2gaa.cif

data_2GAA
# 
_entry.id   2GAA 
# 
_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   2GAA         
RCSB  RCSB036885   
WWPDB D_1000036885 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.details 
_pdbx_database_related.content_type 
PDB 1UJ2 . unspecified 
PDB 2GA8 . unspecified 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        2GAA 
_pdbx_database_status.recvd_initial_deposition_date   2006-03-08 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_cs                  ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Chaptal, V.' 1 
'Morera, S.'  2 
# 
_citation.id                        primary 
_citation.title                     
;Crystal structure and functional analysis identify the P-loop containing protein YFH7 of Saccharomyces cerevisiae as an ATP-dependent kinase.
;
_citation.journal_abbrev            Proteins 
_citation.journal_volume            71 
_citation.page_first                804 
_citation.page_last                 812 
_citation.year                      2007 
_citation.journal_id_ASTM           PSFGEY 
_citation.country                   US 
_citation.journal_id_ISSN           0887-3585 
_citation.journal_id_CSD            0867 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   18004758 
_citation.pdbx_database_id_DOI      10.1002/prot.21740 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Gueguen-Chaignon, V.' 1 
primary 'Chaptal, V.'          2 
primary 'Lariviere, L.'        3 
primary 'Costa, N.'            4 
primary 'Lopes, P.'            5 
primary 'Morera, S.'           6 
primary 'Nessler, S.'          7 
# 
_cell.entry_id           2GAA 
_cell.length_a           134.756 
_cell.length_b           134.756 
_cell.length_c           48.679 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        120.00 
_cell.Z_PDB              9 
_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                         2GAA 
_symmetry.space_group_name_H-M             'H 3' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                146 
_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 'Hypothetical 39.9 kDa protein' 40996.633 1   ? ? ? ? 
2 non-polymer syn 'SULFATE ION'                   96.063    1   ? ? ? ? 
3 water       nat water                           18.015    180 ? ? ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   yes 
_entity_poly.pdbx_seq_one_letter_code       
;MVDTHKLADDVLQLLDNRIEDNYRVCVILVGSPGSGKSTIAEEL(CME)QIINEKYHTFLSEHPNVIEVNDRLKPMVNLV
DSLKTLQPNKVAEMIENQGLFKDHVEDVNFQPVKYSALTSNNEE(CME)TAVVARGGTANAIRIAAVDNPVNVNKLAQDS
INIAQIVPMDGFHLSRRCLDLFKDPQTAHKRRGSPSTFDSNNFLQLCKILAKTSL(CME)KVSSHHKFYSTSSVFEKLSK
TFSQTIPDIFVPGFNHALKDPTPDQYCISKFTRIVILEGLYLLYDQENWKKIYKTLADTGALLVYKIDIDYEATEERVAK
RHLQSGLVTTIAEGREKFRSNDLLNGRDIDNHLIKVDNIVHIRNDHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MVDTHKLADDVLQLLDNRIEDNYRVCVILVGSPGSGKSTIAEELCQIINEKYHTFLSEHPNVIEVNDRLKPMVNLVDSLK
TLQPNKVAEMIENQGLFKDHVEDVNFQPVKYSALTSNNEECTAVVARGGTANAIRIAAVDNPVNVNKLAQDSINIAQIVP
MDGFHLSRRCLDLFKDPQTAHKRRGSPSTFDSNNFLQLCKILAKTSLCKVSSHHKFYSTSSVFEKLSKTFSQTIPDIFVP
GFNHALKDPTPDQYCISKFTRIVILEGLYLLYDQENWKKIYKTLADTGALLVYKIDIDYEATEERVAKRHLQSGLVTTIA
EGREKFRSNDLLNGRDIDNHLIKVDNIVHIRNDHHHHHH
;
_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   VAL n 
1 3   ASP n 
1 4   THR n 
1 5   HIS n 
1 6   LYS n 
1 7   LEU n 
1 8   ALA n 
1 9   ASP n 
1 10  ASP n 
1 11  VAL n 
1 12  LEU n 
1 13  GLN n 
1 14  LEU n 
1 15  LEU n 
1 16  ASP n 
1 17  ASN n 
1 18  ARG n 
1 19  ILE n 
1 20  GLU n 
1 21  ASP n 
1 22  ASN n 
1 23  TYR n 
1 24  ARG n 
1 25  VAL n 
1 26  CYS n 
1 27  VAL n 
1 28  ILE n 
1 29  LEU n 
1 30  VAL n 
1 31  GLY n 
1 32  SER n 
1 33  PRO n 
1 34  GLY n 
1 35  SER n 
1 36  GLY n 
1 37  LYS n 
1 38  SER n 
1 39  THR n 
1 40  ILE n 
1 41  ALA n 
1 42  GLU n 
1 43  GLU n 
1 44  LEU n 
1 45  CME n 
1 46  GLN n 
1 47  ILE n 
1 48  ILE n 
1 49  ASN n 
1 50  GLU n 
1 51  LYS n 
1 52  TYR n 
1 53  HIS n 
1 54  THR n 
1 55  PHE n 
1 56  LEU n 
1 57  SER n 
1 58  GLU n 
1 59  HIS n 
1 60  PRO n 
1 61  ASN n 
1 62  VAL n 
1 63  ILE n 
1 64  GLU n 
1 65  VAL n 
1 66  ASN n 
1 67  ASP n 
1 68  ARG n 
1 69  LEU n 
1 70  LYS n 
1 71  PRO n 
1 72  MET n 
1 73  VAL n 
1 74  ASN n 
1 75  LEU n 
1 76  VAL n 
1 77  ASP n 
1 78  SER n 
1 79  LEU n 
1 80  LYS n 
1 81  THR n 
1 82  LEU n 
1 83  GLN n 
1 84  PRO n 
1 85  ASN n 
1 86  LYS n 
1 87  VAL n 
1 88  ALA n 
1 89  GLU n 
1 90  MET n 
1 91  ILE n 
1 92  GLU n 
1 93  ASN n 
1 94  GLN n 
1 95  GLY n 
1 96  LEU n 
1 97  PHE n 
1 98  LYS n 
1 99  ASP n 
1 100 HIS n 
1 101 VAL n 
1 102 GLU n 
1 103 ASP n 
1 104 VAL n 
1 105 ASN n 
1 106 PHE n 
1 107 GLN n 
1 108 PRO n 
1 109 VAL n 
1 110 LYS n 
1 111 TYR n 
1 112 SER n 
1 113 ALA n 
1 114 LEU n 
1 115 THR n 
1 116 SER n 
1 117 ASN n 
1 118 ASN n 
1 119 GLU n 
1 120 GLU n 
1 121 CME n 
1 122 THR n 
1 123 ALA n 
1 124 VAL n 
1 125 VAL n 
1 126 ALA n 
1 127 ARG n 
1 128 GLY n 
1 129 GLY n 
1 130 THR n 
1 131 ALA n 
1 132 ASN n 
1 133 ALA n 
1 134 ILE n 
1 135 ARG n 
1 136 ILE n 
1 137 ALA n 
1 138 ALA n 
1 139 VAL n 
1 140 ASP n 
1 141 ASN n 
1 142 PRO n 
1 143 VAL n 
1 144 ASN n 
1 145 VAL n 
1 146 ASN n 
1 147 LYS n 
1 148 LEU n 
1 149 ALA n 
1 150 GLN n 
1 151 ASP n 
1 152 SER n 
1 153 ILE n 
1 154 ASN n 
1 155 ILE n 
1 156 ALA n 
1 157 GLN n 
1 158 ILE n 
1 159 VAL n 
1 160 PRO n 
1 161 MET n 
1 162 ASP n 
1 163 GLY n 
1 164 PHE n 
1 165 HIS n 
1 166 LEU n 
1 167 SER n 
1 168 ARG n 
1 169 ARG n 
1 170 CYS n 
1 171 LEU n 
1 172 ASP n 
1 173 LEU n 
1 174 PHE n 
1 175 LYS n 
1 176 ASP n 
1 177 PRO n 
1 178 GLN n 
1 179 THR n 
1 180 ALA n 
1 181 HIS n 
1 182 LYS n 
1 183 ARG n 
1 184 ARG n 
1 185 GLY n 
1 186 SER n 
1 187 PRO n 
1 188 SER n 
1 189 THR n 
1 190 PHE n 
1 191 ASP n 
1 192 SER n 
1 193 ASN n 
1 194 ASN n 
1 195 PHE n 
1 196 LEU n 
1 197 GLN n 
1 198 LEU n 
1 199 CYS n 
1 200 LYS n 
1 201 ILE n 
1 202 LEU n 
1 203 ALA n 
1 204 LYS n 
1 205 THR n 
1 206 SER n 
1 207 LEU n 
1 208 CME n 
1 209 LYS n 
1 210 VAL n 
1 211 SER n 
1 212 SER n 
1 213 HIS n 
1 214 HIS n 
1 215 LYS n 
1 216 PHE n 
1 217 TYR n 
1 218 SER n 
1 219 THR n 
1 220 SER n 
1 221 SER n 
1 222 VAL n 
1 223 PHE n 
1 224 GLU n 
1 225 LYS n 
1 226 LEU n 
1 227 SER n 
1 228 LYS n 
1 229 THR n 
1 230 PHE n 
1 231 SER n 
1 232 GLN n 
1 233 THR n 
1 234 ILE n 
1 235 PRO n 
1 236 ASP n 
1 237 ILE n 
1 238 PHE n 
1 239 VAL n 
1 240 PRO n 
1 241 GLY n 
1 242 PHE n 
1 243 ASN n 
1 244 HIS n 
1 245 ALA n 
1 246 LEU n 
1 247 LYS n 
1 248 ASP n 
1 249 PRO n 
1 250 THR n 
1 251 PRO n 
1 252 ASP n 
1 253 GLN n 
1 254 TYR n 
1 255 CYS n 
1 256 ILE n 
1 257 SER n 
1 258 LYS n 
1 259 PHE n 
1 260 THR n 
1 261 ARG n 
1 262 ILE n 
1 263 VAL n 
1 264 ILE n 
1 265 LEU n 
1 266 GLU n 
1 267 GLY n 
1 268 LEU n 
1 269 TYR n 
1 270 LEU n 
1 271 LEU n 
1 272 TYR n 
1 273 ASP n 
1 274 GLN n 
1 275 GLU n 
1 276 ASN n 
1 277 TRP n 
1 278 LYS n 
1 279 LYS n 
1 280 ILE n 
1 281 TYR n 
1 282 LYS n 
1 283 THR n 
1 284 LEU n 
1 285 ALA n 
1 286 ASP n 
1 287 THR n 
1 288 GLY n 
1 289 ALA n 
1 290 LEU n 
1 291 LEU n 
1 292 VAL n 
1 293 TYR n 
1 294 LYS n 
1 295 ILE n 
1 296 ASP n 
1 297 ILE n 
1 298 ASP n 
1 299 TYR n 
1 300 GLU n 
1 301 ALA n 
1 302 THR n 
1 303 GLU n 
1 304 GLU n 
1 305 ARG n 
1 306 VAL n 
1 307 ALA n 
1 308 LYS n 
1 309 ARG n 
1 310 HIS n 
1 311 LEU n 
1 312 GLN n 
1 313 SER n 
1 314 GLY n 
1 315 LEU n 
1 316 VAL n 
1 317 THR n 
1 318 THR n 
1 319 ILE n 
1 320 ALA n 
1 321 GLU n 
1 322 GLY n 
1 323 ARG n 
1 324 GLU n 
1 325 LYS n 
1 326 PHE n 
1 327 ARG n 
1 328 SER n 
1 329 ASN n 
1 330 ASP n 
1 331 LEU n 
1 332 LEU n 
1 333 ASN n 
1 334 GLY n 
1 335 ARG n 
1 336 ASP n 
1 337 ILE n 
1 338 ASP n 
1 339 ASN n 
1 340 HIS n 
1 341 LEU n 
1 342 ILE n 
1 343 LYS n 
1 344 VAL n 
1 345 ASP n 
1 346 ASN n 
1 347 ILE n 
1 348 VAL n 
1 349 HIS n 
1 350 ILE n 
1 351 ARG n 
1 352 ASN n 
1 353 ASP n 
1 354 HIS n 
1 355 HIS n 
1 356 HIS n 
1 357 HIS n 
1 358 HIS n 
1 359 HIS 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               
;baker's yeast
;
_entity_src_gen.gene_src_genus                     Saccharomyces 
_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      'Saccharomyces cerevisiae' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     4932 
_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               'BL21 Star' 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    YFH7_YEAST 
_struct_ref.pdbx_db_accession          P43591 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MVDTHKLADDVLQLLDNRIEDNYRVCVILVGSPGSGKSTIAEELCQIINEKYHTFLSEHPNVIEVNDRLKPMVNLVDSLK
TLQPNKVAEMIENQGLFKDHVEDVNFQPVKYSALTSNNEECTAVVARGGTANAIRIAAVDNPVNVNKLAQDSINIAQIVP
MDGFHLSRRCLDLFKDPQTAHKRRGSPSTFDSNNFLQLCKILAKTSLCKVSSHHKFYSTSSVFEKLSKTFSQTIPDIFVP
GFNHALKDPTPDQYCISKFTRIVILEGLYLLYDQENWKKIYKTLADTGALLVYKIDIDYEATEERVAKRHLQSGLVTTIA
EGREKFRSNDLLNGRDIDNHLIKVDNIVHIRND
;
_struct_ref.pdbx_align_begin           1 
_struct_ref.pdbx_db_isoform            ? 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              2GAA 
_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                 353 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P43591 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  353 
_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       353 
# 
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 2GAA HIS A 354 ? UNP P43591 ? ? 'EXPRESSION TAG' 354 1 
1 2GAA HIS A 355 ? UNP P43591 ? ? 'EXPRESSION TAG' 355 2 
1 2GAA HIS A 356 ? UNP P43591 ? ? 'EXPRESSION TAG' 356 3 
1 2GAA HIS A 357 ? UNP P43591 ? ? 'EXPRESSION TAG' 357 4 
1 2GAA HIS A 358 ? UNP P43591 ? ? 'EXPRESSION TAG' 358 5 
1 2GAA HIS A 359 ? UNP P43591 ? ? 'EXPRESSION TAG' 359 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 
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 
CME 'L-peptide linking' n 'S,S-(2-HYDROXYETHYL)THIOCYSTEINE' ? 'C5 H11 N O3 S2' 197.276 
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 
SO4 non-polymer         . 'SULFATE ION'                      ? 'O4 S -2'        96.063  
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          2GAA 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.07 
_exptl_crystal.density_percent_sol   40.70 
_exptl_crystal.description           ? 
_exptl_crystal.F_000                 ? 
_exptl_crystal.preparation           ? 
# 
_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              6.5 
_exptl_crystal_grow.pdbx_details    
;PEG 5000MME  
ammonium sulfate, pH 6.5,VAPOR DIFFUSION, HANGING DROP, temperature 298K
;
_exptl_crystal_grow.pdbx_pH_range   . 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               CCD 
_diffrn_detector.type                   MARRESEARCH 
_diffrn_detector.pdbx_collection_date   2005-02-20 
_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   0.98 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'ESRF BEAMLINE ID23-1' 
_diffrn_source.pdbx_synchrotron_site       ESRF 
_diffrn_source.pdbx_synchrotron_beamline   ID23-1 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_wavelength_list        0.98 
# 
_reflns.entry_id                     2GAA 
_reflns.observed_criterion_sigma_I   1 
_reflns.observed_criterion_sigma_F   1 
_reflns.d_resolution_low             20 
_reflns.d_resolution_high            1.95 
_reflns.number_obs                   23765 
_reflns.number_all                   23990 
_reflns.percent_possible_obs         99.1 
_reflns.pdbx_Rmerge_I_obs            ? 
_reflns.pdbx_Rsym_value              0.059 
_reflns.pdbx_netI_over_sigmaI        ? 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              2.8 
_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             1.95 
_reflns_shell.d_res_low              2.06 
_reflns_shell.percent_possible_all   99 
_reflns_shell.Rmerge_I_obs           ? 
_reflns_shell.pdbx_Rsym_value        0.378 
_reflns_shell.meanI_over_sigI_obs    ? 
_reflns_shell.pdbx_redundancy        2.5 
_reflns_shell.percent_possible_obs   ? 
_reflns_shell.number_unique_all      3436 
_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                                 2GAA 
_refine.ls_number_reflns_obs                     23765 
_refine.ls_number_reflns_all                     23990 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          2 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             20 
_refine.ls_d_res_high                            1.95 
_refine.ls_percent_reflns_obs                    ? 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.193 
_refine.ls_R_factor_R_free                       0.232 
_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                  1156 
_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                      2GA8 
_refine.pdbx_method_to_determine_struct          'FOURIER SYNTHESIS' 
_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                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_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.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_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_overall_phase_error                 ? 
_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        2625 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         5 
_refine_hist.number_atoms_solvent             180 
_refine_hist.number_atoms_total               2810 
_refine_hist.d_res_high                       1.95 
_refine_hist.d_res_low                        20 
# 
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 
c_bond_d    0.0048 ? ? ? 'X-RAY DIFFRACTION' ? 
c_angle_deg 1.19   ? ? ? 'X-RAY DIFFRACTION' ? 
# 
_struct.entry_id                  2GAA 
_struct.title                     
'Crystal structure of YFH7 from Saccharomyces cerevisiae: a putative P-loop containing kinase with a circular permutation.' 
_struct.pdbx_descriptor           'Hypothetical 39.9 kDa protein' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        2GAA 
_struct_keywords.pdbx_keywords   'UNKNOWN FUNCTION' 
_struct_keywords.text            'YFR007w, YFH7, UNKNOWN FUNCTION' 
# 
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 ? 
# 
_struct_biol.id        1 
_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  ASP A 3   ? ILE A 19  ? ASP A 3   ILE A 19  1 ? 17 
HELX_P HELX_P2  2  GLY A 36  ? HIS A 59  ? GLY A 36  HIS A 59  1 ? 24 
HELX_P HELX_P3  3  GLN A 83  ? ASN A 93  ? GLN A 83  ASN A 93  1 ? 11 
HELX_P HELX_P4  4  PHE A 97  ? VAL A 101 ? PHE A 97  VAL A 101 5 ? 5  
HELX_P HELX_P5  5  GLY A 128 ? ALA A 133 ? GLY A 128 ALA A 133 5 ? 6  
HELX_P HELX_P6  6  ASP A 162 ? HIS A 165 ? ASP A 162 HIS A 165 5 ? 4  
HELX_P HELX_P7  7  SER A 167 ? LEU A 173 ? SER A 167 LEU A 173 1 ? 7  
HELX_P HELX_P8  8  ASP A 176 ? ARG A 183 ? ASP A 176 ARG A 183 1 ? 8  
HELX_P HELX_P9  9  SER A 186 ? PHE A 190 ? SER A 186 PHE A 190 5 ? 5  
HELX_P HELX_P10 10 ASP A 191 ? LEU A 207 ? ASP A 191 LEU A 207 1 ? 17 
HELX_P HELX_P11 11 SER A 221 ? LYS A 228 ? SER A 221 LYS A 228 1 ? 8  
HELX_P HELX_P12 12 GLN A 274 ? ASP A 286 ? GLN A 274 ASP A 286 1 ? 13 
HELX_P HELX_P13 13 ASP A 298 ? SER A 313 ? ASP A 298 SER A 313 1 ? 16 
HELX_P HELX_P14 14 THR A 318 ? ASN A 329 ? THR A 318 ASN A 329 1 ? 12 
HELX_P HELX_P15 15 GLY A 334 ? HIS A 340 ? GLY A 334 HIS A 340 1 ? 7  
# 
_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 
covale1 covale ? ? A LEU 44  C ? ? ? 1_555 A CME 45  N ? ? A LEU 44  A CME 45  1_555 ? ? ? ? ? ? ? 1.325 ? 
covale2 covale ? ? A CME 45  C ? ? ? 1_555 A GLN 46  N ? ? A CME 45  A GLN 46  1_555 ? ? ? ? ? ? ? 1.464 ? 
covale3 covale ? ? A GLU 120 C ? ? ? 1_555 A CME 121 N ? ? A GLU 120 A CME 121 1_555 ? ? ? ? ? ? ? 1.215 ? 
covale4 covale ? ? A CME 121 C ? ? ? 1_555 A THR 122 N ? ? A CME 121 A THR 122 1_555 ? ? ? ? ? ? ? 1.551 ? 
covale5 covale ? ? A LEU 207 C ? ? ? 1_555 A CME 208 N ? ? A LEU 207 A CME 208 1_555 ? ? ? ? ? ? ? 1.138 ? 
covale6 covale ? ? A CME 208 C ? ? ? 1_555 A LYS 209 N ? ? A CME 208 A LYS 209 1_555 ? ? ? ? ? ? ? 1.452 ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A ? 5 ? 
B ? 2 ? 
C ? 6 ? 
# 
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      
B 1 2 ? parallel      
C 1 2 ? parallel      
C 2 3 ? anti-parallel 
C 3 4 ? anti-parallel 
C 4 5 ? anti-parallel 
C 5 6 ? 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 156 ? PRO A 160 ? ALA A 156 PRO A 160 
A 2 ILE A 262 ? GLY A 267 ? ILE A 262 GLY A 267 
A 3 VAL A 25  ? VAL A 30  ? VAL A 25  VAL A 30  
A 4 LEU A 290 ? ASP A 296 ? LEU A 290 ASP A 296 
A 5 ILE A 347 ? ARG A 351 ? ILE A 347 ARG A 351 
B 1 VAL A 65  ? ASN A 66  ? VAL A 65  ASN A 66  
B 2 PHE A 230 ? SER A 231 ? PHE A 230 SER A 231 
C 1 LYS A 80  ? THR A 81  ? LYS A 80  THR A 81  
C 2 VAL A 109 ? ALA A 113 ? VAL A 109 ALA A 113 
C 3 CME A 121 ? VAL A 125 ? CME A 121 VAL A 125 
C 4 ILE A 134 ? ALA A 137 ? ILE A 134 ALA A 137 
C 5 ILE A 237 ? ASN A 243 ? ILE A 237 ASN A 243 
C 6 ASP A 248 ? ILE A 256 ? ASP A 248 ILE A 256 
# 
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 N VAL A 159 ? N VAL A 159 O ILE A 264 ? O ILE A 264 
A 2 3 O LEU A 265 ? O LEU A 265 N VAL A 27  ? N VAL A 27  
A 3 4 N VAL A 30  ? N VAL A 30  O ILE A 295 ? O ILE A 295 
A 4 5 N ASP A 296 ? N ASP A 296 O ILE A 350 ? O ILE A 350 
B 1 2 N ASN A 66  ? N ASN A 66  O PHE A 230 ? O PHE A 230 
C 1 2 N LYS A 80  ? N LYS A 80  O LYS A 110 ? O LYS A 110 
C 2 3 N VAL A 109 ? N VAL A 109 O VAL A 125 ? O VAL A 125 
C 3 4 N VAL A 124 ? N VAL A 124 O ILE A 134 ? O ILE A 134 
C 4 5 N ARG A 135 ? N ARG A 135 O PHE A 238 ? O PHE A 238 
C 5 6 N GLY A 241 ? N GLY A 241 O THR A 250 ? O THR A 250 
# 
_struct_site.id                   AC1 
_struct_site.pdbx_evidence_code   Software 
_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    9 
_struct_site.details              'BINDING SITE FOR RESIDUE SO4 A 2847' 
# 
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 9 SER A 32  ? SER A 32   . ? 1_555 ? 
2 AC1 9 GLY A 34  ? GLY A 34   . ? 1_555 ? 
3 AC1 9 SER A 35  ? SER A 35   . ? 1_555 ? 
4 AC1 9 GLY A 36  ? GLY A 36   . ? 1_555 ? 
5 AC1 9 LYS A 37  ? LYS A 37   . ? 1_555 ? 
6 AC1 9 SER A 38  ? SER A 38   . ? 1_555 ? 
7 AC1 9 ARG A 309 ? ARG A 309  . ? 1_555 ? 
8 AC1 9 HOH C .   ? HOH A 2857 . ? 1_555 ? 
9 AC1 9 HOH C .   ? HOH A 3005 . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          2GAA 
_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                    2GAA 
_atom_sites.fract_transf_matrix[1][1]   0.007421 
_atom_sites.fract_transf_matrix[1][2]   0.004284 
_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]   0.008569 
_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]   0.020543 
_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   . VAL A 1 2   ? 20.864 -2.201 2.638   1.00 37.70 ? 2    VAL A N   1 
ATOM   2    C CA  . VAL A 1 2   ? 20.651 -2.256 4.114   1.00 36.53 ? 2    VAL A CA  1 
ATOM   3    C C   . VAL A 1 2   ? 19.173 -2.064 4.445   1.00 35.10 ? 2    VAL A C   1 
ATOM   4    O O   . VAL A 1 2   ? 18.454 -1.350 3.745   1.00 37.24 ? 2    VAL A O   1 
ATOM   5    C CB  . VAL A 1 2   ? 21.478 -1.158 4.838   1.00 36.80 ? 2    VAL A CB  1 
ATOM   6    C CG1 . VAL A 1 2   ? 21.004 0.222  4.407   1.00 34.55 ? 2    VAL A CG1 1 
ATOM   7    C CG2 . VAL A 1 2   ? 21.363 -1.322 6.345   1.00 35.24 ? 2    VAL A CG2 1 
ATOM   8    N N   . ASP A 1 3   ? 18.725 -2.715 5.510   1.00 34.98 ? 3    ASP A N   1 
ATOM   9    C CA  . ASP A 1 3   ? 17.336 -2.615 5.945   1.00 34.72 ? 3    ASP A CA  1 
ATOM   10   C C   . ASP A 1 3   ? 17.249 -1.492 6.982   1.00 32.91 ? 3    ASP A C   1 
ATOM   11   O O   . ASP A 1 3   ? 17.628 -1.682 8.136   1.00 32.17 ? 3    ASP A O   1 
ATOM   12   C CB  . ASP A 1 3   ? 16.898 -3.936 6.575   1.00 36.71 ? 3    ASP A CB  1 
ATOM   13   C CG  . ASP A 1 3   ? 15.397 -4.038 6.731   1.00 38.31 ? 3    ASP A CG  1 
ATOM   14   O OD1 . ASP A 1 3   ? 14.777 -3.088 7.247   1.00 42.22 ? 3    ASP A OD1 1 
ATOM   15   O OD2 . ASP A 1 3   ? 14.838 -5.080 6.338   1.00 42.12 ? 3    ASP A OD2 1 
ATOM   16   N N   . THR A 1 4   ? 16.751 -0.330 6.572   1.00 31.80 ? 4    THR A N   1 
ATOM   17   C CA  . THR A 1 4   ? 16.655 0.811  7.477   1.00 31.89 ? 4    THR A CA  1 
ATOM   18   C C   . THR A 1 4   ? 15.604 0.650  8.573   1.00 30.07 ? 4    THR A C   1 
ATOM   19   O O   . THR A 1 4   ? 15.720 1.251  9.640   1.00 27.93 ? 4    THR A O   1 
ATOM   20   C CB  . THR A 1 4   ? 16.390 2.116  6.699   1.00 32.58 ? 4    THR A CB  1 
ATOM   21   O OG1 . THR A 1 4   ? 15.129 2.032  6.025   1.00 34.67 ? 4    THR A OG1 1 
ATOM   22   C CG2 . THR A 1 4   ? 17.489 2.347  5.673   1.00 33.72 ? 4    THR A CG2 1 
ATOM   23   N N   . HIS A 1 5   ? 14.578 -0.156 8.324   1.00 29.53 ? 5    HIS A N   1 
ATOM   24   C CA  . HIS A 1 5   ? 13.565 -0.362 9.350   1.00 29.09 ? 5    HIS A CA  1 
ATOM   25   C C   . HIS A 1 5   ? 14.157 -1.225 10.451  1.00 28.81 ? 5    HIS A C   1 
ATOM   26   O O   . HIS A 1 5   ? 13.807 -1.084 11.623  1.00 29.00 ? 5    HIS A O   1 
ATOM   27   C CB  . HIS A 1 5   ? 12.314 -1.022 8.768   1.00 29.80 ? 5    HIS A CB  1 
ATOM   28   C CG  . HIS A 1 5   ? 11.480 -0.096 7.942   1.00 30.10 ? 5    HIS A CG  1 
ATOM   29   N ND1 . HIS A 1 5   ? 11.807 0.246  6.647   1.00 30.44 ? 5    HIS A ND1 1 
ATOM   30   C CD2 . HIS A 1 5   ? 10.351 0.591  8.239   1.00 30.58 ? 5    HIS A CD2 1 
ATOM   31   C CE1 . HIS A 1 5   ? 10.915 1.103  6.182   1.00 31.63 ? 5    HIS A CE1 1 
ATOM   32   N NE2 . HIS A 1 5   ? 10.021 1.329  7.127   1.00 31.58 ? 5    HIS A NE2 1 
ATOM   33   N N   . LYS A 1 6   ? 15.064 -2.118 10.070  1.00 28.73 ? 6    LYS A N   1 
ATOM   34   C CA  . LYS A 1 6   ? 15.714 -2.982 11.045  1.00 27.94 ? 6    LYS A CA  1 
ATOM   35   C C   . LYS A 1 6   ? 16.684 -2.137 11.870  1.00 25.58 ? 6    LYS A C   1 
ATOM   36   O O   . LYS A 1 6   ? 16.854 -2.373 13.063  1.00 25.60 ? 6    LYS A O   1 
ATOM   37   C CB  . LYS A 1 6   ? 16.468 -4.116 10.347  1.00 30.10 ? 6    LYS A CB  1 
ATOM   38   C CG  . LYS A 1 6   ? 17.317 -4.969 11.288  1.00 34.68 ? 6    LYS A CG  1 
ATOM   39   C CD  . LYS A 1 6   ? 16.473 -5.607 12.387  1.00 38.77 ? 6    LYS A CD  1 
ATOM   40   C CE  . LYS A 1 6   ? 17.345 -6.313 13.420  1.00 39.55 ? 6    LYS A CE  1 
ATOM   41   N NZ  . LYS A 1 6   ? 18.167 -7.393 12.808  1.00 44.52 ? 6    LYS A NZ  1 
ATOM   42   N N   . LEU A 1 7   ? 17.327 -1.161 11.232  1.00 25.04 ? 7    LEU A N   1 
ATOM   43   C CA  . LEU A 1 7   ? 18.250 -0.290 11.956  1.00 23.60 ? 7    LEU A CA  1 
ATOM   44   C C   . LEU A 1 7   ? 17.419 0.486  12.962  1.00 21.28 ? 7    LEU A C   1 
ATOM   45   O O   . LEU A 1 7   ? 17.810 0.651  14.108  1.00 21.68 ? 7    LEU A O   1 
ATOM   46   C CB  . LEU A 1 7   ? 18.952 0.690  11.016  1.00 25.72 ? 7    LEU A CB  1 
ATOM   47   C CG  . LEU A 1 7   ? 20.021 0.137  10.072  1.00 26.98 ? 7    LEU A CG  1 
ATOM   48   C CD1 . LEU A 1 7   ? 20.736 1.293  9.403   1.00 27.98 ? 7    LEU A CD1 1 
ATOM   49   C CD2 . LEU A 1 7   ? 21.012 -0.708 10.847  1.00 29.12 ? 7    LEU A CD2 1 
ATOM   50   N N   . ALA A 1 8   ? 16.263 0.957  12.514  1.00 20.13 ? 8    ALA A N   1 
ATOM   51   C CA  . ALA A 1 8   ? 15.356 1.696  13.377  1.00 20.65 ? 8    ALA A CA  1 
ATOM   52   C C   . ALA A 1 8   ? 14.988 0.824  14.577  1.00 18.91 ? 8    ALA A C   1 
ATOM   53   O O   . ALA A 1 8   ? 14.958 1.298  15.706  1.00 17.30 ? 8    ALA A O   1 
ATOM   54   C CB  . ALA A 1 8   ? 14.101 2.092  12.604  1.00 18.12 ? 8    ALA A CB  1 
ATOM   55   N N   . ASP A 1 9   ? 14.718 -0.454 14.331  1.00 21.05 ? 9    ASP A N   1 
ATOM   56   C CA  . ASP A 1 9   ? 14.360 -1.368 15.415  1.00 22.26 ? 9    ASP A CA  1 
ATOM   57   C C   . ASP A 1 9   ? 15.513 -1.561 16.388  1.00 21.86 ? 9    ASP A C   1 
ATOM   58   O O   . ASP A 1 9   ? 15.302 -1.632 17.596  1.00 18.77 ? 9    ASP A O   1 
ATOM   59   C CB  . ASP A 1 9   ? 13.930 -2.735 14.872  1.00 26.17 ? 9    ASP A CB  1 
ATOM   60   C CG  . ASP A 1 9   ? 12.561 -2.701 14.205  1.00 28.74 ? 9    ASP A CG  1 
ATOM   61   O OD1 . ASP A 1 9   ? 11.800 -1.728 14.410  1.00 27.75 ? 9    ASP A OD1 1 
ATOM   62   O OD2 . ASP A 1 9   ? 12.246 -3.666 13.481  1.00 33.68 ? 9    ASP A OD2 1 
ATOM   63   N N   . ASP A 1 10  ? 16.732 -1.653 15.867  1.00 21.27 ? 10   ASP A N   1 
ATOM   64   C CA  . ASP A 1 10  ? 17.884 -1.826 16.739  1.00 21.60 ? 10   ASP A CA  1 
ATOM   65   C C   . ASP A 1 10  ? 18.143 -0.570 17.566  1.00 19.92 ? 10   ASP A C   1 
ATOM   66   O O   . ASP A 1 10  ? 18.533 -0.659 18.729  1.00 18.54 ? 10   ASP A O   1 
ATOM   67   C CB  . ASP A 1 10  ? 19.129 -2.200 15.926  1.00 25.15 ? 10   ASP A CB  1 
ATOM   68   C CG  . ASP A 1 10  ? 19.000 -3.566 15.259  1.00 28.76 ? 10   ASP A CG  1 
ATOM   69   O OD1 . ASP A 1 10  ? 18.417 -4.482 15.875  1.00 31.77 ? 10   ASP A OD1 1 
ATOM   70   O OD2 . ASP A 1 10  ? 19.487 -3.728 14.127  1.00 29.95 ? 10   ASP A OD2 1 
ATOM   71   N N   . VAL A 1 11  ? 17.910 0.598  16.971  1.00 19.02 ? 11   VAL A N   1 
ATOM   72   C CA  . VAL A 1 11  ? 18.113 1.864  17.675  1.00 18.55 ? 11   VAL A CA  1 
ATOM   73   C C   . VAL A 1 11  ? 17.117 2.007  18.824  1.00 18.28 ? 11   VAL A C   1 
ATOM   74   O O   . VAL A 1 11  ? 17.482 2.418  19.930  1.00 17.50 ? 11   VAL A O   1 
ATOM   75   C CB  . VAL A 1 11  ? 17.949 3.063  16.725  1.00 18.83 ? 11   VAL A CB  1 
ATOM   76   C CG1 . VAL A 1 11  ? 18.005 4.364  17.514  1.00 19.55 ? 11   VAL A CG1 1 
ATOM   77   C CG2 . VAL A 1 11  ? 19.045 3.041  15.675  1.00 19.35 ? 11   VAL A CG2 1 
ATOM   78   N N   . LEU A 1 12  ? 15.858 1.667  18.559  1.00 17.45 ? 12   LEU A N   1 
ATOM   79   C CA  . LEU A 1 12  ? 14.827 1.753  19.582  1.00 19.48 ? 12   LEU A CA  1 
ATOM   80   C C   . LEU A 1 12  ? 15.090 0.738  20.687  1.00 19.28 ? 12   LEU A C   1 
ATOM   81   O O   . LEU A 1 12  ? 14.778 0.984  21.848  1.00 19.80 ? 12   LEU A O   1 
ATOM   82   C CB  . LEU A 1 12  ? 13.443 1.526  18.969  1.00 19.04 ? 12   LEU A CB  1 
ATOM   83   C CG  . LEU A 1 12  ? 12.971 2.637  18.027  1.00 21.93 ? 12   LEU A CG  1 
ATOM   84   C CD1 . LEU A 1 12  ? 11.597 2.296  17.485  1.00 21.73 ? 12   LEU A CD1 1 
ATOM   85   C CD2 . LEU A 1 12  ? 12.935 3.966  18.769  1.00 21.79 ? 12   LEU A CD2 1 
ATOM   86   N N   . GLN A 1 13  ? 15.665 -0.405 20.326  1.00 20.68 ? 13   GLN A N   1 
ATOM   87   C CA  . GLN A 1 13  ? 15.963 -1.418 21.326  1.00 21.51 ? 13   GLN A CA  1 
ATOM   88   C C   . GLN A 1 13  ? 17.042 -0.923 22.286  1.00 20.94 ? 13   GLN A C   1 
ATOM   89   O O   . GLN A 1 13  ? 16.956 -1.150 23.492  1.00 19.81 ? 13   GLN A O   1 
ATOM   90   C CB  . GLN A 1 13  ? 16.414 -2.721 20.663  1.00 23.56 ? 13   GLN A CB  1 
ATOM   91   C CG  . GLN A 1 13  ? 16.854 -3.775 21.665  1.00 28.21 ? 13   GLN A CG  1 
ATOM   92   C CD  . GLN A 1 13  ? 16.979 -5.151 21.048  1.00 34.22 ? 13   GLN A CD  1 
ATOM   93   O OE1 . GLN A 1 13  ? 17.726 -5.349 20.087  1.00 39.47 ? 13   GLN A OE1 1 
ATOM   94   N NE2 . GLN A 1 13  ? 16.245 -6.113 21.597  1.00 36.88 ? 13   GLN A NE2 1 
ATOM   95   N N   . LEU A 1 14  ? 18.061 -0.250 21.756  1.00 20.43 ? 14   LEU A N   1 
ATOM   96   C CA  . LEU A 1 14  ? 19.118 0.274  22.616  1.00 19.68 ? 14   LEU A CA  1 
ATOM   97   C C   . LEU A 1 14  ? 18.561 1.390  23.485  1.00 17.56 ? 14   LEU A C   1 
ATOM   98   O O   . LEU A 1 14  ? 18.808 1.439  24.685  1.00 18.94 ? 14   LEU A O   1 
ATOM   99   C CB  . LEU A 1 14  ? 20.286 0.821  21.794  1.00 20.58 ? 14   LEU A CB  1 
ATOM   100  C CG  . LEU A 1 14  ? 21.439 1.360  22.660  1.00 22.39 ? 14   LEU A CG  1 
ATOM   101  C CD1 . LEU A 1 14  ? 21.941 0.257  23.588  1.00 21.55 ? 14   LEU A CD1 1 
ATOM   102  C CD2 . LEU A 1 14  ? 22.569 1.855  21.777  1.00 21.71 ? 14   LEU A CD2 1 
ATOM   103  N N   . LEU A 1 15  ? 17.809 2.296  22.873  1.00 16.34 ? 15   LEU A N   1 
ATOM   104  C CA  . LEU A 1 15  ? 17.223 3.400  23.619  1.00 16.37 ? 15   LEU A CA  1 
ATOM   105  C C   . LEU A 1 15  ? 16.365 2.870  24.764  1.00 15.78 ? 15   LEU A C   1 
ATOM   106  O O   . LEU A 1 15  ? 16.446 3.358  25.895  1.00 16.43 ? 15   LEU A O   1 
ATOM   107  C CB  . LEU A 1 15  ? 16.366 4.273  22.695  1.00 16.04 ? 15   LEU A CB  1 
ATOM   108  C CG  . LEU A 1 15  ? 15.657 5.460  23.350  1.00 18.52 ? 15   LEU A CG  1 
ATOM   109  C CD1 . LEU A 1 15  ? 16.669 6.337  24.073  1.00 17.06 ? 15   LEU A CD1 1 
ATOM   110  C CD2 . LEU A 1 15  ? 14.913 6.270  22.292  1.00 19.66 ? 15   LEU A CD2 1 
ATOM   111  N N   . ASP A 1 16  ? 15.539 1.872  24.465  1.00 15.59 ? 16   ASP A N   1 
ATOM   112  C CA  . ASP A 1 16  ? 14.674 1.288  25.484  1.00 17.68 ? 16   ASP A CA  1 
ATOM   113  C C   . ASP A 1 16  ? 15.506 0.674  26.602  1.00 18.44 ? 16   ASP A C   1 
ATOM   114  O O   . ASP A 1 16  ? 15.208 0.854  27.776  1.00 17.41 ? 16   ASP A O   1 
ATOM   115  C CB  . ASP A 1 16  ? 13.772 0.212  24.877  1.00 17.15 ? 16   ASP A CB  1 
ATOM   116  C CG  . ASP A 1 16  ? 12.776 -0.326 25.877  1.00 19.26 ? 16   ASP A CG  1 
ATOM   117  O OD1 . ASP A 1 16  ? 11.881 0.437  26.291  1.00 16.49 ? 16   ASP A OD1 1 
ATOM   118  O OD2 . ASP A 1 16  ? 12.898 -1.505 26.260  1.00 19.39 ? 16   ASP A OD2 1 
ATOM   119  N N   . ASN A 1 17  ? 16.551 -0.055 26.229  1.00 21.55 ? 17   ASN A N   1 
ATOM   120  C CA  . ASN A 1 17  ? 17.427 -0.687 27.209  1.00 24.82 ? 17   ASN A CA  1 
ATOM   121  C C   . ASN A 1 17  ? 18.173 0.333  28.075  1.00 24.18 ? 17   ASN A C   1 
ATOM   122  O O   . ASN A 1 17  ? 18.468 0.066  29.237  1.00 23.01 ? 17   ASN A O   1 
ATOM   123  C CB  . ASN A 1 17  ? 18.446 -1.585 26.498  1.00 29.08 ? 17   ASN A CB  1 
ATOM   124  C CG  . ASN A 1 17  ? 17.959 -3.019 26.337  1.00 36.29 ? 17   ASN A CG  1 
ATOM   125  O OD1 . ASN A 1 17  ? 18.382 -3.731 25.419  1.00 38.41 ? 17   ASN A OD1 1 
ATOM   126  N ND2 . ASN A 1 17  ? 17.079 -3.456 27.238  1.00 36.86 ? 17   ASN A ND2 1 
ATOM   127  N N   . ARG A 1 18  ? 18.458 1.503  27.512  1.00 22.14 ? 18   ARG A N   1 
ATOM   128  C CA  . ARG A 1 18  ? 19.204 2.538  28.225  1.00 21.11 ? 18   ARG A CA  1 
ATOM   129  C C   . ARG A 1 18  ? 18.347 3.695  28.725  1.00 20.28 ? 18   ARG A C   1 
ATOM   130  O O   . ARG A 1 18  ? 18.871 4.697  29.206  1.00 20.05 ? 18   ARG A O   1 
ATOM   131  C CB  . ARG A 1 18  ? 20.307 3.086  27.308  1.00 19.04 ? 18   ARG A CB  1 
ATOM   132  C CG  . ARG A 1 18  ? 21.289 2.029  26.802  1.00 20.86 ? 18   ARG A CG  1 
ATOM   133  C CD  . ARG A 1 18  ? 22.124 1.445  27.934  1.00 17.22 ? 18   ARG A CD  1 
ATOM   134  N NE  . ARG A 1 18  ? 22.896 2.489  28.598  1.00 21.54 ? 18   ARG A NE  1 
ATOM   135  C CZ  . ARG A 1 18  ? 23.779 2.280  29.570  1.00 22.00 ? 18   ARG A CZ  1 
ATOM   136  N NH1 . ARG A 1 18  ? 24.015 1.051  30.006  1.00 25.82 ? 18   ARG A NH1 1 
ATOM   137  N NH2 . ARG A 1 18  ? 24.432 3.306  30.105  1.00 23.48 ? 18   ARG A NH2 1 
ATOM   138  N N   . ILE A 1 19  ? 17.032 3.541  28.630  1.00 21.57 ? 19   ILE A N   1 
ATOM   139  C CA  . ILE A 1 19  ? 16.091 4.578  29.026  1.00 22.52 ? 19   ILE A CA  1 
ATOM   140  C C   . ILE A 1 19  ? 16.366 5.218  30.388  1.00 22.98 ? 19   ILE A C   1 
ATOM   141  O O   . ILE A 1 19  ? 16.158 6.416  30.569  1.00 22.41 ? 19   ILE A O   1 
ATOM   142  C CB  . ILE A 1 19  ? 14.643 4.028  28.998  1.00 24.32 ? 19   ILE A CB  1 
ATOM   143  C CG1 . ILE A 1 19  ? 13.653 5.190  29.013  1.00 28.10 ? 19   ILE A CG1 1 
ATOM   144  C CG2 . ILE A 1 19  ? 14.406 3.089  30.174  1.00 26.61 ? 19   ILE A CG2 1 
ATOM   145  C CD1 . ILE A 1 19  ? 13.695 6.035  27.743  1.00 26.20 ? 19   ILE A CD1 1 
ATOM   146  N N   . GLU A 1 20  ? 16.840 4.423  31.341  1.00 22.29 ? 20   GLU A N   1 
ATOM   147  C CA  . GLU A 1 20  ? 17.124 4.933  32.679  1.00 25.26 ? 20   GLU A CA  1 
ATOM   148  C C   . GLU A 1 20  ? 18.565 5.398  32.884  1.00 24.46 ? 20   GLU A C   1 
ATOM   149  O O   . GLU A 1 20  ? 18.870 6.040  33.890  1.00 25.38 ? 20   GLU A O   1 
ATOM   150  C CB  . GLU A 1 20  ? 16.796 3.861  33.720  1.00 27.69 ? 20   GLU A CB  1 
ATOM   151  C CG  . GLU A 1 20  ? 15.312 3.627  33.940  1.00 35.06 ? 20   GLU A CG  1 
ATOM   152  C CD  . GLU A 1 20  ? 15.042 2.413  34.807  1.00 38.57 ? 20   GLU A CD  1 
ATOM   153  O OE1 . GLU A 1 20  ? 15.602 2.333  35.922  1.00 40.85 ? 20   GLU A OE1 1 
ATOM   154  O OE2 . GLU A 1 20  ? 14.269 1.537  34.372  1.00 42.53 ? 20   GLU A OE2 1 
ATOM   155  N N   . ASP A 1 21  ? 19.442 5.090  31.934  1.00 23.19 ? 21   ASP A N   1 
ATOM   156  C CA  . ASP A 1 21  ? 20.853 5.453  32.051  1.00 23.84 ? 21   ASP A CA  1 
ATOM   157  C C   . ASP A 1 21  ? 21.337 6.538  31.090  1.00 23.64 ? 21   ASP A C   1 
ATOM   158  O O   . ASP A 1 21  ? 22.361 7.185  31.336  1.00 23.85 ? 21   ASP A O   1 
ATOM   159  C CB  . ASP A 1 21  ? 21.718 4.210  31.850  1.00 25.50 ? 21   ASP A CB  1 
ATOM   160  C CG  . ASP A 1 21  ? 21.310 3.066  32.752  1.00 28.21 ? 21   ASP A CG  1 
ATOM   161  O OD1 . ASP A 1 21  ? 21.288 3.264  33.984  1.00 30.65 ? 21   ASP A OD1 1 
ATOM   162  O OD2 . ASP A 1 21  ? 21.012 1.973  32.229  1.00 30.29 ? 21   ASP A OD2 1 
ATOM   163  N N   . ASN A 1 22  ? 20.614 6.730  29.995  1.00 19.75 ? 22   ASN A N   1 
ATOM   164  C CA  . ASN A 1 22  ? 21.016 7.725  29.007  1.00 19.93 ? 22   ASN A CA  1 
ATOM   165  C C   . ASN A 1 22  ? 19.827 8.488  28.462  1.00 17.65 ? 22   ASN A C   1 
ATOM   166  O O   . ASN A 1 22  ? 18.840 7.893  28.027  1.00 18.55 ? 22   ASN A O   1 
ATOM   167  C CB  . ASN A 1 22  ? 21.758 7.061  27.836  1.00 17.06 ? 22   ASN A CB  1 
ATOM   168  C CG  . ASN A 1 22  ? 23.050 6.378  28.263  1.00 18.60 ? 22   ASN A CG  1 
ATOM   169  O OD1 . ASN A 1 22  ? 23.065 5.185  28.575  1.00 17.12 ? 22   ASN A OD1 1 
ATOM   170  N ND2 . ASN A 1 22  ? 24.143 7.137  28.279  1.00 16.68 ? 22   ASN A ND2 1 
ATOM   171  N N   . TYR A 1 23  ? 19.934 9.809  28.483  1.00 15.93 ? 23   TYR A N   1 
ATOM   172  C CA  . TYR A 1 23  ? 18.875 10.662 27.978  1.00 17.91 ? 23   TYR A CA  1 
ATOM   173  C C   . TYR A 1 23  ? 18.721 10.478 26.462  1.00 18.54 ? 23   TYR A C   1 
ATOM   174  O O   . TYR A 1 23  ? 17.630 10.613 25.916  1.00 16.88 ? 23   TYR A O   1 
ATOM   175  C CB  . TYR A 1 23  ? 19.184 12.121 28.290  1.00 16.61 ? 23   TYR A CB  1 
ATOM   176  C CG  . TYR A 1 23  ? 18.032 13.023 27.949  1.00 19.53 ? 23   TYR A CG  1 
ATOM   177  C CD1 . TYR A 1 23  ? 16.885 13.040 28.746  1.00 13.88 ? 23   TYR A CD1 1 
ATOM   178  C CD2 . TYR A 1 23  ? 18.062 13.827 26.810  1.00 15.42 ? 23   TYR A CD2 1 
ATOM   179  C CE1 . TYR A 1 23  ? 15.806 13.829 28.418  1.00 16.07 ? 23   TYR A CE1 1 
ATOM   180  C CE2 . TYR A 1 23  ? 16.975 14.628 26.472  1.00 16.75 ? 23   TYR A CE2 1 
ATOM   181  C CZ  . TYR A 1 23  ? 15.850 14.619 27.286  1.00 15.14 ? 23   TYR A CZ  1 
ATOM   182  O OH  . TYR A 1 23  ? 14.768 15.396 26.973  1.00 16.34 ? 23   TYR A OH  1 
ATOM   183  N N   . ARG A 1 24  ? 19.822 10.179 25.782  1.00 19.06 ? 24   ARG A N   1 
ATOM   184  C CA  . ARG A 1 24  ? 19.760 9.968  24.342  1.00 21.20 ? 24   ARG A CA  1 
ATOM   185  C C   . ARG A 1 24  ? 20.767 8.933  23.863  1.00 21.58 ? 24   ARG A C   1 
ATOM   186  O O   . ARG A 1 24  ? 21.793 8.702  24.503  1.00 22.28 ? 24   ARG A O   1 
ATOM   187  C CB  . ARG A 1 24  ? 19.956 11.295 23.589  1.00 24.70 ? 24   ARG A CB  1 
ATOM   188  C CG  . ARG A 1 24  ? 21.053 12.185 24.143  1.00 24.19 ? 24   ARG A CG  1 
ATOM   189  C CD  . ARG A 1 24  ? 21.242 13.453 23.324  1.00 25.16 ? 24   ARG A CD  1 
ATOM   190  N NE  . ARG A 1 24  ? 20.014 14.225 23.175  1.00 26.35 ? 24   ARG A NE  1 
ATOM   191  C CZ  . ARG A 1 24  ? 19.946 15.549 23.278  1.00 21.67 ? 24   ARG A CZ  1 
ATOM   192  N NH1 . ARG A 1 24  ? 21.034 16.258 23.538  1.00 20.50 ? 24   ARG A NH1 1 
ATOM   193  N NH2 . ARG A 1 24  ? 18.789 16.168 23.106  1.00 22.56 ? 24   ARG A NH2 1 
ATOM   194  N N   . VAL A 1 25  ? 20.438 8.273  22.757  1.00 20.47 ? 25   VAL A N   1 
ATOM   195  C CA  . VAL A 1 25  ? 21.323 7.281  22.178  1.00 19.25 ? 25   VAL A CA  1 
ATOM   196  C C   . VAL A 1 25  ? 21.928 7.915  20.940  1.00 17.53 ? 25   VAL A C   1 
ATOM   197  O O   . VAL A 1 25  ? 21.270 8.694  20.242  1.00 17.24 ? 25   VAL A O   1 
ATOM   198  C CB  . VAL A 1 25  ? 20.568 5.991  21.747  1.00 21.59 ? 25   VAL A CB  1 
ATOM   199  C CG1 . VAL A 1 25  ? 19.876 5.361  22.946  1.00 26.23 ? 25   VAL A CG1 1 
ATOM   200  C CG2 . VAL A 1 25  ? 19.561 6.313  20.662  1.00 25.38 ? 25   VAL A CG2 1 
ATOM   201  N N   . CYS A 1 26  ? 23.186 7.600  20.680  1.00 17.08 ? 26   CYS A N   1 
ATOM   202  C CA  . CYS A 1 26  ? 23.859 8.123  19.508  1.00 17.11 ? 26   CYS A CA  1 
ATOM   203  C C   . CYS A 1 26  ? 24.088 6.999  18.516  1.00 16.98 ? 26   CYS A C   1 
ATOM   204  O O   . CYS A 1 26  ? 24.270 5.841  18.896  1.00 15.61 ? 26   CYS A O   1 
ATOM   205  C CB  . CYS A 1 26  ? 25.201 8.745  19.882  1.00 18.74 ? 26   CYS A CB  1 
ATOM   206  S SG  . CYS A 1 26  ? 25.058 10.234 20.896  1.00 20.22 ? 26   CYS A SG  1 
ATOM   207  N N   . VAL A 1 27  ? 24.065 7.356  17.241  1.00 14.34 ? 27   VAL A N   1 
ATOM   208  C CA  . VAL A 1 27  ? 24.304 6.408  16.180  1.00 15.37 ? 27   VAL A CA  1 
ATOM   209  C C   . VAL A 1 27  ? 25.410 6.993  15.313  1.00 14.15 ? 27   VAL A C   1 
ATOM   210  O O   . VAL A 1 27  ? 25.340 8.149  14.908  1.00 15.50 ? 27   VAL A O   1 
ATOM   211  C CB  . VAL A 1 27  ? 23.049 6.194  15.306  1.00 16.88 ? 27   VAL A CB  1 
ATOM   212  C CG1 . VAL A 1 27  ? 23.378 5.269  14.145  1.00 16.27 ? 27   VAL A CG1 1 
ATOM   213  C CG2 . VAL A 1 27  ? 21.912 5.619  16.150  1.00 19.57 ? 27   VAL A CG2 1 
ATOM   214  N N   . ILE A 1 28  ? 26.450 6.209  15.071  1.00 14.23 ? 28   ILE A N   1 
ATOM   215  C CA  . ILE A 1 28  ? 27.534 6.656  14.205  1.00 15.29 ? 28   ILE A CA  1 
ATOM   216  C C   . ILE A 1 28  ? 27.353 5.894  12.899  1.00 16.05 ? 28   ILE A C   1 
ATOM   217  O O   . ILE A 1 28  ? 27.153 4.679  12.914  1.00 17.27 ? 28   ILE A O   1 
ATOM   218  C CB  . ILE A 1 28  ? 28.919 6.329  14.798  1.00 13.57 ? 28   ILE A CB  1 
ATOM   219  C CG1 . ILE A 1 28  ? 29.276 7.359  15.872  1.00 13.94 ? 28   ILE A CG1 1 
ATOM   220  C CG2 . ILE A 1 28  ? 29.976 6.313  13.687  1.00 15.01 ? 28   ILE A CG2 1 
ATOM   221  C CD1 . ILE A 1 28  ? 30.620 7.098  16.539  1.00 16.90 ? 28   ILE A CD1 1 
ATOM   222  N N   . LEU A 1 29  ? 27.390 6.618  11.782  1.00 15.04 ? 29   LEU A N   1 
ATOM   223  C CA  . LEU A 1 29  ? 27.238 6.030  10.455  1.00 15.69 ? 29   LEU A CA  1 
ATOM   224  C C   . LEU A 1 29  ? 28.359 6.572  9.570   1.00 14.66 ? 29   LEU A C   1 
ATOM   225  O O   . LEU A 1 29  ? 28.380 7.757  9.232   1.00 16.14 ? 29   LEU A O   1 
ATOM   226  C CB  . LEU A 1 29  ? 25.881 6.407  9.852   1.00 17.33 ? 29   LEU A CB  1 
ATOM   227  C CG  . LEU A 1 29  ? 25.632 5.889  8.431   1.00 21.06 ? 29   LEU A CG  1 
ATOM   228  C CD1 . LEU A 1 29  ? 25.682 4.361  8.424   1.00 21.03 ? 29   LEU A CD1 1 
ATOM   229  C CD2 . LEU A 1 29  ? 24.284 6.385  7.927   1.00 22.62 ? 29   LEU A CD2 1 
ATOM   230  N N   . VAL A 1 30  ? 29.291 5.705  9.206   1.00 13.32 ? 30   VAL A N   1 
ATOM   231  C CA  . VAL A 1 30  ? 30.422 6.108  8.381   1.00 13.71 ? 30   VAL A CA  1 
ATOM   232  C C   . VAL A 1 30  ? 30.383 5.499  6.990   1.00 14.82 ? 30   VAL A C   1 
ATOM   233  O O   . VAL A 1 30  ? 30.011 4.337  6.811   1.00 15.45 ? 30   VAL A O   1 
ATOM   234  C CB  . VAL A 1 30  ? 31.766 5.715  9.048   1.00 15.18 ? 30   VAL A CB  1 
ATOM   235  C CG1 . VAL A 1 30  ? 32.922 5.911  8.071   1.00 12.89 ? 30   VAL A CG1 1 
ATOM   236  C CG2 . VAL A 1 30  ? 31.987 6.557  10.290  1.00 12.67 ? 30   VAL A CG2 1 
ATOM   237  N N   . GLY A 1 31  ? 30.783 6.304  6.010   1.00 16.91 ? 31   GLY A N   1 
ATOM   238  C CA  . GLY A 1 31  ? 30.829 5.855  4.632   1.00 16.27 ? 31   GLY A CA  1 
ATOM   239  C C   . GLY A 1 31  ? 31.756 6.755  3.837   1.00 16.39 ? 31   GLY A C   1 
ATOM   240  O O   . GLY A 1 31  ? 31.880 7.946  4.136   1.00 13.70 ? 31   GLY A O   1 
ATOM   241  N N   . SER A 1 32  ? 32.415 6.194  2.828   1.00 15.62 ? 32   SER A N   1 
ATOM   242  C CA  . SER A 1 32  ? 33.309 6.983  1.995   1.00 18.04 ? 32   SER A CA  1 
ATOM   243  C C   . SER A 1 32  ? 32.415 7.743  1.017   1.00 18.65 ? 32   SER A C   1 
ATOM   244  O O   . SER A 1 32  ? 31.203 7.517  0.984   1.00 18.67 ? 32   SER A O   1 
ATOM   245  C CB  . SER A 1 32  ? 34.290 6.068  1.251   1.00 18.07 ? 32   SER A CB  1 
ATOM   246  O OG  . SER A 1 32  ? 33.613 5.124  0.446   1.00 21.62 ? 32   SER A OG  1 
ATOM   247  N N   . PRO A 1 33  ? 32.991 8.662  0.224   1.00 18.64 ? 33   PRO A N   1 
ATOM   248  C CA  . PRO A 1 33  ? 32.189 9.428  -0.733  1.00 19.87 ? 33   PRO A CA  1 
ATOM   249  C C   . PRO A 1 33  ? 31.344 8.543  -1.654  1.00 21.79 ? 33   PRO A C   1 
ATOM   250  O O   . PRO A 1 33  ? 31.833 7.562  -2.213  1.00 22.60 ? 33   PRO A O   1 
ATOM   251  C CB  . PRO A 1 33  ? 33.242 10.230 -1.497  1.00 19.94 ? 33   PRO A CB  1 
ATOM   252  C CG  . PRO A 1 33  ? 34.297 10.463 -0.455  1.00 17.31 ? 33   PRO A CG  1 
ATOM   253  C CD  . PRO A 1 33  ? 34.401 9.100  0.191   1.00 18.51 ? 33   PRO A CD  1 
ATOM   254  N N   . GLY A 1 34  ? 30.067 8.892  -1.790  1.00 22.50 ? 34   GLY A N   1 
ATOM   255  C CA  . GLY A 1 34  ? 29.173 8.133  -2.644  1.00 21.59 ? 34   GLY A CA  1 
ATOM   256  C C   . GLY A 1 34  ? 28.627 6.853  -2.040  1.00 19.97 ? 34   GLY A C   1 
ATOM   257  O O   . GLY A 1 34  ? 27.990 6.071  -2.731  1.00 18.96 ? 34   GLY A O   1 
ATOM   258  N N   . SER A 1 35  ? 28.869 6.640  -0.751  1.00 18.91 ? 35   SER A N   1 
ATOM   259  C CA  . SER A 1 35  ? 28.397 5.438  -0.070  1.00 18.71 ? 35   SER A CA  1 
ATOM   260  C C   . SER A 1 35  ? 26.914 5.504  0.260   1.00 18.42 ? 35   SER A C   1 
ATOM   261  O O   . SER A 1 35  ? 26.293 4.482  0.537   1.00 19.98 ? 35   SER A O   1 
ATOM   262  C CB  . SER A 1 35  ? 29.175 5.236  1.229   1.00 20.23 ? 35   SER A CB  1 
ATOM   263  O OG  . SER A 1 35  ? 28.959 6.333  2.103   1.00 18.62 ? 35   SER A OG  1 
ATOM   264  N N   . GLY A 1 36  ? 26.346 6.706  0.243   1.00 19.97 ? 36   GLY A N   1 
ATOM   265  C CA  . GLY A 1 36  ? 24.934 6.852  0.555   1.00 21.57 ? 36   GLY A CA  1 
ATOM   266  C C   . GLY A 1 36  ? 24.624 6.987  2.044   1.00 22.20 ? 36   GLY A C   1 
ATOM   267  O O   . GLY A 1 36  ? 23.503 6.713  2.471   1.00 23.00 ? 36   GLY A O   1 
ATOM   268  N N   . LYS A 1 37  ? 25.605 7.405  2.840   1.00 22.08 ? 37   LYS A N   1 
ATOM   269  C CA  . LYS A 1 37  ? 25.396 7.574  4.279   1.00 22.08 ? 37   LYS A CA  1 
ATOM   270  C C   . LYS A 1 37  ? 24.376 8.678  4.557   1.00 20.82 ? 37   LYS A C   1 
ATOM   271  O O   . LYS A 1 37  ? 23.652 8.647  5.552   1.00 20.50 ? 37   LYS A O   1 
ATOM   272  C CB  . LYS A 1 37  ? 26.721 7.908  4.967   1.00 21.74 ? 37   LYS A CB  1 
ATOM   273  C CG  . LYS A 1 37  ? 27.467 9.069  4.339   1.00 20.55 ? 37   LYS A CG  1 
ATOM   274  C CD  . LYS A 1 37  ? 28.786 9.322  5.042   1.00 20.90 ? 37   LYS A CD  1 
ATOM   275  C CE  . LYS A 1 37  ? 29.577 10.418 4.342   1.00 20.33 ? 37   LYS A CE  1 
ATOM   276  N NZ  . LYS A 1 37  ? 30.007 9.991  2.978   1.00 20.59 ? 37   LYS A NZ  1 
ATOM   277  N N   . SER A 1 38  ? 24.318 9.648  3.660   1.00 22.34 ? 38   SER A N   1 
ATOM   278  C CA  . SER A 1 38  ? 23.395 10.764 3.796   1.00 25.21 ? 38   SER A CA  1 
ATOM   279  C C   . SER A 1 38  ? 21.938 10.293 3.719   1.00 25.32 ? 38   SER A C   1 
ATOM   280  O O   . SER A 1 38  ? 21.117 10.650 4.567   1.00 25.84 ? 38   SER A O   1 
ATOM   281  C CB  . SER A 1 38  ? 23.684 11.793 2.697   1.00 29.01 ? 38   SER A CB  1 
ATOM   282  O OG  . SER A 1 38  ? 22.962 12.992 2.907   1.00 35.07 ? 38   SER A OG  1 
ATOM   283  N N   . THR A 1 39  ? 21.625 9.478  2.714   1.00 25.21 ? 39   THR A N   1 
ATOM   284  C CA  . THR A 1 39  ? 20.267 8.973  2.530   1.00 26.66 ? 39   THR A CA  1 
ATOM   285  C C   . THR A 1 39  ? 19.875 7.922  3.567   1.00 25.12 ? 39   THR A C   1 
ATOM   286  O O   . THR A 1 39  ? 18.722 7.856  3.985   1.00 25.83 ? 39   THR A O   1 
ATOM   287  C CB  . THR A 1 39  ? 20.070 8.375  1.107   1.00 28.17 ? 39   THR A CB  1 
ATOM   288  O OG1 . THR A 1 39  ? 20.914 7.232  0.934   1.00 31.97 ? 39   THR A OG1 1 
ATOM   289  C CG2 . THR A 1 39  ? 20.423 9.404  0.049   1.00 29.49 ? 39   THR A CG2 1 
ATOM   290  N N   . ILE A 1 40  ? 20.826 7.091  3.974   1.00 23.16 ? 40   ILE A N   1 
ATOM   291  C CA  . ILE A 1 40  ? 20.535 6.077  4.974   1.00 21.97 ? 40   ILE A CA  1 
ATOM   292  C C   . ILE A 1 40  ? 20.187 6.781  6.285   1.00 22.37 ? 40   ILE A C   1 
ATOM   293  O O   . ILE A 1 40  ? 19.205 6.437  6.946   1.00 20.99 ? 40   ILE A O   1 
ATOM   294  C CB  . ILE A 1 40  ? 21.749 5.144  5.192   1.00 23.10 ? 40   ILE A CB  1 
ATOM   295  C CG1 . ILE A 1 40  ? 22.022 4.344  3.912   1.00 24.13 ? 40   ILE A CG1 1 
ATOM   296  C CG2 . ILE A 1 40  ? 21.479 4.185  6.349   1.00 22.58 ? 40   ILE A CG2 1 
ATOM   297  C CD1 . ILE A 1 40  ? 23.245 3.445  3.997   1.00 23.01 ? 40   ILE A CD1 1 
ATOM   298  N N   . ALA A 1 41  ? 20.987 7.782  6.642   1.00 19.98 ? 41   ALA A N   1 
ATOM   299  C CA  . ALA A 1 41  ? 20.771 8.536  7.873   1.00 21.06 ? 41   ALA A CA  1 
ATOM   300  C C   . ALA A 1 41  ? 19.419 9.245  7.881   1.00 22.27 ? 41   ALA A C   1 
ATOM   301  O O   . ALA A 1 41  ? 18.692 9.208  8.875   1.00 22.40 ? 41   ALA A O   1 
ATOM   302  C CB  . ALA A 1 41  ? 21.898 9.556  8.059   1.00 17.59 ? 41   ALA A CB  1 
ATOM   303  N N   . GLU A 1 42  ? 19.080 9.887  6.768   1.00 23.90 ? 42   GLU A N   1 
ATOM   304  C CA  . GLU A 1 42  ? 17.816 10.608 6.671   1.00 24.36 ? 42   GLU A CA  1 
ATOM   305  C C   . GLU A 1 42  ? 16.639 9.653  6.728   1.00 23.63 ? 42   GLU A C   1 
ATOM   306  O O   . GLU A 1 42  ? 15.635 9.936  7.378   1.00 21.18 ? 42   GLU A O   1 
ATOM   307  C CB  . GLU A 1 42  ? 17.774 11.430 5.378   1.00 28.59 ? 42   GLU A CB  1 
ATOM   308  C CG  . GLU A 1 42  ? 18.896 12.456 5.288   1.00 35.56 ? 42   GLU A CG  1 
ATOM   309  C CD  . GLU A 1 42  ? 18.804 13.339 4.059   1.00 40.73 ? 42   GLU A CD  1 
ATOM   310  O OE1 . GLU A 1 42  ? 18.796 12.801 2.931   1.00 44.65 ? 42   GLU A OE1 1 
ATOM   311  O OE2 . GLU A 1 42  ? 18.746 14.577 4.223   1.00 44.49 ? 42   GLU A OE2 1 
ATOM   312  N N   . GLU A 1 43  ? 16.773 8.516  6.054   1.00 24.03 ? 43   GLU A N   1 
ATOM   313  C CA  . GLU A 1 43  ? 15.722 7.506  6.022   1.00 24.17 ? 43   GLU A CA  1 
ATOM   314  C C   . GLU A 1 43  ? 15.495 6.940  7.425   1.00 23.17 ? 43   GLU A C   1 
ATOM   315  O O   . GLU A 1 43  ? 14.357 6.832  7.895   1.00 20.45 ? 43   GLU A O   1 
ATOM   316  C CB  . GLU A 1 43  ? 16.116 6.391  5.051   1.00 26.67 ? 43   GLU A CB  1 
ATOM   317  C CG  . GLU A 1 43  ? 15.024 5.392  4.749   1.00 32.59 ? 43   GLU A CG  1 
ATOM   318  C CD  . GLU A 1 43  ? 15.375 4.499  3.572   1.00 37.76 ? 43   GLU A CD  1 
ATOM   319  O OE1 . GLU A 1 43  ? 15.680 5.038  2.485   1.00 41.48 ? 43   GLU A OE1 1 
ATOM   320  O OE2 . GLU A 1 43  ? 15.343 3.260  3.730   1.00 40.84 ? 43   GLU A OE2 1 
ATOM   321  N N   . LEU A 1 44  ? 16.584 6.586  8.095   1.00 20.53 ? 44   LEU A N   1 
ATOM   322  C CA  . LEU A 1 44  ? 16.506 6.047  9.448   1.00 19.58 ? 44   LEU A CA  1 
ATOM   323  C C   . LEU A 1 44  ? 15.817 7.033  10.395  1.00 19.61 ? 44   LEU A C   1 
ATOM   324  O O   . LEU A 1 44  ? 14.911 6.667  11.143  1.00 18.83 ? 44   LEU A O   1 
ATOM   325  C CB  . LEU A 1 44  ? 17.918 5.737  9.959   1.00 19.34 ? 44   LEU A CB  1 
ATOM   326  C CG  . LEU A 1 44  ? 18.087 5.336  11.430  1.00 18.80 ? 44   LEU A CG  1 
ATOM   327  C CD1 . LEU A 1 44  ? 17.248 4.111  11.755  1.00 19.29 ? 44   LEU A CD1 1 
ATOM   328  C CD2 . LEU A 1 44  ? 19.559 5.061  11.697  1.00 19.18 ? 44   LEU A CD2 1 
HETATM 329  N N   . CME A 1 45  ? 16.227 8.277  10.197  1.00 21.17 ? 45   CME A N   1 
HETATM 330  C CA  . CME A 1 45  ? 15.710 9.350  11.042  1.00 22.60 ? 45   CME A CA  1 
HETATM 331  C CB  . CME A 1 45  ? 16.478 10.629 10.733  1.00 26.47 ? 45   CME A CB  1 
HETATM 332  S SG  . CME A 1 45  ? 15.880 12.103 11.604  1.00 27.64 ? 45   CME A SG  1 
HETATM 333  S SD  . CME A 1 45  ? 14.641 12.986 10.255  1.00 40.89 ? 45   CME A SD  1 
HETATM 334  C CE  . CME A 1 45  ? 15.137 14.738 10.296  1.00 42.58 ? 45   CME A CE  1 
HETATM 335  C CZ  . CME A 1 45  ? 16.469 14.971 9.616   1.00 45.56 ? 45   CME A CZ  1 
HETATM 336  O OH  . CME A 1 45  ? 16.752 16.204 9.441   1.00 49.77 ? 45   CME A OH  1 
HETATM 337  C C   . CME A 1 45  ? 14.211 9.610  10.883  1.00 24.58 ? 45   CME A C   1 
HETATM 338  O O   . CME A 1 45  ? 13.414 9.447  11.809  1.00 22.88 ? 45   CME A O   1 
ATOM   339  N N   . GLN A 1 46  ? 14.041 9.307  9.461   1.00 32.96 ? 46   GLN A N   1 
ATOM   340  C CA  . GLN A 1 46  ? 12.615 9.538  9.305   1.00 30.18 ? 46   GLN A CA  1 
ATOM   341  C C   . GLN A 1 46  ? 11.801 8.387  9.879   1.00 27.07 ? 46   GLN A C   1 
ATOM   342  O O   . GLN A 1 46  ? 10.644 8.563  10.264  1.00 24.93 ? 46   GLN A O   1 
ATOM   343  C CB  . GLN A 1 46  ? 12.293 9.728  7.824   1.00 33.13 ? 46   GLN A CB  1 
ATOM   344  C CG  . GLN A 1 46  ? 12.739 11.072 7.297   1.00 38.36 ? 46   GLN A CG  1 
ATOM   345  C CD  . GLN A 1 46  ? 11.926 12.208 7.883   1.00 41.03 ? 46   GLN A CD  1 
ATOM   346  O OE1 . GLN A 1 46  ? 12.312 13.374 7.798   1.00 43.44 ? 46   GLN A OE1 1 
ATOM   347  N NE2 . GLN A 1 46  ? 10.782 11.872 8.475   1.00 43.87 ? 46   GLN A NE2 1 
ATOM   348  N N   . ILE A 1 47  ? 11.937 7.304  9.438   1.00 25.03 ? 47   ILE A N   1 
ATOM   349  C CA  . ILE A 1 47  ? 11.258 6.138  9.985   1.00 24.19 ? 47   ILE A CA  1 
ATOM   350  C C   . ILE A 1 47  ? 10.979 6.229  11.483  1.00 22.85 ? 47   ILE A C   1 
ATOM   351  O O   . ILE A 1 47  ? 9.853  6.004  11.927  1.00 20.38 ? 47   ILE A O   1 
ATOM   352  C CB  . ILE A 1 47  ? 12.066 4.861  9.702   1.00 23.46 ? 47   ILE A CB  1 
ATOM   353  C CG1 . ILE A 1 47  ? 12.126 4.628  8.190   1.00 25.60 ? 47   ILE A CG1 1 
ATOM   354  C CG2 . ILE A 1 47  ? 11.439 3.667  10.418  1.00 25.94 ? 47   ILE A CG2 1 
ATOM   355  C CD1 . ILE A 1 47  ? 12.889 3.384  7.782   1.00 24.98 ? 47   ILE A CD1 1 
ATOM   356  N N   . ILE A 1 48  ? 12.003 6.555  12.263  1.00 22.27 ? 48   ILE A N   1 
ATOM   357  C CA  . ILE A 1 48  ? 11.833 6.660  13.707  1.00 20.44 ? 48   ILE A CA  1 
ATOM   358  C C   . ILE A 1 48  ? 10.824 7.740  14.080  1.00 21.22 ? 48   ILE A C   1 
ATOM   359  O O   . ILE A 1 48  ? 9.934  7.504  14.900  1.00 18.61 ? 48   ILE A O   1 
ATOM   360  C CB  . ILE A 1 48  ? 13.174 6.944  14.409  1.00 19.70 ? 48   ILE A CB  1 
ATOM   361  C CG1 . ILE A 1 48  ? 14.076 5.709  14.292  1.00 20.29 ? 48   ILE A CG1 1 
ATOM   362  C CG2 . ILE A 1 48  ? 12.929 7.321  15.881  1.00 16.36 ? 48   ILE A CG2 1 
ATOM   363  C CD1 . ILE A 1 48  ? 15.540 5.954  14.654  1.00 20.27 ? 48   ILE A CD1 1 
ATOM   364  N N   . ASN A 1 49  ? 10.955 8.921  13.485  1.00 20.28 ? 49   ASN A N   1 
ATOM   365  C CA  . ASN A 1 49  ? 10.021 9.996  13.792  1.00 21.80 ? 49   ASN A CA  1 
ATOM   366  C C   . ASN A 1 49  ? 8.589  9.632  13.387  1.00 22.02 ? 49   ASN A C   1 
ATOM   367  O O   . ASN A 1 49  ? 7.643  9.932  14.113  1.00 21.23 ? 49   ASN A O   1 
ATOM   368  C CB  . ASN A 1 49  ? 10.452 11.302 13.120  1.00 19.06 ? 49   ASN A CB  1 
ATOM   369  C CG  . ASN A 1 49  ? 11.682 11.917 13.771  1.00 20.49 ? 49   ASN A CG  1 
ATOM   370  O OD1 . ASN A 1 49  ? 11.847 11.863 14.991  1.00 20.96 ? 49   ASN A OD1 1 
ATOM   371  N ND2 . ASN A 1 49  ? 12.542 12.521 12.959  1.00 20.81 ? 49   ASN A ND2 1 
ATOM   372  N N   . GLU A 1 50  ? 8.428  8.983  12.236  1.00 22.23 ? 50   GLU A N   1 
ATOM   373  C CA  . GLU A 1 50  ? 7.099  8.570  11.776  1.00 23.23 ? 50   GLU A CA  1 
ATOM   374  C C   . GLU A 1 50  ? 6.460  7.633  12.794  1.00 22.64 ? 50   GLU A C   1 
ATOM   375  O O   . GLU A 1 50  ? 5.274  7.750  13.111  1.00 23.35 ? 50   GLU A O   1 
ATOM   376  C CB  . GLU A 1 50  ? 7.193  7.845  10.430  1.00 24.50 ? 50   GLU A CB  1 
ATOM   377  C CG  . GLU A 1 50  ? 7.226  8.753  9.217   1.00 33.22 ? 50   GLU A CG  1 
ATOM   378  C CD  . GLU A 1 50  ? 7.555  7.995  7.936   1.00 37.95 ? 50   GLU A CD  1 
ATOM   379  O OE1 . GLU A 1 50  ? 7.057  6.858  7.773   1.00 37.20 ? 50   GLU A OE1 1 
ATOM   380  O OE2 . GLU A 1 50  ? 8.305  8.541  7.094   1.00 40.31 ? 50   GLU A OE2 1 
ATOM   381  N N   . LYS A 1 51  ? 7.250  6.683  13.284  1.00 21.70 ? 51   LYS A N   1 
ATOM   382  C CA  . LYS A 1 51  ? 6.777  5.732  14.273  1.00 19.43 ? 51   LYS A CA  1 
ATOM   383  C C   . LYS A 1 51  ? 6.290  6.467  15.517  1.00 20.37 ? 51   LYS A C   1 
ATOM   384  O O   . LYS A 1 51  ? 5.259  6.121  16.100  1.00 18.20 ? 51   LYS A O   1 
ATOM   385  C CB  . LYS A 1 51  ? 7.904  4.779  14.666  1.00 20.84 ? 51   LYS A CB  1 
ATOM   386  C CG  . LYS A 1 51  ? 8.139  3.629  13.706  1.00 24.17 ? 51   LYS A CG  1 
ATOM   387  C CD  . LYS A 1 51  ? 9.351  2.823  14.153  1.00 28.20 ? 51   LYS A CD  1 
ATOM   388  C CE  . LYS A 1 51  ? 9.410  1.457  13.487  1.00 29.98 ? 51   LYS A CE  1 
ATOM   389  N NZ  . LYS A 1 51  ? 8.282  0.579  13.934  1.00 32.17 ? 51   LYS A NZ  1 
ATOM   390  N N   . TYR A 1 52  ? 7.037  7.485  15.926  1.00 17.99 ? 52   TYR A N   1 
ATOM   391  C CA  . TYR A 1 52  ? 6.662  8.237  17.112  1.00 20.24 ? 52   TYR A CA  1 
ATOM   392  C C   . TYR A 1 52  ? 5.365  9.013  16.899  1.00 20.49 ? 52   TYR A C   1 
ATOM   393  O O   . TYR A 1 52  ? 4.505  9.049  17.777  1.00 20.46 ? 52   TYR A O   1 
ATOM   394  C CB  . TYR A 1 52  ? 7.787  9.195  17.519  1.00 19.56 ? 52   TYR A CB  1 
ATOM   395  C CG  . TYR A 1 52  ? 7.559  9.846  18.867  1.00 19.45 ? 52   TYR A CG  1 
ATOM   396  C CD1 . TYR A 1 52  ? 7.395  9.073  20.021  1.00 19.20 ? 52   TYR A CD1 1 
ATOM   397  C CD2 . TYR A 1 52  ? 7.479  11.231 18.987  1.00 19.72 ? 52   TYR A CD2 1 
ATOM   398  C CE1 . TYR A 1 52  ? 7.151  9.668  21.261  1.00 14.92 ? 52   TYR A CE1 1 
ATOM   399  C CE2 . TYR A 1 52  ? 7.237  11.832 20.221  1.00 19.30 ? 52   TYR A CE2 1 
ATOM   400  C CZ  . TYR A 1 52  ? 7.074  11.046 21.347  1.00 17.41 ? 52   TYR A CZ  1 
ATOM   401  O OH  . TYR A 1 52  ? 6.827  11.645 22.556  1.00 20.71 ? 52   TYR A OH  1 
ATOM   402  N N   . HIS A 1 53  ? 5.224  9.627  15.730  1.00 20.21 ? 53   HIS A N   1 
ATOM   403  C CA  . HIS A 1 53  ? 4.021  10.394 15.424  1.00 21.18 ? 53   HIS A CA  1 
ATOM   404  C C   . HIS A 1 53  ? 2.801  9.474  15.426  1.00 21.43 ? 53   HIS A C   1 
ATOM   405  O O   . HIS A 1 53  ? 1.734  9.843  15.915  1.00 22.55 ? 53   HIS A O   1 
ATOM   406  C CB  . HIS A 1 53  ? 4.184  11.084 14.069  1.00 19.26 ? 53   HIS A CB  1 
ATOM   407  C CG  . HIS A 1 53  ? 5.285  12.100 14.047  1.00 21.41 ? 53   HIS A CG  1 
ATOM   408  N ND1 . HIS A 1 53  ? 5.959  12.446 12.896  1.00 21.78 ? 53   HIS A ND1 1 
ATOM   409  C CD2 . HIS A 1 53  ? 5.841  12.834 15.041  1.00 19.13 ? 53   HIS A CD2 1 
ATOM   410  C CE1 . HIS A 1 53  ? 6.885  13.344 13.181  1.00 20.79 ? 53   HIS A CE1 1 
ATOM   411  N NE2 . HIS A 1 53  ? 6.834  13.597 14.477  1.00 20.93 ? 53   HIS A NE2 1 
ATOM   412  N N   . THR A 1 54  ? 2.973  8.271  14.892  1.00 22.47 ? 54   THR A N   1 
ATOM   413  C CA  . THR A 1 54  ? 1.898  7.292  14.847  1.00 23.08 ? 54   THR A CA  1 
ATOM   414  C C   . THR A 1 54  ? 1.511  6.905  16.276  1.00 23.32 ? 54   THR A C   1 
ATOM   415  O O   . THR A 1 54  ? 0.340  6.709  16.584  1.00 23.72 ? 54   THR A O   1 
ATOM   416  C CB  . THR A 1 54  ? 2.345  6.047  14.054  1.00 23.45 ? 54   THR A CB  1 
ATOM   417  O OG1 . THR A 1 54  ? 2.676  6.443  12.719  1.00 22.69 ? 54   THR A OG1 1 
ATOM   418  C CG2 . THR A 1 54  ? 1.232  4.994  14.002  1.00 24.95 ? 54   THR A CG2 1 
ATOM   419  N N   . PHE A 1 55  ? 2.506  6.803  17.151  1.00 24.05 ? 55   PHE A N   1 
ATOM   420  C CA  . PHE A 1 55  ? 2.257  6.468  18.545  1.00 22.71 ? 55   PHE A CA  1 
ATOM   421  C C   . PHE A 1 55  ? 1.497  7.610  19.217  1.00 22.89 ? 55   PHE A C   1 
ATOM   422  O O   . PHE A 1 55  ? 0.556  7.378  19.974  1.00 22.44 ? 55   PHE A O   1 
ATOM   423  C CB  . PHE A 1 55  ? 3.579  6.236  19.281  1.00 21.89 ? 55   PHE A CB  1 
ATOM   424  C CG  . PHE A 1 55  ? 3.453  6.281  20.779  1.00 21.22 ? 55   PHE A CG  1 
ATOM   425  C CD1 . PHE A 1 55  ? 2.945  5.196  21.484  1.00 19.45 ? 55   PHE A CD1 1 
ATOM   426  C CD2 . PHE A 1 55  ? 3.829  7.421  21.481  1.00 20.35 ? 55   PHE A CD2 1 
ATOM   427  C CE1 . PHE A 1 55  ? 2.813  5.244  22.872  1.00 21.58 ? 55   PHE A CE1 1 
ATOM   428  C CE2 . PHE A 1 55  ? 3.700  7.480  22.866  1.00 20.37 ? 55   PHE A CE2 1 
ATOM   429  C CZ  . PHE A 1 55  ? 3.191  6.389  23.562  1.00 20.77 ? 55   PHE A CZ  1 
ATOM   430  N N   . LEU A 1 56  ? 1.922  8.841  18.946  1.00 23.31 ? 56   LEU A N   1 
ATOM   431  C CA  . LEU A 1 56  ? 1.278  10.022 19.519  1.00 24.09 ? 56   LEU A CA  1 
ATOM   432  C C   . LEU A 1 56  ? -0.183 10.139 19.106  1.00 24.02 ? 56   LEU A C   1 
ATOM   433  O O   . LEU A 1 56  ? -1.007 10.644 19.867  1.00 24.08 ? 56   LEU A O   1 
ATOM   434  C CB  . LEU A 1 56  ? 2.007  11.293 19.092  1.00 23.21 ? 56   LEU A CB  1 
ATOM   435  C CG  . LEU A 1 56  ? 3.354  11.554 19.754  1.00 23.54 ? 56   LEU A CG  1 
ATOM   436  C CD1 . LEU A 1 56  ? 3.944  12.840 19.195  1.00 20.42 ? 56   LEU A CD1 1 
ATOM   437  C CD2 . LEU A 1 56  ? 3.172  11.645 21.273  1.00 23.81 ? 56   LEU A CD2 1 
ATOM   438  N N   . SER A 1 57  ? -0.490 9.687  17.894  1.00 21.99 ? 57   SER A N   1 
ATOM   439  C CA  . SER A 1 57  ? -1.853 9.737  17.379  1.00 24.53 ? 57   SER A CA  1 
ATOM   440  C C   . SER A 1 57  ? -2.864 9.167  18.377  1.00 23.60 ? 57   SER A C   1 
ATOM   441  O O   . SER A 1 57  ? -3.924 9.753  18.597  1.00 24.26 ? 57   SER A O   1 
ATOM   442  C CB  . SER A 1 57  ? -1.944 8.959  16.060  1.00 25.38 ? 57   SER A CB  1 
ATOM   443  O OG  . SER A 1 57  ? -3.294 8.819  15.653  1.00 29.75 ? 57   SER A OG  1 
ATOM   444  N N   . GLU A 1 58  ? -2.525 8.035  18.990  1.00 23.58 ? 58   GLU A N   1 
ATOM   445  C CA  . GLU A 1 58  ? -3.411 7.386  19.947  1.00 24.81 ? 58   GLU A CA  1 
ATOM   446  C C   . GLU A 1 58  ? -3.058 7.595  21.417  1.00 24.19 ? 58   GLU A C   1 
ATOM   447  O O   . GLU A 1 58  ? -3.733 7.075  22.308  1.00 23.68 ? 58   GLU A O   1 
ATOM   448  C CB  . GLU A 1 58  ? -3.510 5.894  19.613  1.00 28.87 ? 58   GLU A CB  1 
ATOM   449  C CG  . GLU A 1 58  ? -4.341 5.658  18.359  1.00 34.18 ? 58   GLU A CG  1 
ATOM   450  C CD  . GLU A 1 58  ? -4.364 4.210  17.906  1.00 38.43 ? 58   GLU A CD  1 
ATOM   451  O OE1 . GLU A 1 58  ? -4.458 3.312  18.769  1.00 41.11 ? 58   GLU A OE1 1 
ATOM   452  O OE2 . GLU A 1 58  ? -4.309 3.977  16.680  1.00 38.30 ? 58   GLU A OE2 1 
ATOM   453  N N   . HIS A 1 59  ? -1.994 8.354  21.661  1.00 22.91 ? 59   HIS A N   1 
ATOM   454  C CA  . HIS A 1 59  ? -1.554 8.695  23.012  1.00 21.63 ? 59   HIS A CA  1 
ATOM   455  C C   . HIS A 1 59  ? -1.302 10.193 22.931  1.00 22.50 ? 59   HIS A C   1 
ATOM   456  O O   . HIS A 1 59  ? -0.203 10.655 23.217  1.00 22.28 ? 59   HIS A O   1 
ATOM   457  C CB  . HIS A 1 59  ? -0.253 7.970  23.367  1.00 21.09 ? 59   HIS A CB  1 
ATOM   458  C CG  . HIS A 1 59  ? -0.349 6.483  23.279  1.00 19.75 ? 59   HIS A CG  1 
ATOM   459  N ND1 . HIS A 1 59  ? -0.340 5.806  22.078  1.00 21.64 ? 59   HIS A ND1 1 
ATOM   460  C CD2 . HIS A 1 59  ? -0.510 5.543  24.240  1.00 20.33 ? 59   HIS A CD2 1 
ATOM   461  C CE1 . HIS A 1 59  ? -0.492 4.514  22.302  1.00 21.05 ? 59   HIS A CE1 1 
ATOM   462  N NE2 . HIS A 1 59  ? -0.598 4.327  23.606  1.00 21.66 ? 59   HIS A NE2 1 
ATOM   463  N N   . PRO A 1 60  ? -2.342 10.968 22.549  1.00 22.91 ? 60   PRO A N   1 
ATOM   464  C CA  . PRO A 1 60  ? -2.401 12.425 22.360  1.00 23.54 ? 60   PRO A CA  1 
ATOM   465  C C   . PRO A 1 60  ? -1.764 13.345 23.391  1.00 24.12 ? 60   PRO A C   1 
ATOM   466  O O   . PRO A 1 60  ? -1.156 14.352 23.031  1.00 25.64 ? 60   PRO A O   1 
ATOM   467  C CB  . PRO A 1 60  ? -3.902 12.705 22.239  1.00 21.93 ? 60   PRO A CB  1 
ATOM   468  C CG  . PRO A 1 60  ? -4.472 11.420 21.771  1.00 21.78 ? 60   PRO A CG  1 
ATOM   469  C CD  . PRO A 1 60  ? -3.712 10.420 22.582  1.00 22.72 ? 60   PRO A CD  1 
ATOM   470  N N   . ASN A 1 61  ? -1.910 13.015 24.667  1.00 25.20 ? 61   ASN A N   1 
ATOM   471  C CA  . ASN A 1 61  ? -1.382 13.869 25.721  1.00 24.58 ? 61   ASN A CA  1 
ATOM   472  C C   . ASN A 1 61  ? -0.410 13.168 26.648  1.00 23.82 ? 61   ASN A C   1 
ATOM   473  O O   . ASN A 1 61  ? -0.330 13.484 27.833  1.00 22.45 ? 61   ASN A O   1 
ATOM   474  C CB  . ASN A 1 61  ? -2.556 14.428 26.517  1.00 26.35 ? 61   ASN A CB  1 
ATOM   475  C CG  . ASN A 1 61  ? -3.553 15.137 25.629  1.00 26.81 ? 61   ASN A CG  1 
ATOM   476  O OD1 . ASN A 1 61  ? -3.237 16.165 25.036  1.00 26.67 ? 61   ASN A OD1 1 
ATOM   477  N ND2 . ASN A 1 61  ? -4.757 14.581 25.514  1.00 25.05 ? 61   ASN A ND2 1 
ATOM   478  N N   . VAL A 1 62  ? 0.343  12.228 26.094  1.00 23.79 ? 62   VAL A N   1 
ATOM   479  C CA  . VAL A 1 62  ? 1.303  11.455 26.870  1.00 23.17 ? 62   VAL A CA  1 
ATOM   480  C C   . VAL A 1 62  ? 2.583  12.223 27.192  1.00 24.53 ? 62   VAL A C   1 
ATOM   481  O O   . VAL A 1 62  ? 3.248  11.937 28.191  1.00 24.00 ? 62   VAL A O   1 
ATOM   482  C CB  . VAL A 1 62  ? 1.683  10.168 26.118  1.00 22.67 ? 62   VAL A CB  1 
ATOM   483  C CG1 . VAL A 1 62  ? 2.473  10.522 24.861  1.00 20.15 ? 62   VAL A CG1 1 
ATOM   484  C CG2 . VAL A 1 62  ? 2.474  9.233  27.025  1.00 20.81 ? 62   VAL A CG2 1 
ATOM   485  N N   . ILE A 1 63  ? 2.927  13.199 26.356  1.00 24.86 ? 63   ILE A N   1 
ATOM   486  C CA  . ILE A 1 63  ? 4.152  13.952 26.575  1.00 27.00 ? 63   ILE A CA  1 
ATOM   487  C C   . ILE A 1 63  ? 4.131  14.837 27.808  1.00 29.12 ? 63   ILE A C   1 
ATOM   488  O O   . ILE A 1 63  ? 3.170  15.567 28.065  1.00 29.42 ? 63   ILE A O   1 
ATOM   489  C CB  . ILE A 1 63  ? 4.516  14.838 25.366  1.00 25.23 ? 63   ILE A CB  1 
ATOM   490  C CG1 . ILE A 1 63  ? 4.784  13.968 24.139  1.00 24.39 ? 63   ILE A CG1 1 
ATOM   491  C CG2 . ILE A 1 63  ? 5.755  15.663 25.690  1.00 24.46 ? 63   ILE A CG2 1 
ATOM   492  C CD1 . ILE A 1 63  ? 5.091  14.767 22.880  1.00 21.65 ? 63   ILE A CD1 1 
ATOM   493  N N   . GLU A 1 64  ? 5.219  14.759 28.560  1.00 31.76 ? 64   GLU A N   1 
ATOM   494  C CA  . GLU A 1 64  ? 5.403  15.543 29.769  1.00 33.85 ? 64   GLU A CA  1 
ATOM   495  C C   . GLU A 1 64  ? 6.883  15.882 29.868  1.00 34.09 ? 64   GLU A C   1 
ATOM   496  O O   . GLU A 1 64  ? 7.741  15.054 29.543  1.00 34.43 ? 64   GLU A O   1 
ATOM   497  C CB  . GLU A 1 64  ? 4.985  14.743 30.999  1.00 36.86 ? 64   GLU A CB  1 
ATOM   498  C CG  . GLU A 1 64  ? 3.552  14.263 30.972  1.00 42.10 ? 64   GLU A CG  1 
ATOM   499  C CD  . GLU A 1 64  ? 3.102  13.739 32.316  1.00 45.48 ? 64   GLU A CD  1 
ATOM   500  O OE1 . GLU A 1 64  ? 3.064  14.541 33.274  1.00 48.63 ? 64   GLU A OE1 1 
ATOM   501  O OE2 . GLU A 1 64  ? 2.790  12.531 32.418  1.00 46.94 ? 64   GLU A OE2 1 
ATOM   502  N N   . VAL A 1 65  ? 7.180  17.102 30.296  1.00 32.53 ? 65   VAL A N   1 
ATOM   503  C CA  . VAL A 1 65  ? 8.559  17.531 30.447  1.00 32.11 ? 65   VAL A CA  1 
ATOM   504  C C   . VAL A 1 65  ? 8.857  17.609 31.938  1.00 32.46 ? 65   VAL A C   1 
ATOM   505  O O   . VAL A 1 65  ? 8.194  18.339 32.678  1.00 33.36 ? 65   VAL A O   1 
ATOM   506  C CB  . VAL A 1 65  ? 8.796  18.907 29.786  1.00 31.08 ? 65   VAL A CB  1 
ATOM   507  C CG1 . VAL A 1 65  ? 10.252 19.310 29.932  1.00 31.12 ? 65   VAL A CG1 1 
ATOM   508  C CG2 . VAL A 1 65  ? 8.418  18.844 28.315  1.00 29.86 ? 65   VAL A CG2 1 
ATOM   509  N N   . ASN A 1 66  ? 9.845  16.837 32.376  1.00 31.50 ? 66   ASN A N   1 
ATOM   510  C CA  . ASN A 1 66  ? 10.227 16.796 33.781  1.00 31.30 ? 66   ASN A CA  1 
ATOM   511  C C   . ASN A 1 66  ? 11.372 17.740 34.116  1.00 29.05 ? 66   ASN A C   1 
ATOM   512  O O   . ASN A 1 66  ? 11.747 18.593 33.312  1.00 26.31 ? 66   ASN A O   1 
ATOM   513  C CB  . ASN A 1 66  ? 10.642 15.379 34.163  1.00 35.66 ? 66   ASN A CB  1 
ATOM   514  C CG  . ASN A 1 66  ? 9.609  14.358 33.784  1.00 40.48 ? 66   ASN A CG  1 
ATOM   515  O OD1 . ASN A 1 66  ? 8.513  14.324 34.349  1.00 45.24 ? 66   ASN A OD1 1 
ATOM   516  N ND2 . ASN A 1 66  ? 9.944  13.518 32.814  1.00 42.90 ? 66   ASN A ND2 1 
ATOM   517  N N   . ASP A 1 67  ? 11.913 17.565 35.320  1.00 27.59 ? 67   ASP A N   1 
ATOM   518  C CA  . ASP A 1 67  ? 13.028 18.358 35.823  1.00 30.27 ? 67   ASP A CA  1 
ATOM   519  C C   . ASP A 1 67  ? 12.775 19.853 35.745  1.00 30.41 ? 67   ASP A C   1 
ATOM   520  O O   . ASP A 1 67  ? 13.701 20.642 35.568  1.00 30.70 ? 67   ASP A O   1 
ATOM   521  C CB  . ASP A 1 67  ? 14.299 18.005 35.051  1.00 30.58 ? 67   ASP A CB  1 
ATOM   522  C CG  . ASP A 1 67  ? 14.539 16.511 34.990  1.00 31.91 ? 67   ASP A CG  1 
ATOM   523  O OD1 . ASP A 1 67  ? 14.366 15.841 36.030  1.00 31.36 ? 67   ASP A OD1 1 
ATOM   524  O OD2 . ASP A 1 67  ? 14.902 16.009 33.906  1.00 33.53 ? 67   ASP A OD2 1 
ATOM   525  N N   . ARG A 1 68  ? 11.515 20.239 35.892  1.00 33.05 ? 68   ARG A N   1 
ATOM   526  C CA  . ARG A 1 68  ? 11.136 21.642 35.824  1.00 35.05 ? 68   ARG A CA  1 
ATOM   527  C C   . ARG A 1 68  ? 11.785 22.497 36.917  1.00 34.96 ? 68   ARG A C   1 
ATOM   528  O O   . ARG A 1 68  ? 12.000 23.691 36.719  1.00 36.75 ? 68   ARG A O   1 
ATOM   529  C CB  . ARG A 1 68  ? 9.612  21.769 35.899  1.00 37.39 ? 68   ARG A CB  1 
ATOM   530  C CG  . ARG A 1 68  ? 8.870  20.802 34.979  1.00 42.20 ? 68   ARG A CG  1 
ATOM   531  C CD  . ARG A 1 68  ? 8.302  19.618 35.759  1.00 46.76 ? 68   ARG A CD  1 
ATOM   532  N NE  . ARG A 1 68  ? 9.264  19.044 36.699  1.00 48.12 ? 68   ARG A NE  1 
ATOM   533  C CZ  . ARG A 1 68  ? 8.971  18.080 37.567  1.00 50.28 ? 68   ARG A CZ  1 
ATOM   534  N NH1 . ARG A 1 68  ? 7.744  17.578 37.613  1.00 52.26 ? 68   ARG A NH1 1 
ATOM   535  N NH2 . ARG A 1 68  ? 9.898  17.622 38.397  1.00 50.88 ? 68   ARG A NH2 1 
ATOM   536  N N   . LEU A 1 69  ? 12.102 21.890 38.058  1.00 34.11 ? 69   LEU A N   1 
ATOM   537  C CA  . LEU A 1 69  ? 12.716 22.628 39.166  1.00 34.93 ? 69   LEU A CA  1 
ATOM   538  C C   . LEU A 1 69  ? 14.227 22.435 39.259  1.00 34.98 ? 69   LEU A C   1 
ATOM   539  O O   . LEU A 1 69  ? 14.846 22.804 40.257  1.00 33.89 ? 69   LEU A O   1 
ATOM   540  C CB  . LEU A 1 69  ? 12.084 22.219 40.500  1.00 34.43 ? 69   LEU A CB  1 
ATOM   541  C CG  . LEU A 1 69  ? 10.556 22.256 40.609  1.00 35.56 ? 69   LEU A CG  1 
ATOM   542  C CD1 . LEU A 1 69  ? 10.159 22.046 42.059  1.00 35.48 ? 69   LEU A CD1 1 
ATOM   543  C CD2 . LEU A 1 69  ? 10.018 23.585 40.100  1.00 35.70 ? 69   LEU A CD2 1 
ATOM   544  N N   . LYS A 1 70  ? 14.819 21.854 38.222  1.00 34.15 ? 70   LYS A N   1 
ATOM   545  C CA  . LYS A 1 70  ? 16.257 21.629 38.209  1.00 34.26 ? 70   LYS A CA  1 
ATOM   546  C C   . LYS A 1 70  ? 16.943 22.657 37.325  1.00 32.74 ? 70   LYS A C   1 
ATOM   547  O O   . LYS A 1 70  ? 16.334 23.205 36.412  1.00 33.19 ? 70   LYS A O   1 
ATOM   548  C CB  . LYS A 1 70  ? 16.571 20.218 37.704  1.00 34.40 ? 70   LYS A CB  1 
ATOM   549  C CG  . LYS A 1 70  ? 16.138 19.118 38.643  1.00 36.36 ? 70   LYS A CG  1 
ATOM   550  C CD  . LYS A 1 70  ? 16.717 17.785 38.212  1.00 40.93 ? 70   LYS A CD  1 
ATOM   551  C CE  . LYS A 1 70  ? 16.439 16.701 39.241  1.00 42.14 ? 70   LYS A CE  1 
ATOM   552  N NZ  . LYS A 1 70  ? 17.051 15.400 38.844  1.00 45.36 ? 70   LYS A NZ  1 
ATOM   553  N N   . PRO A 1 71  ? 18.224 22.947 37.596  1.00 32.85 ? 71   PRO A N   1 
ATOM   554  C CA  . PRO A 1 71  ? 18.947 23.926 36.782  1.00 33.18 ? 71   PRO A CA  1 
ATOM   555  C C   . PRO A 1 71  ? 19.334 23.333 35.430  1.00 33.78 ? 71   PRO A C   1 
ATOM   556  O O   . PRO A 1 71  ? 19.417 22.114 35.278  1.00 33.96 ? 71   PRO A O   1 
ATOM   557  C CB  . PRO A 1 71  ? 20.161 24.248 37.642  1.00 32.60 ? 71   PRO A CB  1 
ATOM   558  C CG  . PRO A 1 71  ? 20.444 22.933 38.296  1.00 33.08 ? 71   PRO A CG  1 
ATOM   559  C CD  . PRO A 1 71  ? 19.065 22.460 38.704  1.00 32.39 ? 71   PRO A CD  1 
ATOM   560  N N   . MET A 1 72  ? 19.562 24.195 34.448  1.00 33.87 ? 72   MET A N   1 
ATOM   561  C CA  . MET A 1 72  ? 19.949 23.744 33.119  1.00 34.14 ? 72   MET A CA  1 
ATOM   562  C C   . MET A 1 72  ? 21.289 23.027 33.178  1.00 33.21 ? 72   MET A C   1 
ATOM   563  O O   . MET A 1 72  ? 22.140 23.357 34.000  1.00 32.59 ? 72   MET A O   1 
ATOM   564  C CB  . MET A 1 72  ? 20.070 24.935 32.168  1.00 35.63 ? 72   MET A CB  1 
ATOM   565  C CG  . MET A 1 72  ? 18.780 25.689 31.951  1.00 38.16 ? 72   MET A CG  1 
ATOM   566  S SD  . MET A 1 72  ? 17.520 24.641 31.201  1.00 41.27 ? 72   MET A SD  1 
ATOM   567  C CE  . MET A 1 72  ? 18.110 24.585 29.499  1.00 36.82 ? 72   MET A CE  1 
ATOM   568  N N   . VAL A 1 73  ? 21.470 22.038 32.311  1.00 31.50 ? 73   VAL A N   1 
ATOM   569  C CA  . VAL A 1 73  ? 22.731 21.313 32.255  1.00 31.00 ? 73   VAL A CA  1 
ATOM   570  C C   . VAL A 1 73  ? 23.732 22.304 31.666  1.00 31.94 ? 73   VAL A C   1 
ATOM   571  O O   . VAL A 1 73  ? 23.497 22.850 30.587  1.00 31.93 ? 73   VAL A O   1 
ATOM   572  C CB  . VAL A 1 73  ? 22.633 20.081 31.321  1.00 31.10 ? 73   VAL A CB  1 
ATOM   573  C CG1 . VAL A 1 73  ? 23.979 19.374 31.241  1.00 32.53 ? 73   VAL A CG1 1 
ATOM   574  C CG2 . VAL A 1 73  ? 21.563 19.125 31.827  1.00 31.15 ? 73   VAL A CG2 1 
ATOM   575  N N   . ASN A 1 74  ? 24.829 22.560 32.373  1.00 33.16 ? 74   ASN A N   1 
ATOM   576  C CA  . ASN A 1 74  ? 25.835 23.492 31.867  1.00 35.46 ? 74   ASN A CA  1 
ATOM   577  C C   . ASN A 1 74  ? 26.745 22.695 30.944  1.00 34.16 ? 74   ASN A C   1 
ATOM   578  O O   . ASN A 1 74  ? 27.442 21.787 31.382  1.00 33.87 ? 74   ASN A O   1 
ATOM   579  C CB  . ASN A 1 74  ? 26.653 24.097 33.012  1.00 37.35 ? 74   ASN A CB  1 
ATOM   580  C CG  . ASN A 1 74  ? 27.445 25.319 32.576  1.00 40.16 ? 74   ASN A CG  1 
ATOM   581  O OD1 . ASN A 1 74  ? 28.071 25.321 31.515  1.00 40.85 ? 74   ASN A OD1 1 
ATOM   582  N ND2 . ASN A 1 74  ? 27.424 26.362 33.396  1.00 40.40 ? 74   ASN A ND2 1 
ATOM   583  N N   . LEU A 1 75  ? 26.738 23.033 29.662  1.00 32.71 ? 75   LEU A N   1 
ATOM   584  C CA  . LEU A 1 75  ? 27.543 22.291 28.705  1.00 32.73 ? 75   LEU A CA  1 
ATOM   585  C C   . LEU A 1 75  ? 28.897 22.915 28.386  1.00 34.00 ? 75   LEU A C   1 
ATOM   586  O O   . LEU A 1 75  ? 29.820 22.219 27.964  1.00 36.05 ? 75   LEU A O   1 
ATOM   587  C CB  . LEU A 1 75  ? 26.736 22.109 27.417  1.00 30.12 ? 75   LEU A CB  1 
ATOM   588  C CG  . LEU A 1 75  ? 25.366 21.461 27.648  1.00 29.54 ? 75   LEU A CG  1 
ATOM   589  C CD1 . LEU A 1 75  ? 24.559 21.444 26.359  1.00 27.79 ? 75   LEU A CD1 1 
ATOM   590  C CD2 . LEU A 1 75  ? 25.568 20.050 28.192  1.00 26.88 ? 75   LEU A CD2 1 
ATOM   591  N N   . VAL A 1 76  ? 29.018 24.216 28.616  1.00 33.37 ? 76   VAL A N   1 
ATOM   592  C CA  . VAL A 1 76  ? 30.241 24.946 28.303  1.00 35.22 ? 76   VAL A CA  1 
ATOM   593  C C   . VAL A 1 76  ? 31.118 25.362 29.483  1.00 35.20 ? 76   VAL A C   1 
ATOM   594  O O   . VAL A 1 76  ? 32.191 25.928 29.284  1.00 34.73 ? 76   VAL A O   1 
ATOM   595  C CB  . VAL A 1 76  ? 29.896 26.211 27.500  1.00 35.90 ? 76   VAL A CB  1 
ATOM   596  C CG1 . VAL A 1 76  ? 29.201 25.823 26.207  1.00 33.94 ? 76   VAL A CG1 1 
ATOM   597  C CG2 . VAL A 1 76  ? 28.997 27.116 28.330  1.00 35.23 ? 76   VAL A CG2 1 
ATOM   598  N N   . ASP A 1 77  ? 30.670 25.078 30.702  1.00 35.36 ? 77   ASP A N   1 
ATOM   599  C CA  . ASP A 1 77  ? 31.416 25.441 31.908  1.00 37.08 ? 77   ASP A CA  1 
ATOM   600  C C   . ASP A 1 77  ? 32.903 25.067 31.881  1.00 35.10 ? 77   ASP A C   1 
ATOM   601  O O   . ASP A 1 77  ? 33.735 25.785 32.426  1.00 33.75 ? 77   ASP A O   1 
ATOM   602  C CB  . ASP A 1 77  ? 30.761 24.793 33.133  1.00 40.07 ? 77   ASP A CB  1 
ATOM   603  C CG  . ASP A 1 77  ? 30.764 23.272 33.060  1.00 44.13 ? 77   ASP A CG  1 
ATOM   604  O OD1 . ASP A 1 77  ? 31.857 22.671 33.132  1.00 46.42 ? 77   ASP A OD1 1 
ATOM   605  O OD2 . ASP A 1 77  ? 29.673 22.676 32.923  1.00 46.01 ? 77   ASP A OD2 1 
ATOM   606  N N   . SER A 1 78  ? 33.232 23.945 31.248  1.00 34.47 ? 78   SER A N   1 
ATOM   607  C CA  . SER A 1 78  ? 34.614 23.474 31.184  1.00 33.85 ? 78   SER A CA  1 
ATOM   608  C C   . SER A 1 78  ? 35.489 24.204 30.169  1.00 32.38 ? 78   SER A C   1 
ATOM   609  O O   . SER A 1 78  ? 36.707 24.017 30.152  1.00 30.89 ? 78   SER A O   1 
ATOM   610  C CB  . SER A 1 78  ? 34.639 21.974 30.871  1.00 37.28 ? 78   SER A CB  1 
ATOM   611  O OG  . SER A 1 78  ? 33.944 21.233 31.860  1.00 43.08 ? 78   SER A OG  1 
ATOM   612  N N   . LEU A 1 79  ? 34.879 25.030 29.323  1.00 28.80 ? 79   LEU A N   1 
ATOM   613  C CA  . LEU A 1 79  ? 35.640 25.754 28.314  1.00 27.23 ? 79   LEU A CA  1 
ATOM   614  C C   . LEU A 1 79  ? 36.025 27.152 28.768  1.00 26.06 ? 79   LEU A C   1 
ATOM   615  O O   . LEU A 1 79  ? 35.341 27.773 29.575  1.00 25.47 ? 79   LEU A O   1 
ATOM   616  C CB  . LEU A 1 79  ? 34.849 25.859 27.004  1.00 26.51 ? 79   LEU A CB  1 
ATOM   617  C CG  . LEU A 1 79  ? 34.420 24.560 26.315  1.00 25.14 ? 79   LEU A CG  1 
ATOM   618  C CD1 . LEU A 1 79  ? 33.754 24.904 24.989  1.00 25.81 ? 79   LEU A CD1 1 
ATOM   619  C CD2 . LEU A 1 79  ? 35.626 23.655 26.092  1.00 24.39 ? 79   LEU A CD2 1 
ATOM   620  N N   . LYS A 1 80  ? 37.139 27.629 28.239  1.00 26.45 ? 80   LYS A N   1 
ATOM   621  C CA  . LYS A 1 80  ? 37.639 28.959 28.536  1.00 26.81 ? 80   LYS A CA  1 
ATOM   622  C C   . LYS A 1 80  ? 36.783 29.950 27.753  1.00 26.52 ? 80   LYS A C   1 
ATOM   623  O O   . LYS A 1 80  ? 36.347 29.668 26.635  1.00 24.23 ? 80   LYS A O   1 
ATOM   624  C CB  . LYS A 1 80  ? 39.107 29.050 28.108  1.00 29.65 ? 80   LYS A CB  1 
ATOM   625  C CG  . LYS A 1 80  ? 39.588 30.435 27.722  1.00 34.28 ? 80   LYS A CG  1 
ATOM   626  C CD  . LYS A 1 80  ? 40.974 30.362 27.091  1.00 37.16 ? 80   LYS A CD  1 
ATOM   627  C CE  . LYS A 1 80  ? 41.337 31.665 26.406  1.00 38.86 ? 80   LYS A CE  1 
ATOM   628  N NZ  . LYS A 1 80  ? 41.268 32.806 27.358  1.00 40.94 ? 80   LYS A NZ  1 
ATOM   629  N N   . THR A 1 81  ? 36.523 31.105 28.347  1.00 26.15 ? 81   THR A N   1 
ATOM   630  C CA  . THR A 1 81  ? 35.718 32.114 27.684  1.00 26.58 ? 81   THR A CA  1 
ATOM   631  C C   . THR A 1 81  ? 36.600 32.999 26.819  1.00 27.45 ? 81   THR A C   1 
ATOM   632  O O   . THR A 1 81  ? 37.638 33.484 27.269  1.00 28.06 ? 81   THR A O   1 
ATOM   633  C CB  . THR A 1 81  ? 34.976 33.014 28.699  1.00 27.08 ? 81   THR A CB  1 
ATOM   634  O OG1 . THR A 1 81  ? 34.081 32.220 29.483  1.00 28.84 ? 81   THR A OG1 1 
ATOM   635  C CG2 . THR A 1 81  ? 34.183 34.089 27.977  1.00 27.76 ? 81   THR A CG2 1 
ATOM   636  N N   . LEU A 1 82  ? 36.190 33.194 25.571  1.00 26.37 ? 82   LEU A N   1 
ATOM   637  C CA  . LEU A 1 82  ? 36.933 34.056 24.669  1.00 29.27 ? 82   LEU A CA  1 
ATOM   638  C C   . LEU A 1 82  ? 36.571 35.452 25.154  1.00 29.62 ? 82   LEU A C   1 
ATOM   639  O O   . LEU A 1 82  ? 35.439 35.896 24.976  1.00 30.16 ? 82   LEU A O   1 
ATOM   640  C CB  . LEU A 1 82  ? 36.462 33.866 23.223  1.00 25.59 ? 82   LEU A CB  1 
ATOM   641  C CG  . LEU A 1 82  ? 37.238 34.656 22.164  1.00 25.99 ? 82   LEU A CG  1 
ATOM   642  C CD1 . LEU A 1 82  ? 38.696 34.234 22.181  1.00 24.93 ? 82   LEU A CD1 1 
ATOM   643  C CD2 . LEU A 1 82  ? 36.639 34.412 20.790  1.00 25.61 ? 82   LEU A CD2 1 
ATOM   644  N N   . GLN A 1 83  ? 37.520 36.131 25.787  1.00 32.82 ? 83   GLN A N   1 
ATOM   645  C CA  . GLN A 1 83  ? 37.261 37.468 26.311  1.00 35.12 ? 83   GLN A CA  1 
ATOM   646  C C   . GLN A 1 83  ? 36.736 38.410 25.228  1.00 34.53 ? 83   GLN A C   1 
ATOM   647  O O   . GLN A 1 83  ? 37.117 38.307 24.063  1.00 32.59 ? 83   GLN A O   1 
ATOM   648  C CB  . GLN A 1 83  ? 38.529 38.036 26.948  1.00 37.87 ? 83   GLN A CB  1 
ATOM   649  C CG  . GLN A 1 83  ? 39.064 37.197 28.107  1.00 40.59 ? 83   GLN A CG  1 
ATOM   650  C CD  . GLN A 1 83  ? 38.013 36.923 29.175  1.00 43.70 ? 83   GLN A CD  1 
ATOM   651  O OE1 . GLN A 1 83  ? 37.327 37.836 29.641  1.00 44.30 ? 83   GLN A OE1 1 
ATOM   652  N NE2 . GLN A 1 83  ? 37.892 35.660 29.575  1.00 43.50 ? 83   GLN A NE2 1 
ATOM   653  N N   . PRO A 1 84  ? 35.853 39.348 25.609  1.00 35.99 ? 84   PRO A N   1 
ATOM   654  C CA  . PRO A 1 84  ? 35.252 40.322 24.693  1.00 36.02 ? 84   PRO A CA  1 
ATOM   655  C C   . PRO A 1 84  ? 36.200 40.943 23.671  1.00 35.54 ? 84   PRO A C   1 
ATOM   656  O O   . PRO A 1 84  ? 35.831 41.128 22.514  1.00 35.57 ? 84   PRO A O   1 
ATOM   657  C CB  . PRO A 1 84  ? 34.655 41.351 25.645  1.00 36.33 ? 84   PRO A CB  1 
ATOM   658  C CG  . PRO A 1 84  ? 34.202 40.491 26.781  1.00 36.00 ? 84   PRO A CG  1 
ATOM   659  C CD  . PRO A 1 84  ? 35.410 39.606 26.992  1.00 35.88 ? 84   PRO A CD  1 
ATOM   660  N N   . ASN A 1 85  ? 37.421 41.260 24.088  1.00 36.95 ? 85   ASN A N   1 
ATOM   661  C CA  . ASN A 1 85  ? 38.375 41.860 23.166  1.00 38.01 ? 85   ASN A CA  1 
ATOM   662  C C   . ASN A 1 85  ? 38.786 40.888 22.064  1.00 37.94 ? 85   ASN A C   1 
ATOM   663  O O   . ASN A 1 85  ? 38.902 41.278 20.899  1.00 38.00 ? 85   ASN A O   1 
ATOM   664  C CB  . ASN A 1 85  ? 39.611 42.376 23.920  1.00 40.52 ? 85   ASN A CB  1 
ATOM   665  C CG  . ASN A 1 85  ? 40.321 41.291 24.708  1.00 42.99 ? 85   ASN A CG  1 
ATOM   666  O OD1 . ASN A 1 85  ? 39.739 40.664 25.594  1.00 44.79 ? 85   ASN A OD1 1 
ATOM   667  N ND2 . ASN A 1 85  ? 41.594 41.071 24.392  1.00 44.55 ? 85   ASN A ND2 1 
ATOM   668  N N   . LYS A 1 86  ? 38.998 39.626 22.430  1.00 35.43 ? 86   LYS A N   1 
ATOM   669  C CA  . LYS A 1 86  ? 39.386 38.609 21.455  1.00 34.59 ? 86   LYS A CA  1 
ATOM   670  C C   . LYS A 1 86  ? 38.224 38.278 20.518  1.00 32.49 ? 86   LYS A C   1 
ATOM   671  O O   . LYS A 1 86  ? 38.434 37.982 19.344  1.00 32.10 ? 86   LYS A O   1 
ATOM   672  C CB  . LYS A 1 86  ? 39.861 37.344 22.170  1.00 35.31 ? 86   LYS A CB  1 
ATOM   673  C CG  . LYS A 1 86  ? 41.134 37.535 22.988  1.00 38.83 ? 86   LYS A CG  1 
ATOM   674  C CD  . LYS A 1 86  ? 41.517 36.261 23.741  1.00 40.23 ? 86   LYS A CD  1 
ATOM   675  C CE  . LYS A 1 86  ? 40.427 35.842 24.725  1.00 41.58 ? 86   LYS A CE  1 
ATOM   676  N NZ  . LYS A 1 86  ? 40.759 34.582 25.447  1.00 38.67 ? 86   LYS A NZ  1 
ATOM   677  N N   . VAL A 1 87  ? 37.000 38.325 21.036  1.00 31.43 ? 87   VAL A N   1 
ATOM   678  C CA  . VAL A 1 87  ? 35.827 38.059 20.214  1.00 31.55 ? 87   VAL A CA  1 
ATOM   679  C C   . VAL A 1 87  ? 35.808 39.092 19.092  1.00 32.48 ? 87   VAL A C   1 
ATOM   680  O O   . VAL A 1 87  ? 35.587 38.764 17.925  1.00 30.53 ? 87   VAL A O   1 
ATOM   681  C CB  . VAL A 1 87  ? 34.510 38.182 21.030  1.00 31.10 ? 87   VAL A CB  1 
ATOM   682  C CG1 . VAL A 1 87  ? 33.312 37.965 20.120  1.00 28.76 ? 87   VAL A CG1 1 
ATOM   683  C CG2 . VAL A 1 87  ? 34.496 37.169 22.160  1.00 31.45 ? 87   VAL A CG2 1 
ATOM   684  N N   . ALA A 1 88  ? 36.056 40.346 19.456  1.00 33.41 ? 88   ALA A N   1 
ATOM   685  C CA  . ALA A 1 88  ? 36.075 41.435 18.489  1.00 32.82 ? 88   ALA A CA  1 
ATOM   686  C C   . ALA A 1 88  ? 37.178 41.212 17.454  1.00 33.20 ? 88   ALA A C   1 
ATOM   687  O O   . ALA A 1 88  ? 36.959 41.375 16.255  1.00 32.59 ? 88   ALA A O   1 
ATOM   688  C CB  . ALA A 1 88  ? 36.285 42.767 19.213  1.00 33.98 ? 88   ALA A CB  1 
ATOM   689  N N   . GLU A 1 89  ? 38.364 40.839 17.923  1.00 33.50 ? 89   GLU A N   1 
ATOM   690  C CA  . GLU A 1 89  ? 39.490 40.588 17.029  1.00 35.73 ? 89   GLU A CA  1 
ATOM   691  C C   . GLU A 1 89  ? 39.119 39.495 16.021  1.00 36.18 ? 89   GLU A C   1 
ATOM   692  O O   . GLU A 1 89  ? 39.332 39.650 14.819  1.00 34.97 ? 89   GLU A O   1 
ATOM   693  C CB  . GLU A 1 89  ? 40.717 40.148 17.835  1.00 37.91 ? 89   GLU A CB  1 
ATOM   694  C CG  . GLU A 1 89  ? 41.992 40.037 17.012  1.00 41.83 ? 89   GLU A CG  1 
ATOM   695  C CD  . GLU A 1 89  ? 43.132 39.397 17.781  1.00 44.86 ? 89   GLU A CD  1 
ATOM   696  O OE1 . GLU A 1 89  ? 43.399 39.827 18.924  1.00 46.54 ? 89   GLU A OE1 1 
ATOM   697  O OE2 . GLU A 1 89  ? 43.769 38.467 17.239  1.00 47.86 ? 89   GLU A OE2 1 
ATOM   698  N N   . MET A 1 90  ? 38.567 38.391 16.523  1.00 35.57 ? 90   MET A N   1 
ATOM   699  C CA  . MET A 1 90  ? 38.159 37.273 15.672  1.00 34.09 ? 90   MET A CA  1 
ATOM   700  C C   . MET A 1 90  ? 37.141 37.727 14.639  1.00 33.35 ? 90   MET A C   1 
ATOM   701  O O   . MET A 1 90  ? 37.290 37.459 13.445  1.00 32.50 ? 90   MET A O   1 
ATOM   702  C CB  . MET A 1 90  ? 37.544 36.152 16.516  1.00 34.09 ? 90   MET A CB  1 
ATOM   703  C CG  . MET A 1 90  ? 36.837 35.072 15.695  1.00 32.88 ? 90   MET A CG  1 
ATOM   704  S SD  . MET A 1 90  ? 35.856 33.977 16.734  1.00 35.50 ? 90   MET A SD  1 
ATOM   705  C CE  . MET A 1 90  ? 34.384 34.984 16.986  1.00 36.25 ? 90   MET A CE  1 
ATOM   706  N N   . ILE A 1 91  ? 36.096 38.399 15.109  1.00 33.11 ? 91   ILE A N   1 
ATOM   707  C CA  . ILE A 1 91  ? 35.052 38.898 14.226  1.00 35.23 ? 91   ILE A CA  1 
ATOM   708  C C   . ILE A 1 91  ? 35.677 39.806 13.179  1.00 35.48 ? 91   ILE A C   1 
ATOM   709  O O   . ILE A 1 91  ? 35.290 39.786 12.012  1.00 35.65 ? 91   ILE A O   1 
ATOM   710  C CB  . ILE A 1 91  ? 33.986 39.709 14.998  1.00 35.73 ? 91   ILE A CB  1 
ATOM   711  C CG1 . ILE A 1 91  ? 33.237 38.798 15.975  1.00 36.61 ? 91   ILE A CG1 1 
ATOM   712  C CG2 . ILE A 1 91  ? 33.022 40.370 14.015  1.00 35.48 ? 91   ILE A CG2 1 
ATOM   713  C CD1 . ILE A 1 91  ? 32.534 37.627 15.313  1.00 36.88 ? 91   ILE A CD1 1 
ATOM   714  N N   . GLU A 1 92  ? 36.651 40.598 13.610  1.00 37.20 ? 92   GLU A N   1 
ATOM   715  C CA  . GLU A 1 92  ? 37.337 41.521 12.718  1.00 38.83 ? 92   GLU A CA  1 
ATOM   716  C C   . GLU A 1 92  ? 38.112 40.758 11.649  1.00 36.82 ? 92   GLU A C   1 
ATOM   717  O O   . GLU A 1 92  ? 38.160 41.171 10.492  1.00 35.81 ? 92   GLU A O   1 
ATOM   718  C CB  . GLU A 1 92  ? 38.278 42.413 13.528  1.00 41.97 ? 92   GLU A CB  1 
ATOM   719  C CG  . GLU A 1 92  ? 38.928 43.529 12.735  1.00 47.41 ? 92   GLU A CG  1 
ATOM   720  C CD  . GLU A 1 92  ? 39.451 44.634 13.629  1.00 49.78 ? 92   GLU A CD  1 
ATOM   721  O OE1 . GLU A 1 92  ? 38.625 45.279 14.310  1.00 51.73 ? 92   GLU A OE1 1 
ATOM   722  O OE2 . GLU A 1 92  ? 40.680 44.858 13.657  1.00 51.90 ? 92   GLU A OE2 1 
ATOM   723  N N   . ASN A 1 93  ? 38.713 39.638 12.039  1.00 35.34 ? 93   ASN A N   1 
ATOM   724  C CA  . ASN A 1 93  ? 39.466 38.819 11.096  1.00 32.90 ? 93   ASN A CA  1 
ATOM   725  C C   . ASN A 1 93  ? 38.558 37.825 10.381  1.00 32.00 ? 93   ASN A C   1 
ATOM   726  O O   . ASN A 1 93  ? 38.918 36.662 10.204  1.00 30.21 ? 93   ASN A O   1 
ATOM   727  C CB  . ASN A 1 93  ? 40.586 38.064 11.814  1.00 33.71 ? 93   ASN A CB  1 
ATOM   728  C CG  . ASN A 1 93  ? 41.631 38.990 12.389  1.00 35.22 ? 93   ASN A CG  1 
ATOM   729  O OD1 . ASN A 1 93  ? 42.101 39.905 11.715  1.00 35.94 ? 93   ASN A OD1 1 
ATOM   730  N ND2 . ASN A 1 93  ? 42.011 38.753 13.634  1.00 35.10 ? 93   ASN A ND2 1 
ATOM   731  N N   . GLN A 1 94  ? 37.376 38.291 9.986   1.00 29.98 ? 94   GLN A N   1 
ATOM   732  C CA  . GLN A 1 94  ? 36.407 37.467 9.268   1.00 31.57 ? 94   GLN A CA  1 
ATOM   733  C C   . GLN A 1 94  ? 35.957 36.206 10.022  1.00 31.08 ? 94   GLN A C   1 
ATOM   734  O O   . GLN A 1 94  ? 35.611 35.197 9.400   1.00 30.74 ? 94   GLN A O   1 
ATOM   735  C CB  . GLN A 1 94  ? 36.983 37.058 7.908   1.00 33.39 ? 94   GLN A CB  1 
ATOM   736  C CG  . GLN A 1 94  ? 37.626 38.191 7.115   1.00 34.60 ? 94   GLN A CG  1 
ATOM   737  C CD  . GLN A 1 94  ? 36.721 39.401 6.961   1.00 36.43 ? 94   GLN A CD  1 
ATOM   738  O OE1 . GLN A 1 94  ? 36.576 40.205 7.879   1.00 38.50 ? 94   GLN A OE1 1 
ATOM   739  N NE2 . GLN A 1 94  ? 36.103 39.529 5.798   1.00 38.88 ? 94   GLN A NE2 1 
ATOM   740  N N   . GLY A 1 95  ? 35.962 36.270 11.350  1.00 29.81 ? 95   GLY A N   1 
ATOM   741  C CA  . GLY A 1 95  ? 35.553 35.135 12.163  1.00 28.83 ? 95   GLY A CA  1 
ATOM   742  C C   . GLY A 1 95  ? 36.567 34.003 12.144  1.00 29.50 ? 95   GLY A C   1 
ATOM   743  O O   . GLY A 1 95  ? 36.199 32.830 12.237  1.00 29.44 ? 95   GLY A O   1 
ATOM   744  N N   . LEU A 1 96  ? 37.846 34.358 12.044  1.00 28.23 ? 96   LEU A N   1 
ATOM   745  C CA  . LEU A 1 96  ? 38.919 33.375 11.988  1.00 28.43 ? 96   LEU A CA  1 
ATOM   746  C C   . LEU A 1 96  ? 40.031 33.575 13.013  1.00 28.91 ? 96   LEU A C   1 
ATOM   747  O O   . LEU A 1 96  ? 40.226 34.676 13.530  1.00 26.11 ? 96   LEU A O   1 
ATOM   748  C CB  . LEU A 1 96  ? 39.532 33.387 10.592  1.00 30.37 ? 96   LEU A CB  1 
ATOM   749  C CG  . LEU A 1 96  ? 38.589 32.962 9.469   1.00 30.84 ? 96   LEU A CG  1 
ATOM   750  C CD1 . LEU A 1 96  ? 39.194 33.311 8.127   1.00 34.72 ? 96   LEU A CD1 1 
ATOM   751  C CD2 . LEU A 1 96  ? 38.324 31.473 9.577   1.00 32.43 ? 96   LEU A CD2 1 
ATOM   752  N N   . PHE A 1 97  ? 40.747 32.488 13.298  1.00 30.72 ? 97   PHE A N   1 
ATOM   753  C CA  . PHE A 1 97  ? 41.887 32.488 14.218  1.00 30.84 ? 97   PHE A CA  1 
ATOM   754  C C   . PHE A 1 97  ? 43.086 32.194 13.321  1.00 32.15 ? 97   PHE A C   1 
ATOM   755  O O   . PHE A 1 97  ? 43.454 31.037 13.121  1.00 32.83 ? 97   PHE A O   1 
ATOM   756  C CB  . PHE A 1 97  ? 41.764 31.373 15.260  1.00 30.14 ? 97   PHE A CB  1 
ATOM   757  C CG  . PHE A 1 97  ? 40.611 31.536 16.205  1.00 29.22 ? 97   PHE A CG  1 
ATOM   758  C CD1 . PHE A 1 97  ? 40.536 32.636 17.053  1.00 30.29 ? 97   PHE A CD1 1 
ATOM   759  C CD2 . PHE A 1 97  ? 39.611 30.571 16.269  1.00 28.85 ? 97   PHE A CD2 1 
ATOM   760  C CE1 . PHE A 1 97  ? 39.479 32.773 17.957  1.00 30.19 ? 97   PHE A CE1 1 
ATOM   761  C CE2 . PHE A 1 97  ? 38.552 30.695 17.166  1.00 30.52 ? 97   PHE A CE2 1 
ATOM   762  C CZ  . PHE A 1 97  ? 38.487 31.802 18.015  1.00 29.36 ? 97   PHE A CZ  1 
ATOM   763  N N   . LYS A 1 98  ? 43.689 33.249 12.788  1.00 33.47 ? 98   LYS A N   1 
ATOM   764  C CA  . LYS A 1 98  ? 44.815 33.127 11.869  1.00 35.64 ? 98   LYS A CA  1 
ATOM   765  C C   . LYS A 1 98  ? 45.921 32.131 12.207  1.00 34.96 ? 98   LYS A C   1 
ATOM   766  O O   . LYS A 1 98  ? 46.340 31.358 11.349  1.00 35.84 ? 98   LYS A O   1 
ATOM   767  C CB  . LYS A 1 98  ? 45.448 34.502 11.641  1.00 39.05 ? 98   LYS A CB  1 
ATOM   768  C CG  . LYS A 1 98  ? 46.556 34.498 10.597  1.00 42.98 ? 98   LYS A CG  1 
ATOM   769  C CD  . LYS A 1 98  ? 47.094 35.900 10.347  1.00 46.11 ? 98   LYS A CD  1 
ATOM   770  C CE  . LYS A 1 98  ? 48.195 35.887 9.299   1.00 47.14 ? 98   LYS A CE  1 
ATOM   771  N NZ  . LYS A 1 98  ? 49.329 35.015 9.715   1.00 49.65 ? 98   LYS A NZ  1 
ATOM   772  N N   . ASP A 1 99  ? 46.387 32.137 13.450  1.00 33.88 ? 99   ASP A N   1 
ATOM   773  C CA  . ASP A 1 99  ? 47.488 31.263 13.839  1.00 33.51 ? 99   ASP A CA  1 
ATOM   774  C C   . ASP A 1 99  ? 47.164 29.835 14.266  1.00 31.63 ? 99   ASP A C   1 
ATOM   775  O O   . ASP A 1 99  ? 48.068 29.096 14.656  1.00 31.33 ? 99   ASP A O   1 
ATOM   776  C CB  . ASP A 1 99  ? 48.301 31.936 14.950  1.00 37.13 ? 99   ASP A CB  1 
ATOM   777  C CG  . ASP A 1 99  ? 48.777 33.327 14.563  1.00 40.45 ? 99   ASP A CG  1 
ATOM   778  O OD1 . ASP A 1 99  ? 49.335 33.482 13.452  1.00 42.89 ? 99   ASP A OD1 1 
ATOM   779  O OD2 . ASP A 1 99  ? 48.597 34.262 15.371  1.00 41.62 ? 99   ASP A OD2 1 
ATOM   780  N N   . HIS A 1 100 ? 45.901 29.430 14.183  1.00 29.10 ? 100  HIS A N   1 
ATOM   781  C CA  . HIS A 1 100 ? 45.536 28.083 14.609  1.00 27.59 ? 100  HIS A CA  1 
ATOM   782  C C   . HIS A 1 100 ? 44.725 27.244 13.623  1.00 25.40 ? 100  HIS A C   1 
ATOM   783  O O   . HIS A 1 100 ? 44.268 26.160 13.975  1.00 25.10 ? 100  HIS A O   1 
ATOM   784  C CB  . HIS A 1 100 ? 44.768 28.160 15.933  1.00 28.68 ? 100  HIS A CB  1 
ATOM   785  C CG  . HIS A 1 100 ? 45.576 28.695 17.075  1.00 29.13 ? 100  HIS A CG  1 
ATOM   786  N ND1 . HIS A 1 100 ? 46.619 27.995 17.641  1.00 30.28 ? 100  HIS A ND1 1 
ATOM   787  C CD2 . HIS A 1 100 ? 45.496 29.864 17.753  1.00 29.69 ? 100  HIS A CD2 1 
ATOM   788  C CE1 . HIS A 1 100 ? 47.147 28.709 18.619  1.00 30.63 ? 100  HIS A CE1 1 
ATOM   789  N NE2 . HIS A 1 100 ? 46.484 29.848 18.709  1.00 31.30 ? 100  HIS A NE2 1 
ATOM   790  N N   . VAL A 1 101 ? 44.558 27.713 12.393  1.00 23.98 ? 101  VAL A N   1 
ATOM   791  C CA  . VAL A 1 101 ? 43.759 26.971 11.424  1.00 22.42 ? 101  VAL A CA  1 
ATOM   792  C C   . VAL A 1 101 ? 44.153 25.512 11.177  1.00 22.44 ? 101  VAL A C   1 
ATOM   793  O O   . VAL A 1 101 ? 43.325 24.719 10.742  1.00 21.97 ? 101  VAL A O   1 
ATOM   794  C CB  . VAL A 1 101 ? 43.686 27.720 10.070  1.00 22.08 ? 101  VAL A CB  1 
ATOM   795  C CG1 . VAL A 1 101 ? 43.038 29.082 10.281  1.00 22.18 ? 101  VAL A CG1 1 
ATOM   796  C CG2 . VAL A 1 101 ? 45.077 27.862 9.456   1.00 22.17 ? 101  VAL A CG2 1 
ATOM   797  N N   . GLU A 1 102 ? 45.403 25.150 11.456  1.00 24.23 ? 102  GLU A N   1 
ATOM   798  C CA  . GLU A 1 102 ? 45.859 23.772 11.258  1.00 22.58 ? 102  GLU A CA  1 
ATOM   799  C C   . GLU A 1 102 ? 46.260 23.137 12.593  1.00 24.22 ? 102  GLU A C   1 
ATOM   800  O O   . GLU A 1 102 ? 46.838 22.050 12.633  1.00 24.09 ? 102  GLU A O   1 
ATOM   801  C CB  . GLU A 1 102 ? 47.051 23.738 10.293  1.00 24.97 ? 102  GLU A CB  1 
ATOM   802  C CG  . GLU A 1 102 ? 46.770 24.352 8.927   1.00 24.06 ? 102  GLU A CG  1 
ATOM   803  C CD  . GLU A 1 102 ? 47.999 24.377 8.031   1.00 24.50 ? 102  GLU A CD  1 
ATOM   804  O OE1 . GLU A 1 102 ? 48.427 23.304 7.560   1.00 27.94 ? 102  GLU A OE1 1 
ATOM   805  O OE2 . GLU A 1 102 ? 48.544 25.473 7.803   1.00 24.45 ? 102  GLU A OE2 1 
ATOM   806  N N   . ASP A 1 103 ? 45.943 23.821 13.685  1.00 21.79 ? 103  ASP A N   1 
ATOM   807  C CA  . ASP A 1 103 ? 46.272 23.335 15.019  1.00 20.95 ? 103  ASP A CA  1 
ATOM   808  C C   . ASP A 1 103 ? 45.168 22.438 15.580  1.00 20.87 ? 103  ASP A C   1 
ATOM   809  O O   . ASP A 1 103 ? 44.147 22.923 16.076  1.00 21.27 ? 103  ASP A O   1 
ATOM   810  C CB  . ASP A 1 103 ? 46.501 24.529 15.943  1.00 21.06 ? 103  ASP A CB  1 
ATOM   811  C CG  . ASP A 1 103 ? 46.908 24.118 17.336  1.00 21.76 ? 103  ASP A CG  1 
ATOM   812  O OD1 . ASP A 1 103 ? 47.244 22.933 17.538  1.00 24.64 ? 103  ASP A OD1 1 
ATOM   813  O OD2 . ASP A 1 103 ? 46.899 24.990 18.227  1.00 26.32 ? 103  ASP A OD2 1 
ATOM   814  N N   . VAL A 1 104 ? 45.382 21.128 15.517  1.00 19.37 ? 104  VAL A N   1 
ATOM   815  C CA  . VAL A 1 104 ? 44.389 20.182 16.002  1.00 19.56 ? 104  VAL A CA  1 
ATOM   816  C C   . VAL A 1 104 ? 44.254 20.174 17.520  1.00 19.84 ? 104  VAL A C   1 
ATOM   817  O O   . VAL A 1 104 ? 43.287 19.634 18.059  1.00 21.38 ? 104  VAL A O   1 
ATOM   818  C CB  . VAL A 1 104 ? 44.684 18.747 15.478  1.00 19.70 ? 104  VAL A CB  1 
ATOM   819  C CG1 . VAL A 1 104 ? 44.787 18.776 13.946  1.00 20.04 ? 104  VAL A CG1 1 
ATOM   820  C CG2 . VAL A 1 104 ? 45.980 18.201 16.081  1.00 19.55 ? 104  VAL A CG2 1 
ATOM   821  N N   . ASN A 1 105 ? 45.210 20.791 18.209  1.00 21.01 ? 105  ASN A N   1 
ATOM   822  C CA  . ASN A 1 105 ? 45.174 20.852 19.671  1.00 21.91 ? 105  ASN A CA  1 
ATOM   823  C C   . ASN A 1 105 ? 44.602 22.162 20.213  1.00 21.54 ? 105  ASN A C   1 
ATOM   824  O O   . ASN A 1 105 ? 44.542 22.367 21.425  1.00 20.77 ? 105  ASN A O   1 
ATOM   825  C CB  . ASN A 1 105 ? 46.572 20.618 20.264  1.00 24.93 ? 105  ASN A CB  1 
ATOM   826  C CG  . ASN A 1 105 ? 46.852 19.149 20.544  1.00 28.10 ? 105  ASN A CG  1 
ATOM   827  O OD1 . ASN A 1 105 ? 47.814 18.811 21.235  1.00 33.27 ? 105  ASN A OD1 1 
ATOM   828  N ND2 . ASN A 1 105 ? 46.016 18.271 20.006  1.00 29.03 ? 105  ASN A ND2 1 
ATOM   829  N N   . PHE A 1 106 ? 44.190 23.055 19.320  1.00 20.08 ? 106  PHE A N   1 
ATOM   830  C CA  . PHE A 1 106 ? 43.591 24.309 19.744  1.00 21.01 ? 106  PHE A CA  1 
ATOM   831  C C   . PHE A 1 106 ? 42.290 23.935 20.442  1.00 21.12 ? 106  PHE A C   1 
ATOM   832  O O   . PHE A 1 106 ? 41.438 23.274 19.854  1.00 23.05 ? 106  PHE A O   1 
ATOM   833  C CB  . PHE A 1 106 ? 43.297 25.192 18.530  1.00 23.03 ? 106  PHE A CB  1 
ATOM   834  C CG  . PHE A 1 106 ? 42.666 26.512 18.872  1.00 24.63 ? 106  PHE A CG  1 
ATOM   835  C CD1 . PHE A 1 106 ? 43.357 27.454 19.629  1.00 25.69 ? 106  PHE A CD1 1 
ATOM   836  C CD2 . PHE A 1 106 ? 41.386 26.821 18.425  1.00 25.56 ? 106  PHE A CD2 1 
ATOM   837  C CE1 . PHE A 1 106 ? 42.784 28.683 19.932  1.00 28.52 ? 106  PHE A CE1 1 
ATOM   838  C CE2 . PHE A 1 106 ? 40.802 28.047 18.722  1.00 28.13 ? 106  PHE A CE2 1 
ATOM   839  C CZ  . PHE A 1 106 ? 41.502 28.982 19.477  1.00 28.84 ? 106  PHE A CZ  1 
ATOM   840  N N   . GLN A 1 107 ? 42.135 24.342 21.697  1.00 21.88 ? 107  GLN A N   1 
ATOM   841  C CA  . GLN A 1 107 ? 40.928 24.014 22.445  1.00 21.85 ? 107  GLN A CA  1 
ATOM   842  C C   . GLN A 1 107 ? 39.778 24.952 22.115  1.00 21.69 ? 107  GLN A C   1 
ATOM   843  O O   . GLN A 1 107 ? 39.983 26.138 21.888  1.00 20.72 ? 107  GLN A O   1 
ATOM   844  C CB  . GLN A 1 107 ? 41.201 24.054 23.953  1.00 25.83 ? 107  GLN A CB  1 
ATOM   845  C CG  . GLN A 1 107 ? 42.185 22.997 24.445  1.00 28.15 ? 107  GLN A CG  1 
ATOM   846  C CD  . GLN A 1 107 ? 41.755 21.589 24.079  1.00 31.56 ? 107  GLN A CD  1 
ATOM   847  O OE1 . GLN A 1 107 ? 40.644 21.162 24.400  1.00 33.35 ? 107  GLN A OE1 1 
ATOM   848  N NE2 . GLN A 1 107 ? 42.636 20.859 23.404  1.00 32.61 ? 107  GLN A NE2 1 
ATOM   849  N N   . PRO A 1 108 ? 38.544 24.422 22.079  1.00 21.54 ? 108  PRO A N   1 
ATOM   850  C CA  . PRO A 1 108 ? 37.365 25.234 21.775  1.00 22.05 ? 108  PRO A CA  1 
ATOM   851  C C   . PRO A 1 108 ? 37.168 26.290 22.856  1.00 21.38 ? 108  PRO A C   1 
ATOM   852  O O   . PRO A 1 108 ? 37.507 26.071 24.015  1.00 21.34 ? 108  PRO A O   1 
ATOM   853  C CB  . PRO A 1 108 ? 36.226 24.213 21.780  1.00 20.00 ? 108  PRO A CB  1 
ATOM   854  C CG  . PRO A 1 108 ? 36.905 22.927 21.442  1.00 22.30 ? 108  PRO A CG  1 
ATOM   855  C CD  . PRO A 1 108 ? 38.169 23.010 22.250  1.00 22.74 ? 108  PRO A CD  1 
ATOM   856  N N   . VAL A 1 109 ? 36.626 27.434 22.471  1.00 22.12 ? 109  VAL A N   1 
ATOM   857  C CA  . VAL A 1 109 ? 36.368 28.503 23.421  1.00 22.47 ? 109  VAL A CA  1 
ATOM   858  C C   . VAL A 1 109 ? 34.920 28.950 23.251  1.00 24.24 ? 109  VAL A C   1 
ATOM   859  O O   . VAL A 1 109 ? 34.312 28.720 22.206  1.00 23.32 ? 109  VAL A O   1 
ATOM   860  C CB  . VAL A 1 109 ? 37.321 29.692 23.196  1.00 21.32 ? 109  VAL A CB  1 
ATOM   861  C CG1 . VAL A 1 109 ? 38.758 29.260 23.488  1.00 19.10 ? 109  VAL A CG1 1 
ATOM   862  C CG2 . VAL A 1 109 ? 37.200 30.197 21.766  1.00 18.68 ? 109  VAL A CG2 1 
ATOM   863  N N   . LYS A 1 110 ? 34.367 29.572 24.286  1.00 24.75 ? 110  LYS A N   1 
ATOM   864  C CA  . LYS A 1 110 ? 32.984 30.027 24.254  1.00 26.28 ? 110  LYS A CA  1 
ATOM   865  C C   . LYS A 1 110 ? 32.881 31.534 24.457  1.00 26.55 ? 110  LYS A C   1 
ATOM   866  O O   . LYS A 1 110 ? 33.825 32.175 24.917  1.00 24.64 ? 110  LYS A O   1 
ATOM   867  C CB  . LYS A 1 110 ? 32.187 29.337 25.359  1.00 27.41 ? 110  LYS A CB  1 
ATOM   868  C CG  . LYS A 1 110 ? 32.618 29.772 26.753  1.00 27.80 ? 110  LYS A CG  1 
ATOM   869  C CD  . LYS A 1 110 ? 31.844 29.058 27.832  1.00 31.68 ? 110  LYS A CD  1 
ATOM   870  C CE  . LYS A 1 110 ? 32.383 29.413 29.205  1.00 33.95 ? 110  LYS A CE  1 
ATOM   871  N NZ  . LYS A 1 110 ? 31.791 28.544 30.258  1.00 39.09 ? 110  LYS A NZ  1 
ATOM   872  N N   . TYR A 1 111 ? 31.719 32.081 24.114  1.00 28.40 ? 111  TYR A N   1 
ATOM   873  C CA  . TYR A 1 111 ? 31.438 33.505 24.271  1.00 31.13 ? 111  TYR A CA  1 
ATOM   874  C C   . TYR A 1 111 ? 29.960 33.764 23.994  1.00 33.79 ? 111  TYR A C   1 
ATOM   875  O O   . TYR A 1 111 ? 29.332 33.051 23.211  1.00 31.85 ? 111  TYR A O   1 
ATOM   876  C CB  . TYR A 1 111 ? 32.324 34.346 23.338  1.00 29.13 ? 111  TYR A CB  1 
ATOM   877  C CG  . TYR A 1 111 ? 32.050 34.192 21.855  1.00 28.50 ? 111  TYR A CG  1 
ATOM   878  C CD1 . TYR A 1 111 ? 31.041 34.922 21.228  1.00 27.03 ? 111  TYR A CD1 1 
ATOM   879  C CD2 . TYR A 1 111 ? 32.814 33.326 21.076  1.00 28.38 ? 111  TYR A CD2 1 
ATOM   880  C CE1 . TYR A 1 111 ? 30.802 34.794 19.864  1.00 26.14 ? 111  TYR A CE1 1 
ATOM   881  C CE2 . TYR A 1 111 ? 32.583 33.187 19.714  1.00 26.85 ? 111  TYR A CE2 1 
ATOM   882  C CZ  . TYR A 1 111 ? 31.578 33.922 19.114  1.00 27.64 ? 111  TYR A CZ  1 
ATOM   883  O OH  . TYR A 1 111 ? 31.342 33.766 17.769  1.00 27.72 ? 111  TYR A OH  1 
ATOM   884  N N   . SER A 1 112 ? 29.408 34.775 24.656  1.00 38.13 ? 112  SER A N   1 
ATOM   885  C CA  . SER A 1 112 ? 28.004 35.130 24.492  1.00 42.77 ? 112  SER A CA  1 
ATOM   886  C C   . SER A 1 112 ? 27.781 35.946 23.230  1.00 45.36 ? 112  SER A C   1 
ATOM   887  O O   . SER A 1 112 ? 28.313 37.047 23.090  1.00 47.50 ? 112  SER A O   1 
ATOM   888  C CB  . SER A 1 112 ? 27.514 35.921 25.705  1.00 42.81 ? 112  SER A CB  1 
ATOM   889  O OG  . SER A 1 112 ? 27.537 35.116 26.871  1.00 45.90 ? 112  SER A OG  1 
ATOM   890  N N   . ALA A 1 113 ? 26.987 35.399 22.316  1.00 47.86 ? 113  ALA A N   1 
ATOM   891  C CA  . ALA A 1 113 ? 26.688 36.069 21.058  1.00 49.45 ? 113  ALA A CA  1 
ATOM   892  C C   . ALA A 1 113 ? 25.368 36.826 21.155  1.00 50.27 ? 113  ALA A C   1 
ATOM   893  O O   . ALA A 1 113 ? 24.705 36.808 22.193  1.00 51.68 ? 113  ALA A O   1 
ATOM   894  C CB  . ALA A 1 113 ? 26.629 35.043 19.922  1.00 49.49 ? 113  ALA A CB  1 
ATOM   895  N N   . GLU A 1 119 ? 17.059 36.895 23.201  1.00 62.70 ? 119  GLU A N   1 
ATOM   896  C CA  . GLU A 1 119 ? 17.567 35.980 24.217  1.00 61.88 ? 119  GLU A CA  1 
ATOM   897  C C   . GLU A 1 119 ? 19.054 35.712 24.007  1.00 60.47 ? 119  GLU A C   1 
ATOM   898  O O   . GLU A 1 119 ? 19.566 35.849 22.897  1.00 59.89 ? 119  GLU A O   1 
ATOM   899  C CB  . GLU A 1 119 ? 16.778 34.666 24.193  1.00 63.98 ? 119  GLU A CB  1 
ATOM   900  C CG  . GLU A 1 119 ? 16.030 34.392 22.894  1.00 65.78 ? 119  GLU A CG  1 
ATOM   901  C CD  . GLU A 1 119 ? 16.933 34.426 21.677  1.00 67.92 ? 119  GLU A CD  1 
ATOM   902  O OE1 . GLU A 1 119 ? 17.946 33.693 21.662  1.00 70.21 ? 119  GLU A OE1 1 
ATOM   903  O OE2 . GLU A 1 119 ? 16.627 35.184 20.732  1.00 68.60 ? 119  GLU A OE2 1 
ATOM   904  N N   . GLU A 1 120 ? 19.742 35.325 25.077  1.00 59.33 ? 120  GLU A N   1 
ATOM   905  C CA  . GLU A 1 120 ? 21.178 35.072 25.010  1.00 58.67 ? 120  GLU A CA  1 
ATOM   906  C C   . GLU A 1 120 ? 21.569 33.858 24.174  1.00 56.73 ? 120  GLU A C   1 
ATOM   907  O O   . GLU A 1 120 ? 20.845 32.864 24.108  1.00 56.81 ? 120  GLU A O   1 
ATOM   908  C CB  . GLU A 1 120 ? 21.760 34.915 26.417  1.00 59.87 ? 120  GLU A CB  1 
ATOM   909  C CG  . GLU A 1 120 ? 21.475 33.570 27.067  1.00 62.50 ? 120  GLU A CG  1 
ATOM   910  C CD  . GLU A 1 120 ? 22.159 33.424 28.412  1.00 64.50 ? 120  GLU A CD  1 
ATOM   911  O OE1 . GLU A 1 120 ? 23.390 33.637 28.475  1.00 65.37 ? 120  GLU A OE1 1 
ATOM   912  O OE2 . GLU A 1 120 ? 21.470 33.093 29.403  1.00 65.57 ? 120  GLU A OE2 1 
HETATM 913  N N   . CME A 1 121 ? 22.681 33.432 23.934  1.00 53.95 ? 121  CME A N   1 
HETATM 914  C CA  . CME A 1 121 ? 23.138 32.366 23.055  1.00 50.85 ? 121  CME A CA  1 
HETATM 915  C CB  . CME A 1 121 ? 22.518 32.503 21.668  1.00 49.18 ? 121  CME A CB  1 
HETATM 916  S SG  . CME A 1 121 ? 23.094 31.225 20.506  1.00 45.22 ? 121  CME A SG  1 
HETATM 917  S SD  . CME A 1 121 ? 21.606 29.848 20.552  1.00 45.67 ? 121  CME A SD  1 
HETATM 918  C CE  . CME A 1 121 ? 20.406 30.456 19.325  1.00 46.46 ? 121  CME A CE  1 
HETATM 919  C CZ  . CME A 1 121 ? 20.908 30.297 17.904  1.00 48.56 ? 121  CME A CZ  1 
HETATM 920  O OH  . CME A 1 121 ? 20.186 30.881 17.031  1.00 49.17 ? 121  CME A OH  1 
HETATM 921  C C   . CME A 1 121 ? 24.653 32.431 22.930  1.00 50.21 ? 121  CME A C   1 
HETATM 922  O O   . CME A 1 121 ? 25.260 33.455 23.226  1.00 48.74 ? 121  CME A O   1 
ATOM   923  N N   . THR A 1 122 ? 24.983 30.976 23.355  1.00 25.24 ? 122  THR A N   1 
ATOM   924  C CA  . THR A 1 122 ? 26.408 30.759 23.623  1.00 25.22 ? 122  THR A CA  1 
ATOM   925  C C   . THR A 1 122 ? 27.044 30.122 22.400  1.00 25.36 ? 122  THR A C   1 
ATOM   926  O O   . THR A 1 122 ? 26.585 29.126 21.868  1.00 25.93 ? 122  THR A O   1 
ATOM   927  C CB  . THR A 1 122 ? 26.586 29.833 24.822  1.00 26.13 ? 122  THR A CB  1 
ATOM   928  O OG1 . THR A 1 122 ? 25.914 30.377 25.958  1.00 28.26 ? 122  THR A OG1 1 
ATOM   929  C CG2 . THR A 1 122 ? 28.061 29.644 25.175  1.00 25.41 ? 122  THR A CG2 1 
ATOM   930  N N   . ALA A 1 123 ? 28.080 30.673 21.929  1.00 24.88 ? 123  ALA A N   1 
ATOM   931  C CA  . ALA A 1 123 ? 28.729 30.131 20.746  1.00 24.45 ? 123  ALA A CA  1 
ATOM   932  C C   . ALA A 1 123 ? 30.019 29.431 21.142  1.00 23.77 ? 123  ALA A C   1 
ATOM   933  O O   . ALA A 1 123 ? 30.781 29.930 21.976  1.00 23.99 ? 123  ALA A O   1 
ATOM   934  C CB  . ALA A 1 123 ? 29.032 31.257 19.769  1.00 24.95 ? 123  ALA A CB  1 
ATOM   935  N N   . VAL A 1 124 ? 30.236 28.254 20.571  1.00 21.68 ? 124  VAL A N   1 
ATOM   936  C CA  . VAL A 1 124 ? 31.440 27.495 20.854  1.00 19.61 ? 124  VAL A CA  1 
ATOM   937  C C   . VAL A 1 124 ? 32.189 27.336 19.543  1.00 18.74 ? 124  VAL A C   1 
ATOM   938  O O   . VAL A 1 124 ? 31.662 26.774 18.584  1.00 17.73 ? 124  VAL A O   1 
ATOM   939  C CB  . VAL A 1 124 ? 31.109 26.108 21.430  1.00 19.97 ? 124  VAL A CB  1 
ATOM   940  C CG1 . VAL A 1 124 ? 32.395 25.326 21.672  1.00 20.60 ? 124  VAL A CG1 1 
ATOM   941  C CG2 . VAL A 1 124 ? 30.320 26.258 22.722  1.00 21.13 ? 124  VAL A CG2 1 
ATOM   942  N N   . VAL A 1 125 ? 33.418 27.839 19.505  1.00 17.99 ? 125  VAL A N   1 
ATOM   943  C CA  . VAL A 1 125 ? 34.227 27.763 18.300  1.00 18.43 ? 125  VAL A CA  1 
ATOM   944  C C   . VAL A 1 125 ? 35.603 27.175 18.566  1.00 19.12 ? 125  VAL A C   1 
ATOM   945  O O   . VAL A 1 125 ? 36.102 27.213 19.692  1.00 18.99 ? 125  VAL A O   1 
ATOM   946  C CB  . VAL A 1 125 ? 34.409 29.162 17.654  1.00 19.68 ? 125  VAL A CB  1 
ATOM   947  C CG1 . VAL A 1 125 ? 33.093 29.660 17.099  1.00 16.83 ? 125  VAL A CG1 1 
ATOM   948  C CG2 . VAL A 1 125 ? 34.932 30.147 18.685  1.00 18.42 ? 125  VAL A CG2 1 
ATOM   949  N N   . ALA A 1 126 ? 36.201 26.617 17.517  1.00 19.07 ? 126  ALA A N   1 
ATOM   950  C CA  . ALA A 1 126 ? 37.529 26.036 17.606  1.00 19.45 ? 126  ALA A CA  1 
ATOM   951  C C   . ALA A 1 126 ? 38.370 26.561 16.440  1.00 20.32 ? 126  ALA A C   1 
ATOM   952  O O   . ALA A 1 126 ? 38.141 27.674 15.968  1.00 20.32 ? 126  ALA A O   1 
ATOM   953  C CB  . ALA A 1 126 ? 37.448 24.519 17.591  1.00 19.13 ? 126  ALA A CB  1 
ATOM   954  N N   . ARG A 1 127 ? 39.321 25.770 15.955  1.00 19.72 ? 127  ARG A N   1 
ATOM   955  C CA  . ARG A 1 127 ? 40.199 26.245 14.890  1.00 20.55 ? 127  ARG A CA  1 
ATOM   956  C C   . ARG A 1 127 ? 39.552 26.748 13.595  1.00 19.36 ? 127  ARG A C   1 
ATOM   957  O O   . ARG A 1 127 ? 40.183 27.480 12.841  1.00 23.51 ? 127  ARG A O   1 
ATOM   958  C CB  . ARG A 1 127 ? 41.276 25.195 14.584  1.00 18.75 ? 127  ARG A CB  1 
ATOM   959  C CG  . ARG A 1 127 ? 40.903 24.038 13.664  1.00 15.59 ? 127  ARG A CG  1 
ATOM   960  C CD  . ARG A 1 127 ? 42.126 23.119 13.563  1.00 17.15 ? 127  ARG A CD  1 
ATOM   961  N NE  . ARG A 1 127 ? 42.295 22.455 12.270  1.00 16.85 ? 127  ARG A NE  1 
ATOM   962  C CZ  . ARG A 1 127 ? 41.918 21.210 12.006  1.00 16.12 ? 127  ARG A CZ  1 
ATOM   963  N NH1 . ARG A 1 127 ? 41.335 20.473 12.943  1.00 17.75 ? 127  ARG A NH1 1 
ATOM   964  N NH2 . ARG A 1 127 ? 42.145 20.694 10.808  1.00 16.11 ? 127  ARG A NH2 1 
ATOM   965  N N   . GLY A 1 128 ? 38.302 26.379 13.346  1.00 19.80 ? 128  GLY A N   1 
ATOM   966  C CA  . GLY A 1 128 ? 37.625 26.832 12.142  1.00 18.10 ? 128  GLY A CA  1 
ATOM   967  C C   . GLY A 1 128 ? 36.935 28.180 12.300  1.00 20.02 ? 128  GLY A C   1 
ATOM   968  O O   . GLY A 1 128 ? 36.433 28.755 11.331  1.00 19.46 ? 128  GLY A O   1 
ATOM   969  N N   . GLY A 1 129 ? 36.903 28.693 13.524  1.00 19.53 ? 129  GLY A N   1 
ATOM   970  C CA  . GLY A 1 129 ? 36.270 29.977 13.756  1.00 19.31 ? 129  GLY A CA  1 
ATOM   971  C C   . GLY A 1 129 ? 34.753 29.928 13.709  1.00 18.25 ? 129  GLY A C   1 
ATOM   972  O O   . GLY A 1 129 ? 34.147 28.856 13.797  1.00 17.58 ? 129  GLY A O   1 
ATOM   973  N N   . THR A 1 130 ? 34.137 31.095 13.544  1.00 19.08 ? 130  THR A N   1 
ATOM   974  C CA  . THR A 1 130 ? 32.681 31.202 13.523  1.00 20.39 ? 130  THR A CA  1 
ATOM   975  C C   . THR A 1 130 ? 31.962 30.329 12.507  1.00 19.67 ? 130  THR A C   1 
ATOM   976  O O   . THR A 1 130 ? 30.827 29.930 12.735  1.00 20.62 ? 130  THR A O   1 
ATOM   977  C CB  . THR A 1 130 ? 32.228 32.658 13.294  1.00 19.47 ? 130  THR A CB  1 
ATOM   978  O OG1 . THR A 1 130 ? 32.785 33.145 12.066  1.00 21.34 ? 130  THR A OG1 1 
ATOM   979  C CG2 . THR A 1 130 ? 32.678 33.539 14.444  1.00 20.90 ? 130  THR A CG2 1 
ATOM   980  N N   . ALA A 1 131 ? 32.611 30.030 11.390  1.00 19.13 ? 131  ALA A N   1 
ATOM   981  C CA  . ALA A 1 131 ? 31.968 29.222 10.354  1.00 18.58 ? 131  ALA A CA  1 
ATOM   982  C C   . ALA A 1 131 ? 31.545 27.821 10.811  1.00 18.42 ? 131  ALA A C   1 
ATOM   983  O O   . ALA A 1 131 ? 30.598 27.254 10.270  1.00 17.41 ? 131  ALA A O   1 
ATOM   984  C CB  . ALA A 1 131 ? 32.886 29.123 9.132   1.00 19.73 ? 131  ALA A CB  1 
ATOM   985  N N   . ASN A 1 132 ? 32.238 27.258 11.799  1.00 17.79 ? 132  ASN A N   1 
ATOM   986  C CA  . ASN A 1 132 ? 31.900 25.922 12.289  1.00 17.13 ? 132  ASN A CA  1 
ATOM   987  C C   . ASN A 1 132 ? 31.388 25.969 13.726  1.00 18.59 ? 132  ASN A C   1 
ATOM   988  O O   . ASN A 1 132 ? 31.398 24.966 14.439  1.00 17.70 ? 132  ASN A O   1 
ATOM   989  C CB  . ASN A 1 132 ? 33.129 25.013 12.218  1.00 17.92 ? 132  ASN A CB  1 
ATOM   990  C CG  . ASN A 1 132 ? 33.737 24.964 10.834  1.00 17.42 ? 132  ASN A CG  1 
ATOM   991  O OD1 . ASN A 1 132 ? 34.919 25.257 10.655  1.00 18.58 ? 132  ASN A OD1 1 
ATOM   992  N ND2 . ASN A 1 132 ? 32.933 24.590 9.845   1.00 15.67 ? 132  ASN A ND2 1 
ATOM   993  N N   . ALA A 1 133 ? 30.925 27.139 14.141  1.00 18.58 ? 133  ALA A N   1 
ATOM   994  C CA  . ALA A 1 133 ? 30.440 27.322 15.498  1.00 18.88 ? 133  ALA A CA  1 
ATOM   995  C C   . ALA A 1 133 ? 29.239 26.457 15.864  1.00 17.68 ? 133  ALA A C   1 
ATOM   996  O O   . ALA A 1 133 ? 28.389 26.149 15.032  1.00 19.22 ? 133  ALA A O   1 
ATOM   997  C CB  . ALA A 1 133 ? 30.106 28.805 15.730  1.00 18.10 ? 133  ALA A CB  1 
ATOM   998  N N   . ILE A 1 134 ? 29.200 26.058 17.128  1.00 19.15 ? 134  ILE A N   1 
ATOM   999  C CA  . ILE A 1 134 ? 28.101 25.279 17.686  1.00 19.18 ? 134  ILE A CA  1 
ATOM   1000 C C   . ILE A 1 134 ? 27.415 26.330 18.540  1.00 19.81 ? 134  ILE A C   1 
ATOM   1001 O O   . ILE A 1 134 ? 28.096 27.098 19.214  1.00 18.94 ? 134  ILE A O   1 
ATOM   1002 C CB  . ILE A 1 134 ? 28.617 24.157 18.609  1.00 17.51 ? 134  ILE A CB  1 
ATOM   1003 C CG1 . ILE A 1 134 ? 29.398 23.124 17.788  1.00 17.61 ? 134  ILE A CG1 1 
ATOM   1004 C CG2 . ILE A 1 134 ? 27.447 23.509 19.351  1.00 19.49 ? 134  ILE A CG2 1 
ATOM   1005 C CD1 . ILE A 1 134 ? 30.148 22.114 18.641  1.00 12.41 ? 134  ILE A CD1 1 
ATOM   1006 N N   . ARG A 1 135 ? 26.086 26.387 18.512  1.00 21.73 ? 135  ARG A N   1 
ATOM   1007 C CA  . ARG A 1 135 ? 25.378 27.387 19.305  1.00 21.76 ? 135  ARG A CA  1 
ATOM   1008 C C   . ARG A 1 135 ? 24.417 26.776 20.308  1.00 21.65 ? 135  ARG A C   1 
ATOM   1009 O O   . ARG A 1 135 ? 23.626 25.903 19.970  1.00 20.79 ? 135  ARG A O   1 
ATOM   1010 C CB  . ARG A 1 135 ? 24.639 28.371 18.384  1.00 24.84 ? 135  ARG A CB  1 
ATOM   1011 C CG  . ARG A 1 135 ? 25.594 29.258 17.593  1.00 28.56 ? 135  ARG A CG  1 
ATOM   1012 C CD  . ARG A 1 135 ? 24.896 30.443 16.945  1.00 35.00 ? 135  ARG A CD  1 
ATOM   1013 N NE  . ARG A 1 135 ? 25.874 31.376 16.386  1.00 38.87 ? 135  ARG A NE  1 
ATOM   1014 C CZ  . ARG A 1 135 ? 26.670 31.097 15.358  1.00 40.50 ? 135  ARG A CZ  1 
ATOM   1015 N NH1 . ARG A 1 135 ? 26.600 29.912 14.764  1.00 41.91 ? 135  ARG A NH1 1 
ATOM   1016 N NH2 . ARG A 1 135 ? 27.555 31.993 14.938  1.00 40.31 ? 135  ARG A NH2 1 
ATOM   1017 N N   . ILE A 1 136 ? 24.499 27.245 21.548  1.00 21.59 ? 136  ILE A N   1 
ATOM   1018 C CA  . ILE A 1 136 ? 23.651 26.740 22.619  1.00 24.43 ? 136  ILE A CA  1 
ATOM   1019 C C   . ILE A 1 136 ? 22.742 27.845 23.159  1.00 27.29 ? 136  ILE A C   1 
ATOM   1020 O O   . ILE A 1 136 ? 23.202 28.936 23.483  1.00 25.11 ? 136  ILE A O   1 
ATOM   1021 C CB  . ILE A 1 136 ? 24.517 26.170 23.760  1.00 24.71 ? 136  ILE A CB  1 
ATOM   1022 C CG1 . ILE A 1 136 ? 25.550 25.200 23.176  1.00 23.08 ? 136  ILE A CG1 1 
ATOM   1023 C CG2 . ILE A 1 136 ? 23.636 25.455 24.781  1.00 26.24 ? 136  ILE A CG2 1 
ATOM   1024 C CD1 . ILE A 1 136 ? 26.556 24.681 24.178  1.00 24.74 ? 136  ILE A CD1 1 
ATOM   1025 N N   . ALA A 1 137 ? 21.448 27.553 23.249  1.00 30.12 ? 137  ALA A N   1 
ATOM   1026 C CA  . ALA A 1 137 ? 20.470 28.522 23.732  1.00 34.76 ? 137  ALA A CA  1 
ATOM   1027 C C   . ALA A 1 137 ? 20.306 28.513 25.252  1.00 38.65 ? 137  ALA A C   1 
ATOM   1028 O O   . ALA A 1 137 ? 20.808 27.626 25.941  1.00 40.53 ? 137  ALA A O   1 
ATOM   1029 C CB  . ALA A 1 137 ? 19.128 28.270 23.059  1.00 34.19 ? 137  ALA A CB  1 
ATOM   1030 N N   . ALA A 1 138 ? 19.598 29.514 25.768  1.00 42.99 ? 138  ALA A N   1 
ATOM   1031 C CA  . ALA A 1 138 ? 19.356 29.638 27.204  1.00 44.62 ? 138  ALA A CA  1 
ATOM   1032 C C   . ALA A 1 138 ? 18.719 28.374 27.773  1.00 45.98 ? 138  ALA A C   1 
ATOM   1033 O O   . ALA A 1 138 ? 17.501 28.303 27.946  1.00 46.09 ? 138  ALA A O   1 
ATOM   1034 C CB  . ALA A 1 138 ? 18.458 30.839 27.476  1.00 44.84 ? 138  ALA A CB  1 
ATOM   1035 N N   . SER A 1 152 ? 5.387  17.451 14.429  1.00 44.08 ? 152  SER A N   1 
ATOM   1036 C CA  . SER A 1 152 ? 6.024  18.604 15.061  1.00 43.77 ? 152  SER A CA  1 
ATOM   1037 C C   . SER A 1 152 ? 7.084  18.179 16.074  1.00 41.25 ? 152  SER A C   1 
ATOM   1038 O O   . SER A 1 152 ? 8.180  18.742 16.111  1.00 42.29 ? 152  SER A O   1 
ATOM   1039 C CB  . SER A 1 152 ? 4.978  19.475 15.757  1.00 44.61 ? 152  SER A CB  1 
ATOM   1040 O OG  . SER A 1 152 ? 5.603  20.547 16.443  1.00 48.48 ? 152  SER A OG  1 
ATOM   1041 N N   . ILE A 1 153 ? 6.752  17.197 16.907  1.00 37.74 ? 153  ILE A N   1 
ATOM   1042 C CA  . ILE A 1 153 ? 7.702  16.710 17.898  1.00 33.92 ? 153  ILE A CA  1 
ATOM   1043 C C   . ILE A 1 153 ? 8.481  15.550 17.302  1.00 29.76 ? 153  ILE A C   1 
ATOM   1044 O O   . ILE A 1 153 ? 7.922  14.487 17.042  1.00 29.22 ? 153  ILE A O   1 
ATOM   1045 C CB  . ILE A 1 153 ? 6.999  16.214 19.183  1.00 34.71 ? 153  ILE A CB  1 
ATOM   1046 C CG1 . ILE A 1 153 ? 6.265  17.373 19.864  1.00 35.80 ? 153  ILE A CG1 1 
ATOM   1047 C CG2 . ILE A 1 153 ? 8.027  15.617 20.143  1.00 34.54 ? 153  ILE A CG2 1 
ATOM   1048 C CD1 . ILE A 1 153 ? 7.176  18.479 20.372  1.00 34.61 ? 153  ILE A CD1 1 
ATOM   1049 N N   . ASN A 1 154 ? 9.769  15.762 17.071  1.00 25.95 ? 154  ASN A N   1 
ATOM   1050 C CA  . ASN A 1 154 ? 10.616 14.720 16.512  1.00 24.16 ? 154  ASN A CA  1 
ATOM   1051 C C   . ASN A 1 154 ? 11.634 14.277 17.548  1.00 21.47 ? 154  ASN A C   1 
ATOM   1052 O O   . ASN A 1 154 ? 12.224 15.109 18.238  1.00 19.28 ? 154  ASN A O   1 
ATOM   1053 C CB  . ASN A 1 154 ? 11.326 15.229 15.259  1.00 26.60 ? 154  ASN A CB  1 
ATOM   1054 C CG  . ASN A 1 154 ? 10.356 15.591 14.159  1.00 27.62 ? 154  ASN A CG  1 
ATOM   1055 O OD1 . ASN A 1 154 ? 9.521  14.781 13.769  1.00 28.71 ? 154  ASN A OD1 1 
ATOM   1056 N ND2 . ASN A 1 154 ? 10.457 16.810 13.656  1.00 32.27 ? 154  ASN A ND2 1 
ATOM   1057 N N   . ILE A 1 155 ? 11.833 12.967 17.654  1.00 17.89 ? 155  ILE A N   1 
ATOM   1058 C CA  . ILE A 1 155 ? 12.770 12.426 18.623  1.00 16.79 ? 155  ILE A CA  1 
ATOM   1059 C C   . ILE A 1 155 ? 14.117 12.036 18.010  1.00 16.33 ? 155  ILE A C   1 
ATOM   1060 O O   . ILE A 1 155 ? 15.065 11.727 18.731  1.00 15.72 ? 155  ILE A O   1 
ATOM   1061 C CB  . ILE A 1 155 ? 12.170 11.200 19.339  1.00 15.97 ? 155  ILE A CB  1 
ATOM   1062 C CG1 . ILE A 1 155 ? 11.754 10.149 18.302  1.00 15.90 ? 155  ILE A CG1 1 
ATOM   1063 C CG2 . ILE A 1 155 ? 10.974 11.633 20.208  1.00 15.32 ? 155  ILE A CG2 1 
ATOM   1064 C CD1 . ILE A 1 155 ? 11.307 8.829  18.899  1.00 16.79 ? 155  ILE A CD1 1 
ATOM   1065 N N   . ALA A 1 156 ? 14.192 12.046 16.684  1.00 16.56 ? 156  ALA A N   1 
ATOM   1066 C CA  . ALA A 1 156 ? 15.425 11.697 15.988  1.00 15.35 ? 156  ALA A CA  1 
ATOM   1067 C C   . ALA A 1 156 ? 15.877 12.855 15.128  1.00 15.81 ? 156  ALA A C   1 
ATOM   1068 O O   . ALA A 1 156 ? 15.069 13.508 14.466  1.00 17.00 ? 156  ALA A O   1 
ATOM   1069 C CB  . ALA A 1 156 ? 15.219 10.453 15.122  1.00 14.71 ? 156  ALA A CB  1 
ATOM   1070 N N   . GLN A 1 157 ? 17.178 13.109 15.144  1.00 15.28 ? 157  GLN A N   1 
ATOM   1071 C CA  . GLN A 1 157 ? 17.763 14.188 14.365  1.00 16.47 ? 157  GLN A CA  1 
ATOM   1072 C C   . GLN A 1 157 ? 19.105 13.698 13.823  1.00 17.18 ? 157  GLN A C   1 
ATOM   1073 O O   . GLN A 1 157 ? 19.739 12.819 14.414  1.00 14.87 ? 157  GLN A O   1 
ATOM   1074 C CB  . GLN A 1 157 ? 17.966 15.416 15.261  1.00 16.11 ? 157  GLN A CB  1 
ATOM   1075 C CG  . GLN A 1 157 ? 18.640 16.607 14.606  1.00 18.31 ? 157  GLN A CG  1 
ATOM   1076 C CD  . GLN A 1 157 ? 17.867 17.146 13.412  1.00 21.45 ? 157  GLN A CD  1 
ATOM   1077 O OE1 . GLN A 1 157 ? 17.791 16.504 12.359  1.00 22.30 ? 157  GLN A OE1 1 
ATOM   1078 N NE2 . GLN A 1 157 ? 17.286 18.332 13.573  1.00 20.89 ? 157  GLN A NE2 1 
ATOM   1079 N N   . ILE A 1 158 ? 19.524 14.247 12.690  1.00 16.80 ? 158  ILE A N   1 
ATOM   1080 C CA  . ILE A 1 158 ? 20.803 13.860 12.102  1.00 20.04 ? 158  ILE A CA  1 
ATOM   1081 C C   . ILE A 1 158 ? 21.829 14.962 12.291  1.00 20.55 ? 158  ILE A C   1 
ATOM   1082 O O   . ILE A 1 158 ? 21.491 16.145 12.298  1.00 20.83 ? 158  ILE A O   1 
ATOM   1083 C CB  . ILE A 1 158 ? 20.700 13.602 10.579  1.00 20.82 ? 158  ILE A CB  1 
ATOM   1084 C CG1 . ILE A 1 158 ? 20.261 14.883 9.864   1.00 24.24 ? 158  ILE A CG1 1 
ATOM   1085 C CG2 . ILE A 1 158 ? 19.724 12.472 10.299  1.00 19.47 ? 158  ILE A CG2 1 
ATOM   1086 C CD1 . ILE A 1 158 ? 20.329 14.792 8.339   1.00 26.06 ? 158  ILE A CD1 1 
ATOM   1087 N N   . VAL A 1 159 ? 23.086 14.568 12.456  1.00 20.97 ? 159  VAL A N   1 
ATOM   1088 C CA  . VAL A 1 159 ? 24.170 15.528 12.594  1.00 20.47 ? 159  VAL A CA  1 
ATOM   1089 C C   . VAL A 1 159 ? 25.195 15.219 11.507  1.00 19.92 ? 159  VAL A C   1 
ATOM   1090 O O   . VAL A 1 159 ? 25.974 14.285 11.634  1.00 18.51 ? 159  VAL A O   1 
ATOM   1091 C CB  . VAL A 1 159 ? 24.869 15.433 13.968  1.00 22.06 ? 159  VAL A CB  1 
ATOM   1092 C CG1 . VAL A 1 159 ? 26.123 16.305 13.970  1.00 22.66 ? 159  VAL A CG1 1 
ATOM   1093 C CG2 . VAL A 1 159 ? 23.925 15.872 15.069  1.00 21.64 ? 159  VAL A CG2 1 
ATOM   1094 N N   . PRO A 1 160 ? 25.175 15.977 10.403  1.00 19.65 ? 160  PRO A N   1 
ATOM   1095 C CA  . PRO A 1 160 ? 26.136 15.740 9.320   1.00 20.72 ? 160  PRO A CA  1