 1.00 67.22  ? 223 ASN A CG  1 
ATOM   1605 O OD1 . ASN A 1 223 ? 26.860 28.274 31.536 1.00 27.62  ? 223 ASN A OD1 1 
ATOM   1606 N ND2 . ASN A 1 223 ? 24.861 28.280 30.593 1.00 64.48  ? 223 ASN A ND2 1 
ATOM   1607 N N   . GLU A 1 224 ? 23.827 26.458 29.267 1.00 47.55  ? 224 GLU A N   1 
ATOM   1608 C CA  . GLU A 1 224 ? 23.277 27.123 28.095 1.00 46.02  ? 224 GLU A CA  1 
ATOM   1609 C C   . GLU A 1 224 ? 24.124 28.308 27.633 1.00 57.29  ? 224 GLU A C   1 
ATOM   1610 O O   . GLU A 1 224 ? 24.510 28.339 26.458 1.00 66.53  ? 224 GLU A O   1 
ATOM   1611 C CB  . GLU A 1 224 ? 21.788 27.576 28.308 1.00 43.75  ? 224 GLU A CB  1 
ATOM   1612 C CG  . GLU A 1 224 ? 21.189 28.576 27.302 1.00 29.82  ? 224 GLU A CG  1 
ATOM   1613 C CD  . GLU A 1 224 ? 19.573 28.817 27.259 1.00 62.06  ? 224 GLU A CD  1 
ATOM   1614 O OE1 . GLU A 1 224 ? 18.781 28.325 28.112 1.00 55.54  ? 224 GLU A OE1 1 
ATOM   1615 O OE2 . GLU A 1 224 ? 19.094 29.562 26.345 1.00 89.98  ? 224 GLU A OE2 1 
ATOM   1616 N N   . GLU A 1 225 ? 24.374 29.245 28.569 1.00 53.58  ? 225 GLU A N   1 
ATOM   1617 C CA  . GLU A 1 225 ? 25.157 30.477 28.364 1.00 53.17  ? 225 GLU A CA  1 
ATOM   1618 C C   . GLU A 1 225 ? 26.188 30.411 27.255 1.00 54.57  ? 225 GLU A C   1 
ATOM   1619 O O   . GLU A 1 225 ? 26.021 31.069 26.236 1.00 58.32  ? 225 GLU A O   1 
ATOM   1620 C CB  . GLU A 1 225 ? 25.831 31.019 29.659 1.00 54.62  ? 225 GLU A CB  1 
ATOM   1621 C CG  . GLU A 1 225 ? 26.889 32.103 29.439 1.00 56.54  ? 225 GLU A CG  1 
ATOM   1622 C CD  . GLU A 1 225 ? 27.615 32.630 30.723 1.00 90.52  ? 225 GLU A CD  1 
ATOM   1623 O OE1 . GLU A 1 225 ? 27.780 33.866 30.853 1.00 100.00 ? 225 GLU A OE1 1 
ATOM   1624 O OE2 . GLU A 1 225 ? 28.055 31.837 31.594 1.00 64.14  ? 225 GLU A OE2 1 
ATOM   1625 N N   . GLU A 1 226 ? 27.241 29.620 27.471 1.00 48.14  ? 226 GLU A N   1 
ATOM   1626 C CA  . GLU A 1 226 ? 28.332 29.453 26.504 1.00 52.58  ? 226 GLU A CA  1 
ATOM   1627 C C   . GLU A 1 226 ? 28.040 28.476 25.369 1.00 61.09  ? 226 GLU A C   1 
ATOM   1628 O O   . GLU A 1 226 ? 28.596 28.617 24.277 1.00 57.46  ? 226 GLU A O   1 
ATOM   1629 C CB  . GLU A 1 226 ? 29.657 29.015 27.129 1.00 55.17  ? 226 GLU A CB  1 
ATOM   1630 C CG  . GLU A 1 226 ? 29.814 29.230 28.626 1.00 63.04  ? 226 GLU A CG  1 
ATOM   1631 C CD  . GLU A 1 226 ? 29.592 27.943 29.302 1.00 40.31  ? 226 GLU A CD  1 
ATOM   1632 O OE1 . GLU A 1 226 ? 29.226 27.038 28.547 1.00 19.92  ? 226 GLU A OE1 1 
ATOM   1633 O OE2 . GLU A 1 226 ? 29.762 27.838 30.537 1.00 53.05  ? 226 GLU A OE2 1 
ATOM   1634 N N   . PHE A 1 227 ? 27.181 27.480 25.622 1.00 59.18  ? 227 PHE A N   1 
ATOM   1635 C CA  . PHE A 1 227 ? 26.837 26.499 24.592 1.00 54.50  ? 227 PHE A CA  1 
ATOM   1636 C C   . PHE A 1 227 ? 26.276 27.317 23.444 1.00 51.14  ? 227 PHE A C   1 
ATOM   1637 O O   . PHE A 1 227 ? 26.371 26.954 22.281 1.00 52.63  ? 227 PHE A O   1 
ATOM   1638 C CB  . PHE A 1 227 ? 25.734 25.515 25.061 1.00 54.18  ? 227 PHE A CB  1 
ATOM   1639 C CG  . PHE A 1 227 ? 26.226 24.170 25.603 1.00 55.18  ? 227 PHE A CG  1 
ATOM   1640 C CD1 . PHE A 1 227 ? 27.338 23.516 25.058 1.00 61.52  ? 227 PHE A CD1 1 
ATOM   1641 C CD2 . PHE A 1 227 ? 25.548 23.523 26.662 1.00 52.40  ? 227 PHE A CD2 1 
ATOM   1642 C CE1 . PHE A 1 227 ? 27.767 22.268 25.567 1.00 56.28  ? 227 PHE A CE1 1 
ATOM   1643 C CE2 . PHE A 1 227 ? 25.982 22.302 27.184 1.00 48.65  ? 227 PHE A CE2 1 
ATOM   1644 C CZ  . PHE A 1 227 ? 27.081 21.669 26.624 1.00 43.42  ? 227 PHE A CZ  1 
ATOM   1645 N N   . ALA A 1 228 ? 25.698 28.449 23.831 1.00 46.49  ? 228 ALA A N   1 
ATOM   1646 C CA  . ALA A 1 228 ? 25.089 29.424 22.929 1.00 44.23  ? 228 ALA A CA  1 
ATOM   1647 C C   . ALA A 1 228 ? 26.167 30.337 22.338 1.00 46.27  ? 228 ALA A C   1 
ATOM   1648 O O   . ALA A 1 228 ? 26.029 30.820 21.204 1.00 39.19  ? 228 ALA A O   1 
ATOM   1649 C CB  . ALA A 1 228 ? 23.964 30.210 23.649 1.00 41.58  ? 228 ALA A CB  1 
ATOM   1650 N N   . HIS A 1 229 ? 27.243 30.574 23.123 1.00 47.59  ? 229 HIS A N   1 
ATOM   1651 C CA  . HIS A 1 229 ? 28.377 31.419 22.709 1.00 48.85  ? 229 HIS A CA  1 
ATOM   1652 C C   . HIS A 1 229 ? 29.346 30.505 21.997 1.00 52.55  ? 229 HIS A C   1 
ATOM   1653 O O   . HIS A 1 229 ? 30.370 30.927 21.449 1.00 54.72  ? 229 HIS A O   1 
ATOM   1654 C CB  . HIS A 1 229 ? 29.063 32.324 23.744 1.00 49.15  ? 229 HIS A CB  1 
ATOM   1655 C CG  . HIS A 1 229 ? 28.112 33.249 24.405 1.00 51.08  ? 229 HIS A CG  1 
ATOM   1656 N ND1 . HIS A 1 229 ? 27.109 33.893 23.720 1.00 53.96  ? 229 HIS A ND1 1 
ATOM   1657 C CD2 . HIS A 1 229 ? 28.006 33.625 25.696 1.00 52.70  ? 229 HIS A CD2 1 
ATOM   1658 C CE1 . HIS A 1 229 ? 26.429 34.636 24.574 1.00 54.93  ? 229 HIS A CE1 1 
ATOM   1659 N NE2 . HIS A 1 229 ? 26.959 34.494 25.777 1.00 54.59  ? 229 HIS A NE2 1 
ATOM   1660 N N   . LEU A 1 230 ? 28.974 29.227 22.028 1.00 42.55  ? 230 LEU A N   1 
ATOM   1661 C CA  . LEU A 1 230 ? 29.754 28.190 21.385 1.00 39.03  ? 230 LEU A CA  1 
ATOM   1662 C C   . LEU A 1 230 ? 29.040 27.949 20.071 1.00 41.36  ? 230 LEU A C   1 
ATOM   1663 O O   . LEU A 1 230 ? 29.647 27.852 19.004 1.00 42.27  ? 230 LEU A O   1 
ATOM   1664 C CB  . LEU A 1 230 ? 30.010 26.954 22.202 1.00 35.26  ? 230 LEU A CB  1 
ATOM   1665 C CG  . LEU A 1 230 ? 30.394 25.830 21.289 1.00 28.37  ? 230 LEU A CG  1 
ATOM   1666 C CD1 . LEU A 1 230 ? 31.829 25.426 21.499 1.00 28.74  ? 230 LEU A CD1 1 
ATOM   1667 C CD2 . LEU A 1 230 ? 29.402 24.777 21.560 1.00 17.25  ? 230 LEU A CD2 1 
ATOM   1668 N N   . ALA A 1 231 ? 27.735 27.874 20.153 1.00 38.35  ? 231 ALA A N   1 
ATOM   1669 C CA  . ALA A 1 231 ? 26.890 27.662 18.994 1.00 39.57  ? 231 ALA A CA  1 
ATOM   1670 C C   . ALA A 1 231 ? 27.121 28.841 18.048 1.00 62.51  ? 231 ALA A C   1 
ATOM   1671 O O   . ALA A 1 231 ? 27.247 28.681 16.831 1.00 69.99  ? 231 ALA A O   1 
ATOM   1672 C CB  . ALA A 1 231 ? 25.486 27.658 19.482 1.00 38.67  ? 231 ALA A CB  1 
ATOM   1673 N N   . LYS A 1 232 ? 27.193 30.045 18.628 1.00 60.42  ? 232 LYS A N   1 
ATOM   1674 C CA  . LYS A 1 232 ? 27.437 31.255 17.844 1.00 59.50  ? 232 LYS A CA  1 
ATOM   1675 C C   . LYS A 1 232 ? 28.836 31.176 17.199 1.00 60.45  ? 232 LYS A C   1 
ATOM   1676 O O   . LYS A 1 232 ? 29.148 31.917 16.266 1.00 62.15  ? 232 LYS A O   1 
ATOM   1677 C CB  . LYS A 1 232 ? 27.344 32.524 18.697 1.00 62.14  ? 232 LYS A CB  1 
ATOM   1678 C CG  . LYS A 1 232 ? 26.076 33.371 18.492 1.00 74.86  ? 232 LYS A CG  1 
ATOM   1679 C CD  . LYS A 1 232 ? 26.033 34.749 19.215 1.00 96.95  ? 232 LYS A CD  1 
ATOM   1680 C CE  . LYS A 1 232 ? 26.431 34.845 20.719 1.00 100.00 ? 232 LYS A CE  1 
ATOM   1681 N NZ  . LYS A 1 232 ? 26.456 36.221 21.380 1.00 100.00 ? 232 LYS A NZ  1 
ATOM   1682 N N   . VAL A 1 233 ? 29.674 30.272 17.697 1.00 53.44  ? 233 VAL A N   1 
ATOM   1683 C CA  . VAL A 1 233 ? 31.033 30.117 17.156 1.00 52.20  ? 233 VAL A CA  1 
ATOM   1684 C C   . VAL A 1 233 ? 31.089 29.172 15.937 1.00 70.24  ? 233 VAL A C   1 
ATOM   1685 O O   . VAL A 1 233 ? 32.043 29.238 15.145 1.00 67.86  ? 233 VAL A O   1 
ATOM   1686 C CB  . VAL A 1 233 ? 32.076 29.786 18.207 1.00 47.19  ? 233 VAL A CB  1 
ATOM   1687 C CG1 . VAL A 1 233 ? 32.235 28.320 18.059 1.00 47.98  ? 233 VAL A CG1 1 
ATOM   1688 C CG2 . VAL A 1 233 ? 33.393 30.516 18.001 1.00 43.98  ? 233 VAL A CG2 1 
ATOM   1689 N N   . HIS A 1 234 ? 30.074 28.305 15.790 1.00 73.14  ? 234 HIS A N   1 
ATOM   1690 C CA  . HIS A 1 234 ? 29.987 27.350 14.677 1.00 70.77  ? 234 HIS A CA  1 
ATOM   1691 C C   . HIS A 1 234 ? 28.813 27.582 13.718 1.00 50.80  ? 234 HIS A C   1 
ATOM   1692 O O   . HIS A 1 234 ? 27.725 28.014 14.131 1.00 27.40  ? 234 HIS A O   1 
ATOM   1693 C CB  . HIS A 1 234 ? 30.763 26.014 14.734 1.00 75.50  ? 234 HIS A CB  1 
ATOM   1694 C CG  . HIS A 1 234 ? 31.875 25.855 13.688 1.00 80.13  ? 234 HIS A CG  1 
ATOM   1695 N ND1 . HIS A 1 234 ? 31.792 26.396 12.424 1.00 81.66  ? 234 HIS A ND1 1 
ATOM   1696 C CD2 . HIS A 1 234 ? 33.087 25.212 13.727 1.00 83.10  ? 234 HIS A CD2 1 
ATOM   1697 C CE1 . HIS A 1 234 ? 32.887 26.102 11.736 1.00 83.49  ? 234 HIS A CE1 1 
ATOM   1698 N NE2 . HIS A 1 234 ? 33.697 25.388 12.504 1.00 83.83  ? 234 HIS A NE2 1 
ATOM   1699 N N   . ASN A 1 235 ? 29.080 27.287 12.437 1.00 62.35  ? 235 ASN A N   1 
ATOM   1700 C CA  . ASN A 1 235 ? 28.132 27.432 11.317 1.00 64.61  ? 235 ASN A CA  1 
ATOM   1701 C C   . ASN A 1 235 ? 26.743 27.013 11.736 1.00 74.01  ? 235 ASN A C   1 
ATOM   1702 O O   . ASN A 1 235 ? 26.513 25.822 11.847 1.00 80.84  ? 235 ASN A O   1 
ATOM   1703 C CB  . ASN A 1 235 ? 28.525 26.342 10.292 1.00 50.99  ? 235 ASN A CB  1 
ATOM   1704 C CG  . ASN A 1 235 ? 29.773 26.687 9.475  1.00 64.20  ? 235 ASN A CG  1 
ATOM   1705 O OD1 . ASN A 1 235 ? 30.864 26.950 10.017 1.00 46.10  ? 235 ASN A OD1 1 
ATOM   1706 N ND2 . ASN A 1 235 ? 29.615 26.640 8.118  1.00 72.76  ? 235 ASN A ND2 1 
ATOM   1707 N N   . LEU A 1 236 ? 25.849 27.958 11.952 1.00 69.15  ? 236 LEU A N   1 
ATOM   1708 C CA  . LEU A 1 236 ? 24.528 27.518 12.353 1.00 67.90  ? 236 LEU A CA  1 
ATOM   1709 C C   . LEU A 1 236 ? 23.574 28.637 12.765 1.00 70.76  ? 236 LEU A C   1 
ATOM   1710 O O   . LEU A 1 236 ? 23.709 29.817 12.409 1.00 64.55  ? 236 LEU A O   1 
ATOM   1711 C CB  . LEU A 1 236 ? 24.909 27.005 13.783 1.00 68.00  ? 236 LEU A CB  1 
ATOM   1712 C CG  . LEU A 1 236 ? 25.334 25.616 14.326 1.00 73.95  ? 236 LEU A CG  1 
ATOM   1713 C CD1 . LEU A 1 236 ? 24.866 24.346 13.578 1.00 75.36  ? 236 LEU A CD1 1 
ATOM   1714 C CD2 . LEU A 1 236 ? 26.752 25.503 14.841 1.00 75.16  ? 236 LEU A CD2 1 
ATOM   1715 N N   . VAL A 1 237 ? 22.589 28.191 13.559 1.00 76.58  ? 237 VAL A N   1 
ATOM   1716 C CA  . VAL A 1 237 ? 21.516 28.984 14.160 1.00 80.92  ? 237 VAL A CA  1 
ATOM   1717 C C   . VAL A 1 237 ? 20.916 28.215 15.343 1.00 93.94  ? 237 VAL A C   1 
ATOM   1718 O O   . VAL A 1 237 ? 21.402 27.126 15.684 1.00 96.40  ? 237 VAL A O   1 
ATOM   1719 C CB  . VAL A 1 237 ? 20.558 29.936 13.368 1.00 85.49  ? 237 VAL A CB  1 
ATOM   1720 C CG1 . VAL A 1 237 ? 19.076 29.513 13.408 1.00 85.13  ? 237 VAL A CG1 1 
ATOM   1721 C CG2 . VAL A 1 237 ? 20.633 31.299 14.046 1.00 85.14  ? 237 VAL A CG2 1 
ATOM   1722 N N   . ALA A 1 238 ? 19.877 28.792 15.975 1.00 86.68  ? 238 ALA A N   1 
ATOM   1723 C CA  . ALA A 1 238 ? 19.175 28.192 17.130 1.00 81.41  ? 238 ALA A CA  1 
ATOM   1724 C C   . ALA A 1 238 ? 19.897 28.421 18.464 1.00 54.75  ? 238 ALA A C   1 
ATOM   1725 O O   . ALA A 1 238 ? 21.114 28.509 18.521 1.00 36.49  ? 238 ALA A O   1 
ATOM   1726 C CB  . ALA A 1 238 ? 18.883 26.696 16.939 1.00 84.38  ? 238 ALA A CB  1 
ATOM   1727 N N   . ASP A 1 240 ? 17.986 26.982 21.092 1.00 57.62  ? 240 ASP A N   1 
ATOM   1728 C CA  . ASP A 1 240 ? 17.229 25.909 21.711 1.00 54.91  ? 240 ASP A CA  1 
ATOM   1729 C C   . ASP A 1 240 ? 18.083 24.825 22.353 1.00 54.86  ? 240 ASP A C   1 
ATOM   1730 O O   . ASP A 1 240 ? 19.332 24.840 22.302 1.00 57.88  ? 240 ASP A O   1 
ATOM   1731 C CB  . ASP A 1 240 ? 15.774 25.666 21.258 1.00 53.92  ? 240 ASP A CB  1 
ATOM   1732 N N   . LYS A 1 241 ? 17.370 23.898 22.966 1.00 34.97  ? 241 LYS A N   1 
ATOM   1733 C CA  . LYS A 1 241 ? 17.946 22.770 23.653 1.00 34.86  ? 241 LYS A CA  1 
ATOM   1734 C C   . LYS A 1 241 ? 18.446 21.738 22.626 1.00 47.25  ? 241 LYS A C   1 
ATOM   1735 O O   . LYS A 1 241 ? 19.657 21.620 22.396 1.00 43.00  ? 241 LYS A O   1 
ATOM   1736 C CB  . LYS A 1 241 ? 16.723 22.366 24.444 1.00 37.12  ? 241 LYS A CB  1 
ATOM   1737 N N   . THR A 1 242 ? 17.531 20.994 22.017 1.00 47.51  ? 242 THR A N   1 
ATOM   1738 C CA  . THR A 1 242 ? 17.923 20.000 21.029 1.00 49.83  ? 242 THR A CA  1 
ATOM   1739 C C   . THR A 1 242 ? 18.744 20.688 19.936 1.00 56.97  ? 242 THR A C   1 
ATOM   1740 O O   . THR A 1 242 ? 19.644 20.068 19.358 1.00 55.07  ? 242 THR A O   1 
ATOM   1741 C CB  . THR A 1 242 ? 16.706 19.403 20.241 1.00 57.96  ? 242 THR A CB  1 
ATOM   1742 N N   . ALA A 1 243 ? 18.385 21.950 19.684 1.00 53.31  ? 243 ALA A N   1 
ATOM   1743 C CA  . ALA A 1 243 ? 19.051 22.754 18.675 1.00 54.07  ? 243 ALA A CA  1 
ATOM   1744 C C   . ALA A 1 243 ? 20.521 22.660 18.889 1.00 53.25  ? 243 ALA A C   1 
ATOM   1745 O O   . ALA A 1 243 ? 21.184 21.876 18.226 1.00 55.90  ? 243 ALA A O   1 
ATOM   1746 C CB  . ALA A 1 243 ? 18.637 24.189 18.736 1.00 56.00  ? 243 ALA A CB  1 
ATOM   1747 N N   . LEU A 1 244 ? 21.017 23.439 19.816 1.00 49.29  ? 244 LEU A N   1 
ATOM   1748 C CA  . LEU A 1 244 ? 22.442 23.479 20.155 1.00 51.33  ? 244 LEU A CA  1 
ATOM   1749 C C   . LEU A 1 244 ? 23.018 22.183 20.701 1.00 61.52  ? 244 LEU A C   1 
ATOM   1750 O O   . LEU A 1 244 ? 24.129 21.797 20.320 1.00 71.03  ? 244 LEU A O   1 
ATOM   1751 C CB  . LEU A 1 244 ? 22.589 24.445 21.289 1.00 52.68  ? 244 LEU A CB  1 
ATOM   1752 N N   . SER A 1 245 ? 22.285 21.519 21.597 1.00 50.91  ? 245 SER A N   1 
ATOM   1753 C CA  . SER A 1 245 ? 22.761 20.257 22.180 1.00 45.81  ? 245 SER A CA  1 
ATOM   1754 C C   . SER A 1 245 ? 23.167 19.282 21.045 1.00 35.24  ? 245 SER A C   1 
ATOM   1755 O O   . SER A 1 245 ? 24.337 18.902 20.897 1.00 24.87  ? 245 SER A O   1 
ATOM   1756 C CB  . SER A 1 245 ? 21.723 19.795 23.285 1.00 44.28  ? 245 SER A CB  1 
ATOM   1757 N N   . THR A 1 246 ? 22.205 18.890 20.223 1.00 37.20  ? 246 THR A N   1 
ATOM   1758 C CA  . THR A 1 246 ? 22.522 17.983 19.129 1.00 40.79  ? 246 THR A CA  1 
ATOM   1759 C C   . THR A 1 246 ? 23.319 18.693 18.031 1.00 46.04  ? 246 THR A C   1 
ATOM   1760 O O   . THR A 1 246 ? 24.020 18.042 17.275 1.00 47.10  ? 246 THR A O   1 
ATOM   1761 C CB  . THR A 1 246 ? 21.281 17.553 18.353 1.00 59.99  ? 246 THR A CB  1 
ATOM   1762 N N   . ALA A 1 247 ? 23.215 20.039 17.932 1.00 47.31  ? 247 ALA A N   1 
ATOM   1763 C CA  . ALA A 1 247 ? 23.937 20.776 16.911 1.00 38.70  ? 247 ALA A CA  1 
ATOM   1764 C C   . ALA A 1 247 ? 25.351 20.877 17.358 1.00 33.67  ? 247 ALA A C   1 
ATOM   1765 O O   . ALA A 1 247 ? 26.240 20.757 16.536 1.00 40.81  ? 247 ALA A O   1 
ATOM   1766 C CB  . ALA A 1 247 ? 23.395 22.099 16.544 1.00 38.68  ? 247 ALA A CB  1 
ATOM   1767 N N   . ASN A 1 248 ? 25.580 21.088 18.635 1.00 29.73  ? 248 ASN A N   1 
ATOM   1768 C CA  . ASN A 1 248 ? 26.959 21.163 19.085 1.00 32.63  ? 248 ASN A CA  1 
ATOM   1769 C C   . ASN A 1 248 ? 27.533 19.758 19.058 1.00 39.81  ? 248 ASN A C   1 
ATOM   1770 O O   . ASN A 1 248 ? 28.675 19.543 18.640 1.00 31.53  ? 248 ASN A O   1 
ATOM   1771 C CB  . ASN A 1 248 ? 27.322 22.000 20.238 1.00 33.87  ? 248 ASN A CB  1 
ATOM   1772 N N   . LYS A 1 249 ? 26.747 18.761 19.488 1.00 47.82  ? 249 LYS A N   1 
ATOM   1773 C CA  . LYS A 1 249 ? 27.284 17.398 19.447 1.00 48.03  ? 249 LYS A CA  1 
ATOM   1774 C C   . LYS A 1 249 ? 27.496 17.028 17.963 1.00 54.75  ? 249 LYS A C   1 
ATOM   1775 O O   . LYS A 1 249 ? 28.492 16.399 17.582 1.00 43.27  ? 249 LYS A O   1 
ATOM   1776 C CB  . LYS A 1 249 ? 26.387 16.395 20.230 1.00 47.36  ? 249 LYS A CB  1 
ATOM   1777 N N   . GLU A 1 250 ? 26.557 17.443 17.112 1.00 64.32  ? 250 GLU A N   1 
ATOM   1778 C CA  . GLU A 1 250 ? 26.584 17.199 15.661 1.00 66.22  ? 250 GLU A CA  1 
ATOM   1779 C C   . GLU A 1 250 ? 27.971 17.282 14.999 1.00 72.52  ? 250 GLU A C   1 
ATOM   1780 O O   . GLU A 1 250 ? 28.139 17.017 13.798 1.00 78.09  ? 250 GLU A O   1 
ATOM   1781 C CB  . GLU A 1 250 ? 25.618 18.177 14.989 1.00 68.80  ? 250 GLU A CB  1 
ATOM   1782 N N   . HIS A 1 251 ? 29.001 17.652 15.750 1.00 65.95  ? 251 HIS A N   1 
ATOM   1783 C CA  . HIS A 1 251 ? 30.298 17.718 15.119 1.00 66.64  ? 251 HIS A CA  1 
ATOM   1784 C C   . HIS A 1 251 ? 30.907 16.327 14.973 1.00 83.65  ? 251 HIS A C   1 
ATOM   1785 O O   . HIS A 1 251 ? 30.780 15.530 15.915 1.00 89.90  ? 251 HIS A O   1 
ATOM   1786 C CB  . HIS A 1 251 ? 30.990 19.057 15.148 1.00 64.19  ? 251 HIS A CB  1 
ATOM   1787 N N   . ALA A 1 252 ? 31.523 16.086 13.801 1.00 71.52  ? 252 ALA A N   1 
ATOM   1788 C CA  . ALA A 1 252 ? 32.191 14.847 13.380 1.00 66.77  ? 252 ALA A CA  1 
ATOM   1789 C C   . ALA A 1 252 ? 31.987 13.673 14.307 1.00 69.70  ? 252 ALA A C   1 
ATOM   1790 O O   . ALA A 1 252 ? 30.850 13.370 14.681 1.00 69.96  ? 252 ALA A O   1 
ATOM   1791 C CB  . ALA A 1 252 ? 33.636 15.036 13.059 1.00 66.23  ? 252 ALA A CB  1 
ATOM   1792 N N   . VAL A 1 253 ? 33.083 13.014 14.685 1.00 68.61  ? 253 VAL A N   1 
ATOM   1793 C CA  . VAL A 1 253 ? 32.961 11.862 15.578 1.00 71.31  ? 253 VAL A CA  1 
ATOM   1794 C C   . VAL A 1 253 ? 34.269 11.467 16.293 1.00 69.91  ? 253 VAL A C   1 
ATOM   1795 O O   . VAL A 1 253 ? 35.045 12.315 16.734 1.00 61.15  ? 253 VAL A O   1 
ATOM   1796 C CB  . VAL A 1 253 ? 32.730 10.657 14.645 1.00 79.43  ? 253 VAL A CB  1 
ATOM   1797 N N   . GLU A 1 254 ? 34.473 10.149 16.419 1.00 72.08  ? 254 GLU A N   1 
ATOM   1798 C CA  . GLU A 1 254 ? 35.618 9.478  17.059 1.00 73.52  ? 254 GLU A CA  1 
ATOM   1799 C C   . GLU A 1 254 ? 35.199 8.038  17.370 1.00 87.59  ? 254 GLU A C   1 
ATOM   1800 O O   . GLU A 1 254 ? 35.440 7.543  18.469 1.00 94.84  ? 254 GLU A O   1 
ATOM   1801 C CB  . GLU A 1 254 ? 36.190 10.140 18.338 1.00 71.98  ? 254 GLU A CB  1 
ATOM   1802 N N   . GLY A 1 270 ? 29.344 2.800  28.246 1.00 92.47  ? 270 GLY A N   1 
ATOM   1803 C CA  . GLY A 1 270 ? 28.618 3.758  27.425 1.00 92.45  ? 270 GLY A CA  1 
ATOM   1804 C C   . GLY A 1 270 ? 29.305 5.135  27.337 1.00 93.16  ? 270 GLY A C   1 
ATOM   1805 O O   . GLY A 1 270 ? 28.613 6.143  27.189 1.00 92.95  ? 270 GLY A O   1 
ATOM   1806 N N   . ALA A 1 271 ? 30.623 5.158  27.421 1.00 84.19  ? 271 ALA A N   1 
ATOM   1807 C CA  . ALA A 1 271 ? 31.380 6.401  27.350 1.00 80.09  ? 271 ALA A CA  1 
ATOM   1808 C C   . ALA A 1 271 ? 31.701 6.717  25.916 1.00 69.93  ? 271 ALA A C   1 
ATOM   1809 O O   . ALA A 1 271 ? 32.747 6.276  25.426 1.00 70.29  ? 271 ALA A O   1 
ATOM   1810 C CB  . ALA A 1 271 ? 32.703 6.114  28.009 1.00 82.26  ? 271 ALA A CB  1 
ATOM   1811 N N   . THR A 1 272 ? 30.836 7.477  25.270 1.00 56.83  ? 272 THR A N   1 
ATOM   1812 C CA  . THR A 1 272 ? 31.036 7.837  23.866 1.00 50.10  ? 272 THR A CA  1 
ATOM   1813 C C   . THR A 1 272 ? 31.218 9.339  23.657 1.00 52.85  ? 272 THR A C   1 
ATOM   1814 O O   . THR A 1 272 ? 32.302 9.890  23.916 1.00 49.88  ? 272 THR A O   1 
ATOM   1815 C CB  . THR A 1 272 ? 29.873 7.317  22.937 1.00 37.10  ? 272 THR A CB  1 
ATOM   1816 O OG1 . THR A 1 272 ? 30.283 7.356  21.578 1.00 74.14  ? 272 THR A OG1 1 
ATOM   1817 C CG2 . THR A 1 272 ? 28.596 8.152  23.054 1.00 10.06  ? 272 THR A CG2 1 
ATOM   1818 N N   . LYS A 1 273 ? 30.184 9.975  23.184 1.00 45.68  ? 273 LYS A N   1 
ATOM   1819 C CA  . LYS A 1 273 ? 30.219 11.417 22.917 1.00 50.00  ? 273 LYS A CA  1 
ATOM   1820 C C   . LYS A 1 273 ? 28.980 12.092 23.481 1.00 53.67  ? 273 LYS A C   1 
ATOM   1821 O O   . LYS A 1 273 ? 27.920 12.108 22.844 1.00 44.85  ? 273 LYS A O   1 
ATOM   1822 C CB  . LYS A 1 273 ? 30.269 11.665 21.411 1.00 56.95  ? 273 LYS A CB  1 
ATOM   1823 C CG  . LYS A 1 273 ? 30.853 10.489 20.628 1.00 44.04  ? 273 LYS A CG  1 
ATOM   1824 C CD  . LYS A 1 273 ? 32.156 10.846 19.915 1.00 54.24  ? 273 LYS A CD  1 
ATOM   1825 C CE  . LYS A 1 273 ? 32.839 12.079 20.509 1.00 38.13  ? 273 LYS A CE  1 
ATOM   1826 N NZ  . LYS A 1 273 ? 34.058 11.751 21.262 1.00 64.45  ? 273 LYS A NZ  1 
ATOM   1827 N N   . LEU A 1 274 ? 29.158 12.631 24.664 1.00 54.60  ? 274 LEU A N   1 
ATOM   1828 C CA  . LEU A 1 274 ? 28.094 13.334 25.390 1.00 52.72  ? 274 LEU A CA  1 
ATOM   1829 C C   . LEU A 1 274 ? 28.266 14.852 25.246 1.00 58.90  ? 274 LEU A C   1 
ATOM   1830 O O   . LEU A 1 274 ? 29.278 15.332 24.714 1.00 51.15  ? 274 LEU A O   1 
ATOM   1831 C CB  . LEU A 1 274 ? 28.170 12.992 26.891 1.00 54.05  ? 274 LEU A CB  1 
ATOM   1832 C CG  . LEU A 1 274 ? 27.093 12.015 27.385 1.00 60.25  ? 274 LEU A CG  1 
ATOM   1833 C CD1 . LEU A 1 274 ? 25.812 12.052 26.557 1.00 64.18  ? 274 LEU A CD1 1 
ATOM   1834 C CD2 . LEU A 1 274 ? 27.559 10.555 27.368 1.00 54.90  ? 274 LEU A CD2 1 
ATOM   1835 N N   . VAL A 1 275 ? 27.257 15.527 25.737 1.00 63.39  ? 275 VAL A N   1 
ATOM   1836 C CA  . VAL A 1 275 ? 27.171 16.997 25.786 1.00 58.42  ? 275 VAL A CA  1 
ATOM   1837 C C   . VAL A 1 275 ? 25.992 17.337 26.700 1.00 49.11  ? 275 VAL A C   1 
ATOM   1838 O O   . VAL A 1 275 ? 24.832 17.343 26.271 1.00 44.06  ? 275 VAL A O   1 
ATOM   1839 C CB  . VAL A 1 275 ? 26.975 17.599 24.383 1.00 60.58  ? 275 VAL A CB  1 
ATOM   1840 C CG1 . VAL A 1 275 ? 25.529 17.557 23.900 1.00 62.61  ? 275 VAL A CG1 1 
ATOM   1841 C CG2 . VAL A 1 275 ? 27.392 19.078 24.305 1.00 55.56  ? 275 VAL A CG2 1 
ATOM   1842 N N   . VAL A 1 276 ? 26.348 17.595 27.952 1.00 46.40  ? 276 VAL A N   1 
ATOM   1843 C CA  . VAL A 1 276 ? 25.383 17.920 29.024 1.00 49.21  ? 276 VAL A CA  1 
ATOM   1844 C C   . VAL A 1 276 ? 25.036 19.418 28.999 1.00 39.60  ? 276 VAL A C   1 
ATOM   1845 O O   . VAL A 1 276 ? 25.853 20.274 29.358 1.00 40.22  ? 276 VAL A O   1 
ATOM   1846 C CB  . VAL A 1 276 ? 26.000 17.556 30.380 1.00 54.77  ? 276 VAL A CB  1 
ATOM   1847 C CG1 . VAL A 1 276 ? 27.374 16.884 30.253 1.00 52.83  ? 276 VAL A CG1 1 
ATOM   1848 C CG2 . VAL A 1 276 ? 26.218 18.766 31.288 1.00 54.71  ? 276 VAL A CG2 1 
ATOM   1849 N N   . MET A 1 277 ? 23.806 19.695 28.576 1.00 34.75  ? 277 MET A N   1 
ATOM   1850 C CA  . MET A 1 277 ? 23.296 21.079 28.453 1.00 38.41  ? 277 MET A CA  1 
ATOM   1851 C C   . MET A 1 277 ? 22.527 21.542 29.704 1.00 36.40  ? 277 MET A C   1 
ATOM   1852 O O   . MET A 1 277 ? 21.303 21.727 29.676 1.00 30.67  ? 277 MET A O   1 
ATOM   1853 C CB  . MET A 1 277 ? 22.332 21.188 27.260 1.00 39.88  ? 277 MET A CB  1 
ATOM   1854 C CG  . MET A 1 277 ? 21.649 22.560 27.160 1.00 42.48  ? 277 MET A CG  1 
ATOM   1855 S SD  . MET A 1 277 ? 22.458 23.660 26.014 1.00 52.08  ? 277 MET A SD  1 
ATOM   1856 C CE  . MET A 1 277 ? 21.701 23.537 24.406 1.00 45.03  ? 277 MET A CE  1 
ATOM   1857 N N   . THR A 1 278 ? 23.247 21.738 30.810 1.00 33.37  ? 278 THR A N   1 
ATOM   1858 C CA  . THR A 1 278 ? 22.599 22.216 32.051 1.00 37.20  ? 278 THR A CA  1 
ATOM   1859 C C   . THR A 1 278 ? 21.960 23.578 31.769 1.00 52.63  ? 278 THR A C   1 
ATOM   1860 O O   . THR A 1 278 ? 22.661 24.551 31.447 1.00 49.86  ? 278 THR A O   1 
ATOM   1861 C CB  . THR A 1 278 ? 23.595 22.379 33.207 1.00 44.27  ? 278 THR A CB  1 
ATOM   1862 O OG1 . THR A 1 278 ? 23.841 23.762 33.443 1.00 29.61  ? 278 THR A OG1 1 
ATOM   1863 C CG2 . THR A 1 278 ? 24.939 21.711 32.953 1.00 61.17  ? 278 THR A CG2 1 
ATOM   1864 N N   . ARG A 1 279 ? 20.649 23.574 31.899 1.00 60.11  ? 279 ARG A N   1 
ATOM   1865 C CA  . ARG A 1 279 ? 19.790 24.753 31.673 1.00 63.27  ? 279 ARG A CA  1 
ATOM   1866 C C   . ARG A 1 279 ? 19.451 25.442 33.011 1.00 76.21  ? 279 ARG A C   1 
ATOM   1867 O O   . ARG A 1 279 ? 18.280 25.698 33.316 1.00 81.63  ? 279 ARG A O   1 
ATOM   1868 C CB  . ARG A 1 279 ? 18.457 24.302 31.027 1.00 54.56  ? 279 ARG A CB  1 
ATOM   1869 C CG  . ARG A 1 279 ? 18.338 24.579 29.520 1.00 51.12  ? 279 ARG A CG  1 
ATOM   1870 C CD  . ARG A 1 279 ? 17.880 23.344 28.712 1.00 57.30  ? 279 ARG A CD  1 
ATOM   1871 N NE  . ARG A 1 279 ? 16.405 23.228 28.547 1.00 18.30  ? 279 ARG A NE  1 
ATOM   1872 C CZ  . ARG A 1 279 ? 15.581 22.685 29.466 1.00 38.60  ? 279 ARG A CZ  1 
ATOM   1873 N NH1 . ARG A 1 279 ? 16.058 22.208 30.625 1.00 15.51  ? 279 ARG A NH1 1 
ATOM   1874 N NH2 . ARG A 1 279 ? 14.251 22.573 29.318 1.00 31.53  ? 279 ARG A NH2 1 
ATOM   1875 N N   . GLY A 1 280 ? 20.474 25.735 33.800 1.00 77.25  ? 280 GLY A N   1 
ATOM   1876 C CA  . GLY A 1 280 ? 20.283 26.384 35.124 1.00 81.11  ? 280 GLY A CA  1 
ATOM   1877 C C   . GLY A 1 280 ? 19.447 25.457 36.029 1.00 85.64  ? 280 GLY A C   1 
ATOM   1878 O O   . GLY A 1 280 ? 19.978 24.526 36.653 1.00 85.93  ? 280 GLY A O   1 
ATOM   1879 N N   . HIS A 1 281 ? 18.153 25.749 36.070 1.00 78.44  ? 281 HIS A N   1 
ATOM   1880 C CA  . HIS A 1 281 ? 17.170 24.966 36.850 1.00 77.26  ? 281 HIS A CA  1 
ATOM   1881 C C   . HIS A 1 281 ? 16.406 24.085 35.894 1.00 66.38  ? 281 HIS A C   1 
ATOM   1882 O O   . HIS A 1 281 ? 16.145 22.903 36.177 1.00 69.67  ? 281 HIS A O   1 
ATOM   1883 C CB  . HIS A 1 281 ? 16.196 25.894 37.569 1.00 80.99  ? 281 HIS A CB  1 
ATOM   1884 C CG  . HIS A 1 281 ? 16.764 27.287 37.766 1.00 86.69  ? 281 HIS A CG  1 
ATOM   1885 N ND1 . HIS A 1 281 ? 17.557 27.604 38.861 1.00 88.91  ? 281 HIS A ND1 1 
ATOM   1886 C CD2 . HIS A 1 281 ? 16.659 28.418 37.026 1.00 88.23  ? 281 HIS A CD2 1 
ATOM   1887 C CE1 . HIS A 1 281 ? 17.902 28.872 38.761 1.00 87.32  ? 281 HIS A CE1 1 
ATOM   1888 N NE2 . HIS A 1 281 ? 17.375 29.372 37.671 1.00 87.59  ? 281 HIS A NE2 1 
ATOM   1889 N N   . ASN A 1 282 ? 16.074 24.705 34.781 1.00 42.27  ? 282 ASN A N   1 
ATOM   1890 C CA  . ASN A 1 282 ? 15.370 24.035 33.722 1.00 36.59  ? 282 ASN A CA  1 
ATOM   1891 C C   . ASN A 1 282 ? 16.051 22.682 33.592 1.00 44.89  ? 282 ASN A C   1 
ATOM   1892 O O   . ASN A 1 282 ? 17.211 22.513 34.008 1.00 51.21  ? 282 ASN A O   1 
ATOM   1893 C CB  . ASN A 1 282 ? 15.422 24.908 32.484 1.00 31.09  ? 282 ASN A CB  1 
ATOM   1894 C CG  . ASN A 1 282 ? 14.721 26.257 32.749 1.00 60.85  ? 282 ASN A CG  1 
ATOM   1895 O OD1 . ASN A 1 282 ? 13.492 26.314 32.836 1.00 39.01  ? 282 ASN A OD1 1 
ATOM   1896 N ND2 . ASN A 1 282 ? 15.438 27.356 32.894 1.00 42.89  ? 282 ASN A ND2 1 
ATOM   1897 N N   . PRO A 1 283 ? 15.409 21.699 33.015 1.00 35.63  ? 283 PRO A N   1 
ATOM   1898 C CA  . PRO A 1 283 ? 15.941 20.349 33.003 1.00 25.19  ? 283 PRO A CA  1 
ATOM   1899 C C   . PRO A 1 283 ? 17.248 20.256 32.336 1.00 26.47  ? 283 PRO A C   1 
ATOM   1900 O O   . PRO A 1 283 ? 17.478 20.972 31.326 1.00 26.68  ? 283 PRO A O   1 
ATOM   1901 C CB  . PRO A 1 283 ? 14.906 19.565 32.233 1.00 25.48  ? 283 PRO A CB  1 
ATOM   1902 C CG  . PRO A 1 283 ? 13.805 20.537 31.818 1.00 36.84  ? 283 PRO A CG  1 
ATOM   1903 C CD  . PRO A 1 283 ? 14.131 21.893 32.339 1.00 34.47  ? 283 PRO A CD  1 
ATOM   1904 N N   . VAL A 1 284 ? 18.120 19.407 32.856 1.00 27.21  ? 284 VAL A N   1 
ATOM   1905 C CA  . VAL A 1 284 ? 19.384 19.224 32.171 1.00 30.58  ? 284 VAL A CA  1 
ATOM   1906 C C   . VAL A 1 284 ? 18.972 18.614 30.827 1.00 30.73  ? 284 VAL A C   1 
ATOM   1907 O O   . VAL A 1 284 ? 17.913 17.972 30.717 1.00 28.94  ? 284 VAL A O   1 
ATOM   1908 C CB  . VAL A 1 284 ? 20.337 18.339 32.974 1.00 42.25  ? 284 VAL A CB  1 
ATOM   1909 C CG1 . VAL A 1 284 ? 21.118 17.356 32.105 1.00 43.30  ? 284 VAL A CG1 1 
ATOM   1910 C CG2 . VAL A 1 284 ? 21.403 19.156 33.727 1.00 46.61  ? 284 VAL A CG2 1 
ATOM   1911 N N   . ILE A 1 285 ? 19.785 18.821 29.833 1.00 28.39  ? 285 ILE A N   1 
ATOM   1912 C CA  . ILE A 1 285 ? 19.477 18.362 28.470 1.00 22.40  ? 285 ILE A CA  1 
ATOM   1913 C C   . ILE A 1 285 ? 20.729 17.813 27.776 1.00 34.90  ? 285 ILE A C   1 
ATOM   1914 O O   . ILE A 1 285 ? 21.695 18.542 27.538 1.00 31.01  ? 285 ILE A O   1 
ATOM   1915 C CB  . ILE A 1 285 ? 18.974 19.586 27.688 1.00 26.89  ? 285 ILE A CB  1 
ATOM   1916 C CG1 . ILE A 1 285 ? 17.615 20.122 28.167 1.00 27.77  ? 285 ILE A CG1 1 
ATOM   1917 C CG2 . ILE A 1 285 ? 18.807 19.327 26.200 1.00 41.15  ? 285 ILE A CG2 1 
ATOM   1918 C CD1 . ILE A 1 285 ? 16.812 19.107 28.976 1.00 33.20  ? 285 ILE A CD1 1 
ATOM   1919 N N   . ALA A 1 286 ? 20.706 16.527 27.438 1.00 41.83  ? 286 ALA A N   1 
ATOM   1920 C CA  . ALA A 1 286 ? 21.870 15.886 26.768 1.00 40.96  ? 286 ALA A CA  1 
ATOM   1921 C C   . ALA A 1 286 ? 21.431 14.994 25.595 1.00 48.13  ? 286 ALA A C   1 
ATOM   1922 O O   . ALA A 1 286 ? 20.451 15.292 24.897 1.00 44.26  ? 286 ALA A O   1 
ATOM   1923 C CB  . ALA A 1 286 ? 22.639 15.020 27.765 1.00 42.91  ? 286 ALA A CB  1 
ATOM   1924 N N   . ALA A 1 287 ? 22.194 13.910 25.418 1.00 57.78  ? 287 ALA A N   1 
ATOM   1925 C CA  . ALA A 1 287 ? 21.949 12.918 24.345 1.00 64.62  ? 287 ALA A CA  1 
ATOM   1926 C C   . ALA A 1 287 ? 23.091 11.878 24.280 1.00 76.22  ? 287 ALA A C   1 
ATOM   1927 O O   . ALA A 1 287 ? 24.275 12.221 24.245 1.00 80.92  ? 287 ALA A O   1 
ATOM   1928 C CB  . ALA A 1 287 ? 21.867 13.631 22.988 1.00 66.19  ? 287 ALA A CB  1 
ATOM   1929 N N   . GLU A 1 288 ? 22.699 10.607 24.269 1.00 60.49  ? 288 GLU A N   1 
ATOM   1930 C CA  . GLU A 1 288 ? 23.657 9.469  24.187 1.00 56.13  ? 288 GLU A CA  1 
ATOM   1931 C C   . GLU A 1 288 ? 23.952 9.183  22.706 1.00 57.23  ? 288 GLU A C   1 
ATOM   1932 O O   . GLU A 1 288 ? 23.118 9.422  21.830 1.00 55.29  ? 288 GLU A O   1 
ATOM   1933 C CB  . GLU A 1 288 ? 23.029 8.215  24.826 1.00 58.93  ? 288 GLU A CB  1 
ATOM   1934 C CG  . GLU A 1 288 ? 23.930 6.979  24.739 1.00 92.28  ? 288 GLU A CG  1 
ATOM   1935 C CD  . GLU A 1 288 ? 25.117 7.061  25.692 1.00 100.00 ? 288 GLU A CD  1 
ATOM   1936 O OE1 . GLU A 1 288 ? 25.890 6.044  25.852 1.00 36.98  ? 288 GLU A OE1 1 
ATOM   1937 O OE2 . GLU A 1 288 ? 25.344 8.155  26.337 1.00 100.00 ? 288 GLU A OE2 1 
ATOM   1938 N N   . GLN A 1 289 ? 25.153 8.677  22.373 1.00 55.16  ? 289 GLN A N   1 
ATOM   1939 C CA  . GLN A 1 289 ? 25.402 8.356  20.944 1.00 53.64  ? 289 GLN A CA  1 
ATOM   1940 C C   . GLN A 1 289 ? 25.880 6.946  20.743 1.00 66.06  ? 289 GLN A C   1 
ATOM   1941 O O   . GLN A 1 289 ? 27.103 6.666  20.816 1.00 61.25  ? 289 GLN A O   1 
ATOM   1942 C CB  . GLN A 1 289 ? 26.357 9.213  20.233 1.00 53.54  ? 289 GLN A CB  1 
ATOM   1943 C CG  . GLN A 1 289 ? 26.009 9.166  18.742 1.00 31.56  ? 289 GLN A CG  1 
ATOM   1944 C CD  . GLN A 1 289 ? 27.085 9.714  17.865 1.00 74.82  ? 289 GLN A CD  1 
ATOM   1945 O OE1 . GLN A 1 289 ? 27.438 10.873 18.021 1.00 84.34  ? 289 GLN A OE1 1 
ATOM   1946 N NE2 . GLN A 1 289 ? 27.630 8.953  16.945 1.00 48.88  ? 289 GLN A NE2 1 
ATOM   1947 N N   . THR A 1 290 ? 24.833 6.339  20.511 1.00 69.37  ? 290 THR A N   1 
ATOM   1948 C CA  . THR A 1 290 ? 24.549 5.012  20.274 1.00 69.52  ? 290 THR A CA  1 
ATOM   1949 C C   . THR A 1 290 ? 25.249 4.525  18.998 1.00 83.83  ? 290 THR A C   1 
ATOM   1950 O O   . THR A 1 290 ? 25.199 5.172  17.944 1.00 93.27  ? 290 THR A O   1 
ATOM   1951 C CB  . THR A 1 290 ? 23.036 5.113  20.262 1.00 62.18  ? 290 THR A CB  1 
ATOM   1952 O OG1 . THR A 1 290 ? 22.657 6.404  19.750 1.00 51.02  ? 290 THR A OG1 1 
ATOM   1953 C CG2 . THR A 1 290 ? 22.447 5.037  21.685 1.00 39.76  ? 290 THR A CG2 1 
ATOM   1954 N N   . ALA A 1 291 ? 25.873 3.379  19.214 1.00 72.61  ? 291 ALA A N   1 
ATOM   1955 C CA  . ALA A 1 291 ? 26.698 2.654  18.244 1.00 64.45  ? 291 ALA A CA  1 
ATOM   1956 C C   . ALA A 1 291 ? 26.229 2.759  16.800 1.00 66.19  ? 291 ALA A C   1 
ATOM   1957 O O   . ALA A 1 291 ? 27.004 3.086  15.892 1.00 58.12  ? 291 ALA A O   1 
ATOM   1958 C CB  . ALA A 1 291 ? 26.758 1.171  18.571 1.00 61.74  ? 291 ALA A CB  1 
ATOM   1959 N N   . ASP A 1 292 ? 24.946 2.489  16.472 1.00 71.47  ? 292 ASP A N   1 
ATOM   1960 C CA  . ASP A 1 292 ? 24.688 2.579  15.043 1.00 75.60  ? 292 ASP A CA  1 
ATOM   1961 C C   . ASP A 1 292 ? 24.780 4.013  14.579 1.00 88.64  ? 292 ASP A C   1 
ATOM   1962 O O   . ASP A 1 292 ? 24.519 4.299  13.411 1.00 91.99  ? 292 ASP A O   1 
ATOM   1963 C CB  . ASP A 1 292 ? 23.353 1.987  14.406 1.00 78.76  ? 292 ASP A CB  1 
ATOM   1964 C CG  . ASP A 1 292 ? 21.994 1.880  15.137 1.00 89.09  ? 292 ASP A CG  1 
ATOM   1965 O OD1 . ASP A 1 292 ? 21.357 2.923  15.523 1.00 77.40  ? 292 ASP A OD1 1 
ATOM   1966 O OD2 . ASP A 1 292 ? 21.456 0.701  15.314 1.00 100.00 ? 292 ASP A OD2 1 
ATOM   1967 N N   . GLY A 1 293 ? 25.169 4.884  15.486 1.00 87.12  ? 293 GLY A N   1 
ATOM   1968 C CA  . GLY A 1 293 ? 25.363 6.316  15.160 1.00 87.33  ? 293 GLY A CA  1 
ATOM   1969 C C   . GLY A 1 293 ? 24.107 7.106  15.391 1.00 89.54  ? 293 GLY A C   1 
ATOM   1970 O O   . GLY A 1 293 ? 23.985 8.265  14.974 1.00 95.51  ? 293 GLY A O   1 
ATOM   1971 N N   . THR A 1 294 ? 23.228 6.484  16.073 1.00 72.92  ? 294 THR A N   1 
ATOM   1972 C CA  . THR A 1 294 ? 21.964 7.062  16.345 1.00 70.22  ? 294 THR A CA  1 
ATOM   1973 C C   . THR A 1 294 ? 21.960 7.940  17.543 1.00 56.90  ? 294 THR A C   1 
ATOM   1974 O O   . THR A 1 294 ? 22.266 7.499  18.653 1.00 55.11  ? 294 THR A O   1 
ATOM   1975 C CB  . THR A 1 294 ? 20.972 5.976  16.548 1.00 100.00 ? 294 THR A CB  1 
ATOM   1976 O OG1 . THR A 1 294 ? 20.782 5.304  15.317 1.00 100.00 ? 294 THR A OG1 1 
ATOM   1977 C CG2 . THR A 1 294 ? 19.634 6.515  17.013 1.00 100.00 ? 294 THR A CG2 1 
ATOM   1978 N N   . VAL A 1 295 ? 21.572 9.161  17.243 1.00 36.54  ? 295 VAL A N   1 
ATOM   1979 C CA  . VAL A 1 295 ? 21.487 10.204 18.234 1.00 30.62  ? 295 VAL A CA  1 
ATOM   1980 C C   . VAL A 1 295 ? 20.152 10.207 18.969 1.00 42.61  ? 295 VAL A C   1 
ATOM   1981 O O   . VAL A 1 295 ? 19.076 10.326 18.346 1.00 36.35  ? 295 VAL A O   1 
ATOM   1982 C CB  . VAL A 1 295 ? 21.667 11.580 17.612 1.00 27.02  ? 295 VAL A CB  1 
ATOM   1983 C CG1 . VAL A 1 295 ? 20.531 12.542 17.947 1.00 26.50  ? 295 VAL A CG1 1 
ATOM   1984 C CG2 . VAL A 1 295 ? 22.951 12.267 18.093 1.00 26.87  ? 295 VAL A CG2 1 
ATOM   1985 N N   . VAL A 1 296 ? 20.375 10.074 20.254 1.00 47.82  ? 296 VAL A N   1 
ATOM   1986 C CA  . VAL A 1 296 ? 19.390 10.079 21.317 1.00 52.16  ? 296 VAL A CA  1 
ATOM   1987 C C   . VAL A 1 296 ? 19.621 11.356 22.102 1.00 60.42  ? 296 VAL A C   1 
ATOM   1988 O O   . VAL A 1 296 ? 20.737 11.890 22.133 1.00 61.99  ? 296 VAL A O   1 
ATOM   1989 C CB  . VAL A 1 296 ? 19.619 8.875  22.230 1.00 58.42  ? 296 VAL A CB  1 
ATOM   1990 C CG1 . VAL A 1 296 ? 20.793 8.002  21.782 1.00 60.90  ? 296 VAL A CG1 1 
ATOM   1991 C CG2 . VAL A 1 296 ? 19.939 9.283  23.675 1.00 59.05  ? 296 VAL A CG2 1 
ATOM   1992 N N   . VAL A 1 297 ? 18.599 11.849 22.730 1.00 57.91  ? 297 VAL A N   1 
ATOM   1993 C CA  . VAL A 1 297 ? 18.735 13.078 23.512 1.00 56.69  ? 297 VAL A CA  1 
ATOM   1994 C C   . VAL A 1 297 ? 18.237 12.834 24.938 1.00 59.40  ? 297 VAL A C   1 
ATOM   1995 O O   . VAL A 1 297 ? 17.075 12.464 25.154 1.00 58.30  ? 297 VAL A O   1 
ATOM   1996 C CB  . VAL A 1 297 ? 17.939 14.197 22.845 1.00 60.30  ? 297 VAL A CB  1 
ATOM   1997 C CG1 . VAL A 1 297 ? 16.914 14.839 23.771 1.00 59.60  ? 297 VAL A CG1 1 
ATOM   1998 C CG2 . VAL A 1 297 ? 18.831 15.343 22.349 1.00 59.55  ? 297 VAL A CG2 1 
ATOM   1999 N N   . HIS A 1 298 ? 19.160 13.055 25.865 1.00 59.35  ? 298 HIS A N   1 
ATOM   2000 C CA  . HIS A 1 298 ? 18.925 12.874 27.309 1.00 57.37  ? 298 HIS A CA  1 
ATOM   2001 C C   . HIS A 1 298 ? 18.391 14.168 27.929 1.00 55.93  ? 298 HIS A C   1 
ATOM   2002 O O   . HIS A 1 298 ? 19.021 15.228 27.842 1.00 52.79  ? 298 HIS A O   1 
ATOM   2003 C CB  . HIS A 1 298 ? 20.233 12.481 27.987 1.00 58.35  ? 298 HIS A CB  1 
ATOM   2004 C CG  . HIS A 1 298 ? 20.310 10.983 28.237 1.00 63.56  ? 298 HIS A CG  1 
ATOM   2005 N ND1 . HIS A 1 298 ? 19.177 10.182 28.176 1.00 64.37  ? 298 HIS A ND1 1 
ATOM   2006 C CD2 . HIS A 1 298 ? 21.345 10.160 28.542 1.00 67.32  ? 298 HIS A CD2 1 
ATOM   2007 C CE1 . HIS A 1 298 ? 19.537 8.943  28.437 1.00 62.52  ? 298 HIS A CE1 1 
ATOM   2008 N NE2 . HIS A 1 298 ? 20.826 8.912  28.659 1.00 64.46  ? 298 HIS A NE2 1 
ATOM   2009 N N   . GLU A 1 299 ? 17.226 14.039 28.552 1.00 49.21  ? 299 GLU A N   1 
ATOM   2010 C CA  . GLU A 1 299 ? 16.539 15.181 29.181 1.00 48.45  ? 299 GLU A CA  1 
ATOM   2011 C C   . GLU A 1 299 ? 16.033 14.821 30.598 1.00 41.07  ? 299 GLU A C   1 
ATOM   2012 O O   . GLU A 1 299 ? 15.136 13.979 30.762 1.00 32.62  ? 299 GLU A O   1 
ATOM   2013 C CB  . GLU A 1 299 ? 15.360 15.578 28.303 1.00 48.71  ? 299 GLU A CB  1 
ATOM   2014 C CG  . GLU A 1 299 ? 14.883 16.993 28.560 1.00 58.00  ? 299 GLU A CG  1 
ATOM   2015 C CD  . GLU A 1 299 ? 13.698 17.027 29.505 1.00 63.60  ? 299 GLU A CD  1 
ATOM   2016 O OE1 . GLU A 1 299 ? 13.893 16.962 30.776 1.00 46.71  ? 299 GLU A OE1 1 
ATOM   2017 O OE2 . GLU A 1 299 ? 12.505 17.114 29.031 1.00 22.70  ? 299 GLU A OE2 1 
ATOM   2018 N N   . VAL A 1 300 ? 16.645 15.505 31.571 1.00 32.74  ? 300 VAL A N   1 
ATOM   2019 C CA  . VAL A 1 300 ? 16.365 15.331 33.021 1.00 36.08  ? 300 VAL A CA  1 
ATOM   2020 C C   . VAL A 1 300 ? 16.202 16.725 33.728 1.00 52.93  ? 300 VAL A C   1 
ATOM   2021 O O   . VAL A 1 300 ? 17.179 17.445 33.956 1.00 51.49  ? 300 VAL A O   1 
ATOM   2022 C CB  . VAL A 1 300 ? 17.556 14.580 33.646 1.00 34.43  ? 300 VAL A CB  1 
ATOM   2023 C CG1 . VAL A 1 300 ? 17.790 13.197 33.028 1.00 32.03  ? 300 VAL A CG1 1 
ATOM   2024 C CG2 . VAL A 1 300 ? 18.888 15.328 33.476 1.00 34.80  ? 300 VAL A CG2 1 
ATOM   2025 N N   . GLY A 1 301 ? 14.938 17.087 34.070 1.00 54.90  ? 301 GLY A N   1 
ATOM   2026 C CA  . GLY A 1 301 ? 14.609 18.406 34.757 1.00 54.44  ? 301 GLY A CA  1 
ATOM   2027 C C   . GLY A 1 301 ? 15.543 18.596 35.963 1.00 52.34  ? 301 GLY A C   1 
ATOM   2028 O O   . GLY A 1 301 ? 16.766 18.438 35.847 1.00 60.87  ? 301 GLY A O   1 
ATOM   2029 N N   . VAL A 1 302 ? 14.979 18.968 37.134 1.00 35.13  ? 302 VAL A N   1 
ATOM   2030 C CA  . VAL A 1 302 ? 15.821 19.043 38.358 1.00 37.37  ? 302 VAL A CA  1 
ATOM   2031 C C   . VAL A 1 302 ? 15.032 19.346 39.627 1.00 64.22  ? 302 VAL A C   1 
ATOM   2032 O O   . VAL A 1 302 ? 14.902 20.501 40.026 1.00 65.14  ? 302 VAL A O   1 
ATOM   2033 C CB  . VAL A 1 302 ? 17.025 19.974 38.177 1.00 35.70  ? 302 VAL A CB  1 
ATOM   2034 C CG1 . VAL A 1 302 ? 16.689 21.423 38.014 1.00 38.27  ? 302 VAL A CG1 1 
ATOM   2035 C CG2 . VAL A 1 302 ? 18.012 19.883 39.366 1.00 29.60  ? 302 VAL A CG2 1 
ATOM   2036 N N   . PRO A 1 303 ? 14.501 18.302 40.247 1.00 75.52  ? 303 PRO A N   1 
ATOM   2037 C CA  . PRO A 1 303 ? 13.734 18.473 41.467 1.00 78.55  ? 303 PRO A CA  1 
ATOM   2038 C C   . PRO A 1 303 ? 14.604 19.066 42.578 1.00 87.17  ? 303 PRO A C   1 
ATOM   2039 O O   . PRO A 1 303 ? 15.199 18.357 43.388 1.00 81.17  ? 303 PRO A O   1 
ATOM   2040 C CB  . PRO A 1 303 ? 13.230 17.051 41.730 1.00 80.11  ? 303 PRO A CB  1 
ATOM   2041 C CG  . PRO A 1 303 ? 12.842 16.637 40.331 1.00 84.39  ? 303 PRO A CG  1 
ATOM   2042 C CD  . PRO A 1 303 ? 13.837 17.310 39.373 1.00 79.07  ? 303 PRO A CD  1 
ATOM   2043 N N   . VAL A 1 304 ? 14.663 20.393 42.611 1.00 93.72  ? 304 VAL A N   1 
ATOM   2044 C CA  . VAL A 1 304 ? 15.445 21.121 43.599 1.00 95.14  ? 304 VAL A CA  1 
ATOM   2045 C C   . VAL A 1 304 ? 14.546 21.954 44.504 1.00 97.96  ? 304 VAL A C   1 
ATOM   2046 O O   . VAL A 1 304 ? 14.201 23.096 44.185 1.00 100.00 ? 304 VAL A O   1 
ATOM   2047 C CB  . VAL A 1 304 ? 16.651 21.966 43.032 1.00 100.00 ? 304 VAL A CB  1 
ATOM   2048 C CG1 . VAL A 1 304 ? 17.520 22.570 44.117 1.00 100.00 ? 304 VAL A CG1 1 
ATOM   2049 C CG2 . VAL A 1 304 ? 17.589 21.157 42.127 1.00 100.00 ? 304 VAL A CG2 1 
ATOM   2050 N N   . VAL A 1 305 ? 14.168 21.367 45.636 1.00 95.95  ? 305 VAL A N   1 
ATOM   2051 C CA  . VAL A 1 305 ? 13.313 22.022 46.611 1.00 96.16  ? 305 VAL A CA  1 
ATOM   2052 C C   . VAL A 1 305 ? 14.164 22.791 47.622 1.00 96.63  ? 305 VAL A C   1 
ATOM   2053 O O   . VAL A 1 305 ? 14.720 22.203 48.566 1.00 93.46  ? 305 VAL A O   1 
ATOM   2054 C CB  . VAL A 1 305 ? 12.424 20.921 47.248 1.00 100.00 ? 305 VAL A CB  1 
ATOM   2055 C CG1 . VAL A 1 305 ? 11.478 20.386 46.180 1.00 99.45  ? 305 VAL A CG1 1 
ATOM   2056 C CG2 . VAL A 1 305 ? 13.325 19.781 47.684 1.00 100.00 ? 305 VAL A CG2 1 
ATOM   2057 N N   . ALA A 1 306 ? 14.264 24.109 47.426 1.00 91.22  ? 306 ALA A N   1 
ATOM   2058 C CA  . ALA A 1 306 ? 15.058 24.938 48.329 1.00 90.43  ? 306 ALA A CA  1 
ATOM   2059 C C   . ALA A 1 306 ? 14.772 26.431 48.205 1.00 88.59  ? 306 ALA A C   1 
ATOM   2060 O O   . ALA A 1 306 ? 14.161 26.886 47.249 1.00 88.08  ? 306 ALA A O   1 
ATOM   2061 C CB  . ALA A 1 306 ? 16.548 24.673 48.117 1.00 91.78  ? 306 ALA A CB  1 
ATOM   2062 N N   . ALA A 1 307 ? 15.254 27.176 49.198 1.00 83.07  ? 307 ALA A N   1 
ATOM   2063 C CA  . ALA A 1 307 ? 15.053 28.619 49.208 1.00 84.43  ? 307 ALA A CA  1 
ATOM   2064 C C   . ALA A 1 307 ? 16.367 29.353 48.958 1.00 91.16  ? 307 ALA A C   1 
ATOM   2065 O O   . ALA A 1 307 ? 17.211 28.853 48.195 1.00 91.95  ? 307 ALA A O   1 
ATOM   2066 C CB  . ALA A 1 307 ? 14.484 29.044 50.539 1.00 85.00  ? 307 ALA A CB  1 
ATOM   2067 N N   . GLU A 1 308 ? 16.572 30.528 49.597 1.00 88.51  ? 308 GLU A N   1 
ATOM   2068 C CA  . GLU A 1 308 ? 17.788 31.367 49.461 1.00 87.24  ? 308 GLU A CA  1 
ATOM   2069 C C   . GLU A 1 308 ? 19.081 30.582 49.473 1.00 95.87  ? 308 GLU A C   1 
ATOM   2070 O O   . GLU A 1 308 ? 20.138 31.103 49.104 1.00 94.29  ? 308 GLU A O   1 
ATOM   2071 C CB  . GLU A 1 308 ? 17.757 32.306 48.252 1.00 88.78  ? 308 GLU A CB  1 
ATOM   2072 C CG  . GLU A 1 308 ? 16.908 31.933 47.035 1.00 100.00 ? 308 GLU A CG  1 
ATOM   2073 C CD  . GLU A 1 308 ? 17.444 32.597 45.728 1.00 100.00 ? 308 GLU A CD  1 
ATOM   2074 O OE1 . GLU A 1 308 ? 16.573 32.848 44.858 1.00 100.00 ? 308 GLU A OE1 1 
ATOM   2075 O OE2 . GLU A 1 308 ? 18.701 32.892 45.572 1.00 35.84  ? 308 GLU A OE2 1 
ATOM   2076 N N   . LYS A 1 309 ? 18.939 29.324 49.917 1.00 95.39  ? 309 LYS A N   1 
ATOM   2077 C CA  . LYS A 1 309 ? 19.983 28.317 50.043 1.00 93.99  ? 309 LYS A CA  1 
ATOM   2078 C C   . LYS A 1 309 ? 20.380 27.844 48.660 1.00 100.00 ? 309 LYS A C   1 
ATOM   2079 O O   . LYS A 1 309 ? 20.641 26.652 48.436 1.00 100.00 ? 309 LYS A O   1 
ATOM   2080 C CB  . LYS A 1 309 ? 19.403 27.139 50.861 1.00 97.36  ? 309 LYS A CB  1 
ATOM   2081 C CG  . LYS A 1 309 ? 20.289 26.371 51.827 1.00 97.25  ? 309 LYS A CG  1 
ATOM   2082 C CD  . LYS A 1 309 ? 19.679 25.024 52.124 1.00 84.36  ? 309 LYS A CD  1 
ATOM   2083 C CE  . LYS A 1 309 ? 18.493 25.220 53.025 1.00 84.18  ? 309 LYS A CE  1 
ATOM   2084 N NZ  . LYS A 1 309 ? 17.364 25.820 52.246 1.00 76.29  ? 309 LYS A NZ  1 
ATOM   2085 N N   . ILE A 1 310 ? 20.409 28.812 47.744 1.00 93.50  ? 310 ILE A N   1 
ATOM   2086 C CA  . ILE A 1 310 ? 20.787 28.596 46.350 1.00 90.95  ? 310 ILE A CA  1 
ATOM   2087 C C   . ILE A 1 310 ? 21.971 29.521 46.181 1.00 88.11  ? 310 ILE A C   1 
ATOM   2088 O O   . ILE A 1 310 ? 22.737 29.689 47.122 1.00 89.88  ? 310 ILE A O   1 
ATOM   2089 C CB  . ILE A 1 310 ? 19.803 28.771 45.147 1.00 94.17  ? 310 ILE A CB  1 
ATOM   2090 C CG1 . ILE A 1 310 ? 18.329 28.944 45.654 1.00 94.86  ? 310 ILE A CG1 1 
ATOM   2091 C CG2 . ILE A 1 310 ? 19.955 27.523 44.240 1.00 95.69  ? 310 ILE A CG2 1 
ATOM   2092 C CD1 . ILE A 1 310 ? 17.538 27.638 45.703 1.00 100.00 ? 310 ILE A CD1 1 
ATOM   2093 N N   . VAL A 1 311 ? 22.165 30.150 45.029 1.00 75.90  ? 311 VAL A N   1 
ATOM   2094 C CA  . VAL A 1 311 ? 23.314 31.039 44.915 1.00 71.49  ? 311 VAL A CA  1 
ATOM   2095 C C   . VAL A 1 311 ? 24.600 30.233 45.108 1.00 76.29  ? 311 VAL A C   1 
ATOM   2096 O O   . VAL A 1 311 ? 25.021 29.951 46.244 1.00 76.10  ? 311 VAL A O   1 
ATOM   2097 C CB  . VAL A 1 311 ? 23.080 32.207 45.974 1.00 68.56  ? 311 VAL A CB  1 
ATOM   2098 C CG1 . VAL A 1 311 ? 24.250 33.192 46.240 1.00 67.46  ? 311 VAL A CG1 1 
ATOM   2099 C CG2 . VAL A 1 311 ? 21.671 32.797 45.883 1.00 65.68  ? 311 VAL A CG2 1 
ATOM   2100 N N   . ASP A 1 312 ? 25.198 29.868 43.982 1.00 67.35  ? 312 ASP A N   1 
ATOM   2101 C CA  . ASP A 1 312 ? 26.448 29.102 43.895 1.00 60.57  ? 312 ASP A CA  1 
ATOM   2102 C C   . ASP A 1 312 ? 26.524 28.520 42.484 1.00 64.84  ? 312 ASP A C   1 
ATOM   2103 O O   . ASP A 1 312 ? 26.819 27.328 42.300 1.00 76.47  ? 312 ASP A O   1 
ATOM   2104 C CB  . ASP A 1 312 ? 26.467 27.981 44.917 1.00 58.96  ? 312 ASP A CB  1 
ATOM   2105 C CG  . ASP A 1 312 ? 27.828 27.324 45.027 1.00 72.31  ? 312 ASP A CG  1 
ATOM   2106 O OD1 . ASP A 1 312 ? 28.125 26.779 46.115 1.00 80.04  ? 312 ASP A OD1 1 
ATOM   2107 O OD2 . ASP A 1 312 ? 28.631 27.375 44.028 1.00 50.45  ? 312 ASP A OD2 1 
ATOM   2108 N N   . THR A 1 313 ? 26.235 29.390 41.508 1.00 50.12  ? 313 THR A N   1 
ATOM   2109 C CA  . THR A 1 313 ? 26.228 29.093 40.066 1.00 49.22  ? 313 THR A CA  1 
ATOM   2110 C C   . THR A 1 313 ? 27.428 28.242 39.634 1.00 50.50  ? 313 THR A C   1 
ATOM   2111 O O   . THR A 1 313 ? 27.346 27.400 38.730 1.00 51.96  ? 313 THR A O   1 
ATOM   2112 C CB  . THR A 1 313 ? 26.205 30.477 39.359 1.00 73.13  ? 313 THR A CB  1 
ATOM   2113 O OG1 . THR A 1 313 ? 27.006 31.449 40.081 1.00 71.81  ? 313 THR A OG1 1 
ATOM   2114 C CG2 . THR A 1 313 ? 24.803 30.989 39.493 1.00 66.20  ? 313 THR A CG2 1 
ATOM   2115 N N   . ASN A 1 314 ? 28.568 28.455 40.269 1.00 38.82  ? 314 ASN A N   1 
ATOM   2116 C CA  . ASN A 1 314 ? 29.727 27.683 39.912 1.00 37.59  ? 314 ASN A CA  1 
ATOM   2117 C C   . ASN A 1 314 ? 29.661 26.380 40.691 1.00 43.79  ? 314 ASN A C   1 
ATOM   2118 O O   . ASN A 1 314 ? 29.193 25.371 40.174 1.00 42.37  ? 314 ASN A O   1 
ATOM   2119 C CB  . ASN A 1 314 ? 30.922 28.438 40.406 1.00 37.72  ? 314 ASN A CB  1 
ATOM   2120 C CG  . ASN A 1 314 ? 30.529 29.729 41.033 1.00 70.64  ? 314 ASN A CG  1 
ATOM   2121 O OD1 . ASN A 1 314 ? 30.102 30.663 40.308 1.00 62.81  ? 314 ASN A OD1 1 
ATOM   2122 N ND2 . ASN A 1 314 ? 30.642 29.803 42.393 1.00 48.04  ? 314 ASN A ND2 1 
ATOM   2123 N N   . GLY A 1 315 ? 30.138 26.454 41.934 1.00 37.23  ? 315 GLY A N   1 
ATOM   2124 C CA  . GLY A 1 315 ? 30.213 25.374 42.916 1.00 34.49  ? 315 GLY A CA  1 
ATOM   2125 C C   . GLY A 1 315 ? 29.177 24.270 42.753 1.00 38.50  ? 315 GLY A C   1 
ATOM   2126 O O   . GLY A 1 315 ? 29.385 23.177 43.281 1.00 41.09  ? 315 GLY A O   1 
ATOM   2127 N N   . ALA A 1 316 ? 28.077 24.537 42.055 1.00 28.30  ? 316 ALA A N   1 
ATOM   2128 C CA  . ALA A 1 316 ? 27.036 23.538 41.855 1.00 24.41  ? 316 ALA A CA  1 
ATOM   2129 C C   . ALA A 1 316 ? 27.106 22.923 40.455 1.00 43.10  ? 316 ALA A C   1 
ATOM   2130 O O   . ALA A 1 316 ? 26.616 21.823 40.209 1.00 41.43  ? 316 ALA A O   1 
ATOM   2131 C CB  . ALA A 1 316 ? 25.721 24.186 42.176 1.00 22.46  ? 316 ALA A CB  1 
ATOM   2132 N N   . GLY A 1 317 ? 27.726 23.651 39.527 1.00 48.67  ? 317 GLY A N   1 
ATOM   2133 C CA  . GLY A 1 317 ? 27.871 23.158 38.165 1.00 44.29  ? 317 GLY A CA  1 
ATOM   2134 C C   . GLY A 1 317 ? 29.132 22.297 38.220 1.00 37.65  ? 317 GLY A C   1 
ATOM   2135 O O   . GLY A 1 317 ? 29.338 21.420 37.381 1.00 47.03  ? 317 GLY A O   1 
ATOM   2136 N N   . ASP A 1 318 ? 29.947 22.600 39.258 1.00 16.37  ? 318 ASP A N   1 
ATOM   2137 C CA  . ASP A 1 318 ? 31.213 21.943 39.571 1.00 16.57  ? 318 ASP A CA  1 
ATOM   2138 C C   . ASP A 1 318 ? 30.856 20.658 40.307 1.00 25.87  ? 318 ASP A C   1 
ATOM   2139 O O   . ASP A 1 318 ? 31.608 19.711 40.355 1.00 26.66  ? 318 ASP A O   1 
ATOM   2140 C CB  . ASP A 1 318 ? 32.109 22.714 40.578 1.00 22.84  ? 318 ASP A CB  1 
ATOM   2141 C CG  . ASP A 1 318 ? 33.023 23.807 39.987 1.00 49.52  ? 318 ASP A CG  1 
ATOM   2142 O OD1 . ASP A 1 318 ? 32.777 24.373 38.872 1.00 61.36  ? 318 ASP A OD1 1 
ATOM   2143 O OD2 . ASP A 1 318 ? 34.057 24.076 40.684 1.00 35.25  ? 318 ASP A OD2 1 
ATOM   2144 N N   . ALA A 1 319 ? 29.669 20.668 40.879 1.00 34.39  ? 319 ALA A N   1 
ATOM   2145 C CA  . ALA A 1 319 ? 29.123 19.541 41.615 1.00 37.06  ? 319 ALA A CA  1 
ATOM   2146 C C   . ALA A 1 319 ? 28.598 18.560 40.577 1.00 46.11  ? 319 ALA A C   1 
ATOM   2147 O O   . ALA A 1 319 ? 28.934 17.387 40.633 1.00 51.29  ? 319 ALA A O   1 
ATOM   2148 C CB  . ALA A 1 319 ? 27.850 20.038 42.403 1.00 33.43  ? 319 ALA A CB  1 
ATOM   2149 N N   . PHE A 1 320 ? 27.775 19.068 39.636 1.00 37.07  ? 320 PHE A N   1 
ATOM   2150 C CA  . PHE A 1 320 ? 27.203 18.243 38.577 1.00 36.54  ? 320 PHE A CA  1 
ATOM   2151 C C   . PHE A 1 320 ? 28.307 17.434 37.926 1.00 43.54  ? 320 PHE A C   1 
ATOM   2152 O O   . PHE A 1 320 ? 28.184 16.215 37.764 1.00 47.81  ? 320 PHE A O   1 
ATOM   2153 C CB  . PHE A 1 320 ? 26.384 19.013 37.533 1.00 38.39  ? 320 PHE A CB  1 
ATOM   2154 C CG  . PHE A 1 320 ? 25.846 18.156 36.324 1.00 39.83  ? 320 PHE A CG  1 
ATOM   2155 C CD1 . PHE A 1 320 ? 24.624 17.510 36.332 1.00 45.76  ? 320 PHE A CD1 1 
ATOM   2156 C CD2 . PHE A 1 320 ? 26.566 18.038 35.162 1.00 35.20  ? 320 PHE A CD2 1 
ATOM   2157 C CE1 . PHE A 1 320 ? 24.179 16.763 35.227 1.00 43.76  ? 320 PHE A CE1 1 
ATOM   2158 C CE2 . PHE A 1 320 ? 26.121 17.300 34.092 1.00 36.51  ? 320 PHE A CE2 1 
ATOM   2159 C CZ  . PHE A 1 320 ? 24.940 16.674 34.116 1.00 38.46  ? 320 PHE A CZ  1 
ATOM   2160 N N   . VAL A 1 321 ? 29.389 18.124 37.559 1.00 32.43  ? 321 VAL A N   1 
ATOM   2161 C CA  . VAL A 1 321 ? 30.507 17.441 36.932 1.00 27.83  ? 321 VAL A CA  1 
ATOM   2162 C C   . VAL A 1 321 ? 31.050 16.373 37.865 1.00 52.92  ? 321 VAL A C   1 
ATOM   2163 O O   . VAL A 1 321 ? 31.555 15.355 37.387 1.00 62.06  ? 321 VAL A O   1 
ATOM   2164 C CB  . VAL A 1 321 ? 31.594 18.410 36.373 1.00 22.47  ? 321 VAL A CB  1 
ATOM   2165 C CG1 . VAL A 1 321 ? 33.023 17.943 36.444 1.00 18.76  ? 321 VAL A CG1 1 
ATOM   2166 C CG2 . VAL A 1 321 ? 31.197 19.059 35.044 1.00 18.43  ? 321 VAL A CG2 1 
ATOM   2167 N N   . GLY A 1 322 ? 30.942 16.621 39.179 1.00 50.98  ? 322 GLY A N   1 
ATOM   2168 C CA  . GLY A 1 322 ? 31.419 15.710 40.227 1.00 47.59  ? 322 GLY A CA  1 
ATOM   2169 C C   . GLY A 1 322 ? 30.700 14.358 40.269 1.00 56.74  ? 322 GLY A C   1 
ATOM   2170 O O   . GLY A 1 322 ? 31.334 13.304 40.204 1.00 58.69  ? 322 GLY A O   1 
ATOM   2171 N N   . GLY A 1 323 ? 29.378 14.370 40.382 1.00 51.31  ? 323 GLY A N   1 
ATOM   2172 C CA  . GLY A 1 323 ? 28.607 13.122 40.429 1.00 49.15  ? 323 GLY A CA  1 
ATOM   2173 C C   . GLY A 1 323 ? 28.688 12.477 39.052 1.00 47.09  ? 323 GLY A C   1 
ATOM   2174 O O   . GLY A 1 323 ? 28.793 11.247 38.914 1.00 37.80  ? 323 GLY A O   1 
ATOM   2175 N N   . PHE A 1 324 ? 28.657 13.338 38.040 1.00 46.18  ? 324 PHE A N   1 
ATOM   2176 C CA  . PHE A 1 324 ? 28.734 12.870 36.662 1.00 43.78  ? 324 PHE A CA  1 
ATOM   2177 C C   . PHE A 1 324 ? 29.992 12.031 36.431 1.00 39.77  ? 324 PHE A C   1 
ATOM   2178 O O   . PHE A 1 324 ? 29.921 11.029 35.718 1.00 35.55  ? 324 PHE A O   1 
ATOM   2179 C CB  . PHE A 1 324 ? 28.522 13.987 35.661 1.00 43.49  ? 324 PHE A CB  1 
ATOM   2180 C CG  . PHE A 1 324 ? 27.874 13.572 34.350 1.00 41.27  ? 324 PHE A CG  1 
ATOM   2181 C CD1 . PHE A 1 324 ? 26.630 14.008 34.028 1.00 40.57  ? 324 PHE A CD1 1 
ATOM   2182 C CD2 . PHE A 1 324 ? 28.561 12.773 33.423 1.00 49.14  ? 324 PHE A CD2 1 
ATOM   2183 C CE1 . PHE A 1 324 ? 26.048 13.650 32.816 1.00 46.78  ? 324 PHE A CE1 1 
ATOM   2184 C CE2 . PHE A 1 324 ? 27.992 12.406 32.206 1.00 53.37  ? 324 PHE A CE2 1 
ATOM   2185 C CZ  . PHE A 1 324 ? 26.717 12.840 31.891 1.00 50.47  ? 324 PHE A CZ  1 
ATOM   2186 N N   . LEU A 1 325 ? 31.130 12.425 37.026 1.00 35.58  ? 325 LEU A N   1 
ATOM   2187 C CA  . LEU A 1 325 ? 32.396 11.675 36.872 1.00 37.82  ? 325 LEU A CA  1 
ATOM   2188 C C   . LEU A 1 325 ? 32.577 10.635 37.981 1.00 39.63  ? 325 LEU A C   1 
ATOM   2189 O O   . LEU A 1 325 ? 33.529 9.861  37.960 1.00 33.86  ? 325 LEU A O   1 
ATOM   2190 C CB  . LEU A 1 325 ? 33.701 12.480 36.932 1.00 35.34  ? 325 LEU A CB  1 
ATOM   2191 C CG  . LEU A 1 325 ? 33.842 13.911 36.532 1.00 31.13  ? 325 LEU A CG  1 
ATOM   2192 C CD1 . LEU A 1 325 ? 35.354 14.238 36.670 1.00 22.67  ? 325 LEU A CD1 1 
ATOM   2193 C CD2 . LEU A 1 325 ? 33.084 14.207 35.246 1.00 32.06  ? 325 LEU A CD2 1 
ATOM   2194 N N   . TYR A 1 326 ? 31.661 10.637 38.941 1.00 39.28  ? 326 TYR A N   1 
ATOM   2195 C CA  . TYR A 1 326 ? 31.706 9.697  40.054 1.00 39.37  ? 326 TYR A CA  1 
ATOM   2196 C C   . TYR A 1 326 ? 30.881 8.495  39.682 1.00 36.73  ? 326 TYR A C   1 
ATOM   2197 O O   . TYR A 1 326 ? 31.383 7.382  39.621 1.00 43.67  ? 326 TYR A O   1 
ATOM   2198 C CB  . TYR A 1 326 ? 30.722 10.046 41.138 1.00 45.25  ? 326 TYR A CB  1 
ATOM   2199 C CG  . TYR A 1 326 ? 30.521 8.856  42.111 1.00 45.94  ? 326 TYR A CG  1 
ATOM   2200 C CD1 . TYR A 1 326 ? 31.596 8.322  42.876 1.00 47.47  ? 326 TYR A CD1 1 
ATOM   2201 C CD2 . TYR A 1 326 ? 29.262 8.283  42.279 1.00 45.33  ? 326 TYR A CD2 1 
ATOM   2202 C CE1 . TYR A 1 326 ? 31.388 7.258  43.764 1.00 43.04  ? 326 TYR A CE1 1 
ATOM   2203 C CE2 . TYR A 1 326 ? 29.037 7.207  43.151 1.00 43.98  ? 326 TYR A CE2 1 
ATOM   2204 C CZ  . TYR A 1 326 ? 30.090 6.707  43.887 1.00 50.05  ? 326 TYR A CZ  1 
ATOM   2205 O OH  . TYR A 1 326 ? 29.788 5.661  44.727 1.00 67.49  ? 326 TYR A OH  1 
ATOM   2206 N N   . GLY A 1 327 ? 29.608 8.755  39.438 1.00 29.79  ? 327 GLY A N   1 
ATOM   2207 C CA  . GLY A 1 327 ? 28.668 7.711  39.050 1.00 34.95  ? 327 GLY A CA  1 
ATOM   2208 C C   . GLY A 1 327 ? 29.017 7.226  37.662 1.00 44.48  ? 327 GLY A C   1 
ATOM   2209 O O   . GLY A 1 327 ? 28.362 6.330  37.146 1.00 45.36  ? 327 GLY A O   1 
ATOM   2210 N N   . LEU A 1 328 ? 30.064 7.848  37.090 1.00 48.56  ? 328 LEU A N   1 
ATOM   2211 C CA  . LEU A 1 328 ? 30.628 7.576  35.760 1.00 46.89  ? 328 LEU A CA  1 
ATOM   2212 C C   . LEU A 1 328 ? 31.675 6.464  35.902 1.00 68.88  ? 328 LEU A C   1 
ATOM   2213 O O   . LEU A 1 328 ? 31.864 5.621  35.018 1.00 79.53  ? 328 LEU A O   1 
ATOM   2214 C CB  . LEU A 1 328 ? 31.479 8.752  35.194 1.00 41.15  ? 328 LEU A CB  1 
ATOM   2215 C CG  . LEU A 1 328 ? 31.650 8.258  33.769 1.00 40.90  ? 328 LEU A CG  1 
ATOM   2216 C CD1 . LEU A 1 328 ? 30.359 8.481  33.065 1.00 46.25  ? 328 LEU A CD1 1 
ATOM   2217 C CD2 . LEU A 1 328 ? 32.891 8.598  32.958 1.00 19.47  ? 328 LEU A CD2 1 
ATOM   2218 N N   . SER A 1 329 ? 32.349 6.494  37.047 1.00 59.24  ? 329 SER A N   1 
ATOM   2219 C CA  . SER A 1 329 ? 33.371 5.529  37.378 1.00 51.39  ? 329 SER A CA  1 
ATOM   2220 C C   . SER A 1 329 ? 32.648 4.402  38.090 1.00 50.38  ? 329 SER A C   1 
ATOM   2221 O O   . SER A 1 329 ? 33.257 3.401  38.469 1.00 59.03  ? 329 SER A O   1 
ATOM   2222 C CB  . SER A 1 329 ? 34.322 6.090  38.413 1.00 48.19  ? 329 SER A CB  1 
ATOM   2223 O OG  . SER A 1 329 ? 33.570 6.298  39.582 1.00 54.54  ? 329 SER A OG  1 
ATOM   2224 N N   . GLN A 1 330 ? 31.338 4.555  38.291 1.00 31.39  ? 330 GLN A N   1 
ATOM   2225 C CA  . GLN A 1 330 ? 30.613 3.491  38.969 1.00 29.57  ? 330 GLN A CA  1 
ATOM   2226 C C   . GLN A 1 330 ? 29.362 3.005  38.260 1.00 37.47  ? 330 GLN A C   1 
ATOM   2227 O O   . GLN A 1 330 ? 28.261 3.254  38.716 1.00 42.96  ? 330 GLN A O   1 
ATOM   2228 C CB  . GLN A 1 330 ? 30.676 3.474  40.509 1.00 27.72  ? 330 GLN A CB  1 
ATOM   2229 C CG  . GLN A 1 330 ? 32.103 3.331  41.032 1.00 16.52  ? 330 GLN A CG  1 
ATOM   2230 C CD  . GLN A 1 330 ? 32.196 2.712  42.440 1.00 60.17  ? 330 GLN A CD  1 
ATOM   2231 O OE1 . GLN A 1 330 ? 31.231 2.139  42.896 1.00 57.98  ? 330 GLN A OE1 1 
ATOM   2232 N NE2 . GLN A 1 330 ? 33.359 2.893  43.159 1.00 46.39  ? 330 GLN A NE2 1 
ATOM   2233 N N   . GLY A 1 331 ? 29.520 2.319  37.154 1.00 32.36  ? 331 GLY A N   1 
ATOM   2234 C CA  . GLY A 1 331 ? 28.342 1.824  36.446 1.00 33.50  ? 331 GLY A CA  1 
ATOM   2235 C C   . GLY A 1 331 ? 27.885 2.683  35.274 1.00 38.55  ? 331 GLY A C   1 
ATOM   2236 O O   . GLY A 1 331 ? 27.423 2.160  34.252 1.00 53.05  ? 331 GLY A O   1 
ATOM   2237 N N   . LYS A 1 332 ? 27.963 3.980  35.381 1.00 30.07  ? 332 LYS A N   1 
ATOM   2238 C CA  . LYS A 1 332 ? 27.514 4.793  34.254 1.00 33.18  ? 332 LYS A CA  1 
ATOM   2239 C C   . LYS A 1 332 ? 26.006 4.637  34.021 1.00 45.01  ? 332 LYS A C   1 
ATOM   2240 O O   . LYS A 1 332 ? 25.400 3.703  34.541 1.00 53.27  ? 332 LYS A O   1 
ATOM   2241 C CB  . LYS A 1 332 ? 28.531 4.602  33.026 1.00 39.99  ? 332 LYS A CB  1 
ATOM   2242 C CG  . LYS A 1 332 ? 28.197 3.739  31.746 1.00 50.16  ? 332 LYS A CG  1 
ATOM   2243 C CD  . LYS A 1 332 ? 28.474 4.416  30.354 1.00 45.29  ? 332 LYS A CD  1 
ATOM   2244 C CE  . LYS A 1 332 ? 27.976 5.929  30.114 1.00 33.07  ? 332 LYS A CE  1 
ATOM   2245 N NZ  . LYS A 1 332 ? 29.069 6.853  29.504 1.00 15.96  ? 332 LYS A NZ  1 
ATOM   2246 N N   . THR A 1 333 ? 25.420 5.552  33.252 1.00 44.17  ? 333 THR A N   1 
ATOM   2247 C CA  . THR A 1 333 ? 23.992 5.592  32.893 1.00 45.04  ? 333 THR A CA  1 
ATOM   2248 C C   . THR A 1 333 ? 23.526 7.006  32.590 1.00 51.66  ? 333 THR A C   1 
ATOM   2249 O O   . THR A 1 333 ? 23.539 7.843  33.491 1.00 51.86  ? 333 THR A O   1 
ATOM   2250 C CB  . THR A 1 333 ? 22.912 5.051  33.699 1.00 54.93  ? 333 THR A CB  1 
ATOM   2251 O OG1 . THR A 1 333 ? 22.832 3.654  33.456 1.00 91.57  ? 333 THR A OG1 1 
ATOM   2252 C CG2 . THR A 1 333 ? 21.625 5.665  33.085 1.00 20.81  ? 333 THR A CG2 1 
ATOM   2253 N N   . VAL A 1 334 ? 23.128 7.230  31.336 1.00 50.77  ? 334 VAL A N   1 
ATOM   2254 C CA  . VAL A 1 334 ? 22.645 8.512  30.804 1.00 47.27  ? 334 VAL A CA  1 
ATOM   2255 C C   . VAL A 1 334 ? 22.040 9.473  31.843 1.00 40.38  ? 334 VAL A C   1 
ATOM   2256 O O   . VAL A 1 334 ? 22.716 10.403 32.309 1.00 34.35  ? 334 VAL A O   1 
ATOM   2257 C CB  . VAL A 1 334 ? 23.790 9.149  29.919 1.00 46.39  ? 334 VAL A CB  1 
ATOM   2258 C CG1 . VAL A 1 334 ? 24.987 9.614  30.753 1.00 48.78  ? 334 VAL A CG1 1 
ATOM   2259 C CG2 . VAL A 1 334 ? 24.313 8.181  28.893 1.00 43.62  ? 334 VAL A CG2 1 
ATOM   2260 N N   . LYS A 1 335 ? 20.773 9.239  32.206 1.00 33.45  ? 335 LYS A N   1 
ATOM   2261 C CA  . LYS A 1 335 ? 20.062 10.055 33.172 1.00 34.38  ? 335 LYS A CA  1 
ATOM   2262 C C   . LYS A 1 335 ? 20.621 9.786  34.548 1.00 46.81  ? 335 LYS A C   1 
ATOM   2263 O O   . LYS A 1 335 ? 20.650 10.699 35.384 1.00 47.94  ? 335 LYS A O   1 
ATOM   2264 C CB  . LYS A 1 335 ? 18.573 9.717  33.216 1.00 40.36  ? 335 LYS A CB  1 
ATOM   2265 C CG  . LYS A 1 335 ? 17.655 10.131 32.026 1.00 55.77  ? 335 LYS A CG  1 
ATOM   2266 C CD  . LYS A 1 335 ? 16.169 9.676  32.117 1.00 64.98  ? 335 LYS A CD  1 
ATOM   2267 C CE  . LYS A 1 335 ? 15.488 9.850  33.511 1.00 38.45  ? 335 LYS A CE  1 
ATOM   2268 N NZ  . LYS A 1 335 ? 16.228 9.156  34.622 1.00 26.56  ? 335 LYS A NZ  1 
ATOM   2269 N N   . GLN A 1 336 ? 21.063 8.544  34.788 1.00 45.49  ? 336 GLN A N   1 
ATOM   2270 C CA  . GLN A 1 336 ? 21.628 8.199  36.083 1.00 41.80  ? 336 GLN A CA  1 
ATOM   2271 C C   . GLN A 1 336 ? 22.724 9.198  36.468 1.00 52.56  ? 336 GLN A C   1 
ATOM   2272 O O   . GLN A 1 336 ? 22.551 9.958  37.415 1.00 62.03  ? 336 GLN A O   1 
ATOM   2273 C CB  . GLN A 1 336 ? 21.994 6.763  36.218 1.00 39.91  ? 336 GLN A CB  1 
ATOM   2274 C CG  . GLN A 1 336 ? 21.149 6.274  37.284 1.00 50.55  ? 336 GLN A CG  1 
ATOM   2275 C CD  . GLN A 1 336 ? 21.391 7.023  38.535 1.00 83.86  ? 336 GLN A CD  1 
ATOM   2276 O OE1 . GLN A 1 336 ? 20.803 8.102  38.768 1.00 71.38  ? 336 GLN A OE1 1 
ATOM   2277 N NE2 . GLN A 1 336 ? 22.294 6.468  39.368 1.00 69.76  ? 336 GLN A NE2 1 
ATOM   2278 N N   . CYS A 1 337 ? 23.848 9.231  35.745 1.00 46.33  ? 337 CYS A N   1 
ATOM   2279 C CA  . CYS A 1 337 ? 24.917 10.184 36.083 1.00 42.09  ? 337 CYS A CA  1 
ATOM   2280 C C   . CYS A 1 337 ? 24.416 11.611 36.082 1.00 34.72  ? 337 CYS A C   1 
ATOM   2281 O O   . CYS A 1 337 ? 24.727 12.375 36.987 1.00 40.21  ? 337 CYS A O   1 
ATOM   2282 C CB  . CYS A 1 337 ? 26.021 10.182 35.059 1.00 41.27  ? 337 CYS A CB  1 
ATOM   2283 S SG  . CYS A 1 337 ? 26.156 8.608  34.183 1.00 42.64  ? 337 CYS A SG  1 
ATOM   2284 N N   . ILE A 1 338 ? 23.653 11.979 35.071 1.00 29.37  ? 338 ILE A N   1 
ATOM   2285 C CA  . ILE A 1 338 ? 23.142 13.341 35.019 1.00 35.37  ? 338 ILE A CA  1 
ATOM   2286 C C   . ILE A 1 338 ? 22.154 13.594 36.166 1.00 48.72  ? 338 ILE A C   1 
ATOM   2287 O O   . ILE A 1 338 ? 22.092 14.697 36.715 1.00 49.34  ? 338 ILE A O   1 
ATOM   2288 C CB  . ILE A 1 338 ? 22.309 13.675 33.806 1.00 36.57  ? 338 ILE A CB  1 
ATOM   2289 C CG1 . ILE A 1 338 ? 23.061 13.548 32.471 1.00 34.03  ? 338 ILE A CG1 1 
ATOM   2290 C CG2 . ILE A 1 338 ? 21.753 15.053 33.999 1.00 39.78  ? 338 ILE A CG2 1 
ATOM   2291 C CD1 . ILE A 1 338 ? 22.112 13.884 31.332 1.00 21.97  ? 338 ILE A CD1 1 
ATOM   2292 N N   . MET A 1 339 ? 21.378 12.571 36.523 1.00 44.98  ? 339 MET A N   1 
ATOM   2293 C CA  . MET A 1 339 ? 20.410 12.732 37.607 1.00 49.24  ? 339 MET A CA  1 
ATOM   2294 C C   . MET A 1 339 ? 21.106 12.660 38.958 1.00 42.04  ? 339 MET A C   1 
ATOM   2295 O O   . MET A 1 339 ? 20.477 12.930 39.978 1.00 42.68  ? 339 MET A O   1 
ATOM   2296 C CB  . MET A 1 339 ? 19.136 11.720 37.525 1.00 56.34  ? 339 MET A CB  1 
ATOM   2297 C CG  . MET A 1 339 ? 18.108 11.462 38.716 1.00 61.25  ? 339 MET A CG  1 
ATOM   2298 S SD  . MET A 1 339 ? 17.671 9.618  39.046 1.00 70.88  ? 339 MET A SD  1 
ATOM   2299 C CE  . MET A 1 339 ? 16.970 9.588  40.739 1.00 66.82  ? 339 MET A CE  1 
ATOM   2300 N N   . CYS A 1 340 ? 22.395 12.304 38.957 1.00 37.32  ? 340 CYS A N   1 
ATOM   2301 C CA  . CYS A 1 340 ? 23.179 12.186 40.190 1.00 38.02  ? 340 CYS A CA  1 
ATOM   2302 C C   . CYS A 1 340 ? 23.870 13.458 40.617 1.00 46.69  ? 340 CYS A C   1 
ATOM   2303 O O   . CYS A 1 340 ? 23.862 13.801 41.794 1.00 48.20  ? 340 CYS A O   1 
ATOM   2304 C CB  . CYS A 1 340 ? 24.263 11.154 40.064 1.00 42.43  ? 340 CYS A CB  1 
ATOM   2305 S SG  . CYS A 1 340 ? 25.329 11.247 41.546 1.00 49.61  ? 340 CYS A SG  1 
ATOM   2306 N N   . GLY A 1 341 ? 24.478 14.142 39.659 1.00 50.65  ? 341 GLY A N   1 
ATOM   2307 C CA  . GLY A 1 341 ? 25.175 15.383 39.955 1.00 48.94  ? 341 GLY A CA  1 
ATOM   2308 C C   . GLY A 1 341 ? 24.142 16.400 40.429 1.00 41.01  ? 341 GLY A C   1 
ATOM   2309 O O   . GLY A 1 341 ? 24.462 17.415 41.059 1.00 32.07  ? 341 GLY A O   1 
ATOM   2310 N N   . ASN A 1 342 ? 22.890 16.099 40.098 1.00 39.50  ? 342 ASN A N   1 
ATOM   2311 C CA  . ASN A 1 342 ? 21.758 16.945 40.455 1.00 39.87  ? 342 ASN A CA  1 
ATOM   2312 C C   . ASN A 1 342 ? 21.727 17.116 41.969 1.00 48.67  ? 342 ASN A C   1 
ATOM   2313 O O   . ASN A 1 342 ? 21.551 18.221 42.500 1.00 48.55  ? 342 ASN A O   1 
ATOM   2314 C CB  . ASN A 1 342 ? 20.399 16.465 39.848 1.00 47.34  ? 342 ASN A CB  1 
ATOM   2315 C CG  . ASN A 1 342 ? 20.311 16.679 38.282 1.00 57.98  ? 342 ASN A CG  1 
ATOM   2316 O OD1 . ASN A 1 342 ? 19.263 16.461 37.708 1.00 67.52  ? 342 ASN A OD1 1 
ATOM   2317 N ND2 . ASN A 1 342 ? 21.353 17.147 37.651 1.00 25.04  ? 342 ASN A ND2 1 
ATOM   2318 N N   . ALA A 1 343 ? 21.920 15.999 42.674 1.00 42.13  ? 343 ALA A N   1 
ATOM   2319 C CA  . ALA A 1 343 ? 21.930 16.019 44.126 1.00 41.78  ? 343 ALA A CA  1 
ATOM   2320 C C   . ALA A 1 343 ? 23.333 16.260 44.604 1.00 45.95  ? 343 ALA A C   1 
ATOM   2321 O O   . ALA A 1 343 ? 23.662 16.051 45.774 1.00 50.12  ? 343 ALA A O   1 
ATOM   2322 C CB  . ALA A 1 343 ? 21.445 14.771 44.717 1.00 45.92  ? 343 ALA A CB  1 
ATOM   2323 N N   . CYS A 1 344 ? 24.151 16.704 43.678 1.00 41.01  ? 344 CYS A N   1 
ATOM   2324 C CA  . CYS A 1 344 ? 25.534 16.991 43.982 1.00 42.29  ? 344 CYS A CA  1 
ATOM   2325 C C   . CYS A 1 344 ? 25.652 18.499 44.202 1.00 42.81  ? 344 CYS A C   1 
ATOM   2326 O O   . CYS A 1 344 ? 26.276 18.972 45.147 1.00 40.48  ? 344 CYS A O   1 
ATOM   2327 C CB  . CYS A 1 344 ? 26.401 16.482 42.845 1.00 38.33  ? 344 CYS A CB  1 
ATOM   2328 S SG  . CYS A 1 344 ? 26.965 14.898 43.371 1.00 40.22  ? 344 CYS A SG  1 
ATOM   2329 N N   . ALA A 1 345 ? 25.023 19.211 43.281 1.00 35.49  ? 345 ALA A N   1 
ATOM   2330 C CA  . ALA A 1 345 ? 24.959 20.653 43.248 1.00 33.47  ? 345 ALA A CA  1 
ATOM   2331 C C   . ALA A 1 345 ? 23.890 21.064 44.239 1.00 34.68  ? 345 ALA A C   1 
ATOM   2332 O O   . ALA A 1 345 ? 24.117 21.924 45.071 1.00 34.04  ? 345 ALA A O   1 
ATOM   2333 C CB  . ALA A 1 345 ? 24.419 20.998 41.828 1.00 34.41  ? 345 ALA A CB  1 
ATOM   2334 N N   . GLN A 1 346 ? 22.734 20.420 44.110 1.00 30.19  ? 346 GLN A N   1 
ATOM   2335 C CA  . GLN A 1 346 ? 21.580 20.655 44.959 1.00 33.08  ? 346 GLN A CA  1 
ATOM   2336 C C   . GLN A 1 346 ? 22.038 20.665 46.389 1.00 35.76  ? 346 GLN A C   1 
ATOM   2337 O O   . GLN A 1 346 ? 21.657 21.517 47.170 1.00 44.59  ? 346 GLN A O   1 
ATOM   2338 C CB  . GLN A 1 346 ? 20.637 19.444 44.930 1.00 36.73  ? 346 GLN A CB  1 
ATOM   2339 C CG  . GLN A 1 346 ? 20.193 19.010 46.333 1.00 71.95  ? 346 GLN A CG  1 
ATOM   2340 C CD  . GLN A 1 346 ? 18.933 18.168 46.312 1.00 94.50  ? 346 GLN A CD  1 
ATOM   2341 O OE1 . GLN A 1 346 ? 18.262 17.944 47.351 1.00 82.49  ? 346 GLN A OE1 1 
ATOM   2342 N NE2 . GLN A 1 346 ? 18.602 17.681 45.120 1.00 70.09  ? 346 GLN A NE2 1 
ATOM   2343 N N   . ASP A 1 347 ? 22.871 19.696 46.697 1.00 37.78  ? 347 ASP A N   1 
ATOM   2344 C CA  . ASP A 1 347 ? 23.438 19.523 48.015 1.00 43.90  ? 347 ASP A CA  1 
ATOM   2345 C C   . ASP A 1 347 ? 24.663 20.396 48.129 1.00 42.88  ? 347 ASP A C   1 
ATOM   2346 O O   . ASP A 1 347 ? 25.129 20.674 49.227 1.00 40.63  ? 347 ASP A O   1 
ATOM   2347 C CB  . ASP A 1 347 ? 24.109 18.131 48.054 1.00 50.72  ? 347 ASP A CB  1 
ATOM   2348 C CG  . ASP A 1 347 ? 23.716 17.297 49.281 1.00 62.31  ? 347 ASP A CG  1 
ATOM   2349 O OD1 . ASP A 1 347 ? 24.574 16.613 49.898 1.00 58.87  ? 347 ASP A OD1 1 
ATOM   2350 O OD2 . ASP A 1 347 ? 22.513 17.331 49.623 1.00 69.41  ? 347 ASP A OD2 1 
ATOM   2351 N N   . VAL A 1 348 ? 25.175 20.813 46.973 1.00 41.63  ? 348 VAL A N   1 
ATOM   2352 C CA  . VAL A 1 348 ? 26.355 21.662 46.933 1.00 44.46  ? 348 VAL A CA  1 
ATOM   2353 C C   . VAL A 1 348 ? 26.040 23.139 47.025 1.00 57.40  ? 348 VAL A C   1 
ATOM   2354 O O   . VAL A 1 348 ? 26.549 23.832 47.900 1.00 55.90  ? 348 VAL A O   1 
ATOM   2355 C CB  . VAL A 1 348 ? 27.678 21.104 46.407 1.00 47.50  ? 348 VAL A CB  1 
ATOM   2356 C CG1 . VAL A 1 348 ? 28.726 22.189 46.200 1.00 43.63  ? 348 VAL A CG1 1 
ATOM   2357 C CG2 . VAL A 1 348 ? 28.176 19.923 47.277 1.00 47.30  ? 348 VAL A CG2 1 
ATOM   2358 N N   . ILE A 1 349 ? 25.190 23.620 46.128 1.00 63.32  ? 349 ILE A N   1 
ATOM   2359 C CA  . ILE A 1 349 ? 24.807 25.023 46.132 1.00 65.38  ? 349 ILE A CA  1 
ATOM   2360 C C   . ILE A 1 349 ? 24.179 25.364 47.490 1.00 69.04  ? 349 ILE A C   1 
ATOM   2361 O O   . ILE A 1 349 ? 24.020 26.538 47.817 1.00 75.89  ? 349 ILE A O   1 
ATOM   2362 C CB  . ILE A 1 349 ? 23.825 25.343 44.927 1.00 66.56  ? 349 ILE A CB  1 
ATOM   2363 C CG1 . ILE A 1 349 ? 23.707 26.861 44.606 1.00 63.27  ? 349 ILE A CG1 1 
ATOM   2364 C CG2 . ILE A 1 349 ? 22.441 24.724 45.187 1.00 68.87  ? 349 ILE A CG2 1 
ATOM   2365 C CD1 . ILE A 1 349 ? 23.464 27.218 43.131 1.00 44.92  ? 349 ILE A CD1 1 
ATOM   2366 N N   . GLN A 1 350 ? 23.863 24.317 48.277 1.00 57.53  ? 350 GLN A N   1 
ATOM   2367 C CA  . GLN A 1 350 ? 23.280 24.440 49.597 1.00 56.02  ? 350 GLN A CA  1 
ATOM   2368 C C   . GLN A 1 350 ? 24.280 25.005 50.577 1.00 70.34  ? 350 GLN A C   1 
ATOM   2369 O O   . GLN A 1 350 ? 24.208 26.178 50.951 1.00 70.82  ? 350 GLN A O   1 
ATOM   2370 C CB  . GLN A 1 350 ? 23.022 23.047 50.137 1.00 55.44  ? 350 GLN A CB  1 
ATOM   2371 C CG  . GLN A 1 350 ? 21.654 22.959 50.795 1.00 21.83  ? 350 GLN A CG  1 
ATOM   2372 C CD  . GLN A 1 350 ? 21.498 21.881 51.768 1.00 46.83  ? 350 GLN A CD  1 
ATOM   2373 O OE1 . GLN A 1 350 ? 22.132 21.867 52.832 1.00 55.98  ? 350 GLN A OE1 1 
ATOM   2374 N NE2 . GLN A 1 350 ? 20.620 20.967 51.451 1.00 33.88  ? 350 GLN A NE2 1 
ATOM   2375 N N   . HIS A 1 351 ? 25.204 24.144 50.998 1.00 81.61  ? 351 HIS A N   1 
ATOM   2376 C CA  . HIS A 1 351 ? 26.238 24.542 51.951 1.00 88.70  ? 351 HIS A CA  1 
ATOM   2377 C C   . HIS A 1 351 ? 27.221 25.519 51.325 1.00 95.36  ? 351 HIS A C   1 
ATOM   2378 O O   . HIS A 1 351 ? 27.288 25.653 50.099 1.00 100.00 ? 351 HIS A O   1 
ATOM   2379 C CB  . HIS A 1 351 ? 26.989 23.341 52.583 1.00 92.43  ? 351 HIS A CB  1 
ATOM   2380 C CG  . HIS A 1 351 ? 26.074 22.328 53.197 1.00 97.99  ? 351 HIS A CG  1 
ATOM   2381 N ND1 . HIS A 1 351 ? 26.314 21.717 54.414 1.00 100.00 ? 351 HIS A ND1 1 
ATOM   2382 C CD2 . HIS A 1 351 ? 24.911 21.820 52.737 1.00 100.00 ? 351 HIS A CD2 1 
ATOM   2383 C CE1 . HIS A 1 351 ? 25.322 20.879 54.675 1.00 99.00  ? 351 HIS A CE1 1 
ATOM   2384 N NE2 . HIS A 1 351 ? 24.458 20.925 53.674 1.00 100.00 ? 351 HIS A NE2 1 
ATOM   2385 N N   . VAL A 1 352 ? 27.978 26.200 52.185 1.00 91.00  ? 352 VAL A N   1 
ATOM   2386 C CA  . VAL A 1 352 ? 28.989 27.197 51.815 1.00 92.60  ? 352 VAL A CA  1 
ATOM   2387 C C   . VAL A 1 352 ? 29.761 26.879 50.523 1.00 88.53  ? 352 VAL A C   1 
ATOM   2388 O O   . VAL A 1 352 ? 29.579 25.832 49.887 1.00 86.05  ? 352 VAL A O   1 
ATOM   2389 C CB  . VAL A 1 352 ? 29.939 27.366 53.077 1.00 100.00 ? 352 VAL A CB  1 
ATOM   2390 C CG1 . VAL A 1 352 ? 31.420 27.716 52.816 1.00 100.00 ? 352 VAL A CG1 1 
ATOM   2391 C CG2 . VAL A 1 352 ? 29.297 28.152 54.233 1.00 100.00 ? 352 VAL A CG2 1 
ATOM   2392 N N   . GLY A 1 353 ? 30.636 27.807 50.148 1.00 78.12  ? 353 GLY A N   1 
ATOM   2393 C CA  . GLY A 1 353 ? 31.439 27.632 48.954 1.00 76.13  ? 353 GLY A CA  1 
ATOM   2394 C C   . GLY A 1 353 ? 32.178 26.313 49.062 1.00 76.38  ? 353 GLY A C   1 
ATOM   2395 O O   . GLY A 1 353 ? 33.199 26.213 49.730 1.00 73.13  ? 353 GLY A O   1 
ATOM   2396 N N   . PHE A 1 354 ? 31.614 25.300 48.390 1.00 73.81  ? 354 PHE A N   1 
ATOM   2397 C CA  . PHE A 1 354 ? 32.130 23.911 48.325 1.00 70.14  ? 354 PHE A CA  1 
ATOM   2398 C C   . PHE A 1 354 ? 32.361 23.268 49.673 1.00 63.65  ? 354 PHE A C   1 
ATOM   2399 O O   . PHE A 1 354 ? 33.433 22.695 49.913 1.00 63.86  ? 354 PHE A O   1 
ATOM   2400 C CB  . PHE A 1 354 ? 33.257 23.569 47.338 1.00 72.62  ? 354 PHE A CB  1 
ATOM   2401 C CG  . PHE A 1 354 ? 32.856 22.669 46.150 1.00 73.59  ? 354 PHE A CG  1 
ATOM   2402 C CD1 . PHE A 1 354 ? 32.986 21.298 46.197 1.00 74.45  ? 354 PHE A CD1 1 
ATOM   2403 C CD2 . PHE A 1 354 ? 32.404 23.232 44.950 1.00 74.88  ? 354 PHE A CD2 1 
ATOM   2404 C CE1 . PHE A 1 354 ? 32.635 20.516 45.084 1.00 73.59  ? 354 PHE A CE1 1 
ATOM   2405 C CE2 . PHE A 1 354 ? 32.060 22.449 43.851 1.00 74.69  ? 354 PHE A CE2 1 
ATOM   2406 C CZ  . PHE A 1 354 ? 32.173 21.078 43.910 1.00 71.06  ? 354 PHE A CZ  1 
ATOM   2407 N N   . SER A 1 355 ? 31.354 23.328 50.524 1.00 56.43  ? 355 SER A N   1 
ATOM   2408 C CA  . SER A 1 355 ? 31.475 22.703 51.820 1.00 55.24  ? 355 SER A CA  1 
ATOM   2409 C C   . SER A 1 355 ? 31.182 21.214 51.594 1.00 59.69  ? 355 SER A C   1 
ATOM   2410 O O   . SER A 1 355 ? 30.023 20.852 51.418 1.00 67.25  ? 355 SER A O   1 
ATOM   2411 C CB  . SER A 1 355 ? 30.624 23.405 52.890 1.00 58.47  ? 355 SER A CB  1 
ATOM   2412 O OG  . SER A 1 355 ? 31.507 24.113 53.765 1.00 63.26  ? 355 SER A OG  1 
ATOM   2413 N N   . LEU A 1 356 ? 32.189 20.341 51.558 1.00 52.78  ? 356 LEU A N   1 
ATOM   2414 C CA  . LEU A 1 356 ? 32.007 18.911 51.318 1.00 54.71  ? 356 LEU A CA  1 
ATOM   2415 C C   . LEU A 1 356 ? 31.291 18.131 52.396 1.00 70.87  ? 356 LEU A C   1 
ATOM   2416 O O   . LEU A 1 356 ? 31.718 17.969 53.558 1.00 66.85  ? 356 LEU A O   1 
ATOM   2417 C CB  . LEU A 1 356 ? 33.000 18.234 50.370 1.00 53.87  ? 356 LEU A CB  1 
ATOM   2418 C CG  . LEU A 1 356 ? 32.406 18.608 49.021 1.00 57.39  ? 356 LEU A CG  1 
ATOM   2419 C CD1 . LEU A 1 356 ? 33.249 18.290 47.770 1.00 61.10  ? 356 LEU A CD1 1 
ATOM   2420 C CD2 . LEU A 1 356 ? 30.915 18.295 48.970 1.00 44.95  ? 356 LEU A CD2 1 
HETATM 2421 O O   . HOH B 2 .   ? 48.830 27.601 17.030 1.00 67.37  ? 364 HOH A O   1 
HETATM 2422 O O   . HOH B 2 .   ? 50.592 36.926 48.524 1.00 21.69  ? 365 HOH A O   1 
HETATM 2423 O O   . HOH B 2 .   ? 38.830 9.139  24.244 1.00 21.92  ? 366 HOH A O   1 
HETATM 2424 O O   . HOH B 2 .   ? 48.648 27.727 60.718 1.00 75.73  ? 367 HOH A O   1 
HETATM 2425 O O   . HOH B 2 .   ? 12.680 30.537 46.151 1.00 21.50  ? 368 HOH A O   1 
HETATM 2426 O O   . HOH B 2 .   ? 32.017 19.693 55.017 1.00 35.90  ? 369 HOH A O   1 
HETATM 2427 O O   . HOH B 2 .   ? 29.873 36.195 37.457 1.00 44.80  ? 370 HOH A O   1 
HETATM 2428 O O   . HOH B 2 .   ? 20.253 4.038  54.691 1.00 53.09  ? 371 HOH A O   1 
HETATM 2429 O O   . HOH B 2 .   ? 48.971 37.062 46.916 1.00 35.37  ? 372 HOH A O   1 
HETATM 2430 O O   . HOH B 2 .   ? 56.809 20.140 41.910 1.00 38.77  ? 373 HOH A O   1 
HETATM 2431 O O   . HOH B 2 .   ? 21.196 12.932 50.571 1.00 43.38  ? 374 HOH A O   1 
HETATM 2432 O O   . HOH B 2 .   ? 43.213 30.421 17.756 1.00 31.41  ? 375 HOH A O   1 
HETATM 2433 O O   . HOH B 2 .   ? 45.523 24.782 64.686 1.00 42.65  ? 376 HOH A O   1 
HETATM 2434 O O   . HOH B 2 .   ? 19.805 10.337 15.835 1.00 25.87  ? 377 HOH A O   1 
HETATM 2435 O O   . HOH B 2 .   ? 18.491 20.818 52.462 1.00 27.81  ? 378 HOH A O   1 
HETATM 2436 O O   . HOH B 2 .   ? 23.773 12.797 47.498 1.00 41.04  ? 379 HOH A O   1 
HETATM 2437 O O   . HOH B 2 .   ? 25.606 -0.126 25.165 1.00 33.49  ? 380 HOH A O   1 
HETATM 2438 O O   . HOH B 2 .   ? 23.083 4.201  30.316 1.00 60.17  ? 381 HOH A O   1 
HETATM 2439 O O   . HOH B 2 .   ? 33.556 26.707 6.489  1.00 61.78  ? 382 HOH A O   1 
HETATM 2440 O O   . HOH B 2 .   ? 50.170 35.412 44.165 1.00 44.60  ? 383 HOH A O   1 
HETATM 2441 O O   . HOH B 2 .   ? 53.657 5.234  42.343 1.00 29.56  ? 384 HOH A O   1 
HETATM 2442 O O   . HOH B 2 .   ? 59.396 25.484 24.345 1.00 81.00  ? 385 HOH A O   1 
HETATM 2443 O O   . HOH B 2 .   ? 30.020 42.064 53.326 1.00 45.20  ? 386 HOH A O   1 
HETATM 2444 O O   . HOH B 2 .   ? 26.448 18.898 57.496 1.00 75.32  ? 387 HOH A O   1 
HETATM 2445 O O   . HOH B 2 .   ? 51.785 33.421 54.192 1.00 65.87  ? 388 HOH A O   1 
HETATM 2446 O O   . HOH B 2 .   ? 47.601 33.087 58.486 1.00 38.61  ? 389 HOH A O   1 
HETATM 2447 O O   . HOH B 2 .   ? 24.584 -2.087 34.266 1.00 70.56  ? 390 HOH A O   1 
HETATM 2448 O O   . HOH B 2 .   ? 50.919 10.934 48.637 1.00 54.39  ? 391 HOH A O   1 
HETATM 2449 O O   . HOH B 2 .   ? 52.057 39.617 45.100 1.00 28.44  ? 392 HOH A O   1 
HETATM 2450 O O   . HOH B 2 .   ? 32.560 14.601 17.529 1.00 24.77  ? 393 HOH A O   1 
HETATM 2451 O O   . HOH B 2 .   ? 51.806 4.084  29.394 1.00 30.40  ? 394 HOH A O   1 
HETATM 2452 O O   . HOH B 2 .   ? 35.807 19.259 52.748 1.00 37.36  ? 395 HOH A O   1 
HETATM 2453 O O   . HOH B 2 .   ? 21.709 31.835 27.602 1.00 36.69  ? 396 HOH A O   1 
HETATM 2454 O O   . HOH B 2 .   ? 60.155 21.467 25.521 1.00 60.88  ? 397 HOH A O   1 
HETATM 2455 O O   . HOH B 2 .   ? 26.863 44.791 34.447 1.00 44.30  ? 398 HOH A O   1 
HETATM 2456 O O   . HOH B 2 .   ? 28.646 16.498 47.720 1.00 39.22  ? 399 HOH A O   1 
HETATM 2457 O O   . HOH B 2 .   ? 16.708 29.113 33.567 1.00 43.92  ? 400 HOH A O   1 
HETATM 2458 O O   . HOH B 2 .   ? 59.464 19.934 28.476 1.00 36.31  ? 401 HOH A O   1 
HETATM 2459 O O   . HOH B 2 .   ? 26.338 36.498 27.407 1.00 28.60  ? 402 HOH A O   1 
HETATM 2460 O O   . HOH B 2 .   ? 53.667 20.938 27.244 1.00 39.20  ? 403 HOH A O   1 
HETATM 2461 O O   . HOH B 2 .   ? 58.412 4.877  38.268 1.00 35.83  ? 404 HOH A O   1 
HETATM 2462 O O   . HOH B 2 .   ? 29.926 -6.859 49.099 1.00 81.63  ? 405 HOH A O   1 
HETATM 2463 O O   . HOH B 2 .   ? 33.958 21.261 52.815 1.00 28.23  ? 406 HOH A O   1 
HETATM 2464 O O   . HOH B 2 .   ? 46.329 28.054 63.146 1.00 77.24  ? 407 HOH A O   1 
HETATM 2465 O O   . HOH B 2 .   ? 32.172 10.110 10.192 1.00 31.88  ? 408 HOH A O   1 
HETATM 2466 O O   . HOH B 2 .   ? 17.674 21.707 47.769 1.00 50.47  ? 409 HOH A O   1 
HETATM 2467 O O   . HOH B 2 .   ? 45.933 17.379 15.691 1.00 51.50  ? 410 HOH A O   1 
HETATM 2468 O O   . HOH B 2 .   ? 56.372 21.061 57.543 1.00 64.68  ? 411 HOH A O   1 
HETATM 2469 O O   . HOH B 2 .   ? 31.004 23.463 61.772 1.00 41.90  ? 412 HOH A O   1 
HETATM 2470 O O   . HOH B 2 .   ? 17.016 17.079 53.539 1.00 42.79  ? 413 HOH A O   1 
HETATM 2471 O O   . HOH B 2 .   ? 21.972 34.674 49.221 1.00 24.63  ? 414 HOH A O   1 
HETATM 2472 O O   . HOH B 2 .   ? 28.416 -0.763 24.915 1.00 54.07  ? 415 HOH A O   1 
HETATM 2473 O O   . HOH B 2 .   ? 25.578 38.455 62.471 1.00 42.15  ? 416 HOH A O   1 
HETATM 2474 O O   . HOH B 2 .   ? 18.123 1.743  51.170 1.00 13.15  ? 417 HOH A O   1 
HETATM 2475 O O   . HOH B 2 .   ? 56.526 26.470 37.503 1.00 84.03  ? 418 HOH A O   1 
HETATM 2476 O O   . HOH B 2 .   ? 57.187 41.461 46.460 1.00 47.60  ? 419 HOH A O   1 
HETATM 2477 O O   . HOH B 2 .   ? 26.825 29.240 53.542 1.00 51.44  ? 420 HOH A O   1 
HETATM 2478 O O   . HOH B 2 .   ? 16.580 22.362 53.020 1.00 20.25  ? 421 HOH A O   1 
HETATM 2479 O O   . HOH B 2 .   ? 40.169 24.141 55.577 1.00 40.47  ? 422 HOH A O   1 
HETATM 2480 O O   . HOH B 2 .   ? 32.738 3.744  46.475 1.00 29.48  ? 423 HOH A O   1 
HETATM 2481 O O   . HOH B 2 .   ? 21.403 21.558 35.986 1.00 37.90  ? 424 HOH A O   1 
HETATM 2482 O O   . HOH B 2 .   ? 28.396 45.563 38.620 1.00 53.84  ? 425 HOH A O   1 
HETATM 2483 O O   . HOH B 2 .   ? 20.230 49.774 43.077 1.00 47.96  ? 426 HOH A O   1 
HETATM 2484 O O   . HOH B 2 .   ? 35.844 8.013  39.755 1.00 95.17  ? 427 HOH A O   1 
HETATM 2485 O O   . HOH B 2 .   ? 15.716 4.119  15.655 1.00 34.95  ? 428 HOH A O   1 
HETATM 2486 O O   . HOH B 2 .   ? 26.469 28.167 35.760 1.00 38.78  ? 429 HOH A O   1 
HETATM 2487 O O   . HOH B 2 .   ? 11.238 18.885 30.953 1.00 33.64  ? 430 HOH A O   1 
HETATM 2488 O O   . HOH B 2 .   ? 28.040 38.545 57.140 1.00 22.35  ? 431 HOH A O   1 
HETATM 2489 O O   . HOH B 2 .   ? 24.247 47.827 49.016 1.00 40.29  ? 432 HOH A O   1 
HETATM 2490 O O   . HOH B 2 .   ? 36.105 30.217 61.043 1.00 65.91  ? 433 HOH A O   1 
HETATM 2491 O O   . HOH B 2 .   ? 33.137 33.863 58.796 1.00 64.99  ? 434 HOH A O   1 
HETATM 2492 O O   . HOH B 2 .   ? 28.139 24.122 16.981 1.00 30.54  ? 435 HOH A O   1 
HETATM 2493 O O   . HOH B 2 .   ? 54.601 16.186 23.293 1.00 33.35  ? 436 HOH A O   1 
HETATM 2494 O O   . HOH B 2 .   ? 39.834 29.384 37.976 1.00 38.44  ? 437 HOH A O   1 
HETATM 2495 O O   . HOH B 2 .   ? 45.903 8.579  43.271 1.00 26.77  ? 438 HOH A O   1 
HETATM 2496 O O   . HOH B 2 .   ? 17.334 26.802 13.574 1.00 52.23  ? 439 HOH A O   1 
HETATM 2497 O O   . HOH B 2 .   ? 40.608 23.661 66.550 1.00 34.99  ? 440 HOH A O   1 
HETATM 2498 O O   . HOH B 2 .   ? 17.998 10.321 15.488 1.00 23.79  ? 441 HOH A O   1 
HETATM 2499 O O   . HOH B 2 .   ? 49.803 31.859 35.494 1.00 100.00 ? 442 HOH A O   1 
HETATM 2500 O O   . HOH B 2 .   ? 48.011 36.353 38.044 1.00 27.16  ? 443 HOH A O   1 
HETATM 2501 O O   . HOH B 2 .   ? 44.984 22.243 17.392 1.00 24.98  ? 444 HOH A O   1 
HETATM 2502 O O   . HOH B 2 .   ? 21.427 28.040 23.977 1.00 64.23  ? 445 HOH A O   1 
HETATM 2503 O O   . HOH B 2 .   ? 17.879 -0.374 38.713 1.00 46.62  ? 446 HOH A O   1 
HETATM 2504 O O   . HOH B 2 .   ? 49.657 5.295  39.276 1.00 26.85  ? 447 HOH A O   1 
HETATM 2505 O O   . HOH B 2 .   ? 31.719 -6.231 25.829 1.00 33.48  ? 448 HOH A O   1 
HETATM 2506 O O   . HOH B 2 .   ? 44.076 51.271 48.010 1.00 32.71  ? 449 HOH A O   1 
HETATM 2507 O O   . HOH B 2 .   ? 28.503 33.238 44.672 1.00 78.36  ? 450 HOH A O   1 
HETATM 2508 O O   . HOH B 2 .   ? 23.312 38.468 62.290 1.00 16.87  ? 451 HOH A O   1 
HETATM 2509 O O   . HOH B 2 .   ? 28.381 25.112 59.342 1.00 25.55  ? 452 HOH A O   1 
HETATM 2510 O O   . HOH B 2 .   ? 26.959 9.804  39.762 1.00 90.01  ? 453 HOH A O   1 
HETATM 2511 O O   . HOH B 2 .   ? 15.346 49.169 47.016 1.00 35.30  ? 454 HOH A O   1 
HETATM 2512 O O   . HOH B 2 .   ? 53.825 25.720 17.855 1.00 55.28  ? 455 HOH A O   1 
HETATM 2513 O O   . HOH B 2 .   ? 37.511 52.208 52.686 1.00 34.45  ? 456 HOH A O   1 
HETATM 2514 O O   . HOH B 2 .   ? 51.667 22.932 67.447 1.00 57.29  ? 457 HOH A O   1 
HETATM 2515 O O   . HOH B 2 .   ? 20.903 27.107 40.665 1.00 62.17  ? 458 HOH A O   1 
HETATM 2516 O O   . HOH B 2 .   ? 59.354 38.347 50.177 1.00 51.05  ? 459 HOH A O   1 
HETATM 2517 O O   . HOH B 2 .   ? 22.420 19.532 37.311 1.00 27.42  ? 460 HOH A O   1 
HETATM 2518 O O   . HOH B 2 .   ? 20.441 5.974  30.076 1.00 52.08  ? 461 HOH A O   1 
HETATM 2519 O O   . HOH B 2 .   ? 48.828 12.454 23.719 1.00 36.64  ? 462 HOH A O   1 
HETATM 2520 O O   . HOH B 2 .   ? 51.852 21.107 63.847 1.00 35.33  ? 463 HOH A O   1 
HETATM 2521 O O   . HOH B 2 .   ? 24.777 14.756 14.933 1.00 49.53  ? 464 HOH A O   1 
HETATM 2522 O O   . HOH B 2 .   ? 55.545 31.515 32.923 1.00 41.72  ? 465 HOH A O   1 
HETATM 2523 O O   . HOH B 2 .   ? 18.014 32.672 19.266 1.00 49.19  ? 466 HOH A O   1 
HETATM 2524 O O   . HOH B 2 .   ? 46.772 16.465 60.079 1.00 24.43  ? 467 HOH A O   1 
HETATM 2525 O O   . HOH B 2 .   ? 32.768 19.551 13.058 1.00 57.58  ? 468 HOH A O   1 
HETATM 2526 O O   . HOH B 2 .   ? 30.532 30.669 47.021 1.00 34.77  ? 469 HOH A O   1 
HETATM 2527 O O   . HOH B 2 .   ? 45.657 9.698  19.918 1.00 64.38  ? 470 HOH A O   1 
HETATM 2528 O O   . HOH B 2 .   ? 14.905 18.529 49.632 1.00 34.24  ? 471 HOH A O   1 
HETATM 2529 O O   . HOH B 2 .   ? 26.489 -0.575 45.087 1.00 24.45  ? 472 HOH A O   1 
HETATM 2530 O O   . HOH B 2 .   ? 31.441 47.295 35.861 1.00 45.54  ? 473 HOH A O   1 
HETATM 2531 O O   . HOH B 2 .   ? 50.114 7.265  44.222 1.00 29.35  ? 474 HOH A O   1 
HETATM 2532 O O   . HOH B 2 .   ? 22.672 6.187  27.850 1.00 36.73  ? 475 HOH A O   1 
HETATM 2533 O O   . HOH B 2 .   ? 48.534 39.050 50.150 1.00 41.43  ? 476 HOH A O   1 
HETATM 2534 O O   . HOH B 2 .   ? 15.092 16.799 24.272 1.00 39.88  ? 477 HOH A O   1 
HETATM 2535 O O   . HOH B 2 .   ? 58.634 23.093 58.918 1.00 35.86  ? 478 HOH A O   1 
HETATM 2536 O O   . HOH B 2 .   ? 32.934 33.826 12.847 1.00 51.50  ? 479 HOH A O   1 
HETATM 2537 O O   . HOH B 2 .   ? 24.261 29.732 32.332 1.00 36.23  ? 480 HOH A O   1 
HETATM 2538 O O   . HOH B 2 .   ? 17.715 20.752 57.029 1.00 55.37  ? 481 HOH A O   1 
HETATM 2539 O O   . HOH B 2 .   ? 12.890 20.552 38.350 1.00 41.99  ? 482 HOH A O   1 
HETATM 2540 O O   . HOH B 2 .   ? 12.786 6.870  30.696 1.00 77.56  ? 483 HOH A O   1 
HETATM 2541 O O   . HOH B 2 .   ? 44.275 19.925 64.241 1.00 30.34  ? 484 HOH A O   1 
HETATM 2542 O O   . HOH B 2 .   ? 30.359 31.123 10.727 1.00 42.57  ? 485 HOH A O   1 
HETATM 2543 O O   . HOH B 2 .   ? 40.983 3.502  37.652 1.00 45.06  ? 486 HOH A O   1 
HETATM 2544 O O   . HOH B 2 .   ? 29.764 21.110 13.341 1.00 47.54  ? 487 HOH A O   1 
HETATM 2545 O O   . HOH B 2 .   ? 15.746 1.275  22.950 1.00 43.23  ? 488 HOH A O   1 
HETATM 2546 O O   . HOH B 2 .   ? 21.583 34.769 29.062 1.00 37.55  ? 489 HOH A O   1 
HETATM 2547 O O   . HOH B 2 .   ? 38.254 21.194 58.886 1.00 62.42  ? 490 HOH A O   1 
HETATM 2548 O O   . HOH B 2 .   ? 46.526 3.931  43.656 1.00 30.68  ? 491 HOH A O   1 
HETATM 2549 O O   . HOH B 2 .   ? 56.292 24.647 24.701 1.00 44.36  ? 492 HOH A O   1 
HETATM 2550 O O   . HOH B 2 .   ? 19.254 42.823 50.233 1.00 45.34  ? 493 HOH A O   1 
HETATM 2551 O O   . HOH B 2 .   ? 32.100 24.088 32.127 1.00 36.53  ? 494 HOH A O   1 
HETATM 2552 O O   . HOH B 2 .   ? 27.542 22.949 14.039 1.00 78.41  ? 495 HOH A O   1 
HETATM 2553 O O   . HOH B 2 .   ? 45.429 25.990 18.802 1.00 33.47  ? 496 HOH A O   1 
HETATM 2554 O O   . HOH B 2 .   ? 21.495 1.508  46.730 1.00 54.45  ? 497 HOH A O   1 
HETATM 2555 O O   . HOH B 2 .   ? 25.825 47.696 55.352 1.00 31.63  ? 498 HOH A O   1 
HETATM 2556 O O   . HOH B 2 .   ? 46.929 22.017 14.954 1.00 30.00  ? 499 HOH A O   1 
HETATM 2557 O O   . HOH B 2 .   ? 26.188 -6.348 28.998 1.00 33.13  ? 500 HOH A O   1 
HETATM 2558 O O   . HOH B 2 .   ? 31.154 25.551 36.437 1.00 46.95  ? 501 HOH A O   1 
HETATM 2559 O O   . HOH B 2 .   ? 48.475 7.779  23.653 1.00 53.66  ? 502 HOH A O   1 
HETATM 2560 O O   . HOH B 2 .   ? 37.362 50.603 55.772 1.00 37.60  ? 503 HOH A O   1 
HETATM 2561 O O   . HOH B 2 .   ? 37.532 4.623  35.350 1.00 62.27  ? 504 HOH A O   1 
HETATM 2562 O O   . HOH B 2 .   ? 25.048 39.837 58.667 1.00 42.76  ? 505 HOH A O   1 
HETATM 2563 O O   . HOH B 2 .   ? 19.084 32.981 32.101 1.00 51.37  ? 506 HOH A O   1 
HETATM 2564 O O   . HOH B 2 .   ? 23.618 -4.189 27.920 1.00 50.84  ? 507 HOH A O   1 
HETATM 2565 O O   . HOH B 2 .   ? 23.030 26.444 33.785 1.00 36.77  ? 508 HOH A O   1 
HETATM 2566 O O   . HOH B 2 .   ? 17.462 28.384 53.283 1.00 45.79  ? 509 HOH A O   1 
HETATM 2567 O O   . HOH B 2 .   ? 26.036 23.404 9.903  1.00 93.76  ? 510 HOH A O   1 
HETATM 2568 O O   . HOH B 2 .   ? 57.457 19.432 25.466 1.00 84.82  ? 511 HOH A O   1 
HETATM 2569 O O   . HOH B 2 .   ? 27.280 29.758 6.003  1.00 62.76  ? 512 HOH A O   1 
HETATM 2570 O O   . HOH B 2 .   ? 16.912 32.145 56.956 1.00 24.52  ? 513 HOH A O   1 
HETATM 2571 O O   . HOH B 2 .   ? 21.038 24.727 22.666 1.00 29.53  ? 514 HOH A O   1 
HETATM 2572 O O   . HOH B 2 .   ? 48.704 3.709  23.247 1.00 29.79  ? 515 HOH A O   1 
HETATM 2573 O O   . HOH B 2 .   ? 36.752 29.673 44.751 1.00 20.11  ? 516 HOH A O   1 
HETATM 2574 O O   . HOH B 2 .   ? 19.424 18.545 34.290 1.00 21.82  ? 517 HOH A O   1 
HETATM 2575 O O   . HOH B 2 .   ? 31.032 17.927 20.923 1.00 22.53  ? 518 HOH A O   1 
HETATM 2576 O O   . HOH B 2 .   ? 35.186 6.182  30.803 1.00 23.91  ? 519 HOH A O   1 
HETATM 2577 O O   . HOH B 2 .   ? 27.399 26.582 55.794 1.00 24.51  ? 520 HOH A O   1 
HETATM 2578 O O   . HOH B 2 .   ? 43.812 24.109 26.735 1.00 24.76  ? 521 HOH A O   1 
HETATM 2579 O O   . HOH B 2 .   ? 23.900 35.202 62.834 1.00 25.10  ? 522 HOH A O   1 
HETATM 2580 O O   . HOH B 2 .   ? 49.874 14.342 48.117 1.00 25.58  ? 523 HOH A O   1 
HETATM 2581 O O   . HOH B 2 .   ? 25.932 0.000  47.657 1.00 26.33  ? 524 HOH A O   1 
HETATM 2582 O O   . HOH B 2 .   ? 14.150 27.200 36.615 1.00 26.55  ? 525 HOH A O   1 
HETATM 2583 O O   . HOH B 2 .   ? 52.463 5.625  24.895 1.00 26.82  ? 526 HOH A O   1 
HETATM 2584 O O   . HOH B 2 .   ? 37.636 22.254 11.624 1.00 27.05  ? 527 HOH A O   1 
HETATM 2585 O O   . HOH B 2 .   ? 20.557 14.836 15.692 1.00 27.33  ? 528 HOH A O   1 
HETATM 2586 O O   . HOH B 2 .   ? 25.486 37.709 21.504 1.00 27.58  ? 529 HOH A O   1 
HETATM 2587 O O   . HOH B 2 .   ? 35.973 23.562 47.359 1.00 27.58  ? 530 HOH A O   1 
HETATM 2588 O O   . HOH B 2 .   ? 57.985 28.436 50.563 1.00 28.45  ? 531 HOH A O   1 
HETATM 2589 O O   . HOH B 2 .   ? 15.815 22.254 56.375 1.00 28.47  ? 532 HOH A O   1 
HETATM 2590 O O   . HOH B 2 .   ? 18.634 2.473  16.273 1.00 28.69  ? 533 HOH A O   1 
HETATM 2591 O O   . HOH B 2 .   ? 12.190 12.982 27.897 1.00 29.06  ? 534 HOH A O   1 
HETATM 2592 O O   . HOH B 2 .   ? 50.702 7.418  41.264 1.00 29.97  ? 535 HOH A O   1 
HETATM 2593 O O   . HOH B 2 .   ? 23.410 35.079 62.613 1.00 20.03  ? 536 HOH A O   1 
HETATM 2594 O O   . HOH B 2 .   ? 17.169 14.836 36.615 1.00 20.04  ? 537 HOH A O   1 
HETATM 2595 O O   . HOH B 2 .   ? 26.000 -2.191 41.030 1.00 20.35  ? 538 HOH A O   1 
HETATM 2596 O O   . HOH B 2 .   ? 25.401 45.745 37.777 1.00 20.46  ? 539 HOH A O   1 
HETATM 2597 O O   . HOH B 2 .   ? 36.546 30.347 39.159 1.00 21.44  ? 540 HOH A O   1 
HETATM 2598 O O   . HOH B 2 .   ? 32.117 26.582 27.897 1.00 21.79  ? 541 HOH A O   1 
HETATM 2599 O O   . HOH B 2 .   ? 34.742 12.982 33.128 1.00 22.26  ? 542 HOH A O   1 
# 
_database_PDB_caveat.id     1 
_database_PDB_caveat.text   'CHIRALITY ERRORS AT SOME CA CENTERS.' 
# 
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   1   ?   ?   ?   A . n 
A 1 2   ALA 2   2   ?   ?   ?   A . n 
A 1 3   VAL 3   3   ?   ?   ?   A . n 
A 1 4   ASP 4   4   ?   ?   ?   A . n 
A 1 5   SER 5   5   ?   ?   ?   A . n 
A 1 6   SER 6   6   ?   ?   ?   A . n 
A 1 7   ASN 7   7   ?   ?   ?   A . n 
A 1 8   SER 8   8   ?   ?   ?   A . n 
A 1 9   ALA 9   9   ?   ?   ?   A . n 
A 1 10  THR 10  10  ?   ?   ?   A . n 
A 1 11  GLY 11  11  ?   ?   ?   A . n 
A 1 12  PRO 12  12  12  PRO PRO A . n 
A 1 13  MET 13  13  13  MET MET A . n 
A 1 14  ARG 14  14  14  ARG ARG A . n 
A 1 15  VAL 15  15  15  VAL VAL A . n 
A 1 16  PHE 16  16  16  PHE PHE A . n 
A 1 17  ALA 17  17  17  ALA ALA A . n 
A 1 18  ILE 18  18  18  ILE ILE A . n 
A 1 19  GLY 19  19  19  GLY GLY A . n 
A 1 20  ASN 20  20  20  ASN ASN A . n 
A 1 21  PRO 21  21  21  PRO PRO A . n 
A 1 22  ILE 22  22  22  ILE ILE A . n 
A 1 23  LEU 23  23  23  LEU LEU A . n 
A 1 24  ASP 24  24  24  ASP ASP A . n 
A 1 25  LEU 25  25  25  LEU LEU A . n 
A 1 26  VAL 26  26  26  VAL VAL A . n 
A 1 27  ALA 27  27  27  ALA ALA A . n 
A 1 28  GLU 28  28  28  GLU GLU A . n 
A 1 29  VAL 29  29  29  VAL VAL A . n 
A 1 30  PRO 30  30  30  PRO PRO A . n 
A 1 31  SER 31  31  31  SER SER A . n 
A 1 32  SER 32  32  32  SER SER A . n 
A 1 33  PHE 33  33  33  PHE PHE A . n 
A 1 34  LEU 34  34  34  LEU LEU A . n 
A 1 35  ASP 35  35  35  ASP ASP A . n 
A 1 36  GLU 36  36  36  GLU GLU A . n 
A 1 37  PHE 37  37  37  PHE PHE A . n 
A 1 38  PHE 38  38  38  PHE PHE A . n 
A 1 39  LEU 39  39  39  LEU LEU A . n 
A 1 40  LYS 40  40  40  LYS LYS A . n 
A 1 41  ARG 41  41  41  ARG ARG A . n 
A 1 42  GLY 42  42  42  GLY GLY A . n 
A 1 43  ASP 43  43  43  ASP ASP A . n 
A 1 44  ALA 44  44  44  ALA ALA A . n 
A 1 45  THR 45  45  45  THR THR A . n 
A 1 46  LEU 46  46  46  LEU LEU A . n 
A 1 47  ALA 47  47  47  ALA ALA A . n 
A 1 48  THR 48  48  48  THR THR A . n 
A 1 49  PRO 49  49  49  PRO PRO A . n 
A 1 50  GLU 50  50  50  GLU GLU A . n 
A 1 51  GLN 51  51  51  GLN GLN A . n 
A 1 52  MET 52  52  52  MET MET A . n 
A 1 53  ARG 53  53  53  ARG ARG A . n 
A 1 54  ILE 54  54  54  ILE ILE A . n 
A 1 55  TYR 55  55  55  TYR TYR A . n 
A 1 56  SER 56  56  56  SER SER A . n 
A 1 57  THR 57  57  57  THR THR A . n 
A 1 58  LEU 58  58  58  LEU LEU A . n 
A 1 59  ASP 59  59  59  ASP ASP A . n 
A 1 60  GLN 60  60  60  GLN GLN A . n 
A 1 61  PHE 61  61  61  PHE PHE A . n 
A 1 62  ASN 62  62  62  ASN ASN A . n 
A 1 63  PRO 63  63  63  PRO PRO A . n 
A 1 64  THR 64  64  64  THR THR A . n 
A 1 65  SER 65  65  65  SER SER A . n 
A 1 66  LEU 66  66  66  LEU LEU A . n 
A 1 67  PRO 67  67  67  PRO PRO A . n 
A 1 68  GLY 68  68  68  GLY GLY A . n 
A 1 69  GLY 69  69  69  GLY GLY A . n 
A 1 70  SER 70  70  70  SER SER A . n 
A 1 71  ALA 71  71  71  ALA ALA A . n 
A 1 72  LEU 72  72  72  LEU LEU A . n 
A 1 73  ASN 73  73  73  ASN ASN A . n 
A 1 74  SER 74  74  74  SER SER A . n 
A 1 75  VAL 75  75  75  VAL VAL A . n 
A 1 76  ARG 76  76  76  ARG ARG A . n 
A 1 77  VAL 77  77  77  VAL VAL A . n 
A 1 78  VAL 78  78  78  VAL VAL A . n 
A 1 79  GLN 79  79  79  GLN GLN A . n 
A 1 80  LYS 80  80  80  LYS LYS A . n 
A 1 81  LEU 81  81  81  LEU LEU A . n 
A 1 82  LEU 82  82  82  LEU LEU A . n 
A 1 83  ARG 83  83  83  ARG ARG A . n 
A 1 84  LYS 84  84  84  LYS LYS A . n 
A 1 85  PRO 85  85  85  PRO PRO A . n 
A 1 86  GLY 86  86  86  GLY GLY A . n 
A 1 87  SER 87  87  87  SER SER A . n 
A 1 88  ALA 88  88  88  ALA ALA A . n 
A 1 89  GLY 89  89  89  GLY GLY A . n 
A 1 90  TYR 90  90  90  TYR TYR A . n 
A 1 91  MET 91  91  91  MET MET A . n 
A 1 92  GLY 92  92  92  GLY GLY A . n 
A 1 93  ALA 93  93  93  ALA ALA A . n 
A 1 94  ILE 94  94  94  ILE ILE A . n 
A 1 95  GLY 95  95  95  GLY GLY A . n 
A 1 96  ASP 96  96  96  ASP ASP A . n 
A 1 97  ASP 97  97  97  ASP ASP A . n 
A 1 98  PRO 98  98  98  PRO PRO A . n 
A 1 99  ARG 99  99  99  ARG ARG A . n 
A 1 100 GLY 100 100 100 GLY GLY A . n 
A 1 101 GLN 101 101 101 GLN GLN A . n 
A 1 102 VAL 102 102 102 VAL VAL A . n 
A 1 103 LEU 103 103 103 LEU LEU A . n 
A 1 104 LYS 104 104 104 LYS LYS A . n 
A 1 105 GLU 105 105 105 GLU GLU A . n 
A 1 106 LEU 106 106 106 LEU LEU A . n 
A 1 107 CYS 107 107 107 CYS CYS A . n 
A 1 108 ASP 108 108 108 ASP ASP A . n 
A 1 109 LYS 109 109 109 LYS LYS A . n 
A 1 110 GLU 110 110 110 GLU GLU A . n 
A 1 111 GLY 111 111 111 GLY GLY A . n 
A 1 112 LEU 112 112 112 LEU LEU A . n 
A 1 113 ALA 113 113 113 ALA ALA A . n 
A 1 114 THR 114 114 114 THR THR A . n 
A 1 115 ARG 115 115 115 ARG ARG A . n 
A 1 116 PHE 116 116 116 PHE PHE A . n 
A 1 117 MET 117 117 117 MET MET A . n 
A 1 118 VAL 118 118 118 VAL VAL A . n 
A 1 119 ALA 119 119 119 ALA ALA A . n 
A 1 120 PRO 120 120 120 PRO PRO A . n 
A 1 121 GLY 121 121 121 GLY GLY A . n 
A 1 122 GLN 122 122 122 GLN GLN A . n 
A 1 123 SER 123 123 123 SER SER A . n 
A 1 124 THR 124 124 124 THR THR A . n 
A 1 125 GLY 125 125 125 GLY GLY A . n 
A 1 126 THR 126 126 126 THR THR A . n 
A 1 127 CYS 127 127 127 CYS CYS A . n 
A 1 128 ALA 128 128 128 ALA ALA A . n 
A 1 129 VAL 129 129 129 VAL VAL A . n 
A 1 130 LEU 130 130 130 LEU LEU A . n 
A 1 131 ILE 131 131 131 ILE ILE A . n 
A 1 132 ASN 132 132 132 ASN ASN A . n 
A 1 133 GLU 133 133 133 GLU GLU A . n 
A 1 134 LYS 134 134 134 LYS LYS A . n 
A 1 135 GLU 135 135 135 GLU GLU A . n 
A 1 136 ARG 136 136 136 ARG ARG A . n 
A 1 137 THR 137 137 137 THR THR A . n 
A 1 138 LEU 138 138 138 LEU LEU A . n 
A 1 139 CYS 139 139 139 CYS CYS A . n 
A 1 140 THR 140 140 140 THR THR A . n 
A 1 141 HIS 141 141 141 HIS HIS A . n 
A 1 142 LEU 142 142 142 LEU LEU A . n 
A 1 143 GLY 143 143 143 GLY GLY A . n 
A 1 144 ALA 144 144 144 ALA ALA A . n 
A 1 145 CYS 145 145 145 CYS CYS A . n 
A 1 146 GLY 146 146 146 GLY GLY A . n 
A 1 147 SER 147 147 147 SER SER A . n 
A 1 148 PHE 148 148 148 PHE PHE A . n 
A 1 149 ARG 149 149 149 ARG ARG A . n 
A 1 150 ILE 150 150 150 ILE ILE A . n 
A 1 151 PRO 151 151 151 PRO PRO A . n 
A 1 152 GLU 152 152 152 GLU GLU A . n 
A 1 153 ASP 153 153 153 ASP ASP A . n 
A 1 154 TRP 154 154 154 TRP TRP A . n 
A 1 155 THR 155 155 155 THR THR A . n 
A 1 156 THR 156 156 156 THR THR A . n 
A 1 157 PHE 157 157 157 PHE PHE A . n 
A 1 158 ALA 158 158 158 ALA ALA A . n 
A 1 159 SER 159 159 159 SER SER A . n 
A 1 160 GLY 160 160 160 GLY GLY A . n 
A 1 161 ALA 161 161 161 ALA ALA A . n 
A 1 162 LEU 162 162 162 LEU LEU A . n 
A 1 163 ILE 163 163 163 ILE ILE A . n 
A 1 164 PHE 164 164 164 PHE PHE A . n 
A 1 165 TYR 165 165 165 TYR TYR A . n 
A 1 166 ALA 166 166 166 ALA ALA A . n 
A 1 167 THR 167 167 167 THR THR A . n 
A 1 168 ALA 168 168 168 ALA ALA A . n 
A 1 169 TYR 169 169 169 TYR TYR A . n 
A 1 170 THR 170 170 170 THR THR A . n 
A 1 171 LEU 171 171 171 LEU LEU A . n 
A 1 172 THR 172 172 172 THR THR A . n 
A 1 173 ALA 173 173 173 ALA ALA A . n 
A 1 174 THR 174 174 174 THR THR A . n 
A 1 175 PRO 175 175 175 PRO PRO A . n 
A 1 176 LYS 176 176 176 LYS LYS A . n 
A 1 177 ASN 177 177 177 ASN ASN A . n 
A 1 178 ALA 178 178 178 ALA ALA A . n 
A 1 179 LEU 179 179 179 LEU LEU A . n 
A 1 180 GLU 180 180 180 GLU GLU A . n 
A 1 181 VAL 181 181 181 VAL VAL A . n 
A 1 182 ALA 182 182 182 ALA ALA A . n 
A 1 183 GLY 183 183 183 GLY GLY A . n 
A 1 184 TYR 184 184 184 TYR TYR A . n 
A 1 185 ALA 185 185 185 ALA ALA A . n 
A 1 186 HIS 186 186 186 HIS HIS A . n 
A 1 187 GLY 187 187 187 GLY GLY A . n 
A 1 188 ILE 188 188 188 ILE ILE A . n 
A 1 189 PRO 189 189 189 PRO PRO A . n 
A 1 190 ASN 190 190 190 ASN ASN A . n 
A 1 191 ALA 191 191 191 ALA ALA A . n 
A 1 192 ILE 192 192 192 ILE ILE A . n 
A 1 193 PHE 193 193 193 PHE PHE A . n 
A 1 194 THR 194 194 194 THR THR A . n 
A 1 195 LEU 195 195 195 LEU LEU A . n 
A 1 196 ASN 196 196 196 ASN ASN A . n 
A 1 197 LEU 197 197 197 LEU LEU A . n 
A 1 198 SER 198 198 198 SER SER A . n 
A 1 199 ALA 199 199 199 ALA ALA A . n 
A 1 200 PRO 200 200 200 PRO PRO A . n 
A 1 201 PHE 201 201 201 PHE PHE A . n 
A 1 202 CYS 202 202 202 CYS CYS A . n 
A 1 203 VAL 203 203 203 VAL VAL A . n 
A 1 204 GLU 204 204 204 GLU GLU A . n 
A 1 205 LEU 205 205 205 LEU LEU A . n 
A 1 206 TYR 206 206 206 TYR TYR A . n 
A 1 207 LYS 207 207 207 LYS LYS A . n 
A 1 208 ASP 208 208 208 ASP ASP A . n 
A 1 209 ALA 209 209 209 ALA ALA A . n 
A 1 210 MET 210 210 210 MET MET A . n 
A 1 211 GLN 211 211 211 GLN GLN A . n 
A 1 212 SER 212 212 212 SER SER A . n 
A 1 213 LEU 213 213 213 LEU LEU A . n 
A 1 214 LEU 214 214 214 LEU LEU A . n 
A 1 215 LEU 215 215 215 LEU LEU A . n 
A 1 216 HIS 216 216 216 HIS HIS A . n 
A 1 217 THR 217 217 217 THR THR A . n 
A 1 218 ASN 218 218 218 ASN ASN A . n 
A 1 219 ILE 219 219 219 ILE ILE A . n 
A 1 220 LEU 220 220 220 LEU LEU A . n 
A 1 221 PHE 221 221 221 PHE PHE A . n 
A 1 222 GLY 222 222 222 GLY GLY A . n 
A 1 223 ASN 223 223 223 ASN ASN A . n 
A 1 224 GLU 224 224 224 GLU GLU A . n 
A 1 225 GLU 225 225 225 GLU GLU A . n 
A 1 226 GLU 226 226 226 GLU GLU A . n 
A 1 227 PHE 227 227 227 PHE PHE A . n 
A 1 228 ALA 228 228 228 ALA ALA A . n 
A 1 229 HIS 229 229 229 HIS HIS A . n 
A 1 230 LEU 230 230 230 LEU LEU A . n 
A 1 231 ALA 231 231 231 ALA ALA A . n 
A 1 232 LYS 232 232 232 LYS LYS A . n 
A 1 233 VAL 233 233 233 VAL VAL A . n 
A 1 234 HIS 234 234 234 HIS HIS A . n 
A 1 235 ASN 235 235 235 ASN ASN A . n 
A 1 236 LEU 236 236 236 LEU LEU A . n 
A 1 237 VAL 237 237 237 VAL VAL A . n 
A 1 238 ALA 238 238 238 ALA ALA A . n 
A 1 239 ALA 239 239 ?   ?   ?   A . n 
A 1 240 ASP 240 240 240 ASP ALA A . n 
A 1 241 LYS 241 241 241 LYS ALA A . n 
A 1 242 THR 242 242 242 THR ALA A . n 
A 1 243 ALA 243 243 243 ALA ALA A . n 
A 1 244 LEU 244 244 244 LEU ALA A . n 
A 1 245 SER 245 245 245 SER ALA A . n 
A 1 246 THR 246 246 246 THR ALA A . n 
A 1 247 ALA 247 247 247 ALA ALA A . n 
A 1 248 ASN 248 248 248 ASN ALA A . n 
A 1 249 LYS 249 249 249 LYS ALA A . n 
A 1 250 GLU 250 250 250 GLU ALA A . n 
A 1 251 HIS 251 251 251 HIS ALA A . n 
A 1 252 ALA 252 252 252 ALA ALA A . n 
A 1 253 VAL 253 253 253 VAL ALA A . n 
A 1 254 GLU 254 254 254 GLU ALA A . n 
A 1 255 VAL 255 255 ?   ?   ?   A . n 
A 1 256 CYS 256 256 ?   ?   ?   A . n 
A 1 257 THR 257 257 ?   ?   ?   A . n 
A 1 258 GLY 258 258 ?   ?   ?   A . n 
A 1 259 ALA 259 259 ?   ?   ?   A . n 
A 1 260 LEU 260 260 ?   ?   ?   A . n 
A 1 261 ARG 261 261 ?   ?   ?   A . n 
A 1 262 LEU 262 262 ?   ?   ?   A . n 
A 1 263 LEU 263 263 ?   ?   ?   A . n 
A 1 264 THR 264 264 ?   ?   ?   A . n 
A 1 265 ALA 265 265 ?   ?   ?   A . n 
A 1 266 GLY 266 266 ?   ?   ?   A . n 
A 1 267 GLN 267 267 ?   ?   ?   A . n 
A 1 268 ASN 268 268 ?   ?   ?   A . n 
A 1 269 THR 269 269 ?   ?   ?   A . n 
A 1 270 GLY 270 270 270 GLY GLY A . n 
A 1 271 ALA 271 271 271 ALA ALA A . n 
A 1 272 THR 272 272 272 THR THR A . n 
A 1 273 LYS 273 273 273 LYS LYS A . n 
A 1 274 LEU 274 274 274 LEU LEU A . n 
A 1 275 VAL 275 275 275 VAL VAL A . n 
A 1 276 VAL 276 276 276 VAL VAL A . n 
A 1 277 MET 277 277 277 MET MET A . n 
A 1 278 THR 278 278 278 THR THR A . n 
A 1 279 ARG 279 279 279 ARG ARG A . n 
A 1 280 GLY 280 280 280 GLY GLY A . n 
A 1 281 HIS 281 281 281 HIS HIS A . n 
A 1 282 ASN 282 282 282 ASN ASN A . n 
A 1 283 PRO 283 283 283 PRO PRO A . n 
A 1 284 VAL 284 284 284 VAL VAL A . n 
A 1 285 ILE 285 285 285 ILE ILE A . n 
A 1 286 ALA 286 286 286 ALA ALA A . n 
A 1 287 ALA 287 287 287 ALA ALA A . n 
A 1 288 GLU 288 288 288 GLU GLU A . n 
A 1 289 GLN 289 289 289 GLN GLN A . n 
A 1 290 THR 290 290 290 THR THR A . n 
A 1 291 ALA 291 291 291 ALA ALA A . n 
A 1 292 ASP 292 292 292 ASP ASP A . n 
A 1 293 GLY 293 293 293 GLY GLY A . n 
A 1 294 THR 294 294 294 THR THR A . n 
A 1 295 VAL 295 295 295 VAL VAL A . n 
A 1 296 VAL 296 296 296 VAL VAL A . n 
A 1 297 VAL 297 297 297 VAL VAL A . n 
A 1 298 HIS 298 298 298 HIS HIS A . n 
A 1 299 GLU 299 299 299 GLU GLU A . n 
A 1 300 VAL 300 300 300 VAL VAL A . n 
A 1 301 GLY 301 301 301 GLY GLY A . n 
A 1 302 VAL 302 302 302 VAL VAL A . n 
A 1 303 PRO 303 303 303 PRO PRO A . n 
A 1 304 VAL 304 304 304 VAL VAL A . n 
A 1 305 VAL 305 305 305 VAL VAL A . n 
A 1 306 ALA 306 306 306 ALA ALA A . n 
A 1 307 ALA 307 307 307 ALA ALA A . n 
A 1 308 GLU 308 308 308 GLU GLU A . n 
A 1 309 LYS 309 309 309 LYS LYS A . n 
A 1 310 ILE 310 310 310 ILE ILE A . n 
A 1 311 VAL 311 311 311 VAL VAL A . n 
A 1 312 ASP 312 312 312 ASP ASP A . n 
A 1 313 THR 313 313 313 THR THR A . n 
A 1 314 ASN 314 314 314 ASN ASN A . n 
A 1 315 GLY 315 315 315 GLY GLY A . n 
A 1 316 ALA 316 316 316 ALA ALA A . n 
A 1 317 GLY 317 317 317 GLY GLY A . n 
A 1 318 ASP 318 318 318 ASP ASP A . n 
A 1 319 ALA 319 319 319 ALA ALA A . n 
A 1 320 PHE 320 320 320 PHE PHE A . n 
A 1 321 VAL 321 321 321 VAL VAL A . n 
A 1 322 GLY 322 322 322 GLY GLY A . n 
A 1 323 GLY 323 323 323 GLY GLY A . n 
A 1 324 PHE 324 324 324 PHE PHE A . n 
A 1 325 LEU 325 325 325 LEU LEU A . n 
A 1 326 TYR 326 326 326 TYR TYR A . n 
A 1 327 GLY 327 327 327 GLY GLY A . n 
A 1 328 LEU 328 328 328 LEU LEU A . n 
A 1 329 SER 329 329 329 SER SER A . n 
A 1 330 GLN 330 330 330 GLN GLN A . n 
A 1 331 GLY 331 331 331 GLY GLY A . n 
A 1 332 LYS 332 332 332 LYS LYS A . n 
A 1 333 THR 333 333 333 THR THR A . n 
A 1 334 VAL 334 334 334 VAL VAL A . n 
A 1 335 LYS 335 335 335 LYS LYS A . n 
A 1 336 GLN 336 336 336 GLN GLN A . n 
A 1 337 CYS 337 337 337 CYS CYS A . n 
A 1 338 ILE 338 338 338 ILE ILE A . n 
A 1 339 MET 339 339 339 MET MET A . n 
A 1 340 CYS 340 340 340 CYS CYS A . n 
A 1 341 GLY 341 341 341 GLY GLY A . n 
A 1 342 ASN 342 342 342 ASN ASN A . n 
A 1 343 ALA 343 343 343 ALA ALA A . n 
A 1 344 CYS 344 344 344 CYS CYS A . n 
A 1 345 ALA 345 345 345 ALA ALA A . n 
A 1 346 GLN 346 346 346 GLN GLN A . n 
A 1 347 ASP 347 347 347 ASP ASP A . n 
A 1 348 VAL 348 348 348 VAL VAL A . n 
A 1 349 ILE 349 349 349 ILE ILE A . n 
A 1 350 GLN 350 350 350 GLN GLN A . n 
A 1 351 HIS 351 351 351 HIS HIS A . n 
A 1 352 VAL 352 352 352 VAL VAL A . n 
A 1 353 GLY 353 353 353 GLY GLY A . n 
A 1 354 PHE 354 354 354 PHE PHE A . n 
A 1 355 SER 355 355 355 SER SER A . n 
A 1 356 LEU 356 356 356 LEU LEU A . n 
A 1 357 SER 357 357 ?   ?   ?   A . n 
A 1 358 PHE 358 358 ?   ?   ?   A . n 
A 1 359 THR 359 359 ?   ?   ?   A . n 
A 1 360 SER 360 360 ?   ?   ?   A . n 
A 1 361 LEU 361 361 ?   ?   ?   A . n 
A 1 362 PRO 362 362 ?   ?   ?   A . n 
A 1 363 CYS 363 363 ?   ?   ?   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 HOH 1   364 100 HOH HOH A . 
B 2 HOH 2   365 101 HOH HOH A . 
B 2 HOH 3   366 102 HOH HOH A . 
B 2 HOH 4   367 103 HOH HOH A . 
B 2 HOH 5   368 104 HOH HOH A . 
B 2 HOH 6   369 105 HOH HOH A . 
B 2 HOH 7   370 106 HOH HOH A . 
B 2 HOH 8   371 107 HOH HOH A . 
B 2 HOH 9   372 108 HOH HOH A . 
B 2 HOH 10  373 109 HOH HOH A . 
B 2 HOH 11  374 110 HOH HOH A . 
B 2 HOH 12  375 111 HOH HOH A . 
B 2 HOH 13  376 112 HOH HOH A . 
B 2 HOH 14  377 113 HOH HOH A . 
B 2 HOH 15  378 114 HOH HOH A . 
B 2 HOH 16  379 115 HOH HOH A . 
B 2 HOH 17  380 116 HOH HOH A . 
B 2 HOH 18  381 117 HOH HOH A . 
B 2 HOH 19  382 118 HOH HOH A . 
B 2 HOH 20  383 119 HOH HOH A . 
B 2 HOH 21  384 120 HOH HOH A . 
B 2 HOH 22  385 121 HOH HOH A . 
B 2 HOH 23  386 122 HOH HOH A . 
B 2 HOH 24  387 123 HOH HOH A . 
B 2 HOH 25  388 124 HOH HOH A . 
B 2 HOH 26  389 125 HOH HOH A . 
B 2 HOH 27  390 126 HOH HOH A . 
B 2 HOH 28  391 127 HOH HOH A . 
B 2 HOH 29  392 128 HOH HOH A . 
B 2 HOH 30  393 129 HOH HOH A . 
B 2 HOH 31  394 130 HOH HOH A . 
B 2 HOH 32  395 131 HOH HOH A . 
B 2 HOH 33  396 132 HOH HOH A . 
B 2 HOH 34  397 133 HOH HOH A . 
B 2 HOH 35  398 134 HOH HOH A . 
B 2 HOH 36  399 135 HOH HOH A . 
B 2 HOH 37  400 136 HOH HOH A . 
B 2 HOH 38  401 137 HOH HOH A . 
B 2 HOH 39  402 138 HOH HOH A . 
B 2 HOH 40  403 139 HOH HOH A . 
B 2 HOH 41  404 200 HOH HOH A . 
B 2 HOH 42  405 201 HOH HOH A . 
B 2 HOH 43  406 202 HOH HOH A . 
B 2 HOH 44  407 203 HOH HOH A . 
B 2 HOH 45  408 204 HOH HOH A . 
B 2 HOH 46  409 205 HOH HOH A . 
B 2 HOH 47  410 206 HOH HOH A . 
B 2 HOH 48  411 207 HOH HOH A . 
B 2 HOH 49  412 208 HOH HOH A . 
B 2 HOH 50  413 209 HOH HOH A . 
B 2 HOH 51  414 210 HOH HOH A . 
B 2 HOH 52  415 211 HOH HOH A . 
B 2 HOH 53  416 212 HOH HOH A . 
B 2 HOH 54  417 213 HOH HOH A . 
B 2 HOH 55  418 214 HOH HOH A . 
B 2 HOH 56  419 215 HOH HOH A . 
B 2 HOH 57  420 216 HOH HOH A . 
B 2 HOH 58  421 217 HOH HOH A . 
B 2 HOH 59  422 218 HOH HOH A . 
B 2 HOH 60  423 219 HOH HOH A . 
B 2 HOH 61  424 220 HOH HOH A . 
B 2 HOH 62  425 221 HOH HOH A . 
B 2 HOH 63  426 222 HOH HOH A . 
B 2 HOH 64  427 223 HOH HOH A . 
B 2 HOH 65  428 224 HOH HOH A . 
B 2 HOH 66  429 225 HOH HOH A . 
B 2 HOH 67  430 226 HOH HOH A . 
B 2 HOH 68  431 227 HOH HOH A . 
B 2 HOH 69  432 228 HOH HOH A . 
B 2 HOH 70  433 229 HOH HOH A . 
B 2 HOH 71  434 300 HOH HOH A . 
B 2 HOH 72  435 301 HOH HOH A . 
B 2 HOH 73  436 302 HOH HOH A . 
B 2 HOH 74  437 303 HOH HOH A . 
B 2 HOH 75  438 304 HOH HOH A . 
B 2 HOH 76  439 305 HOH HOH A . 
B 2 HOH 77  440 306 HOH HOH A . 
B 2 HOH 78  441 307 HOH HOH A . 
B 2 HOH 79  442 308 HOH HOH A . 
B 2 HOH 80  443 310 HOH HOH A . 
B 2 HOH 81  444 311 HOH HOH A . 
B 2 HOH 82  445 312 HOH HOH A . 
B 2 HOH 83  446 313 HOH HOH A . 
B 2 HOH 84  447 314 HOH HOH A . 
B 2 HOH 85  448 315 HOH HOH A . 
B 2 HOH 86  449 316 HOH HOH A . 
B 2 HOH 87  450 317 HOH HOH A . 
B 2 HOH 88  451 318 HOH HOH A . 
B 2 HOH 89  452 319 HOH HOH A . 
B 2 HOH 90  453 320 HOH HOH A . 
B 2 HOH 91  454 321 HOH HOH A . 
B 2 HOH 92  455 322 HOH HOH A . 
B 2 HOH 93  456 323 HOH HOH A . 
B 2 HOH 94  457 324 HOH HOH A . 
B 2 HOH 95  458 325 HOH HOH A . 
B 2 HOH 96  459 326 HOH HOH A . 
B 2 HOH 97  460 327 HOH HOH A . 
B 2 HOH 98  461 328 HOH HOH A . 
B 2 HOH 99  462 329 HOH HOH A . 
B 2 HOH 100 463 330 HOH HOH A . 
B 2 HOH 101 464 331 HOH HOH A . 
B 2 HOH 102 465 332 HOH HOH A . 
B 2 HOH 103 466 333 HOH HOH A . 
B 2 HOH 104 467 334 HOH HOH A . 
B 2 HOH 105 468 335 HOH HOH A . 
B 2 HOH 106 469 336 HOH HOH A . 
B 2 HOH 107 470 337 HOH HOH A . 
B 2 HOH 108 471 338 HOH HOH A . 
B 2 HOH 109 472 339 HOH HOH A . 
B 2 HOH 110 473 400 HOH HOH A . 
B 2 HOH 111 474 401 HOH HOH A . 
B 2 HOH 112 475 402 HOH HOH A . 
B 2 HOH 113 476 403 HOH HOH A . 
B 2 HOH 114 477 404 HOH HOH A . 
B 2 HOH 115 478 405 HOH HOH A . 
B 2 HOH 116 479 406 HOH HOH A . 
B 2 HOH 117 480 407 HOH HOH A . 
B 2 HOH 118 481 408 HOH HOH A . 
B 2 HOH 119 482 409 HOH HOH A . 
B 2 HOH 120 483 410 HOH HOH A . 
B 2 HOH 121 484 411 HOH HOH A . 
B 2 HOH 122 485 412 HOH HOH A . 
B 2 HOH 123 486 413 HOH HOH A . 
B 2 HOH 124 487 414 HOH HOH A . 
B 2 HOH 125 488 415 HOH HOH A . 
B 2 HOH 126 489 416 HOH HOH A . 
B 2 HOH 127 490 417 HOH HOH A . 
B 2 HOH 128 491 418 HOH HOH A . 
B 2 HOH 129 492 419 HOH HOH A . 
B 2 HOH 130 493 420 HOH HOH A . 
B 2 HOH 131 494 421 HOH HOH A . 
B 2 HOH 132 495 422 HOH HOH A . 
B 2 HOH 133 496 423 HOH HOH A . 
B 2 HOH 134 497 424 HOH HOH A . 
B 2 HOH 135 498 425 HOH HOH A . 
B 2 HOH 136 499 426 HOH HOH A . 
B 2 HOH 137 500 427 HOH HOH A . 
B 2 HOH 138 501 428 HOH HOH A . 
B 2 HOH 139 502 429 HOH HOH A . 
B 2 HOH 140 503 430 HOH HOH A . 
B 2 HOH 141 504 431 HOH HOH A . 
B 2 HOH 142 505 432 HOH HOH A . 
B 2 HOH 143 506 433 HOH HOH A . 
B 2 HOH 144 507 434 HOH HOH A . 
B 2 HOH 145 508 435 HOH HOH A . 
B 2 HOH 146 509 436 HOH HOH A . 
B 2 HOH 147 510 437 HOH HOH A . 
B 2 HOH 148 511 438 HOH HOH A . 
B 2 HOH 149 512 439 HOH HOH A . 
B 2 HOH 150 513 500 HOH HOH A . 
B 2 HOH 151 514 501 HOH HOH A . 
B 2 HOH 152 515 502 HOH HOH A . 
B 2 HOH 153 516 503 HOH HOH A . 
B 2 HOH 154 517 504 HOH HOH A . 
B 2 HOH 155 518 505 HOH HOH A . 
B 2 HOH 156 519 506 HOH HOH A . 
B 2 HOH 157 520 507 HOH HOH A . 
B 2 HOH 158 521 508 HOH HOH A . 
B 2 HOH 159 522 509 HOH HOH A . 
B 2 HOH 160 523 510 HOH HOH A . 
B 2 HOH 161 524 511 HOH HOH A . 
B 2 HOH 162 525 512 HOH HOH A . 
B 2 HOH 163 526 513 HOH HOH A . 
B 2 HOH 164 527 514 HOH HOH A . 
B 2 HOH 165 528 565 HOH HOH A . 
B 2 HOH 166 529 517 HOH HOH A . 
B 2 HOH 167 530 518 HOH HOH A . 
B 2 HOH 168 531 519 HOH HOH A . 
B 2 HOH 169 532 520 HOH HOH A . 
B 2 HOH 170 533 521 HOH HOH A . 
B 2 HOH 171 534 522 HOH HOH A . 
B 2 HOH 172 535 523 HOH HOH A . 
B 2 HOH 173 536 524 HOH HOH A . 
B 2 HOH 174 537 525 HOH HOH A . 
B 2 HOH 175 538 526 HOH HOH A . 
B 2 HOH 176 539 527 HOH HOH A . 
B 2 HOH 177 540 528 HOH HOH A . 
B 2 HOH 178 541 529 HOH HOH A . 
B 2 HOH 179 542 530 HOH HOH A . 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B 
# 
_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_
_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 2002-06-12 
2 'Structure model' 1 1 2008-04-28 
3 'Structure model' 1 2 2011-07-13 
4 'Structure model' 1 3 2017-10-11 
# 
_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         ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Version format compliance' 
2 3 'Structure model' 'Version format compliance' 
3 4 'Structure model' 'Refinement description'    
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    4 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            software 
# 
_pdbx_audit_revision_item.ordinal             1 
_pdbx_audit_revision_item.revision_ordinal    4 
_pdbx_audit_revision_item.data_content_type   'Structure model' 
_pdbx_audit_revision_item.item                '_software.name' 
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
MERLOT phasing          . ? 1 
TNT    refinement       . ? 2 
bioteX 'data reduction' . ? 3 
bioteX 'data scaling'   . ? 4 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 O   A HOH 522 ? ? O   A HOH 536 ? ? 0.55 
2  1 CB  A LEU 197 ? ? O   A HOH 541 ? ? 1.56 
3  1 OG1 A THR 290 ? ? O   A THR 294 ? ? 1.60 
4  1 CB  A VAL 284 ? ? O   A HOH 517 ? ? 1.61 
5  1 O   A ASP 240 ? ? O   A HOH 514 ? ? 1.75 
6  1 NZ  A LYS 232 ? ? O   A HOH 529 ? ? 1.78 
7  1 CD2 A LEU 171 ? ? O   A HOH 521 ? ? 1.78 
8  1 O   A HOH 377 ? ? O   A HOH 441 ? ? 1.84 
9  1 O   A LEU 197 ? ? O   A HOH 541 ? ? 1.91 
10 1 C   A LEU 197 ? ? O   A HOH 541 ? ? 1.94 
11 1 CG2 A THR 155 ? ? CE1 A TYR 184 ? ? 1.97 
12 1 CA  A LEU 197 ? ? O   A HOH 541 ? ? 1.99 
13 1 NH1 A ARG 279 ? ? O   A PRO 283 ? ? 2.01 
14 1 O   A ILE 22  ? ? O   A GLY 68  ? ? 2.04 
15 1 CB  A LEU 244 ? ? O   A HOH 514 ? ? 2.09 
16 1 N   A VAL 284 ? ? O   A HOH 517 ? ? 2.12 
17 1 CG2 A VAL 284 ? ? O   A HOH 517 ? ? 2.15 
18 1 N   A ALA 286 ? ? O   A HIS 298 ? ? 2.17 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 OE1 A GLU 152 ? ? 1_555 O A HOH 534 ? ? 1_655 0.85 
2 1 CD  A GLU 152 ? ? 1_555 O A HOH 534 ? ? 1_655 1.06 
3 1 CG  A GLU 152 ? ? 1_555 O A HOH 534 ? ? 1_655 1.93 
4 1 OE2 A GLU 152 ? ? 1_555 O A HOH 534 ? ? 1_655 2.16 
# 
loop_
_pdbx_validate_rmsd_bond.id 
_pdbx_validate_rmsd_bond.PDB_model_num 
_pdbx_validate_rmsd_bond.auth_atom_id_1 
_pdbx_validate_rmsd_bond.auth_asym_id_1 
_pdbx_validate_rmsd_bond.auth_comp_id_1 
_pdbx_validate_rmsd_bond.auth_seq_id_1 
_pdbx_validate_rmsd_bond.PDB_ins_code_1 
_pdbx_validate_rmsd_bond.label_alt_id_1 
_pdbx_validate_rmsd_bond.auth_atom_id_2 
_pdbx_validate_rmsd_bond.auth_asym_id_2 
_pdbx_validate_rmsd_bond.auth_comp_id_2 
_pdbx_validate_rmsd_bond.auth_seq_id_2 
_pdbx_validate_rmsd_bond.PDB_ins_code_2 
_pdbx_validate_rmsd_bond.label_alt_id_2 
_pdbx_validate_rmsd_bond.bond_value 
_pdbx_validate_rmsd_bond.bond_target_value 
_pdbx_validate_rmsd_bond.bond_deviation 
_pdbx_validate_rmsd_bond.bond_standard_deviation 
_pdbx_validate_rmsd_bond.linker_flag 
1 1 CB A PHE 61  ? ? CG A PHE 61  ? ? 1.399 1.509 -0.110 0.017 N 
2 1 CA A SER 87  ? ? CB A SER 87  ? ? 1.619 1.525 0.094  0.015 N 
3 1 CG A GLU 105 ? ? CD A GLU 105 ? ? 1.641 1.515 0.126  0.015 N 
4 1 CB A TYR 184 ? ? CG A TYR 184 ? ? 1.626 1.512 0.114  0.015 N 
5 1 CG A GLU 224 ? ? CD A GLU 224 ? ? 1.634 1.515 0.119  0.015 N 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1  1 N   A PHE 38  ? ? CA A PHE 38  ? ? CB  A PHE 38  ? ? 123.79 110.60 13.19  1.80 N 
2  1 CA  A LYS 40  ? ? C  A LYS 40  ? ? N   A ARG 41  ? ? 103.94 117.20 -13.26 2.20 Y 
3  1 O   A LYS 40  ? ? C  A LYS 40  ? ? N   A ARG 41  ? ? 134.98 122.70 12.28  1.60 Y 
4  1 NE  A ARG 41  ? ? CZ A ARG 41  ? ? NH2 A ARG 41  ? ? 124.29 120.30 3.99   0.50 N 
5  1 NE  A ARG 53  ? ? CZ A ARG 53  ? ? NH1 A ARG 53  ? ? 117.15 120.30 -3.15  0.50 N 
6  1 CB  A PHE 61  ? ? CA A PHE 61  ? ? C   A PHE 61  ? ? 97.18  110.40 -13.22 2.00 N 
7  1 N   A THR 64  ? ? CA A THR 64  ? ? CB  A THR 64  ? ? 123.70 110.30 13.40  1.90 N 
8  1 CA  A LEU 72  ? ? CB A LEU 72  ? ? CG  A LEU 72  ? ? 97.36  115.30 -17.94 2.30 N 
9  1 NE  A ARG 83  ? ? CZ A ARG 83  ? ? NH2 A ARG 83  ? ? 123.32 120.30 3.02   0.50 N 
10 1 CB  A LYS 84  ? ? CA A LYS 84  ? ? C   A LYS 84  ? ? 122.48 110.40 12.08  2.00 N 
11 1 C   A LYS 84  ? ? N  A PRO 85  ? ? CD  A PRO 85  ? ? 106.43 128.40 -21.97 2.10 Y 
12 1 CB  A ASP 97  ? ? CA A ASP 97  ? ? C   A ASP 97  ? ? 122.49 110.40 12.09  2.00 N 
13 1 CB  A LEU 103 ? ? CA A LEU 103 ? ? C   A LEU 103 ? ? 124.72 110.20 14.52  1.90 N 
14 1 N   A LEU 103 ? ? CA A LEU 103 ? ? CB  A LEU 103 ? ? 124.44 110.40 14.04  2.00 N 
15 1 CB  A LYS 104 ? ? CA A LYS 104 ? ? C   A LYS 104 ? ? 123.02 110.40 12.62  2.00 N 
16 1 NE  A ARG 115 ? ? CZ A ARG 115 ? ? NH2 A ARG 115 ? ? 124.12 120.30 3.82   0.50 N 
17 1 N   A THR 124 ? ? CA A THR 124 ? ? CB  A THR 124 ? ? 124.80 110.30 14.50  1.90 N 
18 1 CG1 A VAL 129 ? ? CB A VAL 129 ? ? CG2 A VAL 129 ? ? 122.25 110.90 11.35  1.60 N 
19 1 CB  A ARG 136 ? ? CA A ARG 136 ? ? C   A ARG 136 ? ? 97.84  110.40 -12.56 2.00 N 
20 1 NE  A ARG 136 ? ? CZ A ARG 136 ? ? NH1 A ARG 136 ? ? 116.06 120.30 -4.24  0.50 N 
21 1 NE  A ARG 149 ? ? CZ A ARG 149 ? ? NH2 A ARG 149 ? ? 123.77 120.30 3.47   0.50 N 
22 1 CB  A LEU 179 ? ? CA A LEU 179 ? ? C   A LEU 179 ? ? 122.97 110.20 12.77  1.90 N 
23 1 N   A GLU 180 ? ? CA A GLU 180 ? ? CB  A GLU 180 ? ? 96.38  110.60 -14.22 1.80 N 
24 1 CB  A TYR 184 ? ? CG A TYR 184 ? ? CD2 A TYR 184 ? ? 124.79 121.00 3.79   0.60 N 
25 1 CB  A HIS 186 ? ? CA A HIS 186 ? ? C   A HIS 186 ? ? 124.49 110.40 14.09  2.00 N 
26 1 CG1 A ILE 188 ? ? CB A ILE 188 ? ? CG2 A ILE 188 ? ? 128.77 111.40 17.37  2.20 N 
27 1 N   A PHE 193 ? ? CA A PHE 193 ? ? CB  A PHE 193 ? ? 124.31 110.60 13.71  1.80 N 
28 1 N   A THR 194 ? ? CA A THR 194 ? ? CB  A THR 194 ? ? 96.87  110.30 -13.43 1.90 N 
29 1 C   A ALA 199 ? ? N  A PRO 200 ? ? CD  A PRO 200 ? ? 113.60 128.40 -14.80 2.10 Y 
30 1 CB  A LEU 214 ? ? CG A LEU 214 ? ? CD1 A LEU 214 ? ? 121.32 111.00 10.32  1.70 N 
31 1 CB  A HIS 234 ? ? CA A HIS 234 ? ? C   A HIS 234 ? ? 122.55 110.40 12.15  2.00 N 
32 1 CB  A LEU 236 ? ? CA A LEU 236 ? ? C   A LEU 236 ? ? 98.37  110.20 -11.83 1.90 N 
33 1 N   A LEU 236 ? ? CA A LEU 236 ? ? CB  A LEU 236 ? ? 97.49  110.40 -12.91 2.00 N 
34 1 CA  A LEU 236 ? ? CB A LEU 236 ? ? CG  A LEU 236 ? ? 132.82 115.30 17.52  2.30 N 
35 1 N   A VAL 237 ? ? CA A VAL 237 ? ? CB  A VAL 237 ? ? 124.78 111.50 13.28  2.20 N 
36 1 CB  A ASP 240 ? ? CA A ASP 240 ? ? C   A ASP 240 ? ? 122.73 110.40 12.33  2.00 N 
37 1 N   A LYS 241 ? ? CA A LYS 241 ? ? CB  A LYS 241 ? ? 97.78  110.60 -12.82 1.80 N 
38 1 CB  A HIS 251 ? ? CA A HIS 251 ? ? C   A HIS 251 ? ? 128.94 110.40 18.54  2.00 N 
39 1 CG  A MET 277 ? ? SD A MET 277 ? ? CE  A MET 277 ? ? 110.17 100.20 9.97   1.60 N 
40 1 NE  A ARG 279 ? ? CZ A ARG 279 ? ? NH2 A ARG 279 ? ? 124.31 120.30 4.01   0.50 N 
41 1 CA  A GLN 289 ? ? C  A GLN 289 ? ? N   A THR 290 ? ? 102.54 117.20 -14.66 2.20 Y 
42 1 O   A GLN 289 ? ? C  A GLN 289 ? ? N   A THR 290 ? ? 136.72 122.70 14.02  1.60 Y 
43 1 N   A THR 290 ? ? CA A THR 290 ? ? CB  A THR 290 ? ? 98.22  110.30 -12.08 1.90 N 
44 1 C   A VAL 302 ? ? N  A PRO 303 ? ? CD  A PRO 303 ? ? 115.57 128.40 -12.83 2.10 Y 
45 1 CB  A TYR 326 ? ? CA A TYR 326 ? ? C   A TYR 326 ? ? 90.28  110.40 -20.12 2.00 N 
46 1 CA  A LEU 328 ? ? CB A LEU 328 ? ? CG  A LEU 328 ? ? 99.03  115.30 -16.27 2.30 N 
47 1 CB  A LEU 328 ? ? CG A LEU 328 ? ? CD2 A LEU 328 ? ? 121.32 111.00 10.32  1.70 N 
48 1 N   A THR 333 ? ? CA A THR 333 ? ? CB  A THR 333 ? ? 125.14 110.30 14.84  1.90 N 
49 1 CA  A MET 339 ? ? CB A MET 339 ? ? CG  A MET 339 ? ? 124.55 113.30 11.25  1.70 N 
50 1 CB  A VAL 348 ? ? CA A VAL 348 ? ? C   A VAL 348 ? ? 123.87 111.40 12.47  1.90 N 
51 1 CA  A LEU 356 ? ? CB A LEU 356 ? ? CG  A LEU 356 ? ? 100.79 115.30 -14.51 2.30 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 ARG A 14  ? ? -155.81 15.12   
2  1 ALA A 27  ? ? -142.17 -118.68 
3  1 GLU A 28  ? ? 153.60  102.62  
4  1 PHE A 38  ? ? 16.72   79.19   
5  1 THR A 48  ? ? -113.38 -164.98 
6  1 THR A 57  ? ? -48.57  -77.36  
7  1 LEU A 58  ? ? -59.06  3.21    
8  1 PHE A 61  ? ? -24.54  -108.77 
9  1 ASN A 62  ? ? -161.74 44.78   
10 1 SER A 70  ? ? -141.04 -59.88  
11 1 ARG A 76  ? ? -20.99  -65.12  
12 1 VAL A 77  ? ? -38.30  -74.49  
13 1 LEU A 82  ? ? -83.31  -81.62  
14 1 ARG A 83  ? ? 126.20  -23.39  
15 1 SER A 123 ? ? 73.26   177.22  
16 1 THR A 124 ? ? -101.31 -166.43 
17 1 THR A 126 ? ? -129.32 -157.78 
18 1 VAL A 129 ? ? -108.58 61.04   
19 1 LEU A 130 ? ? -49.64  157.05  
20 1 ILE A 131 ? ? -137.12 -144.37 
21 1 ASN A 132 ? ? -166.56 -143.79 
22 1 LYS A 134 ? ? 179.25  -48.27  
23 1 SER A 147 ? ? -179.17 55.07   
24 1 SER A 159 ? ? -40.91  98.46   
25 1 ALA A 166 ? ? 174.35  147.26  
26 1 THR A 170 ? ? -39.44  -39.65  
27 1 THR A 172 ? ? -31.08  -35.23  
28 1 ALA A 173 ? ? -85.14  -78.77  
29 1 PRO A 175 ? ? -61.41  19.75   
30 1 ASN A 177 ? ? -44.21  -73.53  
31 1 ILE A 188 ? ? 167.57  175.66  
32 1 ASN A 190 ? ? 136.84  29.62   
33 1 ALA A 191 ? ? -62.68  -162.53 
34 1 LEU A 197 ? ? -29.61  -24.49  
35 1 SER A 198 ? ? 55.57   -127.40 
36 1 LEU A 205 ? ? -93.88  30.65   
37 1 TYR A 206 ? ? -141.31 -45.89  
38 1 LYS A 207 ? ? 32.85   -118.82 
39 1 ASP A 208 ? ? -17.41  -25.74  
40 1 HIS A 216 ? ? -84.35  40.09   
41 1 GLU A 225 ? ? -25.90  -69.16  
42 1 ASN A 235 ? ? -39.46  105.15  
43 1 LEU A 236 ? ? 172.57  -157.41 
44 1 LYS A 241 ? ? -75.11  -75.49  
45 1 ALA A 243 ? ? -49.57  -81.34  
46 1 GLU A 250 ? ? -37.94  -4.60   
47 1 ALA A 252 ? ? 8.88    -129.99 
48 1 VAL A 253 ? ? -161.50 -141.37 
49 1 THR A 272 ? ? -116.59 -103.28 
50 1 VAL A 275 ? ? -167.85 96.22   
51 1 ARG A 279 ? ? -97.82  51.58   
52 1 ASN A 282 ? ? -43.47  159.37  
53 1 ALA A 286 ? ? -135.64 -146.10 
54 1 ALA A 287 ? ? 172.87  129.90  
55 1 ASP A 292 ? ? -68.83  5.15    
56 1 VAL A 302 ? ? -174.53 85.92   
57 1 PRO A 303 ? ? -62.12  87.43   
58 1 ALA A 307 ? ? -110.16 -144.92 
59 1 GLU A 308 ? ? -42.81  -14.98  
60 1 LYS A 309 ? ? -72.08  38.30   
61 1 ILE A 310 ? ? -120.87 -144.44 
62 1 VAL A 311 ? ? 61.80   97.76   
63 1 ASP A 312 ? ? 161.71  46.16   
64 1 ASN A 314 ? ? -84.81  -83.62  
65 1 TYR A 326 ? ? -92.44  -60.44  
66 1 LYS A 332 ? ? 65.26   164.17  
67 1 THR A 333 ? ? 153.35  115.59  
68 1 VAL A 334 ? ? -25.14  -80.67  
69 1 GLN A 350 ? ? -69.80  -76.54  
70 1 VAL A 352 ? ? -35.80  177.07  
# 
loop_
_pdbx_validate_chiral.id 
_pdbx_validate_chiral.PDB_model_num 
_pdbx_validate_chiral.auth_atom_id 
_pdbx_validate_chiral.label_alt_id 
_pdbx_validate_chiral.auth_asym_id 
_pdbx_validate_chiral.auth_comp_id 
_pdbx_validate_chiral.auth_seq_id 
_pdbx_validate_chiral.PDB_ins_code 
_pdbx_validate_chiral.details 
_pdbx_validate_chiral.omega 
1 1 CA ? A LEU 103 ? PLANAR       . 
2 1 CA ? A THR 124 ? 'WRONG HAND' . 
3 1 CA ? A LEU 179 ? 'WRONG HAND' . 
4 1 CA ? A ILE 188 ? 'WRONG HAND' . 
5 1 CA ? A GLU 308 ? 'WRONG HAND' . 
6 1 CA ? A VAL 334 ? 'WRONG HAND' . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A ASP 240 ? CG  ? A ASP 240 CG  
2  1 Y 1 A ASP 240 ? OD1 ? A ASP 240 OD1 
3  1 Y 1 A ASP 240 ? OD2 ? A ASP 240 OD2 
4  1 Y 1 A LYS 241 ? CG  ? A LYS 241 CG  
5  1 Y 1 A LYS 241 ? CD  ? A LYS 241 CD  
6  1 Y 1 A LYS 241 ? CE  ? A LYS 241 CE  
7  1 Y 1 A LYS 241 ? NZ  ? A LYS 241 NZ  
8  1 Y 1 A THR 242 ? OG1 ? A THR 242 OG1 
9  1 Y 1 A THR 242 ? CG2 ? A THR 242 CG2 
10 1 Y 1 A LEU 244 ? CG  ? A LEU 244 CG  
11 1 Y 1 A LEU 244 ? CD1 ? A LEU 244 CD1 
12 1 Y 1 A LEU 244 ? CD2 ? A LEU 244 CD2 
13 1 Y 1 A SER 245 ? OG  ? A SER 245 OG  
14 1 Y 1 A THR 246 ? OG1 ? A THR 246 OG1 
15 1 Y 1 A THR 246 ? CG2 ? A THR 246 CG2 
16 1 Y 1 A ASN 248 ? CG  ? A ASN 248 CG  
17 1 Y 1 A ASN 248 ? OD1 ? A ASN 248 OD1 
18 1 Y 1 A ASN 248 ? ND2 ? A ASN 248 ND2 
19 1 Y 1 A LYS 249 ? CG  ? A LYS 249 CG  
20 1 Y 1 A LYS 249 ? CD  ? A LYS 249 CD  
21 1 Y 1 A LYS 249 ? CE  ? A LYS 249 CE  
22 1 Y 1 A LYS 249 ? NZ  ? A LYS 249 NZ  
23 1 Y 1 A GLU 250 ? CG  ? A GLU 250 CG  
24 1 Y 1 A GLU 250 ? CD  ? A GLU 250 CD  
25 1 Y 1 A GLU 250 ? OE1 ? A GLU 250 OE1 
26 1 Y 1 A GLU 250 ? OE2 ? A GLU 250 OE2 
27 1 Y 1 A HIS 251 ? CG  ? A HIS 251 CG  
28 1 Y 1 A HIS 251 ? ND1 ? A HIS 251 ND1 
29 1 Y 1 A HIS 251 ? CD2 ? A HIS 251 CD2 
30 1 Y 1 A HIS 251 ? CE1 ? A HIS 251 CE1 
31 1 Y 1 A HIS 251 ? NE2 ? A HIS 251 NE2 
32 1 Y 1 A VAL 253 ? CG1 ? A VAL 253 CG1 
33 1 Y 1 A VAL 253 ? CG2 ? A VAL 253 CG2 
34 1 Y 1 A GLU 254 ? CG  ? A GLU 254 CG  
35 1 Y 1 A GLU 254 ? CD  ? A GLU 254 CD  
36 1 Y 1 A GLU 254 ? OE1 ? A GLU 254 OE1 
37 1 Y 1 A GLU 254 ? OE2 ? A GLU 254 OE2 
# 
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 1   ? A MET 1   
2  1 Y 1 A ALA 2   ? A ALA 2   
3  1 Y 1 A VAL 3   ? A VAL 3   
4  1 Y 1 A ASP 4   ? A ASP 4   
5  1 Y 1 A SER 5   ? A SER 5   
6  1 Y 1 A SER 6   ? A SER 6   
7  1 Y 1 A ASN 7   ? A ASN 7   
8  1 Y 1 A SER 8   ? A SER 8   
9  1 Y 1 A ALA 9   ? A ALA 9   
10 1 Y 1 A THR 10  ? A THR 10  
11 1 Y 1 A GLY 11  ? A GLY 11  
12 1 Y 1 A ALA 239 ? A ALA 239 
13 1 Y 1 A VAL 255 ? A VAL 255 
14 1 Y 1 A CYS 256 ? A CYS 256 
15 1 Y 1 A THR 257 ? A THR 257 
16 1 Y 1 A GLY 258 ? A GLY 258 
17 1 Y 1 A ALA 259 ? A ALA 259 
18 1 Y 1 A LEU 260 ? A LEU 260 
19 1 Y 1 A ARG 261 ? A ARG 261 
20 1 Y 1 A LEU 262 ? A LEU 262 
21 1 Y 1 A LEU 263 ? A LEU 263 
22 1 Y 1 A THR 264 ? A THR 264 
23 1 Y 1 A ALA 265 ? A ALA 265 
24 1 Y 1 A GLY 266 ? A GLY 266 
25 1 Y 1 A GLN 267 ? A GLN 267 
26 1 Y 1 A ASN 268 ? A ASN 268 
27 1 Y 1 A THR 269 ? A THR 269 
28 1 Y 1 A SER 357 ? A SER 357 
29 1 Y 1 A PHE 358 ? A PHE 358 
30 1 Y 1 A THR 359 ? A THR 359 
31 1 Y 1 A SER 360 ? A SER 360 
32 1 Y 1 A LEU 361 ? A LEU 361 
33 1 Y 1 A PRO 362 ? A PRO 362 
34 1 Y 1 A CYS 363 ? A CYS 363 
# 
_pdbx_entity_nonpoly.entity_id   2 
_pdbx_entity_nonpoly.name        water 
_pdbx_entity_nonpoly.comp_id     HOH 
# 


A second structure was input as follows:


data_1LII
# 
_entry.id   1LII 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.281 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   1LII         
RCSB  RCSB015968   
WWPDB D_1000015968 
# 
_pdbx_database_PDB_obs_spr.id               SPRSDE 
_pdbx_database_PDB_obs_spr.pdb_id           1LII 
_pdbx_database_PDB_obs_spr.replace_pdb_id   1DGY 
_pdbx_database_PDB_obs_spr.date             2002-05-15 
_pdbx_database_PDB_obs_spr.details          ? 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.details 
_pdbx_database_related.content_type 
PDB 1LIJ 'STRUCTURE OF T. GONDII ADENOSINE KINASE BOUND TO PRODRUG 2 7-IODOTUBERCIDIN AND AMP-PCP' unspecified 
PDB 1LIK 'STRUCTURE OF T. GONDII ADENOSINE KINASE BOUND TO ADENOSINE'                              unspecified 
PDB 1LIO 'STRUCTURE OF APO T. GONDII ADENOSINE KINASE'                                             unspecified 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        1LII 
_pdbx_database_status.recvd_initial_deposition_date   2002-04-17 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        . 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_cs                  ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Schumacher, M.A.' 1 
'Scott, D.M.'      2 
'Mathews, I.I.'    3 
'Ealick, S.E.'     4 
'Roos, D.S.'       5 
'Ullman, B.'       6 
'Brennan, R.G.'    7 
# 
_citation.id                        primary 
_citation.title                     
'Crystal structures of Toxoplasma gondii adenosine kinase reveal a novel catalytic mechanism and prodrug binding.' 
_citation.journal_abbrev            J.Mol.Biol. 
_citation.journal_volume            298 
_citation.page_first                875 
_citation.page_last                 893 
_citation.year                      2000 
_citation.journal_id_ASTM           JMOBAK 
_citation.country                   UK 
_citation.journal_id_ISSN           0022-2836 
_citation.journal_id_CSD            0070 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   10801355 
_citation.pdbx_database_id_DOI      10.1006/jmbi.2000.3753 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Schumacher, M.A.' 1 
primary 'Scott, D.M.'      2 
primary 'Mathews, I.I.'    3 
primary 'Ealick, S.E.'     4 
primary 'Roos, D.S.'       5 
primary 'Ullman, B.'       6 
primary 'Brennan, R.G.'    7 
# 
_cell.entry_id           1LII 
_cell.length_a           167.800 
_cell.length_b           47.100 
_cell.length_c           44.450 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        90.00 
_cell.Z_PDB              4 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         1LII 
_symmetry.space_group_name_H-M             'P 21 21 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                18 
# 
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 'adenosine kinase'                             38373.824 1   2.7.1.20 ? ? ? 
2 non-polymer syn 'MAGNESIUM ION'                                24.305    1   ?        ? ? ? 
3 non-polymer syn 'CHLORIDE ION'                                 35.453    1   ?        ? ? ? 
4 non-polymer syn ADENOSINE                                      267.241   1   ?        ? ? ? 
5 non-polymer syn 'PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER' 505.208   1   ?        ? ? ? 
6 water       nat water                                          18.015    170 ?        ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
;AK, Adenosine 5'-phosphotransferase
;
# 
_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       
;MAVDSSNSATGPMRVFAIGNPILDLVAEVPSSFLDEFFLKRGDATLATPEQMRIYSTLDQFNPTSLPGGSALNSVRVVQK
LLRKPGSAGYMGAIGDDPRGQVLKELCDKEGLATRFMVAPGQSTGTCAVLINEKERTLCTHLGACGSFRIPENWTTFASG
ALIFYATAYTLTATPKNALEVAGYAHGIPNAIFTLNLSAPFCVELYKDAMQSLLLHTNILFGNEEEFAHLAKVHNLVAAE
KVALSVANKEHAVEVCTGALRLLTAGQNTGATKLVVMTRGHNPVIAAEQTADGTVVVHEVGVPVVAAEKIVDTNGAGDAF
VGGFLYGLSQGKTVKQCIMCGNACAQDVIQHVGFSLSFTSLPC
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MAVDSSNSATGPMRVFAIGNPILDLVAEVPSSFLDEFFLKRGDATLATPEQMRIYSTLDQFNPTSLPGGSALNSVRVVQK
LLRKPGSAGYMGAIGDDPRGQVLKELCDKEGLATRFMVAPGQSTGTCAVLINEKERTLCTHLGACGSFRIPENWTTFASG
ALIFYATAYTLTATPKNALEVAGYAHGIPNAIFTLNLSAPFCVELYKDAMQSLLLHTNILFGNEEEFAHLAKVHNLVAAE
KVALSVANKEHAVEVCTGALRLLTAGQNTGATKLVVMTRGHNPVIAAEQTADGTVVVHEVGVPVVAAEKIVDTNGAGDAF
VGGFLYGLSQGKTVKQCIMCGNACAQDVIQHVGFSLSFTSLPC
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
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   ALA n 
1 3   VAL n 
1 4   ASP n 
1 5   SER n 
1 6   SER n 
1 7   ASN n 
1 8   SER n 
1 9   ALA n 
1 10  THR n 
1 11  GLY n 
1 12  PRO n 
1 13  MET n 
1 14  ARG n 
1 15  VAL n 
1 16  PHE n 
1 17  ALA n 
1 18  ILE n 
1 19  GLY n 
1 20  ASN n 
1 21  PRO n 
1 22  ILE n 
1 23  LEU n 
1 24  ASP n 
1 25  LEU n 
1 26  VAL n 
1 27  ALA n 
1 28  GLU n 
1 29  VAL n 
1 30  PRO n 
1 31  SER n 
1 32  SER n 
1 33  PHE n 
1 34  LEU n 
1 35  ASP n 
1 36  GLU n 
1 37  PHE n 
1 38  PHE n 
1 39  LEU n 
1 40  LYS n 
1 41  ARG n 
1 42  GLY n 
1 43  ASP n 
1 44  ALA n 
1 45  THR n 
1 46  LEU n 
1 47  ALA n 
1 48  THR n 
1 49  PRO n 
1 50  GLU n 
1 51  GLN n 
1 52  MET n 
1 53  ARG n 
1 54  ILE n 
1 55  TYR n 
1 56  SER n 
1 57  THR n 
1 58  LEU n 
1 59  ASP n 
1 60  GLN n 
1 61  PHE n 
1 62  ASN n 
1 63  PRO n 
1 64  THR n 
1 65  SER n 
1 66  LEU n 
1 67  PRO n 
1 68  GLY n 
1 69  GLY n 
1 70  SER n 
1 71  ALA n 
1 72  LEU n 
1 73  ASN n 
1 74  SER n 
1 75  VAL n 
1 76  ARG n 
1 77  VAL n 
1 78  VAL n 
1 79  GLN n 
1 80  LYS n 
1 81  LEU n 
1 82  LEU n 
1 83  ARG n 
1 84  LYS n 
1 85  PRO n 
1 86  GLY n 
1 87  SER n 
1 88  ALA n 
1 89  GLY n 
1 90  TYR n 
1 91  MET n 
1 92  GLY n 
1 93  ALA n 
1 94  ILE n 
1 95  GLY n 
1 96  ASP n 
1 97  ASP n 
1 98  PRO n 
1 99  ARG n 
1 100 GLY n 
1 101 GLN n 
1 102 VAL n 
1 103 LEU n 
1 104 LYS n 
1 105 GLU n 
1 106 LEU n 
1 107 CYS n 
1 108 ASP n 
1 109 LYS n 
1 110 GLU n 
1 111 GLY n 
1 112 LEU n 
1 113 ALA n 
1 114 THR n 
1 115 ARG n 
1 116 PHE n 
1 117 MET n 
1 118 VAL n 
1 119 ALA n 
1 120 PRO n 
1 121 GLY n 
1 122 GLN n 
1 123 SER n 
1 124 THR n 
1 125 GLY n 
1 126 THR n 
1 127 CYS n 
1 128 ALA n 
1 129 VAL n 
1 130 LEU n 
1 131 ILE n 
1 132 ASN n 
1 133 GLU n 
1 134 LYS n 
1 135 GLU n 
1 136 ARG n 
1 137 THR n 
1 138 LEU n 
1 139 CYS n 
1 140 THR n 
1 141 HIS n 
1 142 LEU n 
1 143 GLY n 
1 144 ALA n 
1 145 CYS n 
1 146 GLY n 
1 147 SER n 
1 148 PHE n 
1 149 ARG n 
1 150 ILE n 
1 151 PRO n 
1 152 GLU n 
1 153 ASN n 
1 154 TRP n 
1 155 THR n 
1 156 THR n 
1 157 PHE n 
1 158 ALA n 
1 159 SER n 
1 160 GLY n 
1 161 ALA n 
1 162 LEU n 
1 163 ILE n 
1 164 PHE n 
1 165 TYR n 
1 166 ALA n 
1 167 THR n 
1 168 ALA n 
1 169 TYR n 
1 170 THR n 
1 171 LEU n 
1 172 THR n 
1 173 ALA n 
1 174 THR n 
1 175 PRO n 
1 176 LYS n 
1 177 ASN n 
1 178 ALA n 
1 179 LEU n 
1 180 GLU n 
1 181 VAL n 
1 182 ALA n 
1 183 GLY n 
1 184 TYR n 
1 185 ALA n 
1 186 HIS n 
1 187 GLY n 
1 188 ILE n 
1 189 PRO n 
1 190 ASN n 
1 191 ALA n 
1 192 ILE n 
1 193 PHE n 
1 194 THR n 
1 195 LEU n 
1 196 ASN n 
1 197 LEU n 
1 198 SER n 
1 199 ALA n 
1 200 PRO n 
1 201 PHE n 
1 202 CYS n 
1 203 VAL n 
1 204 GLU n 
1 205 LEU n 
1 206 TYR n 
1 207 LYS n 
1 208 ASP n 
1 209 ALA n 
1 210 MET n 
1 211 GLN n 
1 212 SER n 
1 213 LEU n 
1 214 LEU n 
1 215 LEU n 
1 216 HIS n 
1 217 THR n 
1 218 ASN n 
1 219 ILE n 
1 220 LEU n 
1 221 PHE n 
1 222 GLY n 
1 223 ASN n 
1 224 GLU n 
1 225 GLU n 
1 226 GLU n 
1 227 PHE n 
1 228 ALA n 
1 229 HIS n 
1 230 LEU n 
1 231 ALA n 
1 232 LYS n 
1 233 VAL n 
1 234 HIS n 
1 235 ASN n 
1 236 LEU n 
1 237 VAL n 
1 238 ALA n 
1 239 ALA n 
1 240 GLU n 
1 241 LYS n 
1 242 VAL n 
1 243 ALA n 
1 244 LEU n 
1 245 SER n 
1 246 VAL n 
1 247 ALA n 
1 248 ASN n 
1 249 LYS n 
1 250 GLU n 
1 251 HIS n 
1 252 ALA n 
1 253 VAL n 
1 254 GLU n 
1 255 VAL n 
1 256 CYS n 
1 257 THR n 
1 258 GLY n 
1 259 ALA n 
1 260 LEU n 
1 261 ARG n 
1 262 LEU n 
1 263 LEU n 
1 264 THR n 
1 265 ALA n 
1 266 GLY n 
1 267 GLN n 
1 268 ASN n 
1 269 THR n 
1 270 GLY n 
1 271 ALA n 
1 272 THR n 
1 273 LYS n 
1 274 LEU n 
1 275 VAL n 
1 276 VAL n 
1 277 MET n 
1 278 THR n 
1 279 ARG n 
1 280 GLY n 
1 281 HIS n 
1 282 ASN n 
1 283 PRO n 
1 284 VAL n 
1 285 ILE n 
1 286 ALA n 
1 287 ALA n 
1 288 GLU n 
1 289 GLN n 
1 290 THR n 
1 291 ALA n 
1 292 ASP n 
1 293 GLY n 
1 294 THR n 
1 295 VAL n 
1 296 VAL n 
1 297 VAL n 
1 298 HIS n 
1 299 GLU n 
1 300 VAL n 
1 301 GLY n 
1 302 VAL n 
1 303 PRO n 
1 304 VAL n 
1 305 VAL n 
1 306 ALA n 
1 307 ALA n 
1 308 GLU n 
1 309 LYS n 
1 310 ILE n 
1 311 VAL n 
1 312 ASP n 
1 313 THR n 
1 314 ASN n 
1 315 GLY n 
1 316 ALA n 
1 317 GLY n 
1 318 ASP n 
1 319 ALA n 
1 320 PHE n 
1 321 VAL n 
1 322 GLY n 
1 323 GLY n 
1 324 PHE n 
1 325 LEU n 
1 326 TYR n 
1 327 GLY n 
1 328 LEU n 
1 329 SER n 
1 330 GLN n 
1 331 GLY n 
1 332 LYS n 
1 333 THR n 
1 334 VAL n 
1 335 LYS n 
1 336 GLN n 
1 337 CYS n 
1 338 ILE n 
1 339 MET n 
1 340 CYS n 
1 341 GLY n 
1 342 ASN n 
1 343 ALA n 
1 344 CYS n 
1 345 ALA n 
1 346 GLN n 
1 347 ASP n 
1 348 VAL n 
1 349 ILE n 
1 350 GLN n 
1 351 HIS n 
1 352 VAL n 
1 353 GLY n 
1 354 PHE n 
1 355 SER n 
1 356 LEU n 
1 357 SER n 
1 358 PHE n 
1 359 THR n 
1 360 SER n 
1 361 LEU n 
1 362 PRO n 
1 363 CYS 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                      ? 
_entity_src_gen.pdbx_beg_seq_num                   ? 
_entity_src_gen.pdbx_end_seq_num                   ? 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     Toxoplasma 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_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      'Toxoplasma gondii' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     5811 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     Escherichia 
_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          PLASMID 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       PBACE 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    ADK_TOXGO 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MAVDSSNSATGPMRVFAIGNPILDLVAEVPSSFLDEFFLKRGDATLATPEQMRIYSTLDQFNPTSLPGGSALNSVRVVQK
LLRKPGSAGYMGAIGDDPRGQVLKELCDKEGLATRFMVAPGQSTGVCAVLINEKERTLCTHLGACGSFRLPEDWTTFASG
ALIFYATAYTLTATPKNALEVAGYAHGIPNAIFTLNLSAPFCVELYKDAMQSLLLHTNILFGNEEEFAHLAKVHNLVAAE
KTALSTANKEHAVEVCTGALRLLTAGQNTGATKLVVMTRGHNPVIAAEQTADGTVVVHEVGVPVVAAEKIVDTNGAGDAF
VGGFLYALSQGKTVKQCIMCGNACAQDVIQHVGFSLSFTSLPC
;
_struct_ref.pdbx_align_begin           1 
_struct_ref.pdbx_db_accession          Q9TVW2 
_struct_ref.pdbx_db_isoform            ? 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              1LII 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 363 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q9TVW2 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  363 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       363 
# 
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 1LII THR A 126 ? UNP Q9TVW2 VAL 126 CONFLICT 126 1 
1 1LII ILE A 150 ? UNP Q9TVW2 LEU 150 CONFLICT 150 2 
1 1LII ASN A 153 ? UNP Q9TVW2 ASP 153 CONFLICT 153 3 
1 1LII VAL A 242 ? UNP Q9TVW2 THR 242 CONFLICT 242 4 
1 1LII VAL A 246 ? UNP Q9TVW2 THR 246 CONFLICT 246 5 
1 1LII GLY A 327 ? UNP Q9TVW2 ALA 327 CONFLICT 327 6 
# 
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 
ACP non-polymer         . 'PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER' 
;ADENOSINE-5'-[BETA, GAMMA-METHYLENE]TRIPHOSPHATE
;
'C11 H18 N5 O12 P3' 505.208 
ADN non-polymer         . ADENOSINE                                      ?                                                  
'C10 H13 N5 O4'     267.241 
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 
CL  non-polymer         . 'CHLORIDE ION'                                 ?                                                  
'Cl -1'             35.453  
CYS 'L-peptide linking' y CYSTEINE                                       ?                                                  
'C3 H7 N O2 S'      121.158 
GLN 'L-peptide linking' y GLUTAMINE                                      ?                                                  
'C5 H10 N2 O3'      146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                ?                                                  
'C5 H9 N O4'        147.129 
GLY 'peptide linking'   y GLYCINE                                        ?                                                  
'C2 H5 N O2'        75.067  
HIS 'L-peptide linking' y HISTIDINE                                      ?                                                  
'C6 H10 N3 O2 1'    156.162 
HOH non-polymer         . WATER                                          ?                                                  'H2 O' 
18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                     ?                                                  
'C6 H13 N O2'       131.173 
LEU 'L-peptide linking' y LEUCINE                                        ?                                                  
'C6 H13 N O2'       131.173 
LYS 'L-peptide linking' y LYSINE                                         ?                                                  
'C6 H15 N2 O2 1'    147.195 
MET 'L-peptide linking' y METHIONINE                                     ?                                                  
'C5 H11 N O2 S'     149.211 
MG  non-polymer         . 'MAGNESIUM ION'                                ?                                                  'Mg 2' 
24.305  
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 
# 
_exptl.entry_id          1LII 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.29 
_exptl_crystal.density_percent_sol   46.23 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.temp            298 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              6.50 
_exptl_crystal_grow.pdbx_details    'ammonium sulphate, pH 6.50, VAPOR DIFFUSION, HANGING DROP, temperature 298K' 
_exptl_crystal_grow.pdbx_pH_range   . 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           298.0 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               'IMAGE PLATE' 
_diffrn_detector.type                   MARRESEARCH 
_diffrn_detector.pdbx_collection_date   1998-10-01 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    graphite 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.08 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'SRS BEAMLINE PX7.2' 
_diffrn_source.pdbx_synchrotron_site       SRS 
_diffrn_source.pdbx_synchrotron_beamline   PX7.2 
_diffrn_source.pdbx_wavelength             1.08 
_diffrn_source.pdbx_wavelength_list        ? 
# 
_reflns.entry_id                     1LII 
_reflns.observed_criterion_sigma_I   1.000 
_reflns.observed_criterion_sigma_F   0 
_reflns.d_resolution_low             10.000 
_reflns.d_resolution_high            1.720 
_reflns.number_obs                   38408 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         98.0 
_reflns.pdbx_Rmerge_I_obs            0.0590000 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        8.3000 
_reflns.B_iso_Wilson_estimate        15.000 
_reflns.pdbx_redundancy              4.000 
_reflns.R_free_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.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
# 
_reflns_shell.d_res_high             1.72 
_reflns_shell.d_res_low              1.76 
_reflns_shell.percent_possible_all   98.0 
_reflns_shell.Rmerge_I_obs           0.2420000 
_reflns_shell.pdbx_Rsym_value        ? 
_reflns_shell.meanI_over_sigI_obs    ? 
_reflns_shell.pdbx_redundancy        3.00 
_reflns_shell.percent_possible_obs   ? 
_reflns_shell.number_unique_all      ? 
_reflns_shell.pdbx_diffrn_id         ? 
_reflns_shell.pdbx_ordinal           1 
# 
_refine.entry_id                                 1LII 
_refine.ls_number_reflns_obs                     34526 
_refine.ls_number_reflns_all                     35500 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.000 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_d_res_low                             10.0 
_refine.ls_d_res_high                            1.73 
_refine.ls_percent_reflns_obs                    99.0 
_refine.ls_R_factor_obs                          0.1890000 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.1890000 
_refine.ls_R_factor_R_free                       0.2250000 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 10.000 
_refine.ls_number_reflns_R_free                  3400 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.B_iso_mean                               ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_ls_cross_valid_method               ? 
_refine.details                                  ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       'ENGH & HUBER' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_B                             ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.B_iso_min                                ? 
_refine.B_iso_max                                ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_SU_ML                            ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        2437 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         52 
_refine_hist.number_atoms_solvent             170 
_refine_hist.number_atoms_total               2659 
_refine_hist.d_res_high                       1.73 
_refine_hist.d_res_low                        10.0 
# 
_struct.entry_id                  1LII 
_struct.title                     'STRUCTURE OF T. GONDII ADENOSINE KINASE BOUND TO ADENOSINE 2 AND AMP-PCP' 
_struct.pdbx_descriptor           'ADENOSINE KINASE (E.C.2.7.1.20)' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        1LII 
_struct_keywords.pdbx_keywords   TRANSFERASE 
_struct_keywords.text            'ALPHA-BETA STRUCTURE, TRANSFERASE' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
F N N 6 ? 
# 
_struct_biol.id                    1 
_struct_biol.pdbx_parent_biol_id   ? 
_struct_biol.details               ? 
# 
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  1  PRO A 30  ? PHE A 37  ? PRO A 30  PHE A 37  1 ? 8  
HELX_P HELX_P2  2  THR A 48  ? MET A 52  ? THR A 48  MET A 52  5 ? 5  
HELX_P HELX_P3  3  ARG A 53  ? LEU A 58  ? ARG A 53  LEU A 58  1 ? 6  
HELX_P HELX_P4  4  ASP A 59  ? ASN A 62  ? ASP A 59  ASN A 62  5 ? 4  
HELX_P HELX_P5  5  GLY A 69  ? ARG A 83  ? GLY A 69  ARG A 83  1 ? 15 
HELX_P HELX_P6  6  ASP A 97  ? GLY A 111 ? ASP A 97  GLY A 111 1 ? 15 
HELX_P HELX_P7  7  LEU A 142 ? PHE A 148 ? LEU A 142 PHE A 148 5 ? 7  
HELX_P HELX_P8  8  ASN A 153 ? ALA A 158 ? ASN A 153 ALA A 158 1 ? 6  
HELX_P HELX_P9  9  TYR A 169 ? ALA A 173 ? TYR A 169 ALA A 173 5 ? 5  
HELX_P HELX_P10 10 PRO A 175 ? GLY A 187 ? PRO A 175 GLY A 187 1 ? 13 
HELX_P HELX_P11 11 ALA A 199 ? TYR A 206 ? ALA A 199 TYR A 206 1 ? 8  
HELX_P HELX_P12 12 TYR A 206 ? HIS A 216 ? TYR A 206 HIS A 216 1 ? 11 
HELX_P HELX_P13 13 GLU A 224 ? HIS A 234 ? GLU A 224 HIS A 234 1 ? 11 
HELX_P HELX_P14 14 LYS A 241 ? GLU A 254 ? LYS A 241 GLU A 254 1 ? 14 
HELX_P HELX_P15 15 ALA A 306 ? ILE A 310 ? ALA A 306 ILE A 310 5 ? 5  
HELX_P HELX_P16 16 GLY A 315 ? GLN A 330 ? GLY A 315 GLN A 330 1 ? 16 
HELX_P HELX_P17 17 THR A 333 ? ILE A 349 ? THR A 333 ILE A 349 1 ? 17 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
metalc1 metalc ? ? B MG . MG ? ? ? 1_555 E ACP . O1B ? ? A MG 999 A ACP 799  1_555 ? ? ? ? ? ? ? 2.292 ? 
metalc2 metalc ? ? B MG . MG ? ? ? 1_555 F HOH . O   ? ? A MG 999 A HOH 1118 1_555 ? ? ? ? ? ? ? 2.248 ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A ? 9 ? 
B ? 5 ? 
# 
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 
A 1 2 ? parallel      
A 2 3 ? parallel      
A 3 4 ? parallel      
A 4 5 ? parallel      
A 5 6 ? parallel      
A 6 7 ? parallel      
A 7 8 ? anti-parallel 
A 8 9 ? anti-parallel 
B 1 2 ? parallel      
B 2 3 ? anti-parallel 
B 3 4 ? parallel      
B 4 5 ? 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 
A 1 ALA A 113 ? ALA A 119 ? ALA A 113 ALA A 119 
A 2 ALA A 88  ? GLY A 95  ? ALA A 88  GLY A 95  
A 3 VAL A 15  ? ILE A 18  ? VAL A 15  ILE A 18  
A 4 ILE A 163 ? THR A 167 ? ILE A 163 THR A 167 
A 5 ILE A 192 ? ASN A 196 ? ILE A 192 ASN A 196 
A 6 ILE A 219 ? ASN A 223 ? ILE A 219 ASN A 223 
A 7 LEU A 274 ? ARG A 279 ? LEU A 274 ARG A 279 
A 8 ASN A 282 ? GLN A 289 ? ASN A 282 GLN A 289 
A 9 VAL A 295 ? VAL A 300 ? VAL A 295 VAL A 300 
B 1 ALA A 44  ? LEU A 46  ? ALA A 44  LEU A 46  
B 2 GLU A 135 ? HIS A 141 ? GLU A 135 HIS A 141 
B 3 GLY A 125 ? ASN A 132 ? GLY A 125 ASN A 132 
B 4 ILE A 22  ? GLU A 28  ? ILE A 22  GLU A 28  
B 5 THR A 64  ? GLY A 68  ? THR A 64  GLY A 68  
# 
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 
A 1 2 O ALA A 119 ? O ALA A 119 N ILE A 94  ? N ILE A 94  
A 2 3 O GLY A 89  ? O GLY A 89  N VAL A 15  ? N VAL A 15  
A 3 4 N PHE A 16  ? N PHE A 16  O TYR A 165 ? O TYR A 165 
A 4 5 N PHE A 164 ? N PHE A 164 O THR A 194 ? O THR A 194 
A 5 6 N LEU A 195 ? N LEU A 195 O PHE A 221 ? O PHE A 221 
A 6 7 N LEU A 220 ? N LEU A 220 O VAL A 276 ? O VAL A 276 
A 7 8 N MET A 277 ? N MET A 277 O ILE A 285 ? O ILE A 285 
A 8 9 N ALA A 286 ? N ALA A 286 O HIS A 298 ? O HIS A 298 
B 1 2 N THR A 45  ? N THR A 45  O THR A 140 ? O THR A 140 
B 2 3 O CYS A 139 ? O CYS A 139 N ALA A 128 ? N ALA A 128 
B 3 4 O VAL A 129 ? O VAL A 129 N LEU A 25  ? N LEU A 25  
B 4 5 N ASP A 24  ? N ASP A 24  O LEU A 66  ? O LEU A 66  
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software ? ? ? ? 2  'BINDING SITE FOR RESIDUE MG A 999'  
AC2 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE CL A 899'  
AC3 Software ? ? ? ? 16 'BINDING SITE FOR RESIDUE ADN A 699' 
AC4 Software ? ? ? ? 27 'BINDING SITE FOR RESIDUE ACP A 799' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1  AC1 2  ACP E .   ? ACP A 799  . ? 1_555 ? 
2  AC1 2  HOH F .   ? HOH A 1118 . ? 1_555 ? 
3  AC2 5  GLY A 19  ? GLY A 19   . ? 1_555 ? 
4  AC2 5  ASN A 20  ? ASN A 20   . ? 1_555 ? 
5  AC2 5  ALA A 71  ? ALA A 71   . ? 1_555 ? 
6  AC2 5  THR A 167 ? THR A 167  . ? 1_555 ? 
7  AC2 5  ADN D .   ? ADN A 699  . ? 1_555 ? 
8  AC3 16 ASN A 20  ? ASN A 20   . ? 1_555 ? 
9  AC3 16 ILE A 22  ? ILE A 22   . ? 1_555 ? 
10 AC3 16 ASP A 24  ? ASP A 24   . ? 1_555 ? 
11 AC3 16 GLY A 68  ? GLY A 68   . ? 1_555 ? 
12 AC3 16 GLY A 69  ? GLY A 69   . ? 1_555 ? 
13 AC3 16 SER A 70  ? SER A 70   . ? 1_555 ? 
14 AC3 16 ASN A 73  ? ASN A 73   . ? 1_555 ? 
15 AC3 16 THR A 140 ? THR A 140  . ? 1_555 ? 
16 AC3 16 TYR A 169 ? TYR A 169  . ? 1_555 ? 
17 AC3 16 ASN A 314 ? ASN A 314  . ? 1_555 ? 
18 AC3 16 ASP A 318 ? ASP A 318  . ? 1_555 ? 
19 AC3 16 ACP E .   ? ACP A 799  . ? 1_555 ? 
20 AC3 16 CL  C .   ? CL  A 899  . ? 1_555 ? 
21 AC3 16 HOH F .   ? HOH A 1038 . ? 1_555 ? 
22 AC3 16 HOH F .   ? HOH A 1092 . ? 1_555 ? 
23 AC3 16 HOH F .   ? HOH A 1093 . ? 1_555 ? 
24 AC4 27 ARG A 136 ? ARG A 136  . ? 1_555 ? 
25 AC4 27 ASN A 223 ? ASN A 223  . ? 1_555 ? 
26 AC4 27 THR A 278 ? THR A 278  . ? 1_555 ? 
27 AC4 27 GLY A 280 ? GLY A 280  . ? 1_555 ? 
28 AC4 27 HIS A 281 ? HIS A 281  . ? 1_555 ? 
29 AC4 27 VAL A 284 ? VAL A 284  . ? 1_555 ? 
30 AC4 27 VAL A 302 ? VAL A 302  . ? 1_555 ? 
31 AC4 27 THR A 313 ? THR A 313  . ? 1_555 ? 
32 AC4 27 ASN A 314 ? ASN A 314  . ? 1_555 ? 
33 AC4 27 GLY A 315 ? GLY A 315  . ? 1_555 ? 
34 AC4 27 ALA A 316 ? ALA A 316  . ? 1_555 ? 
35 AC4 27 GLY A 317 ? GLY A 317  . ? 1_555 ? 
36 AC4 27 ASP A 318 ? ASP A 318  . ? 1_555 ? 
37 AC4 27 ASN A 342 ? ASN A 342  . ? 1_555 ? 
38 AC4 27 ALA A 345 ? ALA A 345  . ? 1_555 ? 
39 AC4 27 GLN A 346 ? GLN A 346  . ? 1_555 ? 
40 AC4 27 ADN D .   ? ADN A 699  . ? 1_555 ? 
41 AC4 27 MG  B .   ? MG  A 999  . ? 1_555 ? 
42 AC4 27 HOH F .   ? HOH A 1045 . ? 1_555 ? 
43 AC4 27 HOH F .   ? HOH A 1058 . ? 1_555 ? 
44 AC4 27 HOH F .   ? HOH A 1112 . ? 1_555 ? 
45 AC4 27 HOH F .   ? HOH A 1118 . ? 1_555 ? 
46 AC4 27 HOH F .   ? HOH A 1132 . ? 1_555 ? 
47 AC4 27 HOH F .   ? HOH A 1143 . ? 1_555 ? 
48 AC4 27 HOH F .   ? HOH A 1159 . ? 1_555 ? 
49 AC4 27 HOH F .   ? HOH A 1164 . ? 1_555 ? 
50 AC4 27 HOH F .   ? HOH A 1167 . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          1LII 
_database_PDB_matrix.origx[1][1]       1.000000 
_database_PDB_matrix.origx[1][2]       0.000000 
_database_PDB_matrix.origx[1][3]       0.000000 
_database_PDB_matrix.origx[2][1]       0.000000 
_database_PDB_matrix.origx[2][2]       1.000000 
_database_PDB_matrix.origx[2][3]       0.000000 
_database_PDB_matrix.origx[3][1]       0.000000 
_database_PDB_matrix.origx[3][2]       0.000000 
_database_PDB_matrix.origx[3][3]       1.000000 
_database_PDB_matrix.origx_vector[1]   0.00000 
_database_PDB_matrix.origx_vector[2]   0.00000 
_database_PDB_matrix.origx_vector[3]   0.00000 
# 
_atom_sites.entry_id                    1LII 
_atom_sites.fract_transf_matrix[1][1]   0.005959 
_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]   0.021231 
_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]   0.022497 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
CL 
MG 
N  
O  
P  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N     . GLY A 1 11  ? 146.253 32.840 19.243  1.00 99.34  ? 11   GLY A N     1 
ATOM   2    C  CA    . GLY A 1 11  ? 144.983 33.585 19.224  1.00 96.36  ? 11   GLY A CA    1 
ATOM   3    C  C     . GLY A 1 11  ? 143.862 32.807 18.534  1.00 90.06  ? 11   GLY A C     1 
ATOM   4    O  O     . GLY A 1 11  ? 144.143 31.884 17.755  1.00 92.81  ? 11   GLY A O     1 
ATOM   5    N  N     . PRO A 1 12  ? 142.617 33.179 18.829  1.00 71.21  ? 12   PRO A N     1 
ATOM   6    C  CA    . PRO A 1 12  ? 141.482 32.509 18.240  1.00 60.10  ? 12   PRO A CA    1 
ATOM   7    C  C     . PRO A 1 12  ? 141.637 32.359 16.743  1.00 36.66  ? 12   PRO A C     1 
ATOM   8    O  O     . PRO A 1 12  ? 141.939 31.269 16.284  1.00 35.29  ? 12   PRO A O     1 
ATOM   9    C  CB    . PRO A 1 12  ? 140.614 33.663 18.047  1.00 61.40  ? 12   PRO A CB    1 
ATOM   10   C  CG    . PRO A 1 12  ? 141.025 34.831 18.799  1.00 67.58  ? 12   PRO A CG    1 
ATOM   11   C  CD    . PRO A 1 12  ? 142.486 34.667 18.794  1.00 66.20  ? 12   PRO A CD    1 
ATOM   12   N  N     . MET A 1 13  ? 141.433 33.447 15.994  1.00 23.36  ? 13   MET A N     1 
ATOM   13   C  CA    . MET A 1 13  ? 141.553 33.367 14.544  1.00 18.62  ? 13   MET A CA    1 
ATOM   14   C  C     . MET A 1 13  ? 143.016 33.274 14.142  1.00 26.95  ? 13   MET A C     1 
ATOM   15   O  O     . MET A 1 13  ? 143.805 34.192 14.381  1.00 35.88  ? 13   MET A O     1 
ATOM   16   C  CB    . MET A 1 13  ? 140.844 34.437 13.740  1.00 17.04  ? 13   MET A CB    1 
ATOM   17   C  CG    . MET A 1 13  ? 140.598 33.892 12.311  1.00 18.28  ? 13   MET A CG    1 
ATOM   18   S  SD    . MET A 1 13  ? 139.797 35.197 11.303  1.00 21.27  ? 13   MET A SD    1 
ATOM   19   C  CE    . MET A 1 13  ? 138.164 35.259 11.988  1.00 22.30  ? 13   MET A CE    1 
ATOM   20   N  N     . ARG A 1 14  ? 143.360 32.149 13.532  1.00 21.89  ? 14   ARG A N     1 
ATOM   21   C  CA    . ARG A 1 14  ? 144.714 31.903 13.091  1.00 15.87  ? 14   ARG A CA    1 
ATOM   22   C  C     . ARG A 1 14  ? 144.906 32.168 11.603  1.00 17.01  ? 14   ARG A C     1 
ATOM   23   O  O     . ARG A 1 14  ? 145.930 32.660 11.189  1.00 17.91  ? 14   ARG A O     1 
ATOM   24   C  CB    . ARG A 1 14  ? 145.046 30.485 13.572  1.00 18.25  ? 14   ARG A CB    1 
ATOM   25   C  CG    . ARG A 1 14  ? 145.445 30.584 15.092  1.00 36.09  ? 14   ARG A CG    1 
ATOM   26   C  CD    . ARG A 1 14  ? 144.774 29.691 16.112  1.00 80.52  ? 14   ARG A CD    1 
ATOM   27   N  NE    . ARG A 1 14  ? 145.765 29.121 17.033  1.00 94.22  ? 14   ARG A NE    1 
ATOM   28   C  CZ    . ARG A 1 14  ? 145.568 28.069 17.844  1.00 100.00 ? 14   ARG A CZ    1 
ATOM   29   N  NH1   . ARG A 1 14  ? 144.401 27.399 17.922  1.00 66.33  ? 14   ARG A NH1   1 
ATOM   30   N  NH2   . ARG A 1 14  ? 146.571 27.669 18.611  1.00 81.80  ? 14   ARG A NH2   1 
ATOM   31   N  N     . VAL A 1 15  ? 143.929 31.838 10.782  1.00 15.87  ? 15   VAL A N     1 
ATOM   32   C  CA    . VAL A 1 15  ? 144.070 32.066 9.353   1.00 13.46  ? 15   VAL A CA    1 
ATOM   33   C  C     . VAL A 1 15  ? 142.812 32.743 8.823   1.00 17.39  ? 15   VAL A C     1 
ATOM   34   O  O     . VAL A 1 15  ? 141.712 32.339 9.188   1.00 18.02  ? 15   VAL A O     1 
ATOM   35   C  CB    . VAL A 1 15  ? 144.095 30.646 8.660   1.00 19.74  ? 15   VAL A CB    1 
ATOM   36   C  CG1   . VAL A 1 15  ? 144.121 30.755 7.143   1.00 22.48  ? 15   VAL A CG1   1 
ATOM   37   C  CG2   . VAL A 1 15  ? 145.323 29.823 9.061   1.00 18.49  ? 15   VAL A CG2   1 
ATOM   38   N  N     . PHE A 1 16  ? 142.982 33.758 7.993   1.00 11.66  ? 16   PHE A N     1 
ATOM   39   C  CA    . PHE A 1 16  ? 141.851 34.484 7.399   1.00 12.72  ? 16   PHE A CA    1 
ATOM   40   C  C     . PHE A 1 16  ? 141.969 34.406 5.880   1.00 17.00  ? 16   PHE A C     1 
ATOM   41   O  O     . PHE A 1 16  ? 143.063 34.624 5.330   1.00 18.16  ? 16   PHE A O     1 
ATOM   42   C  CB    . PHE A 1 16  ? 141.886 35.965 7.745   1.00 11.39  ? 16   PHE A CB    1 
ATOM   43   C  CG    . PHE A 1 16  ? 140.862 36.743 6.985   1.00 13.87  ? 16   PHE A CG    1 
ATOM   44   C  CD1   . PHE A 1 16  ? 139.543 36.660 7.350   1.00 18.16  ? 16   PHE A CD1   1 
ATOM   45   C  CD2   . PHE A 1 16  ? 141.227 37.495 5.892   1.00 17.77  ? 16   PHE A CD2   1 
ATOM   46   C  CE1   . PHE A 1 16  ? 138.575 37.367 6.628   1.00 19.90  ? 16   PHE A CE1   1 
ATOM   47   C  CE2   . PHE A 1 16  ? 140.262 38.231 5.148   1.00 19.27  ? 16   PHE A CE2   1 
ATOM   48   C  CZ    . PHE A 1 16  ? 138.927 38.145 5.527   1.00 13.27  ? 16   PHE A CZ    1 
ATOM   49   N  N     . ALA A 1 17  ? 140.855 34.068 5.198   1.00 11.07  ? 17   ALA A N     1 
ATOM   50   C  CA    . ALA A 1 17  ? 140.889 33.973 3.755   1.00 11.59  ? 17   ALA A CA    1 
ATOM   51   C  C     . ALA A 1 17  ? 139.657 34.568 3.093   1.00 19.12  ? 17   ALA A C     1 
ATOM   52   O  O     . ALA A 1 17  ? 138.615 34.713 3.706   1.00 15.64  ? 17   ALA A O     1 
ATOM   53   C  CB    . ALA A 1 17  ? 140.876 32.494 3.357   1.00 11.46  ? 17   ALA A CB    1 
ATOM   54   N  N     . ILE A 1 18  ? 139.815 34.910 1.829   1.00 14.05  ? 18   ILE A N     1 
ATOM   55   C  CA    . ILE A 1 18  ? 138.742 35.458 1.014   1.00 8.86   ? 18   ILE A CA    1 
ATOM   56   C  C     . ILE A 1 18  ? 138.653 34.452 -0.134  1.00 17.75  ? 18   ILE A C     1 
ATOM   57   O  O     . ILE A 1 18  ? 139.666 33.825 -0.485  1.00 13.21  ? 18   ILE A O     1 
ATOM   58   C  CB    . ILE A 1 18  ? 138.918 36.847 0.458   1.00 13.91  ? 18   ILE A CB    1 
ATOM   59   C  CG1   . ILE A 1 18  ? 140.283 37.026 -0.280  1.00 12.00  ? 18   ILE A CG1   1 
ATOM   60   C  CG2   . ILE A 1 18  ? 138.694 37.883 1.572   1.00 16.31  ? 18   ILE A CG2   1 
ATOM   61   C  CD1   . ILE A 1 18  ? 140.257 38.339 -1.091  1.00 16.82  ? 18   ILE A CD1   1 
ATOM   62   N  N     . GLY A 1 19  ? 137.480 34.252 -0.738  1.00 10.76  ? 19   GLY A N     1 
ATOM   63   C  CA    . GLY A 1 19  ? 137.405 33.288 -1.813  1.00 8.11   ? 19   GLY A CA    1 
ATOM   64   C  C     . GLY A 1 19  ? 136.036 33.364 -2.464  1.00 12.44  ? 19   GLY A C     1 
ATOM   65   O  O     . GLY A 1 19  ? 135.260 34.269 -2.147  1.00 11.91  ? 19   GLY A O     1 
ATOM   66   N  N     . ASN A 1 20  ? 135.779 32.448 -3.370  1.00 10.88  ? 20   ASN A N     1 
ATOM   67   C  CA    . ASN A 1 20  ? 134.511 32.367 -4.084  1.00 11.93  ? 20   ASN A CA    1 
ATOM   68   C  C     . ASN A 1 20  ? 133.811 31.116 -3.550  1.00 12.33  ? 20   ASN A C     1 
ATOM   69   O  O     . ASN A 1 20  ? 134.250 30.003 -3.811  1.00 9.62   ? 20   ASN A O     1 
ATOM   70   C  CB    . ASN A 1 20  ? 134.844 32.142 -5.598  1.00 8.13   ? 20   ASN A CB    1 
ATOM   71   C  CG    . ASN A 1 20  ? 135.561 33.311 -6.245  1.00 13.70  ? 20   ASN A CG    1 
ATOM   72   O  OD1   . ASN A 1 20  ? 135.383 34.448 -5.862  1.00 12.17  ? 20   ASN A OD1   1 
ATOM   73   N  ND2   . ASN A 1 20  ? 136.397 33.024 -7.270  1.00 14.29  ? 20   ASN A ND2   1 
ATOM   74   N  N     . PRO A 1 21  ? 132.730 31.265 -2.785  1.00 8.88   ? 21   PRO A N     1 
ATOM   75   C  CA    . PRO A 1 21  ? 132.048 30.079 -2.256  1.00 7.31   ? 21   PRO A CA    1 
ATOM   76   C  C     . PRO A 1 21  ? 131.197 29.481 -3.356  1.00 13.38  ? 21   PRO A C     1 
ATOM   77   O  O     . PRO A 1 21  ? 130.347 30.156 -3.915  1.00 15.53  ? 21   PRO A O     1 
ATOM   78   C  CB    . PRO A 1 21  ? 131.136 30.646 -1.161  1.00 10.57  ? 21   PRO A CB    1 
ATOM   79   C  CG    . PRO A 1 21  ? 131.128 32.100 -1.299  1.00 10.77  ? 21   PRO A CG    1 
ATOM   80   C  CD    . PRO A 1 21  ? 132.215 32.543 -2.259  1.00 11.79  ? 21   PRO A CD    1 
ATOM   81   N  N     . ILE A 1 22  ? 131.425 28.229 -3.671  1.00 9.79   ? 22   ILE A N     1 
ATOM   82   C  CA    . ILE A 1 22  ? 130.660 27.625 -4.734  1.00 8.32   ? 22   ILE A CA    1 
ATOM   83   C  C     . ILE A 1 22  ? 130.265 26.215 -4.416  1.00 10.91  ? 22   ILE A C     1 
ATOM   84   O  O     . ILE A 1 22  ? 130.885 25.529 -3.578  1.00 13.69  ? 22   ILE A O     1 
ATOM   85   C  CB    . ILE A 1 22  ? 131.802 27.485 -5.899  1.00 13.02  ? 22   ILE A CB    1 
ATOM   86   C  CG1   . ILE A 1 22  ? 132.155 28.840 -6.487  1.00 16.64  ? 22   ILE A CG1   1 
ATOM   87   C  CG2   . ILE A 1 22  ? 131.681 26.389 -6.892  1.00 20.37  ? 22   ILE A CG2   1 
ATOM   88   C  CD1   . ILE A 1 22  ? 133.458 28.643 -7.198  1.00 21.60  ? 22   ILE A CD1   1 
ATOM   89   N  N     . LEU A 1 23  ? 129.215 25.791 -5.109  1.00 10.08  ? 23   LEU A N     1 
ATOM   90   C  CA    . LEU A 1 23  ? 128.706 24.447 -4.938  1.00 13.32  ? 23   LEU A CA    1 
ATOM   91   C  C     . LEU A 1 23  ? 129.252 23.570 -6.060  1.00 10.88  ? 23   LEU A C     1 
ATOM   92   O  O     . LEU A 1 23  ? 129.198 23.969 -7.213  1.00 13.48  ? 23   LEU A O     1 
ATOM   93   C  CB    . LEU A 1 23  ? 127.155 24.481 -5.018  1.00 12.90  ? 23   LEU A CB    1 
ATOM   94   C  CG    . LEU A 1 23  ? 126.637 23.104 -4.710  1.00 26.56  ? 23   LEU A CG    1 
ATOM   95   C  CD1   . LEU A 1 23  ? 126.552 22.933 -3.203  1.00 29.07  ? 23   LEU A CD1   1 
ATOM   96   C  CD2   . LEU A 1 23  ? 125.323 22.795 -5.457  1.00 36.44  ? 23   LEU A CD2   1 
ATOM   97   N  N     . ASP A 1 24  ? 129.783 22.398 -5.737  1.00 7.45   ? 24   ASP A N     1 
ATOM   98   C  CA    . ASP A 1 24  ? 130.308 21.528 -6.781  1.00 8.33   ? 24   ASP A CA    1 
ATOM   99   C  C     . ASP A 1 24  ? 129.297 20.426 -7.142  1.00 12.86  ? 24   ASP A C     1 
ATOM   100  O  O     . ASP A 1 24  ? 128.671 19.803 -6.264  1.00 13.00  ? 24   ASP A O     1 
ATOM   101  C  CB    . ASP A 1 24  ? 131.555 20.696 -6.355  1.00 10.05  ? 24   ASP A CB    1 
ATOM   102  C  CG    . ASP A 1 24  ? 132.862 21.512 -6.279  1.00 10.23  ? 24   ASP A CG    1 
ATOM   103  O  OD1   . ASP A 1 24  ? 132.844 22.688 -6.679  1.00 9.24   ? 24   ASP A OD1   1 
ATOM   104  O  OD2   . ASP A 1 24  ? 133.884 21.005 -5.731  1.00 13.42  ? 24   ASP A OD2   1 
ATOM   105  N  N     . LEU A 1 25  ? 129.146 20.192 -8.440  1.00 11.31  ? 25   LEU A N     1 
ATOM   106  C  CA    . LEU A 1 25  ? 128.262 19.163 -8.986  1.00 10.50  ? 25   LEU A CA    1 
ATOM   107  C  C     . LEU A 1 25  ? 129.264 18.208 -9.616  1.00 13.86  ? 25   LEU A C     1 
ATOM   108  O  O     . LEU A 1 25  ? 129.882 18.548 -10.616 1.00 15.28  ? 25   LEU A O     1 
ATOM   109  C  CB    . LEU A 1 25  ? 127.417 19.753 -10.122 1.00 14.30  ? 25   LEU A CB    1 
ATOM   110  C  CG    . LEU A 1 25  ? 125.927 20.043 -9.931  1.00 27.95  ? 25   LEU A CG    1 
ATOM   111  C  CD1   . LEU A 1 25  ? 125.534 20.263 -8.501  1.00 31.18  ? 25   LEU A CD1   1 
ATOM   112  C  CD2   . LEU A 1 25  ? 125.488 21.202 -10.782 1.00 27.04  ? 25   LEU A CD2   1 
ATOM   113  N  N     . VAL A 1 26  ? 129.455 17.031 -9.027  1.00 10.44  ? 26   VAL A N     1 
ATOM   114  C  CA    . VAL A 1 26  ? 130.416 16.069 -9.535  1.00 12.18  ? 26   VAL A CA    1 
ATOM   115  C  C     . VAL A 1 26  ? 129.790 14.924 -10.286 1.00 21.43  ? 26   VAL A C     1 
ATOM   116  O  O     . VAL A 1 26  ? 128.798 14.353 -9.862  1.00 17.71  ? 26   VAL A O     1 
ATOM   117  C  CB    . VAL A 1 26  ? 131.189 15.415 -8.338  1.00 15.48  ? 26   VAL A CB    1 
ATOM   118  C  CG1   . VAL A 1 26  ? 132.291 14.445 -8.777  1.00 17.42  ? 26   VAL A CG1   1 
ATOM   119  C  CG2   . VAL A 1 26  ? 131.761 16.458 -7.375  1.00 16.43  ? 26   VAL A CG2   1 
ATOM   120  N  N     . ALA A 1 27  ? 130.403 14.587 -11.410 1.00 19.66  ? 27   ALA A N     1 
ATOM   121  C  CA    . ALA A 1 27  ? 129.888 13.505 -12.198 1.00 19.05  ? 27   ALA A CA    1 
ATOM   122  C  C     . ALA A 1 27  ? 130.943 12.916 -13.086 1.00 20.22  ? 27   ALA A C     1 
ATOM   123  O  O     . ALA A 1 27  ? 131.823 13.613 -13.570 1.00 18.18  ? 27   ALA A O     1 
ATOM   124  C  CB    . ALA A 1 27  ? 128.849 14.091 -13.090 1.00 25.18  ? 27   ALA A CB    1 
ATOM   125  N  N     . GLU A 1 28  ? 130.829 11.619 -13.288 1.00 17.28  ? 28   GLU A N     1 
ATOM   126  C  CA    . GLU A 1 28  ? 131.736 10.911 -14.132 1.00 19.14  ? 28   GLU A CA    1 
ATOM   127  C  C     . GLU A 1 28  ? 131.089 10.981 -15.505 1.00 22.92  ? 28   GLU A C     1 
ATOM   128  O  O     . GLU A 1 28  ? 129.953 10.558 -15.680 1.00 20.78  ? 28   GLU A O     1 
ATOM   129  C  CB    . GLU A 1 28  ? 131.751 9.483  -13.700 1.00 21.28  ? 28   GLU A CB    1 
ATOM   130  C  CG    . GLU A 1 28  ? 133.061 8.909  -14.223 1.00 48.92  ? 28   GLU A CG    1 
ATOM   131  C  CD    . GLU A 1 28  ? 133.814 8.140  -13.178 1.00 99.42  ? 28   GLU A CD    1 
ATOM   132  O  OE1   . GLU A 1 28  ? 133.335 8.089  -12.020 1.00 100.00 ? 28   GLU A OE1   1 
ATOM   133  O  OE2   . GLU A 1 28  ? 134.905 7.630  -13.515 1.00 94.94  ? 28   GLU A OE2   1 
ATOM   134  N  N     . VAL A 1 29  ? 131.780 11.534 -16.497 1.00 19.43  ? 29   VAL A N     1 
ATOM   135  C  CA    . VAL A 1 29  ? 131.166 11.627 -17.824 1.00 17.40  ? 29   VAL A CA    1 
ATOM   136  C  C     . VAL A 1 29  ? 132.081 11.065 -18.877 1.00 23.11  ? 29   VAL A C     1 
ATOM   137  O  O     . VAL A 1 29  ? 133.277 10.939 -18.668 1.00 23.90  ? 29   VAL A O     1 
ATOM   138  C  CB    . VAL A 1 29  ? 131.100 13.076 -18.247 1.00 20.12  ? 29   VAL A CB    1 
ATOM   139  C  CG1   . VAL A 1 29  ? 130.184 13.809 -17.281 1.00 19.07  ? 29   VAL A CG1   1 
ATOM   140  C  CG2   . VAL A 1 29  ? 132.490 13.700 -18.113 1.00 17.01  ? 29   VAL A CG2   1 
ATOM   141  N  N     . PRO A 1 30  ? 131.512 10.721 -20.005 1.00 19.55  ? 30   PRO A N     1 
ATOM   142  C  CA    . PRO A 1 30  ? 132.312 10.175 -21.080 1.00 22.04  ? 30   PRO A CA    1 
ATOM   143  C  C     . PRO A 1 30  ? 133.083 11.302 -21.794 1.00 26.41  ? 30   PRO A C     1 
ATOM   144  O  O     . PRO A 1 30  ? 132.734 12.473 -21.706 1.00 24.16  ? 30   PRO A O     1 
ATOM   145  C  CB    . PRO A 1 30  ? 131.226 9.563  -21.978 1.00 21.60  ? 30   PRO A CB    1 
ATOM   146  C  CG    . PRO A 1 30  ? 130.007 10.394 -21.746 1.00 27.04  ? 30   PRO A CG    1 
ATOM   147  C  CD    . PRO A 1 30  ? 130.069 10.732 -20.289 1.00 20.92  ? 30   PRO A CD    1 
ATOM   148  N  N     . SER A 1 31  ? 134.141 10.947 -22.509 1.00 24.20  ? 31   SER A N     1 
ATOM   149  C  CA    . SER A 1 31  ? 134.940 11.930 -23.236 1.00 25.27  ? 31   SER A CA    1 
ATOM   150  C  C     . SER A 1 31  ? 134.084 12.672 -24.254 1.00 32.65  ? 31   SER A C     1 
ATOM   151  O  O     . SER A 1 31  ? 134.372 13.816 -24.606 1.00 34.53  ? 31   SER A O     1 
ATOM   152  C  CB    . SER A 1 31  ? 136.052 11.239 -24.052 1.00 33.97  ? 31   SER A CB    1 
ATOM   153  O  OG    . SER A 1 31  ? 137.052 10.742 -23.188 1.00 54.73  ? 31   SER A OG    1 
ATOM   154  N  N     . SER A 1 32  ? 133.029 12.024 -24.739 1.00 25.03  ? 32   SER A N     1 
ATOM   155  C  CA    . SER A 1 32  ? 132.169 12.675 -25.711 1.00 23.83  ? 32   SER A CA    1 
ATOM   156  C  C     . SER A 1 32  ? 131.561 13.935 -25.126 1.00 26.92  ? 32   SER A C     1 
ATOM   157  O  O     . SER A 1 32  ? 131.358 14.929 -25.827 1.00 23.47  ? 32   SER A O     1 
ATOM   158  C  CB    . SER A 1 32  ? 130.988 11.767 -26.068 1.00 26.91  ? 32   SER A CB    1 
ATOM   159  O  OG    . SER A 1 32  ? 130.723 10.843 -25.028 1.00 53.81  ? 32   SER A OG    1 
ATOM   160  N  N     . PHE A 1 33  ? 131.262 13.888 -23.829 1.00 25.10  ? 33   PHE A N     1 
ATOM   161  C  CA    . PHE A 1 33  ? 130.659 15.031 -23.147 1.00 17.95  ? 33   PHE A CA    1 
ATOM   162  C  C     . PHE A 1 33  ? 131.611 16.196 -23.125 1.00 17.38  ? 33   PHE A C     1 
ATOM   163  O  O     . PHE A 1 33  ? 131.222 17.348 -23.284 1.00 21.53  ? 33   PHE A O     1 
ATOM   164  C  CB    . PHE A 1 33  ? 130.345 14.604 -21.755 1.00 18.94  ? 33   PHE A CB    1 
ATOM   165  C  CG    . PHE A 1 33  ? 129.507 15.599 -21.015 1.00 22.91  ? 33   PHE A CG    1 
ATOM   166  C  CD1   . PHE A 1 33  ? 128.121 15.586 -21.142 1.00 23.35  ? 33   PHE A CD1   1 
ATOM   167  C  CD2   . PHE A 1 33  ? 130.104 16.558 -20.208 1.00 22.02  ? 33   PHE A CD2   1 
ATOM   168  C  CE1   . PHE A 1 33  ? 127.336 16.490 -20.484 1.00 22.77  ? 33   PHE A CE1   1 
ATOM   169  C  CE2   . PHE A 1 33  ? 129.308 17.499 -19.525 1.00 27.30  ? 33   PHE A CE2   1 
ATOM   170  C  CZ    . PHE A 1 33  ? 127.924 17.452 -19.661 1.00 26.15  ? 33   PHE A CZ    1 
ATOM   171  N  N     . LEU A 1 34  ? 132.878 15.888 -22.926 1.00 17.53  ? 34   LEU A N     1 
ATOM   172  C  CA    . LEU A 1 34  ? 133.907 16.942 -22.887 1.00 23.64  ? 34   LEU A CA    1 
ATOM   173  C  C     . LEU A 1 34  ? 133.997 17.642 -24.236 1.00 26.19  ? 34   LEU A C     1 
ATOM   174  O  O     . LEU A 1 34  ? 134.115 18.872 -24.321 1.00 20.01  ? 34   LEU A O     1 
ATOM   175  C  CB    . LEU A 1 34  ? 135.299 16.360 -22.661 1.00 22.81  ? 34   LEU A CB    1 
ATOM   176  C  CG    . LEU A 1 34  ? 135.802 16.372 -21.241 1.00 32.61  ? 34   LEU A CG    1 
ATOM   177  C  CD1   . LEU A 1 34  ? 134.718 16.668 -20.300 1.00 32.59  ? 34   LEU A CD1   1 
ATOM   178  C  CD2   . LEU A 1 34  ? 136.564 15.134 -20.848 1.00 32.90  ? 34   LEU A CD2   1 
ATOM   179  N  N     . ASP A 1 35  ? 133.929 16.821 -25.280 1.00 28.41  ? 35   ASP A N     1 
ATOM   180  C  CA    . ASP A 1 35  ? 134.003 17.313 -26.649 1.00 30.44  ? 35   ASP A CA    1 
ATOM   181  C  C     . ASP A 1 35  ? 132.813 18.203 -26.963 1.00 23.71  ? 35   ASP A C     1 
ATOM   182  O  O     . ASP A 1 35  ? 132.996 19.296 -27.489 1.00 23.00  ? 35   ASP A O     1 
ATOM   183  C  CB    . ASP A 1 35  ? 134.052 16.160 -27.691 1.00 33.55  ? 35   ASP A CB    1 
ATOM   184  C  CG    . ASP A 1 35  ? 135.268 15.257 -27.513 1.00 37.22  ? 35   ASP A CG    1 
ATOM   185  O  OD1   . ASP A 1 35  ? 136.277 15.737 -26.962 1.00 38.31  ? 35   ASP A OD1   1 
ATOM   186  O  OD2   . ASP A 1 35  ? 135.192 14.066 -27.869 1.00 58.05  ? 35   ASP A OD2   1 
ATOM   187  N  N     . GLU A 1 36  ? 131.610 17.745 -26.641 1.00 18.66  ? 36   GLU A N     1 
ATOM   188  C  CA    . GLU A 1 36  ? 130.430 18.556 -26.930 1.00 20.27  ? 36   GLU A CA    1 
ATOM   189  C  C     . GLU A 1 36  ? 130.434 19.877 -26.214 1.00 22.92  ? 36   GLU A C     1 
ATOM   190  O  O     . GLU A 1 36  ? 129.870 20.855 -26.726 1.00 22.63  ? 36   GLU A O     1 
ATOM   191  C  CB    . GLU A 1 36  ? 129.100 18.040 -26.481 1.00 23.83  ? 36   GLU A CB    1 
ATOM   192  C  CG    . GLU A 1 36  ? 129.001 16.624 -26.094 1.00 63.78  ? 36   GLU A CG    1 
ATOM   193  C  CD    . GLU A 1 36  ? 127.544 16.306 -26.134 1.00 99.26  ? 36   GLU A CD    1 
ATOM   194  O  OE1   . GLU A 1 36  ? 127.198 15.089 -26.196 1.00 100.00 ? 36   GLU A OE1   1 
ATOM   195  O  OE2   . GLU A 1 36  ? 126.786 17.340 -26.136 1.00 43.09  ? 36   GLU A OE2   1 
ATOM   196  N  N     . PHE A 1 37  ? 131.050 19.900 -25.036 1.00 21.81  ? 37   PHE A N     1 
ATOM   197  C  CA    . PHE A 1 37  ? 131.106 21.124 -24.240 1.00 23.78  ? 37   PHE A CA    1 
ATOM   198  C  C     . PHE A 1 37  ? 132.366 21.958 -24.447 1.00 23.80  ? 37   PHE A C     1 
ATOM   199  O  O     . PHE A 1 37  ? 132.561 22.971 -23.761 1.00 20.93  ? 37   PHE A O     1 
ATOM   200  C  CB    . PHE A 1 37  ? 130.593 20.946 -22.810 1.00 25.27  ? 37   PHE A CB    1 
ATOM   201  C  CG    . PHE A 1 37  ? 129.106 20.848 -22.786 1.00 22.42  ? 37   PHE A CG    1 
ATOM   202  C  CD1   . PHE A 1 37  ? 128.508 19.650 -22.586 1.00 25.17  ? 37   PHE A CD1   1 
ATOM   203  C  CD2   . PHE A 1 37  ? 128.346 21.956 -23.016 1.00 27.40  ? 37   PHE A CD2   1 
ATOM   204  C  CE1   . PHE A 1 37  ? 127.134 19.518 -22.603 1.00 28.42  ? 37   PHE A CE1   1 
ATOM   205  C  CE2   . PHE A 1 37  ? 126.972 21.851 -23.045 1.00 33.42  ? 37   PHE A CE2   1 
ATOM   206  C  CZ    . PHE A 1 37  ? 126.367 20.621 -22.840 1.00 26.23  ? 37   PHE A CZ    1 
ATOM   207  N  N     . PHE A 1 38  ? 133.206 21.536 -25.384 1.00 16.66  ? 38   PHE A N     1 
ATOM   208  C  CA    . PHE A 1 38  ? 134.441 22.263 -25.688 1.00 16.35  ? 38   PHE A CA    1 
ATOM   209  C  C     . PHE A 1 38  ? 135.361 22.412 -24.493 1.00 18.13  ? 38   PHE A C     1 
ATOM   210  O  O     . PHE A 1 38  ? 135.918 23.491 -24.251 1.00 19.35  ? 38   PHE A O     1 
ATOM   211  C  CB    . PHE A 1 38  ? 134.138 23.709 -26.173 1.00 19.35  ? 38   PHE A CB    1 
ATOM   212  C  CG    . PHE A 1 38  ? 132.910 23.810 -27.066 1.00 19.43  ? 38   PHE A CG    1 
ATOM   213  C  CD1   . PHE A 1 38  ? 132.915 23.197 -28.309 1.00 23.54  ? 38   PHE A CD1   1 
ATOM   214  C  CD2   . PHE A 1 38  ? 131.795 24.484 -26.665 1.00 24.64  ? 38   PHE A CD2   1 
ATOM   215  C  CE1   . PHE A 1 38  ? 131.805 23.261 -29.145 1.00 26.34  ? 38   PHE A CE1   1 
ATOM   216  C  CE2   . PHE A 1 38  ? 130.685 24.561 -27.492 1.00 28.71  ? 38   PHE A CE2   1 
ATOM   217  C  CZ    . PHE A 1 38  ? 130.696 23.954 -28.739 1.00 26.27  ? 38   PHE A CZ    1 
ATOM   218  N  N     . LEU A 1 39  ? 135.525 21.335 -23.763 1.00 16.71  ? 39   LEU A N     1 
ATOM   219  C  CA    . LEU A 1 39  ? 136.387 21.389 -22.596 1.00 18.43  ? 39   LEU A CA    1 
ATOM   220  C  C     . LEU A 1 39  ? 137.648 20.568 -22.801 1.00 19.10  ? 39   LEU A C     1 
ATOM   221  O  O     . LEU A 1 39  ? 137.639 19.548 -23.466 1.00 23.19  ? 39   LEU A O     1 
ATOM   222  C  CB    . LEU A 1 39  ? 135.659 20.686 -21.428 1.00 18.56  ? 39   LEU A CB    1 
ATOM   223  C  CG    . LEU A 1 39  ? 134.405 21.434 -20.938 1.00 22.05  ? 39   LEU A CG    1 
ATOM   224  C  CD1   . LEU A 1 39  ? 133.580 20.464 -20.093 1.00 22.18  ? 39   LEU A CD1   1 
ATOM   225  C  CD2   . LEU A 1 39  ? 134.832 22.653 -20.181 1.00 18.25  ? 39   LEU A CD2   1 
ATOM   226  N  N     . LYS A 1 40  ? 138.726 21.027 -22.212 1.00 15.52  ? 40   LYS A N     1 
ATOM   227  C  CA    . LYS A 1 40  ? 139.994 20.338 -22.316 1.00 20.85  ? 40   LYS A CA    1 
ATOM   228  C  C     . LYS A 1 40  ? 140.179 19.566 -21.016 1.00 23.61  ? 40   LYS A C     1 
ATOM   229  O  O     . LYS A 1 40  ? 140.112 20.159 -19.939 1.00 21.56  ? 40   LYS A O     1 
ATOM   230  C  CB    . LYS A 1 40  ? 141.070 21.447 -22.486 1.00 29.25  ? 40   LYS A CB    1 
ATOM   231  C  CG    . LYS A 1 40  ? 142.515 20.990 -22.348 1.00 82.95  ? 40   LYS A CG    1 
ATOM   232  C  CD    . LYS A 1 40  ? 142.842 19.883 -23.373 1.00 100.00 ? 40   LYS A CD    1 
ATOM   233  C  CE    . LYS A 1 40  ? 142.447 18.441 -22.970 1.00 100.00 ? 40   LYS A CE    1 
ATOM   234  N  NZ    . LYS A 1 40  ? 141.324 17.780 -23.741 1.00 100.00 ? 40   LYS A NZ    1 
ATOM   235  N  N     . ARG A 1 41  ? 140.372 18.268 -21.115 1.00 18.22  ? 41   ARG A N     1 
ATOM   236  C  CA    . ARG A 1 41  ? 140.540 17.445 -19.941 1.00 16.53  ? 41   ARG A CA    1 
ATOM   237  C  C     . ARG A 1 41  ? 141.609 17.986 -19.022 1.00 22.82  ? 41   ARG A C     1 
ATOM   238  O  O     . ARG A 1 41  ? 142.704 18.323 -19.468 1.00 24.20  ? 41   ARG A O     1 
ATOM   239  C  CB    . ARG A 1 41  ? 140.808 16.023 -20.337 1.00 18.71  ? 41   ARG A CB    1 
ATOM   240  C  CG    . ARG A 1 41  ? 140.662 15.038 -19.176 1.00 26.07  ? 41   ARG A CG    1 
ATOM   241  C  CD    . ARG A 1 41  ? 140.325 13.565 -19.636 1.00 36.66  ? 41   ARG A CD    1 
ATOM   242  N  NE    . ARG A 1 41  ? 141.124 13.076 -20.751 1.00 47.35  ? 41   ARG A NE    1 
ATOM   243  C  CZ    . ARG A 1 41  ? 140.719 12.546 -21.929 1.00 75.32  ? 41   ARG A CZ    1 
ATOM   244  N  NH1   . ARG A 1 41  ? 139.440 12.374 -22.284 1.00 38.87  ? 41   ARG A NH1   1 
ATOM   245  N  NH2   . ARG A 1 41  ? 141.645 12.164 -22.803 1.00 90.11  ? 41   ARG A NH2   1 
ATOM   246  N  N     . GLY A 1 42  ? 141.271 18.067 -17.738 1.00 16.97  ? 42   GLY A N     1 
ATOM   247  C  CA    . GLY A 1 42  ? 142.162 18.548 -16.698 1.00 12.68  ? 42   GLY A CA    1 
ATOM   248  C  C     . GLY A 1 42  ? 142.209 20.051 -16.559 1.00 17.09  ? 42   GLY A C     1 
ATOM   249  O  O     . GLY A 1 42  ? 142.850 20.552 -15.645 1.00 21.00  ? 42   GLY A O     1 
ATOM   250  N  N     . ASP A 1 43  ? 141.547 20.793 -17.438 1.00 14.50  ? 43   ASP A N     1 
ATOM   251  C  CA    . ASP A 1 43  ? 141.582 22.242 -17.344 1.00 13.36  ? 43   ASP A CA    1 
ATOM   252  C  C     . ASP A 1 43  ? 140.558 22.814 -16.348 1.00 15.26  ? 43   ASP A C     1 
ATOM   253  O  O     . ASP A 1 43  ? 139.681 22.125 -15.876 1.00 15.11  ? 43   ASP A O     1 
ATOM   254  C  CB    . ASP A 1 43  ? 141.233 22.735 -18.765 1.00 20.67  ? 43   ASP A CB    1 
ATOM   255  C  CG    . ASP A 1 43  ? 141.761 24.132 -19.065 1.00 40.85  ? 43   ASP A CG    1 
ATOM   256  O  OD1   . ASP A 1 43  ? 142.457 24.769 -18.249 1.00 37.34  ? 43   ASP A OD1   1 
ATOM   257  O  OD2   . ASP A 1 43  ? 141.432 24.647 -20.128 1.00 45.89  ? 43   ASP A OD2   1 
ATOM   258  N  N     . ALA A 1 44  ? 140.701 24.093 -16.046 1.00 14.31  ? 44   ALA A N     1 
ATOM   259  C  CA    . ALA A 1 44  ? 139.816 24.808 -15.146 1.00 15.01  ? 44   ALA A CA    1 
ATOM   260  C  C     . ALA A 1 44  ? 139.455 26.094 -15.866 1.00 17.79  ? 44   ALA A C     1 
ATOM   261  O  O     . ALA A 1 44  ? 140.339 26.860 -16.241 1.00 20.34  ? 44   ALA A O     1 
ATOM   262  C  CB    . ALA A 1 44  ? 140.463 25.083 -13.773 1.00 16.40  ? 44   ALA A CB    1 
ATOM   263  N  N     . THR A 1 45  ? 138.168 26.347 -16.089 1.00 14.72  ? 45   THR A N     1 
ATOM   264  C  CA    . THR A 1 45  ? 137.801 27.578 -16.790 1.00 13.59  ? 45   THR A CA    1 
ATOM   265  C  C     . THR A 1 45  ? 136.467 28.119 -16.290 1.00 16.37  ? 45   THR A C     1 
ATOM   266  O  O     . THR A 1 45  ? 135.820 27.490 -15.465 1.00 13.70  ? 45   THR A O     1 
ATOM   267  C  CB    . THR A 1 45  ? 137.602 27.111 -18.283 1.00 18.57  ? 45   THR A CB    1 
ATOM   268  O  OG1   . THR A 1 45  ? 137.423 28.238 -19.087 1.00 38.18  ? 45   THR A OG1   1 
ATOM   269  C  CG2   . THR A 1 45  ? 136.417 26.184 -18.438 1.00 10.40  ? 45   THR A CG2   1 
ATOM   270  N  N     . LEU A 1 46  ? 136.081 29.287 -16.785 1.00 12.78  ? 46   LEU A N     1 
ATOM   271  C  CA    . LEU A 1 46  ? 134.821 29.901 -16.411 1.00 13.74  ? 46   LEU A CA    1 
ATOM   272  C  C     . LEU A 1 46  ? 133.894 29.620 -17.591 1.00 20.21  ? 46   LEU A C     1 
ATOM   273  O  O     . LEU A 1 46  ? 134.305 29.752 -18.741 1.00 16.98  ? 46   LEU A O     1 
ATOM   274  C  CB    . LEU A 1 46  ? 134.962 31.374 -16.173 1.00 13.73  ? 46   LEU A CB    1 
ATOM   275  C  CG    . LEU A 1 46  ? 135.848 31.756 -15.022 1.00 19.01  ? 46   LEU A CG    1 
ATOM   276  C  CD1   . LEU A 1 46  ? 135.939 33.257 -14.997 1.00 21.72  ? 46   LEU A CD1   1 
ATOM   277  C  CD2   . LEU A 1 46  ? 135.329 31.284 -13.690 1.00 19.80  ? 46   LEU A CD2   1 
ATOM   278  N  N     . ALA A 1 47  ? 132.665 29.220 -17.335 1.00 13.14  ? 47   ALA A N     1 
ATOM   279  C  CA    . ALA A 1 47  ? 131.721 28.889 -18.398 1.00 14.34  ? 47   ALA A CA    1 
ATOM   280  C  C     . ALA A 1 47  ? 131.385 30.004 -19.378 1.00 21.59  ? 47   ALA A C     1 
ATOM   281  O  O     . ALA A 1 47  ? 131.052 31.111 -18.963 1.00 20.35  ? 47   ALA A O     1 
ATOM   282  C  CB    . ALA A 1 47  ? 130.431 28.404 -17.782 1.00 14.67  ? 47   ALA A CB    1 
ATOM   283  N  N     . THR A 1 48  ? 131.458 29.687 -20.685 1.00 18.60  ? 48   THR A N     1 
ATOM   284  C  CA    . THR A 1 48  ? 131.123 30.659 -21.729 1.00 15.32  ? 48   THR A CA    1 
ATOM   285  C  C     . THR A 1 48  ? 129.626 30.436 -21.977 1.00 22.46  ? 48   THR A C     1 
ATOM   286  O  O     . THR A 1 48  ? 129.070 29.448 -21.501 1.00 20.65  ? 48   THR A O     1 
ATOM   287  C  CB    . THR A 1 48  ? 131.801 30.471 -23.078 1.00 18.65  ? 48   THR A CB    1 
ATOM   288  O  OG1   . THR A 1 48  ? 131.452 29.197 -23.576 1.00 16.29  ? 48   THR A OG1   1 
ATOM   289  C  CG2   . THR A 1 48  ? 133.277 30.563 -22.915 1.00 19.02  ? 48   THR A CG2   1 
ATOM   290  N  N     . PRO A 1 49  ? 128.965 31.329 -22.704 1.00 22.13  ? 49   PRO A N     1 
ATOM   291  C  CA    . PRO A 1 49  ? 127.541 31.192 -22.963 1.00 17.45  ? 49   PRO A CA    1 
ATOM   292  C  C     . PRO A 1 49  ? 127.119 29.831 -23.468 1.00 20.93  ? 49   PRO A C     1 
ATOM   293  O  O     . PRO A 1 49  ? 126.095 29.303 -23.041 1.00 29.17  ? 49   PRO A O     1 
ATOM   294  C  CB    . PRO A 1 49  ? 127.262 32.285 -23.936 1.00 22.68  ? 49   PRO A CB    1 
ATOM   295  C  CG    . PRO A 1 49  ? 128.154 33.355 -23.421 1.00 26.87  ? 49   PRO A CG    1 
ATOM   296  C  CD    . PRO A 1 49  ? 129.437 32.593 -23.251 1.00 25.69  ? 49   PRO A CD    1 
ATOM   297  N  N     . GLU A 1 50  ? 127.889 29.252 -24.366 1.00 26.68  ? 50   GLU A N     1 
ATOM   298  C  CA    . GLU A 1 50  ? 127.549 27.943 -24.909 1.00 28.46  ? 50   GLU A CA    1 
ATOM   299  C  C     . GLU A 1 50  ? 127.651 26.831 -23.872 1.00 38.96  ? 50   GLU A C     1 
ATOM   300  O  O     . GLU A 1 50  ? 126.936 25.827 -23.944 1.00 43.74  ? 50   GLU A O     1 
ATOM   301  C  CB    . GLU A 1 50  ? 128.475 27.610 -26.093 1.00 33.37  ? 50   GLU A CB    1 
ATOM   302  C  CG    . GLU A 1 50  ? 127.790 26.972 -27.295 1.00 73.70  ? 50   GLU A CG    1 
ATOM   303  C  CD    . GLU A 1 50  ? 126.275 27.343 -27.509 1.00 100.00 ? 50   GLU A CD    1 
ATOM   304  O  OE1   . GLU A 1 50  ? 125.987 28.332 -28.254 1.00 100.00 ? 50   GLU A OE1   1 
ATOM   305  O  OE2   . GLU A 1 50  ? 125.372 26.629 -26.969 1.00 100.00 ? 50   GLU A OE2   1 
ATOM   306  N  N     . GLN A 1 51  ? 128.533 26.992 -22.899 1.00 23.15  ? 51   GLN A N     1 
ATOM   307  C  CA    . GLN A 1 51  ? 128.683 25.950 -21.886 1.00 23.12  ? 51   GLN A CA    1 
ATOM   308  C  C     . GLN A 1 51  ? 127.661 26.045 -20.751 1.00 25.41  ? 51   GLN A C     1 
ATOM   309  O  O     . GLN A 1 51  ? 127.582 25.151 -19.896 1.00 22.74  ? 51   GLN A O     1 
ATOM   310  C  CB    . GLN A 1 51  ? 130.149 25.904 -21.392 1.00 22.84  ? 51   GLN A CB    1 
ATOM   311  C  CG    . GLN A 1 51  ? 131.211 25.776 -22.479 1.00 16.56  ? 51   GLN A CG    1 
ATOM   312  C  CD    . GLN A 1 51  ? 132.625 26.093 -21.988 1.00 17.34  ? 51   GLN A CD    1 
ATOM   313  O  OE1   . GLN A 1 51  ? 132.866 27.105 -21.338 1.00 18.41  ? 51   GLN A OE1   1 
ATOM   314  N  NE2   . GLN A 1 51  ? 133.543 25.223 -22.293 1.00 14.54  ? 51   GLN A NE2   1 
ATOM   315  N  N     . MET A 1 52  ? 126.891 27.124 -20.731 1.00 21.47  ? 52   MET A N     1 
ATOM   316  C  CA    . MET A 1 52  ? 125.899 27.280 -19.682 1.00 22.73  ? 52   MET A CA    1 
ATOM   317  C  C     . MET A 1 52  ? 124.976 26.084 -19.627 1.00 24.33  ? 52   MET A C     1 
ATOM   318  O  O     . MET A 1 52  ? 124.499 25.713 -18.572 1.00 30.87  ? 52   MET A O     1 
ATOM   319  C  CB    . MET A 1 52  ? 125.106 28.561 -19.775 1.00 25.01  ? 52   MET A CB    1 
ATOM   320  C  CG    . MET A 1 52  ? 126.000 29.732 -19.389 1.00 29.87  ? 52   MET A CG    1 
ATOM   321  S  SD    . MET A 1 52  ? 126.610 29.595 -17.673 1.00 28.86  ? 52   MET A SD    1 
ATOM   322  C  CE    . MET A 1 52  ? 125.140 30.157 -16.794 1.00 26.82  ? 52   MET A CE    1 
ATOM   323  N  N     . ARG A 1 53  ? 124.733 25.461 -20.763 1.00 26.44  ? 53   ARG A N     1 
ATOM   324  C  CA    . ARG A 1 53  ? 123.840 24.293 -20.811 1.00 28.77  ? 53   ARG A CA    1 
ATOM   325  C  C     . ARG A 1 53  ? 124.404 23.062 -20.090 1.00 31.04  ? 53   ARG A C     1 
ATOM   326  O  O     . ARG A 1 53  ? 123.721 22.044 -19.907 1.00 27.66  ? 53   ARG A O     1 
ATOM   327  C  CB    . ARG A 1 53  ? 123.465 24.105 -22.324 1.00 31.19  ? 53   ARG A CB    1 
ATOM   328  C  CG    . ARG A 1 53  ? 122.997 22.811 -22.908 1.00 50.31  ? 53   ARG A CG    1 
ATOM   329  C  CD    . ARG A 1 53  ? 123.609 22.652 -24.339 1.00 67.18  ? 53   ARG A CD    1 
ATOM   330  N  NE    . ARG A 1 53  ? 122.786 21.998 -25.355 1.00 59.00  ? 53   ARG A NE    1 
ATOM   331  C  CZ    . ARG A 1 53  ? 121.812 21.108 -25.148 1.00 96.30  ? 53   ARG A CZ    1 
ATOM   332  N  NH1   . ARG A 1 53  ? 121.464 20.708 -23.933 1.00 89.58  ? 53   ARG A NH1   1 
ATOM   333  N  NH2   . ARG A 1 53  ? 121.163 20.607 -26.190 1.00 97.09  ? 53   ARG A NH2   1 
ATOM   334  N  N     . ILE A 1 54  ? 125.655 23.132 -19.661 1.00 18.44  ? 54   ILE A N     1 
ATOM   335  C  CA    . ILE A 1 54  ? 126.210 21.978 -18.989 1.00 18.39  ? 54   ILE A CA    1 
ATOM   336  C  C     . ILE A 1 54  ? 125.526 21.686 -17.645 1.00 18.06  ? 54   ILE A C     1 
ATOM   337  O  O     . ILE A 1 54  ? 125.375 20.519 -17.268 1.00 20.48  ? 54   ILE A O     1 
ATOM   338  C  CB    . ILE A 1 54  ? 127.671 22.307 -18.783 1.00 24.91  ? 54   ILE A CB    1 
ATOM   339  C  CG1   . ILE A 1 54  ? 128.563 21.113 -18.770 1.00 35.10  ? 54   ILE A CG1   1 
ATOM   340  C  CG2   . ILE A 1 54  ? 127.861 23.264 -17.680 1.00 28.86  ? 54   ILE A CG2   1 
ATOM   341  C  CD1   . ILE A 1 54  ? 129.900 21.541 -19.376 1.00 46.53  ? 54   ILE A CD1   1 
ATOM   342  N  N     . TYR A 1 55  ? 125.126 22.737 -16.935 1.00 17.83  ? 55   TYR A N     1 
ATOM   343  C  CA    . TYR A 1 55  ? 124.498 22.582 -15.636 1.00 22.88  ? 55   TYR A CA    1 
ATOM   344  C  C     . TYR A 1 55  ? 123.236 21.733 -15.622 1.00 34.60  ? 55   TYR A C     1 
ATOM   345  O  O     . TYR A 1 55  ? 123.110 20.835 -14.786 1.00 34.31  ? 55   TYR A O     1 
ATOM   346  C  CB    . TYR A 1 55  ? 124.511 23.776 -14.754 1.00 21.21  ? 55   TYR A CB    1 
ATOM   347  C  CG    . TYR A 1 55  ? 125.838 24.431 -14.823 1.00 20.13  ? 55   TYR A CG    1 
ATOM   348  C  CD1   . TYR A 1 55  ? 126.078 25.498 -15.676 1.00 22.34  ? 55   TYR A CD1   1 
ATOM   349  C  CD2   . TYR A 1 55  ? 126.842 23.962 -14.031 1.00 17.75  ? 55   TYR A CD2   1 
ATOM   350  C  CE1   . TYR A 1 55  ? 127.302 26.094 -15.735 1.00 17.28  ? 55   TYR A CE1   1 
ATOM   351  C  CE2   . TYR A 1 55  ? 128.077 24.541 -14.063 1.00 15.70  ? 55   TYR A CE2   1 
ATOM   352  C  CZ    . TYR A 1 55  ? 128.290 25.574 -14.919 1.00 19.35  ? 55   TYR A CZ    1 
ATOM   353  O  OH    . TYR A 1 55  ? 129.557 26.113 -14.917 1.00 18.44  ? 55   TYR A OH    1 
ATOM   354  N  N     . SER A 1 56  ? 122.311 21.998 -16.523 1.00 29.38  ? 56   SER A N     1 
ATOM   355  C  CA    . SER A 1 56  ? 121.087 21.204 -16.536 1.00 31.10  ? 56   SER A CA    1 
ATOM   356  C  C     . SER A 1 56  ? 121.311 19.809 -17.110 1.00 38.88  ? 56   SER A C     1 
ATOM   357  O  O     . SER A 1 56  ? 120.719 18.828 -16.657 1.00 45.49  ? 56   SER A O     1 
ATOM   358  C  CB    . SER A 1 56  ? 119.964 21.881 -17.294 1.00 42.12  ? 56   SER A CB    1 
ATOM   359  O  OG    . SER A 1 56  ? 120.460 22.511 -18.453 1.00 59.91  ? 56   SER A OG    1 
ATOM   360  N  N     . THR A 1 57  ? 122.170 19.715 -18.103 1.00 23.42  ? 57   THR A N     1 
ATOM   361  C  CA    . THR A 1 57  ? 122.441 18.442 -18.734 1.00 21.45  ? 57   THR A CA    1 
ATOM   362  C  C     . THR A 1 57  ? 123.139 17.409 -17.863 1.00 27.11  ? 57   THR A C     1 
ATOM   363  O  O     . THR A 1 57  ? 123.106 16.229 -18.187 1.00 25.78  ? 57   THR A O     1 
ATOM   364  C  CB    . THR A 1 57  ? 123.363 18.771 -19.839 1.00 24.94  ? 57   THR A CB    1 
ATOM   365  O  OG1   . THR A 1 57  ? 122.664 19.664 -20.685 1.00 34.76  ? 57   THR A OG1   1 
ATOM   366  C  CG2   . THR A 1 57  ? 123.729 17.547 -20.613 1.00 32.36  ? 57   THR A CG2   1 
ATOM   367  N  N     . LEU A 1 58  ? 123.776 17.824 -16.772 1.00 21.25  ? 58   LEU A N     1 
ATOM   368  C  CA    . LEU A 1 58  ? 124.476 16.860 -15.920 1.00 19.44  ? 58   LEU A CA    1 
ATOM   369  C  C     . LEU A 1 58  ? 123.556 15.872 -15.215 1.00 14.71  ? 58   LEU A C     1 
ATOM   370  O  O     . LEU A 1 58  ? 123.988 14.786 -14.835 1.00 16.11  ? 58   LEU A O     1 
ATOM   371  C  CB    . LEU A 1 58  ? 125.274 17.584 -14.836 1.00 20.36  ? 58   LEU A CB    1 
ATOM   372  C  CG    . LEU A 1 58  ? 126.604 18.214 -15.122 1.00 31.94  ? 58   LEU A CG    1 
ATOM   373  C  CD1   . LEU A 1 58  ? 127.284 18.257 -13.775 1.00 33.39  ? 58   LEU A CD1   1 
ATOM   374  C  CD2   . LEU A 1 58  ? 127.417 17.284 -15.964 1.00 35.65  ? 58   LEU A CD2   1 
ATOM   375  N  N     . ASP A 1 59  ? 122.291 16.250 -15.026 1.00 18.75  ? 59   ASP A N     1 
ATOM   376  C  CA    . ASP A 1 59  ? 121.339 15.368 -14.345 1.00 19.57  ? 59   ASP A CA    1 
ATOM   377  C  C     . ASP A 1 59  ? 121.272 14.000 -14.987 1.00 22.13  ? 59   ASP A C     1 
ATOM   378  O  O     . ASP A 1 59  ? 120.967 13.031 -14.317 1.00 22.95  ? 59   ASP A O     1 
ATOM   379  C  CB    . ASP A 1 59  ? 119.862 15.879 -14.285 1.00 25.84  ? 59   ASP A CB    1 
ATOM   380  C  CG    . ASP A 1 59  ? 119.557 16.857 -13.135 1.00 40.84  ? 59   ASP A CG    1 
ATOM   381  O  OD1   . ASP A 1 59  ? 120.326 17.013 -12.145 1.00 45.06  ? 59   ASP A OD1   1 
ATOM   382  O  OD2   . ASP A 1 59  ? 118.480 17.472 -13.232 1.00 49.61  ? 59   ASP A OD2   1 
ATOM   383  N  N     . GLN A 1 60  ? 121.548 13.897 -16.280 1.00 18.64  ? 60   GLN A N     1 
ATOM   384  C  CA    . GLN A 1 60  ? 121.471 12.579 -16.897 1.00 21.99  ? 60   GLN A CA    1 
ATOM   385  C  C     . GLN A 1 60  ? 122.588 11.676 -16.426 1.00 25.83  ? 60   GLN A C     1 
ATOM   386  O  O     . GLN A 1 60  ? 122.586 10.487 -16.743 1.00 22.95  ? 60   GLN A O     1 
ATOM   387  C  CB    . GLN A 1 60  ? 121.479 12.545 -18.438 1.00 24.42  ? 60   GLN A CB    1 
ATOM   388  C  CG    . GLN A 1 60  ? 121.630 13.894 -19.078 1.00 82.82  ? 60   GLN A CG    1 
ATOM   389  C  CD    . GLN A 1 60  ? 121.455 13.832 -20.592 1.00 84.02  ? 60   GLN A CD    1 
ATOM   390  O  OE1   . GLN A 1 60  ? 120.442 14.304 -21.164 1.00 67.64  ? 60   GLN A OE1   1 
ATOM   391  N  NE2   . GLN A 1 60  ? 122.458 13.262 -21.256 1.00 44.88  ? 60   GLN A NE2   1 
ATOM   392  N  N     . PHE A 1 61  ? 123.548 12.232 -15.687 1.00 14.95  ? 61   PHE A N     1 
ATOM   393  C  CA    . PHE A 1 61  ? 124.654 11.414 -15.215 1.00 11.47  ? 61   PHE A CA    1 
ATOM   394  C  C     . PHE A 1 61  ? 124.579 11.128 -13.715 1.00 18.86  ? 61   PHE A C     1 
ATOM   395  O  O     . PHE A 1 61  ? 125.518 10.603 -13.145 1.00 18.28  ? 61   PHE A O     1 
ATOM   396  C  CB    . PHE A 1 61  ? 125.954 12.095 -15.517 1.00 16.02  ? 61   PHE A CB    1 
ATOM   397  C  CG    . PHE A 1 61  ? 126.195 12.244 -17.018 1.00 18.22  ? 61   PHE A CG    1 
ATOM   398  C  CD1   . PHE A 1 61  ? 125.997 13.453 -17.651 1.00 21.39  ? 61   PHE A CD1   1 
ATOM   399  C  CD2   . PHE A 1 61  ? 126.602 11.128 -17.754 1.00 19.30  ? 61   PHE A CD2   1 
ATOM   400  C  CE1   . PHE A 1 61  ? 126.190 13.535 -19.032 1.00 25.85  ? 61   PHE A CE1   1 
ATOM   401  C  CE2   . PHE A 1 61  ? 126.801 11.204 -19.104 1.00 23.84  ? 61   PHE A CE2   1 
ATOM   402  C  CZ    . PHE A 1 61  ? 126.593 12.410 -19.731 1.00 23.80  ? 61   PHE A CZ    1 
ATOM   403  N  N     . ASN A 1 62  ? 123.464 11.462 -13.084 1.00 16.52  ? 62   ASN A N     1 
ATOM   404  C  CA    . ASN A 1 62  ? 123.280 11.235 -11.652 1.00 12.71  ? 62   ASN A CA    1 
ATOM   405  C  C     . ASN A 1 62  ? 124.451 11.807 -10.847 1.00 18.27  ? 62   ASN A C     1 
ATOM   406  O  O     . ASN A 1 62  ? 125.154 11.100 -10.122 1.00 19.33  ? 62   ASN A O     1 
ATOM   407  C  CB    . ASN A 1 62  ? 123.265 9.756  -11.422 1.00 16.25  ? 62   ASN A CB    1 
ATOM   408  C  CG    . ASN A 1 62  ? 122.075 9.096  -12.074 1.00 29.48  ? 62   ASN A CG    1 
ATOM   409  O  OD1   . ASN A 1 62  ? 122.127 7.962  -12.442 1.00 43.74  ? 62   ASN A OD1   1 
ATOM   410  N  ND2   . ASN A 1 62  ? 121.020 9.802  -12.203 1.00 12.43  ? 62   ASN A ND2   1 
ATOM   411  N  N     . PRO A 1 63  ? 124.667 13.092 -10.966 1.00 15.68  ? 63   PRO A N     1 
ATOM   412  C  CA    . PRO A 1 63  ? 125.758 13.713 -10.243 1.00 14.89  ? 63   PRO A CA    1 
ATOM   413  C  C     . PRO A 1 63  ? 125.482 13.810 -8.754  1.00 21.43  ? 63   PRO A C     1 
ATOM   414  O  O     . PRO A 1 63  ? 124.368 13.609 -8.255  1.00 21.09  ? 63   PRO A O     1 
ATOM   415  C  CB    . PRO A 1 63  ? 125.791 15.160 -10.821 1.00 17.40  ? 63   PRO A CB    1 
ATOM   416  C  CG    . PRO A 1 63  ? 124.373 15.429 -11.227 1.00 18.38  ? 63   PRO A CG    1 
ATOM   417  C  CD    . PRO A 1 63  ? 123.763 14.081 -11.610 1.00 15.90  ? 63   PRO A CD    1 
ATOM   418  N  N     . THR A 1 64  ? 126.533 14.129 -8.035  1.00 14.14  ? 64   THR A N     1 
ATOM   419  C  CA    . THR A 1 64  ? 126.457 14.279 -6.593  1.00 12.00  ? 64   THR A CA    1 
ATOM   420  C  C     . THR A 1 64  ? 126.793 15.732 -6.306  1.00 18.70  ? 64   THR A C     1 
ATOM   421  O  O     . THR A 1 64  ? 127.528 16.351 -7.073  1.00 17.87  ? 64   THR A O     1 
ATOM   422  C  CB    . THR A 1 64  ? 127.540 13.292 -6.141  1.00 25.58  ? 64   THR A CB    1 
ATOM   423  O  OG1   . THR A 1 64  ? 127.100 12.302 -5.229  1.00 48.74  ? 64   THR A OG1   1 
ATOM   424  C  CG2   . THR A 1 64  ? 128.879 13.795 -6.052  1.00 15.19  ? 64   THR A CG2   1 
ATOM   425  N  N     . SER A 1 65  ? 126.276 16.316 -5.237  1.00 11.39  ? 65   SER A N     1 
ATOM   426  C  CA    . SER A 1 65  ? 126.628 17.719 -5.005  1.00 10.07  ? 65   SER A CA    1 
ATOM   427  C  C     . SER A 1 65  ? 127.284 17.887 -3.658  1.00 17.96  ? 65   SER A C     1 
ATOM   428  O  O     . SER A 1 65  ? 126.908 17.214 -2.712  1.00 17.08  ? 65   SER A O     1 
ATOM   429  C  CB    . SER A 1 65  ? 125.532 18.728 -5.199  1.00 18.08  ? 65   SER A CB    1 
ATOM   430  O  OG    . SER A 1 65  ? 124.605 18.407 -4.246  1.00 30.86  ? 65   SER A OG    1 
ATOM   431  N  N     . LEU A 1 66  ? 128.266 18.776 -3.587  1.00 11.57  ? 66   LEU A N     1 
ATOM   432  C  CA    . LEU A 1 66  ? 128.973 19.020 -2.339  1.00 17.15  ? 66   LEU A CA    1 
ATOM   433  C  C     . LEU A 1 66  ? 129.595 20.390 -2.341  1.00 15.82  ? 66   LEU A C     1 
ATOM   434  O  O     . LEU A 1 66  ? 129.844 20.950 -3.400  1.00 14.20  ? 66   LEU A O     1 
ATOM   435  C  CB    . LEU A 1 66  ? 129.877 17.939 -1.917  1.00 21.34  ? 66   LEU A CB    1 
ATOM   436  C  CG    . LEU A 1 66  ? 131.171 17.836 -2.648  1.00 25.18  ? 66   LEU A CG    1 
ATOM   437  C  CD1   . LEU A 1 66  ? 131.876 16.697 -1.917  1.00 22.77  ? 66   LEU A CD1   1 
ATOM   438  C  CD2   . LEU A 1 66  ? 130.851 17.372 -4.020  1.00 31.90  ? 66   LEU A CD2   1 
ATOM   439  N  N     . PRO A 1 67  ? 129.833 20.952 -1.168  1.00 14.27  ? 67   PRO A N     1 
ATOM   440  C  CA    . PRO A 1 67  ? 130.425 22.283 -1.149  1.00 11.59  ? 67   PRO A CA    1 
ATOM   441  C  C     . PRO A 1 67  ? 131.790 22.268 -1.826  1.00 12.99  ? 67   PRO A C     1 
ATOM   442  O  O     . PRO A 1 67  ? 132.511 21.268 -1.778  1.00 15.48  ? 67   PRO A O     1 
ATOM   443  C  CB    . PRO A 1 67  ? 130.697 22.566 0.331   1.00 15.47  ? 67   PRO A CB    1 
ATOM   444  C  CG    . PRO A 1 67  ? 129.742 21.630 1.060   1.00 19.79  ? 67   PRO A CG    1 
ATOM   445  C  CD    . PRO A 1 67  ? 129.638 20.411 0.198   1.00 17.38  ? 67   PRO A CD    1 
ATOM   446  N  N     . GLY A 1 68  ? 132.132 23.396 -2.442  1.00 10.59  ? 68   GLY A N     1 
ATOM   447  C  CA    . GLY A 1 68  ? 133.410 23.563 -3.129  1.00 10.71  ? 68   GLY A CA    1 
ATOM   448  C  C     . GLY A 1 68  ? 133.949 24.969 -2.886  1.00 13.46  ? 68   GLY A C     1 
ATOM   449  O  O     . GLY A 1 68  ? 133.644 25.597 -1.867  1.00 11.76  ? 68   GLY A O     1 
ATOM   450  N  N     . GLY A 1 69  ? 134.744 25.479 -3.832  1.00 6.79   ? 69   GLY A N     1 
ATOM   451  C  CA    . GLY A 1 69  ? 135.329 26.802 -3.684  1.00 6.30   ? 69   GLY A CA    1 
ATOM   452  C  C     . GLY A 1 69  ? 136.760 26.517 -3.220  1.00 12.26  ? 69   GLY A C     1 
ATOM   453  O  O     . GLY A 1 69  ? 136.958 25.925 -2.159  1.00 12.10  ? 69   GLY A O     1 
ATOM   454  N  N     . SER A 1 70  ? 137.757 26.893 -4.011  1.00 11.30  ? 70   SER A N     1 
ATOM   455  C  CA    . SER A 1 70  ? 139.160 26.609 -3.645  1.00 9.07   ? 70   SER A CA    1 
ATOM   456  C  C     . SER A 1 70  ? 139.617 27.072 -2.259  1.00 7.13   ? 70   SER A C     1 
ATOM   457  O  O     . SER A 1 70  ? 140.079 26.262 -1.455  1.00 9.76   ? 70   SER A O     1 
ATOM   458  C  CB    . SER A 1 70  ? 140.116 27.024 -4.798  1.00 14.86  ? 70   SER A CB    1 
ATOM   459  O  OG    . SER A 1 70  ? 141.473 26.818 -4.379  1.00 11.45  ? 70   SER A OG    1 
ATOM   460  N  N     . ALA A 1 71  ? 139.509 28.358 -1.978  1.00 7.85   ? 71   ALA A N     1 
ATOM   461  C  CA    . ALA A 1 71  ? 139.935 28.873 -0.677  1.00 5.17   ? 71   ALA A CA    1 
ATOM   462  C  C     . ALA A 1 71  ? 139.063 28.297 0.461   1.00 15.20  ? 71   ALA A C     1 
ATOM   463  O  O     . ALA A 1 71  ? 139.551 28.026 1.562   1.00 10.93  ? 71   ALA A O     1 
ATOM   464  C  CB    . ALA A 1 71  ? 139.944 30.412 -0.702  1.00 8.98   ? 71   ALA A CB    1 
ATOM   465  N  N     . LEU A 1 72  ? 137.761 28.103 0.200   1.00 10.61  ? 72   LEU A N     1 
ATOM   466  C  CA    . LEU A 1 72  ? 136.867 27.553 1.218   1.00 12.13  ? 72   LEU A CA    1 
ATOM   467  C  C     . LEU A 1 72  ? 137.328 26.153 1.565   1.00 14.61  ? 72   LEU A C     1 
ATOM   468  O  O     . LEU A 1 72  ? 137.409 25.802 2.741   1.00 13.09  ? 72   LEU A O     1 
ATOM   469  C  CB    . LEU A 1 72  ? 135.386 27.557 0.760   1.00 12.99  ? 72   LEU A CB    1 
ATOM   470  C  CG    . LEU A 1 72  ? 134.331 27.188 1.866   1.00 14.39  ? 72   LEU A CG    1 
ATOM   471  C  CD1   . LEU A 1 72  ? 134.507 28.019 3.126   1.00 14.19  ? 72   LEU A CD1   1 
ATOM   472  C  CD2   . LEU A 1 72  ? 132.917 27.438 1.339   1.00 10.63  ? 72   LEU A CD2   1 
ATOM   473  N  N     . ASN A 1 73  ? 137.641 25.352 0.544   1.00 9.33   ? 73   ASN A N     1 
ATOM   474  C  CA    . ASN A 1 73  ? 138.097 24.016 0.820   1.00 6.95   ? 73   ASN A CA    1 
ATOM   475  C  C     . ASN A 1 73  ? 139.335 24.078 1.728   1.00 9.41   ? 73   ASN A C     1 
ATOM   476  O  O     . ASN A 1 73  ? 139.434 23.363 2.727   1.00 13.30  ? 73   ASN A O     1 
ATOM   477  C  CB    . ASN A 1 73  ? 138.586 23.358 -0.489  1.00 8.97   ? 73   ASN A CB    1 
ATOM   478  C  CG    . ASN A 1 73  ? 137.420 22.937 -1.429  1.00 23.93  ? 73   ASN A CG    1 
ATOM   479  O  OD1   . ASN A 1 73  ? 136.282 22.850 -0.977  1.00 13.19  ? 73   ASN A OD1   1 
ATOM   480  N  ND2   . ASN A 1 73  ? 137.726 22.646 -2.725  1.00 12.01  ? 73   ASN A ND2   1 
ATOM   481  N  N     . SER A 1 74  ? 140.290 24.932 1.387   1.00 10.96  ? 74   SER A N     1 
ATOM   482  C  CA    . SER A 1 74  ? 141.523 25.060 2.178   1.00 10.37  ? 74   SER A CA    1 
ATOM   483  C  C     . SER A 1 74  ? 141.281 25.454 3.637   1.00 13.77  ? 74   SER A C     1 
ATOM   484  O  O     . SER A 1 74  ? 141.790 24.780 4.541   1.00 13.57  ? 74   SER A O     1 
ATOM   485  C  CB    . SER A 1 74  ? 142.575 26.017 1.555   1.00 12.15  ? 74   SER A CB    1 
ATOM   486  O  OG    . SER A 1 74  ? 142.941 25.398 0.290   1.00 13.62  ? 74   SER A OG    1 
ATOM   487  N  N     . VAL A 1 75  ? 140.530 26.529 3.861   1.00 10.64  ? 75   VAL A N     1 
ATOM   488  C  CA    . VAL A 1 75  ? 140.255 26.987 5.213   1.00 11.81  ? 75   VAL A CA    1 
ATOM   489  C  C     . VAL A 1 75  ? 139.448 25.982 6.000   1.00 14.73  ? 75   VAL A C     1 
ATOM   490  O  O     . VAL A 1 75  ? 139.527 25.952 7.226   1.00 16.18  ? 75   VAL A O     1 
ATOM   491  C  CB    . VAL A 1 75  ? 139.685 28.423 5.268   1.00 20.84  ? 75   VAL A CB    1 
ATOM   492  C  CG1   . VAL A 1 75  ? 138.357 28.425 5.815   1.00 32.57  ? 75   VAL A CG1   1 
ATOM   493  C  CG2   . VAL A 1 75  ? 140.618 29.306 6.033   1.00 29.39  ? 75   VAL A CG2   1 
ATOM   494  N  N     . ARG A 1 76  ? 138.688 25.155 5.321   1.00 10.60  ? 76   ARG A N     1 
ATOM   495  C  CA    . ARG A 1 76  ? 137.902 24.173 6.048   1.00 10.88  ? 76   ARG A CA    1 
ATOM   496  C  C     . ARG A 1 76  ? 138.825 23.094 6.652   1.00 21.36  ? 76   ARG A C     1 
ATOM   497  O  O     . ARG A 1 76  ? 138.528 22.470 7.674   1.00 17.86  ? 76   ARG A O     1 
ATOM   498  C  CB    . ARG A 1 76  ? 136.800 23.563 5.144   1.00 11.61  ? 76   ARG A CB    1 
ATOM   499  C  CG    . ARG A 1 76  ? 135.518 24.515 5.055   1.00 16.93  ? 76   ARG A CG    1 
ATOM   500  C  CD    . ARG A 1 76  ? 134.250 23.718 4.767   1.00 31.59  ? 76   ARG A CD    1 
ATOM   501  N  NE    . ARG A 1 76  ? 134.649 22.781 3.866   1.00 34.57  ? 76   ARG A NE    1 
ATOM   502  C  CZ    . ARG A 1 76  ? 134.209 21.550 3.661   1.00 36.02  ? 76   ARG A CZ    1 
ATOM   503  N  NH1   . ARG A 1 76  ? 133.305 20.916 4.295   1.00 24.92  ? 76   ARG A NH1   1 
ATOM   504  N  NH2   . ARG A 1 76  ? 134.730 20.828 2.739   1.00 54.38  ? 76   ARG A NH2   1 
ATOM   505  N  N     . VAL A 1 77  ? 139.974 22.862 6.016   1.00 18.50  ? 77   VAL A N     1 
ATOM   506  C  CA    . VAL A 1 77  ? 140.933 21.864 6.514   1.00 14.08  ? 77   VAL A CA    1 
ATOM   507  C  C     . VAL A 1 77  ? 141.600 22.456 7.746   1.00 12.89  ? 77   VAL A C     1 
ATOM   508  O  O     . VAL A 1 77  ? 141.760 21.802 8.770   1.00 19.90  ? 77   VAL A O     1 
ATOM   509  C  CB    . VAL A 1 77  ? 142.021 21.561 5.459   1.00 20.84  ? 77   VAL A CB    1 
ATOM   510  C  CG1   . VAL A 1 77  ? 143.173 20.770 6.143   1.00 21.72  ? 77   VAL A CG1   1 
ATOM   511  C  CG2   . VAL A 1 77  ? 141.385 20.798 4.271   1.00 17.60  ? 77   VAL A CG2   1 
ATOM   512  N  N     . VAL A 1 78  ? 141.977 23.727 7.652   1.00 11.63  ? 78   VAL A N     1 
ATOM   513  C  CA    . VAL A 1 78  ? 142.608 24.387 8.793   1.00 12.37  ? 78   VAL A CA    1 
ATOM   514  C  C     . VAL A 1 78  ? 141.651 24.392 10.000  1.00 20.43  ? 78   VAL A C     1 
ATOM   515  O  O     . VAL A 1 78  ? 142.049 24.099 11.132  1.00 16.42  ? 78   VAL A O     1 
ATOM   516  C  CB    . VAL A 1 78  ? 142.904 25.837 8.485   1.00 15.36  ? 78   VAL A CB    1 
ATOM   517  C  CG1   . VAL A 1 78  ? 143.465 26.560 9.716   1.00 15.91  ? 78   VAL A CG1   1 
ATOM   518  C  CG2   . VAL A 1 78  ? 143.902 25.964 7.323   1.00 16.32  ? 78   VAL A CG2   1 
ATOM   519  N  N     . GLN A 1 79  ? 140.382 24.736 9.769   1.00 14.11  ? 79   GLN A N     1 
ATOM   520  C  CA    . GLN A 1 79  ? 139.414 24.775 10.873  1.00 13.87  ? 79   GLN A CA    1 
ATOM   521  C  C     . GLN A 1 79  ? 139.203 23.391 11.502  1.00 17.79  ? 79   GLN A C     1 
ATOM   522  O  O     . GLN A 1 79  ? 139.109 23.238 12.733  1.00 17.88  ? 79   GLN A O     1 
ATOM   523  C  CB    . GLN A 1 79  ? 138.113 25.369 10.354  1.00 15.33  ? 79   GLN A CB    1 
ATOM   524  C  CG    . GLN A 1 79  ? 136.986 25.163 11.389  1.00 18.69  ? 79   GLN A CG    1 
ATOM   525  C  CD    . GLN A 1 79  ? 137.147 25.992 12.671  1.00 20.03  ? 79   GLN A CD    1 
ATOM   526  O  OE1   . GLN A 1 79  ? 136.802 25.537 13.809  1.00 22.76  ? 79   GLN A OE1   1 
ATOM   527  N  NE2   . GLN A 1 79  ? 137.640 27.187 12.505  1.00 11.61  ? 79   GLN A NE2   1 
ATOM   528  N  N     . LYS A 1 80  ? 139.133 22.364 10.653  1.00 14.26  ? 80   LYS A N     1 
ATOM   529  C  CA    . LYS A 1 80  ? 138.933 20.997 11.124  1.00 14.60  ? 80   LYS A CA    1 
ATOM   530  C  C     . LYS A 1 80  ? 140.107 20.542 11.989  1.00 24.58  ? 80   LYS A C     1 
ATOM   531  O  O     . LYS A 1 80  ? 139.906 19.868 12.996  1.00 21.95  ? 80   LYS A O     1 
ATOM   532  C  CB    . LYS A 1 80  ? 138.736 20.034 9.933   1.00 16.31  ? 80   LYS A CB    1 
ATOM   533  C  CG    . LYS A 1 80  ? 138.571 18.521 10.217  1.00 26.30  ? 80   LYS A CG    1 
ATOM   534  C  CD    . LYS A 1 80  ? 137.326 18.190 11.055  1.00 56.74  ? 80   LYS A CD    1 
ATOM   535  C  CE    . LYS A 1 80  ? 136.087 17.830 10.229  1.00 87.10  ? 80   LYS A CE    1 
ATOM   536  N  NZ    . LYS A 1 80  ? 134.904 18.723 10.499  1.00 78.93  ? 80   LYS A NZ    1 
ATOM   537  N  N     . LEU A 1 81  ? 141.330 20.911 11.603  1.00 19.14  ? 81   LEU A N     1 
ATOM   538  C  CA    . LEU A 1 81  ? 142.517 20.509 12.375  1.00 21.81  ? 81   LEU A CA    1 
ATOM   539  C  C     . LEU A 1 81  ? 142.715 21.350 13.642  1.00 24.70  ? 81   LEU A C     1 
ATOM   540  O  O     . LEU A 1 81  ? 143.196 20.845 14.642  1.00 22.88  ? 81   LEU A O     1 
ATOM   541  C  CB    . LEU A 1 81  ? 143.751 20.559 11.470  1.00 21.90  ? 81   LEU A CB    1 
ATOM   542  C  CG    . LEU A 1 81  ? 143.610 19.571 10.322  1.00 21.47  ? 81   LEU A CG    1 
ATOM   543  C  CD1   . LEU A 1 81  ? 144.875 19.580 9.473   1.00 21.43  ? 81   LEU A CD1   1 
ATOM   544  C  CD2   . LEU A 1 81  ? 143.378 18.223 10.889  1.00 23.81  ? 81   LEU A CD2   1 
ATOM   545  N  N     . LEU A 1 82  ? 142.342 22.628 13.603  1.00 18.62  ? 82   LEU A N     1 
ATOM   546  C  CA    . LEU A 1 82  ? 142.478 23.513 14.761  1.00 19.76  ? 82   LEU A CA    1 
ATOM   547  C  C     . LEU A 1 82  ? 141.308 23.312 15.751  1.00 24.87  ? 82   LEU A C     1 
ATOM   548  O  O     . LEU A 1 82  ? 141.451 23.567 16.945  1.00 20.81  ? 82   LEU A O     1 
ATOM   549  C  CB    . LEU A 1 82  ? 142.589 24.935 14.276  1.00 19.76  ? 82   LEU A CB    1 
ATOM   550  C  CG    . LEU A 1 82  ? 143.970 25.532 14.199  1.00 27.56  ? 82   LEU A CG    1 
ATOM   551  C  CD1   . LEU A 1 82  ? 145.010 24.509 14.186  1.00 33.45  ? 82   LEU A CD1   1 
ATOM   552  C  CD2   . LEU A 1 82  ? 144.053 26.450 13.078  1.00 24.87  ? 82   LEU A CD2   1 
ATOM   553  N  N     . ARG A 1 83  ? 140.158 22.873 15.240  1.00 19.00  ? 83   ARG A N     1 
ATOM   554  C  CA    . ARG A 1 83  ? 138.929 22.588 16.017  1.00 23.15  ? 83   ARG A CA    1 
ATOM   555  C  C     . ARG A 1 83  ? 138.210 23.747 16.713  1.00 19.32  ? 83   ARG A C     1 
ATOM   556  O  O     . ARG A 1 83  ? 137.011 23.869 16.581  1.00 24.49  ? 83   ARG A O     1 
ATOM   557  C  CB    . ARG A 1 83  ? 139.144 21.569 17.120  1.00 24.53  ? 83   ARG A CB    1 
ATOM   558  C  CG    . ARG A 1 83  ? 140.013 20.463 16.687  1.00 42.92  ? 83   ARG A CG    1 
ATOM   559  C  CD    . ARG A 1 83  ? 140.039 19.428 17.740  1.00 43.37  ? 83   ARG A CD    1 
ATOM   560  N  NE    . ARG A 1 83  ? 139.666 18.217 17.087  1.00 55.40  ? 83   ARG A NE    1 
ATOM   561  C  CZ    . ARG A 1 83  ? 138.622 17.516 17.458  1.00 55.71  ? 83   ARG A CZ    1 
ATOM   562  N  NH1   . ARG A 1 83  ? 137.877 17.911 18.487  1.00 39.53  ? 83   ARG A NH1   1 
ATOM   563  N  NH2   . ARG A 1 83  ? 138.348 16.418 16.800  1.00 69.62  ? 83   ARG A NH2   1 
ATOM   564  N  N     . LYS A 1 84  ? 138.908 24.585 17.461  1.00 15.65  ? 84   LYS A N     1 
ATOM   565  C  CA    . LYS A 1 84  ? 138.238 25.688 18.157  1.00 16.91  ? 84   LYS A CA    1 
ATOM   566  C  C     . LYS A 1 84  ? 137.445 26.573 17.228  1.00 21.14  ? 84   LYS A C     1 
ATOM   567  O  O     . LYS A 1 84  ? 137.897 26.884 16.130  1.00 21.87  ? 84   LYS A O     1 
ATOM   568  C  CB    . LYS A 1 84  ? 139.149 26.437 19.042  1.00 21.75  ? 84   LYS A CB    1 
ATOM   569  C  CG    . LYS A 1 84  ? 139.522 25.514 20.211  1.00 40.32  ? 84   LYS A CG    1 
ATOM   570  C  CD    . LYS A 1 84  ? 140.931 24.984 20.098  1.00 77.84  ? 84   LYS A CD    1 
ATOM   571  C  CE    . LYS A 1 84  ? 141.766 25.758 21.094  1.00 82.12  ? 84   LYS A CE    1 
ATOM   572  N  NZ    . LYS A 1 84  ? 140.801 26.710 21.695  1.00 47.48  ? 84   LYS A NZ    1 
ATOM   573  N  N     . PRO A 1 85  ? 136.271 26.983 17.673  1.00 18.83  ? 85   PRO A N     1 
ATOM   574  C  CA    . PRO A 1 85  ? 135.435 27.829 16.831  1.00 17.32  ? 85   PRO A CA    1 
ATOM   575  C  C     . PRO A 1 85  ? 136.144 29.076 16.390  1.00 20.96  ? 85   PRO A C     1 
ATOM   576  O  O     . PRO A 1 85  ? 136.850 29.707 17.173  1.00 18.02  ? 85   PRO A O     1 
ATOM   577  C  CB    . PRO A 1 85  ? 134.252 28.291 17.751  1.00 18.98  ? 85   PRO A CB    1 
ATOM   578  C  CG    . PRO A 1 85  ? 134.404 27.490 19.030  1.00 26.45  ? 85   PRO A CG    1 
ATOM   579  C  CD    . PRO A 1 85  ? 135.854 27.060 19.102  1.00 22.23  ? 85   PRO A CD    1 
ATOM   580  N  N     . GLY A 1 86  ? 135.947 29.444 15.128  1.00 16.13  ? 86   GLY A N     1 
ATOM   581  C  CA    . GLY A 1 86  ? 136.582 30.660 14.631  1.00 12.65  ? 86   GLY A CA    1 
ATOM   582  C  C     . GLY A 1 86  ? 138.084 30.547 14.437  1.00 15.89  ? 86   GLY A C     1 
ATOM   583  O  O     . GLY A 1 86  ? 138.732 31.575 14.250  1.00 19.18  ? 86   GLY A O     1 
ATOM   584  N  N     . SER A 1 87  ? 138.630 29.332 14.449  1.00 14.45  ? 87   SER A N     1 
ATOM   585  C  CA    . SER A 1 87  ? 140.080 29.162 14.243  1.00 17.19  ? 87   SER A CA    1 
ATOM   586  C  C     . SER A 1 87  ? 140.466 29.673 12.845  1.00 20.54  ? 87   SER A C     1 
ATOM   587  O  O     . SER A 1 87  ? 141.579 30.166 12.616  1.00 16.21  ? 87   SER A O     1 
ATOM   588  C  CB    . SER A 1 87  ? 140.522 27.728 14.448  1.00 17.83  ? 87   SER A CB    1 
ATOM   589  O  OG    . SER A 1 87  ? 140.363 27.420 15.829  1.00 18.62  ? 87   SER A OG    1 
ATOM   590  N  N     . ALA A 1 88  ? 139.528 29.542 11.912  1.00 14.11  ? 88   ALA A N     1 
ATOM   591  C  CA    . ALA A 1 88  ? 139.724 30.011 10.535  1.00 15.92  ? 88   ALA A CA    1 
ATOM   592  C  C     . ALA A 1 88  ? 138.545 30.925 10.209  1.00 19.16  ? 88   ALA A C     1 
ATOM   593  O  O     . ALA A 1 88  ? 137.419 30.647 10.626  1.00 15.14  ? 88   ALA A O     1 
ATOM   594  C  CB    . ALA A 1 88  ? 139.829 28.877 9.479   1.00 18.36  ? 88   ALA A CB    1 
ATOM   595  N  N     . GLY A 1 89  ? 138.820 32.003 9.486   1.00 14.00  ? 89   GLY A N     1 
ATOM   596  C  CA    . GLY A 1 89  ? 137.806 32.975 9.105   1.00 13.99  ? 89   GLY A CA    1 
ATOM   597  C  C     . GLY A 1 89  ? 137.724 33.060 7.591   1.00 18.95  ? 89   GLY A C     1 
ATOM   598  O  O     . GLY A 1 89  ? 138.729 32.802 6.906   1.00 14.17  ? 89   GLY A O     1 
ATOM   599  N  N     . TYR A 1 90  ? 136.539 33.386 7.067   1.00 11.89  ? 90   TYR A N     1 
ATOM   600  C  CA    . TYR A 1 90  ? 136.395 33.449 5.613   1.00 8.35   ? 90   TYR A CA    1 
ATOM   601  C  C     . TYR A 1 90  ? 135.297 34.403 5.181   1.00 12.42  ? 90   TYR A C     1 
ATOM   602  O  O     . TYR A 1 90  ? 134.255 34.473 5.828   1.00 14.34  ? 90   TYR A O     1 
ATOM   603  C  CB    . TYR A 1 90  ? 135.912 32.047 5.207   1.00 10.45  ? 90   TYR A CB    1 
ATOM   604  C  CG    . TYR A 1 90  ? 135.625 31.870 3.724   1.00 13.07  ? 90   TYR A CG    1 
ATOM   605  C  CD1   . TYR A 1 90  ? 136.646 31.468 2.846   1.00 12.78  ? 90   TYR A CD1   1 
ATOM   606  C  CD2   . TYR A 1 90  ? 134.337 32.142 3.181   1.00 13.74  ? 90   TYR A CD2   1 
ATOM   607  C  CE1   . TYR A 1 90  ? 136.418 31.296 1.474   1.00 11.00  ? 90   TYR A CE1   1 
ATOM   608  C  CE2   . TYR A 1 90  ? 134.110 31.980 1.825   1.00 13.36  ? 90   TYR A CE2   1 
ATOM   609  C  CZ    . TYR A 1 90  ? 135.145 31.563 0.950   1.00 11.92  ? 90   TYR A CZ    1 
ATOM   610  O  OH    . TYR A 1 90  ? 134.894 31.370 -0.443  1.00 13.79  ? 90   TYR A OH    1 
ATOM   611  N  N     . MET A 1 91  ? 135.556 35.124 4.091   1.00 8.79   ? 91   MET A N     1 
ATOM   612  C  CA    . MET A 1 91  ? 134.596 36.073 3.533   1.00 9.63   ? 91   MET A CA    1 
ATOM   613  C  C     . MET A 1 91  ? 134.424 35.809 2.048   1.00 14.82  ? 91   MET A C     1 
ATOM   614  O  O     . MET A 1 91  ? 135.394 35.498 1.363   1.00 13.05  ? 91   MET A O     1 
ATOM   615  C  CB    . MET A 1 91  ? 134.930 37.529 3.743   1.00 11.81  ? 91   MET A CB    1 
ATOM   616  C  CG    . MET A 1 91  ? 134.754 37.892 5.244   1.00 12.19  ? 91   MET A CG    1 
ATOM   617  S  SD    . MET A 1 91  ? 135.064 39.648 5.377   1.00 19.37  ? 91   MET A SD    1 
ATOM   618  C  CE    . MET A 1 91  ? 134.530 39.990 7.065   1.00 20.57  ? 91   MET A CE    1 
ATOM   619  N  N     . GLY A 1 92  ? 133.194 35.922 1.551   1.00 8.38   ? 92   GLY A N     1 
ATOM   620  C  CA    . GLY A 1 92  ? 132.952 35.694 0.135   1.00 10.20  ? 92   GLY A CA    1 
ATOM   621  C  C     . GLY A 1 92  ? 131.524 36.102 -0.129  1.00 17.17  ? 92   GLY A C     1 
ATOM   622  O  O     . GLY A 1 92  ? 130.868 36.528 0.807   1.00 12.72  ? 92   GLY A O     1 
ATOM   623  N  N     . ALA A 1 93  ? 131.044 35.974 -1.359  1.00 10.14  ? 93   ALA A N     1 
ATOM   624  C  CA    . ALA A 1 93  ? 129.648 36.361 -1.605  1.00 10.51  ? 93   ALA A CA    1 
ATOM   625  C  C     . ALA A 1 93  ? 128.837 35.179 -2.100  1.00 13.94  ? 93   ALA A C     1 
ATOM   626  O  O     . ALA A 1 93  ? 129.293 34.445 -2.968  1.00 11.91  ? 93   ALA A O     1 
ATOM   627  C  CB    . ALA A 1 93  ? 129.595 37.461 -2.659  1.00 11.50  ? 93   ALA A CB    1 
ATOM   628  N  N     . ILE A 1 94  ? 127.640 34.996 -1.550  1.00 13.38  ? 94   ILE A N     1 
ATOM   629  C  CA    . ILE A 1 94  ? 126.757 33.903 -1.961  1.00 13.63  ? 94   ILE A CA    1 
ATOM   630  C  C     . ILE A 1 94  ? 125.473 34.547 -2.529  1.00 18.64  ? 94   ILE A C     1 
ATOM   631  O  O     . ILE A 1 94  ? 125.260 35.743 -2.310  1.00 13.83  ? 94   ILE A O     1 
ATOM   632  C  CB    . ILE A 1 94  ? 126.353 32.969 -0.807  1.00 13.26  ? 94   ILE A CB    1 
ATOM   633  C  CG1   . ILE A 1 94  ? 125.898 33.803 0.391   1.00 13.67  ? 94   ILE A CG1   1 
ATOM   634  C  CG2   . ILE A 1 94  ? 127.485 32.009 -0.523  1.00 16.07  ? 94   ILE A CG2   1 
ATOM   635  C  CD1   . ILE A 1 94  ? 125.239 32.954 1.518   1.00 15.08  ? 94   ILE A CD1   1 
ATOM   636  N  N     . GLY A 1 95  ? 124.635 33.787 -3.254  1.00 14.63  ? 95   GLY A N     1 
ATOM   637  C  CA    . GLY A 1 95  ? 123.415 34.383 -3.787  1.00 16.89  ? 95   GLY A CA    1 
ATOM   638  C  C     . GLY A 1 95  ? 122.312 34.248 -2.720  1.00 23.74  ? 95   GLY A C     1 
ATOM   639  O  O     . GLY A 1 95  ? 122.523 33.592 -1.695  1.00 19.88  ? 95   GLY A O     1 
ATOM   640  N  N     . ASP A 1 96  ? 121.146 34.849 -2.942  1.00 18.39  ? 96   ASP A N     1 
ATOM   641  C  CA    . ASP A 1 96  ? 120.088 34.729 -1.962  1.00 18.82  ? 96   ASP A CA    1 
ATOM   642  C  C     . ASP A 1 96  ? 119.252 33.518 -2.323  1.00 23.39  ? 96   ASP A C     1 
ATOM   643  O  O     . ASP A 1 96  ? 118.077 33.617 -2.666  1.00 24.14  ? 96   ASP A O     1 
ATOM   644  C  CB    . ASP A 1 96  ? 119.496 35.937 -2.110  1.00 23.98  ? 96   ASP A CB    1 
ATOM   645  C  CG    . ASP A 1 96  ? 118.828 36.346 -1.253  1.00 78.05  ? 96   ASP A CG    1 
ATOM   646  O  OD1   . ASP A 1 96  ? 119.790 37.634 -1.194  1.00 100.00 ? 96   ASP A OD1   1 
ATOM   647  O  OD2   . ASP A 1 96  ? 117.659 35.945 -1.146  1.00 100.00 ? 96   ASP A OD2   1 
ATOM   648  N  N     . ASP A 1 97  ? 119.855 32.345 -2.264  1.00 22.35  ? 97   ASP A N     1 
ATOM   649  C  CA    . ASP A 1 97  ? 119.092 31.157 -2.626  1.00 17.06  ? 97   ASP A CA    1 
ATOM   650  C  C     . ASP A 1 97  ? 119.361 29.959 -1.743  1.00 19.43  ? 97   ASP A C     1 
ATOM   651  O  O     . ASP A 1 97  ? 120.250 29.946 -0.890  1.00 20.56  ? 97   ASP A O     1 
ATOM   652  C  CB    . ASP A 1 97  ? 119.440 30.875 -4.096  1.00 20.11  ? 97   ASP A CB    1 
ATOM   653  C  CG    . ASP A 1 97  ? 120.977 30.738 -4.308  1.00 31.97  ? 97   ASP A CG    1 
ATOM   654  O  OD1   . ASP A 1 97  ? 121.407 30.549 -5.465  1.00 25.45  ? 97   ASP A OD1   1 
ATOM   655  O  OD2   . ASP A 1 97  ? 121.757 30.784 -3.304  1.00 21.96  ? 97   ASP A OD2   1 
ATOM   656  N  N     . PRO A 1 98  ? 118.579 28.926 -1.955  1.00 20.10  ? 98   PRO A N     1 
ATOM   657  C  CA    . PRO A 1 98  ? 118.734 27.719 -1.183  1.00 22.07  ? 98   PRO A CA    1 
ATOM   658  C  C     . PRO A 1 98  ? 120.151 27.185 -1.267  1.00 23.35  ? 98   PRO A C     1 
ATOM   659  O  O     . PRO A 1 98  ? 120.682 26.592 -0.328  1.00 24.55  ? 98   PRO A O     1 
ATOM   660  C  CB    . PRO A 1 98  ? 117.735 26.757 -1.867  1.00 21.43  ? 98   PRO A CB    1 
ATOM   661  C  CG    . PRO A 1 98  ? 116.669 27.702 -2.281  1.00 22.79  ? 98   PRO A CG    1 
ATOM   662  C  CD    . PRO A 1 98  ? 117.432 28.848 -2.861  1.00 20.92  ? 98   PRO A CD    1 
ATOM   663  N  N     . ARG A 1 99  ? 120.786 27.386 -2.395  1.00 19.31  ? 99   ARG A N     1 
ATOM   664  C  CA    . ARG A 1 99  ? 122.144 26.886 -2.528  1.00 20.85  ? 99   ARG A CA    1 
ATOM   665  C  C     . ARG A 1 99  ? 123.089 27.641 -1.576  1.00 16.74  ? 99   ARG A C     1 
ATOM   666  O  O     . ARG A 1 99  ? 123.962 27.061 -0.930  1.00 18.42  ? 99   ARG A O     1 
ATOM   667  C  CB    . ARG A 1 99  ? 122.518 26.960 -4.004  1.00 23.87  ? 99   ARG A CB    1 
ATOM   668  C  CG    . ARG A 1 99  ? 123.916 26.604 -4.234  1.00 28.47  ? 99   ARG A CG    1 
ATOM   669  C  CD    . ARG A 1 99  ? 124.252 26.915 -5.654  1.00 42.87  ? 99   ARG A CD    1 
ATOM   670  N  NE    . ARG A 1 99  ? 123.588 25.941 -6.504  1.00 31.26  ? 99   ARG A NE    1 
ATOM   671  C  CZ    . ARG A 1 99  ? 123.142 26.244 -7.711  1.00 52.95  ? 99   ARG A CZ    1 
ATOM   672  N  NH1   . ARG A 1 99  ? 123.283 27.499 -8.171  1.00 34.94  ? 99   ARG A NH1   1 
ATOM   673  N  NH2   . ARG A 1 99  ? 122.562 25.301 -8.437  1.00 31.88  ? 99   ARG A NH2   1 
ATOM   674  N  N     . GLY A 1 100 ? 122.906 28.934 -1.502  1.00 14.70  ? 100  GLY A N     1 
ATOM   675  C  CA    . GLY A 1 100 ? 123.738 29.735 -0.625  1.00 14.21  ? 100  GLY A CA    1 
ATOM   676  C  C     . GLY A 1 100 ? 123.499 29.316 0.820   1.00 26.27  ? 100  GLY A C     1 
ATOM   677  O  O     . GLY A 1 100 ? 124.437 29.254 1.643   1.00 20.03  ? 100  GLY A O     1 
ATOM   678  N  N     . GLN A 1 101 ? 122.236 29.008 1.142   1.00 18.78  ? 101  GLN A N     1 
ATOM   679  C  CA    . GLN A 1 101 ? 121.925 28.590 2.497   1.00 16.29  ? 101  GLN A CA    1 
ATOM   680  C  C     . GLN A 1 101 ? 122.633 27.299 2.861   1.00 21.82  ? 101  GLN A C     1 
ATOM   681  O  O     . GLN A 1 101 ? 123.068 27.128 3.992   1.00 25.34  ? 101  GLN A O     1 
ATOM   682  C  CB    . GLN A 1 101 ? 120.452 28.632 2.779   1.00 20.57  ? 101  GLN A CB    1 
ATOM   683  C  CG    . GLN A 1 101 ? 120.062 30.151 2.630   1.00 35.15  ? 101  GLN A CG    1 
ATOM   684  C  CD    . GLN A 1 101 ? 121.011 31.091 3.385   1.00 94.18  ? 101  GLN A CD    1 
ATOM   685  O  OE1   . GLN A 1 101 ? 121.315 30.854 4.556   1.00 100.00 ? 101  GLN A OE1   1 
ATOM   686  N  NE2   . GLN A 1 101 ? 121.482 32.163 2.723   1.00 76.92  ? 101  GLN A NE2   1 
ATOM   687  N  N     . VAL A 1 102 ? 122.776 26.380 1.921   1.00 17.50  ? 102  VAL A N     1 
ATOM   688  C  CA    . VAL A 1 102 ? 123.456 25.122 2.228   1.00 21.82  ? 102  VAL A CA    1 
ATOM   689  C  C     . VAL A 1 102 ? 124.931 25.340 2.567   1.00 20.83  ? 102  VAL A C     1 
ATOM   690  O  O     . VAL A 1 102 ? 125.502 24.713 3.475   1.00 17.34  ? 102  VAL A O     1 
ATOM   691  C  CB    . VAL A 1 102 ? 123.431 24.184 1.031   1.00 32.21  ? 102  VAL A CB    1 
ATOM   692  C  CG1   . VAL A 1 102 ? 124.288 22.974 1.347   1.00 35.87  ? 102  VAL A CG1   1 
ATOM   693  C  CG2   . VAL A 1 102 ? 122.029 23.731 0.838   1.00 29.66  ? 102  VAL A CG2   1 
ATOM   694  N  N     . LEU A 1 103 ? 125.568 26.242 1.828   1.00 16.60  ? 103  LEU A N     1 
ATOM   695  C  CA    . LEU A 1 103 ? 126.974 26.524 2.088   1.00 19.05  ? 103  LEU A CA    1 
ATOM   696  C  C     . LEU A 1 103 ? 127.118 27.175 3.454   1.00 22.12  ? 103  LEU A C     1 
ATOM   697  O  O     . LEU A 1 103 ? 127.982 26.806 4.240   1.00 22.07  ? 103  LEU A O     1 
ATOM   698  C  CB    . LEU A 1 103 ? 127.700 27.443 1.057   1.00 18.28  ? 103  LEU A CB    1 
ATOM   699  C  CG    . LEU A 1 103 ? 127.918 26.846 -0.320  1.00 20.50  ? 103  LEU A CG    1 
ATOM   700  C  CD1   . LEU A 1 103 ? 128.465 27.861 -1.232  1.00 18.68  ? 103  LEU A CD1   1 
ATOM   701  C  CD2   . LEU A 1 103 ? 128.762 25.610 -0.295  1.00 28.60  ? 103  LEU A CD2   1 
ATOM   702  N  N     . LYS A 1 104 ? 126.257 28.144 3.731   1.00 17.25  ? 104  LYS A N     1 
ATOM   703  C  CA    . LYS A 1 104 ? 126.288 28.846 5.003   1.00 18.00  ? 104  LYS A CA    1 
ATOM   704  C  C     . LYS A 1 104 ? 126.090 27.898 6.178   1.00 20.03  ? 104  LYS A C     1 
ATOM   705  O  O     . LYS A 1 104 ? 126.868 27.915 7.139   1.00 23.53  ? 104  LYS A O     1 
ATOM   706  C  CB    . LYS A 1 104 ? 125.245 29.942 5.016   1.00 23.90  ? 104  LYS A CB    1 
ATOM   707  C  CG    . LYS A 1 104 ? 125.064 30.463 6.434   1.00 34.49  ? 104  LYS A CG    1 
ATOM   708  C  CD    . LYS A 1 104 ? 125.293 31.917 6.485   1.00 36.16  ? 104  LYS A CD    1 
ATOM   709  C  CE    . LYS A 1 104 ? 125.793 32.269 7.888   1.00 40.69  ? 104  LYS A CE    1 
ATOM   710  N  NZ    . LYS A 1 104 ? 124.765 32.048 8.897   1.00 51.32  ? 104  LYS A NZ    1 
ATOM   711  N  N     . GLU A 1 105 ? 125.057 27.069 6.101   1.00 18.53  ? 105  GLU A N     1 
ATOM   712  C  CA    . GLU A 1 105 ? 124.773 26.121 7.171   1.00 21.27  ? 105  GLU A CA    1 
ATOM   713  C  C     . GLU A 1 105 ? 125.955 25.213 7.413   1.00 22.35  ? 105  GLU A C     1 
ATOM   714  O  O     . GLU A 1 105 ? 126.281 24.870 8.555   1.00 20.73  ? 105  GLU A O     1 
ATOM   715  C  CB    . GLU A 1 105 ? 123.653 25.128 6.798   1.00 22.74  ? 105  GLU A CB    1 
ATOM   716  C  CG    . GLU A 1 105 ? 122.346 25.465 7.445   1.00 48.05  ? 105  GLU A CG    1 
ATOM   717  C  CD    . GLU A 1 105 ? 121.468 24.246 7.677   1.00 75.11  ? 105  GLU A CD    1 
ATOM   718  O  OE1   . GLU A 1 105 ? 120.905 23.784 6.682   1.00 51.49  ? 105  GLU A OE1   1 
ATOM   719  O  OE2   . GLU A 1 105 ? 121.359 23.754 8.821   1.00 73.81  ? 105  GLU A OE2   1 
ATOM   720  N  N     . LEU A 1 106 ? 126.590 24.798 6.332   1.00 18.55  ? 106  LEU A N     1 
ATOM   721  C  CA    . LEU A 1 106 ? 127.744 23.918 6.454   1.00 19.20  ? 106  LEU A CA    1 
ATOM   722  C  C     . LEU A 1 106 ? 128.907 24.618 7.171   1.00 18.44  ? 106  LEU A C     1 
ATOM   723  O  O     . LEU A 1 106 ? 129.572 24.016 8.003   1.00 19.11  ? 106  LEU A O     1 
ATOM   724  C  CB    . LEU A 1 106 ? 128.077 23.327 5.092   1.00 24.92  ? 106  LEU A CB    1 
ATOM   725  C  CG    . LEU A 1 106 ? 126.945 22.410 4.451   1.00 42.44  ? 106  LEU A CG    1 
ATOM   726  C  CD1   . LEU A 1 106 ? 125.501 22.410 5.054   1.00 36.20  ? 106  LEU A CD1   1 
ATOM   727  C  CD2   . LEU A 1 106 ? 126.945 22.393 2.902   1.00 55.60  ? 106  LEU A CD2   1 
ATOM   728  N  N     . CYS A 1 107 ? 129.172 25.886 6.879   1.00 12.57  ? 107  CYS A N     1 
ATOM   729  C  CA    . CYS A 1 107 ? 130.268 26.569 7.549   1.00 13.60  ? 107  CYS A CA    1 
ATOM   730  C  C     . CYS A 1 107 ? 129.973 26.713 9.043   1.00 21.58  ? 107  CYS A C     1 
ATOM   731  O  O     . CYS A 1 107 ? 130.843 26.516 9.894   1.00 21.46  ? 107  CYS A O     1 
ATOM   732  C  CB    . CYS A 1 107 ? 130.475 27.951 6.938   1.00 17.79  ? 107  CYS A CB    1 
ATOM   733  S  SG    . CYS A 1 107 ? 131.136 27.775 5.205   1.00 21.57  ? 107  CYS A SG    1 
ATOM   734  N  N     . ASP A 1 108 ? 128.729 27.065 9.366   1.00 21.43  ? 108  ASP A N     1 
ATOM   735  C  CA    . ASP A 1 108 ? 128.341 27.215 10.771  1.00 20.67  ? 108  ASP A CA    1 
ATOM   736  C  C     . ASP A 1 108 ? 128.541 25.893 11.519  1.00 15.47  ? 108  ASP A C     1 
ATOM   737  O  O     . ASP A 1 108 ? 129.102 25.848 12.597  1.00 19.32  ? 108  ASP A O     1 
ATOM   738  C  CB    . ASP A 1 108 ? 126.849 27.600 10.880  1.00 16.64  ? 108  ASP A CB    1 
ATOM   739  C  CG    . ASP A 1 108 ? 126.578 29.007 10.446  1.00 23.99  ? 108  ASP A CG    1 
ATOM   740  O  OD1   . ASP A 1 108 ? 127.525 29.836 10.252  1.00 20.38  ? 108  ASP A OD1   1 
ATOM   741  O  OD2   . ASP A 1 108 ? 125.373 29.313 10.263  1.00 27.55  ? 108  ASP A OD2   1 
ATOM   742  N  N     . LYS A 1 109 ? 128.090 24.805 10.944  1.00 13.39  ? 109  LYS A N     1 
ATOM   743  C  CA    . LYS A 1 109 ? 128.233 23.514 11.588  1.00 13.23  ? 109  LYS A CA    1 
ATOM   744  C  C     . LYS A 1 109 ? 129.673 23.069 11.733  1.00 18.88  ? 109  LYS A C     1 
ATOM   745  O  O     . LYS A 1 109 ? 129.960 22.215 12.555  1.00 18.37  ? 109  LYS A O     1 
ATOM   746  C  CB    . LYS A 1 109 ? 127.586 22.439 10.722  1.00 19.62  ? 109  LYS A CB    1 
ATOM   747  C  CG    . LYS A 1 109 ? 126.853 21.345 11.487  1.00 74.07  ? 109  LYS A CG    1 
ATOM   748  C  CD    . LYS A 1 109 ? 127.007 19.968 10.815  1.00 79.39  ? 109  LYS A CD    1 
ATOM   749  C  CE    . LYS A 1 109 ? 125.817 19.038 11.077  1.00 67.62  ? 109  LYS A CE    1 
ATOM   750  N  NZ    . LYS A 1 109 ? 126.254 17.611 11.127  1.00 100.00 ? 109  LYS A NZ    1 
ATOM   751  N  N     . GLU A 1 110 ? 130.580 23.622 10.938  1.00 13.59  ? 110  GLU A N     1 
ATOM   752  C  CA    . GLU A 1 110 ? 131.979 23.244 11.015  1.00 11.86  ? 110  GLU A CA    1 
ATOM   753  C  C     . GLU A 1 110 ? 132.747 24.134 11.971  1.00 18.58  ? 110  GLU A C     1 
ATOM   754  O  O     . GLU A 1 110 ? 133.902 23.868 12.283  1.00 17.17  ? 110  GLU A O     1 
ATOM   755  C  CB    . GLU A 1 110 ? 132.666 23.121 9.634   1.00 12.97  ? 110  GLU A CB    1 
ATOM   756  C  CG    . GLU A 1 110 ? 132.202 21.829 8.988   1.00 14.38  ? 110  GLU A CG    1 
ATOM   757  C  CD    . GLU A 1 110 ? 132.805 21.640 7.636   1.00 34.57  ? 110  GLU A CD    1 
ATOM   758  O  OE1   . GLU A 1 110 ? 132.370 20.814 6.842   1.00 22.37  ? 110  GLU A OE1   1 
ATOM   759  O  OE2   . GLU A 1 110 ? 133.740 22.374 7.328   1.00 22.18  ? 110  GLU A OE2   1 
ATOM   760  N  N     . GLY A 1 111 ? 132.114 25.195 12.439  1.00 17.95  ? 111  GLY A N     1 
ATOM   761  C  CA    . GLY A 1 111 ? 132.765 26.103 13.383  1.00 14.25  ? 111  GLY A CA    1 
ATOM   762  C  C     . GLY A 1 111 ? 133.580 27.201 12.725  1.00 21.36  ? 111  GLY A C     1 
ATOM   763  O  O     . GLY A 1 111 ? 134.304 27.956 13.394  1.00 17.08  ? 111  GLY A O     1 
ATOM   764  N  N     . LEU A 1 112 ? 133.495 27.326 11.414  1.00 15.15  ? 112  LEU A N     1 
ATOM   765  C  CA    . LEU A 1 112 ? 134.283 28.395 10.799  1.00 13.40  ? 112  LEU A CA    1 
ATOM   766  C  C     . LEU A 1 112 ? 133.645 29.746 11.084  1.00 13.78  ? 112  LEU A C     1 
ATOM   767  O  O     . LEU A 1 112 ? 132.427 29.869 11.192  1.00 17.30  ? 112  LEU A O     1 
ATOM   768  C  CB    . LEU A 1 112 ? 134.114 28.286 9.272   1.00 15.90  ? 112  LEU A CB    1 
ATOM   769  C  CG    . LEU A 1 112 ? 135.123 27.632 8.339   1.00 27.18  ? 112  LEU A CG    1 
ATOM   770  C  CD1   . LEU A 1 112 ? 134.628 27.857 6.885   1.00 30.64  ? 112  LEU A CD1   1 
ATOM   771  C  CD2   . LEU A 1 112 ? 136.441 28.338 8.439   1.00 22.89  ? 112  LEU A CD2   1 
ATOM   772  N  N     . ALA A 1 113 ? 134.451 30.779 11.168  1.00 12.01  ? 113  ALA A N     1 
ATOM   773  C  CA    . ALA A 1 113 ? 133.919 32.106 11.385  1.00 13.28  ? 113  ALA A CA    1 
ATOM   774  C  C     . ALA A 1 113 ? 133.715 32.668 9.975   1.00 19.64  ? 113  ALA A C     1 
ATOM   775  O  O     . ALA A 1 113 ? 134.638 32.653 9.154   1.00 16.57  ? 113  ALA A O     1 
ATOM   776  C  CB    . ALA A 1 113 ? 134.859 33.049 12.139  1.00 15.10  ? 113  ALA A CB    1 
ATOM   777  N  N     . THR A 1 114 ? 132.526 33.157 9.666   1.00 16.21  ? 114  THR A N     1 
ATOM   778  C  CA    . THR A 1 114 ? 132.299 33.694 8.329   1.00 12.27  ? 114  THR A CA    1 
ATOM   779  C  C     . THR A 1 114 ? 131.435 34.932 8.365   1.00 21.21  ? 114  THR A C     1 
ATOM   780  O  O     . THR A 1 114 ? 130.667 35.172 9.294   1.00 14.91  ? 114  THR A O     1 
ATOM   781  C  CB    . THR A 1 114 ? 131.446 32.703 7.451   1.00 14.65  ? 114  THR A CB    1 
ATOM   782  O  OG1   . THR A 1 114 ? 130.151 32.502 8.039   1.00 17.47  ? 114  THR A OG1   1 
ATOM   783  C  CG2   . THR A 1 114 ? 132.102 31.328 7.216   1.00 14.05  ? 114  THR A CG2   1 
ATOM   784  N  N     . ARG A 1 115 ? 131.579 35.722 7.328   1.00 12.81  ? 115  ARG A N     1 
ATOM   785  C  CA    . ARG A 1 115 ? 130.826 36.936 7.150   1.00 14.46  ? 115  ARG A CA    1 
ATOM   786  C  C     . ARG A 1 115 ? 130.487 36.914 5.673   1.00 19.05  ? 115  ARG A C     1 
ATOM   787  O  O     . ARG A 1 115 ? 131.175 37.529 4.865   1.00 22.19  ? 115  ARG A O     1 
ATOM   788  C  CB    . ARG A 1 115 ? 131.568 38.210 7.578   1.00 19.20  ? 115  ARG A CB    1 
ATOM   789  C  CG    . ARG A 1 115 ? 130.659 38.965 8.563   1.00 48.83  ? 115  ARG A CG    1 
ATOM   790  C  CD    . ARG A 1 115 ? 130.443 40.447 8.266   1.00 42.70  ? 115  ARG A CD    1 
ATOM   791  N  NE    . ARG A 1 115 ? 131.247 41.066 9.300   1.00 36.26  ? 115  ARG A NE    1 
ATOM   792  C  CZ    . ARG A 1 115 ? 131.749 42.292 9.288   1.00 32.30  ? 115  ARG A CZ    1 
ATOM   793  N  NH1   . ARG A 1 115 ? 131.549 43.155 8.262   1.00 33.57  ? 115  ARG A NH1   1 
ATOM   794  N  NH2   . ARG A 1 115 ? 132.470 42.626 10.354  1.00 33.38  ? 115  ARG A NH2   1 
ATOM   795  N  N     . PHE A 1 116 ? 129.451 36.185 5.299   1.00 10.53  ? 116  PHE A N     1 
ATOM   796  C  CA    . PHE A 1 116 ? 129.109 36.150 3.884   1.00 10.67  ? 116  PHE A CA    1 
ATOM   797  C  C     . PHE A 1 116 ? 128.293 37.355 3.455   1.00 18.58  ? 116  PHE A C     1 
ATOM   798  O  O     . PHE A 1 116 ? 127.404 37.848 4.171   1.00 17.32  ? 116  PHE A O     1 
ATOM   799  C  CB    . PHE A 1 116 ? 128.193 34.981 3.591   1.00 11.64  ? 116  PHE A CB    1 
ATOM   800  C  CG    . PHE A 1 116 ? 128.865 33.666 3.562   1.00 13.47  ? 116  PHE A CG    1 
ATOM   801  C  CD1   . PHE A 1 116 ? 128.643 32.737 4.528   1.00 13.45  ? 116  PHE A CD1   1 
ATOM   802  C  CD2   . PHE A 1 116 ? 129.764 33.334 2.517   1.00 17.52  ? 116  PHE A CD2   1 
ATOM   803  C  CE1   . PHE A 1 116 ? 129.294 31.492 4.488   1.00 14.65  ? 116  PHE A CE1   1 
ATOM   804  C  CE2   . PHE A 1 116 ? 130.406 32.101 2.460   1.00 13.13  ? 116  PHE A CE2   1 
ATOM   805  C  CZ    . PHE A 1 116 ? 130.181 31.187 3.432   1.00 12.23  ? 116  PHE A CZ    1 
ATOM   806  N  N     . MET A 1 117 ? 128.600 37.831 2.269   1.00 12.96  ? 117  MET A N     1 
ATOM   807  C  CA    . MET A 1 117 ? 127.885 38.955 1.702   1.00 11.96  ? 117  MET A CA    1 
ATOM   808  C  C     . MET A 1 117 ? 126.816 38.270 0.847   1.00 17.79  ? 117  MET A C     1 
ATOM   809  O  O     . MET A 1 117 ? 127.092 37.282 0.167   1.00 17.31  ? 117  MET A O     1 
ATOM   810  C  CB    . MET A 1 117 ? 128.806 39.772 0.779   1.00 13.15  ? 117  MET A CB    1 
ATOM   811  C  CG    . MET A 1 117 ? 128.076 40.821 -0.013  1.00 23.68  ? 117  MET A CG    1 
ATOM   812  S  SD    . MET A 1 117 ? 129.215 41.705 -1.215  1.00 31.30  ? 117  MET A SD    1 
ATOM   813  C  CE    . MET A 1 117 ? 130.060 40.172 -1.413  1.00 39.40  ? 117  MET A CE    1 
ATOM   814  N  N     . VAL A 1 118 ? 125.590 38.752 0.870   1.00 13.73  ? 118  VAL A N     1 
ATOM   815  C  CA    . VAL A 1 118 ? 124.588 38.100 0.061   1.00 17.74  ? 118  VAL A CA    1 
ATOM   816  C  C     . VAL A 1 118 ? 124.274 38.998 -1.113  1.00 22.17  ? 118  VAL A C     1 
ATOM   817  O  O     . VAL A 1 118 ? 124.021 40.187 -0.944  1.00 24.04  ? 118  VAL A O     1 
ATOM   818  C  CB    . VAL A 1 118 ? 123.280 37.767 0.822   1.00 25.15  ? 118  VAL A CB    1 
ATOM   819  C  CG1   . VAL A 1 118 ? 122.285 37.228 -0.146  1.00 26.84  ? 118  VAL A CG1   1 
ATOM   820  C  CG2   . VAL A 1 118 ? 123.492 36.667 1.841   1.00 23.85  ? 118  VAL A CG2   1 
ATOM   821  N  N     . ALA A 1 119 ? 124.305 38.433 -2.297  1.00 23.61  ? 119  ALA A N     1 
ATOM   822  C  CA    . ALA A 1 119 ? 123.996 39.220 -3.485  1.00 25.56  ? 119  ALA A CA    1 
ATOM   823  C  C     . ALA A 1 119 ? 122.568 38.889 -3.925  1.00 30.27  ? 119  ALA A C     1 
ATOM   824  O  O     . ALA A 1 119 ? 122.308 37.848 -4.528  1.00 30.37  ? 119  ALA A O     1 
ATOM   825  C  CB    . ALA A 1 119 ? 124.994 39.005 -4.613  1.00 24.48  ? 119  ALA A CB    1 
ATOM   826  N  N     . PRO A 1 120 ? 121.645 39.774 -3.602  1.00 26.69  ? 120  PRO A N     1 
ATOM   827  C  CA    . PRO A 1 120 ? 120.262 39.541 -3.981  1.00 32.86  ? 120  PRO A CA    1 
ATOM   828  C  C     . PRO A 1 120 ? 120.129 39.592 -5.511  1.00 30.61  ? 120  PRO A C     1 
ATOM   829  O  O     . PRO A 1 120 ? 120.826 40.331 -6.207  1.00 38.20  ? 120  PRO A O     1 
ATOM   830  C  CB    . PRO A 1 120 ? 119.506 40.693 -3.247  1.00 33.59  ? 120  PRO A CB    1 
ATOM   831  C  CG    . PRO A 1 120 ? 120.514 41.815 -3.220  1.00 30.91  ? 120  PRO A CG    1 
ATOM   832  C  CD    . PRO A 1 120 ? 121.925 41.198 -3.364  1.00 25.82  ? 120  PRO A CD    1 
ATOM   833  N  N     . GLY A 1 121 ? 119.238 38.802 -6.048  1.00 28.35  ? 121  GLY A N     1 
ATOM   834  C  CA    . GLY A 1 121 ? 119.068 38.815 -7.485  1.00 26.57  ? 121  GLY A CA    1 
ATOM   835  C  C     . GLY A 1 121 ? 120.104 37.977 -8.202  1.00 28.85  ? 121  GLY A C     1 
ATOM   836  O  O     . GLY A 1 121 ? 120.054 37.886 -9.422  1.00 34.81  ? 121  GLY A O     1 
ATOM   837  N  N     . GLN A 1 122 ? 121.040 37.362 -7.477  1.00 19.06  ? 122  GLN A N     1 
ATOM   838  C  CA    . GLN A 1 122 ? 122.047 36.545 -8.176  1.00 14.76  ? 122  GLN A CA    1 
ATOM   839  C  C     . GLN A 1 122 ? 122.141 35.181 -7.556  1.00 18.41  ? 122  GLN A C     1 
ATOM   840  O  O     . GLN A 1 122 ? 121.830 35.023 -6.392  1.00 23.35  ? 122  GLN A O     1 
ATOM   841  C  CB    . GLN A 1 122 ? 123.415 37.141 -8.166  1.00 17.35  ? 122  GLN A CB    1 
ATOM   842  C  CG    . GLN A 1 122 ? 123.424 38.518 -8.754  1.00 22.99  ? 122  GLN A CG    1 
ATOM   843  C  CD    . GLN A 1 122 ? 124.831 38.915 -8.906  1.00 46.48  ? 122  GLN A CD    1 
ATOM   844  O  OE1   . GLN A 1 122 ? 125.280 39.818 -8.232  1.00 35.59  ? 122  GLN A OE1   1 
ATOM   845  N  NE2   . GLN A 1 122 ? 125.565 38.220 -9.774  1.00 52.81  ? 122  GLN A NE2   1 
ATOM   846  N  N     . SER A 1 123 ? 122.563 34.194 -8.323  1.00 15.35  ? 123  SER A N     1 
ATOM   847  C  CA    . SER A 1 123 ? 122.651 32.836 -7.790  1.00 18.20  ? 123  SER A CA    1 
ATOM   848  C  C     . SER A 1 123 ? 124.029 32.450 -7.254  1.00 17.33  ? 123  SER A C     1 
ATOM   849  O  O     . SER A 1 123 ? 125.054 32.980 -7.669  1.00 16.75  ? 123  SER A O     1 
ATOM   850  C  CB    . SER A 1 123 ? 122.280 31.876 -8.928  1.00 23.72  ? 123  SER A CB    1 
ATOM   851  O  OG    . SER A 1 123 ? 123.275 31.977 -9.948  1.00 31.29  ? 123  SER A OG    1 
ATOM   852  N  N     . THR A 1 124 ? 124.042 31.514 -6.322  1.00 12.02  ? 124  THR A N     1 
ATOM   853  C  CA    . THR A 1 124 ? 125.295 31.061 -5.745  1.00 11.99  ? 124  THR A CA    1 
ATOM   854  C  C     . THR A 1 124 ? 126.100 30.387 -6.830  1.00 19.69  ? 124  THR A C     1 
ATOM   855  O  O     . THR A 1 124 ? 125.543 29.639 -7.640  1.00 17.12  ? 124  THR A O     1 
ATOM   856  C  CB    . THR A 1 124 ? 124.979 30.153 -4.626  1.00 15.17  ? 124  THR A CB    1 
ATOM   857  O  OG1   . THR A 1 124 ? 124.420 31.031 -3.641  1.00 14.02  ? 124  THR A OG1   1 
ATOM   858  C  CG2   . THR A 1 124 ? 126.234 29.497 -4.069  1.00 11.54  ? 124  THR A CG2   1 
ATOM   859  N  N     . GLY A 1 125 ? 127.402 30.644 -6.857  1.00 13.69  ? 125  GLY A N     1 
ATOM   860  C  CA    . GLY A 1 125 ? 128.257 30.040 -7.891  1.00 11.94  ? 125  GLY A CA    1 
ATOM   861  C  C     . GLY A 1 125 ? 128.179 28.524 -7.890  1.00 15.14  ? 125  GLY A C     1 
ATOM   862  O  O     . GLY A 1 125 ? 127.869 27.884 -6.880  1.00 12.02  ? 125  GLY A O     1 
ATOM   863  N  N     . THR A 1 126 ? 128.477 27.934 -9.034  1.00 8.47   ? 126  THR A N     1 
ATOM   864  C  CA    . THR A 1 126 ? 128.441 26.487 -9.144  1.00 6.57   ? 126  THR A CA    1 
ATOM   865  C  C     . THR A 1 126 ? 129.566 26.064 -10.072 1.00 12.29  ? 126  THR A C     1 
ATOM   866  O  O     . THR A 1 126 ? 129.933 26.777 -11.002 1.00 11.75  ? 126  THR A O     1 
ATOM   867  C  CB    . THR A 1 126 ? 127.056 26.010 -9.678  1.00 19.54  ? 126  THR A CB    1 
ATOM   868  O  OG1   . THR A 1 126 ? 127.105 24.589 -9.916  1.00 26.76  ? 126  THR A OG1   1 
ATOM   869  C  CG2   . THR A 1 126 ? 126.787 26.735 -10.982 1.00 19.53  ? 126  THR A CG2   1 
ATOM   870  N  N     . CYS A 1 127 ? 130.120 24.911 -9.797  1.00 11.30  ? 127  CYS A N     1 
ATOM   871  C  CA    . CYS A 1 127 ? 131.202 24.415 -10.615 1.00 10.87  ? 127  CYS A CA    1 
ATOM   872  C  C     . CYS A 1 127 ? 130.913 22.990 -11.010 1.00 12.77  ? 127  CYS A C     1 
ATOM   873  O  O     . CYS A 1 127 ? 130.580 22.142 -10.183 1.00 11.65  ? 127  CYS A O     1 
ATOM   874  C  CB    . CYS A 1 127 ? 132.518 24.402 -9.767  1.00 10.32  ? 127  CYS A CB    1 
ATOM   875  S  SG    . CYS A 1 127 ? 133.903 23.585 -10.675 1.00 12.92  ? 127  CYS A SG    1 
ATOM   876  N  N     . ALA A 1 128 ? 131.018 22.713 -12.289 1.00 10.50  ? 128  ALA A N     1 
ATOM   877  C  CA    . ALA A 1 128 ? 130.774 21.354 -12.698 1.00 11.14  ? 128  ALA A CA    1 
ATOM   878  C  C     . ALA A 1 128 ? 132.135 20.670 -12.641 1.00 14.90  ? 128  ALA A C     1 
ATOM   879  O  O     . ALA A 1 128 ? 133.088 21.107 -13.279 1.00 14.27  ? 128  ALA A O     1 
ATOM   880  C  CB    . ALA A 1 128 ? 130.220 21.285 -14.130 1.00 14.80  ? 128  ALA A CB    1 
ATOM   881  N  N     . VAL A 1 129 ? 132.235 19.614 -11.876 1.00 11.34  ? 129  VAL A N     1 
ATOM   882  C  CA    . VAL A 1 129 ? 133.490 18.894 -11.755 1.00 11.26  ? 129  VAL A CA    1 
ATOM   883  C  C     . VAL A 1 129 ? 133.288 17.637 -12.555 1.00 16.78  ? 129  VAL A C     1 
ATOM   884  O  O     . VAL A 1 129 ? 132.584 16.730 -12.105 1.00 15.70  ? 129  VAL A O     1 
ATOM   885  C  CB    . VAL A 1 129 ? 133.750 18.562 -10.259 1.00 13.03  ? 129  VAL A CB    1 
ATOM   886  C  CG1   . VAL A 1 129 ? 135.049 17.779 -10.093 1.00 14.20  ? 129  VAL A CG1   1 
ATOM   887  C  CG2   . VAL A 1 129 ? 133.713 19.840 -9.410  1.00 10.41  ? 129  VAL A CG2   1 
ATOM   888  N  N     . LEU A 1 130 ? 133.880 17.599 -13.740 1.00 11.98  ? 130  LEU A N     1 
ATOM   889  C  CA    . LEU A 1 130 ? 133.731 16.450 -14.618 1.00 13.08  ? 130  LEU A CA    1 
ATOM   890  C  C     . LEU A 1 130 ? 134.900 15.506 -14.499 1.00 16.72  ? 130  LEU A C     1 
ATOM   891  O  O     . LEU A 1 130 ? 136.034 15.872 -14.751 1.00 15.61  ? 130  LEU A O     1 
ATOM   892  C  CB    . LEU A 1 130 ? 133.561 17.000 -16.067 1.00 12.72  ? 130  LEU A CB    1 
ATOM   893  C  CG    . LEU A 1 130 ? 132.609 18.195 -16.033 1.00 19.30  ? 130  LEU A CG    1 
ATOM   894  C  CD1   . LEU A 1 130 ? 132.656 18.809 -17.354 1.00 24.85  ? 130  LEU A CD1   1 
ATOM   895  C  CD2   . LEU A 1 130 ? 131.196 17.704 -15.836 1.00 20.67  ? 130  LEU A CD2   1 
ATOM   896  N  N     . ILE A 1 131 ? 134.605 14.293 -14.110 1.00 14.31  ? 131  ILE A N     1 
ATOM   897  C  CA    . ILE A 1 131 ? 135.634 13.286 -13.935 1.00 13.26  ? 131  ILE A CA    1 
ATOM   898  C  C     . ILE A 1 131 ? 135.657 12.385 -15.148 1.00 20.55  ? 131  ILE A C     1 
ATOM   899  O  O     . ILE A 1 131 ? 134.642 11.842 -15.555 1.00 19.15  ? 131  ILE A O     1 
ATOM   900  C  CB    . ILE A 1 131 ? 135.335 12.425 -12.690 1.00 18.32  ? 131  ILE A CB    1 
ATOM   901  C  CG1   . ILE A 1 131 ? 135.118 13.305 -11.416 1.00 20.70  ? 131  ILE A CG1   1 
ATOM   902  C  CG2   . ILE A 1 131 ? 136.421 11.374 -12.512 1.00 17.65  ? 131  ILE A CG2   1 
ATOM   903  C  CD1   . ILE A 1 131 ? 136.249 14.314 -11.231 1.00 21.55  ? 131  ILE A CD1   1 
ATOM   904  N  N     . ASN A 1 132 ? 136.820 12.235 -15.738 1.00 21.34  ? 132  ASN A N     1 
ATOM   905  C  CA    . ASN A 1 132 ? 136.961 11.399 -16.913 1.00 18.57  ? 132  ASN A CA    1 
ATOM   906  C  C     . ASN A 1 132 ? 138.337 10.802 -16.850 1.00 33.54  ? 132  ASN A C     1 
ATOM   907  O  O     . ASN A 1 132 ? 139.326 11.514 -16.589 1.00 22.93  ? 132  ASN A O     1 
ATOM   908  C  CB    . ASN A 1 132 ? 136.703 12.176 -18.153 1.00 19.90  ? 132  ASN A CB    1 
ATOM   909  C  CG    . ASN A 1 132 ? 136.836 11.332 -19.399 1.00 42.10  ? 132  ASN A CG    1 
ATOM   910  O  OD1   . ASN A 1 132 ? 135.945 10.579 -19.828 1.00 34.61  ? 132  ASN A OD1   1 
ATOM   911  N  ND2   . ASN A 1 132 ? 137.969 11.462 -19.989 1.00 34.20  ? 132  ASN A ND2   1 
ATOM   912  N  N     . GLU A 1 133 ? 138.389 9.491  -16.995 1.00 47.55  ? 133  GLU A N     1 
ATOM   913  C  CA    . GLU A 1 133 ? 139.659 8.820  -16.883 1.00 53.80  ? 133  GLU A CA    1 
ATOM   914  C  C     . GLU A 1 133 ? 139.994 9.035  -15.429 1.00 58.00  ? 133  GLU A C     1 
ATOM   915  O  O     . GLU A 1 133 ? 139.226 8.643  -14.548 1.00 63.12  ? 133  GLU A O     1 
ATOM   916  C  CB    . GLU A 1 133 ? 140.723 9.401  -17.831 1.00 57.58  ? 133  GLU A CB    1 
ATOM   917  C  CG    . GLU A 1 133 ? 141.161 8.379  -18.915 1.00 82.32  ? 133  GLU A CG    1 
ATOM   918  C  CD    . GLU A 1 133 ? 141.057 8.837  -20.408 1.00 100.00 ? 133  GLU A CD    1 
ATOM   919  O  OE1   . GLU A 1 133 ? 139.968 8.737  -21.012 1.00 75.24  ? 133  GLU A OE1   1 
ATOM   920  O  OE2   . GLU A 1 133 ? 142.078 9.249  -21.002 1.00 100.00 ? 133  GLU A OE2   1 
ATOM   921  N  N     . LYS A 1 134 ? 141.094 9.674  -15.148 1.00 50.59  ? 134  LYS A N     1 
ATOM   922  C  CA    . LYS A 1 134 ? 141.307 9.862  -13.747 1.00 56.70  ? 134  LYS A CA    1 
ATOM   923  C  C     . LYS A 1 134 ? 141.202 11.346 -13.423 1.00 49.37  ? 134  LYS A C     1 
ATOM   924  O  O     . LYS A 1 134 ? 141.397 11.726 -12.280 1.00 51.15  ? 134  LYS A O     1 
ATOM   925  C  CB    . LYS A 1 134 ? 142.805 9.394  -13.515 1.00 69.71  ? 134  LYS A CB    1 
ATOM   926  C  CG    . LYS A 1 134 ? 143.013 7.904  -13.731 1.00 100.00 ? 134  LYS A CG    1 
ATOM   927  C  CD    . LYS A 1 134 ? 141.790 7.150  -13.227 1.00 99.32  ? 134  LYS A CD    1 
ATOM   928  C  CE    . LYS A 1 134 ? 141.465 7.531  -11.793 1.00 65.59  ? 134  LYS A CE    1 
ATOM   929  N  NZ    . LYS A 1 134 ? 142.013 6.485  -10.886 1.00 85.11  ? 134  LYS A NZ    1 
ATOM   930  N  N     . GLU A 1 135 ? 141.249 12.158 -14.453 1.00 35.99  ? 135  GLU A N     1 
ATOM   931  C  CA    . GLU A 1 135 ? 141.348 13.593 -14.312 1.00 30.07  ? 135  GLU A CA    1 
ATOM   932  C  C     . GLU A 1 135 ? 140.050 14.293 -14.092 1.00 32.27  ? 135  GLU A C     1 
ATOM   933  O  O     . GLU A 1 135 ? 138.965 13.820 -14.469 1.00 23.97  ? 135  GLU A O     1 
ATOM   934  C  CB    . GLU A 1 135 ? 141.968 14.204 -15.595 1.00 29.08  ? 135  GLU A CB    1 
ATOM   935  C  CG    . GLU A 1 135 ? 143.290 13.567 -16.106 1.00 49.13  ? 135  GLU A CG    1 
ATOM   936  C  CD    . GLU A 1 135 ? 144.004 14.381 -17.231 1.00 96.18  ? 135  GLU A CD    1 
ATOM   937  O  OE1   . GLU A 1 135 ? 144.931 15.189 -16.970 1.00 100.00 ? 135  GLU A OE1   1 
ATOM   938  O  OE2   . GLU A 1 135 ? 143.650 14.202 -18.414 1.00 100.00 ? 135  GLU A OE2   1 
ATOM   939  N  N     . ARG A 1 136 ? 140.186 15.450 -13.475 1.00 22.73  ? 136  ARG A N     1 
ATOM   940  C  CA    . ARG A 1 136 ? 139.045 16.281 -13.184 1.00 21.17  ? 136  ARG A CA    1 
ATOM   941  C  C     . ARG A 1 136 ? 139.122 17.528 -14.060 1.00 24.30  ? 136  ARG A C     1 
ATOM   942  O  O     . ARG A 1 136 ? 140.203 18.095 -14.238 1.00 18.94  ? 136  ARG A O     1 
ATOM   943  C  CB    . ARG A 1 136 ? 139.142 16.741 -11.727 1.00 21.57  ? 136  ARG A CB    1 
ATOM   944  C  CG    . ARG A 1 136 ? 140.522 17.476 -11.365 1.00 38.29  ? 136  ARG A CG    1 
ATOM   945  C  CD    . ARG A 1 136 ? 140.088 18.817 -10.899 1.00 50.78  ? 136  ARG A CD    1 
ATOM   946  N  NE    . ARG A 1 136 ? 141.044 19.866 -10.511 1.00 39.40  ? 136  ARG A NE    1 
ATOM   947  C  CZ    . ARG A 1 136 ? 141.735 20.604 -11.358 1.00 43.40  ? 136  ARG A CZ    1 
ATOM   948  N  NH1   . ARG A 1 136 ? 141.617 20.382 -12.662 1.00 24.28  ? 136  ARG A NH1   1 
ATOM   949  N  NH2   . ARG A 1 136 ? 142.538 21.550 -10.896 1.00 35.61  ? 136  ARG A NH2   1 
ATOM   950  N  N     . THR A 1 137 ? 137.990 17.949 -14.609 1.00 12.63  ? 137  THR A N     1 
ATOM   951  C  CA    . THR A 1 137 ? 137.937 19.146 -15.450 1.00 9.22   ? 137  THR A CA    1 
ATOM   952  C  C     . THR A 1 137 ? 136.953 20.051 -14.730 1.00 14.17  ? 137  THR A C     1 
ATOM   953  O  O     . THR A 1 137 ? 135.886 19.577 -14.295 1.00 16.49  ? 137  THR A O     1 
ATOM   954  C  CB    . THR A 1 137 ? 137.462 18.791 -16.845 1.00 11.84  ? 137  THR A CB    1 
ATOM   955  O  OG1   . THR A 1 137 ? 138.365 17.806 -17.312 1.00 14.77  ? 137  THR A OG1   1 
ATOM   956  C  CG2   . THR A 1 137 ? 137.482 20.030 -17.699 1.00 15.03  ? 137  THR A CG2   1 
ATOM   957  N  N     . LEU A 1 138 ? 137.280 21.320 -14.569 1.00 12.14  ? 138  LEU A N     1 
ATOM   958  C  CA    . LEU A 1 138 ? 136.375 22.225 -13.861 1.00 10.57  ? 138  LEU A CA    1 
ATOM   959  C  C     . LEU A 1 138 ? 135.804 23.311 -14.753 1.00 16.33  ? 138  LEU A C     1 
ATOM   960  O  O     . LEU A 1 138 ? 136.541 23.987 -15.459 1.00 13.84  ? 138  LEU A O     1 
ATOM   961  C  CB    . LEU A 1 138 ? 137.173 22.933 -12.776 1.00 9.08   ? 138  LEU A CB    1 
ATOM   962  C  CG    . LEU A 1 138 ? 138.016 22.000 -11.874 1.00 14.35  ? 138  LEU A CG    1 
ATOM   963  C  CD1   . LEU A 1 138 ? 138.810 22.861 -10.889 1.00 14.71  ? 138  LEU A CD1   1 
ATOM   964  C  CD2   . LEU A 1 138 ? 137.070 21.054 -11.106 1.00 17.32  ? 138  LEU A CD2   1 
ATOM   965  N  N     . CYS A 1 139 ? 134.487 23.481 -14.717 1.00 10.93  ? 139  CYS A N     1 
ATOM   966  C  CA    . CYS A 1 139 ? 133.816 24.519 -15.530 1.00 10.04  ? 139  CYS A CA    1 
ATOM   967  C  C     . CYS A 1 139 ? 132.913 25.275 -14.551 1.00 11.53  ? 139  CYS A C     1 
ATOM   968  O  O     . CYS A 1 139 ? 131.929 24.711 -14.075 1.00 11.98  ? 139  CYS A O     1 
ATOM   969  C  CB    . CYS A 1 139 ? 133.096 23.849 -16.652 1.00 13.64  ? 139  CYS A CB    1 
ATOM   970  S  SG    . CYS A 1 139 ? 132.409 25.114 -17.735 1.00 18.01  ? 139  CYS A SG    1 
ATOM   971  N  N     . THR A 1 140 ? 133.261 26.518 -14.255 1.00 8.86   ? 140  THR A N     1 
ATOM   972  C  CA    . THR A 1 140 ? 132.493 27.281 -13.299 1.00 9.14   ? 140  THR A CA    1 
ATOM   973  C  C     . THR A 1 140 ? 131.732 28.512 -13.732 1.00 13.54  ? 140  THR A C     1 
ATOM   974  O  O     . THR A 1 140 ? 132.114 29.238 -14.627 1.00 14.02  ? 140  THR A O     1 
ATOM   975  C  CB    . THR A 1 140 ? 133.673 27.834 -12.355 1.00 9.41   ? 140  THR A CB    1 
ATOM   976  O  OG1   . THR A 1 140 ? 134.378 26.696 -11.798 1.00 13.25  ? 140  THR A OG1   1 
ATOM   977  C  CG2   . THR A 1 140 ? 133.176 28.659 -11.190 1.00 9.75   ? 140  THR A CG2   1 
ATOM   978  N  N     . HIS A 1 141 ? 130.628 28.716 -13.027 1.00 9.80   ? 141  HIS A N     1 
ATOM   979  C  CA    . HIS A 1 141 ? 129.768 29.852 -13.249 1.00 12.44  ? 141  HIS A CA    1 
ATOM   980  C  C     . HIS A 1 141 ? 129.786 30.573 -11.902 1.00 13.35  ? 141  HIS A C     1 
ATOM   981  O  O     . HIS A 1 141 ? 129.198 30.114 -10.940 1.00 14.13  ? 141  HIS A O     1 
ATOM   982  C  CB    . HIS A 1 141 ? 128.370 29.401 -13.719 1.00 14.49  ? 141  HIS A CB    1 
ATOM   983  C  CG    . HIS A 1 141 ? 127.533 30.602 -13.897 1.00 21.28  ? 141  HIS A CG    1 
ATOM   984  N  ND1   . HIS A 1 141 ? 126.423 30.860 -13.139 1.00 23.84  ? 141  HIS A ND1   1 
ATOM   985  C  CD2   . HIS A 1 141 ? 127.713 31.665 -14.708 1.00 23.66  ? 141  HIS A CD2   1 
ATOM   986  C  CE1   . HIS A 1 141 ? 125.928 32.030 -13.505 1.00 25.50  ? 141  HIS A CE1   1 
ATOM   987  N  NE2   . HIS A 1 141 ? 126.695 32.536 -14.452 1.00 26.70  ? 141  HIS A NE2   1 
ATOM   988  N  N     . LEU A 1 142 ? 130.492 31.680 -11.833 1.00 9.30   ? 142  LEU A N     1 
ATOM   989  C  CA    . LEU A 1 142 ? 130.648 32.459 -10.614 1.00 12.37  ? 142  LEU A CA    1 
ATOM   990  C  C     . LEU A 1 142 ? 129.381 33.027 -9.972  1.00 17.12  ? 142  LEU A C     1 
ATOM   991  O  O     . LEU A 1 142 ? 129.270 33.044 -8.750  1.00 15.88  ? 142  LEU A O     1 
ATOM   992  C  CB    . LEU A 1 142 ? 131.731 33.533 -10.808 1.00 13.20  ? 142  LEU A CB    1 
ATOM   993  C  CG    . LEU A 1 142 ? 133.209 33.017 -10.922 1.00 17.95  ? 142  LEU A CG    1 
ATOM   994  C  CD1   . LEU A 1 142 ? 134.075 34.241 -10.938 1.00 22.08  ? 142  LEU A CD1   1 
ATOM   995  C  CD2   . LEU A 1 142 ? 133.602 32.256 -9.705  1.00 14.29  ? 142  LEU A CD2   1 
ATOM   996  N  N     . GLY A 1 143 ? 128.461 33.509 -10.771 1.00 14.90  ? 143  GLY A N     1 
ATOM   997  C  CA    . GLY A 1 143 ? 127.242 34.074 -10.216 1.00 15.80  ? 143  GLY A CA    1 
ATOM   998  C  C     . GLY A 1 143 ? 127.543 35.166 -9.192  1.00 15.90  ? 143  GLY A C     1 
ATOM   999  O  O     . GLY A 1 143 ? 128.323 36.075 -9.440  1.00 14.27  ? 143  GLY A O     1 
ATOM   1000 N  N     . ALA A 1 144 ? 126.908 35.067 -8.023  1.00 13.89  ? 144  ALA A N     1 
ATOM   1001 C  CA    . ALA A 1 144 ? 127.089 36.046 -6.960  1.00 13.36  ? 144  ALA A CA    1 
ATOM   1002 C  C     . ALA A 1 144 ? 128.540 36.284 -6.538  1.00 13.82  ? 144  ALA A C     1 
ATOM   1003 O  O     . ALA A 1 144 ? 128.849 37.381 -6.076  1.00 14.68  ? 144  ALA A O     1 
ATOM   1004 C  CB    . ALA A 1 144 ? 126.324 35.576 -5.719  1.00 13.92  ? 144  ALA A CB    1 
ATOM   1005 N  N     . CYS A 1 145 ? 129.428 35.287 -6.686  1.00 14.69  ? 145  CYS A N     1 
ATOM   1006 C  CA    . CYS A 1 145 ? 130.835 35.503 -6.270  1.00 12.82  ? 145  CYS A CA    1 
ATOM   1007 C  C     . CYS A 1 145 ? 131.468 36.727 -6.898  1.00 21.62  ? 145  CYS A C     1 
ATOM   1008 O  O     . CYS A 1 145 ? 132.342 37.364 -6.305  1.00 20.83  ? 145  CYS A O     1 
ATOM   1009 C  CB    . CYS A 1 145 ? 131.774 34.377 -6.639  1.00 11.22  ? 145  CYS A CB    1 
ATOM   1010 S  SG    . CYS A 1 145 ? 131.315 32.824 -5.985  1.00 16.97  ? 145  CYS A SG    1 
ATOM   1011 N  N     . GLY A 1 146 ? 131.044 37.062 -8.103  1.00 18.67  ? 146  GLY A N     1 
ATOM   1012 C  CA    . GLY A 1 146 ? 131.616 38.220 -8.768  1.00 17.29  ? 146  GLY A CA    1 
ATOM   1013 C  C     . GLY A 1 146 ? 131.279 39.572 -8.126  1.00 24.38  ? 146  GLY A C     1 
ATOM   1014 O  O     . GLY A 1 146 ? 131.917 40.572 -8.468  1.00 23.50  ? 146  GLY A O     1 
ATOM   1015 N  N     . SER A 1 147 ? 130.296 39.632 -7.212  1.00 17.39  ? 147  SER A N     1 
ATOM   1016 C  CA    . SER A 1 147 ? 129.938 40.910 -6.595  1.00 11.88  ? 147  SER A CA    1 
ATOM   1017 C  C     . SER A 1 147 ? 130.616 41.133 -5.272  1.00 19.83  ? 147  SER A C     1 
ATOM   1018 O  O     . SER A 1 147 ? 130.403 42.151 -4.616  1.00 18.18  ? 147  SER A O     1 
ATOM   1019 C  CB    . SER A 1 147 ? 128.460 40.773 -6.142  1.00 21.63  ? 147  SER A CB    1 
ATOM   1020 O  OG    . SER A 1 147 ? 127.709 40.675 -7.318  1.00 37.17  ? 147  SER A OG    1 
ATOM   1021 N  N     . PHE A 1 148 ? 131.419 40.187 -4.868  1.00 15.78  ? 148  PHE A N     1 
ATOM   1022 C  CA    . PHE A 1 148 ? 132.091 40.331 -3.587  1.00 13.93  ? 148  PHE A CA    1 
ATOM   1023 C  C     . PHE A 1 148 ? 132.954 41.584 -3.428  1.00 15.32  ? 148  PHE A C     1 
ATOM   1024 O  O     . PHE A 1 148 ? 133.770 41.875 -4.264  1.00 16.47  ? 148  PHE A O     1 
ATOM   1025 C  CB    . PHE A 1 148 ? 132.930 39.058 -3.263  1.00 13.39  ? 148  PHE A CB    1 
ATOM   1026 C  CG    . PHE A 1 148 ? 133.609 39.185 -1.919  1.00 14.82  ? 148  PHE A CG    1 
ATOM   1027 C  CD1   . PHE A 1 148 ? 132.852 39.344 -0.737  1.00 16.92  ? 148  PHE A CD1   1 
ATOM   1028 C  CD2   . PHE A 1 148 ? 134.980 39.179 -1.818  1.00 15.74  ? 148  PHE A CD2   1 
ATOM   1029 C  CE1   . PHE A 1 148 ? 133.459 39.481 0.515   1.00 18.95  ? 148  PHE A CE1   1 
ATOM   1030 C  CE2   . PHE A 1 148 ? 135.577 39.338 -0.587  1.00 16.03  ? 148  PHE A CE2   1 
ATOM   1031 C  CZ    . PHE A 1 148 ? 134.842 39.494 0.582   1.00 18.57  ? 148  PHE A CZ    1 
ATOM   1032 N  N     . ARG A 1 149 ? 132.758 42.309 -2.333  1.00 12.77  ? 149  ARG A N     1 
ATOM   1033 C  CA    . ARG A 1 149 ? 133.519 43.510 -2.007  1.00 12.08  ? 149  ARG A CA    1 
ATOM   1034 C  C     . ARG A 1 149 ? 133.867 43.384 -0.530  1.00 17.99  ? 149  ARG A C     1 
ATOM   1035 O  O     . ARG A 1 149 ? 132.972 43.097 0.264   1.00 19.17  ? 149  ARG A O     1 
ATOM   1036 C  CB    . ARG A 1 149 ? 132.822 44.852 -2.291  1.00 20.27  ? 149  ARG A CB    1 
ATOM   1037 C  CG    . ARG A 1 149 ? 132.279 45.007 -3.744  1.00 21.86  ? 149  ARG A CG    1 
ATOM   1038 C  CD    . ARG A 1 149 ? 133.373 45.176 -4.790  1.00 27.72  ? 149  ARG A CD    1 
ATOM   1039 N  NE    . ARG A 1 149 ? 132.739 45.293 -6.121  1.00 28.62  ? 149  ARG A NE    1 
ATOM   1040 C  CZ    . ARG A 1 149 ? 132.655 44.334 -7.043  1.00 49.91  ? 149  ARG A CZ    1 
ATOM   1041 N  NH1   . ARG A 1 149 ? 133.165 43.104 -6.893  1.00 29.00  ? 149  ARG A NH1   1 
ATOM   1042 N  NH2   . ARG A 1 149 ? 132.040 44.631 -8.156  1.00 44.27  ? 149  ARG A NH2   1 
ATOM   1043 N  N     . ILE A 1 150 ? 135.138 43.536 -0.117  1.00 16.70  ? 150  ILE A N     1 
ATOM   1044 C  CA    . ILE A 1 150 ? 135.429 43.374 1.322   1.00 17.26  ? 150  ILE A CA    1 
ATOM   1045 C  C     . ILE A 1 150 ? 134.802 44.500 2.107   1.00 20.97  ? 150  ILE A C     1 
ATOM   1046 O  O     . ILE A 1 150 ? 134.906 45.643 1.671   1.00 25.77  ? 150  ILE A O     1 
ATOM   1047 C  CB    . ILE A 1 150 ? 136.915 43.335 1.876   1.00 22.72  ? 150  ILE A CB    1 
ATOM   1048 C  CG1   . ILE A 1 150 ? 137.922 43.675 0.927   1.00 31.68  ? 150  ILE A CG1   1 
ATOM   1049 C  CG2   . ILE A 1 150 ? 137.477 41.927 2.316   1.00 20.28  ? 150  ILE A CG2   1 
ATOM   1050 C  CD1   . ILE A 1 150 ? 139.184 43.165 1.618   1.00 32.82  ? 150  ILE A CD1   1 
ATOM   1051 N  N     . PRO A 1 151 ? 134.163 44.191 3.240   1.00 19.65  ? 151  PRO A N     1 
ATOM   1052 C  CA    . PRO A 1 151 ? 133.542 45.229 4.052   1.00 18.65  ? 151  PRO A CA    1 
ATOM   1053 C  C     . PRO A 1 151 ? 134.623 46.065 4.720   1.00 24.96  ? 151  PRO A C     1 
ATOM   1054 O  O     . PRO A 1 151 ? 135.730 45.583 4.949   1.00 22.40  ? 151  PRO A O     1 
ATOM   1055 C  CB    . PRO A 1 151 ? 132.688 44.455 5.036   1.00 19.79  ? 151  PRO A CB    1 
ATOM   1056 C  CG    . PRO A 1 151 ? 133.369 43.161 5.150   1.00 23.68  ? 151  PRO A CG    1 
ATOM   1057 C  CD    . PRO A 1 151 ? 133.824 42.868 3.766   1.00 18.23  ? 151  PRO A CD    1 
ATOM   1058 N  N     . GLU A 1 152 ? 134.300 47.312 5.030   1.00 33.16  ? 152  GLU A N     1 
ATOM   1059 C  CA    . GLU A 1 152 ? 135.255 48.221 5.664   1.00 41.09  ? 152  GLU A CA    1 
ATOM   1060 C  C     . GLU A 1 152 ? 135.834 47.725 6.983   1.00 30.77  ? 152  GLU A C     1 
ATOM   1061 O  O     . GLU A 1 152 ? 136.974 48.030 7.311   1.00 34.87  ? 152  GLU A O     1 
ATOM   1062 C  CB    . GLU A 1 152 ? 134.699 49.640 5.861   1.00 49.48  ? 152  GLU A CB    1 
ATOM   1063 C  CG    . GLU A 1 152 ? 135.605 50.728 5.223   1.00 96.76  ? 152  GLU A CG    1 
ATOM   1064 C  CD    . GLU A 1 152 ? 136.279 51.766 6.194   1.00 100.00 ? 152  GLU A CD    1 
ATOM   1065 O  OE1   . GLU A 1 152 ? 137.497 51.585 6.480   1.00 100.00 ? 152  GLU A OE1   1 
ATOM   1066 O  OE2   . GLU A 1 152 ? 135.598 52.758 6.615   1.00 100.00 ? 152  GLU A OE2   1 
ATOM   1067 N  N     . ASN A 1 153 ? 135.075 46.972 7.743   1.00 19.30  ? 153  ASN A N     1 
ATOM   1068 C  CA    . ASN A 1 153 ? 135.583 46.483 9.015   1.00 17.89  ? 153  ASN A CA    1 
ATOM   1069 C  C     . ASN A 1 153 ? 136.117 45.043 8.963   1.00 24.31  ? 153  ASN A C     1 
ATOM   1070 O  O     . ASN A 1 153 ? 136.169 44.343 9.978   1.00 23.49  ? 153  ASN A O     1 
ATOM   1071 C  CB    . ASN A 1 153 ? 134.432 46.550 9.991   1.00 30.93  ? 153  ASN A CB    1 
ATOM   1072 C  CG    . ASN A 1 153 ? 133.285 45.695 9.559   1.00 36.74  ? 153  ASN A CG    1 
ATOM   1073 O  OD1   . ASN A 1 153 ? 133.068 45.453 8.377   1.00 35.10  ? 153  ASN A OD1   1 
ATOM   1074 N  ND2   . ASN A 1 153 ? 132.555 45.229 10.508  1.00 34.45  ? 153  ASN A ND2   1 
ATOM   1075 N  N     . TRP A 1 154 ? 136.525 44.575 7.794   1.00 18.77  ? 154  TRP A N     1 
ATOM   1076 C  CA    . TRP A 1 154 ? 137.042 43.218 7.727   1.00 18.91  ? 154  TRP A CA    1 
ATOM   1077 C  C     . TRP A 1 154 ? 138.250 43.029 8.663   1.00 19.12  ? 154  TRP A C     1 
ATOM   1078 O  O     . TRP A 1 154 ? 138.461 41.955 9.189   1.00 16.69  ? 154  TRP A O     1 
ATOM   1079 C  CB    . TRP A 1 154 ? 137.311 42.815 6.282   1.00 18.15  ? 154  TRP A CB    1 
ATOM   1080 C  CG    . TRP A 1 154 ? 138.577 43.431 5.789   1.00 20.87  ? 154  TRP A CG    1 
ATOM   1081 C  CD1   . TRP A 1 154 ? 138.742 44.666 5.181   1.00 23.22  ? 154  TRP A CD1   1 
ATOM   1082 C  CD2   . TRP A 1 154 ? 139.897 42.828 5.864   1.00 21.69  ? 154  TRP A CD2   1 
ATOM   1083 N  NE1   . TRP A 1 154 ? 140.078 44.842 4.898   1.00 19.23  ? 154  TRP A NE1   1 
ATOM   1084 C  CE2   . TRP A 1 154 ? 140.796 43.737 5.285   1.00 24.78  ? 154  TRP A CE2   1 
ATOM   1085 C  CE3   . TRP A 1 154 ? 140.381 41.616 6.367   1.00 23.11  ? 154  TRP A CE3   1 
ATOM   1086 C  CZ2   . TRP A 1 154 ? 142.187 43.472 5.204   1.00 23.86  ? 154  TRP A CZ2   1 
ATOM   1087 C  CZ3   . TRP A 1 154 ? 141.711 41.346 6.283   1.00 25.13  ? 154  TRP A CZ3   1 
ATOM   1088 C  CH2   . TRP A 1 154 ? 142.607 42.271 5.703   1.00 24.26  ? 154  TRP A CH2   1 
ATOM   1089 N  N     . THR A 1 155 ? 139.048 44.079 8.873   1.00 23.15  ? 155  THR A N     1 
ATOM   1090 C  CA    . THR A 1 155 ? 140.211 43.969 9.759   1.00 22.78  ? 155  THR A CA    1 
ATOM   1091 C  C     . THR A 1 155 ? 139.761 43.605 11.176  1.00 30.84  ? 155  THR A C     1 
ATOM   1092 O  O     . THR A 1 155 ? 140.454 42.880 11.894  1.00 31.32  ? 155  THR A O     1 
ATOM   1093 C  CB    . THR A 1 155 ? 141.082 45.173 9.733   1.00 24.00  ? 155  THR A CB    1 
ATOM   1094 O  OG1   . THR A 1 155 ? 140.253 46.323 9.819   1.00 37.33  ? 155  THR A OG1   1 
ATOM   1095 C  CG2   . THR A 1 155 ? 141.645 45.286 8.360   1.00 27.29  ? 155  THR A CG2   1 
ATOM   1096 N  N     . THR A 1 156 ? 138.589 44.088 11.593  1.00 21.67  ? 156  THR A N     1 
ATOM   1097 C  CA    . THR A 1 156 ? 138.103 43.764 12.922  1.00 19.39  ? 156  THR A CA    1 
ATOM   1098 C  C     . THR A 1 156 ? 137.684 42.299 13.006  1.00 26.88  ? 156  THR A C     1 
ATOM   1099 O  O     . THR A 1 156 ? 137.969 41.600 13.977  1.00 30.63  ? 156  THR A O     1 
ATOM   1100 C  CB    . THR A 1 156 ? 136.858 44.574 13.286  1.00 30.61  ? 156  THR A CB    1 
ATOM   1101 O  OG1   . THR A 1 156 ? 137.200 45.946 13.328  1.00 34.67  ? 156  THR A OG1   1 
ATOM   1102 C  CG2   . THR A 1 156 ? 136.407 44.164 14.659  1.00 31.26  ? 156  THR A CG2   1 
ATOM   1103 N  N     . PHE A 1 157 ? 137.002 41.808 11.992  1.00 19.83  ? 157  PHE A N     1 
ATOM   1104 C  CA    . PHE A 1 157 ? 136.573 40.422 12.026  1.00 16.27  ? 157  PHE A CA    1 
ATOM   1105 C  C     . PHE A 1 157 ? 137.766 39.483 12.050  1.00 19.04  ? 157  PHE A C     1 
ATOM   1106 O  O     . PHE A 1 157 ? 137.732 38.438 12.698  1.00 22.06  ? 157  PHE A O     1 
ATOM   1107 C  CB    . PHE A 1 157 ? 135.695 40.189 10.768  1.00 20.07  ? 157  PHE A CB    1 
ATOM   1108 C  CG    . PHE A 1 157 ? 135.325 38.760 10.479  1.00 18.52  ? 157  PHE A CG    1 
ATOM   1109 C  CD1   . PHE A 1 157 ? 134.185 38.238 10.950  1.00 20.06  ? 157  PHE A CD1   1 
ATOM   1110 C  CD2   . PHE A 1 157 ? 136.145 37.949 9.680   1.00 25.33  ? 157  PHE A CD2   1 
ATOM   1111 C  CE1   . PHE A 1 157 ? 133.861 36.931 10.666  1.00 24.32  ? 157  PHE A CE1   1 
ATOM   1112 C  CE2   . PHE A 1 157 ? 135.805 36.627 9.375   1.00 24.70  ? 157  PHE A CE2   1 
ATOM   1113 C  CZ    . PHE A 1 157 ? 134.649 36.113 9.876   1.00 22.36  ? 157  PHE A CZ    1 
ATOM   1114 N  N     . ALA A 1 158 ? 138.825 39.852 11.346  1.00 18.20  ? 158  ALA A N     1 
ATOM   1115 C  CA    . ALA A 1 158 ? 140.041 39.021 11.282  1.00 20.72  ? 158  ALA A CA    1 
ATOM   1116 C  C     . ALA A 1 158 ? 141.100 39.377 12.322  1.00 34.50  ? 158  ALA A C     1 
ATOM   1117 O  O     . ALA A 1 158 ? 142.214 38.833 12.286  1.00 27.79  ? 158  ALA A O     1 
ATOM   1118 C  CB    . ALA A 1 158 ? 140.718 39.184 9.946   1.00 19.59  ? 158  ALA A CB    1 
ATOM   1119 N  N     . SER A 1 159 ? 140.772 40.281 13.233  1.00 42.47  ? 159  SER A N     1 
ATOM   1120 C  CA    . SER A 1 159 ? 141.730 40.686 14.269  1.00 46.32  ? 159  SER A CA    1 
ATOM   1121 C  C     . SER A 1 159 ? 142.349 39.479 14.973  1.00 42.43  ? 159  SER A C     1 
ATOM   1122 O  O     . SER A 1 159 ? 141.651 38.555 15.396  1.00 44.35  ? 159  SER A O     1 
ATOM   1123 C  CB    . SER A 1 159 ? 141.129 41.675 15.287  1.00 54.49  ? 159  SER A CB    1 
ATOM   1124 O  OG    . SER A 1 159 ? 142.091 42.665 15.643  1.00 75.04  ? 159  SER A OG    1 
ATOM   1125 N  N     . GLY A 1 160 ? 143.670 39.489 15.063  1.00 35.96  ? 160  GLY A N     1 
ATOM   1126 C  CA    . GLY A 1 160 ? 144.369 38.390 15.714  1.00 32.72  ? 160  GLY A CA    1 
ATOM   1127 C  C     . GLY A 1 160 ? 144.986 37.404 14.732  1.00 34.25  ? 160  GLY A C     1 
ATOM   1128 O  O     . GLY A 1 160 ? 145.924 36.688 15.075  1.00 36.54  ? 160  GLY A O     1 
ATOM   1129 N  N     . ALA A 1 161 ? 144.476 37.348 13.511  1.00 26.67  ? 161  ALA A N     1 
ATOM   1130 C  CA    . ALA A 1 161 ? 145.038 36.409 12.536  1.00 24.12  ? 161  ALA A CA    1 
ATOM   1131 C  C     . ALA A 1 161 ? 146.403 36.868 12.040  1.00 24.27  ? 161  ALA A C     1 
ATOM   1132 O  O     . ALA A 1 161 ? 146.635 38.056 11.824  1.00 26.95  ? 161  ALA A O     1 
ATOM   1133 C  CB    . ALA A 1 161 ? 144.065 36.229 11.346  1.00 26.26  ? 161  ALA A CB    1 
ATOM   1134 N  N     . LEU A 1 162 ? 147.312 35.925 11.862  1.00 20.29  ? 162  LEU A N     1 
ATOM   1135 C  CA    . LEU A 1 162 ? 148.643 36.267 11.387  1.00 26.24  ? 162  LEU A CA    1 
ATOM   1136 C  C     . LEU A 1 162 ? 148.899 35.698 10.004  1.00 23.39  ? 162  LEU A C     1 
ATOM   1137 O  O     . LEU A 1 162 ? 149.896 36.031 9.364   1.00 23.21  ? 162  LEU A O     1 
ATOM   1138 C  CB    . LEU A 1 162 ? 149.778 35.904 12.373  1.00 31.06  ? 162  LEU A CB    1 
ATOM   1139 C  CG    . LEU A 1 162 ? 149.836 36.907 13.552  1.00 33.87  ? 162  LEU A CG    1 
ATOM   1140 C  CD1   . LEU A 1 162 ? 150.864 36.510 14.514  1.00 36.45  ? 162  LEU A CD1   1 
ATOM   1141 C  CD2   . LEU A 1 162 ? 150.210 38.261 13.082  1.00 41.47  ? 162  LEU A CD2   1 
ATOM   1142 N  N     . ILE A 1 163 ? 148.007 34.848 9.543   1.00 17.41  ? 163  ILE A N     1 
ATOM   1143 C  CA    . ILE A 1 163 ? 148.172 34.269 8.225   1.00 14.22  ? 163  ILE A CA    1 
ATOM   1144 C  C     . ILE A 1 163 ? 146.955 34.670 7.376   1.00 21.80  ? 163  ILE A C     1 
ATOM   1145 O  O     . ILE A 1 163 ? 145.829 34.366 7.735   1.00 17.86  ? 163  ILE A O     1 
ATOM   1146 C  CB    . ILE A 1 163 ? 148.284 32.826 8.384   1.00 19.22  ? 163  ILE A CB    1 
ATOM   1147 C  CG1   . ILE A 1 163 ? 149.567 32.481 9.108   1.00 21.28  ? 163  ILE A CG1   1 
ATOM   1148 C  CG2   . ILE A 1 163 ? 148.230 32.133 7.042   1.00 19.63  ? 163  ILE A CG2   1 
ATOM   1149 C  CD1   . ILE A 1 163 ? 149.575 31.003 9.383   1.00 24.59  ? 163  ILE A CD1   1 
ATOM   1150 N  N     . PHE A 1 164 ? 147.196 35.370 6.266   1.00 19.66  ? 164  PHE A N     1 
ATOM   1151 C  CA    . PHE A 1 164 ? 146.155 35.840 5.340   1.00 15.10  ? 164  PHE A CA    1 
ATOM   1152 C  C     . PHE A 1 164 ? 146.284 35.089 4.038   1.00 19.56  ? 164  PHE A C     1 
ATOM   1153 O  O     . PHE A 1 164 ? 147.383 34.959 3.502   1.00 18.49  ? 164  PHE A O     1 
ATOM   1154 C  CB    . PHE A 1 164 ? 146.346 37.304 5.108   1.00 14.57  ? 164  PHE A CB    1 
ATOM   1155 C  CG    . PHE A 1 164 ? 146.117 38.057 6.375   1.00 18.70  ? 164  PHE A CG    1 
ATOM   1156 C  CD1   . PHE A 1 164 ? 144.838 38.523 6.702   1.00 20.36  ? 164  PHE A CD1   1 
ATOM   1157 C  CD2   . PHE A 1 164 ? 147.169 38.246 7.265   1.00 18.77  ? 164  PHE A CD2   1 
ATOM   1158 C  CE1   . PHE A 1 164 ? 144.631 39.187 7.893   1.00 25.43  ? 164  PHE A CE1   1 
ATOM   1159 C  CE2   . PHE A 1 164 ? 146.975 38.912 8.446   1.00 21.14  ? 164  PHE A CE2   1 
ATOM   1160 C  CZ    . PHE A 1 164 ? 145.710 39.395 8.773   1.00 23.77  ? 164  PHE A CZ    1 
ATOM   1161 N  N     . TYR A 1 165 ? 145.175 34.572 3.514   1.00 13.75  ? 165  TYR A N     1 
ATOM   1162 C  CA    . TYR A 1 165 ? 145.289 33.823 2.259   1.00 11.59  ? 165  TYR A CA    1 
ATOM   1163 C  C     . TYR A 1 165 ? 144.253 34.258 1.229   1.00 20.32  ? 165  TYR A C     1 
ATOM   1164 O  O     . TYR A 1 165 ? 143.124 34.577 1.576   1.00 15.79  ? 165  TYR A O     1 
ATOM   1165 C  CB    . TYR A 1 165 ? 145.002 32.387 2.588   1.00 10.61  ? 165  TYR A CB    1 
ATOM   1166 C  CG    . TYR A 1 165 ? 145.024 31.415 1.468   1.00 14.95  ? 165  TYR A CG    1 
ATOM   1167 C  CD1   . TYR A 1 165 ? 146.184 31.194 0.720   1.00 16.03  ? 165  TYR A CD1   1 
ATOM   1168 C  CD2   . TYR A 1 165 ? 143.870 30.693 1.136   1.00 12.87  ? 165  TYR A CD2   1 
ATOM   1169 C  CE1   . TYR A 1 165 ? 146.198 30.268 -0.322  1.00 12.33  ? 165  TYR A CE1   1 
ATOM   1170 C  CE2   . TYR A 1 165 ? 143.866 29.771 0.112   1.00 10.78  ? 165  TYR A CE2   1 
ATOM   1171 C  CZ    . TYR A 1 165 ? 145.051 29.553 -0.623  1.00 11.66  ? 165  TYR A CZ    1 
ATOM   1172 O  OH    . TYR A 1 165 ? 145.092 28.635 -1.650  1.00 12.76  ? 165  TYR A OH    1 
ATOM   1173 N  N     . ALA A 1 166 ? 144.658 34.260 -0.036  1.00 15.17  ? 166  ALA A N     1 
ATOM   1174 C  CA    . ALA A 1 166 ? 143.764 34.631 -1.117  1.00 12.28  ? 166  ALA A CA    1 
ATOM   1175 C  C     . ALA A 1 166 ? 144.110 33.769 -2.309  1.00 19.67  ? 166  ALA A C     1 
ATOM   1176 O  O     . ALA A 1 166 ? 145.260 33.381 -2.474  1.00 15.29  ? 166  ALA A O     1 
ATOM   1177 C  CB    . ALA A 1 166 ? 143.832 36.078 -1.504  1.00 15.15  ? 166  ALA A CB    1 
ATOM   1178 N  N     . THR A 1 167 ? 143.130 33.448 -3.142  1.00 15.50  ? 167  THR A N     1 
ATOM   1179 C  CA    . THR A 1 167 ? 143.396 32.645 -4.316  1.00 12.60  ? 167  THR A CA    1 
ATOM   1180 C  C     . THR A 1 167 ? 143.341 33.619 -5.496  1.00 12.49  ? 167  THR A C     1 
ATOM   1181 O  O     . THR A 1 167 ? 142.658 34.657 -5.419  1.00 13.46  ? 167  THR A O     1 
ATOM   1182 C  CB    . THR A 1 167 ? 142.363 31.617 -4.561  1.00 13.89  ? 167  THR A CB    1 
ATOM   1183 O  OG1   . THR A 1 167 ? 141.122 32.330 -4.564  1.00 14.46  ? 167  THR A OG1   1 
ATOM   1184 C  CG2   . THR A 1 167 ? 142.421 30.629 -3.420  1.00 13.64  ? 167  THR A CG2   1 
ATOM   1185 N  N     . ALA A 1 168 ? 144.060 33.317 -6.582  1.00 10.44  ? 168  ALA A N     1 
ATOM   1186 C  CA    . ALA A 1 168 ? 144.032 34.220 -7.727  1.00 9.46   ? 168  ALA A CA    1 
ATOM   1187 C  C     . ALA A 1 168 ? 142.611 34.194 -8.343  1.00 12.58  ? 168  ALA A C     1 
ATOM   1188 O  O     . ALA A 1 168 ? 142.202 35.105 -9.053  1.00 14.30  ? 168  ALA A O     1 
ATOM   1189 C  CB    . ALA A 1 168 ? 145.164 33.885 -8.730  1.00 12.68  ? 168  ALA A CB    1 
ATOM   1190 N  N     . TYR A 1 169 ? 141.843 33.143 -8.052  1.00 10.17  ? 169  TYR A N     1 
ATOM   1191 C  CA    . TYR A 1 169 ? 140.482 33.061 -8.582  1.00 9.82   ? 169  TYR A CA    1 
ATOM   1192 C  C     . TYR A 1 169 ? 139.649 34.246 -8.087  1.00 11.80  ? 169  TYR A C     1 
ATOM   1193 O  O     . TYR A 1 169 ? 138.649 34.591 -8.690  1.00 14.29  ? 169  TYR A O     1 
ATOM   1194 C  CB    . TYR A 1 169 ? 139.825 31.853 -7.980  1.00 9.82   ? 169  TYR A CB    1 
ATOM   1195 C  CG    . TYR A 1 169 ? 140.083 30.514 -8.627  1.00 11.03  ? 169  TYR A CG    1 
ATOM   1196 C  CD1   . TYR A 1 169 ? 140.341 29.366 -7.840  1.00 12.91  ? 169  TYR A CD1   1 
ATOM   1197 C  CD2   . TYR A 1 169 ? 140.015 30.335 -9.961  1.00 11.58  ? 169  TYR A CD2   1 
ATOM   1198 C  CE1   . TYR A 1 169 ? 140.528 28.097 -8.409  1.00 12.75  ? 169  TYR A CE1   1 
ATOM   1199 C  CE2   . TYR A 1 169 ? 140.200 29.071 -10.536 1.00 12.09  ? 169  TYR A CE2   1 
ATOM   1200 C  CZ    . TYR A 1 169 ? 140.462 27.955 -9.742  1.00 11.75  ? 169  TYR A CZ    1 
ATOM   1201 O  OH    . TYR A 1 169 ? 140.648 26.709 -10.270 1.00 14.54  ? 169  TYR A OH    1 
ATOM   1202 N  N     . THR A 1 170 ? 140.038 34.888 -6.985  1.00 10.46  ? 170  THR A N     1 
ATOM   1203 C  CA    . THR A 1 170 ? 139.263 36.036 -6.478  1.00 10.36  ? 170  THR A CA    1 
ATOM   1204 C  C     . THR A 1 170 ? 139.465 37.296 -7.328  1.00 15.83  ? 170  THR A C     1 
ATOM   1205 O  O     . THR A 1 170 ? 138.726 38.267 -7.199  1.00 18.71  ? 170  THR A O     1 
ATOM   1206 C  CB    . THR A 1 170 ? 139.569 36.457 -5.025  1.00 16.29  ? 170  THR A CB    1 
ATOM   1207 O  OG1   . THR A 1 170 ? 140.904 36.978 -4.994  1.00 22.01  ? 170  THR A OG1   1 
ATOM   1208 C  CG2   . THR A 1 170 ? 139.580 35.300 -4.050  1.00 12.49  ? 170  THR A CG2   1 
ATOM   1209 N  N     . LEU A 1 171 ? 140.463 37.287 -8.197  1.00 14.47  ? 171  LEU A N     1 
ATOM   1210 C  CA    . LEU A 1 171 ? 140.736 38.439 -9.035  1.00 13.58  ? 171  LEU A CA    1 
ATOM   1211 C  C     . LEU A 1 171 ? 139.653 38.696 -10.062 1.00 17.14  ? 171  LEU A C     1 
ATOM   1212 O  O     . LEU A 1 171 ? 139.518 39.811 -10.549 1.00 19.72  ? 171  LEU A O     1 
ATOM   1213 C  CB    . LEU A 1 171 ? 142.124 38.286 -9.678  1.00 15.64  ? 171  LEU A CB    1 
ATOM   1214 C  CG    . LEU A 1 171 ? 143.321 38.062 -8.697  1.00 22.48  ? 171  LEU A CG    1 
ATOM   1215 C  CD1   . LEU A 1 171 ? 144.639 37.888 -9.405  1.00 22.98  ? 171  LEU A CD1   1 
ATOM   1216 C  CD2   . LEU A 1 171 ? 143.447 39.144 -7.698  1.00 17.90  ? 171  LEU A CD2   1 
ATOM   1217 N  N     . THR A 1 172 ? 138.885 37.686 -10.407 1.00 16.28  ? 172  THR A N     1 
ATOM   1218 C  CA    . THR A 1 172 ? 137.817 37.884 -11.395 1.00 15.51  ? 172  THR A CA    1 
ATOM   1219 C  C     . THR A 1 172 ? 136.780 38.900 -10.918 1.00 21.58  ? 172  THR A C     1 
ATOM   1220 O  O     . THR A 1 172 ? 136.314 39.724 -11.687 1.00 29.95  ? 172  THR A O     1 
ATOM   1221 C  CB    . THR A 1 172 ? 137.118 36.557 -11.640 1.00 16.91  ? 172  THR A CB    1 
ATOM   1222 O  OG1   . THR A 1 172 ? 138.135 35.629 -12.084 1.00 17.11  ? 172  THR A OG1   1 
ATOM   1223 C  CG2   . THR A 1 172 ? 136.044 36.711 -12.704 1.00 16.19  ? 172  THR A CG2   1 
ATOM   1224 N  N     . ALA A 1 173 ? 136.418 38.857 -9.645  1.00 16.21  ? 173  ALA A N     1 
ATOM   1225 C  CA    . ALA A 1 173 ? 135.436 39.799 -9.129  1.00 17.99  ? 173  ALA A CA    1 
ATOM   1226 C  C     . ALA A 1 173 ? 136.061 41.175 -9.178  1.00 30.07  ? 173  ALA A C     1 
ATOM   1227 O  O     . ALA A 1 173 ? 135.471 42.121 -9.691  1.00 30.08  ? 173  ALA A O     1 
ATOM   1228 C  CB    . ALA A 1 173 ? 135.095 39.427 -7.681  1.00 19.53  ? 173  ALA A CB    1 
ATOM   1229 N  N     . THR A 1 174 ? 137.275 41.258 -8.643  1.00 22.00  ? 174  THR A N     1 
ATOM   1230 C  CA    . THR A 1 174 ? 138.044 42.489 -8.606  1.00 16.72  ? 174  THR A CA    1 
ATOM   1231 C  C     . THR A 1 174 ? 139.353 42.231 -7.879  1.00 20.45  ? 174  THR A C     1 
ATOM   1232 O  O     . THR A 1 174 ? 139.402 41.529 -6.884  1.00 20.92  ? 174  THR A O     1 
ATOM   1233 C  CB    . THR A 1 174 ? 137.386 43.755 -7.978  1.00 22.09  ? 174  THR A CB    1 
ATOM   1234 O  OG1   . THR A 1 174 ? 138.413 44.775 -7.837  1.00 25.35  ? 174  THR A OG1   1 
ATOM   1235 C  CG2   . THR A 1 174 ? 136.864 43.479 -6.570  1.00 19.73  ? 174  THR A CG2   1 
ATOM   1236 N  N     . PRO A 1 175 ? 140.427 42.793 -8.377  1.00 23.70  ? 175  PRO A N     1 
ATOM   1237 C  CA    . PRO A 1 175 ? 141.715 42.591 -7.734  1.00 19.22  ? 175  PRO A CA    1 
ATOM   1238 C  C     . PRO A 1 175 ? 141.828 43.428 -6.471  1.00 16.33  ? 175  PRO A C     1 
ATOM   1239 O  O     . PRO A 1 175 ? 142.712 43.210 -5.657  1.00 19.21  ? 175  PRO A O     1 
ATOM   1240 C  CB    . PRO A 1 175 ? 142.697 43.061 -8.840  1.00 22.96  ? 175  PRO A CB    1 
ATOM   1241 C  CG    . PRO A 1 175 ? 141.909 43.959 -9.703  1.00 28.71  ? 175  PRO A CG    1 
ATOM   1242 C  CD    . PRO A 1 175 ? 140.609 43.229 -9.772  1.00 25.55  ? 175  PRO A CD    1 
ATOM   1243 N  N     . LYS A 1 176 ? 140.935 44.396 -6.286  1.00 17.12  ? 176  LYS A N     1 
ATOM   1244 C  CA    . LYS A 1 176 ? 141.028 45.219 -5.082  1.00 16.75  ? 176  LYS A CA    1 
ATOM   1245 C  C     . LYS A 1 176 ? 140.953 44.397 -3.797  1.00 19.55  ? 176  LYS A C     1 
ATOM   1246 O  O     . LYS A 1 176 ? 141.666 44.670 -2.848  1.00 18.33  ? 176  LYS A O     1 
ATOM   1247 C  CB    . LYS A 1 176 ? 139.966 46.346 -4.948  1.00 17.06  ? 176  LYS A CB    1 
ATOM   1248 C  CG    . LYS A 1 176 ? 139.886 47.218 -6.162  1.00 64.15  ? 176  LYS A CG    1 
ATOM   1249 C  CD    . LYS A 1 176 ? 138.471 47.751 -6.348  1.00 97.77  ? 176  LYS A CD    1 
ATOM   1250 C  CE    . LYS A 1 176 ? 138.122 47.863 -7.826  1.00 91.60  ? 176  LYS A CE    1 
ATOM   1251 N  NZ    . LYS A 1 176 ? 139.272 48.506 -8.525  1.00 85.06  ? 176  LYS A NZ    1 
ATOM   1252 N  N     . ASN A 1 177 ? 140.092 43.391 -3.765  1.00 12.86  ? 177  ASN A N     1 
ATOM   1253 C  CA    . ASN A 1 177 ? 139.977 42.600 -2.552  1.00 14.51  ? 177  ASN A CA    1 
ATOM   1254 C  C     . ASN A 1 177 ? 141.292 42.013 -2.089  1.00 20.37  ? 177  ASN A C     1 
ATOM   1255 O  O     . ASN A 1 177 ? 141.720 42.234 -0.950  1.00 18.11  ? 177  ASN A O     1 
ATOM   1256 C  CB    . ASN A 1 177 ? 138.961 41.514 -2.619  1.00 13.71  ? 177  ASN A CB    1 
ATOM   1257 C  CG    . ASN A 1 177 ? 137.566 42.093 -2.915  1.00 29.54  ? 177  ASN A CG    1 
ATOM   1258 O  OD1   . ASN A 1 177 ? 137.208 43.138 -2.362  1.00 19.25  ? 177  ASN A OD1   1 
ATOM   1259 N  ND2   . ASN A 1 177 ? 136.800 41.452 -3.779  1.00 16.88  ? 177  ASN A ND2   1 
ATOM   1260 N  N     . ALA A 1 178 ? 141.924 41.249 -2.962  1.00 15.43  ? 178  ALA A N     1 
ATOM   1261 C  CA    . ALA A 1 178 ? 143.188 40.647 -2.571  1.00 13.11  ? 178  ALA A CA    1 
ATOM   1262 C  C     . ALA A 1 178 ? 144.239 41.735 -2.280  1.00 18.81  ? 178  ALA A C     1 
ATOM   1263 O  O     . ALA A 1 178 ? 145.077 41.580 -1.378  1.00 16.29  ? 178  ALA A O     1 
ATOM   1264 C  CB    . ALA A 1 178 ? 143.633 39.661 -3.617  1.00 15.45  ? 178  ALA A CB    1 
ATOM   1265 N  N     . LEU A 1 179 ? 144.215 42.837 -3.040  1.00 19.30  ? 179  LEU A N     1 
ATOM   1266 C  CA    . LEU A 1 179 ? 145.202 43.892 -2.798  1.00 18.65  ? 179  LEU A CA    1 
ATOM   1267 C  C     . LEU A 1 179 ? 145.016 44.482 -1.413  1.00 24.22  ? 179  LEU A C     1 
ATOM   1268 O  O     . LEU A 1 179 ? 145.986 44.809 -0.713  1.00 20.28  ? 179  LEU A O     1 
ATOM   1269 C  CB    . LEU A 1 179 ? 145.239 44.982 -3.843  1.00 18.62  ? 179  LEU A CB    1 
ATOM   1270 C  CG    . LEU A 1 179 ? 145.812 44.506 -5.168  1.00 30.96  ? 179  LEU A CG    1 
ATOM   1271 C  CD1   . LEU A 1 179 ? 145.386 45.443 -6.288  1.00 37.88  ? 179  LEU A CD1   1 
ATOM   1272 C  CD2   . LEU A 1 179 ? 147.327 44.505 -5.094  1.00 27.44  ? 179  LEU A CD2   1 
ATOM   1273 N  N     . GLU A 1 180 ? 143.773 44.622 -0.991  1.00 17.17  ? 180  GLU A N     1 
ATOM   1274 C  CA    . GLU A 1 180 ? 143.577 45.192 0.331   1.00 17.44  ? 180  GLU A CA    1 
ATOM   1275 C  C     . GLU A 1 180 ? 144.055 44.263 1.402   1.00 23.50  ? 180  GLU A C     1 
ATOM   1276 O  O     . GLU A 1 180 ? 144.602 44.705 2.419   1.00 22.85  ? 180  GLU A O     1 
ATOM   1277 C  CB    . GLU A 1 180 ? 142.132 45.493 0.558   1.00 20.44  ? 180  GLU A CB    1 
ATOM   1278 C  CG    . GLU A 1 180 ? 141.755 46.428 -0.635  1.00 42.77  ? 180  GLU A CG    1 
ATOM   1279 C  CD    . GLU A 1 180 ? 141.066 47.874 -0.208  1.00 82.66  ? 180  GLU A CD    1 
ATOM   1280 O  OE1   . GLU A 1 180 ? 139.848 47.968 -0.344  1.00 100.00 ? 180  GLU A OE1   1 
ATOM   1281 O  OE2   . GLU A 1 180 ? 141.816 48.602 0.756   1.00 75.28  ? 180  GLU A OE2   1 
ATOM   1282 N  N     . VAL A 1 181 ? 143.840 42.968 1.190   1.00 15.87  ? 181  VAL A N     1 
ATOM   1283 C  CA    . VAL A 1 181 ? 144.285 42.012 2.200   1.00 14.13  ? 181  VAL A CA    1 
ATOM   1284 C  C     . VAL A 1 181 ? 145.811 42.013 2.298   1.00 14.95  ? 181  VAL A C     1 
ATOM   1285 O  O     . VAL A 1 181 ? 146.391 42.041 3.374   1.00 21.45  ? 181  VAL A O     1 
ATOM   1286 C  CB    . VAL A 1 181 ? 143.790 40.581 1.920   1.00 19.27  ? 181  VAL A CB    1 
ATOM   1287 C  CG1   . VAL A 1 181 ? 144.335 39.626 2.985   1.00 18.02  ? 181  VAL A CG1   1 
ATOM   1288 C  CG2   . VAL A 1 181 ? 142.244 40.605 2.042   1.00 20.00  ? 181  VAL A CG2   1 
ATOM   1289 N  N     . ALA A 1 182 ? 146.458 41.981 1.173   1.00 16.74  ? 182  ALA A N     1 
ATOM   1290 C  CA    . ALA A 1 182 ? 147.919 41.971 1.168   1.00 19.78  ? 182  ALA A CA    1 
ATOM   1291 C  C     . ALA A 1 182 ? 148.465 43.252 1.790   1.00 26.20  ? 182  ALA A C     1 
ATOM   1292 O  O     . ALA A 1 182 ? 149.442 43.246 2.550   1.00 26.70  ? 182  ALA A O     1 
ATOM   1293 C  CB    . ALA A 1 182 ? 148.455 41.784 -0.260  1.00 17.73  ? 182  ALA A CB    1 
ATOM   1294 N  N     . GLY A 1 183 ? 147.828 44.357 1.469   1.00 19.18  ? 183  GLY A N     1 
ATOM   1295 C  CA    . GLY A 1 183 ? 148.257 45.637 2.000   1.00 19.20  ? 183  GLY A CA    1 
ATOM   1296 C  C     . GLY A 1 183 ? 148.224 45.593 3.511   1.00 31.77  ? 183  GLY A C     1 
ATOM   1297 O  O     . GLY A 1 183 ? 149.190 45.958 4.181   1.00 36.23  ? 183  GLY A O     1 
ATOM   1298 N  N     . TYR A 1 184 ? 147.107 45.151 4.054   1.00 24.56  ? 184  TYR A N     1 
ATOM   1299 C  CA    . TYR A 1 184 ? 146.987 45.098 5.493   1.00 23.97  ? 184  TYR A CA    1 
ATOM   1300 C  C     . TYR A 1 184 ? 148.046 44.215 6.135   1.00 28.66  ? 184  TYR A C     1 
ATOM   1301 O  O     . TYR A 1 184 ? 148.729 44.646 7.065   1.00 28.03  ? 184  TYR A O     1 
ATOM   1302 C  CB    . TYR A 1 184 ? 145.611 44.727 5.851   1.00 23.71  ? 184  TYR A CB    1 
ATOM   1303 C  CG    . TYR A 1 184 ? 145.432 44.556 7.263   1.00 24.77  ? 184  TYR A CG    1 
ATOM   1304 C  CD1   . TYR A 1 184 ? 145.340 45.670 8.100   1.00 29.69  ? 184  TYR A CD1   1 
ATOM   1305 C  CD2   . TYR A 1 184 ? 145.348 43.285 7.808   1.00 25.76  ? 184  TYR A CD2   1 
ATOM   1306 C  CE1   . TYR A 1 184 ? 145.122 45.529 9.483   1.00 27.68  ? 184  TYR A CE1   1 
ATOM   1307 C  CE2   . TYR A 1 184 ? 145.130 43.117 9.162   1.00 28.95  ? 184  TYR A CE2   1 
ATOM   1308 C  CZ    . TYR A 1 184 ? 145.027 44.245 10.002  1.00 29.21  ? 184  TYR A CZ    1 
ATOM   1309 O  OH    . TYR A 1 184 ? 144.805 44.059 11.327  1.00 47.43  ? 184  TYR A OH    1 
ATOM   1310 N  N     . ALA A 1 185 ? 148.181 42.987 5.647   1.00 21.27  ? 185  ALA A N     1 
ATOM   1311 C  CA    . ALA A 1 185 ? 149.159 42.042 6.182   1.00 22.27  ? 185  ALA A CA    1 
ATOM   1312 C  C     . ALA A 1 185 ? 150.566 42.627 6.186   1.00 28.86  ? 185  ALA A C     1 
ATOM   1313 O  O     . ALA A 1 185 ? 151.316 42.474 7.157   1.00 27.47  ? 185  ALA A O     1 
ATOM   1314 C  CB    . ALA A 1 185 ? 149.187 40.792 5.329   1.00 21.35  ? 185  ALA A CB    1 
ATOM   1315 N  N     . HIS A 1 186 ? 150.913 43.285 5.094   1.00 26.36  ? 186  HIS A N     1 
ATOM   1316 C  CA    . HIS A 1 186 ? 152.232 43.883 4.974   1.00 30.32  ? 186  HIS A CA    1 
ATOM   1317 C  C     . HIS A 1 186 ? 152.588 44.817 6.144   1.00 37.67  ? 186  HIS A C     1 
ATOM   1318 O  O     . HIS A 1 186 ? 153.690 44.789 6.675   1.00 41.24  ? 186  HIS A O     1 
ATOM   1319 C  CB    . HIS A 1 186 ? 152.271 44.646 3.658   1.00 32.99  ? 186  HIS A CB    1 
ATOM   1320 C  CG    . HIS A 1 186 ? 153.645 45.093 3.247   1.00 45.69  ? 186  HIS A CG    1 
ATOM   1321 N  ND1   . HIS A 1 186 ? 154.629 44.209 2.847   1.00 50.62  ? 186  HIS A ND1   1 
ATOM   1322 C  CD2   . HIS A 1 186 ? 154.198 46.329 3.163   1.00 49.53  ? 186  HIS A CD2   1 
ATOM   1323 C  CE1   . HIS A 1 186 ? 155.719 44.883 2.532   1.00 49.19  ? 186  HIS A CE1   1 
ATOM   1324 N  NE2   . HIS A 1 186 ? 155.484 46.167 2.718   1.00 49.19  ? 186  HIS A NE2   1 
ATOM   1325 N  N     . GLY A 1 187 ? 151.660 45.649 6.553   1.00 33.57  ? 187  GLY A N     1 
ATOM   1326 C  CA    . GLY A 1 187 ? 151.926 46.566 7.637   1.00 34.65  ? 187  GLY A CA    1 
ATOM   1327 C  C     . GLY A 1 187 ? 151.908 45.905 8.998   1.00 44.92  ? 187  GLY A C     1 
ATOM   1328 O  O     . GLY A 1 187 ? 152.140 46.563 10.002  1.00 52.00  ? 187  GLY A O     1 
ATOM   1329 N  N     . ILE A 1 188 ? 151.628 44.622 9.060   1.00 37.73  ? 188  ILE A N     1 
ATOM   1330 C  CA    . ILE A 1 188 ? 151.605 43.975 10.362  1.00 36.24  ? 188  ILE A CA    1 
ATOM   1331 C  C     . ILE A 1 188 ? 152.815 43.079 10.538  1.00 44.41  ? 188  ILE A C     1 
ATOM   1332 O  O     . ILE A 1 188 ? 153.019 42.136 9.774   1.00 42.90  ? 188  ILE A O     1 
ATOM   1333 C  CB    . ILE A 1 188 ? 150.478 42.987 10.576  1.00 38.69  ? 188  ILE A CB    1 
ATOM   1334 C  CG1   . ILE A 1 188 ? 149.100 43.643 10.659  1.00 34.87  ? 188  ILE A CG1   1 
ATOM   1335 C  CG2   . ILE A 1 188 ? 150.879 42.115 11.744  1.00 37.53  ? 188  ILE A CG2   1 
ATOM   1336 C  CD1   . ILE A 1 188 ? 149.215 45.123 10.443  1.00 62.78  ? 188  ILE A CD1   1 
ATOM   1337 N  N     . PRO A 1 189 ? 153.616 43.374 11.544  1.00 49.42  ? 189  PRO A N     1 
ATOM   1338 C  CA    . PRO A 1 189 ? 154.800 42.576 11.803  1.00 49.51  ? 189  PRO A CA    1 
ATOM   1339 C  C     . PRO A 1 189 ? 154.386 41.199 12.322  1.00 43.80  ? 189  PRO A C     1 
ATOM   1340 O  O     . PRO A 1 189 ? 153.497 41.076 13.167  1.00 48.53  ? 189  PRO A O     1 
ATOM   1341 C  CB    . PRO A 1 189 ? 155.484 43.399 12.858  1.00 52.25  ? 189  PRO A CB    1 
ATOM   1342 C  CG    . PRO A 1 189 ? 154.307 43.771 13.722  1.00 55.69  ? 189  PRO A CG    1 
ATOM   1343 C  CD    . PRO A 1 189 ? 153.193 44.074 12.762  1.00 51.24  ? 189  PRO A CD    1 
ATOM   1344 N  N     . ASN A 1 190 ? 155.033 40.172 11.802  1.00 28.28  ? 190  ASN A N     1 
ATOM   1345 C  CA    . ASN A 1 190 ? 154.757 38.794 12.183  1.00 32.03  ? 190  ASN A CA    1 
ATOM   1346 C  C     . ASN A 1 190 ? 153.591 38.200 11.401  1.00 41.10  ? 190  ASN A C     1 
ATOM   1347 O  O     . ASN A 1 190 ? 153.200 37.059 11.638  1.00 46.72  ? 190  ASN A O     1 
ATOM   1348 C  CB    . ASN A 1 190 ? 154.647 38.578 13.656  1.00 41.62  ? 190  ASN A CB    1 
ATOM   1349 C  CG    . ASN A 1 190 ? 155.735 39.229 14.312  1.00 83.80  ? 190  ASN A CG    1 
ATOM   1350 O  OD1   . ASN A 1 190 ? 155.557 39.974 15.263  1.00 100.00 ? 190  ASN A OD1   1 
ATOM   1351 N  ND2   . ASN A 1 190 ? 156.925 39.038 13.743  1.00 64.41  ? 190  ASN A ND2   1 
ATOM   1352 N  N     . ALA A 1 191 ? 153.049 38.977 10.467  1.00 29.50  ? 191  ALA A N     1 
ATOM   1353 C  CA    . ALA A 1 191 ? 151.924 38.531 9.639   1.00 28.42  ? 191  ALA A CA    1 
ATOM   1354 C  C     . ALA A 1 191 ? 152.424 38.209 8.236   1.00 25.14  ? 191  ALA A C     1 
ATOM   1355 O  O     . ALA A 1 191 ? 153.342 38.852 7.739   1.00 25.74  ? 191  ALA A O     1 
ATOM   1356 C  CB    . ALA A 1 191 ? 150.927 39.731 9.491   1.00 27.80  ? 191  ALA A CB    1 
ATOM   1357 N  N     . ILE A 1 192 ? 151.832 37.224 7.577   1.00 21.45  ? 192  ILE A N     1 
ATOM   1358 C  CA    . ILE A 1 192 ? 152.271 36.905 6.229   1.00 17.55  ? 192  ILE A CA    1 
ATOM   1359 C  C     . ILE A 1 192 ? 151.078 36.822 5.287   1.00 22.11  ? 192  ILE A C     1 
ATOM   1360 O  O     . ILE A 1 192 ? 149.980 36.454 5.696   1.00 20.82  ? 192  ILE A O     1 
ATOM   1361 C  CB    . ILE A 1 192 ? 152.902 35.543 6.094   1.00 22.86  ? 192  ILE A CB    1 
ATOM   1362 C  CG1   . ILE A 1 192 ? 152.104 34.527 6.762   1.00 20.82  ? 192  ILE A CG1   1 
ATOM   1363 C  CG2   . ILE A 1 192 ? 154.209 35.430 6.871   1.00 26.61  ? 192  ILE A CG2   1 
ATOM   1364 C  CD1   . ILE A 1 192 ? 152.859 33.234 6.739   1.00 34.77  ? 192  ILE A CD1   1 
ATOM   1365 N  N     . PHE A 1 193 ? 151.310 37.154 4.036   1.00 18.18  ? 193  PHE A N     1 
ATOM   1366 C  CA    . PHE A 1 193 ? 150.282 37.104 3.021   1.00 14.74  ? 193  PHE A CA    1 
ATOM   1367 C  C     . PHE A 1 193 ? 150.641 35.925 2.121   1.00 18.95  ? 193  PHE A C     1 
ATOM   1368 O  O     . PHE A 1 193 ? 151.785 35.807 1.662   1.00 18.32  ? 193  PHE A O     1 
ATOM   1369 C  CB    . PHE A 1 193 ? 150.166 38.401 2.235   1.00 16.09  ? 193  PHE A CB    1 
ATOM   1370 C  CG    . PHE A 1 193 ? 149.150 38.255 1.130   1.00 17.97  ? 193  PHE A CG    1 
ATOM   1371 C  CD1   . PHE A 1 193 ? 149.537 38.165 -0.183  1.00 17.80  ? 193  PHE A CD1   1 
ATOM   1372 C  CD2   . PHE A 1 193 ? 147.757 38.157 1.443   1.00 20.41  ? 193  PHE A CD2   1 
ATOM   1373 C  CE1   . PHE A 1 193 ? 148.614 37.991 -1.169  1.00 20.37  ? 193  PHE A CE1   1 
ATOM   1374 C  CE2   . PHE A 1 193 ? 146.820 37.988 0.438   1.00 18.47  ? 193  PHE A CE2   1 
ATOM   1375 C  CZ    . PHE A 1 193 ? 147.258 37.898 -0.865  1.00 18.75  ? 193  PHE A CZ    1 
ATOM   1376 N  N     . THR A 1 194 ? 149.684 35.033 1.879   1.00 12.58  ? 194  THR A N     1 
ATOM   1377 C  CA    . THR A 1 194 ? 149.926 33.859 1.027   1.00 12.95  ? 194  THR A CA    1 
ATOM   1378 C  C     . THR A 1 194 ? 148.955 33.895 -0.148  1.00 20.02  ? 194  THR A C     1 
ATOM   1379 O  O     . THR A 1 194 ? 147.801 34.301 0.004   1.00 17.27  ? 194  THR A O     1 
ATOM   1380 C  CB    . THR A 1 194 ? 149.846 32.523 1.765   1.00 18.29  ? 194  THR A CB    1 
ATOM   1381 O  OG1   . THR A 1 194 ? 148.510 32.413 2.299   1.00 23.16  ? 194  THR A OG1   1 
ATOM   1382 C  CG2   . THR A 1 194 ? 150.667 32.630 3.066   1.00 20.94  ? 194  THR A CG2   1 
ATOM   1383 N  N     . LEU A 1 195 ? 149.430 33.482 -1.312  1.00 13.02  ? 195  LEU A N     1 
ATOM   1384 C  CA    . LEU A 1 195 ? 148.621 33.491 -2.511  1.00 12.05  ? 195  LEU A CA    1 
ATOM   1385 C  C     . LEU A 1 195 ? 148.751 32.209 -3.312  1.00 13.23  ? 195  LEU A C     1 
ATOM   1386 O  O     . LEU A 1 195 ? 149.796 31.580 -3.352  1.00 14.83  ? 195  LEU A O     1 
ATOM   1387 C  CB    . LEU A 1 195 ? 149.204 34.630 -3.330  1.00 15.90  ? 195  LEU A CB    1 
ATOM   1388 C  CG    . LEU A 1 195 ? 148.635 34.984 -4.692  1.00 22.49  ? 195  LEU A CG    1 
ATOM   1389 C  CD1   . LEU A 1 195 ? 147.183 35.478 -4.536  1.00 20.74  ? 195  LEU A CD1   1 
ATOM   1390 C  CD2   . LEU A 1 195 ? 149.525 36.025 -5.337  1.00 23.88  ? 195  LEU A CD2   1 
ATOM   1391 N  N     . ASN A 1 196 ? 147.648 31.823 -3.960  1.00 10.71  ? 196  ASN A N     1 
ATOM   1392 C  CA    . ASN A 1 196 ? 147.619 30.625 -4.788  1.00 10.51  ? 196  ASN A CA    1 
ATOM   1393 C  C     . ASN A 1 196 ? 147.444 31.104 -6.238  1.00 16.27  ? 196  ASN A C     1 
ATOM   1394 O  O     . ASN A 1 196 ? 146.629 31.998 -6.507  1.00 15.02  ? 196  ASN A O     1 
ATOM   1395 C  CB    . ASN A 1 196 ? 146.429 29.738 -4.421  1.00 9.05   ? 196  ASN A CB    1 
ATOM   1396 C  CG    . ASN A 1 196 ? 146.585 28.355 -4.897  1.00 15.76  ? 196  ASN A CG    1 
ATOM   1397 O  OD1   . ASN A 1 196 ? 146.439 27.393 -4.109  1.00 22.41  ? 196  ASN A OD1   1 
ATOM   1398 N  ND2   . ASN A 1 196 ? 146.892 28.186 -6.182  1.00 11.58  ? 196  ASN A ND2   1 
ATOM   1399 N  N     . LEU A 1 197 ? 148.210 30.545 -7.180  1.00 12.81  ? 197  LEU A N     1 
ATOM   1400 C  CA    . LEU A 1 197 ? 148.094 30.949 -8.590  1.00 13.47  ? 197  LEU A CA    1 
ATOM   1401 C  C     . LEU A 1 197 ? 146.735 30.471 -9.167  1.00 18.73  ? 197  LEU A C     1 
ATOM   1402 O  O     . LEU A 1 197 ? 146.271 30.969 -10.200 1.00 16.39  ? 197  LEU A O     1 
ATOM   1403 C  CB    . LEU A 1 197 ? 149.276 30.491 -9.407  1.00 11.78  ? 197  LEU A CB    1 
ATOM   1404 C  CG    . LEU A 1 197 ? 150.600 31.129 -8.983  1.00 16.44  ? 197  LEU A CG    1 
ATOM   1405 C  CD1   . LEU A 1 197 ? 151.685 30.434 -9.851  1.00 24.21  ? 197  LEU A CD1   1 
ATOM   1406 C  CD2   . LEU A 1 197 ? 150.628 32.584 -9.243  1.00 19.32  ? 197  LEU A CD2   1 
ATOM   1407 N  N     . SER A 1 198 ? 146.122 29.496 -8.489  1.00 12.56  ? 198  SER A N     1 
ATOM   1408 C  CA    . SER A 1 198 ? 144.808 28.940 -8.834  1.00 10.45  ? 198  SER A CA    1 
ATOM   1409 C  C     . SER A 1 198 ? 144.631 28.222 -10.161 1.00 14.07  ? 198  SER A C     1 
ATOM   1410 O  O     . SER A 1 198 ? 144.193 27.074 -10.169 1.00 13.20  ? 198  SER A O     1 
ATOM   1411 C  CB    . SER A 1 198 ? 143.790 30.122 -8.776  1.00 11.81  ? 198  SER A CB    1 
ATOM   1412 O  OG    . SER A 1 198 ? 143.679 30.527 -7.426  1.00 16.75  ? 198  SER A OG    1 
ATOM   1413 N  N     . ALA A 1 199 ? 144.931 28.877 -11.274 1.00 15.21  ? 199  ALA A N     1 
ATOM   1414 C  CA    . ALA A 1 199 ? 144.774 28.235 -12.586 1.00 15.88  ? 199  ALA A CA    1 
ATOM   1415 C  C     . ALA A 1 199 ? 145.501 29.059 -13.650 1.00 18.10  ? 199  ALA A C     1 
ATOM   1416 O  O     . ALA A 1 199 ? 145.742 30.257 -13.471 1.00 18.32  ? 199  ALA A O     1 
ATOM   1417 C  CB    . ALA A 1 199 ? 143.296 28.163 -12.993 1.00 15.59  ? 199  ALA A CB    1 
ATOM   1418 N  N     . PRO A 1 200 ? 145.846 28.419 -14.756 1.00 19.22  ? 200  PRO A N     1 
ATOM   1419 C  CA    . PRO A 1 200 ? 146.557 29.134 -15.824 1.00 17.41  ? 200  PRO A CA    1 
ATOM   1420 C  C     . PRO A 1 200 ? 145.806 30.367 -16.261 1.00 20.40  ? 200  PRO A C     1 
ATOM   1421 O  O     . PRO A 1 200 ? 146.409 31.419 -16.453 1.00 22.49  ? 200  PRO A O     1 
ATOM   1422 C  CB    . PRO A 1 200 ? 146.661 28.114 -16.950 1.00 20.26  ? 200  PRO A CB    1 
ATOM   1423 C  CG    . PRO A 1 200 ? 146.752 26.799 -16.253 1.00 25.16  ? 200  PRO A CG    1 
ATOM   1424 C  CD    . PRO A 1 200 ? 145.738 26.976 -15.059 1.00 19.30  ? 200  PRO A CD    1 
ATOM   1425 N  N     . PHE A 1 201 ? 144.486 30.263 -16.402 1.00 21.62  ? 201  PHE A N     1 
ATOM   1426 C  CA    . PHE A 1 201 ? 143.718 31.434 -16.833 1.00 18.69  ? 201  PHE A CA    1 
ATOM   1427 C  C     . PHE A 1 201 ? 143.938 32.655 -15.961 1.00 19.54  ? 201  PHE A C     1 
ATOM   1428 O  O     . PHE A 1 201 ? 143.967 33.780 -16.455 1.00 19.05  ? 201  PHE A O     1 
ATOM   1429 C  CB    . PHE A 1 201 ? 142.240 31.192 -17.194 1.00 20.60  ? 201  PHE A CB    1 
ATOM   1430 C  CG    . PHE A 1 201 ? 141.305 31.259 -16.049 1.00 18.09  ? 201  PHE A CG    1 
ATOM   1431 C  CD1   . PHE A 1 201 ? 140.873 32.482 -15.584 1.00 20.18  ? 201  PHE A CD1   1 
ATOM   1432 C  CD2   . PHE A 1 201 ? 140.849 30.093 -15.461 1.00 19.11  ? 201  PHE A CD2   1 
ATOM   1433 C  CE1   . PHE A 1 201 ? 139.992 32.536 -14.527 1.00 19.20  ? 201  PHE A CE1   1 
ATOM   1434 C  CE2   . PHE A 1 201 ? 139.973 30.166 -14.379 1.00 15.60  ? 201  PHE A CE2   1 
ATOM   1435 C  CZ    . PHE A 1 201 ? 139.560 31.387 -13.934 1.00 14.76  ? 201  PHE A CZ    1 
ATOM   1436 N  N     . CYS A 1 202 ? 144.089 32.465 -14.653 1.00 19.10  ? 202  CYS A N     1 
ATOM   1437 C  CA    . CYS A 1 202 ? 144.286 33.623 -13.799 1.00 16.43  ? 202  CYS A CA    1 
ATOM   1438 C  C     . CYS A 1 202 ? 145.649 34.251 -14.044 1.00 17.55  ? 202  CYS A C     1 
ATOM   1439 O  O     . CYS A 1 202 ? 145.787 35.463 -14.013 1.00 19.64  ? 202  CYS A O     1 
ATOM   1440 C  CB    . CYS A 1 202 ? 144.214 33.305 -12.359 1.00 19.63  ? 202  CYS A CB    1 
ATOM   1441 S  SG    . CYS A 1 202 ? 142.685 32.444 -11.820 1.00 21.38  ? 202  CYS A SG    1 
ATOM   1442 N  N     . VAL A 1 203 ? 146.646 33.409 -14.276 1.00 16.01  ? 203  VAL A N     1 
ATOM   1443 C  CA    . VAL A 1 203 ? 148.006 33.902 -14.526 1.00 20.41  ? 203  VAL A CA    1 
ATOM   1444 C  C     . VAL A 1 203 ? 148.060 34.751 -15.788 1.00 22.82  ? 203  VAL A C     1 
ATOM   1445 O  O     . VAL A 1 203 ? 148.677 35.816 -15.842 1.00 22.84  ? 203  VAL A O     1 
ATOM   1446 C  CB    . VAL A 1 203 ? 148.958 32.739 -14.615 1.00 23.87  ? 203  VAL A CB    1 
ATOM   1447 C  CG1   . VAL A 1 203 ? 150.330 33.212 -15.056 1.00 26.85  ? 203  VAL A CG1   1 
ATOM   1448 C  CG2   . VAL A 1 203 ? 149.068 32.220 -13.208 1.00 23.12  ? 203  VAL A CG2   1 
ATOM   1449 N  N     . GLU A 1 204 ? 147.395 34.271 -16.809 1.00 24.96  ? 204  GLU A N     1 
ATOM   1450 C  CA    . GLU A 1 204 ? 147.361 34.974 -18.083 1.00 29.01  ? 204  GLU A CA    1 
ATOM   1451 C  C     . GLU A 1 204 ? 146.445 36.206 -18.107 1.00 38.35  ? 204  GLU A C     1 
ATOM   1452 O  O     . GLU A 1 204 ? 146.785 37.214 -18.726 1.00 42.15  ? 204  GLU A O     1 
ATOM   1453 C  CB    . GLU A 1 204 ? 147.009 33.948 -19.161 1.00 31.86  ? 204  GLU A CB    1 
ATOM   1454 C  CG    . GLU A 1 204 ? 148.141 32.973 -19.421 1.00 34.32  ? 204  GLU A CG    1 
ATOM   1455 C  CD    . GLU A 1 204 ? 148.954 33.294 -20.623 1.00 76.79  ? 204  GLU A CD    1 
ATOM   1456 O  OE1   . GLU A 1 204 ? 149.445 32.216 -21.095 1.00 100.00 ? 204  GLU A OE1   1 
ATOM   1457 O  OE2   . GLU A 1 204 ? 149.136 34.481 -21.019 1.00 78.33  ? 204  GLU A OE2   1 
ATOM   1458 N  N     . LEU A 1 205 ? 145.292 36.154 -17.450 1.00 28.22  ? 205  LEU A N     1 
ATOM   1459 C  CA    . LEU A 1 205 ? 144.387 37.314 -17.477 1.00 24.54  ? 205  LEU A CA    1 
ATOM   1460 C  C     . LEU A 1 205 ? 144.678 38.438 -16.502 1.00 27.40  ? 205  LEU A C     1 
ATOM   1461 O  O     . LEU A 1 205 ? 144.401 39.602 -16.812 1.00 28.77  ? 205  LEU A O     1 
ATOM   1462 C  CB    . LEU A 1 205 ? 142.967 36.883 -17.176 1.00 23.83  ? 205  LEU A CB    1 
ATOM   1463 C  CG    . LEU A 1 205 ? 142.221 36.405 -18.380 1.00 38.74  ? 205  LEU A CG    1 
ATOM   1464 C  CD1   . LEU A 1 205 ? 143.228 35.797 -19.320 1.00 48.20  ? 205  LEU A CD1   1 
ATOM   1465 C  CD2   . LEU A 1 205 ? 141.089 35.414 -17.988 1.00 37.16  ? 205  LEU A CD2   1 
ATOM   1466 N  N     . TYR A 1 206 ? 145.212 38.134 -15.321 1.00 26.51  ? 206  TYR A N     1 
ATOM   1467 C  CA    . TYR A 1 206 ? 145.458 39.212 -14.374 1.00 21.14  ? 206  TYR A CA    1 
ATOM   1468 C  C     . TYR A 1 206 ? 146.917 39.554 -14.146 1.00 29.60  ? 206  TYR A C     1 
ATOM   1469 O  O     . TYR A 1 206 ? 147.322 39.823 -13.017 1.00 28.54  ? 206  TYR A O     1 
ATOM   1470 C  CB    . TYR A 1 206 ? 144.680 38.865 -13.109 1.00 20.84  ? 206  TYR A CB    1 
ATOM   1471 C  CG    . TYR A 1 206 ? 143.273 38.311 -13.448 1.00 26.22  ? 206  TYR A CG    1 
ATOM   1472 C  CD1   . TYR A 1 206 ? 142.959 36.970 -13.340 1.00 33.70  ? 206  TYR A CD1   1 
ATOM   1473 C  CD2   . TYR A 1 206 ? 142.277 39.131 -13.878 1.00 28.70  ? 206  TYR A CD2   1 
ATOM   1474 C  CE1   . TYR A 1 206 ? 141.681 36.474 -13.654 1.00 29.06  ? 206  TYR A CE1   1 
ATOM   1475 C  CE2   . TYR A 1 206 ? 141.017 38.635 -14.200 1.00 31.03  ? 206  TYR A CE2   1 
ATOM   1476 C  CZ    . TYR A 1 206 ? 140.735 37.319 -14.091 1.00 35.00  ? 206  TYR A CZ    1 
ATOM   1477 O  OH    . TYR A 1 206 ? 139.480 36.830 -14.394 1.00 44.21  ? 206  TYR A OH    1 
ATOM   1478 N  N     . LYS A 1 207 ? 147.707 39.571 -15.216 1.00 34.65  ? 207  LYS A N     1 
ATOM   1479 C  CA    . LYS A 1 207 ? 149.141 39.867 -15.160 1.00 35.27  ? 207  LYS A CA    1 
ATOM   1480 C  C     . LYS A 1 207 ? 149.510 41.113 -14.377 1.00 41.00  ? 207  LYS A C     1 
ATOM   1481 O  O     . LYS A 1 207 ? 150.394 41.089 -13.533 1.00 47.31  ? 207  LYS A O     1 
ATOM   1482 C  CB    . LYS A 1 207 ? 150.016 39.553 -16.421 1.00 45.68  ? 207  LYS A CB    1 
ATOM   1483 C  CG    . LYS A 1 207 ? 150.072 40.587 -17.543 1.00 96.14  ? 207  LYS A CG    1 
ATOM   1484 C  CD    . LYS A 1 207 ? 150.315 39.957 -18.936 1.00 100.00 ? 207  LYS A CD    1 
ATOM   1485 C  CE    . LYS A 1 207 ? 149.218 40.330 -19.964 1.00 100.00 ? 207  LYS A CE    1 
ATOM   1486 N  NZ    . LYS A 1 207 ? 149.438 39.993 -21.420 1.00 100.00 ? 207  LYS A NZ    1 
ATOM   1487 N  N     . ASP A 1 208 ? 148.847 42.213 -14.639 1.00 37.22  ? 208  ASP A N     1 
ATOM   1488 C  CA    . ASP A 1 208 ? 149.178 43.427 -13.917 1.00 41.01  ? 208  ASP A CA    1 
ATOM   1489 C  C     . ASP A 1 208 ? 148.886 43.338 -12.437 1.00 38.92  ? 208  ASP A C     1 
ATOM   1490 O  O     . ASP A 1 208 ? 149.782 43.549 -11.631 1.00 44.40  ? 208  ASP A O     1 
ATOM   1491 C  CB    . ASP A 1 208 ? 148.589 44.668 -14.557 1.00 51.03  ? 208  ASP A CB    1 
ATOM   1492 C  CG    . ASP A 1 208 ? 148.324 44.445 -16.051 1.00 96.82  ? 208  ASP A CG    1 
ATOM   1493 O  OD1   . ASP A 1 208 ? 147.478 43.549 -16.398 1.00 100.00 ? 208  ASP A OD1   1 
ATOM   1494 O  OD2   . ASP A 1 208 ? 149.003 45.135 -16.863 1.00 100.00 ? 208  ASP A OD2   1 
ATOM   1495 N  N     . ALA A 1 209 ? 147.648 43.032 -12.078 1.00 28.61  ? 209  ALA A N     1 
ATOM   1496 C  CA    . ALA A 1 209 ? 147.302 42.946 -10.666 1.00 26.41  ? 209  ALA A CA    1 
ATOM   1497 C  C     . ALA A 1 209 ? 148.215 41.980 -9.946  1.00 25.80  ? 209  ALA A C     1 
ATOM   1498 O  O     . ALA A 1 209 ? 148.674 42.243 -8.832  1.00 28.80  ? 209  ALA A O     1 
ATOM   1499 C  CB    . ALA A 1 209 ? 145.831 42.540 -10.431 1.00 26.93  ? 209  ALA A CB    1 
ATOM   1500 N  N     . MET A 1 210 ? 148.484 40.857 -10.585 1.00 27.04  ? 210  MET A N     1 
ATOM   1501 C  CA    . MET A 1 210 ? 149.349 39.874 -9.954  1.00 31.41  ? 210  MET A CA    1 
ATOM   1502 C  C     . MET A 1 210 ? 150.722 40.446 -9.647  1.00 35.63  ? 210  MET A C     1 
ATOM   1503 O  O     . MET A 1 210 ? 151.302 40.170 -8.594  1.00 30.14  ? 210  MET A O     1 
ATOM   1504 C  CB    . MET A 1 210 ? 149.372 38.535 -10.647 1.00 35.35  ? 210  MET A CB    1 
ATOM   1505 C  CG    . MET A 1 210 ? 148.310 37.644 -10.044 1.00 44.47  ? 210  MET A CG    1 
ATOM   1506 S  SD    . MET A 1 210 ? 148.515 35.995 -10.642 1.00 52.71  ? 210  MET A SD    1 
ATOM   1507 C  CE    . MET A 1 210 ? 150.273 35.961 -10.580 1.00 49.52  ? 210  MET A CE    1 
ATOM   1508 N  N     . GLN A 1 211 ? 151.243 41.250 -10.565 1.00 31.58  ? 211  GLN A N     1 
ATOM   1509 C  CA    . GLN A 1 211 ? 152.561 41.841 -10.355 1.00 35.45  ? 211  GLN A CA    1 
ATOM   1510 C  C     . GLN A 1 211 ? 152.601 42.666 -9.077  1.00 35.65  ? 211  GLN A C     1 
ATOM   1511 O  O     . GLN A 1 211 ? 153.516 42.545 -8.260  1.00 35.10  ? 211  GLN A O     1 
ATOM   1512 C  CB    . GLN A 1 211 ? 153.066 42.652 -11.558 1.00 40.20  ? 211  GLN A CB    1 
ATOM   1513 C  CG    . GLN A 1 211 ? 154.593 42.556 -11.758 1.00 76.71  ? 211  GLN A CG    1 
ATOM   1514 C  CD    . GLN A 1 211 ? 155.212 43.696 -12.613 1.00 100.00 ? 211  GLN A CD    1 
ATOM   1515 O  OE1   . GLN A 1 211 ? 154.713 44.831 -12.677 1.00 99.11  ? 211  GLN A OE1   1 
ATOM   1516 N  NE2   . GLN A 1 211 ? 156.325 43.380 -13.261 1.00 100.00 ? 211  GLN A NE2   1 
ATOM   1517 N  N     . SER A 1 212 ? 151.608 43.516 -8.889  1.00 24.65  ? 212  SER A N     1 
ATOM   1518 C  CA    . SER A 1 212 ? 151.599 44.322 -7.686  1.00 22.09  ? 212  SER A CA    1 
ATOM   1519 C  C     . SER A 1 212 ? 151.411 43.432 -6.475  1.00 30.13  ? 212  SER A C     1 
ATOM   1520 O  O     . SER A 1 212 ? 152.003 43.649 -5.425  1.00 33.43  ? 212  SER A O     1 
ATOM   1521 C  CB    . SER A 1 212 ? 150.388 45.242 -7.711  1.00 35.25  ? 212  SER A CB    1 
ATOM   1522 O  OG    . SER A 1 212 ? 150.307 45.852 -8.997  1.00 68.00  ? 212  SER A OG    1 
ATOM   1523 N  N     . LEU A 1 213 ? 150.577 42.415 -6.623  1.00 22.87  ? 213  LEU A N     1 
ATOM   1524 C  CA    . LEU A 1 213 ? 150.301 41.493 -5.519  1.00 23.48  ? 213  LEU A CA    1 
ATOM   1525 C  C     . LEU A 1 213 ? 151.526 40.681 -5.083  1.00 24.52  ? 213  LEU A C     1 
ATOM   1526 O  O     . LEU A 1 213 ? 151.784 40.536 -3.888  1.00 24.02  ? 213  LEU A O     1 
ATOM   1527 C  CB    . LEU A 1 213 ? 149.161 40.549 -5.976  1.00 25.11  ? 213  LEU A CB    1 
ATOM   1528 C  CG    . LEU A 1 213 ? 147.940 40.119 -5.142  1.00 31.16  ? 213  LEU A CG    1 
ATOM   1529 C  CD1   . LEU A 1 213 ? 147.686 40.889 -3.850  1.00 22.89  ? 213  LEU A CD1   1 
ATOM   1530 C  CD2   . LEU A 1 213 ? 146.749 39.923 -6.079  1.00 28.35  ? 213  LEU A CD2   1 
ATOM   1531 N  N     . LEU A 1 214 ? 152.270 40.145 -6.053  1.00 20.85  ? 214  LEU A N     1 
ATOM   1532 C  CA    . LEU A 1 214 ? 153.457 39.332 -5.781  1.00 22.08  ? 214  LEU A CA    1 
ATOM   1533 C  C     . LEU A 1 214 ? 154.482 40.059 -4.905  1.00 32.60  ? 214  LEU A C     1 
ATOM   1534 O  O     . LEU A 1 214 ? 155.143 39.449 -4.062  1.00 31.05  ? 214  LEU A O     1 
ATOM   1535 C  CB    . LEU A 1 214 ? 154.069 38.719 -7.062  1.00 20.01  ? 214  LEU A CB    1 
ATOM   1536 C  CG    . LEU A 1 214 ? 153.279 37.633 -7.825  1.00 28.53  ? 214  LEU A CG    1 
ATOM   1537 C  CD1   . LEU A 1 214 ? 153.771 37.422 -9.270  1.00 26.48  ? 214  LEU A CD1   1 
ATOM   1538 C  CD2   . LEU A 1 214 ? 153.244 36.330 -7.074  1.00 29.59  ? 214  LEU A CD2   1 
ATOM   1539 N  N     . LEU A 1 215 ? 154.621 41.360 -5.103  1.00 28.10  ? 215  LEU A N     1 
ATOM   1540 C  CA    . LEU A 1 215 ? 155.571 42.134 -4.316  1.00 31.47  ? 215  LEU A CA    1 
ATOM   1541 C  C     . LEU A 1 215 ? 155.270 42.006 -2.836  1.00 29.29  ? 215  LEU A C     1 
ATOM   1542 O  O     . LEU A 1 215 ? 156.186 42.009 -2.017  1.00 30.08  ? 215  LEU A O     1 
ATOM   1543 C  CB    . LEU A 1 215 ? 155.370 43.612 -4.571  1.00 36.84  ? 215  LEU A CB    1 
ATOM   1544 C  CG    . LEU A 1 215 ? 156.352 44.323 -5.472  1.00 52.67  ? 215  LEU A CG    1 
ATOM   1545 C  CD1   . LEU A 1 215 ? 156.892 45.476 -4.649  1.00 61.47  ? 215  LEU A CD1   1 
ATOM   1546 C  CD2   . LEU A 1 215 ? 157.429 43.333 -5.931  1.00 52.04  ? 215  LEU A CD2   1 
ATOM   1547 N  N     . HIS A 1 216 ? 153.981 41.921 -2.497  1.00 24.39  ? 216  HIS A N     1 
ATOM   1548 C  CA    . HIS A 1 216 ? 153.552 41.827 -1.101  1.00 28.65  ? 216  HIS A CA    1 
ATOM   1549 C  C     . HIS A 1 216 ? 153.234 40.399 -0.674  1.00 24.83  ? 216  HIS A C     1 
ATOM   1550 O  O     . HIS A 1 216 ? 152.574 40.179 0.340   1.00 21.49  ? 216  HIS A O     1 
ATOM   1551 C  CB    . HIS A 1 216 ? 152.326 42.714 -0.856  1.00 35.00  ? 216  HIS A CB    1 
ATOM   1552 C  CG    . HIS A 1 216 ? 152.652 44.177 -0.854  1.00 47.09  ? 216  HIS A CG    1 
ATOM   1553 N  ND1   . HIS A 1 216 ? 153.772 44.681 -1.482  1.00 52.20  ? 216  HIS A ND1   1 
ATOM   1554 C  CD2   . HIS A 1 216 ? 152.020 45.238 -0.300  1.00 52.24  ? 216  HIS A CD2   1 
ATOM   1555 C  CE1   . HIS A 1 216 ? 153.814 45.986 -1.317  1.00 52.31  ? 216  HIS A CE1   1 
ATOM   1556 N  NE2   . HIS A 1 216 ? 152.766 46.350 -0.600  1.00 53.33  ? 216  HIS A NE2   1 
ATOM   1557 N  N     . THR A 1 217 ? 153.707 39.429 -1.436  1.00 18.83  ? 217  THR A N     1 
ATOM   1558 C  CA    . THR A 1 217 ? 153.428 38.039 -1.079  1.00 16.31  ? 217  THR A CA    1 
ATOM   1559 C  C     . THR A 1 217 ? 154.612 37.385 -0.400  1.00 21.01  ? 217  THR A C     1 
ATOM   1560 O  O     . THR A 1 217 ? 155.748 37.540 -0.838  1.00 21.08  ? 217  THR A O     1 
ATOM   1561 C  CB    . THR A 1 217 ? 153.017 37.263 -2.374  1.00 21.73  ? 217  THR A CB    1 
ATOM   1562 O  OG1   . THR A 1 217 ? 151.775 37.785 -2.833  1.00 23.29  ? 217  THR A OG1   1 
ATOM   1563 C  CG2   . THR A 1 217 ? 152.897 35.752 -2.168  1.00 19.23  ? 217  THR A CG2   1 
ATOM   1564 N  N     . ASN A 1 218 ? 154.327 36.652 0.670   1.00 15.96  ? 218  ASN A N     1 
ATOM   1565 C  CA    . ASN A 1 218 ? 155.348 35.950 1.434   1.00 17.92  ? 218  ASN A CA    1 
ATOM   1566 C  C     . ASN A 1 218 ? 155.464 34.513 0.971   1.00 25.66  ? 218  ASN A C     1 
ATOM   1567 O  O     . ASN A 1 218 ? 156.576 34.014 0.818   1.00 22.70  ? 218  ASN A O     1 
ATOM   1568 C  CB    . ASN A 1 218 ? 155.023 35.966 2.913   1.00 16.44  ? 218  ASN A CB    1 
ATOM   1569 C  CG    . ASN A 1 218 ? 155.113 37.324 3.466   1.00 29.95  ? 218  ASN A CG    1 
ATOM   1570 O  OD1   . ASN A 1 218 ? 156.206 37.868 3.638   1.00 24.96  ? 218  ASN A OD1   1 
ATOM   1571 N  ND2   . ASN A 1 218 ? 153.994 37.928 3.697   1.00 13.35  ? 218  ASN A ND2   1 
ATOM   1572 N  N     . ILE A 1 219 ? 154.311 33.852 0.753   1.00 15.69  ? 219  ILE A N     1 
ATOM   1573 C  CA    . ILE A 1 219 ? 154.302 32.456 0.297   1.00 12.59  ? 219  ILE A CA    1 
ATOM   1574 C  C     . ILE A 1 219 ? 153.408 32.284 -0.928  1.00 21.42  ? 219  ILE A C     1 
ATOM   1575 O  O     . ILE A 1 219 ? 152.228 32.595 -0.898  1.00 16.91  ? 219  ILE A O     1 
ATOM   1576 C  CB    . ILE A 1 219 ? 153.888 31.426 1.314   1.00 15.47  ? 219  ILE A CB    1 
ATOM   1577 C  CG1   . ILE A 1 219 ? 154.757 31.499 2.570   1.00 17.56  ? 219  ILE A CG1   1 
ATOM   1578 C  CG2   . ILE A 1 219 ? 154.034 30.043 0.688   1.00 13.52  ? 219  ILE A CG2   1 
ATOM   1579 C  CD1   . ILE A 1 219 ? 154.290 30.659 3.736   1.00 15.51  ? 219  ILE A CD1   1 
ATOM   1580 N  N     . LEU A 1 220 ? 153.981 31.788 -2.011  1.00 16.09  ? 220  LEU A N     1 
ATOM   1581 C  CA    . LEU A 1 220 ? 153.237 31.593 -3.229  1.00 14.00  ? 220  LEU A CA    1 
ATOM   1582 C  C     . LEU A 1 220 ? 153.092 30.127 -3.506  1.00 17.79  ? 220  LEU A C     1 
ATOM   1583 O  O     . LEU A 1 220 ? 154.070 29.391 -3.507  1.00 19.28  ? 220  LEU A O     1 
ATOM   1584 C  CB    . LEU A 1 220 ? 154.031 32.178 -4.382  1.00 16.19  ? 220  LEU A CB    1 
ATOM   1585 C  CG    . LEU A 1 220 ? 153.320 32.177 -5.724  1.00 19.03  ? 220  LEU A CG    1 
ATOM   1586 C  CD1   . LEU A 1 220 ? 152.060 33.022 -5.687  1.00 19.04  ? 220  LEU A CD1   1 
ATOM   1587 C  CD2   . LEU A 1 220 ? 154.246 32.900 -6.661  1.00 23.35  ? 220  LEU A CD2   1 
ATOM   1588 N  N     . PHE A 1 221 ? 151.861 29.703 -3.749  1.00 11.94  ? 221  PHE A N     1 
ATOM   1589 C  CA    . PHE A 1 221 ? 151.610 28.316 -4.039  1.00 11.36  ? 221  PHE A CA    1 
ATOM   1590 C  C     . PHE A 1 221 ? 151.033 28.184 -5.438  1.00 13.42  ? 221  PHE A C     1 
ATOM   1591 O  O     . PHE A 1 221 ? 150.351 29.082 -5.936  1.00 15.27  ? 221  PHE A O     1 
ATOM   1592 C  CB    . PHE A 1 221 ? 150.399 27.889 -3.143  1.00 16.57  ? 221  PHE A CB    1 
ATOM   1593 C  CG    . PHE A 1 221 ? 150.682 27.831 -1.679  1.00 15.24  ? 221  PHE A CG    1 
ATOM   1594 C  CD1   . PHE A 1 221 ? 150.238 28.811 -0.880  1.00 17.01  ? 221  PHE A CD1   1 
ATOM   1595 C  CD2   . PHE A 1 221 ? 151.347 26.775 -1.136  1.00 19.26  ? 221  PHE A CD2   1 
ATOM   1596 C  CE1   . PHE A 1 221 ? 150.466 28.770 0.481   1.00 20.07  ? 221  PHE A CE1   1 
ATOM   1597 C  CE2   . PHE A 1 221 ? 151.566 26.726 0.216   1.00 16.91  ? 221  PHE A CE2   1 
ATOM   1598 C  CZ    . PHE A 1 221 ? 151.130 27.728 1.023   1.00 15.57  ? 221  PHE A CZ    1 
ATOM   1599 N  N     . GLY A 1 222 ? 151.305 27.045 -6.066  1.00 13.67  ? 222  GLY A N     1 
ATOM   1600 C  CA    . GLY A 1 222 ? 150.799 26.784 -7.403  1.00 14.26  ? 222  GLY A CA    1 
ATOM   1601 C  C     . GLY A 1 222 ? 151.293 25.422 -7.862  1.00 20.63  ? 222  GLY A C     1 
ATOM   1602 O  O     . GLY A 1 222 ? 152.112 24.786 -7.176  1.00 17.67  ? 222  GLY A O     1 
ATOM   1603 N  N     . ASN A 1 223 ? 150.791 24.972 -9.010  1.00 18.26  ? 223  ASN A N     1 
ATOM   1604 C  CA    . ASN A 1 223 ? 151.219 23.690 -9.546  1.00 16.95  ? 223  ASN A CA    1 
ATOM   1605 C  C     . ASN A 1 223 ? 152.192 23.976 -10.690 1.00 18.98  ? 223  ASN A C     1 
ATOM   1606 O  O     . ASN A 1 223 ? 152.375 25.128 -11.104 1.00 19.29  ? 223  ASN A O     1 
ATOM   1607 C  CB    . ASN A 1 223 ? 150.150 22.700 -9.822  1.00 16.50  ? 223  ASN A CB    1 
ATOM   1608 C  CG    . ASN A 1 223 ? 149.181 23.173 -10.825 1.00 20.20  ? 223  ASN A CG    1 
ATOM   1609 O  OD1   . ASN A 1 223 ? 148.152 22.521 -11.002 1.00 38.77  ? 223  ASN A OD1   1 
ATOM   1610 N  ND2   . ASN A 1 223 ? 149.479 24.235 -11.533 1.00 17.02  ? 223  ASN A ND2   1 
ATOM   1611 N  N     . GLU A 1 224 ? 152.825 22.943 -11.216 1.00 23.94  ? 224  GLU A N     1 
ATOM   1612 C  CA    . GLU A 1 224 ? 153.780 23.130 -12.313 1.00 23.99  ? 224  GLU A CA    1 
ATOM   1613 C  C     . GLU A 1 224 ? 153.181 23.894 -13.483 1.00 21.86  ? 224  GLU A C     1 
ATOM   1614 O  O     . GLU A 1 224 ? 153.804 24.818 -14.020 1.00 23.75  ? 224  GLU A O     1 
ATOM   1615 C  CB    . GLU A 1 224 ? 154.232 21.778 -12.810 1.00 25.84  ? 224  GLU A CB    1 
ATOM   1616 C  CG    . GLU A 1 224 ? 155.498 21.858 -13.656 1.00 50.40  ? 224  GLU A CG    1 
ATOM   1617 C  CD    . GLU A 1 224 ? 156.415 20.633 -13.490 1.00 63.12  ? 224  GLU A CD    1 
ATOM   1618 O  OE1   . GLU A 1 224 ? 156.008 19.497 -13.163 1.00 48.68  ? 224  GLU A OE1   1 
ATOM   1619 O  OE2   . GLU A 1 224 ? 157.602 20.803 -13.673 1.00 58.32  ? 224  GLU A OE2   1 
ATOM   1620 N  N     . GLU A 1 225 ? 151.974 23.516 -13.888 1.00 26.78  ? 225  GLU A N     1 
ATOM   1621 C  CA    . GLU A 1 225 ? 151.327 24.195 -15.006 1.00 29.75  ? 225  GLU A CA    1 
ATOM   1622 C  C     . GLU A 1 225 ? 151.197 25.698 -14.767 1.00 31.52  ? 225  GLU A C     1 
ATOM   1623 O  O     . GLU A 1 225 ? 151.564 26.496 -15.631 1.00 30.35  ? 225  GLU A O     1 
ATOM   1624 C  CB    . GLU A 1 225 ? 150.066 23.516 -15.512 1.00 31.93  ? 225  GLU A CB    1 
ATOM   1625 C  CG    . GLU A 1 225 ? 148.786 24.227 -15.084 1.00 73.12  ? 225  GLU A CG    1 
ATOM   1626 C  CD    . GLU A 1 225 ? 148.045 23.468 -13.976 1.00 100.00 ? 225  GLU A CD    1 
ATOM   1627 O  OE1   . GLU A 1 225 ? 146.862 23.826 -13.655 1.00 70.92  ? 225  GLU A OE1   1 
ATOM   1628 O  OE2   . GLU A 1 225 ? 148.668 22.486 -13.474 1.00 97.41  ? 225  GLU A OE2   1 
ATOM   1629 N  N     . GLU A 1 226 ? 150.686 26.095 -13.597 1.00 18.86  ? 226  GLU A N     1 
ATOM   1630 C  CA    . GLU A 1 226 ? 150.544 27.520 -13.306 1.00 19.48  ? 226  GLU A CA    1 
ATOM   1631 C  C     . GLU A 1 226 ? 151.904 28.264 -13.347 1.00 21.98  ? 226  GLU A C     1 
ATOM   1632 O  O     . GLU A 1 226 ? 152.021 29.333 -13.937 1.00 23.00  ? 226  GLU A O     1 
ATOM   1633 C  CB    . GLU A 1 226 ? 149.808 27.734 -11.984 1.00 20.53  ? 226  GLU A CB    1 
ATOM   1634 C  CG    . GLU A 1 226 ? 148.405 27.166 -12.049 1.00 19.32  ? 226  GLU A CG    1 
ATOM   1635 C  CD    . GLU A 1 226 ? 147.938 26.663 -10.752 1.00 25.79  ? 226  GLU A CD    1 
ATOM   1636 O  OE1   . GLU A 1 226 ? 148.621 26.863 -9.736  1.00 19.79  ? 226  GLU A OE1   1 
ATOM   1637 O  OE2   . GLU A 1 226 ? 146.872 26.043 -10.758 1.00 32.18  ? 226  GLU A OE2   1 
ATOM   1638 N  N     . PHE A 1 227 ? 152.945 27.717 -12.710 1.00 21.44  ? 227  PHE A N     1 
ATOM   1639 C  CA    . PHE A 1 227 ? 154.275 28.379 -12.711 1.00 22.69  ? 227  PHE A CA    1 
ATOM   1640 C  C     . PHE A 1 227 ? 154.833 28.518 -14.142 1.00 30.23  ? 227  PHE A C     1 
ATOM   1641 O  O     . PHE A 1 227 ? 155.446 29.535 -14.498 1.00 30.16  ? 227  PHE A O     1 
ATOM   1642 C  CB    . PHE A 1 227 ? 155.318 27.690 -11.822 1.00 24.76  ? 227  PHE A CB    1 
ATOM   1643 C  CG    . PHE A 1 227 ? 155.165 28.046 -10.388 1.00 29.40  ? 227  PHE A CG    1 
ATOM   1644 C  CD1   . PHE A 1 227 ? 155.631 29.233 -9.902  1.00 28.67  ? 227  PHE A CD1   1 
ATOM   1645 C  CD2   . PHE A 1 227 ? 154.486 27.170 -9.505  1.00 25.40  ? 227  PHE A CD2   1 
ATOM   1646 C  CE1   . PHE A 1 227 ? 155.440 29.504 -8.555  1.00 32.39  ? 227  PHE A CE1   1 
ATOM   1647 C  CE2   . PHE A 1 227 ? 154.294 27.480 -8.169  1.00 23.95  ? 227  PHE A CE2   1 
ATOM   1648 C  CZ    . PHE A 1 227 ? 154.770 28.658 -7.689  1.00 26.22  ? 227  PHE A CZ    1 
ATOM   1649 N  N     . ALA A 1 228 ? 154.615 27.487 -14.966 1.00 32.11  ? 228  ALA A N     1 
ATOM   1650 C  CA    . ALA A 1 228 ? 155.073 27.506 -16.353 1.00 28.50  ? 228  ALA A CA    1 
ATOM   1651 C  C     . ALA A 1 228 ? 154.515 28.766 -17.020 1.00 39.86  ? 228  ALA A C     1 
ATOM   1652 O  O     . ALA A 1 228 ? 155.269 29.521 -17.639 1.00 41.94  ? 228  ALA A O     1 
ATOM   1653 C  CB    . ALA A 1 228 ? 154.625 26.292 -17.101 1.00 25.08  ? 228  ALA A CB    1 
ATOM   1654 N  N     . HIS A 1 229 ? 153.194 29.001 -16.880 1.00 28.15  ? 229  HIS A N     1 
ATOM   1655 C  CA    . HIS A 1 229 ? 152.580 30.183 -17.474 1.00 21.78  ? 229  HIS A CA    1 
ATOM   1656 C  C     . HIS A 1 229 ? 153.135 31.421 -16.803 1.00 27.59  ? 229  HIS A C     1 
ATOM   1657 O  O     . HIS A 1 229 ? 153.375 32.451 -17.427 1.00 32.61  ? 229  HIS A O     1 
ATOM   1658 C  CB    . HIS A 1 229 ? 151.056 30.182 -17.350 1.00 22.52  ? 229  HIS A CB    1 
ATOM   1659 C  CG    . HIS A 1 229 ? 150.386 29.229 -18.275 1.00 26.80  ? 229  HIS A CG    1 
ATOM   1660 N  ND1   . HIS A 1 229 ? 150.339 27.876 -18.022 1.00 31.77  ? 229  HIS A ND1   1 
ATOM   1661 C  CD2   . HIS A 1 229 ? 149.740 29.420 -19.448 1.00 28.88  ? 229  HIS A CD2   1 
ATOM   1662 C  CE1   . HIS A 1 229 ? 149.687 27.264 -19.001 1.00 32.45  ? 229  HIS A CE1   1 
ATOM   1663 N  NE2   . HIS A 1 229 ? 149.308 28.179 -19.876 1.00 32.05  ? 229  HIS A NE2   1 
ATOM   1664 N  N     . LEU A 1 230 ? 153.358 31.331 -15.502 1.00 27.01  ? 230  LEU A N     1 
ATOM   1665 C  CA    . LEU A 1 230 ? 153.899 32.481 -14.797 1.00 26.37  ? 230  LEU A CA    1 
ATOM   1666 C  C     . LEU A 1 230 ? 155.297 32.794 -15.328 1.00 35.97  ? 230  LEU A C     1 
ATOM   1667 O  O     . LEU A 1 230 ? 155.683 33.958 -15.429 1.00 35.98  ? 230  LEU A O     1 
ATOM   1668 C  CB    . LEU A 1 230 ? 153.973 32.273 -13.289 1.00 25.79  ? 230  LEU A CB    1 
ATOM   1669 C  CG    . LEU A 1 230 ? 154.397 33.496 -12.498 1.00 27.34  ? 230  LEU A CG    1 
ATOM   1670 C  CD1   . LEU A 1 230 ? 153.296 34.556 -12.322 1.00 26.05  ? 230  LEU A CD1   1 
ATOM   1671 C  CD2   . LEU A 1 230 ? 154.963 33.074 -11.186 1.00 27.79  ? 230  LEU A CD2   1 
ATOM   1672 N  N     . ALA A 1 231 ? 156.059 31.756 -15.669 1.00 34.78  ? 231  ALA A N     1 
ATOM   1673 C  CA    . ALA A 1 231 ? 157.412 31.988 -16.195 1.00 36.63  ? 231  ALA A CA    1 
ATOM   1674 C  C     . ALA A 1 231 ? 157.319 32.731 -17.522 1.00 43.70  ? 231  ALA A C     1 
ATOM   1675 O  O     . ALA A 1 231 ? 157.967 33.753 -17.720 1.00 46.91  ? 231  ALA A O     1 
ATOM   1676 C  CB    . ALA A 1 231 ? 158.227 30.717 -16.320 1.00 36.22  ? 231  ALA A CB    1 
ATOM   1677 N  N     . LYS A 1 232 ? 156.494 32.211 -18.424 1.00 37.17  ? 232  LYS A N     1 
ATOM   1678 C  CA    . LYS A 1 232 ? 156.284 32.810 -19.741 1.00 37.43  ? 232  LYS A CA    1 
ATOM   1679 C  C     . LYS A 1 232 ? 155.775 34.252 -19.624 1.00 51.12  ? 232  LYS A C     1 
ATOM   1680 O  O     . LYS A 1 232 ? 156.402 35.176 -20.144 1.00 53.93  ? 232  LYS A O     1 
ATOM   1681 C  CB    . LYS A 1 232 ? 155.287 31.935 -20.510 1.00 37.85  ? 232  LYS A CB    1 
ATOM   1682 C  CG    . LYS A 1 232 ? 155.094 32.189 -21.989 1.00 72.31  ? 232  LYS A CG    1 
ATOM   1683 C  CD    . LYS A 1 232 ? 153.764 32.870 -22.300 1.00 100.00 ? 232  LYS A CD    1 
ATOM   1684 C  CE    . LYS A 1 232 ? 152.552 32.099 -21.826 1.00 99.81  ? 232  LYS A CE    1 
ATOM   1685 N  NZ    . LYS A 1 232 ? 151.456 32.961 -22.270 1.00 100.00 ? 232  LYS A NZ    1 
ATOM   1686 N  N     . VAL A 1 233 ? 154.638 34.446 -18.937 1.00 47.62  ? 233  VAL A N     1 
ATOM   1687 C  CA    . VAL A 1 233 ? 154.052 35.777 -18.763 1.00 44.39  ? 233  VAL A CA    1 
ATOM   1688 C  C     . VAL A 1 233 ? 155.100 36.752 -18.250 1.00 53.71  ? 233  VAL A C     1 
ATOM   1689 O  O     . VAL A 1 233 ? 155.117 37.926 -18.608 1.00 54.11  ? 233  VAL A O     1 
ATOM   1690 C  CB    . VAL A 1 233 ? 152.827 35.783 -17.826 1.00 45.70  ? 233  VAL A CB    1 
ATOM   1691 C  CG1   . VAL A 1 233 ? 152.243 37.181 -17.713 1.00 45.84  ? 233  VAL A CG1   1 
ATOM   1692 C  CG2   . VAL A 1 233 ? 151.786 34.858 -18.391 1.00 45.87  ? 233  VAL A CG2   1 
ATOM   1693 N  N     . HIS A 1 234 ? 155.978 36.256 -17.408 1.00 56.30  ? 234  HIS A N     1 
ATOM   1694 C  CA    . HIS A 1 234 ? 157.011 37.107 -16.884 1.00 59.03  ? 234  HIS A CA    1 
ATOM   1695 C  C     . HIS A 1 234 ? 158.268 36.817 -17.664 1.00 73.36  ? 234  HIS A C     1 
ATOM   1696 O  O     . HIS A 1 234 ? 158.200 36.490 -18.847 1.00 78.92  ? 234  HIS A O     1 
ATOM   1697 C  CB    . HIS A 1 234 ? 156.994 37.210 -15.362 1.00 59.63  ? 234  HIS A CB    1 
ATOM   1698 C  CG    . HIS A 1 234 ? 155.781 37.945 -14.924 1.00 66.23  ? 234  HIS A CG    1 
ATOM   1699 N  ND1   . HIS A 1 234 ? 155.824 39.105 -14.183 1.00 72.33  ? 234  HIS A ND1   1 
ATOM   1700 C  CD2   . HIS A 1 234 ? 154.470 37.712 -15.176 1.00 72.43  ? 234  HIS A CD2   1 
ATOM   1701 C  CE1   . HIS A 1 234 ? 154.590 39.543 -13.972 1.00 74.00  ? 234  HIS A CE1   1 
ATOM   1702 N  NE2   . HIS A 1 234 ? 153.747 38.715 -14.566 1.00 74.13  ? 234  HIS A NE2   1 
ATOM   1703 N  N     . ASN A 1 235 ? 159.407 36.909 -17.029 1.00 70.60  ? 235  ASN A N     1 
ATOM   1704 C  CA    . ASN A 1 235 ? 160.663 36.639 -17.703 1.00 72.85  ? 235  ASN A CA    1 
ATOM   1705 C  C     . ASN A 1 235 ? 161.049 35.183 -17.479 1.00 76.73  ? 235  ASN A C     1 
ATOM   1706 O  O     . ASN A 1 235 ? 160.477 34.312 -18.122 1.00 78.99  ? 235  ASN A O     1 
ATOM   1707 C  CB    . ASN A 1 235 ? 161.679 37.644 -17.098 1.00 90.85  ? 235  ASN A CB    1 
ATOM   1708 C  CG    . ASN A 1 235 ? 161.038 38.631 -15.989 1.00 100.00 ? 235  ASN A CG    1 
ATOM   1709 O  OD1   . ASN A 1 235 ? 159.804 38.844 -15.888 1.00 100.00 ? 235  ASN A OD1   1 
ATOM   1710 N  ND2   . ASN A 1 235 ? 161.926 39.229 -15.171 1.00 99.34  ? 235  ASN A ND2   1 
ATOM   1711 N  N     . LEU A 1 236 ? 162.010 34.973 -16.570 1.00 71.74  ? 236  LEU A N     1 
ATOM   1712 C  CA    . LEU A 1 236 ? 162.556 33.679 -16.148 1.00 72.49  ? 236  LEU A CA    1 
ATOM   1713 C  C     . LEU A 1 236 ? 162.360 32.493 -17.109 1.00 83.98  ? 236  LEU A C     1 
ATOM   1714 O  O     . LEU A 1 236 ? 163.324 31.810 -17.452 1.00 80.72  ? 236  LEU A O     1 
ATOM   1715 C  CB    . LEU A 1 236 ? 161.828 33.391 -14.848 1.00 72.55  ? 236  LEU A CB    1 
ATOM   1716 C  CG    . LEU A 1 236 ? 160.394 33.965 -14.792 1.00 77.19  ? 236  LEU A CG    1 
ATOM   1717 C  CD1   . LEU A 1 236 ? 159.400 33.002 -14.137 1.00 74.51  ? 236  LEU A CD1   1 
ATOM   1718 C  CD2   . LEU A 1 236 ? 160.367 35.350 -14.137 1.00 79.18  ? 236  LEU A CD2   1 
ATOM   1719 N  N     . VAL A 1 237 ? 161.124 32.236 -17.527 1.00 90.30  ? 237  VAL A N     1 
ATOM   1720 C  CA    . VAL A 1 237 ? 160.799 31.133 -18.435 1.00 92.71  ? 237  VAL A CA    1 
ATOM   1721 C  C     . VAL A 1 237 ? 161.363 29.821 -17.907 1.00 100.00 ? 237  VAL A C     1 
ATOM   1722 O  O     . VAL A 1 237 ? 161.070 29.425 -16.777 1.00 100.00 ? 237  VAL A O     1 
ATOM   1723 C  CB    . VAL A 1 237 ? 161.079 31.377 -19.953 1.00 95.42  ? 237  VAL A CB    1 
ATOM   1724 C  CG1   . VAL A 1 237 ? 160.010 32.268 -20.576 1.00 94.62  ? 237  VAL A CG1   1 
ATOM   1725 C  CG2   . VAL A 1 237 ? 162.478 31.915 -20.196 1.00 94.32  ? 237  VAL A CG2   1 
ATOM   1726 N  N     . ALA A 1 238 ? 162.168 29.154 -18.725 1.00 99.16  ? 238  ALA A N     1 
ATOM   1727 C  CA    . ALA A 1 238 ? 162.794 27.881 -18.359 1.00 99.61  ? 238  ALA A CA    1 
ATOM   1728 C  C     . ALA A 1 238 ? 162.059 26.645 -18.873 1.00 100.00 ? 238  ALA A C     1 
ATOM   1729 O  O     . ALA A 1 238 ? 162.164 26.305 -20.055 1.00 100.00 ? 238  ALA A O     1 
ATOM   1730 C  CB    . ALA A 1 238 ? 163.309 27.772 -16.917 1.00 100.00 ? 238  ALA A CB    1 
ATOM   1731 N  N     . LYS A 1 241 ? 160.619 22.832 -13.497 1.00 68.64  ? 241  LYS A N     1 
ATOM   1732 C  CA    . LYS A 1 241 ? 160.930 22.505 -12.102 1.00 55.18  ? 241  LYS A CA    1 
ATOM   1733 C  C     . LYS A 1 241 ? 161.704 23.495 -11.244 1.00 39.72  ? 241  LYS A C     1 
ATOM   1734 O  O     . LYS A 1 241 ? 161.246 24.593 -10.974 1.00 38.45  ? 241  LYS A O     1 
ATOM   1735 C  CB    . LYS A 1 241 ? 160.570 21.163 -11.535 1.00 56.58  ? 241  LYS A CB    1 
ATOM   1736 N  N     . VAL A 1 242 ? 162.881 23.081 -10.794 1.00 28.47  ? 242  VAL A N     1 
ATOM   1737 C  CA    . VAL A 1 242 ? 163.731 23.909 -9.938  1.00 22.55  ? 242  VAL A CA    1 
ATOM   1738 C  C     . VAL A 1 242 ? 164.010 25.309 -10.433 1.00 26.52  ? 242  VAL A C     1 
ATOM   1739 O  O     . VAL A 1 242 ? 163.959 26.265 -9.654  1.00 31.18  ? 242  VAL A O     1 
ATOM   1740 C  CB    . VAL A 1 242 ? 165.012 23.190 -9.391  1.00 28.20  ? 242  VAL A CB    1 
ATOM   1741 N  N     . ALA A 1 243 ? 164.331 25.452 -11.711 1.00 24.85  ? 243  ALA A N     1 
ATOM   1742 C  CA    . ALA A 1 243 ? 164.632 26.780 -12.243 1.00 28.18  ? 243  ALA A CA    1 
ATOM   1743 C  C     . ALA A 1 243 ? 163.397 27.673 -12.223 1.00 35.31  ? 243  ALA A C     1 
ATOM   1744 O  O     . ALA A 1 243 ? 163.450 28.824 -11.783 1.00 35.27  ? 243  ALA A O     1 
ATOM   1745 C  CB    . ALA A 1 243 ? 165.186 26.679 -13.654 1.00 32.14  ? 243  ALA A CB    1 
ATOM   1746 N  N     . LEU A 1 244 ? 162.287 27.134 -12.696 1.00 38.03  ? 244  LEU A N     1 
ATOM   1747 C  CA    . LEU A 1 244 ? 161.038 27.864 -12.719 1.00 39.49  ? 244  LEU A CA    1 
ATOM   1748 C  C     . LEU A 1 244 ? 160.747 28.354 -11.307 1.00 29.52  ? 244  LEU A C     1 
ATOM   1749 O  O     . LEU A 1 244 ? 160.417 29.524 -11.097 1.00 30.78  ? 244  LEU A O     1 
ATOM   1750 C  CB    . LEU A 1 244 ? 160.017 26.818 -13.133 1.00 44.93  ? 244  LEU A CB    1 
ATOM   1751 N  N     . SER A 1 245 ? 160.888 27.434 -10.352 1.00 26.32  ? 245  SER A N     1 
ATOM   1752 C  CA    . SER A 1 245 ? 160.657 27.712 -8.937  1.00 22.64  ? 245  SER A CA    1 
ATOM   1753 C  C     . SER A 1 245 ? 161.596 28.805 -8.440  1.00 33.89  ? 245  SER A C     1 
ATOM   1754 O  O     . SER A 1 245 ? 161.142 29.763 -7.829  1.00 31.40  ? 245  SER A O     1 
ATOM   1755 C  CB    . SER A 1 245 ? 160.668 26.364 -8.128  1.00 33.51  ? 245  SER A CB    1 
ATOM   1756 O  OG    . SER A 1 245 ? 159.894 26.240 -6.914  1.00 25.16  ? 245  SER A OG    1 
ATOM   1757 N  N     . VAL A 1 246 ? 162.908 28.682 -8.705  1.00 31.85  ? 246  VAL A N     1 
ATOM   1758 C  CA    . VAL A 1 246 ? 163.860 29.711 -8.256  1.00 31.25  ? 246  VAL A CA    1 
ATOM   1759 C  C     . VAL A 1 246 ? 163.584 30.998 -8.999  1.00 31.29  ? 246  VAL A C     1 
ATOM   1760 O  O     . VAL A 1 246 ? 163.797 32.110 -8.504  1.00 32.80  ? 246  VAL A O     1 
ATOM   1761 C  CB    . VAL A 1 246 ? 165.362 29.318 -8.342  1.00 31.52  ? 246  VAL A CB    1 
ATOM   1762 N  N     . ALA A 1 247 ? 163.086 30.830 -10.202 1.00 33.77  ? 247  ALA A N     1 
ATOM   1763 C  CA    . ALA A 1 247 ? 162.757 31.976 -11.018 1.00 41.48  ? 247  ALA A CA    1 
ATOM   1764 C  C     . ALA A 1 247 ? 161.693 32.818 -10.320 1.00 39.71  ? 247  ALA A C     1 
ATOM   1765 O  O     . ALA A 1 247 ? 161.909 33.992 -10.022 1.00 39.81  ? 247  ALA A O     1 
ATOM   1766 C  CB    . ALA A 1 247 ? 162.129 31.425 -12.293 1.00 48.77  ? 247  ALA A CB    1 
ATOM   1767 N  N     . ASN A 1 248 ? 160.547 32.208 -10.056 1.00 34.38  ? 248  ASN A N     1 
ATOM   1768 C  CA    . ASN A 1 248 ? 159.448 32.906 -9.403  1.00 32.79  ? 248  ASN A CA    1 
ATOM   1769 C  C     . ASN A 1 248 ? 159.821 33.641 -8.132  1.00 33.45  ? 248  ASN A C     1 
ATOM   1770 O  O     . ASN A 1 248 ? 159.227 34.663 -7.816  1.00 32.14  ? 248  ASN A O     1 
ATOM   1771 C  CB    . ASN A 1 248 ? 158.333 32.016 -9.006  1.00 27.06  ? 248  ASN A CB    1 
ATOM   1772 N  N     . LYS A 1 249 ? 160.799 33.146 -7.408  1.00 31.49  ? 249  LYS A N     1 
ATOM   1773 C  CA    . LYS A 1 249 ? 161.140 33.832 -6.182  1.00 33.13  ? 249  LYS A CA    1 
ATOM   1774 C  C     . LYS A 1 249 ? 161.688 35.264 -6.409  1.00 33.98  ? 249  LYS A C     1 
ATOM   1775 O  O     . LYS A 1 249 ? 161.745 36.045 -5.471  1.00 39.34  ? 249  LYS A O     1 
ATOM   1776 C  CB    . LYS A 1 249 ? 161.923 32.838 -5.323  1.00 37.29  ? 249  LYS A CB    1 
ATOM   1777 N  N     . GLU A 1 250 ? 162.067 35.614 -7.626  1.00 39.09  ? 250  GLU A N     1 
ATOM   1778 C  CA    . GLU A 1 250 ? 162.543 36.975 -7.888  1.00 42.15  ? 250  GLU A CA    1 
ATOM   1779 C  C     . GLU A 1 250 ? 161.326 37.886 -7.867  1.00 46.15  ? 250  GLU A C     1 
ATOM   1780 O  O     . GLU A 1 250 ? 161.338 38.954 -7.259  1.00 46.27  ? 250  GLU A O     1 
ATOM   1781 C  CB    . GLU A 1 250 ? 163.379 37.039 -9.177  1.00 45.72  ? 250  GLU A CB    1 
ATOM   1782 N  N     . HIS A 1 251 ? 160.256 37.446 -8.532  1.00 37.57  ? 251  HIS A N     1 
ATOM   1783 C  CA    . HIS A 1 251 ? 159.025 38.217 -8.582  1.00 35.51  ? 251  HIS A CA    1 
ATOM   1784 C  C     . HIS A 1 251 ? 158.569 38.653 -7.200  1.00 46.94  ? 251  HIS A C     1 
ATOM   1785 O  O     . HIS A 1 251 ? 157.990 39.729 -7.054  1.00 55.64  ? 251  HIS A O     1 
ATOM   1786 C  CB    . HIS A 1 251 ? 157.947 37.257 -8.901  1.00 39.99  ? 251  HIS A CB    1 
ATOM   1787 N  N     . ALA A 1 252 ? 158.818 37.824 -6.188  1.00 35.02  ? 252  ALA A N     1 
ATOM   1788 C  CA    . ALA A 1 252 ? 158.405 38.177 -4.836  1.00 30.37  ? 252  ALA A CA    1 
ATOM   1789 C  C     . ALA A 1 252 ? 159.467 39.014 -4.147  1.00 43.56  ? 252  ALA A C     1 
ATOM   1790 O  O     . ALA A 1 252 ? 159.152 39.810 -3.261  1.00 41.19  ? 252  ALA A O     1 
ATOM   1791 C  CB    . ALA A 1 252 ? 158.291 36.955 -3.886  1.00 28.85  ? 252  ALA A CB    1 
ATOM   1792 N  N     . VAL A 1 253 ? 160.707 38.802 -4.572  1.00 50.20  ? 253  VAL A N     1 
ATOM   1793 C  CA    . VAL A 1 253 ? 161.889 39.465 -4.040  1.00 53.96  ? 253  VAL A CA    1 
ATOM   1794 C  C     . VAL A 1 253 ? 162.058 40.962 -4.264  1.00 65.62  ? 253  VAL A C     1 
ATOM   1795 O  O     . VAL A 1 253 ? 161.775 41.730 -3.354  1.00 70.16  ? 253  VAL A O     1 
ATOM   1796 C  CB    . VAL A 1 253 ? 163.077 38.587 -4.307  1.00 55.72  ? 253  VAL A CB    1 
ATOM   1797 N  N     . GLU A 1 254 ? 162.536 41.346 -5.441  1.00 70.96  ? 254  GLU A N     1 
ATOM   1798 C  CA    . GLU A 1 254 ? 162.777 42.748 -5.796  1.00 79.97  ? 254  GLU A CA    1 
ATOM   1799 C  C     . GLU A 1 254 ? 161.811 43.776 -5.198  1.00 92.98  ? 254  GLU A C     1 
ATOM   1800 O  O     . GLU A 1 254 ? 162.085 44.352 -4.137  1.00 91.54  ? 254  GLU A O     1 
ATOM   1801 C  CB    . GLU A 1 254 ? 163.456 43.037 -7.148  1.00 83.10  ? 254  GLU A CB    1 
ATOM   1802 N  N     . GLY A 1 270 ? 164.968 39.236 8.342   1.00 100.00 ? 270  GLY A N     1 
ATOM   1803 C  CA    . GLY A 1 270 ? 164.305 38.098 7.705   1.00 99.25  ? 270  GLY A CA    1 
ATOM   1804 C  C     . GLY A 1 270 ? 162.796 38.308 7.503   1.00 94.80  ? 270  GLY A C     1 
ATOM   1805 O  O     . GLY A 1 270 ? 162.022 38.382 8.459   1.00 100.00 ? 270  GLY A O     1 
ATOM   1806 N  N     . ALA A 1 271 ? 162.404 38.381 6.232   1.00 77.02  ? 271  ALA A N     1 
ATOM   1807 C  CA    . ALA A 1 271 ? 161.013 38.539 5.806   1.00 72.60  ? 271  ALA A CA    1 
ATOM   1808 C  C     . ALA A 1 271 ? 160.681 37.315 4.943   1.00 51.67  ? 271  ALA A C     1 
ATOM   1809 O  O     . ALA A 1 271 ? 161.319 37.082 3.920   1.00 42.75  ? 271  ALA A O     1 
ATOM   1810 C  CB    . ALA A 1 271 ? 160.746 39.812 5.052   1.00 74.79  ? 271  ALA A CB    1 
ATOM   1811 N  N     . THR A 1 272 ? 159.706 36.522 5.342   1.00 34.00  ? 272  THR A N     1 
ATOM   1812 C  CA    . THR A 1 272 ? 159.359 35.332 4.573   1.00 29.11  ? 272  THR A CA    1 
ATOM   1813 C  C     . THR A 1 272 ? 159.125 35.466 3.065   1.00 27.82  ? 272  THR A C     1 
ATOM   1814 O  O     . THR A 1 272 ? 158.266 36.203 2.592   1.00 27.12  ? 272  THR A O     1 
ATOM   1815 C  CB    . THR A 1 272 ? 158.859 34.217 5.279   1.00 35.39  ? 272  THR A CB    1 
ATOM   1816 O  OG1   . THR A 1 272 ? 158.040 33.456 4.383   1.00 33.62  ? 272  THR A OG1   1 
ATOM   1817 C  CG2   . THR A 1 272 ? 158.240 34.694 6.518   1.00 25.89  ? 272  THR A CG2   1 
ATOM   1818 N  N     . LYS A 1 273 ? 159.910 34.719 2.304   1.00 17.93  ? 273  LYS A N     1 
ATOM   1819 C  CA    . LYS A 1 273 ? 159.825 34.702 0.852   1.00 17.55  ? 273  LYS A CA    1 
ATOM   1820 C  C     . LYS A 1 273 ? 160.017 33.251 0.445   1.00 26.64  ? 273  LYS A C     1 
ATOM   1821 O  O     . LYS A 1 273 ? 161.132 32.745 0.469   1.00 21.79  ? 273  LYS A O     1 
ATOM   1822 C  CB    . LYS A 1 273 ? 160.824 35.629 0.160   1.00 20.75  ? 273  LYS A CB    1 
ATOM   1823 C  CG    . LYS A 1 273 ? 160.562 37.095 0.561   1.00 22.89  ? 273  LYS A CG    1 
ATOM   1824 C  CD    . LYS A 1 273 ? 159.357 37.561 -0.297  1.00 25.21  ? 273  LYS A CD    1 
ATOM   1825 C  CE    . LYS A 1 273 ? 158.729 38.898 0.179   1.00 28.62  ? 273  LYS A CE    1 
ATOM   1826 N  NZ    . LYS A 1 273 ? 157.809 39.561 -0.860  1.00 31.28  ? 273  LYS A NZ    1 
ATOM   1827 N  N     . LEU A 1 274 ? 158.923 32.576 0.116   1.00 15.86  ? 274  LEU A N     1 
ATOM   1828 C  CA    . LEU A 1 274 ? 159.001 31.191 -0.245  1.00 11.99  ? 274  LEU A CA    1 
ATOM   1829 C  C     . LEU A 1 274 ? 158.025 30.863 -1.367  1.00 20.21  ? 274  LEU A C     1 
ATOM   1830 O  O     . LEU A 1 274 ? 156.936 31.423 -1.446  1.00 16.25  ? 274  LEU A O     1 
ATOM   1831 C  CB    . LEU A 1 274 ? 158.498 30.535 1.085   1.00 10.84  ? 274  LEU A CB    1 
ATOM   1832 C  CG    . LEU A 1 274 ? 158.100 29.098 1.058   1.00 18.48  ? 274  LEU A CG    1 
ATOM   1833 C  CD1   . LEU A 1 274 ? 159.270 28.178 0.717   1.00 24.20  ? 274  LEU A CD1   1 
ATOM   1834 C  CD2   . LEU A 1 274 ? 157.609 28.788 2.423   1.00 18.36  ? 274  LEU A CD2   1 
ATOM   1835 N  N     . VAL A 1 275 ? 158.430 29.952 -2.239  1.00 16.03  ? 275  VAL A N     1 
ATOM   1836 C  CA    . VAL A 1 275 ? 157.593 29.523 -3.358  1.00 14.84  ? 275  VAL A CA    1 
ATOM   1837 C  C     . VAL A 1 275 ? 157.409 28.017 -3.227  1.00 21.55  ? 275  VAL A C     1 
ATOM   1838 O  O     . VAL A 1 275 ? 158.387 27.303 -3.003  1.00 17.23  ? 275  VAL A O     1 
ATOM   1839 C  CB    . VAL A 1 275 ? 157.955 29.967 -4.817  1.00 23.59  ? 275  VAL A CB    1 
ATOM   1840 C  CG1   . VAL A 1 275 ? 158.293 31.430 -4.967  1.00 22.05  ? 275  VAL A CG1   1 
ATOM   1841 C  CG2   . VAL A 1 275 ? 159.046 29.133 -5.405  1.00 32.02  ? 275  VAL A CG2   1 
ATOM   1842 N  N     . VAL A 1 276 ? 156.170 27.524 -3.320  1.00 14.72  ? 276  VAL A N     1 
ATOM   1843 C  CA    . VAL A 1 276 ? 155.908 26.100 -3.179  1.00 12.98  ? 276  VAL A CA    1 
ATOM   1844 C  C     . VAL A 1 276 ? 155.230 25.605 -4.437  1.00 23.60  ? 276  VAL A C     1 
ATOM   1845 O  O     . VAL A 1 276 ? 154.118 26.045 -4.752  1.00 20.52  ? 276  VAL A O     1 
ATOM   1846 C  CB    . VAL A 1 276 ? 154.953 25.813 -1.981  1.00 16.04  ? 276  VAL A CB    1 
ATOM   1847 C  CG1   . VAL A 1 276 ? 154.854 24.312 -1.766  1.00 17.00  ? 276  VAL A CG1   1 
ATOM   1848 C  CG2   . VAL A 1 276 ? 155.548 26.315 -0.654  1.00 17.39  ? 276  VAL A CG2   1 
ATOM   1849 N  N     . MET A 1 277 ? 155.890 24.700 -5.160  1.00 16.18  ? 277  MET A N     1 
ATOM   1850 C  CA    . MET A 1 277 ? 155.312 24.186 -6.392  1.00 15.19  ? 277  MET A CA    1 
ATOM   1851 C  C     . MET A 1 277 ? 154.896 22.736 -6.265  1.00 20.43  ? 277  MET A C     1 
ATOM   1852 O  O     . MET A 1 277 ? 155.715 21.882 -5.964  1.00 19.44  ? 277  MET A O     1 
ATOM   1853 C  CB    . MET A 1 277 ? 156.352 24.317 -7.487  1.00 17.05  ? 277  MET A CB    1 
ATOM   1854 C  CG    . MET A 1 277 ? 155.811 23.825 -8.779  1.00 22.93  ? 277  MET A CG    1 
ATOM   1855 S  SD    . MET A 1 277 ? 157.156 23.478 -10.002 1.00 31.57  ? 277  MET A SD    1 
ATOM   1856 C  CE    . MET A 1 277 ? 157.405 25.100 -10.529 1.00 24.87  ? 277  MET A CE    1 
ATOM   1857 N  N     . THR A 1 278 ? 153.614 22.440 -6.494  1.00 16.09  ? 278  THR A N     1 
ATOM   1858 C  CA    . THR A 1 278 ? 153.172 21.055 -6.387  1.00 14.15  ? 278  THR A CA    1 
ATOM   1859 C  C     . THR A 1 278 ? 153.099 20.497 -7.784  1.00 18.90  ? 278  THR A C     1 
ATOM   1860 O  O     . THR A 1 278 ? 152.968 21.257 -8.730  1.00 24.54  ? 278  THR A O     1 
ATOM   1861 C  CB    . THR A 1 278 ? 151.743 20.876 -5.710  1.00 18.74  ? 278  THR A CB    1 
ATOM   1862 O  OG1   . THR A 1 278 ? 150.883 21.743 -6.415  1.00 18.34  ? 278  THR A OG1   1 
ATOM   1863 C  CG2   . THR A 1 278 ? 151.719 21.253 -4.217  1.00 19.27  ? 278  THR A CG2   1 
ATOM   1864 N  N     . ARG A 1 279 ? 153.167 19.184 -7.917  1.00 20.33  ? 279  ARG A N     1 
ATOM   1865 C  CA    . ARG A 1 279 ? 153.125 18.584 -9.227  1.00 24.66  ? 279  ARG A CA    1 
ATOM   1866 C  C     . ARG A 1 279 ? 152.657 17.140 -9.224  1.00 27.63  ? 279  ARG A C     1 
ATOM   1867 O  O     . ARG A 1 279 ? 153.450 16.234 -9.499  1.00 23.35  ? 279  ARG A O     1 
ATOM   1868 C  CB    . ARG A 1 279 ? 154.598 18.600 -9.800  1.00 24.08  ? 279  ARG A CB    1 
ATOM   1869 C  CG    . ARG A 1 279 ? 155.690 18.626 -8.766  1.00 33.27  ? 279  ARG A CG    1 
ATOM   1870 C  CD    . ARG A 1 279 ? 156.928 19.494 -9.193  1.00 35.67  ? 279  ARG A CD    1 
ATOM   1871 N  NE    . ARG A 1 279 ? 157.637 18.902 -10.320 1.00 40.33  ? 279  ARG A NE    1 
ATOM   1872 C  CZ    . ARG A 1 279 ? 158.670 18.048 -10.258 1.00 35.80  ? 279  ARG A CZ    1 
ATOM   1873 N  NH1   . ARG A 1 279 ? 159.201 17.632 -9.132  1.00 24.52  ? 279  ARG A NH1   1 
ATOM   1874 N  NH2   . ARG A 1 279 ? 159.176 17.606 -11.390 1.00 43.32  ? 279  ARG A NH2   1 
ATOM   1875 N  N     . GLY A 1 280 ? 151.382 16.931 -8.950  1.00 21.05  ? 280  GLY A N     1 
ATOM   1876 C  CA    . GLY A 1 280 ? 150.835 15.584 -8.951  1.00 17.20  ? 280  GLY A CA    1 
ATOM   1877 C  C     . GLY A 1 280 ? 151.642 14.653 -8.091  1.00 22.05  ? 280  GLY A C     1 
ATOM   1878 O  O     . GLY A 1 280 ? 151.994 15.007 -6.968  1.00 22.81  ? 280  GLY A O     1 
ATOM   1879 N  N     . HIS A 1 281 ? 151.942 13.465 -8.626  1.00 20.76  ? 281  HIS A N     1 
ATOM   1880 C  CA    . HIS A 1 281 ? 152.710 12.482 -7.887  1.00 22.83  ? 281  HIS A CA    1 
ATOM   1881 C  C     . HIS A 1 281 ? 154.215 12.797 -7.799  1.00 29.75  ? 281  HIS A C     1 
ATOM   1882 O  O     . HIS A 1 281 ? 154.912 12.119 -7.066  1.00 26.44  ? 281  HIS A O     1 
ATOM   1883 C  CB    . HIS A 1 281 ? 152.454 11.067 -8.405  1.00 27.25  ? 281  HIS A CB    1 
ATOM   1884 C  CG    . HIS A 1 281 ? 152.959 10.867 -9.791  1.00 36.22  ? 281  HIS A CG    1 
ATOM   1885 N  ND1   . HIS A 1 281 ? 154.282 10.575 -10.066 1.00 42.00  ? 281  HIS A ND1   1 
ATOM   1886 C  CD2   . HIS A 1 281 ? 152.330 10.923 -10.989 1.00 46.11  ? 281  HIS A CD2   1 
ATOM   1887 C  CE1   . HIS A 1 281 ? 154.448 10.467 -11.372 1.00 44.52  ? 281  HIS A CE1   1 
ATOM   1888 N  NE2   . HIS A 1 281 ? 153.276 10.673 -11.955 1.00 46.77  ? 281  HIS A NE2   1 
ATOM   1889 N  N     . ASN A 1 282 ? 154.720 13.800 -8.528  1.00 24.40  ? 282  ASN A N     1 
ATOM   1890 C  CA    . ASN A 1 282 ? 156.147 14.146 -8.480  1.00 20.58  ? 282  ASN A CA    1 
ATOM   1891 C  C     . ASN A 1 282 ? 156.483 14.939 -7.222  1.00 27.95  ? 282  ASN A C     1 
ATOM   1892 O  O     . ASN A 1 282 ? 155.608 15.604 -6.667  1.00 22.79  ? 282  ASN A O     1 
ATOM   1893 C  CB    . ASN A 1 282 ? 156.523 14.900 -9.740  1.00 25.40  ? 282  ASN A CB    1 
ATOM   1894 C  CG    . ASN A 1 282 ? 156.421 13.989 -10.895 1.00 39.64  ? 282  ASN A CG    1 
ATOM   1895 O  OD1   . ASN A 1 282 ? 156.904 12.885 -10.812 1.00 31.50  ? 282  ASN A OD1   1 
ATOM   1896 N  ND2   . ASN A 1 282 ? 155.717 14.368 -11.921 1.00 38.69  ? 282  ASN A ND2   1 
ATOM   1897 N  N     . PRO A 1 283 ? 157.747 14.871 -6.774  1.00 25.48  ? 283  PRO A N     1 
ATOM   1898 C  CA    . PRO A 1 283 ? 158.170 15.580 -5.573  1.00 18.04  ? 283  PRO A CA    1 
ATOM   1899 C  C     . PRO A 1 283 ? 157.790 17.050 -5.565  1.00 19.94  ? 283  PRO A C     1 
ATOM   1900 O  O     . PRO A 1 283 ? 157.819 17.744 -6.588  1.00 19.52  ? 283  PRO A O     1 
ATOM   1901 C  CB    . PRO A 1 283 ? 159.721 15.499 -5.606  1.00 22.09  ? 283  PRO A CB    1 
ATOM   1902 C  CG    . PRO A 1 283 ? 159.972 14.268 -6.422  1.00 28.08  ? 283  PRO A CG    1 
ATOM   1903 C  CD    . PRO A 1 283 ? 158.943 14.396 -7.524  1.00 27.51  ? 283  PRO A CD    1 
ATOM   1904 N  N     . VAL A 1 284 ? 157.451 17.528 -4.385  1.00 17.15  ? 284  VAL A N     1 
ATOM   1905 C  CA    . VAL A 1 284 ? 157.088 18.921 -4.256  1.00 14.02  ? 284  VAL A CA    1 
ATOM   1906 C  C     . VAL A 1 284 ? 158.383 19.725 -4.169  1.00 24.24  ? 284  VAL A C     1 
ATOM   1907 O  O     . VAL A 1 284 ? 159.343 19.300 -3.524  1.00 21.85  ? 284  VAL A O     1 
ATOM   1908 C  CB    . VAL A 1 284 ? 156.281 19.120 -2.990  1.00 18.50  ? 284  VAL A CB    1 
ATOM   1909 C  CG1   . VAL A 1 284 ? 156.193 20.604 -2.721  1.00 17.69  ? 284  VAL A CG1   1 
ATOM   1910 C  CG2   . VAL A 1 284 ? 154.932 18.349 -3.074  1.00 19.66  ? 284  VAL A CG2   1 
ATOM   1911 N  N     . ILE A 1 285 ? 158.406 20.870 -4.828  1.00 16.39  ? 285  ILE A N     1 
ATOM   1912 C  CA    . ILE A 1 285 ? 159.580 21.711 -4.808  1.00 17.51  ? 285  ILE A CA    1 
ATOM   1913 C  C     . ILE A 1 285 ? 159.281 23.045 -4.156  1.00 21.70  ? 285  ILE A C     1 
ATOM   1914 O  O     . ILE A 1 285 ? 158.361 23.746 -4.572  1.00 23.30  ? 285  ILE A O     1 
ATOM   1915 C  CB    . ILE A 1 285 ? 160.088 21.947 -6.261  1.00 16.74  ? 285  ILE A CB    1 
ATOM   1916 C  CG1   . ILE A 1 285 ? 160.532 20.614 -6.861  1.00 19.06  ? 285  ILE A CG1   1 
ATOM   1917 C  CG2   . ILE A 1 285 ? 161.245 22.956 -6.253  1.00 23.81  ? 285  ILE A CG2   1 
ATOM   1918 C  CD1   . ILE A 1 285 ? 160.835 20.794 -8.330  1.00 35.99  ? 285  ILE A CD1   1 
ATOM   1919 N  N     . ALA A 1 286 ? 160.075 23.373 -3.134  1.00 16.34  ? 286  ALA A N     1 
ATOM   1920 C  CA    . ALA A 1 286 ? 159.951 24.616 -2.401  1.00 16.86  ? 286  ALA A CA    1 
ATOM   1921 C  C     . ALA A 1 286 ? 161.278 25.366 -2.416  1.00 24.40  ? 286  ALA A C     1 
ATOM   1922 O  O     . ALA A 1 286 ? 162.337 24.793 -2.128  1.00 22.39  ? 286  ALA A O     1 
ATOM   1923 C  CB    . ALA A 1 286 ? 159.575 24.383 -0.988  1.00 20.97  ? 286  ALA A CB    1 
ATOM   1924 N  N     . ALA A 1 287 ? 161.212 26.649 -2.752  1.00 20.16  ? 287  ALA A N     1 
ATOM   1925 C  CA    . ALA A 1 287 ? 162.415 27.478 -2.791  1.00 19.81  ? 287  ALA A CA    1 
ATOM   1926 C  C     . ALA A 1 287 ? 162.193 28.675 -1.904  1.00 24.63  ? 287  ALA A C     1 
ATOM   1927 O  O     . ALA A 1 287 ? 161.187 29.363 -2.056  1.00 19.99  ? 287  ALA A O     1 
ATOM   1928 C  CB    . ALA A 1 287 ? 162.693 27.964 -4.175  1.00 15.60  ? 287  ALA A CB    1 
ATOM   1929 N  N     . GLU A 1 288 ? 163.132 28.912 -0.981  1.00 18.62  ? 288  GLU A N     1 
ATOM   1930 C  CA    . GLU A 1 288 ? 163.020 30.032 -0.075  1.00 13.53  ? 288  GLU A CA    1 
ATOM   1931 C  C     . GLU A 1 288 ? 164.251 30.916 -0.158  1.00 30.16  ? 288  GLU A C     1 
ATOM   1932 O  O     . GLU A 1 288 ? 165.363 30.450 -0.472  1.00 21.83  ? 288  GLU A O     1 
ATOM   1933 C  CB    . GLU A 1 288 ? 163.059 29.475 1.351   1.00 17.87  ? 288  GLU A CB    1 
ATOM   1934 C  CG    . GLU A 1 288 ? 163.040 30.628 2.294   1.00 34.53  ? 288  GLU A CG    1 
ATOM   1935 C  CD    . GLU A 1 288 ? 162.857 30.135 3.675   1.00 75.40  ? 288  GLU A CD    1 
ATOM   1936 O  OE1   . GLU A 1 288 ? 163.061 28.890 3.798   1.00 38.36  ? 288  GLU A OE1   1 
ATOM   1937 O  OE2   . GLU A 1 288 ? 162.548 30.969 4.593   1.00 50.83  ? 288  GLU A OE2   1 
ATOM   1938 N  N     . GLN A 1 289 ? 164.050 32.192 0.121   1.00 21.97  ? 289  GLN A N     1 
ATOM   1939 C  CA    . GLN A 1 289 ? 165.147 33.145 0.109   1.00 25.88  ? 289  GLN A CA    1 
ATOM   1940 C  C     . GLN A 1 289 ? 165.307 33.642 1.534   1.00 31.98  ? 289  GLN A C     1 
ATOM   1941 O  O     . GLN A 1 289 ? 164.433 34.312 2.049   1.00 30.82  ? 289  GLN A O     1 
ATOM   1942 C  CB    . GLN A 1 289 ? 164.976 34.251 -0.904  1.00 27.01  ? 289  GLN A CB    1 
ATOM   1943 C  CG    . GLN A 1 289 ? 166.198 35.128 -0.963  1.00 38.93  ? 289  GLN A CG    1 
ATOM   1944 C  CD    . GLN A 1 289 ? 166.053 36.276 -1.920  1.00 43.75  ? 289  GLN A CD    1 
ATOM   1945 O  OE1   . GLN A 1 289 ? 166.042 36.103 -3.120  1.00 49.62  ? 289  GLN A OE1   1 
ATOM   1946 N  NE2   . GLN A 1 289 ? 165.927 37.471 -1.386  1.00 37.43  ? 289  GLN A NE2   1 
ATOM   1947 N  N     . THR A 1 290 ? 166.410 33.295 2.174   1.00 27.58  ? 290  THR A N     1 
ATOM   1948 C  CA    . THR A 1 290 ? 166.641 33.724 3.545   1.00 24.28  ? 290  THR A CA    1 
ATOM   1949 C  C     . THR A 1 290 ? 167.073 35.174 3.609   1.00 21.59  ? 290  THR A C     1 
ATOM   1950 O  O     . THR A 1 290 ? 167.270 35.820 2.583   1.00 26.43  ? 290  THR A O     1 
ATOM   1951 C  CB    . THR A 1 290 ? 167.615 32.873 4.231   1.00 38.48  ? 290  THR A CB    1 
ATOM   1952 O  OG1   . THR A 1 290 ? 168.816 32.916 3.468   1.00 49.39  ? 290  THR A OG1   1 
ATOM   1953 C  CG2   . THR A 1 290 ? 167.087 31.461 4.258   1.00 25.61  ? 290  THR A CG2   1 
ATOM   1954 N  N     . ALA A 1 291 ? 167.202 35.691 4.822   1.00 31.61  ? 291  ALA A N     1 
ATOM   1955 C  CA    . ALA A 1 291 ? 167.584 37.083 5.048   1.00 34.82  ? 291  ALA A CA    1 
ATOM   1956 C  C     . ALA A 1 291 ? 168.870 37.526 4.356   1.00 51.97  ? 291  ALA A C     1 
ATOM   1957 O  O     . ALA A 1 291 ? 168.914 38.617 3.773   1.00 53.18  ? 291  ALA A O     1 
ATOM   1958 C  CB    . ALA A 1 291 ? 167.560 37.447 6.495   1.00 34.77  ? 291  ALA A CB    1 
ATOM   1959 N  N     . ASP A 1 292 ? 169.907 36.682 4.426   1.00 51.74  ? 292  ASP A N     1 
ATOM   1960 C  CA    . ASP A 1 292 ? 171.222 36.962 3.825   1.00 44.82  ? 292  ASP A CA    1 
ATOM   1961 C  C     . ASP A 1 292 ? 171.229 36.830 2.312   1.00 43.50  ? 292  ASP A C     1 
ATOM   1962 O  O     . ASP A 1 292 ? 172.238 37.094 1.671   1.00 45.68  ? 292  ASP A O     1 
ATOM   1963 C  CB    . ASP A 1 292 ? 172.286 36.001 4.344   1.00 43.23  ? 292  ASP A CB    1 
ATOM   1964 C  CG    . ASP A 1 292 ? 171.857 34.584 4.128   1.00 61.53  ? 292  ASP A CG    1 
ATOM   1965 O  OD1   . ASP A 1 292 ? 171.317 34.188 3.135   1.00 59.21  ? 292  ASP A OD1   1 
ATOM   1966 O  OD2   . ASP A 1 292 ? 172.040 33.759 5.055   1.00 82.82  ? 292  ASP A OD2   1 
ATOM   1967 N  N     . GLY A 1 293 ? 170.113 36.414 1.736   1.00 33.86  ? 293  GLY A N     1 
ATOM   1968 C  CA    . GLY A 1 293 ? 170.060 36.272 0.297   1.00 23.87  ? 293  GLY A CA    1 
ATOM   1969 C  C     . GLY A 1 293 ? 170.356 34.833 -0.090  1.00 22.59  ? 293  GLY A C     1 
ATOM   1970 O  O     . GLY A 1 293 ? 170.368 34.488 -1.273  1.00 30.43  ? 293  GLY A O     1 
ATOM   1971 N  N     . THR A 1 294 ? 170.587 33.984 0.901   1.00 20.21  ? 294  THR A N     1 
ATOM   1972 C  CA    . THR A 1 294 ? 170.862 32.586 0.579   1.00 18.24  ? 294  THR A CA    1 
ATOM   1973 C  C     . THR A 1 294 ? 169.581 31.936 0.056   1.00 26.58  ? 294  THR A C     1 
ATOM   1974 O  O     . THR A 1 294 ? 168.497 32.197 0.582   1.00 25.83  ? 294  THR A O     1 
ATOM   1975 C  CB    . THR A 1 294 ? 171.248 31.739 1.820   1.00 29.65  ? 294  THR A CB    1 
ATOM   1976 O  OG1   . THR A 1 294 ? 172.419 32.277 2.441   1.00 31.60  ? 294  THR A OG1   1 
ATOM   1977 C  CG2   . THR A 1 294 ? 171.535 30.307 1.428   1.00 24.86  ? 294  THR A CG2   1 
ATOM   1978 N  N     . VAL A 1 295 ? 169.711 31.103 -0.970  1.00 23.58  ? 295  VAL A N     1 
ATOM   1979 C  CA    . VAL A 1 295 ? 168.549 30.427 -1.529  1.00 20.55  ? 295  VAL A CA    1 
ATOM   1980 C  C     . VAL A 1 295 ? 168.596 28.965 -1.154  1.00 27.45  ? 295  VAL A C     1 
ATOM   1981 O  O     . VAL A 1 295 ? 169.574 28.281 -1.484  1.00 24.89  ? 295  VAL A O     1 
ATOM   1982 C  CB    . VAL A 1 295 ? 168.503 30.451 -3.049  1.00 23.49  ? 295  VAL A CB    1 
ATOM   1983 C  CG1   . VAL A 1 295 ? 167.346 29.611 -3.592  1.00 23.34  ? 295  VAL A CG1   1 
ATOM   1984 C  CG2   . VAL A 1 295 ? 168.286 31.874 -3.503  1.00 27.08  ? 295  VAL A CG2   1 
ATOM   1985 N  N     . VAL A 1 296 ? 167.544 28.502 -0.471  1.00 19.32  ? 296  VAL A N     1 
ATOM   1986 C  CA    . VAL A 1 296 ? 167.436 27.111 -0.044  1.00 14.68  ? 296  VAL A CA    1 
ATOM   1987 C  C     . VAL A 1 296 ? 166.287 26.467 -0.834  1.00 28.15  ? 296  VAL A C     1 
ATOM   1988 O  O     . VAL A 1 296 ? 165.178 27.021 -0.913  1.00 24.08  ? 296  VAL A O     1 
ATOM   1989 C  CB    . VAL A 1 296 ? 167.181 27.095 1.423   1.00 20.21  ? 296  VAL A CB    1 
ATOM   1990 C  CG1   . VAL A 1 296 ? 167.412 25.720 1.943   1.00 23.64  ? 296  VAL A CG1   1 
ATOM   1991 C  CG2   . VAL A 1 296 ? 168.135 28.037 2.140   1.00 24.65  ? 296  VAL A CG2   1 
ATOM   1992 N  N     . VAL A 1 297 ? 166.550 25.310 -1.419  1.00 21.57  ? 297  VAL A N     1 
ATOM   1993 C  CA    . VAL A 1 297 ? 165.537 24.620 -2.190  1.00 24.33  ? 297  VAL A CA    1 
ATOM   1994 C  C     . VAL A 1 297 ? 165.299 23.229 -1.643  1.00 29.61  ? 297  VAL A C     1 
ATOM   1995 O  O     . VAL A 1 297 ? 166.252 22.498 -1.400  1.00 22.58  ? 297  VAL A O     1 
ATOM   1996 C  CB    . VAL A 1 297 ? 166.106 24.431 -3.606  1.00 28.79  ? 297  VAL A CB    1 
ATOM   1997 C  CG1   . VAL A 1 297 ? 165.210 23.589 -4.467  1.00 30.61  ? 297  VAL A CG1   1 
ATOM   1998 C  CG2   . VAL A 1 297 ? 166.335 25.781 -4.249  1.00 29.87  ? 297  VAL A CG2   1 
ATOM   1999 N  N     . HIS A 1 298 ? 164.038 22.864 -1.422  1.00 21.83  ? 298  HIS A N     1 
ATOM   2000 C  CA    . HIS A 1 298 ? 163.777 21.531 -0.914  1.00 18.40  ? 298  HIS A CA    1 
ATOM   2001 C  C     . HIS A 1 298 ? 162.992 20.751 -1.967  1.00 24.32  ? 298  HIS A C     1 
ATOM   2002 O  O     . HIS A 1 298 ? 162.104 21.306 -2.595  1.00 22.84  ? 298  HIS A O     1 
ATOM   2003 C  CB    . HIS A 1 298 ? 162.883 21.467 0.310   1.00 19.00  ? 298  HIS A CB    1 
ATOM   2004 C  CG    . HIS A 1 298 ? 163.521 21.931 1.564   1.00 22.54  ? 298  HIS A CG    1 
ATOM   2005 N  ND1   . HIS A 1 298 ? 163.924 21.072 2.563   1.00 25.52  ? 298  HIS A ND1   1 
ATOM   2006 C  CD2   . HIS A 1 298 ? 163.808 23.173 1.988   1.00 15.32  ? 298  HIS A CD2   1 
ATOM   2007 C  CE1   . HIS A 1 298 ? 164.443 21.789 3.555   1.00 22.87  ? 298  HIS A CE1   1 
ATOM   2008 N  NE2   . HIS A 1 298 ? 164.375 23.069 3.224   1.00 21.97  ? 298  HIS A NE2   1 
ATOM   2009 N  N     . GLU A 1 299 ? 163.335 19.476 -2.146  1.00 20.59  ? 299  GLU A N     1 
ATOM   2010 C  CA    . GLU A 1 299 ? 162.679 18.575 -3.080  1.00 18.81  ? 299  GLU A CA    1 
ATOM   2011 C  C     . GLU A 1 299 ? 162.186 17.436 -2.214  1.00 21.18  ? 299  GLU A C     1 
ATOM   2012 O  O     . GLU A 1 299 ? 162.960 16.571 -1.847  1.00 19.66  ? 299  GLU A O     1 
ATOM   2013 C  CB    . GLU A 1 299 ? 163.613 18.137 -4.187  1.00 22.42  ? 299  GLU A CB    1 
ATOM   2014 C  CG    . GLU A 1 299 ? 164.355 19.287 -4.833  1.00 31.98  ? 299  GLU A CG    1 
ATOM   2015 C  CD    . GLU A 1 299 ? 165.024 18.889 -6.169  1.00 52.01  ? 299  GLU A CD    1 
ATOM   2016 O  OE1   . GLU A 1 299 ? 164.929 17.710 -6.560  1.00 51.91  ? 299  GLU A OE1   1 
ATOM   2017 O  OE2   . GLU A 1 299 ? 165.657 19.759 -6.811  1.00 49.65  ? 299  GLU A OE2   1 
ATOM   2018 N  N     . VAL A 1 300 ? 160.897 17.448 -1.860  1.00 20.00  ? 300  VAL A N     1 
ATOM   2019 C  CA    . VAL A 1 300 ? 160.304 16.418 -0.998  1.00 14.40  ? 300  VAL A CA    1 
ATOM   2020 C  C     . VAL A 1 300 ? 159.415 15.444 -1.754  1.00 27.34  ? 300  VAL A C     1 
ATOM   2021 O  O     . VAL A 1 300 ? 158.468 15.839 -2.456  1.00 23.84  ? 300  VAL A O     1 
ATOM   2022 C  CB    . VAL A 1 300 ? 159.423 17.151 -0.029  1.00 17.96  ? 300  VAL A CB    1 
ATOM   2023 C  CG1   . VAL A 1 300 ? 158.882 16.190 1.006   1.00 21.35  ? 300  VAL A CG1   1 
ATOM   2024 C  CG2   . VAL A 1 300 ? 160.199 18.264 0.656   1.00 17.32  ? 300  VAL A CG2   1 
ATOM   2025 N  N     . GLY A 1 301 ? 159.727 14.162 -1.606  1.00 20.70  ? 301  GLY A N     1 
ATOM   2026 C  CA    . GLY A 1 301 ? 158.958 13.143 -2.292  1.00 19.86  ? 301  GLY A CA    1 
ATOM   2027 C  C     . GLY A 1 301 ? 157.535 13.038 -1.758  1.00 26.95  ? 301  GLY A C     1 
ATOM   2028 O  O     . GLY A 1 301 ? 157.240 13.378 -0.620  1.00 24.96  ? 301  GLY A O     1 
ATOM   2029 N  N     . VAL A 1 302 ? 156.663 12.561 -2.612  1.00 24.63  ? 302  VAL A N     1 
ATOM   2030 C  CA    . VAL A 1 302 ? 155.273 12.380 -2.252  1.00 18.24  ? 302  VAL A CA    1 
ATOM   2031 C  C     . VAL A 1 302 ? 155.044 10.878 -2.186  1.00 20.63  ? 302  VAL A C     1 
ATOM   2032 O  O     . VAL A 1 302 ? 155.338 10.175 -3.148  1.00 22.32  ? 302  VAL A O     1 
ATOM   2033 C  CB    . VAL A 1 302 ? 154.493 12.923 -3.432  1.00 23.53  ? 302  VAL A CB    1 
ATOM   2034 C  CG1   . VAL A 1 302 ? 153.066 12.425 -3.474  1.00 24.60  ? 302  VAL A CG1   1 
ATOM   2035 C  CG2   . VAL A 1 302 ? 154.531 14.417 -3.391  1.00 21.27  ? 302  VAL A CG2   1 
ATOM   2036 N  N     . PRO A 1 303 ? 154.567 10.406 -1.059  1.00 23.70  ? 303  PRO A N     1 
ATOM   2037 C  CA    . PRO A 1 303 ? 154.290 8.979  -0.865  1.00 26.40  ? 303  PRO A CA    1 
ATOM   2038 C  C     . PRO A 1 303 ? 153.448 8.444  -2.017  1.00 28.16  ? 303  PRO A C     1 
ATOM   2039 O  O     . PRO A 1 303 ? 152.518 9.076  -2.510  1.00 26.72  ? 303  PRO A O     1 
ATOM   2040 C  CB    . PRO A 1 303 ? 153.630 8.949  0.482   1.00 28.47  ? 303  PRO A CB    1 
ATOM   2041 C  CG    . PRO A 1 303 ? 154.303 10.096 1.197   1.00 34.34  ? 303  PRO A CG    1 
ATOM   2042 C  CD    . PRO A 1 303 ? 154.584 11.173 0.179   1.00 26.93  ? 303  PRO A CD    1 
ATOM   2043 N  N     . VAL A 1 304 ? 153.781 7.266  -2.468  1.00 30.70  ? 304  VAL A N     1 
ATOM   2044 C  CA    . VAL A 1 304 ? 153.060 6.659  -3.579  1.00 33.57  ? 304  VAL A CA    1 
ATOM   2045 C  C     . VAL A 1 304 ? 151.649 6.199  -3.242  1.00 32.87  ? 304  VAL A C     1 
ATOM   2046 O  O     . VAL A 1 304 ? 151.396 5.611  -2.188  1.00 34.81  ? 304  VAL A O     1 
ATOM   2047 C  CB    . VAL A 1 304 ? 153.779 5.362  -3.903  1.00 41.91  ? 304  VAL A CB    1 
ATOM   2048 C  CG1   . VAL A 1 304 ? 152.959 4.533  -4.875  1.00 43.49  ? 304  VAL A CG1   1 
ATOM   2049 C  CG2   . VAL A 1 304 ? 155.181 5.662  -4.365  1.00 42.63  ? 304  VAL A CG2   1 
ATOM   2050 N  N     . VAL A 1 305 ? 150.740 6.463  -4.161  1.00 30.80  ? 305  VAL A N     1 
ATOM   2051 C  CA    . VAL A 1 305 ? 149.346 6.066  -4.000  1.00 29.70  ? 305  VAL A CA    1 
ATOM   2052 C  C     . VAL A 1 305 ? 148.957 5.297  -5.257  1.00 27.10  ? 305  VAL A C     1 
ATOM   2053 O  O     . VAL A 1 305 ? 148.972 5.865  -6.340  1.00 28.30  ? 305  VAL A O     1 
ATOM   2054 C  CB    . VAL A 1 305 ? 148.351 7.241  -3.765  1.00 30.17  ? 305  VAL A CB    1 
ATOM   2055 C  CG1   . VAL A 1 305 ? 146.963 6.635  -3.593  1.00 30.58  ? 305  VAL A CG1   1 
ATOM   2056 C  CG2   . VAL A 1 305 ? 148.688 8.132  -2.566  1.00 28.07  ? 305  VAL A CG2   1 
ATOM   2057 N  N     . ALA A 1 306 ? 148.634 4.019  -5.124  1.00 20.87  ? 306  ALA A N     1 
ATOM   2058 C  CA    . ALA A 1 306 ? 148.258 3.221  -6.288  1.00 23.30  ? 306  ALA A CA    1 
ATOM   2059 C  C     . ALA A 1 306 ? 147.140 3.896  -7.045  1.00 26.28  ? 306  ALA A C     1 
ATOM   2060 O  O     . ALA A 1 306 ? 146.235 4.453  -6.433  1.00 33.49  ? 306  ALA A O     1 
ATOM   2061 C  CB    . ALA A 1 306 ? 147.836 1.867  -5.864  1.00 24.26  ? 306  ALA A CB    1 
ATOM   2062 N  N     . ALA A 1 307 ? 147.208 3.862  -8.362  1.00 27.31  ? 307  ALA A N     1 
ATOM   2063 C  CA    . ALA A 1 307 ? 146.171 4.505  -9.157  1.00 32.13  ? 307  ALA A CA    1 
ATOM   2064 C  C     . ALA A 1 307 ? 144.764 3.955  -8.882  1.00 34.37  ? 307  ALA A C     1 
ATOM   2065 O  O     . ALA A 1 307 ? 143.786 4.705  -8.821  1.00 32.51  ? 307  ALA A O     1 
ATOM   2066 C  CB    . ALA A 1 307 ? 146.515 4.532  -10.660 1.00 32.93  ? 307  ALA A CB    1 
ATOM   2067 N  N     . GLU A 1 308 ? 144.654 2.647  -8.732  1.00 25.56  ? 308  GLU A N     1 
ATOM   2068 C  CA    . GLU A 1 308 ? 143.349 2.057  -8.498  1.00 28.09  ? 308  GLU A CA    1 
ATOM   2069 C  C     . GLU A 1 308 ? 142.719 2.525  -7.200  1.00 28.61  ? 308  GLU A C     1 
ATOM   2070 O  O     . GLU A 1 308 ? 141.531 2.315  -6.947  1.00 32.99  ? 308  GLU A O     1 
ATOM   2071 C  CB    . GLU A 1 308 ? 143.137 0.591  -9.001  1.00 31.51  ? 308  GLU A CB    1 
ATOM   2072 C  CG    . GLU A 1 308 ? 144.325 -0.320 -8.907  1.00 50.29  ? 308  GLU A CG    1 
ATOM   2073 C  CD    . GLU A 1 308 ? 145.431 0.031  -9.880  1.00 74.13  ? 308  GLU A CD    1 
ATOM   2074 O  OE1   . GLU A 1 308 ? 145.261 -0.288 -11.066 1.00 64.98  ? 308  GLU A OE1   1 
ATOM   2075 O  OE2   . GLU A 1 308 ? 146.477 0.607  -9.472  1.00 52.99  ? 308  GLU A OE2   1 
ATOM   2076 N  N     . LYS A 1 309 ? 143.502 3.177  -6.359  1.00 21.67  ? 309  LYS A N     1 
ATOM   2077 C  CA    . LYS A 1 309 ? 142.959 3.651  -5.093  1.00 22.16  ? 309  LYS A CA    1 
ATOM   2078 C  C     . LYS A 1 309 ? 142.497 5.098  -5.197  1.00 26.55  ? 309  LYS A C     1 
ATOM   2079 O  O     . LYS A 1 309 ? 141.876 5.632  -4.278  1.00 27.66  ? 309  LYS A O     1 
ATOM   2080 C  CB    . LYS A 1 309 ? 144.001 3.551  -3.962  1.00 30.55  ? 309  LYS A CB    1 
ATOM   2081 C  CG    . LYS A 1 309 ? 143.925 2.251  -3.177  1.00 57.75  ? 309  LYS A CG    1 
ATOM   2082 C  CD    . LYS A 1 309 ? 144.906 2.357  -2.052  1.00 68.19  ? 309  LYS A CD    1 
ATOM   2083 C  CE    . LYS A 1 309 ? 144.984 3.832  -1.707  1.00 100.00 ? 309  LYS A CE    1 
ATOM   2084 N  NZ    . LYS A 1 309 ? 146.007 4.048  -0.647  1.00 100.00 ? 309  LYS A NZ    1 
ATOM   2085 N  N     . ILE A 1 310 ? 142.803 5.739  -6.310  1.00 24.17  ? 310  ILE A N     1 
ATOM   2086 C  CA    . ILE A 1 310 ? 142.398 7.124  -6.464  1.00 28.45  ? 310  ILE A CA    1 
ATOM   2087 C  C     . ILE A 1 310 ? 140.967 7.229  -6.937  1.00 26.23  ? 310  ILE A C     1 
ATOM   2088 O  O     . ILE A 1 310 ? 140.622 6.564  -7.897  1.00 29.73  ? 310  ILE A O     1 
ATOM   2089 C  CB    . ILE A 1 310 ? 143.264 7.766  -7.521  1.00 30.38  ? 310  ILE A CB    1 
ATOM   2090 C  CG1   . ILE A 1 310 ? 144.697 7.705  -6.971  1.00 33.62  ? 310  ILE A CG1   1 
ATOM   2091 C  CG2   . ILE A 1 310 ? 142.770 9.198  -7.805  1.00 27.67  ? 310  ILE A CG2   1 
ATOM   2092 C  CD1   . ILE A 1 310 ? 145.643 8.693  -7.559  1.00 28.81  ? 310  ILE A CD1   1 
ATOM   2093 N  N     . VAL A 1 311 ? 140.155 8.053  -6.258  1.00 24.09  ? 311  VAL A N     1 
ATOM   2094 C  CA    . VAL A 1 311 ? 138.740 8.269  -6.623  1.00 21.59  ? 311  VAL A CA    1 
ATOM   2095 C  C     . VAL A 1 311 ? 138.715 9.388  -7.658  1.00 24.61  ? 311  VAL A C     1 
ATOM   2096 O  O     . VAL A 1 311 ? 138.380 9.179  -8.810  1.00 27.86  ? 311  VAL A O     1 
ATOM   2097 C  CB    . VAL A 1 311 ? 137.908 8.613  -5.406  1.00 28.05  ? 311  VAL A CB    1 
ATOM   2098 C  CG1   . VAL A 1 311 ? 136.450 8.906  -5.799  1.00 27.47  ? 311  VAL A CG1   1 
ATOM   2099 C  CG2   . VAL A 1 311 ? 137.958 7.421  -4.441  1.00 28.47  ? 311  VAL A CG2   1 
ATOM   2100 N  N     . ASP A 1 312 ? 139.130 10.571 -7.237  1.00 18.44  ? 312  ASP A N     1 
ATOM   2101 C  CA    . ASP A 1 312 ? 139.232 11.754 -8.100  1.00 17.15  ? 312  ASP A CA    1 
ATOM   2102 C  C     . ASP A 1 312 ? 140.253 12.707 -7.481  1.00 20.06  ? 312  ASP A C     1 
ATOM   2103 O  O     . ASP A 1 312 ? 140.490 12.771 -6.356  1.00 19.92  ? 312  ASP A O     1 
ATOM   2104 C  CB    . ASP A 1 312 ? 137.909 12.382 -8.536  1.00 15.98  ? 312  ASP A CB    1 
ATOM   2105 C  CG    . ASP A 1 312 ? 137.267 13.204 -7.471  1.00 21.94  ? 312  ASP A CG    1 
ATOM   2106 O  OD1   . ASP A 1 312 ? 136.159 12.928 -6.981  1.00 21.60  ? 312  ASP A OD1   1 
ATOM   2107 O  OD2   . ASP A 1 312 ? 137.858 14.175 -7.065  1.00 18.74  ? 312  ASP A OD2   1 
ATOM   2108 N  N     . THR A 1 313 ? 140.956 13.512 -8.256  1.00 18.23  ? 313  THR A N     1 
ATOM   2109 C  CA    . THR A 1 313 ? 141.951 14.425 -7.675  1.00 18.33  ? 313  THR A CA    1 
ATOM   2110 C  C     . THR A 1 313 ? 141.375 15.831 -7.464  1.00 24.29  ? 313  THR A C     1 
ATOM   2111 O  O     . THR A 1 313 ? 142.117 16.788 -7.215  1.00 21.67  ? 313  THR A O     1 
ATOM   2112 C  CB    . THR A 1 313 ? 143.201 14.547 -8.548  1.00 26.91  ? 313  THR A CB    1 
ATOM   2113 O  OG1   . THR A 1 313 ? 142.792 14.963 -9.861  1.00 25.70  ? 313  THR A OG1   1 
ATOM   2114 C  CG2   . THR A 1 313 ? 143.791 13.165 -8.682  1.00 23.98  ? 313  THR A CG2   1 
ATOM   2115 N  N     . ASN A 1 314 ? 140.065 15.976 -7.527  1.00 18.05  ? 314  ASN A N     1 
ATOM   2116 C  CA    . ASN A 1 314 ? 139.520 17.304 -7.310  1.00 15.38  ? 314  ASN A CA    1 
ATOM   2117 C  C     . ASN A 1 314 ? 139.831 17.723 -5.886  1.00 15.66  ? 314  ASN A C     1 
ATOM   2118 O  O     . ASN A 1 314 ? 139.588 16.956 -4.969  1.00 19.23  ? 314  ASN A O     1 
ATOM   2119 C  CB    . ASN A 1 314 ? 137.916 17.296 -7.369  1.00 14.47  ? 314  ASN A CB    1 
ATOM   2120 C  CG    . ASN A 1 314 ? 137.303 18.697 -7.181  1.00 19.49  ? 314  ASN A CG    1 
ATOM   2121 O  OD1   . ASN A 1 314 ? 136.426 18.966 -6.314  1.00 27.69  ? 314  ASN A OD1   1 
ATOM   2122 N  ND2   . ASN A 1 314 ? 137.749 19.588 -7.997  1.00 12.17  ? 314  ASN A ND2   1 
ATOM   2123 N  N     . GLY A 1 315 ? 140.364 18.929 -5.710  1.00 12.63  ? 315  GLY A N     1 
ATOM   2124 C  CA    . GLY A 1 315 ? 140.694 19.468 -4.395  1.00 15.99  ? 315  GLY A CA    1 
ATOM   2125 C  C     . GLY A 1 315 ? 142.042 19.035 -3.834  1.00 18.33  ? 315  GLY A C     1 
ATOM   2126 O  O     . GLY A 1 315 ? 142.379 19.440 -2.717  1.00 15.64  ? 315  GLY A O     1 
ATOM   2127 N  N     . ALA A 1 316 ? 142.810 18.237 -4.578  1.00 13.89  ? 316  ALA A N     1 
ATOM   2128 C  CA    . ALA A 1 316 ? 144.118 17.812 -4.060  1.00 14.84  ? 316  ALA A CA    1 
ATOM   2129 C  C     . ALA A 1 316 ? 144.983 19.020 -3.673  1.00 14.99  ? 316  ALA A C     1 
ATOM   2130 O  O     . ALA A 1 316 ? 145.544 19.084 -2.588  1.00 15.51  ? 316  ALA A O     1 
ATOM   2131 C  CB    . ALA A 1 316 ? 144.832 16.947 -5.065  1.00 14.54  ? 316  ALA A CB    1 
ATOM   2132 N  N     . GLY A 1 317 ? 145.096 20.006 -4.548  1.00 10.35  ? 317  GLY A N     1 
ATOM   2133 C  CA    . GLY A 1 317 ? 145.915 21.182 -4.214  1.00 10.94  ? 317  GLY A CA    1 
ATOM   2134 C  C     . GLY A 1 317 ? 145.339 21.997 -3.067  1.00 16.21  ? 317  GLY A C     1 
ATOM   2135 O  O     . GLY A 1 317 ? 146.070 22.566 -2.271  1.00 15.60  ? 317  GLY A O     1 
ATOM   2136 N  N     . ASP A 1 318 ? 144.016 22.085 -2.981  1.00 11.35  ? 318  ASP A N     1 
ATOM   2137 C  CA    . ASP A 1 318 ? 143.406 22.855 -1.911  1.00 9.15   ? 318  ASP A CA    1 
ATOM   2138 C  C     . ASP A 1 318 ? 143.697 22.185 -0.586  1.00 8.75   ? 318  ASP A C     1 
ATOM   2139 O  O     . ASP A 1 318 ? 143.962 22.874 0.392   1.00 13.43  ? 318  ASP A O     1 
ATOM   2140 C  CB    . ASP A 1 318 ? 141.886 22.866 -2.087  1.00 13.63  ? 318  ASP A CB    1 
ATOM   2141 C  CG    . ASP A 1 318 ? 141.452 23.542 -3.372  1.00 18.38  ? 318  ASP A CG    1 
ATOM   2142 O  OD1   . ASP A 1 318 ? 142.215 24.397 -3.904  1.00 14.72  ? 318  ASP A OD1   1 
ATOM   2143 O  OD2   . ASP A 1 318 ? 140.356 23.203 -3.886  1.00 14.49  ? 318  ASP A OD2   1 
ATOM   2144 N  N     . ALA A 1 319 ? 143.642 20.850 -0.559  1.00 10.36  ? 319  ALA A N     1 
ATOM   2145 C  CA    . ALA A 1 319 ? 143.919 20.086 0.679   1.00 13.22  ? 319  ALA A CA    1 
ATOM   2146 C  C     . ALA A 1 319 ? 145.395 20.253 1.065   1.00 15.77  ? 319  ALA A C     1 
ATOM   2147 O  O     . ALA A 1 319 ? 145.742 20.437 2.226   1.00 15.35  ? 319  ALA A O     1 
ATOM   2148 C  CB    . ALA A 1 319 ? 143.591 18.602 0.541   1.00 12.85  ? 319  ALA A CB    1 
ATOM   2149 N  N     . PHE A 1 320 ? 146.275 20.235 0.074   1.00 12.45  ? 320  PHE A N     1 
ATOM   2150 C  CA    . PHE A 1 320 ? 147.698 20.419 0.340   1.00 12.14  ? 320  PHE A CA    1 
ATOM   2151 C  C     . PHE A 1 320 ? 147.921 21.790 0.980   1.00 13.42  ? 320  PHE A C     1 
ATOM   2152 O  O     . PHE A 1 320 ? 148.589 21.922 2.001   1.00 13.82  ? 320  PHE A O     1 
ATOM   2153 C  CB    . PHE A 1 320 ? 148.456 20.326 -1.017  1.00 10.58  ? 320  PHE A CB    1 
ATOM   2154 C  CG    . PHE A 1 320 ? 149.920 20.655 -0.841  1.00 10.67  ? 320  PHE A CG    1 
ATOM   2155 C  CD1   . PHE A 1 320 ? 150.807 19.629 -0.617  1.00 13.60  ? 320  PHE A CD1   1 
ATOM   2156 C  CD2   . PHE A 1 320 ? 150.345 21.958 -0.839  1.00 14.97  ? 320  PHE A CD2   1 
ATOM   2157 C  CE1   . PHE A 1 320 ? 152.175 19.902 -0.423  1.00 15.66  ? 320  PHE A CE1   1 
ATOM   2158 C  CE2   . PHE A 1 320 ? 151.710 22.275 -0.666  1.00 20.46  ? 320  PHE A CE2   1 
ATOM   2159 C  CZ    . PHE A 1 320 ? 152.617 21.225 -0.457  1.00 19.44  ? 320  PHE A CZ    1 
ATOM   2160 N  N     . VAL A 1 321 ? 147.359 22.845 0.396   1.00 10.76  ? 321  VAL A N     1 
ATOM   2161 C  CA    . VAL A 1 321 ? 147.526 24.185 0.963   1.00 12.72  ? 321  VAL A CA    1 
ATOM   2162 C  C     . VAL A 1 321 ? 146.945 24.278 2.363   1.00 15.24  ? 321  VAL A C     1 
ATOM   2163 O  O     . VAL A 1 321 ? 147.504 24.939 3.233   1.00 16.67  ? 321  VAL A O     1 
ATOM   2164 C  CB    . VAL A 1 321 ? 146.891 25.288 0.071   1.00 16.01  ? 321  VAL A CB    1 
ATOM   2165 C  CG1   . VAL A 1 321 ? 146.757 26.559 0.836   1.00 15.52  ? 321  VAL A CG1   1 
ATOM   2166 C  CG2   . VAL A 1 321 ? 147.705 25.454 -1.221  1.00 14.12  ? 321  VAL A CG2   1 
ATOM   2167 N  N     . GLY A 1 322 ? 145.832 23.607 2.599   1.00 11.78  ? 322  GLY A N     1 
ATOM   2168 C  CA    . GLY A 1 322 ? 145.223 23.649 3.933   1.00 12.20  ? 322  GLY A CA    1 
ATOM   2169 C  C     . GLY A 1 322 ? 146.122 22.973 4.983   1.00 17.94  ? 322  GLY A C     1 
ATOM   2170 O  O     . GLY A 1 322 ? 146.299 23.487 6.090   1.00 18.45  ? 322  GLY A O     1 
ATOM   2171 N  N     . GLY A 1 323 ? 146.698 21.827 4.647   1.00 15.31  ? 323  GLY A N     1 
ATOM   2172 C  CA    . GLY A 1 323 ? 147.561 21.132 5.609   1.00 13.83  ? 323  GLY A CA    1 
ATOM   2173 C  C     . GLY A 1 323 ? 148.809 21.961 5.837   1.00 16.86  ? 323  GLY A C     1 
ATOM   2174 O  O     . GLY A 1 323 ? 149.286 22.074 6.956   1.00 20.44  ? 323  GLY A O     1 
ATOM   2175 N  N     . PHE A 1 324 ? 149.333 22.544 4.758   1.00 16.82  ? 324  PHE A N     1 
ATOM   2176 C  CA    . PHE A 1 324 ? 150.527 23.380 4.825   1.00 16.25  ? 324  PHE A CA    1 
ATOM   2177 C  C     . PHE A 1 324 ? 150.300 24.582 5.751   1.00 21.28  ? 324  PHE A C     1 
ATOM   2178 O  O     . PHE A 1 324 ? 151.110 24.834 6.631   1.00 19.20  ? 324  PHE A O     1 
ATOM   2179 C  CB    . PHE A 1 324 ? 150.947 23.834 3.430   1.00 14.68  ? 324  PHE A CB    1 
ATOM   2180 C  CG    . PHE A 1 324 ? 152.292 24.537 3.370   1.00 17.41  ? 324  PHE A CG    1 
ATOM   2181 C  CD1   . PHE A 1 324 ? 153.368 23.922 2.737   1.00 19.75  ? 324  PHE A CD1   1 
ATOM   2182 C  CD2   . PHE A 1 324 ? 152.481 25.830 3.936   1.00 15.93  ? 324  PHE A CD2   1 
ATOM   2183 C  CE1   . PHE A 1 324 ? 154.614 24.601 2.655   1.00 20.73  ? 324  PHE A CE1   1 
ATOM   2184 C  CE2   . PHE A 1 324 ? 153.731 26.506 3.879   1.00 20.36  ? 324  PHE A CE2   1 
ATOM   2185 C  CZ    . PHE A 1 324 ? 154.796 25.884 3.230   1.00 17.73  ? 324  PHE A CZ    1 
ATOM   2186 N  N     . LEU A 1 325 ? 149.199 25.319 5.559   1.00 17.07  ? 325  LEU A N     1 
ATOM   2187 C  CA    . LEU A 1 325 ? 148.886 26.478 6.392   1.00 12.55  ? 325  LEU A CA    1 
ATOM   2188 C  C     . LEU A 1 325 ? 148.637 26.088 7.845   1.00 16.29  ? 325  LEU A C     1 
ATOM   2189 O  O     . LEU A 1 325 ? 149.019 26.818 8.745   1.00 18.41  ? 325  LEU A O     1 
ATOM   2190 C  CB    . LEU A 1 325 ? 147.722 27.278 5.891   1.00 12.27  ? 325  LEU A CB    1 
ATOM   2191 C  CG    . LEU A 1 325 ? 147.909 27.861 4.510   1.00 18.26  ? 325  LEU A CG    1 
ATOM   2192 C  CD1   . LEU A 1 325 ? 146.608 28.564 4.056   1.00 20.29  ? 325  LEU A CD1   1 
ATOM   2193 C  CD2   . LEU A 1 325 ? 149.065 28.844 4.548   1.00 22.94  ? 325  LEU A CD2   1 
ATOM   2194 N  N     . TYR A 1 326 ? 148.000 24.947 8.084   1.00 14.66  ? 326  TYR A N     1 
ATOM   2195 C  CA    . TYR A 1 326 ? 147.764 24.539 9.455   1.00 15.72  ? 326  TYR A CA    1 
ATOM   2196 C  C     . TYR A 1 326 ? 149.121 24.275 10.142  1.00 24.15  ? 326  TYR A C     1 
ATOM   2197 O  O     . TYR A 1 326 ? 149.378 24.700 11.276  1.00 21.79  ? 326  TYR A O     1 
ATOM   2198 C  CB    . TYR A 1 326 ? 147.071 23.224 9.390   1.00 15.74  ? 326  TYR A CB    1 
ATOM   2199 C  CG    . TYR A 1 326 ? 147.165 22.453 10.693  1.00 23.75  ? 326  TYR A CG    1 
ATOM   2200 C  CD1   . TYR A 1 326 ? 146.514 22.926 11.836  1.00 26.66  ? 326  TYR A CD1   1 
ATOM   2201 C  CD2   . TYR A 1 326 ? 147.897 21.276 10.801  1.00 27.46  ? 326  TYR A CD2   1 
ATOM   2202 C  CE1   . TYR A 1 326 ? 146.599 22.255 13.031  1.00 26.03  ? 326  TYR A CE1   1 
ATOM   2203 C  CE2   . TYR A 1 326 ? 147.978 20.604 12.019  1.00 26.85  ? 326  TYR A CE2   1 
ATOM   2204 C  CZ    . TYR A 1 326 ? 147.315 21.097 13.111  1.00 35.96  ? 326  TYR A CZ    1 
ATOM   2205 O  OH    . TYR A 1 326 ? 147.334 20.462 14.355  1.00 54.20  ? 326  TYR A OH    1 
ATOM   2206 N  N     . GLY A 1 327 ? 150.005 23.577 9.461   1.00 17.58  ? 327  GLY A N     1 
ATOM   2207 C  CA    . GLY A 1 327 ? 151.298 23.295 10.071  1.00 19.87  ? 327  GLY A CA    1 
ATOM   2208 C  C     . GLY A 1 327 ? 152.112 24.554 10.258  1.00 24.41  ? 327  GLY A C     1 
ATOM   2209 O  O     . GLY A 1 327 ? 152.852 24.671 11.238  1.00 23.29  ? 327  GLY A O     1 
ATOM   2210 N  N     . LEU A 1 328 ? 152.008 25.474 9.312   1.00 18.54  ? 328  LEU A N     1 
ATOM   2211 C  CA    . LEU A 1 328 ? 152.788 26.691 9.388   1.00 18.49  ? 328  LEU A CA    1 
ATOM   2212 C  C     . LEU A 1 328 ? 152.265 27.411 10.649  1.00 25.57  ? 328  LEU A C     1 
ATOM   2213 O  O     . LEU A 1 328 ? 153.031 28.021 11.382  1.00 23.65  ? 328  LEU A O     1 
ATOM   2214 C  CB    . LEU A 1 328 ? 152.483 27.574 8.184   1.00 19.26  ? 328  LEU A CB    1 
ATOM   2215 C  CG    . LEU A 1 328 ? 153.304 28.830 8.107   1.00 25.92  ? 328  LEU A CG    1 
ATOM   2216 C  CD1   . LEU A 1 328 ? 154.664 28.525 7.605   1.00 27.28  ? 328  LEU A CD1   1 
ATOM   2217 C  CD2   . LEU A 1 328 ? 152.662 29.742 7.127   1.00 28.01  ? 328  LEU A CD2   1 
ATOM   2218 N  N     . SER A 1 329 ? 150.957 27.323 10.891  1.00 22.80  ? 329  SER A N     1 
ATOM   2219 C  CA    . SER A 1 329 ? 150.314 27.944 12.045  1.00 23.99  ? 329  SER A CA    1 
ATOM   2220 C  C     . SER A 1 329 ? 150.897 27.421 13.356  1.00 27.55  ? 329  SER A C     1 
ATOM   2221 O  O     . SER A 1 329 ? 150.919 28.136 14.356  1.00 29.49  ? 329  SER A O     1 
ATOM   2222 C  CB    . SER A 1 329 ? 148.850 27.280 12.183  1.00 21.93  ? 329  SER A CB    1 
ATOM   2223 O  OG    . SER A 1 329 ? 147.951 28.283 12.144  1.00 43.57  ? 329  SER A OG    1 
ATOM   2224 N  N     . GLN A 1 330 ? 151.330 26.168 13.330  1.00 23.48  ? 330  GLN A N     1 
ATOM   2225 C  CA    . GLN A 1 330 ? 151.895 25.509 14.508  1.00 23.36  ? 330  GLN A CA    1 
ATOM   2226 C  C     . GLN A 1 330 ? 153.402 25.680 14.617  1.00 32.84  ? 330  GLN A C     1 
ATOM   2227 O  O     . GLN A 1 330 ? 154.027 25.098 15.493  1.00 38.99  ? 330  GLN A O     1 
ATOM   2228 C  CB    . GLN A 1 330 ? 151.620 24.029 14.408  1.00 23.72  ? 330  GLN A CB    1 
ATOM   2229 C  CG    . GLN A 1 330 ? 150.104 23.716 14.413  1.00 28.74  ? 330  GLN A CG    1 
ATOM   2230 C  CD    . GLN A 1 330 ? 149.433 24.208 15.667  1.00 46.89  ? 330  GLN A CD    1 
ATOM   2231 O  OE1   . GLN A 1 330 ? 149.298 23.464 16.632  1.00 57.89  ? 330  GLN A OE1   1 
ATOM   2232 N  NE2   . GLN A 1 330 ? 149.012 25.461 15.671  1.00 73.87  ? 330  GLN A NE2   1 
ATOM   2233 N  N     . GLY A 1 331 ? 153.976 26.466 13.729  1.00 28.06  ? 331  GLY A N     1 
ATOM   2234 C  CA    . GLY A 1 331 ? 155.414 26.721 13.728  1.00 30.27  ? 331  GLY A CA    1 
ATOM   2235 C  C     . GLY A 1 331 ? 156.275 25.569 13.214  1.00 33.47  ? 331  GLY A C     1 
ATOM   2236 O  O     . GLY A 1 331 ? 157.459 25.498 13.528  1.00 33.40  ? 331  GLY A O     1 
ATOM   2237 N  N     . LYS A 1 332 ? 155.723 24.660 12.430  1.00 25.64  ? 332  LYS A N     1 
ATOM   2238 C  CA    . LYS A 1 332 ? 156.551 23.569 11.935  1.00 21.98  ? 332  LYS A CA    1 
ATOM   2239 C  C     . LYS A 1 332 ? 157.476 24.074 10.845  1.00 19.97  ? 332  LYS A C     1 
ATOM   2240 O  O     . LYS A 1 332 ? 157.287 25.171 10.342  1.00 23.90  ? 332  LYS A O     1 
ATOM   2241 C  CB    . LYS A 1 332 ? 155.682 22.508 11.379  1.00 22.23  ? 332  LYS A CB    1 
ATOM   2242 C  CG    . LYS A 1 332 ? 154.664 22.025 12.375  1.00 30.34  ? 332  LYS A CG    1 
ATOM   2243 C  CD    . LYS A 1 332 ? 155.304 21.612 13.637  1.00 50.34  ? 332  LYS A CD    1 
ATOM   2244 C  CE    . LYS A 1 332 ? 154.310 21.792 14.758  1.00 78.02  ? 332  LYS A CE    1 
ATOM   2245 N  NZ    . LYS A 1 332 ? 154.079 20.464 15.372  1.00 75.13  ? 332  LYS A NZ    1 
ATOM   2246 N  N     . THR A 1 333 ? 158.483 23.300 10.462  1.00 23.33  ? 333  THR A N     1 
ATOM   2247 C  CA    . THR A 1 333 ? 159.399 23.754 9.406   1.00 25.29  ? 333  THR A CA    1 
ATOM   2248 C  C     . THR A 1 333 ? 158.822 23.535 7.999   1.00 25.27  ? 333  THR A C     1 
ATOM   2249 O  O     . THR A 1 333 ? 157.865 22.789 7.818   1.00 25.35  ? 333  THR A O     1 
ATOM   2250 C  CB    . THR A 1 333 ? 160.688 22.929 9.402   1.00 21.87  ? 333  THR A CB    1 
ATOM   2251 O  OG1   . THR A 1 333 ? 160.313 21.623 9.081   1.00 26.17  ? 333  THR A OG1   1 
ATOM   2252 C  CG2   . THR A 1 333 ? 161.279 22.763 10.786  1.00 20.27  ? 333  THR A CG2   1 
ATOM   2253 N  N     . VAL A 1 334 ? 159.425 24.184 7.001   1.00 21.51  ? 334  VAL A N     1 
ATOM   2254 C  CA    . VAL A 1 334 ? 158.981 24.058 5.615   1.00 20.12  ? 334  VAL A CA    1 
ATOM   2255 C  C     . VAL A 1 334 ? 158.789 22.594 5.190   1.00 29.87  ? 334  VAL A C     1 
ATOM   2256 O  O     . VAL A 1 334 ? 157.752 22.225 4.643   1.00 25.69  ? 334  VAL A O     1 
ATOM   2257 C  CB    . VAL A 1 334 ? 159.904 24.865 4.684   1.00 22.75  ? 334  VAL A CB    1 
ATOM   2258 C  CG1   . VAL A 1 334 ? 159.597 24.599 3.244   1.00 24.36  ? 334  VAL A CG1   1 
ATOM   2259 C  CG2   . VAL A 1 334 ? 159.693 26.328 4.915   1.00 25.26  ? 334  VAL A CG2   1 
ATOM   2260 N  N     . LYS A 1 335 ? 159.786 21.741 5.438   1.00 22.18  ? 335  LYS A N     1 
ATOM   2261 C  CA    . LYS A 1 335 ? 159.650 20.344 5.056   1.00 18.80  ? 335  LYS A CA    1 
ATOM   2262 C  C     . LYS A 1 335 ? 158.467 19.719 5.787   1.00 21.11  ? 335  LYS A C     1 
ATOM   2263 O  O     . LYS A 1 335 ? 157.723 18.903 5.226   1.00 20.27  ? 335  LYS A O     1 
ATOM   2264 C  CB    . LYS A 1 335 ? 160.851 19.547 5.531   1.00 23.00  ? 335  LYS A CB    1 
ATOM   2265 C  CG    . LYS A 1 335 ? 160.861 18.069 5.174   1.00 27.02  ? 335  LYS A CG    1 
ATOM   2266 C  CD    . LYS A 1 335 ? 162.117 17.549 5.844   1.00 37.70  ? 335  LYS A CD    1 
ATOM   2267 C  CE    . LYS A 1 335 ? 162.316 16.539 4.817   1.00 46.92  ? 335  LYS A CE    1 
ATOM   2268 N  NZ    . LYS A 1 335 ? 161.122 15.678 4.506   1.00 65.02  ? 335  LYS A NZ    1 
ATOM   2269 N  N     . GLN A 1 336 ? 158.293 20.090 7.043   1.00 17.23  ? 336  GLN A N     1 
ATOM   2270 C  CA    . GLN A 1 336 ? 157.182 19.536 7.821   1.00 16.81  ? 336  GLN A CA    1 
ATOM   2271 C  C     . GLN A 1 336 ? 155.871 20.041 7.238   1.00 15.62  ? 336  GLN A C     1 
ATOM   2272 O  O     . GLN A 1 336 ? 154.882 19.317 7.178   1.00 17.06  ? 336  GLN A O     1 
ATOM   2273 C  CB    . GLN A 1 336 ? 157.263 19.971 9.285   1.00 21.46  ? 336  GLN A CB    1 
ATOM   2274 C  CG    . GLN A 1 336 ? 158.534 19.422 10.065  1.00 35.76  ? 336  GLN A CG    1 
ATOM   2275 C  CD    . GLN A 1 336 ? 158.667 20.006 11.490  1.00 33.89  ? 336  GLN A CD    1 
ATOM   2276 O  OE1   . GLN A 1 336 ? 158.771 19.250 12.462  1.00 63.20  ? 336  GLN A OE1   1 
ATOM   2277 N  NE2   . GLN A 1 336 ? 158.623 21.329 11.613  1.00 36.22  ? 336  GLN A NE2   1 
ATOM   2278 N  N     . CYS A 1 337 ? 155.874 21.286 6.815   1.00 14.88  ? 337  CYS A N     1 
ATOM   2279 C  CA    . CYS A 1 337 ? 154.684 21.845 6.215   1.00 18.26  ? 337  CYS A CA    1 
ATOM   2280 C  C     . CYS A 1 337 ? 154.256 21.042 5.033   1.00 21.86  ? 337  CYS A C     1 
ATOM   2281 O  O     . CYS A 1 337 ? 153.111 20.636 4.853   1.00 18.44  ? 337  CYS A O     1 
ATOM   2282 C  CB    . CYS A 1 337 ? 154.754 23.292 6.022   1.00 17.84  ? 337  CYS A CB    1 
ATOM   2283 S  SG    . CYS A 1 337 ? 154.852 24.293 7.522   1.00 20.50  ? 337  CYS A SG    1 
ATOM   2284 N  N     . ILE A 1 338 ? 155.229 20.815 4.192   1.00 15.59  ? 338  ILE A N     1 
ATOM   2285 C  CA    . ILE A 1 338 ? 154.992 20.057 2.976   1.00 13.44  ? 338  ILE A CA    1 
ATOM   2286 C  C     . ILE A 1 338 ? 154.468 18.652 3.263   1.00 23.00  ? 338  ILE A C     1 
ATOM   2287 O  O     . ILE A 1 338 ? 153.558 18.172 2.583   1.00 20.87  ? 338  ILE A O     1 
ATOM   2288 C  CB    . ILE A 1 338 ? 156.265 19.986 2.207   1.00 13.84  ? 338  ILE A CB    1 
ATOM   2289 C  CG1   . ILE A 1 338 ? 156.519 21.400 1.692   1.00 20.21  ? 338  ILE A CG1   1 
ATOM   2290 C  CG2   . ILE A 1 338 ? 156.093 19.033 1.092   1.00 15.71  ? 338  ILE A CG2   1 
ATOM   2291 C  CD1   . ILE A 1 338 ? 157.762 21.531 0.856   1.00 27.44  ? 338  ILE A CD1   1 
ATOM   2292 N  N     . MET A 1 339 ? 155.035 17.973 4.266   1.00 18.13  ? 339  MET A N     1 
ATOM   2293 C  CA    . MET A 1 339 ? 154.587 16.611 4.600   1.00 16.46  ? 339  MET A CA    1 
ATOM   2294 C  C     . MET A 1 339 ? 153.129 16.603 5.063   1.00 19.52  ? 339  MET A C     1 
ATOM   2295 O  O     . MET A 1 339 ? 152.370 15.683 4.758   1.00 20.22  ? 339  MET A O     1 
ATOM   2296 C  CB    . MET A 1 339 ? 155.553 15.975 5.619   1.00 17.82  ? 339  MET A CB    1 
ATOM   2297 C  CG    . MET A 1 339 ? 156.826 15.594 4.840   1.00 24.95  ? 339  MET A CG    1 
ATOM   2298 S  SD    . MET A 1 339 ? 158.036 15.053 6.035   1.00 35.52  ? 339  MET A SD    1 
ATOM   2299 C  CE    . MET A 1 339 ? 157.538 13.336 6.183   1.00 35.72  ? 339  MET A CE    1 
ATOM   2300 N  N     . CYS A 1 340 ? 152.742 17.633 5.804   1.00 14.88  ? 340  CYS A N     1 
ATOM   2301 C  CA    . CYS A 1 340 ? 151.374 17.718 6.281   1.00 17.25  ? 340  CYS A CA    1 
ATOM   2302 C  C     . CYS A 1 340 ? 150.440 17.984 5.085   1.00 21.87  ? 340  CYS A C     1 
ATOM   2303 O  O     . CYS A 1 340 ? 149.351 17.410 4.968   1.00 23.28  ? 340  CYS A O     1 
ATOM   2304 C  CB    . CYS A 1 340 ? 151.329 18.775 7.348   1.00 22.04  ? 340  CYS A CB    1 
ATOM   2305 S  SG    . CYS A 1 340 ? 149.631 18.989 8.045   1.00 29.21  ? 340  CYS A SG    1 
ATOM   2306 N  N     . GLY A 1 341 ? 150.869 18.849 4.183   1.00 15.35  ? 341  GLY A N     1 
ATOM   2307 C  CA    . GLY A 1 341 ? 150.048 19.135 3.019   1.00 13.56  ? 341  GLY A CA    1 
ATOM   2308 C  C     . GLY A 1 341 ? 149.866 17.847 2.222   1.00 20.46  ? 341  GLY A C     1 
ATOM   2309 O  O     . GLY A 1 341 ? 148.756 17.497 1.816   1.00 16.28  ? 341  GLY A O     1 
ATOM   2310 N  N     . ASN A 1 342 ? 150.969 17.124 1.992   1.00 15.77  ? 342  ASN A N     1 
ATOM   2311 C  CA    . ASN A 1 342 ? 150.898 15.880 1.233   1.00 16.13  ? 342  ASN A CA    1 
ATOM   2312 C  C     . ASN A 1 342 ? 149.943 14.880 1.883   1.00 17.80  ? 342  ASN A C     1 
ATOM   2313 O  O     . ASN A 1 342 ? 149.154 14.211 1.204   1.00 18.17  ? 342  ASN A O     1 
ATOM   2314 C  CB    . ASN A 1 342 ? 152.258 15.190 1.198   1.00 16.83  ? 342  ASN A CB    1 
ATOM   2315 C  CG    . ASN A 1 342 ? 153.154 15.788 0.184   1.00 27.64  ? 342  ASN A CG    1 
ATOM   2316 O  OD1   . ASN A 1 342 ? 154.343 15.519 0.243   1.00 32.86  ? 342  ASN A OD1   1 
ATOM   2317 N  ND2   . ASN A 1 342 ? 152.637 16.577 -0.763  1.00 13.79  ? 342  ASN A ND2   1 
ATOM   2318 N  N     . ALA A 1 343 ? 150.013 14.763 3.190   1.00 14.88  ? 343  ALA A N     1 
ATOM   2319 C  CA    . ALA A 1 343 ? 149.122 13.819 3.859   1.00 14.83  ? 343  ALA A CA    1 
ATOM   2320 C  C     . ALA A 1 343 ? 147.652 14.217 3.664   1.00 21.24  ? 343  ALA A C     1 
ATOM   2321 O  O     . ALA A 1 343 ? 146.810 13.360 3.366   1.00 19.17  ? 343  ALA A O     1 
ATOM   2322 C  CB    . ALA A 1 343 ? 149.457 13.672 5.297   1.00 19.85  ? 343  ALA A CB    1 
ATOM   2323 N  N     . CYS A 1 344 ? 147.343 15.507 3.822   1.00 16.25  ? 344  CYS A N     1 
ATOM   2324 C  CA    . CYS A 1 344 ? 145.954 15.942 3.640   1.00 17.86  ? 344  CYS A CA    1 
ATOM   2325 C  C     . CYS A 1 344 ? 145.494 15.683 2.210   1.00 20.58  ? 344  CYS A C     1 
ATOM   2326 O  O     . CYS A 1 344 ? 144.373 15.244 1.985   1.00 18.35  ? 344  CYS A O     1 
ATOM   2327 C  CB    . CYS A 1 344 ? 145.769 17.413 3.903   1.00 17.47  ? 344  CYS A CB    1 
ATOM   2328 S  SG    . CYS A 1 344 ? 146.045 17.781 5.616   1.00 21.94  ? 344  CYS A SG    1 
ATOM   2329 N  N     . ALA A 1 345 ? 146.363 15.956 1.234   1.00 14.68  ? 345  ALA A N     1 
ATOM   2330 C  CA    . ALA A 1 345 ? 146.014 15.750 -0.176  1.00 14.17  ? 345  ALA A CA    1 
ATOM   2331 C  C     . ALA A 1 345 ? 145.808 14.293 -0.515  1.00 17.22  ? 345  ALA A C     1 
ATOM   2332 O  O     . ALA A 1 345 ? 144.946 13.939 -1.308  1.00 23.53  ? 345  ALA A O     1 
ATOM   2333 C  CB    . ALA A 1 345 ? 147.076 16.304 -1.094  1.00 15.84  ? 345  ALA A CB    1 
ATOM   2334 N  N     . GLN A 1 346 ? 146.614 13.428 0.087   1.00 16.12  ? 346  GLN A N     1 
ATOM   2335 C  CA    . GLN A 1 346 ? 146.485 11.996 -0.176  1.00 21.50  ? 346  GLN A CA    1 
ATOM   2336 C  C     . GLN A 1 346 ? 145.149 11.460 0.336   1.00 22.32  ? 346  GLN A C     1 
ATOM   2337 O  O     . GLN A 1 346 ? 144.585 10.524 -0.210  1.00 20.82  ? 346  GLN A O     1 
ATOM   2338 C  CB    . GLN A 1 346 ? 147.661 11.252 0.403   1.00 21.77  ? 346  GLN A CB    1 
ATOM   2339 C  CG    . GLN A 1 346 ? 148.897 11.883 -0.319  1.00 71.57  ? 346  GLN A CG    1 
ATOM   2340 C  CD    . GLN A 1 346 ? 149.899 10.888 -0.855  1.00 71.99  ? 346  GLN A CD    1 
ATOM   2341 O  OE1   . GLN A 1 346 ? 150.094 9.839  -0.260  1.00 67.46  ? 346  GLN A OE1   1 
ATOM   2342 N  NE2   . GLN A 1 346 ? 150.546 11.215 -1.971  1.00 48.49  ? 346  GLN A NE2   1 
ATOM   2343 N  N     . ASP A 1 347 ? 144.641 12.059 1.388   1.00 17.09  ? 347  ASP A N     1 
ATOM   2344 C  CA    . ASP A 1 347 ? 143.375 11.603 1.904   1.00 17.10  ? 347  ASP A CA    1 
ATOM   2345 C  C     . ASP A 1 347 ? 142.280 12.038 0.947   1.00 23.04  ? 347  ASP A C     1 
ATOM   2346 O  O     . ASP A 1 347 ? 141.432 11.239 0.549   1.00 22.94  ? 347  ASP A O     1 
ATOM   2347 C  CB    . ASP A 1 347 ? 143.066 12.308 3.174   1.00 20.71  ? 347  ASP A CB    1 
ATOM   2348 C  CG    . ASP A 1 347 ? 142.075 11.555 4.014   1.00 51.51  ? 347  ASP A CG    1 
ATOM   2349 O  OD1   . ASP A 1 347 ? 142.308 10.380 4.363   1.00 57.94  ? 347  ASP A OD1   1 
ATOM   2350 O  OD2   . ASP A 1 347 ? 141.040 12.165 4.295   1.00 61.26  ? 347  ASP A OD2   1 
ATOM   2351 N  N     . VAL A 1 348 ? 142.310 13.314 0.575   1.00 15.34  ? 348  VAL A N     1 
ATOM   2352 C  CA    . VAL A 1 348 ? 141.301 13.876 -0.343  1.00 14.83  ? 348  VAL A CA    1 
ATOM   2353 C  C     . VAL A 1 348 ? 141.213 13.181 -1.701  1.00 23.21  ? 348  VAL A C     1 
ATOM   2354 O  O     . VAL A 1 348 ? 140.128 13.084 -2.276  1.00 22.43  ? 348  VAL A O     1 
ATOM   2355 C  CB    . VAL A 1 348 ? 141.550 15.376 -0.535  1.00 19.78  ? 348  VAL A CB    1 
ATOM   2356 C  CG1   . VAL A 1 348 ? 140.849 15.897 -1.758  1.00 23.17  ? 348  VAL A CG1   1 
ATOM   2357 C  CG2   . VAL A 1 348 ? 141.090 16.115 0.681   1.00 22.28  ? 348  VAL A CG2   1 
ATOM   2358 N  N     . ILE A 1 349 ? 142.339 12.708 -2.232  1.00 15.17  ? 349  ILE A N     1 
ATOM   2359 C  CA    . ILE A 1 349 ? 142.296 12.055 -3.530  1.00 14.83  ? 349  ILE A CA    1 
ATOM   2360 C  C     . ILE A 1 349 ? 141.691 10.661 -3.451  1.00 17.23  ? 349  ILE A C     1 
ATOM   2361 O  O     . ILE A 1 349 ? 141.467 10.020 -4.472  1.00 17.82  ? 349  ILE A O     1 
ATOM   2362 C  CB    . ILE A 1 349 ? 143.611 12.002 -4.332  1.00 20.16  ? 349  ILE A CB    1 
ATOM   2363 C  CG1   . ILE A 1 349 ? 144.588 11.048 -3.660  1.00 19.74  ? 349  ILE A CG1   1 
ATOM   2364 C  CG2   . ILE A 1 349 ? 144.292 13.389 -4.444  1.00 22.03  ? 349  ILE A CG2   1 
ATOM   2365 C  CD1   . ILE A 1 349 ? 145.815 10.945 -4.566  1.00 29.22  ? 349  ILE A CD1   1 
ATOM   2366 N  N     . GLN A 1 350 ? 141.435 10.198 -2.243  1.00 14.90  ? 350  GLN A N     1 
ATOM   2367 C  CA    . GLN A 1 350 ? 140.842 8.875  -2.081  1.00 20.28  ? 350  GLN A CA    1 
ATOM   2368 C  C     . GLN A 1 350 ? 139.343 9.006  -1.804  1.00 26.87  ? 350  GLN A C     1 
ATOM   2369 O  O     . GLN A 1 350 ? 138.687 8.070  -1.355  1.00 26.87  ? 350  GLN A O     1 
ATOM   2370 C  CB    . GLN A 1 350 ? 141.593 8.157  -1.002  1.00 22.24  ? 350  GLN A CB    1 
ATOM   2371 C  CG    . GLN A 1 350 ? 142.950 7.791  -1.607  1.00 26.06  ? 350  GLN A CG    1 
ATOM   2372 C  CD    . GLN A 1 350 ? 143.788 6.981  -0.635  1.00 50.00  ? 350  GLN A CD    1 
ATOM   2373 O  OE1   . GLN A 1 350 ? 143.383 5.900  -0.182  1.00 41.03  ? 350  GLN A OE1   1 
ATOM   2374 N  NE2   . GLN A 1 350 ? 144.939 7.523  -0.274  1.00 55.65  ? 350  GLN A NE2   1 
ATOM   2375 N  N     . HIS A 1 351 ? 138.809 10.195 -2.073  1.00 20.82  ? 351  HIS A N     1 
ATOM   2376 C  CA    . HIS A 1 351 ? 137.389 10.472 -1.851  1.00 23.72  ? 351  HIS A CA    1 
ATOM   2377 C  C     . HIS A 1 351 ? 136.778 11.214 -3.025  1.00 24.60  ? 351  HIS A C     1 
ATOM   2378 O  O     . HIS A 1 351 ? 137.474 11.671 -3.896  1.00 21.42  ? 351  HIS A O     1 
ATOM   2379 C  CB    . HIS A 1 351 ? 137.281 11.352 -0.625  1.00 29.98  ? 351  HIS A CB    1 
ATOM   2380 C  CG    . HIS A 1 351 ? 137.524 10.598 0.626   1.00 43.82  ? 351  HIS A CG    1 
ATOM   2381 N  ND1   . HIS A 1 351 ? 137.178 9.271  0.761   1.00 53.87  ? 351  HIS A ND1   1 
ATOM   2382 C  CD2   . HIS A 1 351 ? 138.099 10.960 1.785   1.00 50.71  ? 351  HIS A CD2   1 
ATOM   2383 C  CE1   . HIS A 1 351 ? 137.519 8.853  1.964   1.00 54.76  ? 351  HIS A CE1   1 
ATOM   2384 N  NE2   . HIS A 1 351 ? 138.083 9.861  2.603   1.00 53.59  ? 351  HIS A NE2   1 
ATOM   2385 N  N     . VAL A 1 352 ? 135.450 11.318 -3.025  1.00 21.44  ? 352  VAL A N     1 
ATOM   2386 C  CA    . VAL A 1 352 ? 134.731 12.016 -4.082  1.00 18.06  ? 352  VAL A CA    1 
ATOM   2387 C  C     . VAL A 1 352 ? 134.735 13.507 -3.822  1.00 20.26  ? 352  VAL A C     1 
ATOM   2388 O  O     . VAL A 1 352 ? 134.285 13.961 -2.774  1.00 21.15  ? 352  VAL A O     1 
ATOM   2389 C  CB    . VAL A 1 352 ? 133.271 11.567 -4.095  1.00 20.64  ? 352  VAL A CB    1 
ATOM   2390 C  CG1   . VAL A 1 352 ? 132.545 12.495 -5.037  1.00 24.95  ? 352  VAL A CG1   1 
ATOM   2391 C  CG2   . VAL A 1 352 ? 133.268 10.161 -4.638  1.00 21.13  ? 352  VAL A CG2   1 
ATOM   2392 N  N     . GLY A 1 353 ? 135.228 14.283 -4.789  1.00 18.48  ? 353  GLY A N     1 
ATOM   2393 C  CA    . GLY A 1 353 ? 135.256 15.725 -4.611  1.00 18.12  ? 353  GLY A CA    1 
ATOM   2394 C  C     . GLY A 1 353 ? 136.102 16.098 -3.390  1.00 24.95  ? 353  GLY A C     1 
ATOM   2395 O  O     . GLY A 1 353 ? 136.978 15.337 -2.980  1.00 23.98  ? 353  GLY A O     1 
ATOM   2396 N  N     . PHE A 1 354 ? 135.840 17.277 -2.810  1.00 22.93  ? 354  PHE A N     1 
ATOM   2397 C  CA    . PHE A 1 354 ? 136.597 17.725 -1.645  1.00 19.30  ? 354  PHE A CA    1 
ATOM   2398 C  C     . PHE A 1 354 ? 136.024 17.179 -0.348  1.00 25.66  ? 354  PHE A C     1 
ATOM   2399 O  O     . PHE A 1 354 ? 135.076 17.736 0.207   1.00 22.39  ? 354  PHE A O     1 
ATOM   2400 C  CB    . PHE A 1 354 ? 136.645 19.227 -1.486  1.00 18.80  ? 354  PHE A CB    1 
ATOM   2401 C  CG    . PHE A 1 354 ? 137.591 19.589 -0.415  1.00 21.57  ? 354  PHE A CG    1 
ATOM   2402 C  CD1   . PHE A 1 354 ? 137.132 19.848 0.860   1.00 27.89  ? 354  PHE A CD1   1 
ATOM   2403 C  CD2   . PHE A 1 354 ? 138.964 19.619 -0.667  1.00 23.99  ? 354  PHE A CD2   1 
ATOM   2404 C  CE1   . PHE A 1 354 ? 137.979 20.160 1.891   1.00 29.61  ? 354  PHE A CE1   1 
ATOM   2405 C  CE2   . PHE A 1 354 ? 139.804 19.945 0.376   1.00 23.69  ? 354  PHE A CE2   1 
ATOM   2406 C  CZ    . PHE A 1 354 ? 139.309 20.226 1.638   1.00 24.83  ? 354  PHE A CZ    1 
ATOM   2407 N  N     . SER A 1 355 ? 136.604 16.095 0.144   1.00 22.42  ? 355  SER A N     1 
ATOM   2408 C  CA    . SER A 1 355 ? 136.117 15.491 1.391   1.00 26.29  ? 355  SER A CA    1 
ATOM   2409 C  C     . SER A 1 355 ? 136.871 15.964 2.628   1.00 35.16  ? 355  SER A C     1 
ATOM   2410 O  O     . SER A 1 355 ? 137.906 16.619 2.549   1.00 37.04  ? 355  SER A O     1 
ATOM   2411 C  CB    . SER A 1 355 ? 136.449 14.020 1.483   1.00 32.84  ? 355  SER A CB    1 
ATOM   2412 O  OG    . SER A 1 355 ? 137.792 13.854 1.214   1.00 33.03  ? 355  SER A OG    1 
ATOM   2413 N  N     . LEU A 1 356 ? 136.336 15.615 3.780   1.00 37.54  ? 356  LEU A N     1 
ATOM   2414 C  CA    . LEU A 1 356 ? 136.956 15.983 5.049   1.00 48.04  ? 356  LEU A CA    1 
ATOM   2415 C  C     . LEU A 1 356 ? 137.120 14.715 5.897   1.00 73.50  ? 356  LEU A C     1 
ATOM   2416 O  O     . LEU A 1 356 ? 136.152 13.990 6.119   1.00 87.47  ? 356  LEU A O     1 
ATOM   2417 C  CB    . LEU A 1 356 ? 136.009 16.952 5.788   1.00 48.12  ? 356  LEU A CB    1 
ATOM   2418 C  CG    . LEU A 1 356 ? 136.232 18.457 5.838   1.00 52.78  ? 356  LEU A CG    1 
ATOM   2419 C  CD1   . LEU A 1 356 ? 135.686 19.076 7.135   1.00 54.77  ? 356  LEU A CD1   1 
ATOM   2420 C  CD2   . LEU A 1 356 ? 137.686 18.789 5.664   1.00 54.18  ? 356  LEU A CD2   1 
ATOM   2421 N  N     . SER A 1 357 ? 138.313 14.402 6.379   1.00 70.51  ? 357  SER A N     1 
ATOM   2422 C  CA    . SER A 1 357 ? 138.430 13.171 7.182   1.00 71.45  ? 357  SER A CA    1 
ATOM   2423 C  C     . SER A 1 357 ? 139.705 13.146 8.006   1.00 76.07  ? 357  SER A C     1 
ATOM   2424 O  O     . SER A 1 357 ? 139.762 13.689 9.112   1.00 78.26  ? 357  SER A O     1 
ATOM   2425 C  CB    . SER A 1 357 ? 138.404 11.922 6.312   1.00 74.79  ? 357  SER A CB    1 
ATOM   2426 O  OG    . SER A 1 357 ? 138.944 10.847 7.061   1.00 92.45  ? 357  SER A OG    1 
ATOM   2427 N  N     . PHE A 1 358 ? 140.734 12.508 7.457   1.00 71.91  ? 358  PHE A N     1 
ATOM   2428 C  CA    . PHE A 1 358 ? 142.017 12.431 8.134   1.00 74.81  ? 358  PHE A CA    1 
ATOM   2429 C  C     . PHE A 1 358 ? 142.288 11.140 8.906   1.00 94.50  ? 358  PHE A C     1 
ATOM   2430 O  O     . PHE A 1 358 ? 143.193 10.382 8.545   1.00 99.63  ? 358  PHE A O     1 
ATOM   2431 C  CB    . PHE A 1 358 ? 142.481 13.826 8.508   1.00 74.47  ? 358  PHE A CB    1 
ATOM   2432 C  CG    . PHE A 1 358 ? 142.106 14.814 7.434   1.00 72.50  ? 358  PHE A CG    1 
ATOM   2433 C  CD1   . PHE A 1 358 ? 142.678 14.785 6.174   1.00 72.74  ? 358  PHE A CD1   1 
ATOM   2434 C  CD2   . PHE A 1 358 ? 141.123 15.743 7.671   1.00 72.52  ? 358  PHE A CD2   1 
ATOM   2435 C  CE1   . PHE A 1 358 ? 142.280 15.704 5.195   1.00 71.27  ? 358  PHE A CE1   1 
ATOM   2436 C  CE2   . PHE A 1 358 ? 140.718 16.650 6.698   1.00 73.17  ? 358  PHE A CE2   1 
ATOM   2437 C  CZ    . PHE A 1 358 ? 141.297 16.631 5.458   1.00 68.49  ? 358  PHE A CZ    1 
HETATM 2438 MG MG    . MG  B 2 .   ? 145.744 17.305 -10.587 1.00 17.48  ? 999  MG  A MG    1 
HETATM 2439 CL CL    . CL  C 3 .   ? 138.483 30.675 -4.020  1.00 8.50   ? 899  CL  A CL    1 
HETATM 2440 O  "O5'" . ADN D 4 .   ? 140.362 22.818 -6.535  1.00 15.29  ? 699  ADN A "O5'" 1 
HETATM 2441 C  "C5'" . ADN D 4 .   ? 139.111 22.238 -6.887  1.00 13.10  ? 699  ADN A "C5'" 1 
HETATM 2442 C  "C4'" . ADN D 4 .   ? 138.047 23.221 -6.449  1.00 10.39  ? 699  ADN A "C4'" 1 
HETATM 2443 O  "O4'" . ADN D 4 .   ? 138.179 24.420 -7.224  1.00 10.36  ? 699  ADN A "O4'" 1 
HETATM 2444 C  "C3'" . ADN D 4 .   ? 136.586 22.778 -6.606  1.00 10.04  ? 699  ADN A "C3'" 1 
HETATM 2445 O  "O3'" . ADN D 4 .   ? 136.062 22.462 -5.329  1.00 11.13  ? 699  ADN A "O3'" 1 
HETATM 2446 C  "C2'" . ADN D 4 .   ? 135.874 23.985 -7.230  1.00 9.63   ? 699  ADN A "C2'" 1 
HETATM 2447 O  "O2'" . ADN D 4 .   ? 134.744 24.399 -6.493  1.00 11.47  ? 699  ADN A "O2'" 1 
HETATM 2448 C  "C1'" . ADN D 4 .   ? 136.928 25.075 -7.118  1.00 10.49  ? 699  ADN A "C1'" 1 
HETATM 2449 N  N9    . ADN D 4 .   ? 136.837 26.090 -8.135  1.00 9.43   ? 699  ADN A N9    1 
HETATM 2450 C  C8    . ADN D 4 .   ? 136.707 25.919 -9.487  1.00 10.17  ? 699  ADN A C8    1 
HETATM 2451 N  N7    . ADN D 4 .   ? 136.642 27.060 -10.150 1.00 10.21  ? 699  ADN A N7    1 
HETATM 2452 C  C5    . ADN D 4 .   ? 136.763 28.029 -9.160  1.00 9.84   ? 699  ADN A C5    1 
HETATM 2453 C  C6    . ADN D 4 .   ? 136.778 29.427 -9.214  1.00 10.29  ? 699  ADN A C6    1 
HETATM 2454 N  N6    . ADN D 4 .   ? 136.673 30.138 -10.354 1.00 10.97  ? 699  ADN A N6    1 
HETATM 2455 N  N1    . ADN D 4 .   ? 136.905 30.078 -8.049  1.00 10.70  ? 699  ADN A N1    1 
HETATM 2456 C  C2    . ADN D 4 .   ? 137.015 29.367 -6.929  1.00 10.30  ? 699  ADN A C2    1 
HETATM 2457 N  N3    . ADN D 4 .   ? 137.017 28.068 -6.743  1.00 10.16  ? 699  ADN A N3    1 
HETATM 2458 C  C4    . ADN D 4 .   ? 136.880 27.443 -7.914  1.00 10.17  ? 699  ADN A C4    1 
HETATM 2459 P  PG    . ACP E 5 .   ? 142.304 20.687 -7.515  1.00 36.20  ? 799  ACP A PG    1 
HETATM 2460 O  O1G   . ACP E 5 .   ? 142.405 21.604 -6.277  1.00 37.69  ? 799  ACP A O1G   1 
HETATM 2461 O  O2G   . ACP E 5 .   ? 142.489 21.840 -8.515  1.00 38.10  ? 799  ACP A O2G   1 
HETATM 2462 O  O3G   . ACP E 5 .   ? 141.260 19.801 -8.048  1.00 37.03  ? 799  ACP A O3G   1 
HETATM 2463 P  PB    . ACP E 5 .   ? 145.398 19.650 -8.258  1.00 27.05  ? 799  ACP A PB    1 
HETATM 2464 O  O1B   . ACP E 5 .   ? 144.700 18.475 -8.916  1.00 29.31  ? 799  ACP A O1B   1 
HETATM 2465 O  O2B   . ACP E 5 .   ? 146.158 20.609 -9.088  1.00 28.28  ? 799  ACP A O2B   1 
HETATM 2466 C  C3B   . ACP E 5 .   ? 143.851 19.750 -7.361  1.00 32.48  ? 799  ACP A C3B   1 
HETATM 2467 P  PA    . ACP E 5 .   ? 148.325 19.009 -7.600  1.00 21.14  ? 799  ACP A PA    1 
HETATM 2468 O  O1A   . ACP E 5 .   ? 148.940 18.478 -8.825  1.00 22.48  ? 799  ACP A O1A   1 
HETATM 2469 O  O2A   . ACP E 5 .   ? 148.595 20.439 -7.271  1.00 21.82  ? 799  ACP A O2A   1 
HETATM 2470 O  O3A   . ACP E 5 .   ? 146.646 18.928 -7.394  1.00 25.32  ? 799  ACP A O3A   1 
HETATM 2471 O  "O5'" . ACP E 5 .   ? 148.730 18.030 -6.523  1.00 21.02  ? 799  ACP A "O5'" 1 
HETATM 2472 C  "C5'" . ACP E 5 .   ? 148.794 18.504 -5.194  1.00 18.72  ? 799  ACP A "C5'" 1 
HETATM 2473 C  "C4'" . ACP E 5 .   ? 149.182 17.436 -4.174  1.00 17.29  ? 799  ACP A "C4'" 1 
HETATM 2474 O  "O4'" . ACP E 5 .   ? 148.281 16.291 -4.286  1.00 17.71  ? 799  ACP A "O4'" 1 
HETATM 2475 C  "C3'" . ACP E 5 .   ? 150.554 16.853 -4.424  1.00 17.27  ? 799  ACP A "C3'" 1 
HETATM 2476 O  "O3'" . ACP E 5 .   ? 151.547 17.660 -3.784  1.00 18.50  ? 799  ACP A "O3'" 1 
HETATM 2477 C  "C2'" . ACP E 5 .   ? 150.405 15.486 -3.780  1.00 17.09  ? 799  ACP A "C2'" 1 
HETATM 2478 O  "O2'" . ACP E 5 .   ? 150.559 15.643 -2.408  1.00 18.44  ? 799  ACP A "O2'" 1 
HETATM 2479 C  "C1'" . ACP E 5 .   ? 148.960 15.091 -4.068  1.00 17.84  ? 799  ACP A "C1'" 1 
HETATM 2480 N  N9    . ACP E 5 .   ? 148.781 14.339 -5.282  1.00 17.68  ? 799  ACP A N9    1 
HETATM 2481 C  C8    . ACP E 5 .   ? 148.253 14.730 -6.483  1.00 18.36  ? 799  ACP A C8    1 
HETATM 2482 N  N7    . ACP E 5 .   ? 148.240 13.754 -7.366  1.00 18.88  ? 799  ACP A N7    1 
HETATM 2483 C  C5    . ACP E 5 .   ? 148.811 12.666 -6.673  1.00 18.79  ? 799  ACP A C5    1 
HETATM 2484 C  C6    . ACP E 5 .   ? 149.064 11.333 -7.032  1.00 19.77  ? 799  ACP A C6    1 
HETATM 2485 N  N6    . ACP E 5 .   ? 148.815 10.857 -8.253  1.00 21.76  ? 799  ACP A N6    1 
HETATM 2486 N  N1    . ACP E 5 .   ? 149.603 10.510 -6.099  1.00 19.89  ? 799  ACP A N1    1 
HETATM 2487 C  C2    . ACP E 5 .   ? 149.860 10.985 -4.892  1.00 19.42  ? 799  ACP A C2    1 
HETATM 2488 N  N3    . ACP E 5 .   ? 149.669 12.209 -4.458  1.00 18.86  ? 799  ACP A N3    1 
HETATM 2489 C  C4    . ACP E 5 .   ? 149.126 13.006 -5.401  1.00 18.74  ? 799  ACP A C4    1 
HETATM 2490 O  O     . HOH F 6 .   ? 143.597 22.766 -13.521 1.00 38.03  ? 1000 HOH A O     1 
HETATM 2491 O  O     . HOH F 6 .   ? 137.424 23.595 -18.243 1.00 34.79  ? 1001 HOH A O     1 
HETATM 2492 O  O     . HOH F 6 .   ? 138.654 14.294 -4.325  1.00 2.54   ? 1002 HOH A O     1 
HETATM 2493 O  O     . HOH F 6 .   ? 142.930 27.798 -17.041 1.00 29.93  ? 1003 HOH A O     1 
HETATM 2494 O  O     . HOH F 6 .   ? 163.935 42.011 9.404   1.00 98.63  ? 1004 HOH A O     1 
HETATM 2495 O  O     . HOH F 6 .   ? 133.141 35.706 -3.327  1.00 13.98  ? 1005 HOH A O     1 
HETATM 2496 O  O     . HOH F 6 .   ? 145.663 45.682 -19.049 1.00 75.21  ? 1006 HOH A O     1 
HETATM 2497 O  O     . HOH F 6 .   ? 149.497 48.730 -11.223 1.00 76.68  ? 1007 HOH A O     1 
HETATM 2498 O  O     . HOH F 6 .   ? 156.456 40.985 10.221  1.00 38.82  ? 1008 HOH A O     1 
HETATM 2499 O  O     . HOH F 6 .   ? 151.567 29.303 -22.875 1.00 72.99  ? 1009 HOH A O     1 
HETATM 2500 O  O     . HOH F 6 .   ? 140.235 46.794 -20.106 1.00 76.92  ? 1010 HOH A O     1 
HETATM 2501 O  O     . HOH F 6 .   ? 150.453 13.143 -11.545 1.00 44.12  ? 1011 HOH A O     1 
HETATM 2502 O  O     . HOH F 6 .   ? 136.927 45.935 -2.396  1.00 45.31  ? 1012 HOH A O     1 
HETATM 2503 O  O     . HOH F 6 .   ? 160.393 4.542  3.839   1.00 100.00 ? 1013 HOH A O     1 
HETATM 2504 O  O     . HOH F 6 .   ? 132.111 10.434 -9.522  1.00 59.56  ? 1014 HOH A O     1 
HETATM 2505 O  O     . HOH F 6 .   ? 120.019 23.477 -14.047 1.00 80.85  ? 1015 HOH A O     1 
HETATM 2506 O  O     . HOH F 6 .   ? 163.753 49.488 -13.400 1.00 100.00 ? 1016 HOH A O     1 
HETATM 2507 O  O     . HOH F 6 .   ? 128.159 13.133 -24.671 1.00 61.44  ? 1017 HOH A O     1 
HETATM 2508 O  O     . HOH F 6 .   ? 141.545 52.050 -9.269  1.00 76.53  ? 1018 HOH A O     1 
HETATM 2509 O  O     . HOH F 6 .   ? 118.462 20.943 -12.600 1.00 68.32  ? 1019 HOH A O     1 
HETATM 2510 O  O     . HOH F 6 .   ? 116.165 13.896 -14.148 1.00 66.04  ? 1020 HOH A O     1 
HETATM 2511 O  O     . HOH F 6 .   ? 130.489 29.550 18.228  1.00 31.13  ? 1021 HOH A O     1 
HETATM 2512 O  O     . HOH F 6 .   ? 136.842 25.226 -22.257 1.00 17.31  ? 1022 HOH A O     1 
HETATM 2513 O  O     . HOH F 6 .   ? 134.009 19.456 -3.663  1.00 15.66  ? 1023 HOH A O     1 
HETATM 2514 O  O     . HOH F 6 .   ? 128.922 34.493 -13.616 1.00 26.65  ? 1024 HOH A O     1 
HETATM 2515 O  O     . HOH F 6 .   ? 144.576 24.746 -5.517  1.00 26.35  ? 1025 HOH A O     1 
HETATM 2516 O  O     . HOH F 6 .   ? 133.257 11.721 -1.341  1.00 45.14  ? 1026 HOH A O     1 
HETATM 2517 O  O     . HOH F 6 .   ? 142.996 27.042 -1.932  1.00 15.01  ? 1027 HOH A O     1 
HETATM 2518 O  O     . HOH F 6 .   ? 129.703 46.274 7.753   1.00 47.97  ? 1028 HOH A O     1 
HETATM 2519 O  O     . HOH F 6 .   ? 134.358 11.132 -8.479  1.00 41.71  ? 1029 HOH A O     1 
HETATM 2520 O  O     . HOH F 6 .   ? 140.750 39.873 -5.284  1.00 16.46  ? 1030 HOH A O     1 
HETATM 2521 O  O     . HOH F 6 .   ? 171.500 35.041 -23.398 1.00 99.16  ? 1031 HOH A O     1 
HETATM 2522 O  O     . HOH F 6 .   ? 129.498 8.018  -17.385 1.00 52.76  ? 1032 HOH A O     1 
HETATM 2523 O  O     . HOH F 6 .   ? 143.068 16.308 -13.142 1.00 33.14  ? 1033 HOH A O     1 
HETATM 2524 O  O     . HOH F 6 .   ? 123.068 12.419 -18.967 1.00 63.74  ? 1034 HOH A O     1 
HETATM 2525 O  O     . HOH F 6 .   ? 136.322 29.645 -2.029  1.00 10.26  ? 1035 HOH A O     1 
HETATM 2526 O  O     . HOH F 6 .   ? 123.631 34.955 -10.987 1.00 45.10  ? 1036 HOH A O     1 
HETATM 2527 O  O     . HOH F 6 .   ? 153.589 41.159 -17.826 1.00 62.16  ? 1037 HOH A O     1 
HETATM 2528 O  O     . HOH F 6 .   ? 137.557 33.044 -10.735 1.00 17.58  ? 1038 HOH A O     1 
HETATM 2529 O  O     . HOH F 6 .   ? 163.520 46.138 -15.939 1.00 73.14  ? 1039 HOH A O     1 
HETATM 2530 O  O     . HOH F 6 .   ? 161.993 39.885 -0.736  1.00 61.20  ? 1040 HOH A O     1 
HETATM 2531 O  O     . HOH F 6 .   ? 134.072 41.163 -11.563 1.00 68.55  ? 1041 HOH A O     1 
HETATM 2532 O  O     . HOH F 6 .   ? 137.127 38.888 -4.833  1.00 20.97  ? 1042 HOH A O     1 
HETATM 2533 O  O     . HOH F 6 .   ? 165.038 24.808 6.128   1.00 75.57  ? 1043 HOH A O     1 
HETATM 2534 O  O     . HOH F 6 .   ? 168.797 8.612  -6.915  1.00 71.68  ? 1044 HOH A O     1 
HETATM 2535 O  O     . HOH F 6 .   ? 151.464 8.046  -6.080  1.00 44.54  ? 1045 HOH A O     1 
HETATM 2536 O  O     . HOH F 6 .   ? 144.889 47.411 3.087   1.00 46.80  ? 1046 HOH A O     1 
HETATM 2537 O  O     . HOH F 6 .   ? 121.323 32.442 0.361   1.00 35.90  ? 1047 HOH A O     1 
HETATM 2538 O  O     . HOH F 6 .   ? 134.316 24.033 0.534   1.00 15.04  ? 1048 HOH A O     1 
HETATM 2539 O  O     . HOH F 6 .   ? 164.679 40.361 4.489   1.00 45.41  ? 1049 HOH A O     1 
HETATM 2540 O  O     . HOH F 6 .   ? 169.993 29.779 -19.187 1.00 74.12  ? 1050 HOH A O     1 
HETATM 2541 O  O     . HOH F 6 .   ? 143.344 28.172 -5.939  1.00 16.20  ? 1051 HOH A O     1 
HETATM 2542 O  O     . HOH F 6 .   ? 133.140 19.622 0.575   1.00 22.13  ? 1052 HOH A O     1 
HETATM 2543 O  O     . HOH F 6 .   ? 138.336 31.034 -18.245 1.00 36.75  ? 1053 HOH A O     1 
HETATM 2544 O  O     . HOH F 6 .   ? 136.181 22.596 8.854   1.00 19.66  ? 1054 HOH A O     1 
HETATM 2545 O  O     . HOH F 6 .   ? 146.686 25.706 -7.878  1.00 24.34  ? 1055 HOH A O     1 
HETATM 2546 O  O     . HOH F 6 .   ? 128.385 32.063 -4.455  1.00 13.66  ? 1056 HOH A O     1 
HETATM 2547 O  O     . HOH F 6 .   ? 129.146 11.687 -8.746  1.00 37.76  ? 1057 HOH A O     1 
HETATM 2548 O  O     . HOH F 6 .   ? 153.419 16.922 -6.008  1.00 18.55  ? 1058 HOH A O     1 
HETATM 2549 O  O     . HOH F 6 .   ? 146.581 48.909 4.607   1.00 54.86  ? 1059 HOH A O     1 
HETATM 2550 O  O     . HOH F 6 .   ? 147.300 7.517  14.451  1.00 85.47  ? 1060 HOH A O     1 
HETATM 2551 O  O     . HOH F 6 .   ? 130.783 22.962 4.532   1.00 37.18  ? 1061 HOH A O     1 
HETATM 2552 O  O     . HOH F 6 .   ? 168.934 35.594 -7.282  1.00 74.44  ? 1062 HOH A O     1 
HETATM 2553 O  O     . HOH F 6 .   ? 120.419 17.287 -24.231 1.00 90.75  ? 1063 HOH A O     1 
HETATM 2554 O  O     . HOH F 6 .   ? 157.936 37.267 7.570   1.00 73.83  ? 1064 HOH A O     1 
HETATM 2555 O  O     . HOH F 6 .   ? 172.280 33.081 -3.370  1.00 34.65  ? 1065 HOH A O     1 
HETATM 2556 O  O     . HOH F 6 .   ? 131.102 32.295 -26.341 1.00 39.80  ? 1066 HOH A O     1 
HETATM 2557 O  O     . HOH F 6 .   ? 138.385 43.992 -19.631 1.00 76.75  ? 1067 HOH A O     1 
HETATM 2558 O  O     . HOH F 6 .   ? 165.764 23.994 9.204   1.00 86.86  ? 1068 HOH A O     1 
HETATM 2559 O  O     . HOH F 6 .   ? 142.887 48.781 10.952  1.00 90.94  ? 1069 HOH A O     1 
HETATM 2560 O  O     . HOH F 6 .   ? 137.800 15.418 -16.699 1.00 24.43  ? 1070 HOH A O     1 
HETATM 2561 O  O     . HOH F 6 .   ? 118.070 12.318 -15.281 1.00 64.53  ? 1071 HOH A O     1 
HETATM 2562 O  O     . HOH F 6 .   ? 163.295 25.617 0.881   1.00 30.71  ? 1072 HOH A O     1 
HETATM 2563 O  O     . HOH F 6 .   ? 155.172 13.769 2.100   1.00 31.81  ? 1073 HOH A O     1 
HETATM 2564 O  O     . HOH F 6 .   ? 146.404 26.373 24.276  1.00 60.43  ? 1074 HOH A O     1 
HETATM 2565 O  O     . HOH F 6 .   ? 125.875 19.897 14.430  1.00 79.36  ? 1075 HOH A O     1 
HETATM 2566 O  O     . HOH F 6 .   ? 165.607 31.979 -18.717 1.00 71.83  ? 1076 HOH A O     1 
HETATM 2567 O  O     . HOH F 6 .   ? 173.125 35.950 -3.125  1.00 80.12  ? 1077 HOH A O     1 
HETATM 2568 O  O     . HOH F 6 .   ? 135.919 22.481 -30.242 1.00 37.95  ? 1078 HOH A O     1 
HETATM 2569 O  O     . HOH F 6 .   ? 132.724 8.364  -7.597  1.00 90.76  ? 1079 HOH A O     1 
HETATM 2570 O  O     . HOH F 6 .   ? 119.467 27.878 -6.599  1.00 55.52  ? 1080 HOH A O     1 
HETATM 2571 O  O     . HOH F 6 .   ? 153.941 47.630 -8.834  1.00 95.40  ? 1081 HOH A O     1 
HETATM 2572 O  O     . HOH F 6 .   ? 138.931 9.210  -25.154 1.00 56.52  ? 1082 HOH A O     1 
HETATM 2573 O  O     . HOH F 6 .   ? 118.704 34.962 -8.275  1.00 88.61  ? 1083 HOH A O     1 
HETATM 2574 O  O     . HOH F 6 .   ? 164.954 15.060 -16.811 1.00 75.41  ? 1084 HOH A O     1 
HETATM 2575 O  O     . HOH F 6 .   ? 148.545 46.903 8.391   1.00 35.73  ? 1085 HOH A O     1 
HETATM 2576 O  O     . HOH F 6 .   ? 142.746 4.654  13.218  1.00 77.04  ? 1086 HOH A O     1 
HETATM 2577 O  O     . HOH F 6 .   ? 157.360 35.330 13.035  1.00 70.36  ? 1087 HOH A O     1 
HETATM 2578 O  O     . HOH F 6 .   ? 138.543 23.593 -20.724 1.00 20.73  ? 1088 HOH A O     1 
HETATM 2579 O  O     . HOH F 6 .   ? 128.096 34.427 7.423   1.00 19.43  ? 1089 HOH A O     1 
HETATM 2580 O  O     . HOH F 6 .   ? 142.336 28.609 17.347  1.00 35.65  ? 1090 HOH A O     1 
HETATM 2581 O  O     . HOH F 6 .   ? 124.168 8.181  -16.232 1.00 38.47  ? 1091 HOH A O     1 
HETATM 2582 O  O     . HOH F 6 .   ? 137.370 28.169 -12.905 1.00 17.71  ? 1092 HOH A O     1 
HETATM 2583 O  O     . HOH F 6 .   ? 141.095 24.641 -8.630  1.00 22.06  ? 1093 HOH A O     1 
HETATM 2584 O  O     . HOH F 6 .   ? 151.932 13.911 9.916   1.00 65.82  ? 1094 HOH A O     1 
HETATM 2585 O  O     . HOH F 6 .   ? 148.124 50.417 3.802   1.00 60.53  ? 1095 HOH A O     1 
HETATM 2586 O  O     . HOH F 6 .   ? 159.063 21.413 14.493  1.00 50.48  ? 1096 HOH A O     1 
HETATM 2587 O  O     . HOH F 6 .   ? 165.789 20.753 5.830   1.00 67.56  ? 1097 HOH A O     1 
HETATM 2588 O  O     . HOH F 6 .   ? 128.755 21.064 14.770  1.00 30.98  ? 1098 HOH A O     1 
HETATM 2589 O  O     . HOH F 6 .   ? 161.376 13.282 0.759   1.00 32.61  ? 1099 HOH A O     1 
HETATM 2590 O  O     . HOH F 6 .   ? 130.241 31.893 -16.548 1.00 27.66  ? 1100 HOH A O     1 
HETATM 2591 O  O     . HOH F 6 .   ? 150.859 17.274 10.741  1.00 66.47  ? 1101 HOH A O     1 
HETATM 2592 O  O     . HOH F 6 .   ? 131.628 32.917 -14.311 1.00 25.28  ? 1102 HOH A O     1 
HETATM 2593 O  O     . HOH F 6 .   ? 131.790 39.860 3.859   1.00 42.66  ? 1103 HOH A O     1 
HETATM 2594 O  O     . HOH F 6 .   ? 119.527 10.235 -14.312 1.00 32.60  ? 1104 HOH A O     1 
HETATM 2595 O  O     . HOH F 6 .   ? 135.407 21.699 11.326  1.00 31.30  ? 1105 HOH A O     1 
HETATM 2596 O  O     . HOH F 6 .   ? 130.134 42.134 1.383   1.00 60.99  ? 1106 HOH A O     1 
HETATM 2597 O  O     . HOH F 6 .   ? 152.708 33.967 10.981  1.00 62.80  ? 1107 HOH A O     1 
HETATM 2598 O  O     . HOH F 6 .   ? 152.253 41.436 2.344   1.00 44.99  ? 1108 HOH A O     1 
HETATM 2599 O  O     . HOH F 6 .   ? 135.408 7.973  -21.892 1.00 44.84  ? 1109 HOH A O     1 
HETATM 2600 O  O     . HOH F 6 .   ? 157.461 12.104 -5.495  1.00 41.24  ? 1110 HOH A O     1 
HETATM 2601 O  O     . HOH F 6 .   ? 155.939 23.095 16.627  1.00 78.65  ? 1111 HOH A O     1 
HETATM 2602 O  O     . HOH F 6 .   ? 145.973 20.597 -11.934 1.00 43.53  ? 1112 HOH A O     1 
HETATM 2603 O  O     . HOH F 6 .   ? 138.322 50.505 4.639   1.00 63.93  ? 1113 HOH A O     1 
HETATM 2604 O  O     . HOH F 6 .   ? 138.920 41.362 -12.956 1.00 51.29  ? 1114 HOH A O     1 
HETATM 2605 O  O     . HOH F 6 .   ? 147.405 24.536 -4.677  1.00 41.78  ? 1115 HOH A O     1 
HETATM 2606 O  O     . HOH F 6 .   ? 151.051 20.846 -13.001 1.00 35.85  ? 1116 HOH A O     1 
HETATM 2607 O  O     . HOH F 6 .   ? 143.667 25.943 -7.645  1.00 26.22  ? 1117 HOH A O     1 
HETATM 2608 O  O     . HOH F 6 .   ? 147.311 16.563 -9.156  1.00 43.25  ? 1118 HOH A O     1 
HETATM 2609 O  O     . HOH F 6 .   ? 130.117 30.322 9.673   1.00 25.92  ? 1119 HOH A O     1 
HETATM 2610 O  O     . HOH F 6 .   ? 162.523 22.518 6.285   1.00 33.09  ? 1120 HOH A O     1 
HETATM 2611 O  O     . HOH F 6 .   ? 153.952 41.432 6.948   1.00 31.55  ? 1121 HOH A O     1 
HETATM 2612 O  O     . HOH F 6 .   ? 154.228 9.564  -5.751  1.00 41.62  ? 1122 HOH A O     1 
HETATM 2613 O  O     . HOH F 6 .   ? 162.419 33.425 3.724   1.00 34.68  ? 1123 HOH A O     1 
HETATM 2614 O  O     . HOH F 6 .   ? 140.574 12.923 -10.557 1.00 44.05  ? 1124 HOH A O     1 
HETATM 2615 O  O     . HOH F 6 .   ? 136.206 6.688  -20.141 1.00 73.69  ? 1125 HOH A O     1 
HETATM 2616 O  O     . HOH F 6 .   ? 143.782 24.365 18.329  1.00 40.61  ? 1126 HOH A O     1 
HETATM 2617 O  O     . HOH F 6 .   ? 129.348 37.061 -11.735 1.00 40.09  ? 1127 HOH A O     1 
HETATM 2618 O  O     . HOH F 6 .   ? 128.215 10.497 -11.700 1.00 46.05  ? 1128 HOH A O     1 
HETATM 2619 O  O     . HOH F 6 .   ? 126.527 18.926 0.653   1.00 41.14  ? 1129 HOH A O     1 
HETATM 2620 O  O     . HOH F 6 .   ? 125.599 30.535 -10.506 1.00 46.92  ? 1130 HOH A O     1 
HETATM 2621 O  O     . HOH F 6 .   ? 128.858 44.576 -4.916  1.00 50.31  ? 1131 HOH A O     1 
HETATM 2622 O  O     . HOH F 6 .   ? 148.962 19.518 -11.072 1.00 51.64  ? 1132 HOH A O     1 
HETATM 2623 O  O     . HOH F 6 .   ? 133.626 33.667 19.763  1.00 74.60  ? 1133 HOH A O     1 
HETATM 2624 O  O     . HOH F 6 .   ? 146.913 10.928 4.495   1.00 45.29  ? 1134 HOH A O     1 
HETATM 2625 O  O     . HOH F 6 .   ? 162.466 19.476 9.079   1.00 46.52  ? 1135 HOH A O     1 
HETATM 2626 O  O     . HOH F 6 .   ? 167.136 19.262 -8.785  1.00 58.69  ? 1136 HOH A O     1 
HETATM 2627 O  O     . HOH F 6 .   ? 140.605 17.675 14.688  1.00 43.52  ? 1137 HOH A O     1 
HETATM 2628 O  O     . HOH F 6 .   ? 143.668 24.772 -11.416 1.00 41.32  ? 1138 HOH A O     1 
HETATM 2629 O  O     . HOH F 6 .   ? 149.027 2.740  -2.483  1.00 51.88  ? 1139 HOH A O     1 
HETATM 2630 O  O     . HOH F 6 .   ? 153.538 40.587 4.402   1.00 39.60  ? 1140 HOH A O     1 
HETATM 2631 O  O     . HOH F 6 .   ? 135.025 37.149 -5.513  1.00 46.25  ? 1141 HOH A O     1 
HETATM 2632 O  O     . HOH F 6 .   ? 153.004 21.432 8.345   1.00 75.46  ? 1142 HOH A O     1 
HETATM 2633 O  O     . HOH F 6 .   ? 147.674 13.448 -10.097 1.00 54.01  ? 1143 HOH A O     1 
HETATM 2634 O  O     . HOH F 6 .   ? 139.231 14.613 3.456   1.00 53.49  ? 1144 HOH A O     1 
HETATM 2635 O  O     . HOH F 6 .   ? 135.001 27.973 -20.725 1.00 61.60  ? 1145 HOH A O     1 
HETATM 2636 O  O     . HOH F 6 .   ? 132.948 9.042  -25.174 1.00 59.16  ? 1146 HOH A O     1 
HETATM 2637 O  O     . HOH F 6 .   ? 137.008 19.985 -30.232 1.00 78.43  ? 1147 HOH A O     1 
HETATM 2638 O  O     . HOH F 6 .   ? 124.580 19.673 -1.529  1.00 59.39  ? 1148 HOH A O     1 
HETATM 2639 O  O     . HOH F 6 .   ? 150.388 36.423 -13.906 1.00 64.39  ? 1149 HOH A O     1 
HETATM 2640 O  O     . HOH F 6 .   ? 137.676 33.804 15.006  1.00 72.77  ? 1150 HOH A O     1 
HETATM 2641 O  O     . HOH F 6 .   ? 148.444 46.027 -2.243  1.00 61.71  ? 1151 HOH A O     1 
HETATM 2642 O  O     . HOH F 6 .   ? 131.872 30.218 14.444  1.00 78.75  ? 1152 HOH A O     1 
HETATM 2643 O  O     . HOH F 6 .   ? 133.954 33.394 -19.268 1.00 69.62  ? 1153 HOH A O     1 
HETATM 2644 O  O     . HOH F 6 .   ? 135.230 13.026 -0.926  1.00 100.00 ? 1154 HOH A O     1 
HETATM 2645 O  O     . HOH F 6 .   ? 129.880 47.461 5.497   1.00 74.90  ? 1155 HOH A O     1 
HETATM 2646 O  O     . HOH F 6 .   ? 163.747 37.086 2.287   1.00 64.97  ? 1156 HOH A O     1 
HETATM 2647 O  O     . HOH F 6 .   ? 136.862 35.746 -3.699  1.00 87.74  ? 1157 HOH A O     1 
HETATM 2648 O  O     . HOH F 6 .   ? 137.635 27.645 -22.363 1.00 63.60  ? 1158 HOH A O     1 
HETATM 2649 O  O     . HOH F 6 .   ? 149.153 7.888  -8.130  1.00 59.65  ? 1159 HOH A O     1 
HETATM 2650 O  O     . HOH F 6 .   ? 137.844 38.141 -15.325 1.00 77.90  ? 1160 HOH A O     1 
HETATM 2651 O  O     . HOH F 6 .   ? 161.695 26.081 7.805   1.00 83.25  ? 1161 HOH A O     1 
HETATM 2652 O  O     . HOH F 6 .   ? 144.475 18.513 14.919  1.00 75.39  ? 1162 HOH A O     1 
HETATM 2653 O  O     . HOH F 6 .   ? 136.460 7.699  -17.112 1.00 77.48  ? 1163 HOH A O     1 
HETATM 2654 O  O     . HOH F 6 .   ? 147.353 22.942 -7.136  1.00 76.98  ? 1164 HOH A O     1 
HETATM 2655 O  O     . HOH F 6 .   ? 132.797 37.369 -12.581 1.00 81.58  ? 1165 HOH A O     1 
HETATM 2656 O  O     . HOH F 6 .   ? 122.943 28.641 -11.156 1.00 67.55  ? 1166 HOH A O     1 
HETATM 2657 O  O     . HOH F 6 .   ? 144.226 22.998 -8.671  1.00 68.92  ? 1167 HOH A O     1 
HETATM 2658 O  O     . HOH F 6 .   ? 132.843 42.631 -10.070 1.00 94.72  ? 1168 HOH A O     1 
HETATM 2659 O  O     . HOH F 6 .   ? 126.276 6.871  -17.377 1.00 64.89  ? 1169 HOH A O     1 
# 
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   1   ?   ?   ?   A . n 
A 1 2   ALA 2   2   ?   ?   ?   A . n 
A 1 3   VAL 3   3   ?   ?   ?   A . n 
A 1 4   ASP 4   4   ?   ?   ?   A . n 
A 1 5   SER 5   5   ?   ?   ?   A . n 
A 1 6   SER 6   6   ?   ?   ?   A . n 
A 1 7   ASN 7   7   ?   ?   ?   A . n 
A 1 8   SER 8   8   ?   ?   ?   A . n 
A 1 9   ALA 9   9   ?   ?   ?   A . n 
A 1 10  THR 10  10  ?   ?   ?   A . n 
A 1 11  GLY 11  11  11  GLY GLY A . n 
A 1 12  PRO 12  12  12  PRO PRO A . n 
A 1 13  MET 13  13  13  MET MET A . n 
A 1 14  ARG 14  14  14  ARG ARG A . n 
A 1 15  VAL 15  15  15  VAL VAL A . n 
A 1 16  PHE 16  16  16  PHE PHE A . n 
A 1 17  ALA 17  17  17  ALA ALA A . n 
A 1 18  ILE 18  18  18  ILE ILE A . n 
A 1 19  GLY 19  19  19  GLY GLY A . n 
A 1 20  ASN 20  20  20  ASN ASN A . n 
A 1 21  PRO 21  21  21  PRO PRO A . n 
A 1 22  ILE 22  22  22  ILE ILE A . n 
A 1 23  LEU 23  23  23  LEU LEU A . n 
A 1 24  ASP 24  24  24  ASP ASP A . n 
A 1 25  LEU 25  25  25  LEU LEU A . n 
A 1 26  VAL 26  26  26  VAL VAL A . n 
A 1 27  ALA 27  27  27  ALA ALA A . n 
A 1 28  GLU 28  28  28  GLU GLU A . n 
A 1 29  VAL 29  29  29  VAL VAL A . n 
A 1 30  PRO 30  30  30  PRO PRO A . n 
A 1 31  SER 31  31  31  SER SER A . n 
A 1 32  SER 32  32  32  SER SER A . n 
A 1 33  PHE 33  33  33  PHE PHE A . n 
A 1 34  LEU 34  34  34  LEU LEU A . n 
A 1 35  ASP 35  35  35  ASP ASP A . n 
A 1 36  GLU 36  36  36  GLU GLU A . n 
A 1 37  PHE 37  37  37  PHE PHE A . n 
A 1 38  PHE 38  38  38  PHE PHE A . n 
A 1 39  LEU 39  39  39  LEU LEU A . n 
A 1 40  LYS 40  40  40  LYS LYS A . n 
A 1 41  ARG 41  41  41  ARG ARG A . n 
A 1 42  GLY 42  42  42  GLY GLY A . n 
A 1 43  ASP 43  43  43  ASP ASP A . n 
A 1 44  ALA 44  44  44  ALA ALA A . n 
A 1 45  THR 45  45  45  THR THR A . n 
A 1 46  LEU 46  46  46  LEU LEU A . n 
A 1 47  ALA 47  47  47  ALA ALA A . n 
A 1 48  THR 48  48  48  THR THR A . n 
A 1 49  PRO 49  49  49  PRO PRO A . n 
A 1 50  GLU 50  50  50  GLU GLU A . n 
A 1 51  GLN 51  51  51  GLN GLN A . n 
A 1 52  MET 52  52  52  MET MET A . n 
A 1 53  ARG 53  53  53  ARG ARG A . n 
A 1 54  ILE 54  54  54  ILE ILE A . n 
A 1 55  TYR 55  55  55  TYR TYR A . n 
A 1 56  SER 56  56  56  SER SER A . n 
A 1 57  THR 57  57  57  THR THR A . n 
A 1 58  LEU 58  58  58  LEU LEU A . n 
A 1 59  ASP 59  59  59  ASP ASP A . n 
A 1 60  GLN 60  60  60  GLN GLN A . n 
A 1 61  PHE 61  61  61  PHE PHE A . n 
A 1 62  ASN 62  62  62  ASN ASN A . n 
A 1 63  PRO 63  63  63  PRO PRO A . n 
A 1 64  THR 64  64  64  THR THR A . n 
A 1 65  SER 65  65  65  SER SER A . n 
A 1 66  LEU 66  66  66  LEU LEU A . n 
A 1 67  PRO 67  67  67  PRO PRO A . n 
A 1 68  GLY 68  68  68  GLY GLY A . n 
A 1 69  GLY 69  69  69  GLY GLY A . n 
A 1 70  SER 70  70  70  SER SER A . n 
A 1 71  ALA 71  71  71  ALA ALA A . n 
A 1 72  LEU 72  72  72  LEU LEU A . n 
A 1 73  ASN 73  73  73  ASN ASN A . n 
A 1 74  SER 74  74  74  SER SER A . n 
A 1 75  VAL 75  75  75  VAL VAL A . n 
A 1 76  ARG 76  76  76  ARG ARG A . n 
A 1 77  VAL 77  77  77  VAL VAL A . n 
A 1 78  VAL 78  78  78  VAL VAL A . n 
A 1 79  GLN 79  79  79  GLN GLN A . n 
A 1 80  LYS 80  80  80  LYS LYS A . n 
A 1 81  LEU 81  81  81  LEU LEU A . n 
A 1 82  LEU 82  82  82  LEU LEU A . n 
A 1 83  ARG 83  83  83  ARG ARG A . n 
A 1 84  LYS 84  84  84  LYS LYS A . n 
A 1 85  PRO 85  85  85  PRO PRO A . n 
A 1 86  GLY 86  86  86  GLY GLY A . n 
A 1 87  SER 87  87  87  SER SER A . n 
A 1 88  ALA 88  88  88  ALA ALA A . n 
A 1 89  GLY 89  89  89  GLY GLY A . n 
A 1 90  TYR 90  90  90  TYR TYR A . n 
A 1 91  MET 91  91  91  MET MET A . n 
A 1 92  GLY 92  92  92  GLY GLY A . n 
A 1 93  ALA 93  93  93  ALA ALA A . n 
A 1 94  ILE 94  94  94  ILE ILE A . n 
A 1 95  GLY 95  95  95  GLY GLY A . n 
A 1 96  ASP 96  96  96  ASP ASP A . n 
A 1 97  ASP 97  97  97  ASP ASP A . n 
A 1 98  PRO 98  98  98  PRO PRO A . n 
A 1 99  ARG 99  99  99  ARG ARG A . n 
A 1 100 GLY 100 100 100 GLY GLY A . n 
A 1 101 GLN 101 101 101 GLN GLN A . n 
A 1 102 VAL 102 102 102 VAL VAL A . n 
A 1 103 LEU 103 103 103 LEU LEU A . n 
A 1 104 LYS 104 104 104 LYS LYS A . n 
A 1 105 GLU 105 105 105 GLU GLU A . n 
A 1 106 LEU 106 106 106 LEU LEU A . n 
A 1 107 CYS 107 107 107 CYS CYS A . n 
A 1 108 ASP 108 108 108 ASP ASP A . n 
A 1 109 LYS 109 109 109 LYS LYS A . n 
A 1 110 GLU 110 110 110 GLU GLU A . n 
A 1 111 GLY 111 111 111 GLY GLY A . n 
A 1 112 LEU 112 112 112 LEU LEU A . n 
A 1 113 ALA 113 113 113 ALA ALA A . n 
A 1 114 THR 114 114 114 THR THR A . n 
A 1 115 ARG 115 115 115 ARG ARG A . n 
A 1 116 PHE 116 116 116 PHE PHE A . n 
A 1 117 MET 117 117 117 MET MET A . n 
A 1 118 VAL 118 118 118 VAL VAL A . n 
A 1 119 ALA 119 119 119 ALA ALA A . n 
A 1 120 PRO 120 120 120 PRO PRO A . n 
A 1 121 GLY 121 121 121 GLY GLY A . n 
A 1 122 GLN 122 122 122 GLN GLN A . n 
A 1 123 SER 123 123 123 SER SER A . n 
A 1 124 THR 124 124 124 THR THR A . n 
A 1 125 GLY 125 125 125 GLY GLY A . n 
A 1 126 THR 126 126 126 THR THR A . n 
A 1 127 CYS 127 127 127 CYS CYS A . n 
A 1 128 ALA 128 128 128 ALA ALA A . n 
A 1 129 VAL 129 129 129 VAL VAL A . n 
A 1 130 LEU 130 130 130 LEU LEU A . n 
A 1 131 ILE 131 131 131 ILE ILE A . n 
A 1 132 ASN 132 132 132 ASN ASN A . n 
A 1 133 GLU 133 133 133 GLU GLU A . n 
A 1 134 LYS 134 134 134 LYS LYS A . n 
A 1 135 GLU 135 135 135 GLU GLU A . n 
A 1 136 ARG 136 136 136 ARG ARG A . n 
A 1 137 THR 137 137 137 THR THR A . n 
A 1 138 LEU 138 138 138 LEU LEU A . n 
A 1 139 CYS 139 139 139 CYS CYS A . n 
A 1 140 THR 140 140 140 THR THR A . n 
A 1 141 HIS 141 141 141 HIS HIS A . n 
A 1 142 LEU 142 142 142 LEU LEU A . n 
A 1 143 GLY 143 143 143 GLY GLY A . n 
A 1 144 ALA 144 144 144 ALA ALA A . n 
A 1 145 CYS 145 145 145 CYS CYS A . n 
A 1 146 GLY 146 146 146 GLY GLY A . n 
A 1 147 SER 147 147 147 SER SER A . n 
A 1 148 PHE 148 148 148 PHE PHE A . n 
A 1 149 ARG 149 149 149 ARG ARG A . n 
A 1 150 ILE 150 150 150 ILE ILE A . n 
A 1 151 PRO 151 151 151 PRO PRO A . n 
A 1 152 GLU 152 152 152 GLU GLU A . n 
A 1 153 ASN 153 153 153 ASN ASN A . n 
A 1 154 TRP 154 154 154 TRP TRP A . n 
A 1 155 THR 155 155 155 THR THR A . n 
A 1 156 THR 156 156 156 THR THR A . n 
A 1 157 PHE 157 157 157 PHE PHE A . n 
A 1 158 ALA 158 158 158 ALA ALA A . n 
A 1 159 SER 159 159 159 SER SER A . n 
A 1 160 GLY 160 160 160 GLY GLY A . n 
A 1 161 ALA 161 161 161 ALA ALA A . n 
A 1 162 LEU 162 162 162 LEU LEU A . n 
A 1 163 ILE 163 163 163 ILE ILE A . n 
A 1 164 PHE 164 164 164 PHE PHE A . n 
A 1 165 TYR 165 165 165 TYR TYR A . n 
A 1 166 ALA 166 166 166 ALA ALA A . n 
A 1 167 THR 167 167 167 THR THR A . n 
A 1 168 ALA 168 168 168 ALA ALA A . n 
A 1 169 TYR 169 169 169 TYR TYR A . n 
A 1 170 THR 170 170 170 THR THR A . n 
A 1 171 LEU 171 171 171 LEU LEU A . n 
A 1 172 THR 172 172 172 THR THR A . n 
A 1 173 ALA 173 173 173 ALA ALA A . n 
A 1 174 THR 174 174 174 THR THR A . n 
A 1 175 PRO 175 175 175 PRO PRO A . n 
A 1 176 LYS 176 176 176 LYS LYS A . n 
A 1 177 ASN 177 177 177 ASN ASN A . n 
A 1 178 ALA 178 178 178 ALA ALA A . n 
A 1 179 LEU 179 179 179 LEU LEU A . n 
A 1 180 GLU 180 180 180 GLU GLU A . n 
A 1 181 VAL 181 181 181 VAL VAL A . n 
A 1 182 ALA 182 182 182 ALA ALA A . n 
A 1 183 GLY 183 183 183 GLY GLY A . n 
A 1 184 TYR 184 184 184 TYR TYR A . n 
A 1 185 ALA 185 185 185 ALA ALA A . n 
A 1 186 HIS 186 186 186 HIS HIS A . n 
A 1 187 GLY 187 187 187 GLY GLY A . n 
A 1 188 ILE 188 188 188 ILE ILE A . n 
A 1 189 PRO 189 189 189 PRO PRO A . n 
A 1 190 ASN 190 190 190 ASN ASN A . n 
A 1 191 ALA 191 191 191 ALA ALA A . n 
A 1 192 ILE 192 192 192 ILE ILE A . n 
A 1 193 PHE 193 193 193 PHE PHE A . n 
A 1 194 THR 194 194 194 THR THR A . n 
A 1 195 LEU 195 195 195 LEU LEU A . n 
A 1 196 ASN 196 196 196 ASN ASN A . n 
A 1 197 LEU 197 197 197 LEU LEU A . n 
A 1 198 SER 198 198 198 SER SER A . n 
A 1 199 ALA 199 199 199 ALA ALA A . n 
A 1 200 PRO 200 200 200 PRO PRO A . n 
A 1 201 PHE 201 201 201 PHE PHE A . n 
A 1 202 CYS 202 202 202 CYS CYS A . n 
A 1 203 VAL 203 203 203 VAL VAL A . n 
A 1 204 GLU 204 204 204 GLU GLU A . n 
A 1 205 LEU 205 205 205 LEU LEU A . n 
A 1 206 TYR 206 206 206 TYR TYR A . n 
A 1 207 LYS 207 207 207 LYS LYS A . n 
A 1 208 ASP 208 208 208 ASP ASP A . n 
A 1 209 ALA 209 209 209 ALA ALA A . n 
A 1 210 MET 210 210 210 MET MET A . n 
A 1 211 GLN 211 211 211 GLN GLN A . n 
A 1 212 SER 212 212 212 SER SER A . n 
A 1 213 LEU 213 213 213 LEU LEU A . n 
A 1 214 LEU 214 214 214 LEU LEU A . n 
A 1 215 LEU 215 215 215 LEU LEU A . n 
A 1 216 HIS 216 216 216 HIS HIS A . n 
A 1 217 THR 217 217 217 THR THR A . n 
A 1 218 ASN 218 218 218 ASN ASN A . n 
A 1 219 ILE 219 219 219 ILE ILE A . n 
A 1 220 LEU 220 220 220 LEU LEU A . n 
A 1 221 PHE 221 221 221 PHE PHE A . n 
A 1 222 GLY 222 222 222 GLY GLY A . n 
A 1 223 ASN 223 223 223 ASN ASN A . n 
A 1 224 GLU 224 224 224 GLU GLU A . n 
A 1 225 GLU 225 225 225 GLU GLU A . n 
A 1 226 GLU 226 226 226 GLU GLU A . n 
A 1 227 PHE 227 227 227 PHE PHE A . n 
A 1 228 ALA 228 228 228 ALA ALA A . n 
A 1 229 HIS 229 229 229 HIS HIS A . n 
A 1 230 LEU 230 230 230 LEU LEU A . n 
A 1 231 ALA 231 231 231 ALA ALA A . n 
A 1 232 LYS 232 232 232 LYS LYS A . n 
A 1 233 VAL 233 233 233 VAL VAL A . n 
A 1 234 HIS 234 234 234 HIS HIS A . n 
A 1 235 ASN 235 235 235 ASN ASN A . n 
A 1 236 LEU 236 236 236 LEU LEU A . n 
A 1 237 VAL 237 237 237 VAL VAL A . n 
A 1 238 ALA 238 238 238 ALA ALA A . n 
A 1 239 ALA 239 239 ?   ?   ?   A . n 
A 1 240 GLU 240 240 ?   ?   ?   A . n 
A 1 241 LYS 241 241 241 LYS ALA A . n 
A 1 242 VAL 242 242 242 VAL ALA A . n 
A 1 243 ALA 243 243 243 ALA ALA A . n 
A 1 244 LEU 244 244 244 LEU ALA A . n 
A 1 245 SER 245 245 245 SER ALA A . n 
A 1 246 VAL 246 246 246 VAL ALA A . n 
A 1 247 ALA 247 247 247 ALA ALA A . n 
A 1 248 ASN 248 248 248 ASN ALA A . n 
A 1 249 LYS 249 249 249 LYS ALA A . n 
A 1 250 GLU 250 250 250 GLU ALA A . n 
A 1 251 HIS 251 251 251 HIS ALA A . n 
A 1 252 ALA 252 252 252 ALA ALA A . n 
A 1 253 VAL 253 253 253 VAL ALA A . n 
A 1 254 GLU 254 254 254 GLU ALA A . n 
A 1 255 VAL 255 255 ?   ?   ?   A . n 
A 1 256 CYS 256 256 ?   ?   ?   A . n 
A 1 257 THR 257 257 ?   ?   ?   A . n 
A 1 258 GLY 258 258 ?   ?   ?   A . n 
A 1 259 ALA 259 259 ?   ?   ?   A . n 
A 1 260 LEU 260 260 ?   ?   ?   A . n 
A 1 261 ARG 261 261 ?   ?   ?   A . n 
A 1 262 LEU 262 262 ?   ?   ?   A . n 
A 1 263 LEU 263 263 ?   ?   ?   A . n 
A 1 264 THR 264 264 ?   ?   ?   A . n 
A 1 265 ALA 265 265 ?   ?   ?   A . n 
A 1 266 GLY 266 266 ?   ?   ?   A . n 
A 1 267 GLN 267 267 ?   ?   ?   A . n 
A 1 268 ASN 268 268 ?   ?   ?   A . n 
A 1 269 THR 269 269 ?   ?   ?   A . n 
A 1 270 GLY 270 270 270 GLY GLY A . n 
A 1 271 ALA 271 271 271 ALA ALA A . n 
A 1 272 THR 272 272 272 THR THR A . n 
A 1 273 LYS 273 273 273 LYS LYS A . n 
A 1 274 LEU 274 274 274 LEU LEU A . n 
A 1 275 VAL 275 275 275 VAL VAL A . n 
A 1 276 VAL 276 276 276 VAL VAL A . n 
A 1 277 MET 277 277 277 MET MET A . n 
A 1 278 THR 278 278 278 THR THR A . n 
A 1 279 ARG 279 279 279 ARG ARG A . n 
A 1 280 GLY 280 280 280 GLY GLY A . n 
A 1 281 HIS 281 281 281 HIS HIS A . n 
A 1 282 ASN 282 282 282 ASN ASN A . n 
A 1 283 PRO 283 283 283 PRO PRO A . n 
A 1 284 VAL 284 284 284 VAL VAL A . n 
A 1 285 ILE 285 285 285 ILE ILE A . n 
A 1 286 ALA 286 286 286 ALA ALA A . n 
A 1 287 ALA 287 287 287 ALA ALA A . n 
A 1 288 GLU 288 288 288 GLU GLU A . n 
A 1 289 GLN 289 289 289 GLN GLN A . n 
A 1 290 THR 290 290 290 THR THR A . n 
A 1 291 ALA 291 291 291 ALA ALA A . n 
A 1 292 ASP 292 292 292 ASP ASP A . n 
A 1 293 GLY 293 293 293 GLY GLY A . n 
A 1 294 THR 294 294 294 THR THR A . n 
A 1 295 VAL 295 295 295 VAL VAL A . n 
A 1 296 VAL 296 296 296 VAL VAL A . n 
A 1 297 VAL 297 297 297 VAL VAL A . n 
A 1 298 HIS 298 298 298 HIS HIS A . n 
A 1 299 GLU 299 299 299 GLU GLU A . n 
A 1 300 VAL 300 300 300 VAL VAL A . n 
A 1 301 GLY 301 301 301 GLY GLY A . n 
A 1 302 VAL 302 302 302 VAL VAL A . n 
A 1 303 PRO 303 303 303 PRO PRO A . n 
A 1 304 VAL 304 304 304 VAL VAL A . n 
A 1 305 VAL 305 305 305 VAL VAL A . n 
A 1 306 ALA 306 306 306 ALA ALA A . n 
A 1 307 ALA 307 307 307 ALA ALA A . n 
A 1 308 GLU 308 308 308 GLU GLU A . n 
A 1 309 LYS 309 309 309 LYS LYS A . n 
A 1 310 ILE 310 310 310 ILE ILE A . n 
A 1 311 VAL 311 311 311 VAL VAL A . n 
A 1 312 ASP 312 312 312 ASP ASP A . n 
A 1 313 THR 313 313 313 THR THR A . n 
A 1 314 ASN 314 314 314 ASN ASN A . n 
A 1 315 GLY 315 315 315 GLY GLY A . n 
A 1 316 ALA 316 316 316 ALA ALA A . n 
A 1 317 GLY 317 317 317 GLY GLY A . n 
A 1 318 ASP 318 318 318 ASP ASP A . n 
A 1 319 ALA 319 319 319 ALA ALA A . n 
A 1 320 PHE 320 320 320 PHE PHE A . n 
A 1 321 VAL 321 321 321 VAL VAL A . n 
A 1 322 GLY 322 322 322 GLY GLY A . n 
A 1 323 GLY 323 323 323 GLY GLY A . n 
A 1 324 PHE 324 324 324 PHE PHE A . n 
A 1 325 LEU 325 325 325 LEU LEU A . n 
A 1 326 TYR 326 326 326 TYR TYR A . n 
A 1 327 GLY 327 327 327 GLY GLY A . n 
A 1 328 LEU 328 328 328 LEU LEU A . n 
A 1 329 SER 329 329 329 SER SER A . n 
A 1 330 GLN 330 330 330 GLN GLN A . n 
A 1 331 GLY 331 331 331 GLY GLY A . n 
A 1 332 LYS 332 332 332 LYS LYS A . n 
A 1 333 THR 333 333 333 THR THR A . n 
A 1 334 VAL 334 334 334 VAL VAL A . n 
A 1 335 LYS 335 335 335 LYS LYS A . n 
A 1 336 GLN 336 336 336 GLN GLN A . n 
A 1 337 CYS 337 337 337 CYS CYS A . n 
A 1 338 ILE 338 338 338 ILE ILE A . n 
A 1 339 MET 339 339 339 MET MET A . n 
A 1 340 CYS 340 340 340 CYS CYS A . n 
A 1 341 GLY 341 341 341 GLY GLY A . n 
A 1 342 ASN 342 342 342 ASN ASN A . n 
A 1 343 ALA 343 343 343 ALA ALA A . n 
A 1 344 CYS 344 344 344 CYS CYS A . n 
A 1 345 ALA 345 345 345 ALA ALA A . n 
A 1 346 GLN 346 346 346 GLN GLN A . n 
A 1 347 ASP 347 347 347 ASP ASP A . n 
A 1 348 VAL 348 348 348 VAL VAL A . n 
A 1 349 ILE 349 349 349 ILE ILE A . n 
A 1 350 GLN 350 350 350 GLN GLN A . n 
A 1 351 HIS 351 351 351 HIS HIS A . n 
A 1 352 VAL 352 352 352 VAL VAL A . n 
A 1 353 GLY 353 353 353 GLY GLY A . n 
A 1 354 PHE 354 354 354 PHE PHE A . n 
A 1 355 SER 355 355 355 SER SER A . n 
A 1 356 LEU 356 356 356 LEU LEU A . n 
A 1 357 SER 357 357 357 SER SER A . n 
A 1 358 PHE 358 358 358 PHE PHE A . n 
A 1 359 THR 359 359 ?   ?   ?   A . n 
A 1 360 SER 360 360 ?   ?   ?   A . n 
A 1 361 LEU 361 361 ?   ?   ?   A . n 
A 1 362 PRO 362 362 ?   ?   ?   A . n 
A 1 363 CYS 363 363 ?   ?   ?   A . n 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F 
# 
_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 
# 
_pdbx_struct_conn_angle.id                    1 
_pdbx_struct_conn_angle.ptnr1_label_atom_id   O1B 
_pdbx_struct_conn_angle.ptnr1_label_alt_id    ? 
_pdbx_struct_conn_angle.ptnr1_label_asym_id   E 
_pdbx_struct_conn_angle.ptnr1_label_comp_id   ACP 
_pdbx_struct_conn_angle.ptnr1_label_seq_id    . 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id    ? 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id    A 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id    ACP 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id     799 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code    ? 
_pdbx_struct_conn_angle.ptnr1_symmetry        1_555 
_pdbx_struct_conn_angle.ptnr2_label_atom_id   MG 
_pdbx_struct_conn_angle.ptnr2_label_alt_id    ? 
_pdbx_struct_conn_angle.ptnr2_label_asym_id   B 
_pdbx_struct_conn_angle.ptnr2_label_comp_id   MG 
_pdbx_struct_conn_angle.ptnr2_label_seq_id    . 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id    ? 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id    A 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id    MG 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id     999 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code    ? 
_pdbx_struct_conn_angle.ptnr2_symmetry        1_555 
_pdbx_struct_conn_angle.ptnr3_label_atom_id   O 
_pdbx_struct_conn_angle.ptnr3_label_alt_id    ? 
_pdbx_struct_conn_angle.ptnr3_label_asym_id   F 
_pdbx_struct_conn_angle.ptnr3_label_comp_id   HOH 
_pdbx_struct_conn_angle.ptnr3_label_seq_id    . 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id    ? 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id    A 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id    HOH 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id     1118 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code    ? 
_pdbx_struct_conn_angle.ptnr3_symmetry        1_555 
_pdbx_struct_conn_angle.value                 91.3 
_pdbx_struct_conn_angle.value_esd             ? 
# 
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 2002-05-15 
2 'Structure model' 1 1 2008-04-28 
3 'Structure model' 1 2 2011-07-13 
# 
_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         ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Version format compliance' 
2 3 'Structure model' 'Version format compliance' 
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
EPMR      phasing          . ? 1 
TNT       refinement       . ? 2 
MOSFLM    'data reduction' . ? 3 
SCALEPACK 'data scaling'   . ? 4 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 CB  A GLN 60  ? ? O A HOH 1034 ? ? 1.68 
2 1 CG  A GLN 60  ? ? O A HOH 1034 ? ? 2.06 
3 1 O2G A ACP 799 ? ? O A HOH 1167 ? ? 2.09 
# 
loop_
_pdbx_validate_rmsd_bond.id 
_pdbx_validate_rmsd_bond.PDB_model_num 
_pdbx_validate_rmsd_bond.auth_atom_id_1 
_pdbx_validate_rmsd_bond.auth_asym_id_1 
_pdbx_validate_rmsd_bond.auth_comp_id_1 
_pdbx_validate_rmsd_bond.auth_seq_id_1 
_pdbx_validate_rmsd_bond.PDB_ins_code_1 
_pdbx_validate_rmsd_bond.label_alt_id_1 
_pdbx_validate_rmsd_bond.auth_atom_id_2 
_pdbx_validate_rmsd_bond.auth_asym_id_2 
_pdbx_validate_rmsd_bond.auth_comp_id_2 
_pdbx_validate_rmsd_bond.auth_seq_id_2 
_pdbx_validate_rmsd_bond.PDB_ins_code_2 
_pdbx_validate_rmsd_bond.label_alt_id_2 
_pdbx_validate_rmsd_bond.bond_value 
_pdbx_validate_rmsd_bond.bond_target_value 
_pdbx_validate_rmsd_bond.bond_deviation 
_pdbx_validate_rmsd_bond.bond_standard_deviation 
_pdbx_validate_rmsd_bond.linker_flag 
1 1 CA A ASP 96  ? ? CB  A ASP 96  ? ? 1.353 1.535 -0.182 0.022 N 
2 1 CB A ASP 96  ? ? CG  A ASP 96  ? ? 1.161 1.513 -0.352 0.021 N 
3 1 CG A ASP 96  ? ? OD1 A ASP 96  ? ? 1.609 1.249 0.360  0.023 N 
4 1 CG A GLU 180 ? ? CD  A GLU 180 ? ? 1.658 1.515 0.143  0.015 N 
5 1 CD A GLU 180 ? ? OE2 A GLU 180 ? ? 1.422 1.252 0.170  0.011 N 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1  1 C   A GLY 11  ? ? N  A PRO 12  ? ? CD  A PRO 12  ? ? 110.78 128.40 -17.62 2.10 Y 
2  1 CB  A PRO 12  ? ? CA A PRO 12  ? ? C   A PRO 12  ? ? 90.49  111.70 -21.21 2.10 N 
3  1 NE  A ARG 14  ? ? CZ A ARG 14  ? ? NH1 A ARG 14  ? ? 123.46 120.30 3.16   0.50 N 
4  1 NE  A ARG 41  ? ? CZ A ARG 41  ? ? NH1 A ARG 41  ? ? 124.54 120.30 4.24   0.50 N 
5  1 NH1 A ARG 76  ? ? CZ A ARG 76  ? ? NH2 A ARG 76  ? ? 111.49 119.40 -7.91  1.10 N 
6  1 NE  A ARG 76  ? ? CZ A ARG 76  ? ? NH1 A ARG 76  ? ? 128.48 120.30 8.18   0.50 N 
7  1 OD1 A ASP 96  ? ? CG A ASP 96  ? ? OD2 A ASP 96  ? ? 145.00 123.30 21.70  1.90 N 
8  1 CB  A ASP 96  ? ? CG A ASP 96  ? ? OD1 A ASP 96  ? ? 88.00  118.30 -30.30 0.90 N 
9  1 NE  A ARG 115 ? ? CZ A ARG 115 ? ? NH2 A ARG 115 ? ? 115.51 120.30 -4.79  0.50 N 
10 1 CG  A MET 117 ? ? SD A MET 117 ? ? CE  A MET 117 ? ? 87.32  100.20 -12.88 1.60 N 
11 1 NE  A ARG 149 ? ? CZ A ARG 149 ? ? NH1 A ARG 149 ? ? 123.99 120.30 3.69   0.50 N 
12 1 NE  A ARG 149 ? ? CZ A ARG 149 ? ? NH2 A ARG 149 ? ? 117.10 120.30 -3.20  0.50 N 
13 1 CB  A HIS 234 ? ? CA A HIS 234 ? ? C   A HIS 234 ? ? 122.58 110.40 12.18  2.00 N 
14 1 NE  A ARG 279 ? ? CZ A ARG 279 ? ? NH1 A ARG 279 ? ? 123.56 120.30 3.26   0.50 N 
15 1 CB  A ASP 292 ? ? CG A ASP 292 ? ? OD1 A ASP 292 ? ? 124.20 118.30 5.90   0.90 N 
16 1 CB  A SER 329 ? ? CA A SER 329 ? ? C   A SER 329 ? ? 97.59  110.10 -12.51 1.90 N 
17 1 CG  A LYS 335 ? ? CD A LYS 335 ? ? CE  A LYS 335 ? ? 92.26  111.90 -19.64 3.00 N 
18 1 CB  A SER 355 ? ? CA A SER 355 ? ? C   A SER 355 ? ? 98.28  110.10 -11.82 1.90 N 
19 1 CB  A PHE 358 ? ? CA A PHE 358 ? ? C   A PHE 358 ? ? 126.73 110.40 16.33  2.00 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 PRO A 12  ? ? -48.05  -76.10  
2  1 ARG A 83  ? ? 65.44   -49.25  
3  1 GLU A 133 ? ? 66.63   -120.33 
4  1 THR A 174 ? ? 177.84  139.47  
5  1 ASN A 190 ? ? 84.50   3.00    
6  1 SER A 198 ? ? 63.34   -56.54  
7  1 TYR A 206 ? ? -109.44 41.07   
8  1 HIS A 234 ? ? -100.58 -146.69 
9  1 ASN A 235 ? ? -93.92  -103.10 
10 1 LEU A 236 ? ? 20.77   -52.96  
11 1 VAL A 237 ? ? 52.35   -124.04 
12 1 VAL A 253 ? ? -67.00  -81.14  
13 1 ARG A 279 ? ? -156.69 70.32   
14 1 SER A 357 ? ? -162.72 -95.09  
# 
loop_
_pdbx_validate_planes.id 
_pdbx_validate_planes.PDB_model_num 
_pdbx_validate_planes.auth_comp_id 
_pdbx_validate_planes.auth_asym_id 
_pdbx_validate_planes.auth_seq_id 
_pdbx_validate_planes.PDB_ins_code 
_pdbx_validate_planes.label_alt_id 
_pdbx_validate_planes.rmsd 
_pdbx_validate_planes.type 
1 1 ASP A 96  ? ? 0.083 'SIDE CHAIN' 
2 1 GLU A 180 ? ? 0.083 'SIDE CHAIN' 
# 
_pdbx_validate_chiral.id              1 
_pdbx_validate_chiral.PDB_model_num   1 
_pdbx_validate_chiral.auth_atom_id    CA 
_pdbx_validate_chiral.label_alt_id    ? 
_pdbx_validate_chiral.auth_asym_id    A 
_pdbx_validate_chiral.auth_comp_id    LYS 
_pdbx_validate_chiral.auth_seq_id     241 
_pdbx_validate_chiral.PDB_ins_code    ? 
_pdbx_validate_chiral.details         PLANAR 
_pdbx_validate_chiral.omega           . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A LYS 241 ? CG  ? A LYS 241 CG  
2  1 Y 1 A LYS 241 ? CD  ? A LYS 241 CD  
3  1 Y 1 A LYS 241 ? CE  ? A LYS 241 CE  
4  1 Y 1 A LYS 241 ? NZ  ? A LYS 241 NZ  
5  1 Y 1 A VAL 242 ? CG1 ? A VAL 242 CG1 
6  1 Y 1 A VAL 242 ? CG2 ? A VAL 242 CG2 
7  1 Y 1 A LEU 244 ? CG  ? A LEU 244 CG  
8  1 Y 1 A LEU 244 ? CD1 ? A LEU 244 CD1 
9  1 Y 1 A LEU 244 ? CD2 ? A LEU 244 CD2 
10 1 Y 1 A VAL 246 ? CG1 ? A VAL 246 CG1 
11 1 Y 1 A VAL 246 ? CG2 ? A VAL 246 CG2 
12 1 Y 1 A ASN 248 ? CG  ? A ASN 248 CG  
13 1 Y 1 A ASN 248 ? OD1 ? A ASN 248 OD1 
14 1 Y 1 A ASN 248 ? ND2 ? A ASN 248 ND2 
15 1 Y 1 A LYS 249 ? CG  ? A LYS 249 CG  
16 1 Y 1 A LYS 249 ? CD  ? A LYS 249 CD  
17 1 Y 1 A LYS 249 ? CE  ? A LYS 249 CE  
18 1 Y 1 A LYS 249 ? NZ  ? A LYS 249 NZ  
19 1 Y 1 A GLU 250 ? CG  ? A GLU 250 CG  
20 1 Y 1 A GLU 250 ? CD  ? A GLU 250 CD  
21 1 Y 1 A GLU 250 ? OE1 ? A GLU 250 OE1 
22 1 Y 1 A GLU 250 ? OE2 ? A GLU 250 OE2 
23 1 Y 1 A HIS 251 ? CG  ? A HIS 251 CG  
24 1 Y 1 A HIS 251 ? ND1 ? A HIS 251 ND1 
25 1 Y 1 A HIS 251 ? CD2 ? A HIS 251 CD2 
26 1 Y 1 A HIS 251 ? CE1 ? A HIS 251 CE1 
27 1 Y 1 A HIS 251 ? NE2 ? A HIS 251 NE2 
28 1 Y 1 A VAL 253 ? CG1 ? A VAL 253 CG1 
29 1 Y 1 A VAL 253 ? CG2 ? A VAL 253 CG2 
30 1 Y 1 A GLU 254 ? CG  ? A GLU 254 CG  
31 1 Y 1 A GLU 254 ? CD  ? A GLU 254 CD  
32 1 Y 1 A GLU 254 ? OE1 ? A GLU 254 OE1 
33 1 Y 1 A GLU 254 ? OE2 ? A GLU 254 OE2 
# 
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 1   ? A MET 1   
2  1 Y 1 A ALA 2   ? A ALA 2   
3  1 Y 1 A VAL 3   ? A VAL 3   
4  1 Y 1 A ASP 4   ? A ASP 4   
5  1 Y 1 A SER 5   ? A SER 5   
6  1 Y 1 A SER 6   ? A SER 6   
7  1 Y 1 A ASN 7   ? A ASN 7   
8  1 Y 1 A SER 8   ? A SER 8   
9  1 Y 1 A ALA 9   ? A ALA 9   
10 1 Y 1 A THR 10  ? A THR 10  
11 1 Y 1 A ALA 239 ? A ALA 239 
12 1 Y 1 A GLU 240 ? A GLU 240 
13 1 Y 1 A VAL 255 ? A VAL 255 
14 1 Y 1 A CYS 256 ? A CYS 256 
15 1 Y 1 A THR 257 ? A THR 257 
16 1 Y 1 A GLY 258 ? A GLY 258 
17 1 Y 1 A ALA 259 ? A ALA 259 
18 1 Y 1 A LEU 260 ? A LEU 260 
19 1 Y 1 A ARG 261 ? A ARG 261 
20 1 Y 1 A LEU 262 ? A LEU 262 
21 1 Y 1 A LEU 263 ? A LEU 263 
22 1 Y 1 A THR 264 ? A THR 264 
23 1 Y 1 A ALA 265 ? A ALA 265 
24 1 Y 1 A GLY 266 ? A GLY 266 
25 1 Y 1 A GLN 267 ? A GLN 267 
26 1 Y 1 A ASN 268 ? A ASN 268 
27 1 Y 1 A THR 269 ? A THR 269 
28 1 Y 1 A THR 359 ? A THR 359 
29 1 Y 1 A SER 360 ? A SER 360 
30 1 Y 1 A LEU 361 ? A LEU 361 
31 1 Y 1 A PRO 362 ? A PRO 362 
32 1 Y 1 A CYS 363 ? A CYS 363 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'MAGNESIUM ION'                                MG  
3 'CHLORIDE ION'                                 CL  
4 ADENOSINE                                      ADN 
5 'PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER' ACP 
6 water                                          HOH 
# 
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 MG  1   999  999 MG  MG  A . 
C 3 CL  1   899  899 CL  CL  A . 
D 4 ADN 1   699  699 ADN ADN A . 
E 5 ACP 1   799  799 ACP ACP A . 
F 6 HOH 1   1000 100 HOH HOH A . 
F 6 HOH 2   1001 101 HOH HOH A . 
F 6 HOH 3   1002 102 HOH HOH A . 
F 6 HOH 4   1003 103 HOH HOH A . 
F 6 HOH 5   1004 104 HOH HOH A . 
F 6 HOH 6   1005 105 HOH HOH A . 
F 6 HOH 7   1006 106 HOH HOH A . 
F 6 HOH 8   1007 107 HOH HOH A . 
F 6 HOH 9   1008 108 HOH HOH A . 
F 6 HOH 10  1009 109 HOH HOH A . 
F 6 HOH 11  1010 110 HOH HOH A . 
F 6 HOH 12  1011 111 HOH HOH A . 
F 6 HOH 13  1012 112 HOH HOH A . 
F 6 HOH 14  1013 113 HOH HOH A . 
F 6 HOH 15  1014 114 HOH HOH A . 
F 6 HOH 16  1015 115 HOH HOH A . 
F 6 HOH 17  1016 116 HOH HOH A . 
F 6 HOH 18  1017 117 HOH HOH A . 
F 6 HOH 19  1018 118 HOH HOH A . 
F 6 HOH 20  1019 119 HOH HOH A . 
F 6 HOH 21  1020 120 HOH HOH A . 
F 6 HOH 22  1021 121 HOH HOH A . 
F 6 HOH 23  1022 122 HOH HOH A . 
F 6 HOH 24  1023 123 HOH HOH A . 
F 6 HOH 25  1024 124 HOH HOH A . 
F 6 HOH 26  1025 125 HOH HOH A . 
F 6 HOH 27  1026 126 HOH HOH A . 
F 6 HOH 28  1027 127 HOH HOH A . 
F 6 HOH 29  1028 128 HOH HOH A . 
F 6 HOH 30  1029 129 HOH HOH A . 
F 6 HOH 31  1030 130 HOH HOH A . 
F 6 HOH 32  1031 131 HOH HOH A . 
F 6 HOH 33  1032 132 HOH HOH A . 
F 6 HOH 34  1033 133 HOH HOH A . 
F 6 HOH 35  1034 134 HOH HOH A . 
F 6 HOH 36  1035 135 HOH HOH A . 
F 6 HOH 37  1036 136 HOH HOH A . 
F 6 HOH 38  1037 137 HOH HOH A . 
F 6 HOH 39  1038 138 HOH HOH A . 
F 6 HOH 40  1039 139 HOH HOH A . 
F 6 HOH 41  1040 140 HOH HOH A . 
F 6 HOH 42  1041 141 HOH HOH A . 
F 6 HOH 43  1042 142 HOH HOH A . 
F 6 HOH 44  1043 143 HOH HOH A . 
F 6 HOH 45  1044 144 HOH HOH A . 
F 6 HOH 46  1045 145 HOH HOH A . 
F 6 HOH 47  1046 146 HOH HOH A . 
F 6 HOH 48  1047 147 HOH HOH A . 
F 6 HOH 49  1048 148 HOH HOH A . 
F 6 HOH 50  1049 149 HOH HOH A . 
F 6 HOH 51  1050 150 HOH HOH A . 
F 6 HOH 52  1051 200 HOH HOH A . 
F 6 HOH 53  1052 201 HOH HOH A . 
F 6 HOH 54  1053 202 HOH HOH A . 
F 6 HOH 55  1054 203 HOH HOH A . 
F 6 HOH 56  1055 204 HOH HOH A . 
F 6 HOH 57  1056 205 HOH HOH A . 
F 6 HOH 58  1057 206 HOH HOH A . 
F 6 HOH 59  1058 207 HOH HOH A . 
F 6 HOH 60  1059 208 HOH HOH A . 
F 6 HOH 61  1060 209 HOH HOH A . 
F 6 HOH 62  1061 210 HOH HOH A . 
F 6 HOH 63  1062 211 HOH HOH A . 
F 6 HOH 64  1063 212 HOH HOH A . 
F 6 HOH 65  1064 213 HOH HOH A . 
F 6 HOH 66  1065 214 HOH HOH A . 
F 6 HOH 67  1066 215 HOH HOH A . 
F 6 HOH 68  1067 216 HOH HOH A . 
F 6 HOH 69  1068 217 HOH HOH A . 
F 6 HOH 70  1069 218 HOH HOH A . 
F 6 HOH 71  1070 219 HOH HOH A . 
F 6 HOH 72  1071 220 HOH HOH A . 
F 6 HOH 73  1072 221 HOH HOH A . 
F 6 HOH 74  1073 222 HOH HOH A . 
F 6 HOH 75  1074 223 HOH HOH A . 
F 6 HOH 76  1075 224 HOH HOH A . 
F 6 HOH 77  1076 225 HOH HOH A . 
F 6 HOH 78  1077 226 HOH HOH A . 
F 6 HOH 79  1078 227 HOH HOH A . 
F 6 HOH 80  1079 228 HOH HOH A . 
F 6 HOH 81  1080 229 HOH HOH A . 
F 6 HOH 82  1081 230 HOH HOH A . 
F 6 HOH 83  1082 231 HOH HOH A . 
F 6 HOH 84  1083 232 HOH HOH A . 
F 6 HOH 85  1084 233 HOH HOH A . 
F 6 HOH 86  1085 234 HOH HOH A . 
F 6 HOH 87  1086 235 HOH HOH A . 
F 6 HOH 88  1087 236 HOH HOH A . 
F 6 HOH 89  1088 301 HOH HOH A . 
F 6 HOH 90  1089 302 HOH HOH A . 
F 6 HOH 91  1090 303 HOH HOH A . 
F 6 HOH 92  1091 304 HOH HOH A . 
F 6 HOH 93  1092 305 HOH HOH A . 
F 6 HOH 94  1093 306 HOH HOH A . 
F 6 HOH 95  1094 307 HOH HOH A . 
F 6 HOH 96  1095 308 HOH HOH A . 
F 6 HOH 97  1096 309 HOH HOH A . 
F 6 HOH 98  1097 310 HOH HOH A . 
F 6 HOH 99  1098 312 HOH HOH A . 
F 6 HOH 100 1099 313 HOH HOH A . 
F 6 HOH 101 1100 314 HOH HOH A . 
F 6 HOH 102 1101 315 HOH HOH A . 
F 6 HOH 103 1102 316 HOH HOH A . 
F 6 HOH 104 1103 317 HOH HOH A . 
F 6 HOH 105 1104 318 HOH HOH A . 
F 6 HOH 106 1105 319 HOH HOH A . 
F 6 HOH 107 1106 320 HOH HOH A . 
F 6 HOH 108 1107 321 HOH HOH A . 
F 6 HOH 109 1108 322 HOH HOH A . 
F 6 HOH 110 1109 323 HOH HOH A . 
F 6 HOH 111 1110 324 HOH HOH A . 
F 6 HOH 112 1111 325 HOH HOH A . 
F 6 HOH 113 1112 326 HOH HOH A . 
F 6 HOH 114 1113 327 HOH HOH A . 
F 6 HOH 115 1114 328 HOH HOH A . 
F 6 HOH 116 1115 329 HOH HOH A . 
F 6 HOH 117 1116 330 HOH HOH A . 
F 6 HOH 118 1117 400 HOH HOH A . 
F 6 HOH 119 1118 401 HOH HOH A . 
F 6 HOH 120 1119 402 HOH HOH A . 
F 6 HOH 121 1120 403 HOH HOH A . 
F 6 HOH 122 1121 404 HOH HOH A . 
F 6 HOH 123 1122 405 HOH HOH A . 
F 6 HOH 124 1123 406 HOH HOH A . 
F 6 HOH 125 1124 407 HOH HOH A . 
F 6 HOH 126 1125 408 HOH HOH A . 
F 6 HOH 127 1126 409 HOH HOH A . 
F 6 HOH 128 1127 410 HOH HOH A . 
F 6 HOH 129 1128 411 HOH HOH A . 
F 6 HOH 130 1129 412 HOH HOH A . 
F 6 HOH 131 1130 413 HOH HOH A . 
F 6 HOH 132 1131 414 HOH HOH A . 
F 6 HOH 133 1132 415 HOH HOH A . 
F 6 HOH 134 1133 416 HOH HOH A . 
F 6 HOH 135 1134 417 HOH HOH A . 
F 6 HOH 136 1135 418 HOH HOH A . 
F 6 HOH 137 1136 419 HOH HOH A . 
F 6 HOH 138 1137 420 HOH HOH A . 
F 6 HOH 139 1138 421 HOH HOH A . 
F 6 HOH 140 1139 423 HOH HOH A . 
F 6 HOH 141 1140 424 HOH HOH A . 
F 6 HOH 142 1141 425 HOH HOH A . 
F 6 HOH 143 1142 500 HOH HOH A . 
F 6 HOH 144 1143 501 HOH HOH A . 
F 6 HOH 145 1144 502 HOH HOH A . 
F 6 HOH 146 1145 503 HOH HOH A . 
F 6 HOH 147 1146 504 HOH HOH A . 
F 6 HOH 148 1147 505 HOH HOH A . 
F 6 HOH 149 1148 506 HOH HOH A . 
F 6 HOH 150 1149 507 HOH HOH A . 
F 6 HOH 151 1150 508 HOH HOH A . 
F 6 HOH 152 1151 509 HOH HOH A . 
F 6 HOH 153 1152 510 HOH HOH A . 
F 6 HOH 154 1153 511 HOH HOH A . 
F 6 HOH 155 1154 512 HOH HOH A . 
F 6 HOH 156 1155 513 HOH HOH A . 
F 6 HOH 157 1156 514 HOH HOH A . 
F 6 HOH 158 1157 515 HOH HOH A . 
F 6 HOH 159 1158 516 HOH HOH A . 
F 6 HOH 160 1159 517 HOH HOH A . 
F 6 HOH 161 1160 518 HOH HOH A . 
F 6 HOH 162 1161 519 HOH HOH A . 
F 6 HOH 163 1162 520 HOH HOH A . 
F 6 HOH 164 1163 521 HOH HOH A . 
F 6 HOH 165 1164 522 HOH HOH A . 
F 6 HOH 166 1165 523 HOH HOH A . 
F 6 HOH 167 1166 524 HOH HOH A . 
F 6 HOH 168 1167 525 HOH HOH A . 
F 6 HOH 169 1168 526 HOH HOH A . 
F 6 HOH 170 1169 527 HOH HOH A . 
# 



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elNémo is maintained by Yves-Henri Sanejouand.
It was developed by Karsten Suhre.
Between 2003 and 2014, it was hosted by IGS (Marseille).
Last modification: October 18th, 2018.