data_1H1M
# 
_entry.id   1H1M 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.279 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   1H1M         
PDBE  EBI-11140    
WWPDB D_1290011140 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
_pdbx_database_related.details 
PDB 1HUJ unspecified 'CRYSTAL STRUCTURE OF QUERCETIN 2,3-DIOXYGENASE'                                                      
PDB 1H1I unspecified 'CRYSTAL STRUCTURE OF QUERCETIN 2,3-DIOXYGENASE ANAEROBICALLY COMPLEXED WITH THE SUBSTRATE QUERCETIN' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        1H1M 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.SG_entry                        . 
_pdbx_database_status.recvd_initial_deposition_date   2002-07-19 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Steiner, R.A.'  1 
'Dijkstra, B.W.' 2 
# 
_citation.id                        primary 
_citation.title                     
;Anaerobic Enzyme.Substrate Structures Provide Insight Into the Reaction Mechanism of the Copper- Dependent Quercetin 2,3-Dioxygenase.
;
_citation.journal_abbrev            Proc.Natl.Acad.Sci.USA 
_citation.journal_volume            99 
_citation.page_first                16625 
_citation.page_last                 ? 
_citation.year                      2002 
_citation.journal_id_ASTM           PNASA6 
_citation.country                   US 
_citation.journal_id_ISSN           0027-8424 
_citation.journal_id_CSD            0040 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   12486225 
_citation.pdbx_database_id_DOI      10.1073/PNAS.262506299 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Steiner, R.A.'  1 
primary 'Kalk, K.H.'     2 
primary 'Dijkstra, B.W.' 3 
# 
_cell.entry_id           1H1M 
_cell.length_a           109.272 
_cell.length_b           55.377 
_cell.length_c           123.929 
_cell.angle_alpha        90.00 
_cell.angle_beta         98.33 
_cell.angle_gamma        90.00 
_cell.Z_PDB              8 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         1H1M 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
# 
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 'QUERCETIN 2,3-DIOXYGENASE'                             37958.195 4    1.13.11.24 ? ? ? 
2 non-polymer man N-ACETYL-D-GLUCOSAMINE                                  221.208   21   ?          ? ? ? 
3 non-polymer man BETA-D-MANNOSE                                          180.156   3    ?          ? ? ? 
4 non-polymer man ALPHA-D-MANNOSE                                         180.156   4    ?          ? ? ? 
5 non-polymer syn '3,5,7-TRIHYDROXY-2-(4-HYDROXYPHENYL)-4H-CHROMEN-4-ONE' 286.236   4    ?          ? ? ? 
6 non-polymer syn 'COPPER (II) ION'                                       63.546    4    ?          ? ? ? 
7 non-polymer syn '(4S)-2-METHYL-2,4-PENTANEDIOL'                         118.174   4    ?          ? ? ? 
8 water       nat water                                                   18.015    1547 ?          ? ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;DTSSLIVEDAPDHVRPYVIRHYSHARAVTVDTQLYRFYVTGPSSGYAFTLMGTNAPHSDALGVLPHIHQKHYENFYCNKG
SFQLWAQSGNETQQTRVLSSGDYGSVPRNVTHTFQIQDPDTEMTGVIVPGGFEDLFYYLGTNATDTTHTPYIPSSSDSSS
TTGPDSSTISTLQSFDVYAELSFTPRTDTVNGTAPANTVWHTGANALASTAGDPYFIANGWGPKYLNSQYGYQIVAPFVT
ATQAQDTNYTLSTISMSTTPSTVTVPTWSFPGACAFQVQEGRVVVQIGDYAATELGSGDVAFIPGGVEFKYYSEAYFSKV
LFVSSGSDGLDQNLVNGGEEWSSVSFPADW
;
_entity_poly.pdbx_seq_one_letter_code_can   
;DTSSLIVEDAPDHVRPYVIRHYSHARAVTVDTQLYRFYVTGPSSGYAFTLMGTNAPHSDALGVLPHIHQKHYENFYCNKG
SFQLWAQSGNETQQTRVLSSGDYGSVPRNVTHTFQIQDPDTEMTGVIVPGGFEDLFYYLGTNATDTTHTPYIPSSSDSSS
TTGPDSSTISTLQSFDVYAELSFTPRTDTVNGTAPANTVWHTGANALASTAGDPYFIANGWGPKYLNSQYGYQIVAPFVT
ATQAQDTNYTLSTISMSTTPSTVTVPTWSFPGACAFQVQEGRVVVQIGDYAATELGSGDVAFIPGGVEFKYYSEAYFSKV
LFVSSGSDGLDQNLVNGGEEWSSVSFPADW
;
_entity_poly.pdbx_strand_id                 A,B,C,D 
_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   ASP n 
1 2   THR n 
1 3   SER n 
1 4   SER n 
1 5   LEU n 
1 6   ILE n 
1 7   VAL n 
1 8   GLU n 
1 9   ASP n 
1 10  ALA n 
1 11  PRO n 
1 12  ASP n 
1 13  HIS n 
1 14  VAL n 
1 15  ARG n 
1 16  PRO n 
1 17  TYR n 
1 18  VAL n 
1 19  ILE n 
1 20  ARG n 
1 21  HIS n 
1 22  TYR n 
1 23  SER n 
1 24  HIS n 
1 25  ALA n 
1 26  ARG n 
1 27  ALA n 
1 28  VAL n 
1 29  THR n 
1 30  VAL n 
1 31  ASP n 
1 32  THR n 
1 33  GLN n 
1 34  LEU n 
1 35  TYR n 
1 36  ARG n 
1 37  PHE n 
1 38  TYR n 
1 39  VAL n 
1 40  THR n 
1 41  GLY n 
1 42  PRO n 
1 43  SER n 
1 44  SER n 
1 45  GLY n 
1 46  TYR n 
1 47  ALA n 
1 48  PHE n 
1 49  THR n 
1 50  LEU n 
1 51  MET n 
1 52  GLY n 
1 53  THR n 
1 54  ASN n 
1 55  ALA n 
1 56  PRO n 
1 57  HIS n 
1 58  SER n 
1 59  ASP n 
1 60  ALA n 
1 61  LEU n 
1 62  GLY n 
1 63  VAL n 
1 64  LEU n 
1 65  PRO n 
1 66  HIS n 
1 67  ILE n 
1 68  HIS n 
1 69  GLN n 
1 70  LYS n 
1 71  HIS n 
1 72  TYR n 
1 73  GLU n 
1 74  ASN n 
1 75  PHE n 
1 76  TYR n 
1 77  CYS n 
1 78  ASN n 
1 79  LYS n 
1 80  GLY n 
1 81  SER n 
1 82  PHE n 
1 83  GLN n 
1 84  LEU n 
1 85  TRP n 
1 86  ALA n 
1 87  GLN n 
1 88  SER n 
1 89  GLY n 
1 90  ASN n 
1 91  GLU n 
1 92  THR n 
1 93  GLN n 
1 94  GLN n 
1 95  THR n 
1 96  ARG n 
1 97  VAL n 
1 98  LEU n 
1 99  SER n 
1 100 SER n 
1 101 GLY n 
1 102 ASP n 
1 103 TYR n 
1 104 GLY n 
1 105 SER n 
1 106 VAL n 
1 107 PRO n 
1 108 ARG n 
1 109 ASN n 
1 110 VAL n 
1 111 THR n 
1 112 HIS n 
1 113 THR n 
1 114 PHE n 
1 115 GLN n 
1 116 ILE n 
1 117 GLN n 
1 118 ASP n 
1 119 PRO n 
1 120 ASP n 
1 121 THR n 
1 122 GLU n 
1 123 MET n 
1 124 THR n 
1 125 GLY n 
1 126 VAL n 
1 127 ILE n 
1 128 VAL n 
1 129 PRO n 
1 130 GLY n 
1 131 GLY n 
1 132 PHE n 
1 133 GLU n 
1 134 ASP n 
1 135 LEU n 
1 136 PHE n 
1 137 TYR n 
1 138 TYR n 
1 139 LEU n 
1 140 GLY n 
1 141 THR n 
1 142 ASN n 
1 143 ALA n 
1 144 THR n 
1 145 ASP n 
1 146 THR n 
1 147 THR n 
1 148 HIS n 
1 149 THR n 
1 150 PRO n 
1 151 TYR n 
1 152 ILE n 
1 153 PRO n 
1 154 SER n 
1 155 SER n 
1 156 SER n 
1 157 ASP n 
1 158 SER n 
1 159 SER n 
1 160 SER n 
1 161 THR n 
1 162 THR n 
1 163 GLY n 
1 164 PRO n 
1 165 ASP n 
1 166 SER n 
1 167 SER n 
1 168 THR n 
1 169 ILE n 
1 170 SER n 
1 171 THR n 
1 172 LEU n 
1 173 GLN n 
1 174 SER n 
1 175 PHE n 
1 176 ASP n 
1 177 VAL n 
1 178 TYR n 
1 179 ALA n 
1 180 GLU n 
1 181 LEU n 
1 182 SER n 
1 183 PHE n 
1 184 THR n 
1 185 PRO n 
1 186 ARG n 
1 187 THR n 
1 188 ASP n 
1 189 THR n 
1 190 VAL n 
1 191 ASN n 
1 192 GLY n 
1 193 THR n 
1 194 ALA n 
1 195 PRO n 
1 196 ALA n 
1 197 ASN n 
1 198 THR n 
1 199 VAL n 
1 200 TRP n 
1 201 HIS n 
1 202 THR n 
1 203 GLY n 
1 204 ALA n 
1 205 ASN n 
1 206 ALA n 
1 207 LEU n 
1 208 ALA n 
1 209 SER n 
1 210 THR n 
1 211 ALA n 
1 212 GLY n 
1 213 ASP n 
1 214 PRO n 
1 215 TYR n 
1 216 PHE n 
1 217 ILE n 
1 218 ALA n 
1 219 ASN n 
1 220 GLY n 
1 221 TRP n 
1 222 GLY n 
1 223 PRO n 
1 224 LYS n 
1 225 TYR n 
1 226 LEU n 
1 227 ASN n 
1 228 SER n 
1 229 GLN n 
1 230 TYR n 
1 231 GLY n 
1 232 TYR n 
1 233 GLN n 
1 234 ILE n 
1 235 VAL n 
1 236 ALA n 
1 237 PRO n 
1 238 PHE n 
1 239 VAL n 
1 240 THR n 
1 241 ALA n 
1 242 THR n 
1 243 GLN n 
1 244 ALA n 
1 245 GLN n 
1 246 ASP n 
1 247 THR n 
1 248 ASN n 
1 249 TYR n 
1 250 THR n 
1 251 LEU n 
1 252 SER n 
1 253 THR n 
1 254 ILE n 
1 255 SER n 
1 256 MET n 
1 257 SER n 
1 258 THR n 
1 259 THR n 
1 260 PRO n 
1 261 SER n 
1 262 THR n 
1 263 VAL n 
1 264 THR n 
1 265 VAL n 
1 266 PRO n 
1 267 THR n 
1 268 TRP n 
1 269 SER n 
1 270 PHE n 
1 271 PRO n 
1 272 GLY n 
1 273 ALA n 
1 274 CYS n 
1 275 ALA n 
1 276 PHE n 
1 277 GLN n 
1 278 VAL n 
1 279 GLN n 
1 280 GLU n 
1 281 GLY n 
1 282 ARG n 
1 283 VAL n 
1 284 VAL n 
1 285 VAL n 
1 286 GLN n 
1 287 ILE n 
1 288 GLY n 
1 289 ASP n 
1 290 TYR n 
1 291 ALA n 
1 292 ALA n 
1 293 THR n 
1 294 GLU n 
1 295 LEU n 
1 296 GLY n 
1 297 SER n 
1 298 GLY n 
1 299 ASP n 
1 300 VAL n 
1 301 ALA n 
1 302 PHE n 
1 303 ILE n 
1 304 PRO n 
1 305 GLY n 
1 306 GLY n 
1 307 VAL n 
1 308 GLU n 
1 309 PHE n 
1 310 LYS n 
1 311 TYR n 
1 312 TYR n 
1 313 SER n 
1 314 GLU n 
1 315 ALA n 
1 316 TYR n 
1 317 PHE n 
1 318 SER n 
1 319 LYS n 
1 320 VAL n 
1 321 LEU n 
1 322 PHE n 
1 323 VAL n 
1 324 SER n 
1 325 SER n 
1 326 GLY n 
1 327 SER n 
1 328 ASP n 
1 329 GLY n 
1 330 LEU n 
1 331 ASP n 
1 332 GLN n 
1 333 ASN n 
1 334 LEU n 
1 335 VAL n 
1 336 ASN n 
1 337 GLY n 
1 338 GLY n 
1 339 GLU n 
1 340 GLU n 
1 341 TRP n 
1 342 SER n 
1 343 SER n 
1 344 VAL n 
1 345 SER n 
1 346 PHE n 
1 347 PRO n 
1 348 ALA n 
1 349 ASP n 
1 350 TRP n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      ? 
_entity_src_gen.pdbx_beg_seq_num                   ? 
_entity_src_gen.pdbx_end_seq_num                   ? 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_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      'ASPERGILLUS JAPONICUS' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     34381 
_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      'ASPERGILLUS AWAMORI' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     105351 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    QDOI_ASPJA 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   ? 
_struct_ref.pdbx_align_begin           ? 
_struct_ref.pdbx_db_accession          Q7SIC2 
_struct_ref.pdbx_db_isoform            ? 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 1H1M A 1 ? 350 ? Q7SIC2 1 ? 350 ? 1 350 
2 1 1H1M B 1 ? 350 ? Q7SIC2 1 ? 350 ? 1 350 
3 1 1H1M C 1 ? 350 ? Q7SIC2 1 ? 350 ? 1 350 
4 1 1H1M D 1 ? 350 ? Q7SIC2 1 ? 350 ? 1 350 
# 
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 
BMA D-saccharide        . BETA-D-MANNOSE                                          ?          'C6 H12 O6'      180.156 
CU  non-polymer         . 'COPPER (II) ION'                                       ?          'Cu 2'           63.546  
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 
KMP non-polymer         . '3,5,7-TRIHYDROXY-2-(4-HYDROXYPHENYL)-4H-CHROMEN-4-ONE' KAEMPHEROL 'C15 H10 O6'     286.236 
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 
MAN D-saccharide        . ALPHA-D-MANNOSE                                         ?          'C6 H12 O6'      180.156 
MET 'L-peptide linking' y METHIONINE                                              ?          'C5 H11 N O2 S'  149.211 
MPD non-polymer         . '(4S)-2-METHYL-2,4-PENTANEDIOL'                         ?          'C6 H14 O2'      118.174 
NAG D-saccharide        . N-ACETYL-D-GLUCOSAMINE                                  ?          'C8 H15 N O6'    221.208 
PHE 'L-peptide linking' y PHENYLALANINE                                           ?          'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE                                                 ?          'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE                                                  ?          'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE                                               ?          'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                              ?          'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE                                                ?          'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE                                                  ?          'C5 H11 N O2'    117.146 
# 
_exptl.entry_id          1H1M 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.32 
_exptl_crystal.density_percent_sol   46.5 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          ? 
_exptl_crystal_grow.temp            ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              5.20 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.pdbx_details    'HANGING DROP, 21-23% PEG 8000, 200 MM AMMONIUM SULFATE, 100 MM CITRATE BUFFER, PH 5.2' 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100.0 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               'IMAGE PLATE' 
_diffrn_detector.type                   MARRESEARCH 
_diffrn_detector.pdbx_collection_date   ? 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.033 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'ESRF BEAMLINE BM14' 
_diffrn_source.pdbx_synchrotron_site       ESRF 
_diffrn_source.pdbx_synchrotron_beamline   BM14 
_diffrn_source.pdbx_wavelength             1.033 
_diffrn_source.pdbx_wavelength_list        ? 
# 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.entry_id                     1H1M 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             50.000 
_reflns.d_resolution_high            1.900 
_reflns.number_obs                   111775 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         96.7 
_reflns.pdbx_Rmerge_I_obs            0.08500 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        12.0000 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              2.400 
# 
_reflns_shell.pdbx_diffrn_id         1 
_reflns_shell.pdbx_ordinal           1 
_reflns_shell.d_res_high             1.90 
_reflns_shell.d_res_low              1.94 
_reflns_shell.percent_possible_all   94.8 
_reflns_shell.Rmerge_I_obs           0.38000 
_reflns_shell.pdbx_Rsym_value        ? 
_reflns_shell.meanI_over_sigI_obs    2.900 
_reflns_shell.pdbx_redundancy        2.25 
# 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.entry_id                                 1H1M 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               'LIKELY RESIDUAL' 
_refine.ls_number_reflns_obs                     106147 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             49.39 
_refine.ls_d_res_high                            1.90 
_refine.ls_percent_reflns_obs                    96.5 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.154 
_refine.ls_R_factor_R_free                       0.204 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.000 
_refine.ls_number_reflns_R_free                  5608 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.964 
_refine.correlation_coeff_Fo_to_Fc_free          0.938 
_refine.B_iso_mean                               12.83 
_refine.aniso_B[1][1]                            1.21000 
_refine.aniso_B[2][2]                            0.60000 
_refine.aniso_B[3][3]                            -1.69000 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            0.39000 
_refine.aniso_B[2][3]                            0.00000 
_refine.solvent_model_details                    'BABINET MODEL PLUS MASK' 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             1.40 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          OTHER 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       0.144 
_refine.pdbx_overall_ESU_R_Free                  0.138 
_refine.overall_SU_ML                            0.093 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             3.219 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_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        10568 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         491 
_refine_hist.number_atoms_solvent             1547 
_refine_hist.number_atoms_total               12606 
_refine_hist.d_res_high                       1.90 
_refine_hist.d_res_low                        49.39 
# 
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 
r_bond_refined_d             0.019 0.021 ? 11466 'X-RAY DIFFRACTION' ? 
r_bond_other_d               ?     ?     ? ?     'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          ?     ?     ? ?     'X-RAY DIFFRACTION' ? 
r_angle_other_deg            1.740 1.969 ? 15770 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       6.794 5.000 ? 1366  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       ?     ?     ? ?     'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       ?     ?     ? ?     'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       ?     ?     ? ?     'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.124 0.200 ? 1772  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.009 0.020 ? 8832  'X-RAY DIFFRACTION' ? 
r_gen_planes_other           ?     ?     ? ?     'X-RAY DIFFRACTION' ? 
r_nbd_refined                0.214 0.200 ? 5556  'X-RAY DIFFRACTION' ? 
r_nbd_other                  ?     ?     ? ?     'X-RAY DIFFRACTION' ? 
r_nbtor_refined              ?     ?     ? ?     'X-RAY DIFFRACTION' ? 
r_nbtor_other                ?     ?     ? ?     'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_refined        0.139 0.200 ? 1395  'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_other          ?     ?     ? ?     'X-RAY DIFFRACTION' ? 
r_metal_ion_refined          0.062 0.200 ? 5     'X-RAY DIFFRACTION' ? 
r_metal_ion_other            ?     ?     ? ?     'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_refined       0.197 0.200 ? 216   'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_other         ?     ?     ? ?     'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_refined     0.151 0.200 ? 90    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_other       ?     ?     ? ?     'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_refined ?     ?     ? ?     'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_other   ?     ?     ? ?     'X-RAY DIFFRACTION' ? 
r_mcbond_it                  0.940 1.500 ? 6830  'X-RAY DIFFRACTION' ? 
r_mcbond_other               ?     ?     ? ?     'X-RAY DIFFRACTION' ? 
r_mcangle_it                 1.500 2.000 ? 11093 'X-RAY DIFFRACTION' ? 
r_mcangle_other              ?     ?     ? ?     'X-RAY DIFFRACTION' ? 
r_scbond_it                  2.692 3.000 ? 4617  'X-RAY DIFFRACTION' ? 
r_scbond_other               ?     ?     ? ?     'X-RAY DIFFRACTION' ? 
r_scangle_it                 3.989 4.500 ? 4636  'X-RAY DIFFRACTION' ? 
r_scangle_other              ?     ?     ? ?     'X-RAY DIFFRACTION' ? 
r_long_range_B_refined       ?     ?     ? ?     'X-RAY DIFFRACTION' ? 
r_long_range_B_other         ?     ?     ? ?     'X-RAY DIFFRACTION' ? 
r_rigid_bond_restr           ?     ?     ? ?     'X-RAY DIFFRACTION' ? 
r_sphericity_free            ?     ?     ? ?     'X-RAY DIFFRACTION' ? 
r_sphericity_bonded          ?     ?     ? ?     'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.d_res_high                       1.90 
_refine_ls_shell.d_res_low                        1.95 
_refine_ls_shell.number_reflns_R_work             7450 
_refine_ls_shell.R_factor_R_work                  0.2160 
_refine_ls_shell.percent_reflns_obs               ? 
_refine_ls_shell.R_factor_R_free                  0.2710 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             434 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
# 
_struct.entry_id                  1H1M 
_struct.title                     
'CRYSTAL STRUCTURE OF QUERCETIN 2,3-DIOXYGENASE ANAEROBICALLY COMPLEXED WITH THE SUBSTRATE KAEMPFEROL' 
_struct.pdbx_descriptor           'QUERCETIN 2,3-DIOXYGENASE (E.C.1.13.11.24)' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        1H1M 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
_struct_keywords.text            'OXIDOREDUCTASE, DIOXYGENASE, FLAVONOL' 
# 
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 1 ? 
C  N N 1 ? 
D  N N 1 ? 
E  N N 2 ? 
F  N N 2 ? 
G  N N 2 ? 
H  N N 3 ? 
I  N N 4 ? 
J  N N 4 ? 
K  N N 2 ? 
L  N N 2 ? 
M  N N 2 ? 
N  N N 5 ? 
O  N N 6 ? 
P  N N 7 ? 
Q  N N 2 ? 
R  N N 2 ? 
S  N N 2 ? 
T  N N 3 ? 
U  N N 4 ? 
V  N N 2 ? 
W  N N 2 ? 
X  N N 5 ? 
Y  N N 6 ? 
Z  N N 7 ? 
AA N N 7 ? 
BA N N 2 ? 
CA N N 2 ? 
DA N N 2 ? 
EA N N 3 ? 
FA N N 4 ? 
GA N N 2 ? 
HA N N 2 ? 
IA N N 5 ? 
JA N N 6 ? 
KA N N 7 ? 
LA N N 2 ? 
MA N N 2 ? 
NA N N 2 ? 
OA N N 2 ? 
PA N N 2 ? 
QA N N 5 ? 
RA N N 6 ? 
SA N N 8 ? 
TA N N 8 ? 
UA N N 8 ? 
VA N N 8 ? 
# 
_struct_biol.id   1 
# 
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  THR A 40  ? GLY A 45  ? THR A 40  GLY A 45  1 ? 6  
HELX_P HELX_P2  2  GLU A 133 ? GLY A 140 ? GLU A 133 GLY A 140 1 ? 8  
HELX_P HELX_P3  3  ASP A 165 ? SER A 170 ? ASP A 165 SER A 170 1 ? 6  
HELX_P HELX_P4  4  THR A 171 ? ASP A 176 ? THR A 171 ASP A 176 5 ? 6  
HELX_P HELX_P5  5  THR A 240 ? GLN A 245 ? THR A 240 GLN A 245 1 ? 6  
HELX_P HELX_P6  6  GLY A 329 ? GLY A 338 ? GLY A 329 GLY A 338 1 ? 10 
HELX_P HELX_P7  7  THR B 40  ? GLY B 45  ? THR B 40  GLY B 45  1 ? 6  
HELX_P HELX_P8  8  GLU B 133 ? GLY B 140 ? GLU B 133 GLY B 140 1 ? 8  
HELX_P HELX_P9  9  ASP B 165 ? SER B 170 ? ASP B 165 SER B 170 1 ? 6  
HELX_P HELX_P10 10 THR B 171 ? ASP B 176 ? THR B 171 ASP B 176 5 ? 6  
HELX_P HELX_P11 11 THR B 240 ? GLN B 245 ? THR B 240 GLN B 245 1 ? 6  
HELX_P HELX_P12 12 GLY B 329 ? GLY B 337 ? GLY B 329 GLY B 337 1 ? 9  
HELX_P HELX_P13 13 THR C 40  ? GLY C 45  ? THR C 40  GLY C 45  1 ? 6  
HELX_P HELX_P14 14 GLU C 133 ? GLY C 140 ? GLU C 133 GLY C 140 1 ? 8  
HELX_P HELX_P15 15 ASP C 165 ? SER C 170 ? ASP C 165 SER C 170 1 ? 6  
HELX_P HELX_P16 16 THR C 171 ? ASP C 176 ? THR C 171 ASP C 176 5 ? 6  
HELX_P HELX_P17 17 THR C 240 ? GLN C 245 ? THR C 240 GLN C 245 1 ? 6  
HELX_P HELX_P18 18 GLY C 329 ? GLY C 337 ? GLY C 329 GLY C 337 1 ? 9  
HELX_P HELX_P19 19 THR D 40  ? GLY D 45  ? THR D 40  GLY D 45  1 ? 6  
HELX_P HELX_P20 20 GLU D 133 ? GLY D 140 ? GLU D 133 GLY D 140 1 ? 8  
HELX_P HELX_P21 21 ASP D 165 ? SER D 170 ? ASP D 165 SER D 170 1 ? 6  
HELX_P HELX_P22 22 LEU D 172 ? ASP D 176 ? LEU D 172 ASP D 176 5 ? 5  
HELX_P HELX_P23 23 THR D 240 ? GLN D 245 ? THR D 240 GLN D 245 1 ? 6  
HELX_P HELX_P24 24 GLY D 329 ? GLY D 337 ? GLY D 329 GLY D 337 1 ? 9  
# 
_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  ASN 90  ND2 ? ? ? 1_555 L  NAG .   C1  ? ? A ASN 90   A NAG 1355 1_555 ? ? ? ? ? ? ? 1.448 ? 
covale2  covale ? ? A  ASN 109 ND2 ? ? ? 1_555 E  NAG .   C1  ? ? A ASN 109  A NAG 1351 1_555 ? ? ? ? ? ? ? 1.442 ? 
covale3  covale ? ? A  ASN 142 ND2 ? ? ? 1_555 M  NAG .   C1  ? ? A ASN 142  A NAG 1356 1_555 ? ? ? ? ? ? ? 1.456 ? 
covale4  covale ? ? A  ASN 191 ND2 ? ? ? 1_555 F  NAG .   C1  ? ? A ASN 191  A NAG 1352 1_555 ? ? ? ? ? ? ? 1.447 ? 
covale5  covale ? ? A  ASN 248 ND2 ? ? ? 1_555 K  NAG .   C1  ? ? A ASN 248  A NAG 1354 1_555 ? ? ? ? ? ? ? 1.437 ? 
covale6  covale ? ? F  NAG .   O4  ? ? ? 1_555 G  NAG .   C1  ? ? A NAG 1352 A NAG 1353 1_555 ? ? ? ? ? ? ? 1.445 ? 
covale7  covale ? ? G  NAG .   O4  ? ? ? 1_555 H  BMA .   C1  ? ? A NAG 1353 A BMA 1357 1_555 ? ? ? ? ? ? ? 1.434 ? 
covale8  covale ? ? H  BMA .   O6  ? ? ? 1_555 I  MAN .   C1  ? ? A BMA 1357 A MAN 1358 1_555 ? ? ? ? ? ? ? 1.440 ? 
covale9  covale ? ? I  MAN .   O3  ? ? ? 1_555 J  MAN .   C1  ? ? A MAN 1358 A MAN 1359 1_555 ? ? ? ? ? ? ? 1.437 ? 
metalc1  metalc ? ? N  KMP .   O27 ? ? ? 1_555 O  CU  .   CU  ? ? A KMP 1360 A CU  1361 1_555 ? ? ? ? ? ? ? 1.986 ? 
metalc2  metalc ? ? O  CU  .   CU  ? ? ? 1_555 A  HIS 112 NE2 ? ? A CU  1361 A HIS 112  1_555 ? ? ? ? ? ? ? 2.051 ? 
metalc3  metalc ? ? O  CU  .   CU  ? ? ? 1_555 A  HIS 66  NE2 ? ? A CU  1361 A HIS 66   1_555 ? ? ? ? ? ? ? 2.078 ? 
metalc4  metalc ? ? O  CU  .   CU  ? ? ? 1_555 A  GLU 73  OE1 ? ? A CU  1361 A GLU 73   1_555 ? ? ? ? ? ? ? 2.053 ? 
metalc5  metalc ? ? O  CU  .   CU  ? ? ? 1_555 A  HIS 68  NE2 ? ? A CU  1361 A HIS 68   1_555 ? ? ? ? ? ? ? 2.091 ? 
covale10 covale ? ? B  ASN 109 ND2 ? ? ? 1_555 Q  NAG .   C1  ? ? B ASN 109  B NAG 1351 1_555 ? ? ? ? ? ? ? 1.443 ? 
covale11 covale ? ? B  ASN 142 ND2 ? ? ? 1_555 W  NAG .   C1  ? ? B ASN 142  B NAG 1355 1_555 ? ? ? ? ? ? ? 1.441 ? 
covale12 covale ? ? B  ASN 191 ND2 ? ? ? 1_555 R  NAG .   C1  ? ? B ASN 191  B NAG 1352 1_555 ? ? ? ? ? ? ? 1.449 ? 
covale13 covale ? ? B  ASN 248 ND2 ? ? ? 1_555 V  NAG .   C1  ? ? B ASN 248  B NAG 1354 1_555 ? ? ? ? ? ? ? 1.455 ? 
covale14 covale ? ? R  NAG .   O4  ? ? ? 1_555 S  NAG .   C1  ? ? B NAG 1352 B NAG 1353 1_555 ? ? ? ? ? ? ? 1.442 ? 
covale15 covale ? ? S  NAG .   O4  ? ? ? 1_555 T  BMA .   C1  ? ? B NAG 1353 B BMA 1356 1_555 ? ? ? ? ? ? ? 1.446 ? 
covale16 covale ? ? T  BMA .   O6  ? ? ? 1_555 U  MAN .   C1  ? ? B BMA 1356 B MAN 1357 1_555 ? ? ? ? ? ? ? 1.453 ? 
metalc6  metalc ? ? Y  CU  .   CU  ? ? ? 1_555 X  KMP .   O27 ? ? B CU  1359 B KMP 1358 1_555 ? ? ? ? ? ? ? 2.153 ? 
metalc7  metalc ? ? Y  CU  .   CU  ? ? ? 1_555 B  HIS 112 NE2 ? ? B CU  1359 B HIS 112  1_555 ? ? ? ? ? ? ? 2.093 ? 
metalc8  metalc ? ? Y  CU  .   CU  ? ? ? 1_555 B  HIS 68  NE2 ? ? B CU  1359 B HIS 68   1_555 ? ? ? ? ? ? ? 2.125 ? 
metalc9  metalc ? ? Y  CU  .   CU  ? ? ? 1_555 B  HIS 66  NE2 ? ? B CU  1359 B HIS 66   1_555 ? ? ? ? ? ? ? 2.029 ? 
metalc10 metalc ? ? Y  CU  .   CU  ? ? ? 1_555 B  GLU 73  OE1 ? ? B CU  1359 B GLU 73   1_555 ? ? ? ? ? ? ? 1.906 ? 
covale17 covale ? ? C  ASN 109 ND2 ? ? ? 1_555 BA NAG .   C1  ? ? C ASN 109  C NAG 1351 1_555 ? ? ? ? ? ? ? 1.442 ? 
covale18 covale ? ? C  ASN 142 ND2 ? ? ? 1_555 HA NAG .   C1  ? ? C ASN 142  C NAG 1355 1_555 ? ? ? ? ? ? ? 1.427 ? 
covale19 covale ? ? C  ASN 191 ND2 ? ? ? 1_555 CA NAG .   C1  ? ? C ASN 191  C NAG 1352 1_555 ? ? ? ? ? ? ? 1.438 ? 
covale20 covale ? ? C  ASN 248 ND2 ? ? ? 1_555 GA NAG .   C1  ? ? C ASN 248  C NAG 1354 1_555 ? ? ? ? ? ? ? 1.448 ? 
covale21 covale ? ? CA NAG .   O4  ? ? ? 1_555 DA NAG .   C1  ? ? C NAG 1352 C NAG 1353 1_555 ? ? ? ? ? ? ? 1.429 ? 
covale22 covale ? ? DA NAG .   O4  ? ? ? 1_555 EA BMA .   C1  ? ? C NAG 1353 C BMA 1356 1_555 ? ? ? ? ? ? ? 1.426 ? 
covale23 covale ? ? EA BMA .   O6  ? ? ? 1_555 FA MAN .   C1  ? ? C BMA 1356 C MAN 1357 1_555 ? ? ? ? ? ? ? 1.448 ? 
metalc11 metalc ? ? JA CU  .   CU  ? ? ? 1_555 C  HIS 112 NE2 ? ? C CU  1359 C HIS 112  1_555 ? ? ? ? ? ? ? 2.066 ? 
metalc12 metalc ? ? JA CU  .   CU  ? ? ? 1_555 C  HIS 68  NE2 ? ? C CU  1359 C HIS 68   1_555 ? ? ? ? ? ? ? 2.103 ? 
metalc13 metalc ? ? JA CU  .   CU  ? ? ? 1_555 IA KMP .   O27 ? ? C CU  1359 C KMP 1358 1_555 ? ? ? ? ? ? ? 2.112 ? 
metalc14 metalc ? ? JA CU  .   CU  ? ? ? 1_555 C  GLU 73  OE1 ? ? C CU  1359 C GLU 73   1_555 ? ? ? ? ? ? ? 2.009 ? 
metalc15 metalc ? ? JA CU  .   CU  ? ? ? 1_555 C  HIS 66  NE2 ? ? C CU  1359 C HIS 66   1_555 ? ? ? ? ? ? ? 1.921 ? 
covale24 covale ? ? D  ASN 109 ND2 B ? ? 1_555 LA NAG .   C1  ? ? D ASN 109  D NAG 1351 1_555 ? ? ? ? ? ? ? 1.477 ? 
covale25 covale ? ? D  ASN 109 ND2 A ? ? 1_555 LA NAG .   C1  ? ? D ASN 109  D NAG 1351 1_555 ? ? ? ? ? ? ? 1.416 ? 
covale26 covale ? ? D  ASN 142 ND2 ? ? ? 1_555 OA NAG .   C1  ? ? D ASN 142  D NAG 1354 1_555 ? ? ? ? ? ? ? 1.465 ? 
covale27 covale ? ? D  ASN 191 ND2 ? ? ? 1_555 MA NAG .   C1  ? ? D ASN 191  D NAG 1352 1_555 ? ? ? ? ? ? ? 1.430 ? 
covale28 covale ? ? D  ASN 248 ND2 ? ? ? 1_555 PA NAG .   C1  ? ? D ASN 248  D NAG 1355 1_555 ? ? ? ? ? ? ? 1.452 ? 
covale29 covale ? ? MA NAG .   O4  ? ? ? 1_555 NA NAG .   C1  ? ? D NAG 1352 D NAG 1353 1_555 ? ? ? ? ? ? ? 1.429 ? 
metalc16 metalc ? ? RA CU  .   CU  ? ? ? 1_555 QA KMP .   O27 ? ? D CU  1357 D KMP 1356 1_555 ? ? ? ? ? ? ? 2.090 ? 
metalc17 metalc ? ? RA CU  .   CU  ? ? ? 1_555 D  HIS 66  NE2 ? ? D CU  1357 D HIS 66   1_555 ? ? ? ? ? ? ? 2.017 ? 
metalc18 metalc ? ? RA CU  .   CU  ? ? ? 1_555 D  HIS 112 NE2 ? ? D CU  1357 D HIS 112  1_555 ? ? ? ? ? ? ? 2.098 ? 
metalc19 metalc ? ? RA CU  .   CU  ? ? ? 1_555 D  GLU 73  OE1 ? ? D CU  1357 D GLU 73   1_555 ? ? ? ? ? ? ? 2.197 ? 
metalc20 metalc ? ? RA CU  .   CU  ? ? ? 1_555 D  HIS 68  NE2 ? ? D CU  1357 D HIS 68   1_555 ? ? ? ? ? ? ? 2.247 ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
covale ? ? 
metalc ? ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 VAL 128 A . ? VAL 128 A PRO 129 A ? PRO 129 A 1 -2.41 
2 ALA 194 A . ? ALA 194 A PRO 195 A ? PRO 195 A 1 -1.38 
3 VAL 128 B . ? VAL 128 B PRO 129 B ? PRO 129 B 1 -3.12 
4 ALA 194 B . ? ALA 194 B PRO 195 B ? PRO 195 B 1 -2.09 
5 VAL 128 C . ? VAL 128 C PRO 129 C ? PRO 129 C 1 -4.59 
6 ALA 194 C . ? ALA 194 C PRO 195 C ? PRO 195 C 1 3.67  
7 VAL 128 D . ? VAL 128 D PRO 129 D ? PRO 129 D 1 -2.66 
8 ALA 194 D . ? ALA 194 D PRO 195 D ? PRO 195 D 1 1.97  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA ? 8 ? 
AB ? 8 ? 
AC ? 2 ? 
AD ? 4 ? 
AE ? 3 ? 
BA ? 9 ? 
BB ? 8 ? 
BC ? 2 ? 
BD ? 4 ? 
BE ? 3 ? 
CA ? 8 ? 
CB ? 8 ? 
CC ? 2 ? 
CD ? 4 ? 
CE ? 3 ? 
DA ? 8 ? 
DB ? 8 ? 
DC ? 2 ? 
DD ? 4 ? 
DE ? 3 ? 
# 
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 
AA 1 2 ? anti-parallel 
AA 2 3 ? anti-parallel 
AA 3 4 ? anti-parallel 
AA 4 5 ? anti-parallel 
AA 5 6 ? anti-parallel 
AA 6 7 ? anti-parallel 
AA 7 8 ? anti-parallel 
AB 1 2 ? anti-parallel 
AB 2 3 ? anti-parallel 
AB 3 4 ? anti-parallel 
AB 4 5 ? anti-parallel 
AB 5 6 ? anti-parallel 
AB 6 7 ? anti-parallel 
AB 7 8 ? anti-parallel 
AC 1 2 ? anti-parallel 
AD 1 2 ? anti-parallel 
AD 2 3 ? anti-parallel 
AD 3 4 ? anti-parallel 
AE 1 2 ? anti-parallel 
AE 2 3 ? anti-parallel 
BA 1 2 ? parallel      
BA 2 3 ? anti-parallel 
BA 3 4 ? anti-parallel 
BA 4 5 ? anti-parallel 
BA 5 6 ? anti-parallel 
BA 6 7 ? anti-parallel 
BA 7 8 ? anti-parallel 
BA 8 9 ? anti-parallel 
BB 1 2 ? anti-parallel 
BB 2 3 ? anti-parallel 
BB 3 4 ? anti-parallel 
BB 4 5 ? anti-parallel 
BB 5 6 ? anti-parallel 
BB 6 7 ? anti-parallel 
BB 7 8 ? anti-parallel 
BC 1 2 ? anti-parallel 
BD 1 2 ? anti-parallel 
BD 2 3 ? anti-parallel 
BD 3 4 ? anti-parallel 
BE 1 2 ? anti-parallel 
BE 2 3 ? anti-parallel 
CA 1 2 ? anti-parallel 
CA 2 3 ? anti-parallel 
CA 3 4 ? anti-parallel 
CA 4 5 ? anti-parallel 
CA 5 6 ? anti-parallel 
CA 6 7 ? anti-parallel 
CA 7 8 ? anti-parallel 
CB 1 2 ? anti-parallel 
CB 2 3 ? anti-parallel 
CB 3 4 ? anti-parallel 
CB 4 5 ? anti-parallel 
CB 5 6 ? anti-parallel 
CB 6 7 ? anti-parallel 
CB 7 8 ? anti-parallel 
CC 1 2 ? anti-parallel 
CD 1 2 ? anti-parallel 
CD 2 3 ? anti-parallel 
CD 3 4 ? anti-parallel 
CE 1 2 ? anti-parallel 
CE 2 3 ? anti-parallel 
DA 1 2 ? anti-parallel 
DA 2 3 ? anti-parallel 
DA 3 4 ? anti-parallel 
DA 4 5 ? anti-parallel 
DA 5 6 ? anti-parallel 
DA 6 7 ? anti-parallel 
DA 7 8 ? anti-parallel 
DB 1 2 ? anti-parallel 
DB 2 3 ? anti-parallel 
DB 3 4 ? anti-parallel 
DB 4 5 ? anti-parallel 
DB 5 6 ? anti-parallel 
DB 6 7 ? anti-parallel 
DB 7 8 ? anti-parallel 
DC 1 2 ? anti-parallel 
DD 1 2 ? anti-parallel 
DD 2 3 ? anti-parallel 
DD 3 4 ? anti-parallel 
DE 1 2 ? anti-parallel 
DE 2 3 ? 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 
AA 1 TYR A 17  ? ILE A 19  ? TYR A 17  ILE A 19  
AA 2 VAL A 300 ? ILE A 303 ? VAL A 300 ILE A 303 
AA 3 CYS A 274 ? GLU A 280 ? CYS A 274 GLU A 280 
AA 4 SER A 318 ? SER A 325 ? SER A 318 SER A 325 
AA 5 TYR A 249 ? MET A 256 ? TYR A 249 MET A 256 
AA 6 GLN A 233 ? VAL A 239 ? GLN A 233 VAL A 239 
AA 7 LYS A 224 ? ASN A 227 ? LYS A 224 ASN A 227 
AA 8 GLU A 339 ? TRP A 341 ? GLU A 339 TRP A 341 
AB 1 THR A 141 ? ASN A 142 ? THR A 141 ASN A 142 
AB 2 VAL A 28  ? VAL A 30  ? VAL A 28  VAL A 30  
AB 3 GLN A 33  ? VAL A 39  ? GLN A 33  VAL A 39  
AB 4 THR A 49  ? ALA A 55  ? THR A 49  ALA A 55  
AB 5 THR A 121 ? VAL A 128 ? THR A 121 VAL A 128 
AB 6 TYR A 72  ? LYS A 79  ? TYR A 72  LYS A 79  
AB 7 TYR A 103 ? VAL A 106 ? TYR A 103 VAL A 106 
AB 8 TYR A 215 ? ILE A 217 ? TYR A 215 ILE A 217 
AC 1 HIS A 66  ? ILE A 67  ? HIS A 66  ILE A 67  
AC 2 TYR A 178 ? ALA A 179 ? TYR A 178 ALA A 179 
AD 1 THR A 111 ? ILE A 116 ? THR A 111 ILE A 116 
AD 2 SER A 81  ? GLN A 87  ? SER A 81  GLN A 87  
AD 3 GLN A 94  ? SER A 99  ? GLN A 94  SER A 99  
AD 4 THR A 193 ? ALA A 194 ? THR A 193 ALA A 194 
AE 1 THR A 293 ? LEU A 295 ? THR A 293 LEU A 295 
AE 2 VAL A 283 ? ILE A 287 ? VAL A 283 ILE A 287 
AE 3 PHE A 309 ? SER A 313 ? PHE A 309 SER A 313 
BA 1 ILE B 6   ? VAL B 7   ? ILE B 6   VAL B 7   
BA 2 TYR B 17  ? ILE B 19  ? TYR B 17  ILE B 19  
BA 3 VAL B 300 ? ILE B 303 ? VAL B 300 ILE B 303 
BA 4 CYS B 274 ? GLU B 280 ? CYS B 274 GLU B 280 
BA 5 SER B 318 ? SER B 325 ? SER B 318 SER B 325 
BA 6 TYR B 249 ? MET B 256 ? TYR B 249 MET B 256 
BA 7 GLN B 233 ? VAL B 239 ? GLN B 233 VAL B 239 
BA 8 LYS B 224 ? ASN B 227 ? LYS B 224 ASN B 227 
BA 9 GLU B 339 ? TRP B 341 ? GLU B 339 TRP B 341 
BB 1 THR B 141 ? ASN B 142 ? THR B 141 ASN B 142 
BB 2 VAL B 28  ? VAL B 30  ? VAL B 28  VAL B 30  
BB 3 GLN B 33  ? VAL B 39  ? GLN B 33  VAL B 39  
BB 4 THR B 49  ? ALA B 55  ? THR B 49  ALA B 55  
BB 5 THR B 121 ? VAL B 128 ? THR B 121 VAL B 128 
BB 6 TYR B 72  ? LYS B 79  ? TYR B 72  LYS B 79  
BB 7 TYR B 103 ? VAL B 106 ? TYR B 103 VAL B 106 
BB 8 TYR B 215 ? ILE B 217 ? TYR B 215 ILE B 217 
BC 1 HIS B 66  ? ILE B 67  ? HIS B 66  ILE B 67  
BC 2 TYR B 178 ? ALA B 179 ? TYR B 178 ALA B 179 
BD 1 THR B 111 ? ILE B 116 ? THR B 111 ILE B 116 
BD 2 SER B 81  ? GLN B 87  ? SER B 81  GLN B 87  
BD 3 GLN B 94  ? SER B 99  ? GLN B 94  SER B 99  
BD 4 THR B 193 ? ALA B 194 ? THR B 193 ALA B 194 
BE 1 THR B 293 ? LEU B 295 ? THR B 293 LEU B 295 
BE 2 VAL B 283 ? ILE B 287 ? VAL B 283 ILE B 287 
BE 3 PHE B 309 ? SER B 313 ? PHE B 309 SER B 313 
CA 1 TYR C 17  ? ILE C 19  ? TYR C 17  ILE C 19  
CA 2 VAL C 300 ? ILE C 303 ? VAL C 300 ILE C 303 
CA 3 CYS C 274 ? GLU C 280 ? CYS C 274 GLU C 280 
CA 4 SER C 318 ? SER C 325 ? SER C 318 SER C 325 
CA 5 TYR C 249 ? MET C 256 ? TYR C 249 MET C 256 
CA 6 GLN C 233 ? VAL C 239 ? GLN C 233 VAL C 239 
CA 7 LYS C 224 ? ASN C 227 ? LYS C 224 ASN C 227 
CA 8 GLU C 339 ? TRP C 341 ? GLU C 339 TRP C 341 
CB 1 THR C 141 ? ASN C 142 ? THR C 141 ASN C 142 
CB 2 VAL C 28  ? VAL C 30  ? VAL C 28  VAL C 30  
CB 3 GLN C 33  ? VAL C 39  ? GLN C 33  VAL C 39  
CB 4 THR C 49  ? ALA C 55  ? THR C 49  ALA C 55  
CB 5 THR C 121 ? VAL C 128 ? THR C 121 VAL C 128 
CB 6 TYR C 72  ? LYS C 79  ? TYR C 72  LYS C 79  
CB 7 TYR C 103 ? VAL C 106 ? TYR C 103 VAL C 106 
CB 8 TYR C 215 ? ILE C 217 ? TYR C 215 ILE C 217 
CC 1 HIS C 66  ? ILE C 67  ? HIS C 66  ILE C 67  
CC 2 TYR C 178 ? ALA C 179 ? TYR C 178 ALA C 179 
CD 1 VAL C 110 ? ILE C 116 ? VAL C 110 ILE C 116 
CD 2 SER C 81  ? SER C 88  ? SER C 81  SER C 88  
CD 3 GLN C 94  ? SER C 99  ? GLN C 94  SER C 99  
CD 4 THR C 193 ? ALA C 194 ? THR C 193 ALA C 194 
CE 1 THR C 293 ? LEU C 295 ? THR C 293 LEU C 295 
CE 2 VAL C 283 ? ILE C 287 ? VAL C 283 ILE C 287 
CE 3 PHE C 309 ? SER C 313 ? PHE C 309 SER C 313 
DA 1 TYR D 17  ? ILE D 19  ? TYR D 17  ILE D 19  
DA 2 VAL D 300 ? ILE D 303 ? VAL D 300 ILE D 303 
DA 3 CYS D 274 ? GLU D 280 ? CYS D 274 GLU D 280 
DA 4 SER D 318 ? SER D 325 ? SER D 318 SER D 325 
DA 5 TYR D 249 ? MET D 256 ? TYR D 249 MET D 256 
DA 6 GLN D 233 ? VAL D 239 ? GLN D 233 VAL D 239 
DA 7 LYS D 224 ? ASN D 227 ? LYS D 224 ASN D 227 
DA 8 GLU D 339 ? TRP D 341 ? GLU D 339 TRP D 341 
DB 1 THR D 141 ? ASN D 142 ? THR D 141 ASN D 142 
DB 2 VAL D 28  ? VAL D 30  ? VAL D 28  VAL D 30  
DB 3 GLN D 33  ? VAL D 39  ? GLN D 33  VAL D 39  
DB 4 THR D 49  ? ALA D 55  ? THR D 49  ALA D 55  
DB 5 THR D 121 ? VAL D 128 ? THR D 121 VAL D 128 
DB 6 TYR D 72  ? LYS D 79  ? TYR D 72  LYS D 79  
DB 7 TYR D 103 ? VAL D 106 ? TYR D 103 VAL D 106 
DB 8 TYR D 215 ? ILE D 217 ? TYR D 215 ILE D 217 
DC 1 HIS D 66  ? ILE D 67  ? HIS D 66  ILE D 67  
DC 2 TYR D 178 ? ALA D 179 ? TYR D 178 ALA D 179 
DD 1 THR D 111 ? ILE D 116 ? THR D 111 ILE D 116 
DD 2 PHE D 82  ? GLN D 87  ? PHE D 82  GLN D 87  
DD 3 GLN D 94  ? LEU D 98  ? GLN D 94  LEU D 98  
DD 4 THR D 193 ? ALA D 194 ? THR D 193 ALA D 194 
DE 1 THR D 293 ? LEU D 295 ? THR D 293 LEU D 295 
DE 2 VAL D 283 ? ILE D 287 ? VAL D 283 ILE D 287 
DE 3 PHE D 309 ? SER D 313 ? PHE D 309 SER D 313 
# 
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 
AA 1 2 N ILE A 19  ? N ILE A 19  O VAL A 300 ? O VAL A 300 
AA 2 3 N ILE A 303 ? N ILE A 303 O CYS A 274 ? O CYS A 274 
AA 3 4 N GLN A 279 ? N GLN A 279 O LYS A 319 ? O LYS A 319 
AA 4 5 N SER A 324 ? N SER A 324 O THR A 250 ? O THR A 250 
AA 5 6 N SER A 255 ? N SER A 255 O ILE A 234 ? O ILE A 234 
AA 6 7 N VAL A 235 ? N VAL A 235 O TYR A 225 ? O TYR A 225 
AA 7 8 N LEU A 226 ? N LEU A 226 O GLU A 339 ? O GLU A 339 
AB 1 2 N THR A 141 ? N THR A 141 O THR A 29  ? O THR A 29  
AB 2 3 N VAL A 30  ? N VAL A 30  O GLN A 33  ? O GLN A 33  
AB 3 4 N VAL A 39  ? N VAL A 39  O LEU A 50  ? O LEU A 50  
AB 4 5 N ALA A 55  ? N ALA A 55  O THR A 121 ? O THR A 121 
AB 5 6 N VAL A 128 ? N VAL A 128 O TYR A 72  ? O TYR A 72  
AB 6 7 N PHE A 75  ? N PHE A 75  O GLY A 104 ? O GLY A 104 
AB 7 8 N SER A 105 ? N SER A 105 O TYR A 215 ? O TYR A 215 
AC 1 2 N ILE A 67  ? N ILE A 67  O TYR A 178 ? O TYR A 178 
AD 1 2 N GLN A 115 ? N GLN A 115 O GLN A 83  ? O GLN A 83  
AD 2 3 N ALA A 86  ? N ALA A 86  O GLN A 94  ? O GLN A 94  
AD 3 4 N THR A 95  ? N THR A 95  O ALA A 194 ? O ALA A 194 
AE 1 2 N LEU A 295 ? N LEU A 295 O VAL A 283 ? O VAL A 283 
AE 2 3 N GLN A 286 ? N GLN A 286 O LYS A 310 ? O LYS A 310 
BA 1 2 N VAL B 7   ? N VAL B 7   O VAL B 18  ? O VAL B 18  
BA 2 3 N ILE B 19  ? N ILE B 19  O VAL B 300 ? O VAL B 300 
BA 3 4 N ILE B 303 ? N ILE B 303 O CYS B 274 ? O CYS B 274 
BA 4 5 N GLN B 279 ? N GLN B 279 O LYS B 319 ? O LYS B 319 
BA 5 6 N SER B 324 ? N SER B 324 O THR B 250 ? O THR B 250 
BA 6 7 N SER B 255 ? N SER B 255 O ILE B 234 ? O ILE B 234 
BA 7 8 N VAL B 235 ? N VAL B 235 O TYR B 225 ? O TYR B 225 
BA 8 9 N LEU B 226 ? N LEU B 226 O GLU B 339 ? O GLU B 339 
BB 1 2 N THR B 141 ? N THR B 141 O THR B 29  ? O THR B 29  
BB 2 3 N VAL B 30  ? N VAL B 30  O GLN B 33  ? O GLN B 33  
BB 3 4 N VAL B 39  ? N VAL B 39  O LEU B 50  ? O LEU B 50  
BB 4 5 N ALA B 55  ? N ALA B 55  O THR B 121 ? O THR B 121 
BB 5 6 N VAL B 128 ? N VAL B 128 O TYR B 72  ? O TYR B 72  
BB 6 7 N PHE B 75  ? N PHE B 75  O GLY B 104 ? O GLY B 104 
BB 7 8 N SER B 105 ? N SER B 105 O TYR B 215 ? O TYR B 215 
BC 1 2 N ILE B 67  ? N ILE B 67  O TYR B 178 ? O TYR B 178 
BD 1 2 N GLN B 115 ? N GLN B 115 O GLN B 83  ? O GLN B 83  
BD 2 3 N ALA B 86  ? N ALA B 86  O GLN B 94  ? O GLN B 94  
BD 3 4 N THR B 95  ? N THR B 95  O ALA B 194 ? O ALA B 194 
BE 1 2 N LEU B 295 ? N LEU B 295 O VAL B 283 ? O VAL B 283 
BE 2 3 N GLN B 286 ? N GLN B 286 O LYS B 310 ? O LYS B 310 
CA 1 2 N ILE C 19  ? N ILE C 19  O VAL C 300 ? O VAL C 300 
CA 2 3 N ILE C 303 ? N ILE C 303 O CYS C 274 ? O CYS C 274 
CA 3 4 N GLN C 279 ? N GLN C 279 O LYS C 319 ? O LYS C 319 
CA 4 5 N SER C 324 ? N SER C 324 O THR C 250 ? O THR C 250 
CA 5 6 N SER C 255 ? N SER C 255 O ILE C 234 ? O ILE C 234 
CA 6 7 N VAL C 235 ? N VAL C 235 O TYR C 225 ? O TYR C 225 
CA 7 8 N LEU C 226 ? N LEU C 226 O GLU C 339 ? O GLU C 339 
CB 1 2 N THR C 141 ? N THR C 141 O THR C 29  ? O THR C 29  
CB 2 3 N VAL C 30  ? N VAL C 30  O GLN C 33  ? O GLN C 33  
CB 3 4 N VAL C 39  ? N VAL C 39  O LEU C 50  ? O LEU C 50  
CB 4 5 N ALA C 55  ? N ALA C 55  O THR C 121 ? O THR C 121 
CB 5 6 N VAL C 128 ? N VAL C 128 O TYR C 72  ? O TYR C 72  
CB 6 7 N PHE C 75  ? N PHE C 75  O GLY C 104 ? O GLY C 104 
CB 7 8 N SER C 105 ? N SER C 105 O TYR C 215 ? O TYR C 215 
CC 1 2 N ILE C 67  ? N ILE C 67  O TYR C 178 ? O TYR C 178 
CD 1 2 N GLN C 115 ? N GLN C 115 O GLN C 83  ? O GLN C 83  
CD 2 3 N ALA C 86  ? N ALA C 86  O GLN C 94  ? O GLN C 94  
CD 3 4 N THR C 95  ? N THR C 95  O ALA C 194 ? O ALA C 194 
CE 1 2 N LEU C 295 ? N LEU C 295 O VAL C 283 ? O VAL C 283 
CE 2 3 N GLN C 286 ? N GLN C 286 O LYS C 310 ? O LYS C 310 
DA 1 2 N ILE D 19  ? N ILE D 19  O VAL D 300 ? O VAL D 300 
DA 2 3 N ILE D 303 ? N ILE D 303 O CYS D 274 ? O CYS D 274 
DA 3 4 N GLN D 279 ? N GLN D 279 O LYS D 319 ? O LYS D 319 
DA 4 5 N SER D 324 ? N SER D 324 O THR D 250 ? O THR D 250 
DA 5 6 N SER D 255 ? N SER D 255 O ILE D 234 ? O ILE D 234 
DA 6 7 N VAL D 235 ? N VAL D 235 O TYR D 225 ? O TYR D 225 
DA 7 8 N LEU D 226 ? N LEU D 226 O GLU D 339 ? O GLU D 339 
DB 1 2 N THR D 141 ? N THR D 141 O THR D 29  ? O THR D 29  
DB 2 3 N VAL D 30  ? N VAL D 30  O GLN D 33  ? O GLN D 33  
DB 3 4 N VAL D 39  ? N VAL D 39  O LEU D 50  ? O LEU D 50  
DB 4 5 N ALA D 55  ? N ALA D 55  O THR D 121 ? O THR D 121 
DB 5 6 N VAL D 128 ? N VAL D 128 O TYR D 72  ? O TYR D 72  
DB 6 7 N PHE D 75  ? N PHE D 75  O GLY D 104 ? O GLY D 104 
DB 7 8 N SER D 105 ? N SER D 105 O TYR D 215 ? O TYR D 215 
DC 1 2 N ILE D 67  ? N ILE D 67  O TYR D 178 ? O TYR D 178 
DD 1 2 N GLN D 115 ? N GLN D 115 O GLN D 83  ? O GLN D 83  
DD 2 3 N ALA D 86  ? N ALA D 86  O GLN D 94  ? O GLN D 94  
DD 3 4 N THR D 95  ? N THR D 95  O ALA D 194 ? O ALA D 194 
DE 1 2 N LEU D 295 ? N LEU D 295 O VAL D 283 ? O VAL D 283 
DE 2 3 N GLN D 286 ? N GLN D 286 O LYS D 310 ? O LYS D 310 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE NAG A1351'                                         
AC2 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE NAG B1351'                                         
AC3 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE NAG C1351'                                         
AC4 Software ? ? ? ? 9  'BINDING SITE FOR RESIDUE NAG D1354'                                         
AC5 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE NAG D1355'                                         
AC6 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE CU A1361'                                          
AC7 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE CU B1359'                                          
AC8 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE CU C1359'                                          
AC9 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE CU D1357'                                          
BC1 Software ? ? ? ? 18 'BINDING SITE FOR RESIDUE KMP A1360'                                         
BC2 Software ? ? ? ? 16 'BINDING SITE FOR RESIDUE KMP B1358'                                         
BC3 Software ? ? ? ? 18 'BINDING SITE FOR RESIDUE KMP C1358'                                         
BC4 Software ? ? ? ? 18 'BINDING SITE FOR RESIDUE KMP D1356'                                         
BC5 Software ? ? ? ? 9  'BINDING SITE FOR RESIDUE MPD A1362'                                         
BC6 Software ? ? ? ? 7  'BINDING SITE FOR RESIDUE MPD B1360'                                         
BC7 Software ? ? ? ? 8  'BINDING SITE FOR RESIDUE MPD B1361'                                         
BC8 Software ? ? ? ? 7  'BINDING SITE FOR RESIDUE MPD C1360'                                         
BC9 Software ? ? ? ? 25 'BINDING SITE FOR CHAIN A OF SUGAR BOUND TO ASN A 191 RESIDUES 1352 TO 1359' 
CC1 Software ? ? ? ? 23 'BINDING SITE FOR CHAIN B OF SUGAR BOUND TO ASN B 191 RESIDUES 1352 TO 1357' 
CC2 Software ? ? ? ? 23 'BINDING SITE FOR CHAIN C OF SUGAR BOUND TO ASN C 191 RESIDUES 1352 TO 1357' 
# 
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 5  GLN A  69  ? GLN A 69   . ? 1_555 ? 
2   AC1 5  ARG A  108 ? ARG A 108  . ? 1_555 ? 
3   AC1 5  ASN A  109 ? ASN A 109  . ? 1_555 ? 
4   AC1 5  HOH SA .   ? HOH A 2095 . ? 1_555 ? 
5   AC1 5  HOH SA .   ? HOH A 2403 . ? 1_555 ? 
6   AC2 5  ARG B  108 ? ARG B 108  . ? 1_555 ? 
7   AC2 5  ASN B  109 ? ASN B 109  . ? 1_555 ? 
8   AC2 5  HOH TA .   ? HOH B 2080 . ? 1_555 ? 
9   AC2 5  HOH TA .   ? HOH B 2377 . ? 1_555 ? 
10  AC2 5  HOH TA .   ? HOH B 2378 . ? 1_555 ? 
11  AC3 4  ARG C  108 ? ARG C 108  . ? 1_555 ? 
12  AC3 4  ASN C  109 ? ASN C 109  . ? 1_555 ? 
13  AC3 4  HOH UA .   ? HOH C 2106 . ? 1_555 ? 
14  AC3 4  HOH UA .   ? HOH C 2370 . ? 1_555 ? 
15  AC4 9  LEU A  139 ? LEU A 139  . ? 1_555 ? 
16  AC4 9  GLY A  163 ? GLY A 163  . ? 1_555 ? 
17  AC4 9  PRO A  164 ? PRO A 164  . ? 1_555 ? 
18  AC4 9  THR D  141 ? THR D 141  . ? 1_555 ? 
19  AC4 9  ASN D  142 ? ASN D 142  . ? 1_555 ? 
20  AC4 9  HOH VA .   ? HOH D 2166 . ? 1_555 ? 
21  AC4 9  HOH VA .   ? HOH D 2359 . ? 1_555 ? 
22  AC4 9  HOH VA .   ? HOH D 2360 . ? 1_555 ? 
23  AC4 9  HOH VA .   ? HOH D 2361 . ? 1_555 ? 
24  AC5 5  ASN D  248 ? ASN D 248  . ? 1_555 ? 
25  AC5 5  GLY D  272 ? GLY D 272  . ? 1_555 ? 
26  AC5 5  SER D  325 ? SER D 325  . ? 1_555 ? 
27  AC5 5  GLY D  326 ? GLY D 326  . ? 1_555 ? 
28  AC5 5  HOH VA .   ? HOH D 2362 . ? 1_555 ? 
29  AC6 5  HIS A  66  ? HIS A 66   . ? 1_555 ? 
30  AC6 5  HIS A  68  ? HIS A 68   . ? 1_555 ? 
31  AC6 5  GLU A  73  ? GLU A 73   . ? 1_555 ? 
32  AC6 5  HIS A  112 ? HIS A 112  . ? 1_555 ? 
33  AC6 5  KMP N  .   ? KMP A 1360 . ? 1_555 ? 
34  AC7 5  HIS B  66  ? HIS B 66   . ? 1_555 ? 
35  AC7 5  HIS B  68  ? HIS B 68   . ? 1_555 ? 
36  AC7 5  GLU B  73  ? GLU B 73   . ? 1_555 ? 
37  AC7 5  HIS B  112 ? HIS B 112  . ? 1_555 ? 
38  AC7 5  KMP X  .   ? KMP B 1358 . ? 1_555 ? 
39  AC8 5  HIS C  66  ? HIS C 66   . ? 1_555 ? 
40  AC8 5  HIS C  68  ? HIS C 68   . ? 1_555 ? 
41  AC8 5  GLU C  73  ? GLU C 73   . ? 1_555 ? 
42  AC8 5  HIS C  112 ? HIS C 112  . ? 1_555 ? 
43  AC8 5  KMP IA .   ? KMP C 1358 . ? 1_555 ? 
44  AC9 5  HIS D  66  ? HIS D 66   . ? 1_555 ? 
45  AC9 5  HIS D  68  ? HIS D 68   . ? 1_555 ? 
46  AC9 5  GLU D  73  ? GLU D 73   . ? 1_555 ? 
47  AC9 5  HIS D  112 ? HIS D 112  . ? 1_555 ? 
48  AC9 5  KMP QA .   ? KMP D 1356 . ? 1_555 ? 
49  BC1 18 MET A  51  ? MET A 51   . ? 1_555 ? 
50  BC1 18 VAL A  63  ? VAL A 63   . ? 1_555 ? 
51  BC1 18 HIS A  66  ? HIS A 66   . ? 1_555 ? 
52  BC1 18 HIS A  68  ? HIS A 68   . ? 1_555 ? 
53  BC1 18 GLU A  73  ? GLU A 73   . ? 1_555 ? 
54  BC1 18 PHE A  75  ? PHE A 75   . ? 1_555 ? 
55  BC1 18 PHE A  114 ? PHE A 114  . ? 1_555 ? 
56  BC1 18 GLY A  125 ? GLY A 125  . ? 1_555 ? 
57  BC1 18 PHE A  132 ? PHE A 132  . ? 1_555 ? 
58  BC1 18 LEU A  135 ? LEU A 135  . ? 1_555 ? 
59  BC1 18 PHE A  136 ? PHE A 136  . ? 1_555 ? 
60  BC1 18 LEU A  139 ? LEU A 139  . ? 1_555 ? 
61  BC1 18 GLY A  163 ? GLY A 163  . ? 1_555 ? 
62  BC1 18 PRO A  164 ? PRO A 164  . ? 1_555 ? 
63  BC1 18 VAL A  177 ? VAL A 177  . ? 1_555 ? 
64  BC1 18 CU  O  .   ? CU  A 1361 . ? 1_555 ? 
65  BC1 18 HOH SA .   ? HOH A 2415 . ? 1_555 ? 
66  BC1 18 HOH SA .   ? HOH A 2416 . ? 1_555 ? 
67  BC2 16 MET B  51  ? MET B 51   . ? 1_555 ? 
68  BC2 16 VAL B  63  ? VAL B 63   . ? 1_555 ? 
69  BC2 16 HIS B  66  ? HIS B 66   . ? 1_555 ? 
70  BC2 16 HIS B  68  ? HIS B 68   . ? 1_555 ? 
71  BC2 16 GLU B  73  ? GLU B 73   . ? 1_555 ? 
72  BC2 16 PHE B  75  ? PHE B 75   . ? 1_555 ? 
73  BC2 16 MET B  123 ? MET B 123  . ? 1_555 ? 
74  BC2 16 GLY B  125 ? GLY B 125  . ? 1_555 ? 
75  BC2 16 LEU B  135 ? LEU B 135  . ? 1_555 ? 
76  BC2 16 PHE B  136 ? PHE B 136  . ? 1_555 ? 
77  BC2 16 LEU B  139 ? LEU B 139  . ? 1_555 ? 
78  BC2 16 PRO B  164 ? PRO B 164  . ? 1_555 ? 
79  BC2 16 VAL B  177 ? VAL B 177  . ? 1_555 ? 
80  BC2 16 CU  Y  .   ? CU  B 1359 . ? 1_555 ? 
81  BC2 16 HOH TA .   ? HOH B 2078 . ? 1_555 ? 
82  BC2 16 HOH TA .   ? HOH B 2387 . ? 1_555 ? 
83  BC3 18 TYR C  35  ? TYR C 35   . ? 1_555 ? 
84  BC3 18 MET C  51  ? MET C 51   . ? 1_555 ? 
85  BC3 18 VAL C  63  ? VAL C 63   . ? 1_555 ? 
86  BC3 18 HIS C  66  ? HIS C 66   . ? 1_555 ? 
87  BC3 18 HIS C  68  ? HIS C 68   . ? 1_555 ? 
88  BC3 18 GLU C  73  ? GLU C 73   . ? 1_555 ? 
89  BC3 18 PHE C  75  ? PHE C 75   . ? 1_555 ? 
90  BC3 18 MET C  123 ? MET C 123  . ? 1_555 ? 
91  BC3 18 GLY C  125 ? GLY C 125  . ? 1_555 ? 
92  BC3 18 PHE C  132 ? PHE C 132  . ? 1_555 ? 
93  BC3 18 LEU C  135 ? LEU C 135  . ? 1_555 ? 
94  BC3 18 PHE C  136 ? PHE C 136  . ? 1_555 ? 
95  BC3 18 LEU C  139 ? LEU C 139  . ? 1_555 ? 
96  BC3 18 PRO C  164 ? PRO C 164  . ? 1_555 ? 
97  BC3 18 VAL C  177 ? VAL C 177  . ? 1_555 ? 
98  BC3 18 CU  JA .   ? CU  C 1359 . ? 1_555 ? 
99  BC3 18 HOH UA .   ? HOH C 2098 . ? 1_555 ? 
100 BC3 18 HOH UA .   ? HOH C 2381 . ? 1_555 ? 
101 BC4 18 TYR D  35  ? TYR D 35   . ? 1_555 ? 
102 BC4 18 MET D  51  ? MET D 51   . ? 1_555 ? 
103 BC4 18 VAL D  63  ? VAL D 63   . ? 1_555 ? 
104 BC4 18 HIS D  66  ? HIS D 66   . ? 1_555 ? 
105 BC4 18 HIS D  68  ? HIS D 68   . ? 1_555 ? 
106 BC4 18 GLU D  73  ? GLU D 73   . ? 1_555 ? 
107 BC4 18 PHE D  75  ? PHE D 75   . ? 1_555 ? 
108 BC4 18 PHE D  114 ? PHE D 114  . ? 1_555 ? 
109 BC4 18 GLY D  125 ? GLY D 125  . ? 1_555 ? 
110 BC4 18 PHE D  132 ? PHE D 132  . ? 1_555 ? 
111 BC4 18 LEU D  135 ? LEU D 135  . ? 1_555 ? 
112 BC4 18 PHE D  136 ? PHE D 136  . ? 1_555 ? 
113 BC4 18 GLY D  163 ? GLY D 163  . ? 1_555 ? 
114 BC4 18 PRO D  164 ? PRO D 164  . ? 1_555 ? 
115 BC4 18 VAL D  177 ? VAL D 177  . ? 1_555 ? 
116 BC4 18 CU  RA .   ? CU  D 1357 . ? 1_555 ? 
117 BC4 18 HOH VA .   ? HOH D 2085 . ? 1_555 ? 
118 BC4 18 HOH VA .   ? HOH D 2363 . ? 1_555 ? 
119 BC5 9  VAL A  97  ? VAL A 97   . ? 1_555 ? 
120 BC5 9  SER A  99  ? SER A 99   . ? 1_555 ? 
121 BC5 9  ASP A  102 ? ASP A 102  . ? 1_555 ? 
122 BC5 9  TRP A  200 ? TRP A 200  . ? 1_555 ? 
123 BC5 9  HIS A  201 ? HIS A 201  . ? 1_555 ? 
124 BC5 9  SER C  81  ? SER C 81   . ? 1_555 ? 
125 BC5 9  GLN C  117 ? GLN C 117  . ? 1_555 ? 
126 BC5 9  ASP C  118 ? ASP C 118  . ? 1_555 ? 
127 BC5 9  MPD KA .   ? MPD C 1360 . ? 1_555 ? 
128 BC6 7  GLN B  117 ? GLN B 117  . ? 1_555 ? 
129 BC6 7  ASP B  118 ? ASP B 118  . ? 1_555 ? 
130 BC6 7  MPD AA .   ? MPD B 1361 . ? 1_555 ? 
131 BC6 7  VAL D  97  ? VAL D 97   . ? 1_555 ? 
132 BC6 7  SER D  99  ? SER D 99   . ? 1_555 ? 
133 BC6 7  ASP D  102 ? ASP D 102  . ? 1_555 ? 
134 BC6 7  HIS D  201 ? HIS D 201  . ? 1_555 ? 
135 BC7 8  VAL B  97  ? VAL B 97   . ? 1_555 ? 
136 BC7 8  SER B  99  ? SER B 99   . ? 1_555 ? 
137 BC7 8  ASP B  102 ? ASP B 102  . ? 1_555 ? 
138 BC7 8  HIS B  201 ? HIS B 201  . ? 1_555 ? 
139 BC7 8  MPD Z  .   ? MPD B 1360 . ? 1_555 ? 
140 BC7 8  SER D  81  ? SER D 81   . ? 1_555 ? 
141 BC7 8  GLN D  117 ? GLN D 117  . ? 1_555 ? 
142 BC7 8  ASP D  118 ? ASP D 118  . ? 1_555 ? 
143 BC8 7  GLN A  117 ? GLN A 117  . ? 1_555 ? 
144 BC8 7  ASP A  118 ? ASP A 118  . ? 1_555 ? 
145 BC8 7  MPD P  .   ? MPD A 1362 . ? 1_555 ? 
146 BC8 7  VAL C  97  ? VAL C 97   . ? 1_555 ? 
147 BC8 7  SER C  99  ? SER C 99   . ? 1_555 ? 
148 BC8 7  ASP C  102 ? ASP C 102  . ? 1_555 ? 
149 BC8 7  HIS C  201 ? HIS C 201  . ? 1_555 ? 
150 BC9 25 ASN A  90  ? ASN A 90   . ? 1_555 ? 
151 BC9 25 THR A  141 ? THR A 141  . ? 1_555 ? 
152 BC9 25 ASN A  142 ? ASN A 142  . ? 1_555 ? 
153 BC9 25 ASN A  191 ? ASN A 191  . ? 1_555 ? 
154 BC9 25 ASN A  248 ? ASN A 248  . ? 1_555 ? 
155 BC9 25 GLY A  272 ? GLY A 272  . ? 1_555 ? 
156 BC9 25 SER A  325 ? SER A 325  . ? 1_555 ? 
157 BC9 25 GLY A  326 ? GLY A 326  . ? 1_555 ? 
158 BC9 25 HOH SA .   ? HOH A 2128 . ? 1_555 ? 
159 BC9 25 HOH SA .   ? HOH A 2404 . ? 1_555 ? 
160 BC9 25 HOH SA .   ? HOH A 2405 . ? 1_555 ? 
161 BC9 25 HOH SA .   ? HOH A 2407 . ? 1_555 ? 
162 BC9 25 HOH SA .   ? HOH A 2409 . ? 1_555 ? 
163 BC9 25 HOH SA .   ? HOH A 2410 . ? 1_555 ? 
164 BC9 25 HOH SA .   ? HOH A 2412 . ? 1_555 ? 
165 BC9 25 HOH SA .   ? HOH A 2414 . ? 1_555 ? 
166 BC9 25 GLN C  83  ? GLN C 83   . ? 1_555 ? 
167 BC9 25 THR C  184 ? THR C 184  . ? 1_555 ? 
168 BC9 25 THR C  187 ? THR C 187  . ? 1_555 ? 
169 BC9 25 ASP C  188 ? ASP C 188  . ? 1_555 ? 
170 BC9 25 THR C  189 ? THR C 189  . ? 1_555 ? 
171 BC9 25 LEU D  139 ? LEU D 139  . ? 1_555 ? 
172 BC9 25 GLY D  163 ? GLY D 163  . ? 1_555 ? 
173 BC9 25 PRO D  164 ? PRO D 164  . ? 1_555 ? 
174 BC9 25 HOH VA .   ? HOH D 2186 . ? 1_555 ? 
175 CC1 23 ARG B  26  ? ARG B 26   . ? 1_555 ? 
176 CC1 23 ASN B  142 ? ASN B 142  . ? 1_555 ? 
177 CC1 23 VAL B  190 ? VAL B 190  . ? 1_555 ? 
178 CC1 23 ASN B  191 ? ASN B 191  . ? 1_555 ? 
179 CC1 23 ASN B  248 ? ASN B 248  . ? 1_555 ? 
180 CC1 23 GLY B  272 ? GLY B 272  . ? 1_555 ? 
181 CC1 23 SER B  325 ? SER B 325  . ? 1_555 ? 
182 CC1 23 GLY B  326 ? GLY B 326  . ? 1_555 ? 
183 CC1 23 HOH TA .   ? HOH B 2155 . ? 1_555 ? 
184 CC1 23 HOH TA .   ? HOH B 2379 . ? 1_555 ? 
185 CC1 23 HOH TA .   ? HOH B 2380 . ? 1_555 ? 
186 CC1 23 HOH TA .   ? HOH B 2381 . ? 1_555 ? 
187 CC1 23 HOH TA .   ? HOH B 2382 . ? 1_555 ? 
188 CC1 23 HOH TA .   ? HOH B 2383 . ? 1_555 ? 
189 CC1 23 HOH TA .   ? HOH B 2384 . ? 1_555 ? 
190 CC1 23 HOH TA .   ? HOH B 2385 . ? 1_555 ? 
191 CC1 23 HOH TA .   ? HOH B 2386 . ? 1_555 ? 
192 CC1 23 NAG HA .   ? NAG C 1355 . ? 1_555 ? 
193 CC1 23 GLN D  83  ? GLN D 83   . ? 1_555 ? 
194 CC1 23 THR D  187 ? THR D 187  . ? 1_555 ? 
195 CC1 23 THR D  189 ? THR D 189  . ? 1_555 ? 
196 CC1 23 HOH VA .   ? HOH D 2208 . ? 1_555 ? 
197 CC1 23 HOH VA .   ? HOH D 2212 . ? 1_555 ? 
198 CC2 23 GLN A  83  ? GLN A 83   . ? 1_555 ? 
199 CC2 23 THR A  187 ? THR A 187  . ? 1_555 ? 
200 CC2 23 ASP A  188 ? ASP A 188  . ? 1_555 ? 
201 CC2 23 THR A  189 ? THR A 189  . ? 1_555 ? 
202 CC2 23 HOH SA .   ? HOH A 2235 . ? 1_555 ? 
203 CC2 23 ARG B  26  ? ARG B 26   . ? 1_555 ? 
204 CC2 23 NAG W  .   ? NAG B 1355 . ? 1_555 ? 
205 CC2 23 HOH TA .   ? HOH B 2384 . ? 1_555 ? 
206 CC2 23 ASN C  142 ? ASN C 142  . ? 1_555 ? 
207 CC2 23 VAL C  190 ? VAL C 190  . ? 1_555 ? 
208 CC2 23 ASN C  191 ? ASN C 191  . ? 1_555 ? 
209 CC2 23 ASN C  248 ? ASN C 248  . ? 1_555 ? 
210 CC2 23 GLY C  272 ? GLY C 272  . ? 1_555 ? 
211 CC2 23 SER C  325 ? SER C 325  . ? 1_555 ? 
212 CC2 23 GLY C  326 ? GLY C 326  . ? 1_555 ? 
213 CC2 23 HOH UA .   ? HOH C 2057 . ? 1_555 ? 
214 CC2 23 HOH UA .   ? HOH C 2221 . ? 1_555 ? 
215 CC2 23 HOH UA .   ? HOH C 2372 . ? 1_555 ? 
216 CC2 23 HOH UA .   ? HOH C 2373 . ? 1_555 ? 
217 CC2 23 HOH UA .   ? HOH C 2374 . ? 1_555 ? 
218 CC2 23 HOH UA .   ? HOH C 2377 . ? 1_555 ? 
219 CC2 23 HOH UA .   ? HOH C 2378 . ? 1_555 ? 
220 CC2 23 HOH UA .   ? HOH C 2380 . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          1H1M 
_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                    1H1M 
_atom_sites.fract_transf_matrix[1][1]   0.009151 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.001340 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.018058 
_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]   0.008155 
_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  
CU 
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   . SER A  1 3   ? 66.517  40.050  71.701  1.00 23.10 ? 3    SER A N   1 
ATOM   2     C  CA  . SER A  1 3   ? 65.335  40.499  70.851  1.00 23.46 ? 3    SER A CA  1 
ATOM   3     C  C   . SER A  1 3   ? 65.446  40.154  69.335  1.00 21.87 ? 3    SER A C   1 
ATOM   4     O  O   . SER A  1 3   ? 64.438  40.125  68.607  1.00 23.14 ? 3    SER A O   1 
ATOM   5     C  CB  . SER A  1 3   ? 65.112  42.009  71.024  1.00 24.62 ? 3    SER A CB  1 
ATOM   6     O  OG  . SER A  1 3   ? 64.320  42.574  69.978  1.00 28.20 ? 3    SER A OG  1 
ATOM   7     N  N   . SER A  1 4   ? 66.662  39.940  68.856  1.00 18.43 ? 4    SER A N   1 
ATOM   8     C  CA  . SER A  1 4   ? 66.891  39.426  67.512  1.00 15.88 ? 4    SER A CA  1 
ATOM   9     C  C   . SER A  1 4   ? 66.372  38.003  67.264  1.00 13.00 ? 4    SER A C   1 
ATOM   10    O  O   . SER A  1 4   ? 66.272  37.234  68.196  1.00 11.62 ? 4    SER A O   1 
ATOM   11    C  CB  . SER A  1 4   ? 68.377  39.484  67.300  1.00 16.44 ? 4    SER A CB  1 
ATOM   12    O  OG  . SER A  1 4   ? 68.707  40.836  67.685  1.00 16.67 ? 4    SER A OG  1 
ATOM   13    N  N   . LEU A  1 5   ? 66.064  37.675  66.015  1.00 10.54 ? 5    LEU A N   1 
ATOM   14    C  CA  . LEU A  1 5   ? 65.367  36.453  65.664  1.00 9.46  ? 5    LEU A CA  1 
ATOM   15    C  C   . LEU A  1 5   ? 66.248  35.227  65.923  1.00 8.43  ? 5    LEU A C   1 
ATOM   16    O  O   . LEU A  1 5   ? 65.820  34.202  66.455  1.00 7.12  ? 5    LEU A O   1 
ATOM   17    C  CB  . LEU A  1 5   ? 64.944  36.482  64.200  1.00 8.91  ? 5    LEU A CB  1 
ATOM   18    C  CG  . LEU A  1 5   ? 64.271  35.173  63.748  1.00 9.54  ? 5    LEU A CG  1 
ATOM   19    C  CD1 . LEU A  1 5   ? 62.801  35.060  64.259  1.00 10.38 ? 5    LEU A CD1 1 
ATOM   20    C  CD2 . LEU A  1 5   ? 64.322  35.060  62.230  1.00 12.35 ? 5    LEU A CD2 1 
ATOM   21    N  N   . ILE A  1 6   ? 67.506  35.348  65.553  1.00 8.90  ? 6    ILE A N   1 
ATOM   22    C  CA  . ILE A  1 6   ? 68.415  34.225  65.672  1.00 7.73  ? 6    ILE A CA  1 
ATOM   23    C  C   . ILE A  1 6   ? 68.988  34.213  67.083  1.00 8.49  ? 6    ILE A C   1 
ATOM   24    O  O   . ILE A  1 6   ? 69.486  35.236  67.546  1.00 10.09 ? 6    ILE A O   1 
ATOM   25    C  CB  . ILE A  1 6   ? 69.534  34.344  64.598  1.00 8.12  ? 6    ILE A CB  1 
ATOM   26    C  CG1 . ILE A  1 6   ? 68.922  34.167  63.190  1.00 8.29  ? 6    ILE A CG1 1 
ATOM   27    C  CG2 . ILE A  1 6   ? 70.555  33.243  64.787  1.00 8.52  ? 6    ILE A CG2 1 
ATOM   28    C  CD1 . ILE A  1 6   ? 69.910  34.459  62.036  1.00 8.39  ? 6    ILE A CD1 1 
ATOM   29    N  N   . VAL A  1 7   ? 68.975  33.047  67.728  1.00 8.60  ? 7    VAL A N   1 
ATOM   30    C  CA  . VAL A  1 7   ? 69.483  32.891  69.102  1.00 8.50  ? 7    VAL A CA  1 
ATOM   31    C  C   . VAL A  1 7   ? 70.479  31.743  69.133  1.00 8.81  ? 7    VAL A C   1 
ATOM   32    O  O   . VAL A  1 7   ? 70.451  30.909  68.241  1.00 7.51  ? 7    VAL A O   1 
ATOM   33    C  CB  . VAL A  1 7   ? 68.330  32.606  70.125  1.00 8.58  ? 7    VAL A CB  1 
ATOM   34    C  CG1 . VAL A  1 7   ? 67.405  33.837  70.204  1.00 8.55  ? 7    VAL A CG1 1 
ATOM   35    C  CG2 . VAL A  1 7   ? 67.514  31.365  69.746  1.00 3.17  ? 7    VAL A CG2 1 
ATOM   36    N  N   . GLU A  1 8   ? 71.333  31.709  70.167  1.00 8.08  ? 8    GLU A N   1 
ATOM   37    C  CA  . GLU A  1 8   ? 72.353  30.680  70.286  1.00 8.39  ? 8    GLU A CA  1 
ATOM   38    C  C   . GLU A  1 8   ? 71.873  29.606  71.276  1.00 7.88  ? 8    GLU A C   1 
ATOM   39    O  O   . GLU A  1 8   ? 72.373  28.488  71.226  1.00 8.23  ? 8    GLU A O   1 
ATOM   40    C  CB  . GLU A  1 8   ? 73.728  31.319  70.713  1.00 7.71  ? 8    GLU A CB  1 
ATOM   41    C  CG  A GLU A  1 8   ? 74.851  30.316  70.945  0.50 9.09  ? 8    GLU A CG  1 
ATOM   42    C  CG  B GLU A  1 8   ? 74.217  32.443  69.809  0.50 7.17  ? 8    GLU A CG  1 
ATOM   43    C  CD  A GLU A  1 8   ? 75.468  29.744  69.669  0.50 5.10  ? 8    GLU A CD  1 
ATOM   44    C  CD  B GLU A  1 8   ? 74.566  32.032  68.372  0.50 8.30  ? 8    GLU A CD  1 
ATOM   45    O  OE1 A GLU A  1 8   ? 75.154  30.201  68.557  0.50 5.63  ? 8    GLU A OE1 1 
ATOM   46    O  OE1 B GLU A  1 8   ? 74.883  30.858  68.106  0.50 8.01  ? 8    GLU A OE1 1 
ATOM   47    O  OE2 A GLU A  1 8   ? 76.267  28.816  69.791  0.50 2.89  ? 8    GLU A OE2 1 
ATOM   48    O  OE2 B GLU A  1 8   ? 74.531  32.905  67.474  0.50 8.00  ? 8    GLU A OE2 1 
ATOM   49    N  N   . ASP A  1 9   ? 70.902  29.952  72.154  1.00 7.12  ? 9    ASP A N   1 
ATOM   50    C  CA  . ASP A  1 9   ? 70.233  28.994  73.036  1.00 7.78  ? 9    ASP A CA  1 
ATOM   51    C  C   . ASP A  1 9   ? 68.764  29.298  72.923  1.00 7.52  ? 9    ASP A C   1 
ATOM   52    O  O   . ASP A  1 9   ? 68.415  30.444  72.700  1.00 7.69  ? 9    ASP A O   1 
ATOM   53    C  CB  . ASP A  1 9   ? 70.641  29.178  74.508  1.00 6.97  ? 9    ASP A CB  1 
ATOM   54    C  CG  . ASP A  1 9   ? 72.119  28.949  74.722  1.00 9.06  ? 9    ASP A CG  1 
ATOM   55    O  OD1 . ASP A  1 9   ? 72.530  27.778  74.966  1.00 9.62  ? 9    ASP A OD1 1 
ATOM   56    O  OD2 . ASP A  1 9   ? 72.958  29.874  74.600  1.00 13.07 ? 9    ASP A OD2 1 
ATOM   57    N  N   . ALA A  1 10  ? 67.924  28.300  73.077  1.00 7.55  ? 10   ALA A N   1 
ATOM   58    C  CA  . ALA A  1 10  ? 66.468  28.547  72.961  1.00 10.03 ? 10   ALA A CA  1 
ATOM   59    C  C   . ALA A  1 10  ? 66.043  29.557  74.021  1.00 9.42  ? 10   ALA A C   1 
ATOM   60    O  O   . ALA A  1 10  ? 66.571  29.540  75.130  1.00 10.46 ? 10   ALA A O   1 
ATOM   61    C  CB  . ALA A  1 10  ? 65.664  27.195  73.103  1.00 7.96  ? 10   ALA A CB  1 
ATOM   62    N  N   . PRO A  1 11  ? 65.123  30.466  73.702  1.00 10.21 ? 11   PRO A N   1 
ATOM   63    C  CA  . PRO A  1 11  ? 64.686  31.448  74.700  1.00 9.08  ? 11   PRO A CA  1 
ATOM   64    C  C   . PRO A  1 11  ? 64.035  30.817  75.928  1.00 9.38  ? 11   PRO A C   1 
ATOM   65    O  O   . PRO A  1 11  ? 63.539  29.662  75.912  1.00 9.40  ? 11   PRO A O   1 
ATOM   66    C  CB  . PRO A  1 11  ? 63.643  32.296  73.946  1.00 9.07  ? 11   PRO A CB  1 
ATOM   67    C  CG  . PRO A  1 11  ? 63.958  32.092  72.476  1.00 10.23 ? 11   PRO A CG  1 
ATOM   68    C  CD  . PRO A  1 11  ? 64.471  30.653  72.390  1.00 9.16  ? 11   PRO A CD  1 
ATOM   69    N  N   . ASP A  1 12  ? 63.980  31.615  76.981  1.00 9.03  ? 12   ASP A N   1 
ATOM   70    C  CA  . ASP A  1 12  ? 63.407  31.170  78.245  1.00 10.94 ? 12   ASP A CA  1 
ATOM   71    C  C   . ASP A  1 12  ? 61.911  31.437  78.339  1.00 10.36 ? 12   ASP A C   1 
ATOM   72    O  O   . ASP A  1 12  ? 61.332  31.338  79.426  1.00 12.67 ? 12   ASP A O   1 
ATOM   73    C  CB  . ASP A  1 12  ? 64.185  31.769  79.427  1.00 8.72  ? 12   ASP A CB  1 
ATOM   74    C  CG  . ASP A  1 12  ? 64.009  33.281  79.553  1.00 12.45 ? 12   ASP A CG  1 
ATOM   75    O  OD1 . ASP A  1 12  ? 63.143  33.870  78.844  1.00 10.14 ? 12   ASP A OD1 1 
ATOM   76    O  OD2 . ASP A  1 12  ? 64.678  33.939  80.384  1.00 16.12 ? 12   ASP A OD2 1 
ATOM   77    N  N   . HIS A  1 13  ? 61.284  31.770  77.202  1.00 10.50 ? 13   HIS A N   1 
ATOM   78    C  CA  . HIS A  1 13  ? 59.861  32.097  77.165  1.00 10.81 ? 13   HIS A CA  1 
ATOM   79    C  C   . HIS A  1 13  ? 59.441  31.983  75.686  1.00 11.13 ? 13   HIS A C   1 
ATOM   80    O  O   . HIS A  1 13  ? 60.309  31.846  74.800  1.00 10.68 ? 13   HIS A O   1 
ATOM   81    C  CB  . HIS A  1 13  ? 59.632  33.511  77.712  1.00 11.11 ? 13   HIS A CB  1 
ATOM   82    C  CG  . HIS A  1 13  ? 60.191  34.576  76.823  1.00 13.55 ? 13   HIS A CG  1 
ATOM   83    N  ND1 . HIS A  1 13  ? 61.525  34.906  76.816  1.00 11.85 ? 13   HIS A ND1 1 
ATOM   84    C  CD2 . HIS A  1 13  ? 59.599  35.360  75.881  1.00 13.25 ? 13   HIS A CD2 1 
ATOM   85    C  CE1 . HIS A  1 13  ? 61.733  35.858  75.917  1.00 15.59 ? 13   HIS A CE1 1 
ATOM   86    N  NE2 . HIS A  1 13  ? 60.583  36.136  75.327  1.00 13.33 ? 13   HIS A NE2 1 
ATOM   87    N  N   . VAL A  1 14  ? 58.142  32.051  75.412  1.00 10.07 ? 14   VAL A N   1 
ATOM   88    C  CA  . VAL A  1 14  ? 57.633  31.789  74.061  1.00 10.00 ? 14   VAL A CA  1 
ATOM   89    C  C   . VAL A  1 14  ? 57.837  33.027  73.233  1.00 9.43  ? 14   VAL A C   1 
ATOM   90    O  O   . VAL A  1 14  ? 57.324  34.087  73.581  1.00 9.72  ? 14   VAL A O   1 
ATOM   91    C  CB  . VAL A  1 14  ? 56.124  31.410  74.097  1.00 11.05 ? 14   VAL A CB  1 
ATOM   92    C  CG1 . VAL A  1 14  ? 55.501  31.316  72.675  1.00 10.47 ? 14   VAL A CG1 1 
ATOM   93    C  CG2 . VAL A  1 14  ? 55.980  30.104  74.821  1.00 11.04 ? 14   VAL A CG2 1 
ATOM   94    N  N   . ARG A  1 15  ? 58.564  32.885  72.123  1.00 9.07  ? 15   ARG A N   1 
ATOM   95    C  CA  . ARG A  1 15  ? 58.701  33.967  71.154  1.00 7.90  ? 15   ARG A CA  1 
ATOM   96    C  C   . ARG A  1 15  ? 59.154  33.314  69.844  1.00 8.11  ? 15   ARG A C   1 
ATOM   97    O  O   . ARG A  1 15  ? 59.607  32.177  69.829  1.00 9.51  ? 15   ARG A O   1 
ATOM   98    C  CB  . ARG A  1 15  ? 59.722  35.020  71.664  1.00 7.17  ? 15   ARG A CB  1 
ATOM   99    C  CG  . ARG A  1 15  ? 60.990  34.348  72.152  1.00 8.47  ? 15   ARG A CG  1 
ATOM   100   C  CD  . ARG A  1 15  ? 62.223  35.176  72.005  1.00 9.91  ? 15   ARG A CD  1 
ATOM   101   N  NE  . ARG A  1 15  ? 62.635  35.284  70.591  1.00 11.78 ? 15   ARG A NE  1 
ATOM   102   C  CZ  . ARG A  1 15  ? 63.771  35.885  70.197  1.00 11.84 ? 15   ARG A CZ  1 
ATOM   103   N  NH1 . ARG A  1 15  ? 64.616  36.385  71.118  1.00 7.22  ? 15   ARG A NH1 1 
ATOM   104   N  NH2 . ARG A  1 15  ? 64.093  35.911  68.921  1.00 8.47  ? 15   ARG A NH2 1 
ATOM   105   N  N   . PRO A  1 16  ? 58.975  33.983  68.725  1.00 7.52  ? 16   PRO A N   1 
ATOM   106   C  CA  . PRO A  1 16  ? 59.518  33.443  67.477  1.00 7.18  ? 16   PRO A CA  1 
ATOM   107   C  C   . PRO A  1 16  ? 61.049  33.461  67.534  1.00 6.72  ? 16   PRO A C   1 
ATOM   108   O  O   . PRO A  1 16  ? 61.652  34.389  68.126  1.00 8.15  ? 16   PRO A O   1 
ATOM   109   C  CB  . PRO A  1 16  ? 59.051  34.427  66.427  1.00 7.28  ? 16   PRO A CB  1 
ATOM   110   C  CG  . PRO A  1 16  ? 58.159  35.412  67.105  1.00 7.25  ? 16   PRO A CG  1 
ATOM   111   C  CD  . PRO A  1 16  ? 58.300  35.284  68.569  1.00 6.99  ? 16   PRO A CD  1 
ATOM   112   N  N   . TYR A  1 17  ? 61.682  32.454  66.953  1.00 7.06  ? 17   TYR A N   1 
ATOM   113   C  CA  . TYR A  1 17  ? 63.149  32.467  66.882  1.00 7.46  ? 17   TYR A CA  1 
ATOM   114   C  C   . TYR A  1 17  ? 63.637  31.446  65.864  1.00 8.34  ? 17   TYR A C   1 
ATOM   115   O  O   . TYR A  1 17  ? 62.900  30.487  65.485  1.00 8.03  ? 17   TYR A O   1 
ATOM   116   C  CB  . TYR A  1 17  ? 63.800  32.190  68.258  1.00 5.01  ? 17   TYR A CB  1 
ATOM   117   C  CG  . TYR A  1 17  ? 63.617  30.779  68.811  1.00 7.26  ? 17   TYR A CG  1 
ATOM   118   C  CD1 . TYR A  1 17  ? 62.513  30.471  69.604  1.00 7.30  ? 17   TYR A CD1 1 
ATOM   119   C  CD2 . TYR A  1 17  ? 64.588  29.794  68.589  1.00 5.06  ? 17   TYR A CD2 1 
ATOM   120   C  CE1 . TYR A  1 17  ? 62.339  29.170  70.149  1.00 6.76  ? 17   TYR A CE1 1 
ATOM   121   C  CE2 . TYR A  1 17  ? 64.431  28.472  69.118  1.00 8.32  ? 17   TYR A CE2 1 
ATOM   122   C  CZ  . TYR A  1 17  ? 63.308  28.199  69.926  1.00 7.73  ? 17   TYR A CZ  1 
ATOM   123   O  OH  . TYR A  1 17  ? 63.145  26.975  70.493  1.00 8.29  ? 17   TYR A OH  1 
ATOM   124   N  N   . VAL A  1 18  ? 64.890  31.653  65.463  1.00 7.18  ? 18   VAL A N   1 
ATOM   125   C  CA  . VAL A  1 18  ? 65.631  30.751  64.612  1.00 5.46  ? 18   VAL A CA  1 
ATOM   126   C  C   . VAL A  1 18  ? 66.876  30.398  65.358  1.00 6.98  ? 18   VAL A C   1 
ATOM   127   O  O   . VAL A  1 18  ? 67.476  31.231  66.026  1.00 6.23  ? 18   VAL A O   1 
ATOM   128   C  CB  . VAL A  1 18  ? 65.936  31.412  63.223  1.00 5.32  ? 18   VAL A CB  1 
ATOM   129   C  CG1 . VAL A  1 18  ? 67.060  30.663  62.426  1.00 4.70  ? 18   VAL A CG1 1 
ATOM   130   C  CG2 . VAL A  1 18  ? 64.648  31.389  62.432  1.00 6.18  ? 18   VAL A CG2 1 
ATOM   131   N  N   . ILE A  1 19  ? 67.239  29.110  65.307  1.00 7.93  ? 19   ILE A N   1 
ATOM   132   C  CA  . ILE A  1 19  ? 68.477  28.662  65.956  1.00 7.60  ? 19   ILE A CA  1 
ATOM   133   C  C   . ILE A  1 19  ? 69.199  27.804  64.912  1.00 7.17  ? 19   ILE A C   1 
ATOM   134   O  O   . ILE A  1 19  ? 68.622  26.848  64.363  1.00 6.95  ? 19   ILE A O   1 
ATOM   135   C  CB  . ILE A  1 19  ? 68.204  27.931  67.346  1.00 8.30  ? 19   ILE A CB  1 
ATOM   136   C  CG1 . ILE A  1 19  ? 69.502  27.461  68.038  1.00 4.24  ? 19   ILE A CG1 1 
ATOM   137   C  CG2 . ILE A  1 19  ? 67.230  26.748  67.214  1.00 8.65  ? 19   ILE A CG2 1 
ATOM   138   C  CD1 . ILE A  1 19  ? 69.339  27.311  69.680  1.00 5.08  ? 19   ILE A CD1 1 
ATOM   139   N  N   . ARG A  1 20  ? 70.454  28.179  64.619  1.00 6.36  ? 20   ARG A N   1 
ATOM   140   C  CA  . ARG A  1 20  ? 71.267  27.483  63.583  1.00 7.37  ? 20   ARG A CA  1 
ATOM   141   C  C   . ARG A  1 20  ? 71.730  26.101  64.074  1.00 7.57  ? 20   ARG A C   1 
ATOM   142   O  O   . ARG A  1 20  ? 71.962  25.909  65.277  1.00 9.04  ? 20   ARG A O   1 
ATOM   143   C  CB  . ARG A  1 20  ? 72.539  28.293  63.270  1.00 6.38  ? 20   ARG A CB  1 
ATOM   144   C  CG  . ARG A  1 20  ? 72.274  29.667  62.658  1.00 8.33  ? 20   ARG A CG  1 
ATOM   145   C  CD  . ARG A  1 20  ? 71.573  29.585  61.322  1.00 4.98  ? 20   ARG A CD  1 
ATOM   146   N  NE  . ARG A  1 20  ? 71.501  30.923  60.728  1.00 6.69  ? 20   ARG A NE  1 
ATOM   147   C  CZ  . ARG A  1 20  ? 70.995  31.176  59.511  1.00 7.29  ? 20   ARG A CZ  1 
ATOM   148   N  NH1 . ARG A  1 20  ? 70.513  30.175  58.764  1.00 6.83  ? 20   ARG A NH1 1 
ATOM   149   N  NH2 . ARG A  1 20  ? 70.980  32.445  59.058  1.00 8.55  ? 20   ARG A NH2 1 
ATOM   150   N  N   . HIS A  1 21  ? 71.830  25.144  63.156  1.00 7.72  ? 21   HIS A N   1 
ATOM   151   C  CA  . HIS A  1 21  ? 72.440  23.826  63.427  1.00 7.38  ? 21   HIS A CA  1 
ATOM   152   C  C   . HIS A  1 21  ? 73.732  23.933  64.256  1.00 6.30  ? 21   HIS A C   1 
ATOM   153   O  O   . HIS A  1 21  ? 74.607  24.773  63.922  1.00 6.35  ? 21   HIS A O   1 
ATOM   154   C  CB  . HIS A  1 21  ? 72.838  23.176  62.095  1.00 6.62  ? 21   HIS A CB  1 
ATOM   155   C  CG  . HIS A  1 21  ? 72.844  21.679  62.149  1.00 8.87  ? 21   HIS A CG  1 
ATOM   156   N  ND1 . HIS A  1 21  ? 73.505  20.895  61.221  1.00 11.68 ? 21   HIS A ND1 1 
ATOM   157   C  CD2 . HIS A  1 21  ? 72.287  20.820  63.042  1.00 7.26  ? 21   HIS A CD2 1 
ATOM   158   C  CE1 . HIS A  1 21  ? 73.295  19.616  61.504  1.00 10.44 ? 21   HIS A CE1 1 
ATOM   159   N  NE2 . HIS A  1 21  ? 72.567  19.541  62.607  1.00 8.57  ? 21   HIS A NE2 1 
ATOM   160   N  N   . TYR A  1 22  ? 73.868  23.090  65.291  1.00 7.12  ? 22   TYR A N   1 
ATOM   161   C  CA  . TYR A  1 22  ? 75.054  23.067  66.167  1.00 7.46  ? 22   TYR A CA  1 
ATOM   162   C  C   . TYR A  1 22  ? 75.313  24.379  66.971  1.00 8.39  ? 22   TYR A C   1 
ATOM   163   O  O   . TYR A  1 22  ? 76.432  24.576  67.486  1.00 8.75  ? 22   TYR A O   1 
ATOM   164   C  CB  . TYR A  1 22  ? 76.319  22.703  65.382  1.00 6.97  ? 22   TYR A CB  1 
ATOM   165   C  CG  . TYR A  1 22  ? 76.187  21.440  64.573  1.00 8.16  ? 22   TYR A CG  1 
ATOM   166   C  CD1 . TYR A  1 22  ? 75.858  20.226  65.180  1.00 10.01 ? 22   TYR A CD1 1 
ATOM   167   C  CD2 . TYR A  1 22  ? 76.398  21.474  63.195  1.00 8.54  ? 22   TYR A CD2 1 
ATOM   168   C  CE1 . TYR A  1 22  ? 75.750  19.052  64.431  1.00 8.13  ? 22   TYR A CE1 1 
ATOM   169   C  CE2 . TYR A  1 22  ? 76.332  20.289  62.434  1.00 9.88  ? 22   TYR A CE2 1 
ATOM   170   C  CZ  . TYR A  1 22  ? 75.997  19.100  63.061  1.00 11.21 ? 22   TYR A CZ  1 
ATOM   171   O  OH  . TYR A  1 22  ? 75.875  17.965  62.308  1.00 12.13 ? 22   TYR A OH  1 
ATOM   172   N  N   . SER A  1 23  ? 74.326  25.279  67.071  1.00 7.71  ? 23   SER A N   1 
ATOM   173   C  CA  . SER A  1 23  ? 74.387  26.309  68.107  1.00 6.55  ? 23   SER A CA  1 
ATOM   174   C  C   . SER A  1 23  ? 74.580  25.626  69.461  1.00 7.08  ? 23   SER A C   1 
ATOM   175   O  O   . SER A  1 23  ? 74.246  24.427  69.656  1.00 6.54  ? 23   SER A O   1 
ATOM   176   C  CB  . SER A  1 23  ? 73.100  27.195  68.141  1.00 7.54  ? 23   SER A CB  1 
ATOM   177   O  OG  . SER A  1 23  ? 72.865  27.877  66.865  1.00 5.96  ? 23   SER A OG  1 
ATOM   178   N  N   . HIS A  1 24  ? 75.089  26.393  70.427  1.00 7.08  ? 24   HIS A N   1 
ATOM   179   C  CA  . HIS A  1 24  ? 75.208  25.900  71.787  1.00 7.75  ? 24   HIS A CA  1 
ATOM   180   C  C   . HIS A  1 24  ? 73.997  25.175  72.339  1.00 7.57  ? 24   HIS A C   1 
ATOM   181   O  O   . HIS A  1 24  ? 74.088  24.030  72.800  1.00 8.95  ? 24   HIS A O   1 
ATOM   182   C  CB  . HIS A  1 24  ? 75.626  27.002  72.793  1.00 7.53  ? 24   HIS A CB  1 
ATOM   183   C  CG  . HIS A  1 24  ? 75.914  26.429  74.153  1.00 8.36  ? 24   HIS A CG  1 
ATOM   184   N  ND1 . HIS A  1 24  ? 75.048  26.560  75.222  1.00 9.93  ? 24   HIS A ND1 1 
ATOM   185   C  CD2 . HIS A  1 24  ? 76.951  25.673  74.592  1.00 8.72  ? 24   HIS A CD2 1 
ATOM   186   C  CE1 . HIS A  1 24  ? 75.561  25.940  76.275  1.00 9.98  ? 24   HIS A CE1 1 
ATOM   187   N  NE2 . HIS A  1 24  ? 76.711  25.379  75.917  1.00 8.27  ? 24   HIS A NE2 1 
ATOM   188   N  N   . ALA A  1 25  ? 72.874  25.856  72.316  1.00 6.97  ? 25   ALA A N   1 
ATOM   189   C  CA  . ALA A  1 25  ? 71.577  25.213  72.640  1.00 6.80  ? 25   ALA A CA  1 
ATOM   190   C  C   . ALA A  1 25  ? 71.603  24.366  73.927  1.00 7.79  ? 25   ALA A C   1 
ATOM   191   O  O   . ALA A  1 25  ? 71.118  23.203  73.964  1.00 7.37  ? 25   ALA A O   1 
ATOM   192   C  CB  . ALA A  1 25  ? 71.022  24.453  71.403  1.00 5.34  ? 25   ALA A CB  1 
ATOM   193   N  N   . ARG A  1 26  ? 72.176  24.985  74.976  1.00 8.30  ? 26   ARG A N   1 
ATOM   194   C  CA  . ARG A  1 26  ? 72.230  24.403  76.306  1.00 8.84  ? 26   ARG A CA  1 
ATOM   195   C  C   . ARG A  1 26  ? 72.851  23.009  76.247  1.00 9.61  ? 26   ARG A C   1 
ATOM   196   O  O   . ARG A  1 26  ? 72.363  22.072  76.913  1.00 8.75  ? 26   ARG A O   1 
ATOM   197   C  CB  . ARG A  1 26  ? 70.833  24.332  76.952  1.00 9.83  ? 26   ARG A CB  1 
ATOM   198   C  CG  . ARG A  1 26  ? 70.313  25.724  77.433  1.00 11.69 ? 26   ARG A CG  1 
ATOM   199   C  CD  . ARG A  1 26  ? 69.162  25.615  78.401  1.00 10.82 ? 26   ARG A CD  1 
ATOM   200   N  NE  . ARG A  1 26  ? 68.706  26.899  78.936  1.00 12.16 ? 26   ARG A NE  1 
ATOM   201   C  CZ  . ARG A  1 26  ? 67.654  27.007  79.743  1.00 13.65 ? 26   ARG A CZ  1 
ATOM   202   N  NH1 . ARG A  1 26  ? 66.938  25.913  80.060  1.00 14.52 ? 26   ARG A NH1 1 
ATOM   203   N  NH2 . ARG A  1 26  ? 67.293  28.196  80.214  1.00 14.56 ? 26   ARG A NH2 1 
ATOM   204   N  N   . ALA A  1 27  ? 73.941  22.899  75.476  1.00 7.60  ? 27   ALA A N   1 
ATOM   205   C  CA  . ALA A  1 27  ? 74.584  21.609  75.226  1.00 9.79  ? 27   ALA A CA  1 
ATOM   206   C  C   . ALA A  1 27  ? 74.990  20.875  76.517  1.00 8.42  ? 27   ALA A C   1 
ATOM   207   O  O   . ALA A  1 27  ? 75.422  21.498  77.466  1.00 9.23  ? 27   ALA A O   1 
ATOM   208   C  CB  . ALA A  1 27  ? 75.835  21.804  74.351  1.00 8.74  ? 27   ALA A CB  1 
ATOM   209   N  N   . VAL A  1 28  ? 74.836  19.549  76.511  1.00 7.64  ? 28   VAL A N   1 
ATOM   210   C  CA  . VAL A  1 28  ? 75.337  18.700  77.566  1.00 7.68  ? 28   VAL A CA  1 
ATOM   211   C  C   . VAL A  1 28  ? 75.924  17.487  76.869  1.00 7.39  ? 28   VAL A C   1 
ATOM   212   O  O   . VAL A  1 28  ? 75.540  17.118  75.742  1.00 6.82  ? 28   VAL A O   1 
ATOM   213   C  CB  . VAL A  1 28  ? 74.270  18.185  78.584  1.00 8.46  ? 28   VAL A CB  1 
ATOM   214   C  CG1 . VAL A  1 28  ? 73.605  19.341  79.368  1.00 6.01  ? 28   VAL A CG1 1 
ATOM   215   C  CG2 . VAL A  1 28  ? 73.191  17.297  77.882  1.00 6.57  ? 28   VAL A CG2 1 
ATOM   216   N  N   . THR A  1 29  ? 76.859  16.845  77.557  1.00 6.82  ? 29   THR A N   1 
ATOM   217   C  CA  . THR A  1 29  ? 77.227  15.533  77.108  1.00 8.26  ? 29   THR A CA  1 
ATOM   218   C  C   . THR A  1 29  ? 76.726  14.480  78.063  1.00 10.10 ? 29   THR A C   1 
ATOM   219   O  O   . THR A  1 29  ? 76.638  14.721  79.276  1.00 9.53  ? 29   THR A O   1 
ATOM   220   C  CB  . THR A  1 29  ? 78.771  15.383  76.981  1.00 7.63  ? 29   THR A CB  1 
ATOM   221   O  OG1 . THR A  1 29  ? 79.428  15.795  78.192  1.00 9.02  ? 29   THR A OG1 1 
ATOM   222   C  CG2 . THR A  1 29  ? 79.260  16.366  75.887  1.00 8.08  ? 29   THR A CG2 1 
ATOM   223   N  N   . VAL A  1 30  ? 76.468  13.291  77.495  1.00 9.32  ? 30   VAL A N   1 
ATOM   224   C  CA  . VAL A  1 30  ? 76.280  12.106  78.274  1.00 9.67  ? 30   VAL A CA  1 
ATOM   225   C  C   . VAL A  1 30  ? 77.256  11.091  77.675  1.00 9.27  ? 30   VAL A C   1 
ATOM   226   O  O   . VAL A  1 30  ? 77.008  10.550  76.600  1.00 7.62  ? 30   VAL A O   1 
ATOM   227   C  CB  . VAL A  1 30  ? 74.814  11.590  78.196  1.00 11.29 ? 30   VAL A CB  1 
ATOM   228   C  CG1 . VAL A  1 30  ? 74.684  10.228  78.914  1.00 9.93  ? 30   VAL A CG1 1 
ATOM   229   C  CG2 . VAL A  1 30  ? 73.886  12.598  78.826  1.00 12.14 ? 30   VAL A CG2 1 
ATOM   230   N  N   . ASP A  1 31  ? 78.349  10.842  78.386  1.00 7.67  ? 31   ASP A N   1 
ATOM   231   C  CA  . ASP A  1 31  ? 79.480  10.095  77.833  1.00 10.46 ? 31   ASP A CA  1 
ATOM   232   C  C   . ASP A  1 31  ? 79.863  10.669  76.470  1.00 9.81  ? 31   ASP A C   1 
ATOM   233   O  O   . ASP A  1 31  ? 80.151  11.896  76.372  1.00 9.08  ? 31   ASP A O   1 
ATOM   234   C  CB  . ASP A  1 31  ? 79.204  8.562   77.784  1.00 11.57 ? 31   ASP A CB  1 
ATOM   235   C  CG  . ASP A  1 31  ? 78.892  7.965   79.189  1.00 16.66 ? 31   ASP A CG  1 
ATOM   236   O  OD1 . ASP A  1 31  ? 79.766  8.057   80.067  1.00 18.94 ? 31   ASP A OD1 1 
ATOM   237   O  OD2 . ASP A  1 31  ? 77.815  7.393   79.490  1.00 20.86 ? 31   ASP A OD2 1 
ATOM   238   N  N   . THR A  1 32  ? 79.778  9.845   75.408  1.00 9.11  ? 32   THR A N   1 
ATOM   239   C  CA  . THR A  1 32  ? 80.182  10.313  74.065  1.00 8.97  ? 32   THR A CA  1 
ATOM   240   C  C   . THR A  1 32  ? 79.131  11.115  73.282  1.00 8.58  ? 32   THR A C   1 
ATOM   241   O  O   . THR A  1 32  ? 79.450  11.670  72.259  1.00 8.08  ? 32   THR A O   1 
ATOM   242   C  CB  . THR A  1 32  ? 80.683  9.204   73.162  1.00 10.83 ? 32   THR A CB  1 
ATOM   243   O  OG1 . THR A  1 32  ? 79.623  8.238   72.971  1.00 12.47 ? 32   THR A OG1 1 
ATOM   244   C  CG2 . THR A  1 32  ? 81.836  8.457   73.822  1.00 12.26 ? 32   THR A CG2 1 
ATOM   245   N  N   . GLN A  1 33  ? 77.905  11.188  73.793  1.00 7.12  ? 33   GLN A N   1 
ATOM   246   C  CA  . GLN A  1 33  ? 76.789  11.776  73.084  1.00 7.87  ? 33   GLN A CA  1 
ATOM   247   C  C   . GLN A  1 33  ? 76.689  13.213  73.440  1.00 8.39  ? 33   GLN A C   1 
ATOM   248   O  O   . GLN A  1 33  ? 76.816  13.532  74.635  1.00 8.84  ? 33   GLN A O   1 
ATOM   249   C  CB  . GLN A  1 33  ? 75.495  11.113  73.552  1.00 5.44  ? 33   GLN A CB  1 
ATOM   250   C  CG  . GLN A  1 33  ? 75.490  9.616   73.268  1.00 7.68  ? 33   GLN A CG  1 
ATOM   251   C  CD  . GLN A  1 33  ? 74.318  8.864   73.930  1.00 11.35 ? 33   GLN A CD  1 
ATOM   252   O  OE1 . GLN A  1 33  ? 73.511  9.434   74.676  1.00 11.82 ? 33   GLN A OE1 1 
ATOM   253   N  NE2 . GLN A  1 33  ? 74.214  7.603   73.614  1.00 9.63  ? 33   GLN A NE2 1 
ATOM   254   N  N   . LEU A  1 34  ? 76.395  14.059  72.446  1.00 8.16  ? 34   LEU A N   1 
ATOM   255   C  CA  . LEU A  1 34  ? 76.241  15.481  72.731  1.00 7.36  ? 34   LEU A CA  1 
ATOM   256   C  C   . LEU A  1 34  ? 74.847  15.836  72.300  1.00 6.61  ? 34   LEU A C   1 
ATOM   257   O  O   . LEU A  1 34  ? 74.477  15.634  71.131  1.00 7.78  ? 34   LEU A O   1 
ATOM   258   C  CB  . LEU A  1 34  ? 77.294  16.353  72.003  1.00 7.65  ? 34   LEU A CB  1 
ATOM   259   C  CG  . LEU A  1 34  ? 77.468  17.757  72.553  1.00 9.28  ? 34   LEU A CG  1 
ATOM   260   C  CD1 . LEU A  1 34  ? 78.791  18.326  72.129  1.00 13.63 ? 34   LEU A CD1 1 
ATOM   261   C  CD2 . LEU A  1 34  ? 76.252  18.686  72.103  1.00 6.80  ? 34   LEU A CD2 1 
ATOM   262   N  N   . TYR A  1 35  ? 74.090  16.385  73.255  1.00 7.74  ? 35   TYR A N   1 
ATOM   263   C  CA  . TYR A  1 35  ? 72.671  16.787  73.134  1.00 8.77  ? 35   TYR A CA  1 
ATOM   264   C  C   . TYR A  1 35  ? 72.552  18.311  72.997  1.00 9.06  ? 35   TYR A C   1 
ATOM   265   O  O   . TYR A  1 35  ? 73.230  19.113  73.710  1.00 9.52  ? 35   TYR A O   1 
ATOM   266   C  CB  . TYR A  1 35  ? 71.888  16.329  74.371  1.00 8.03  ? 35   TYR A CB  1 
ATOM   267   C  CG  . TYR A  1 35  ? 71.678  14.842  74.443  1.00 8.78  ? 35   TYR A CG  1 
ATOM   268   C  CD1 . TYR A  1 35  ? 72.692  14.011  74.884  1.00 10.53 ? 35   TYR A CD1 1 
ATOM   269   C  CD2 . TYR A  1 35  ? 70.461  14.265  74.060  1.00 12.52 ? 35   TYR A CD2 1 
ATOM   270   C  CE1 . TYR A  1 35  ? 72.506  12.621  74.969  1.00 9.37  ? 35   TYR A CE1 1 
ATOM   271   C  CE2 . TYR A  1 35  ? 70.265  12.864  74.095  1.00 11.59 ? 35   TYR A CE2 1 
ATOM   272   C  CZ  . TYR A  1 35  ? 71.305  12.060  74.524  1.00 12.56 ? 35   TYR A CZ  1 
ATOM   273   O  OH  . TYR A  1 35  ? 71.152  10.702  74.564  1.00 13.13 ? 35   TYR A OH  1 
ATOM   274   N  N   . ARG A  1 36  ? 71.643  18.739  72.124  1.00 9.45  ? 36   ARG A N   1 
ATOM   275   C  CA  . ARG A  1 36  ? 71.424  20.166  71.959  1.00 8.84  ? 36   ARG A CA  1 
ATOM   276   C  C   . ARG A  1 36  ? 69.931  20.352  71.977  1.00 8.95  ? 36   ARG A C   1 
ATOM   277   O  O   . ARG A  1 36  ? 69.234  19.608  71.333  1.00 9.88  ? 36   ARG A O   1 
ATOM   278   C  CB  . ARG A  1 36  ? 71.959  20.646  70.605  1.00 9.10  ? 36   ARG A CB  1 
ATOM   279   C  CG  . ARG A  1 36  ? 73.432  21.028  70.625  1.00 8.28  ? 36   ARG A CG  1 
ATOM   280   C  CD  . ARG A  1 36  ? 73.989  21.397  69.237  1.00 6.50  ? 36   ARG A CD  1 
ATOM   281   N  NE  . ARG A  1 36  ? 75.425  21.642  69.325  1.00 5.57  ? 36   ARG A NE  1 
ATOM   282   C  CZ  . ARG A  1 36  ? 76.347  20.720  69.010  1.00 7.12  ? 36   ARG A CZ  1 
ATOM   283   N  NH1 . ARG A  1 36  ? 75.965  19.476  68.609  1.00 5.43  ? 36   ARG A NH1 1 
ATOM   284   N  NH2 . ARG A  1 36  ? 77.641  21.039  69.130  1.00 4.37  ? 36   ARG A NH2 1 
ATOM   285   N  N   . PHE A  1 37  ? 69.449  21.394  72.647  1.00 8.51  ? 37   PHE A N   1 
ATOM   286   C  CA  . PHE A  1 37  ? 68.002  21.621  72.795  1.00 7.81  ? 37   PHE A CA  1 
ATOM   287   C  C   . PHE A  1 37  ? 67.539  22.834  72.013  1.00 6.71  ? 37   PHE A C   1 
ATOM   288   O  O   . PHE A  1 37  ? 67.532  23.914  72.528  1.00 8.47  ? 37   PHE A O   1 
ATOM   289   C  CB  . PHE A  1 37  ? 67.718  21.712  74.305  1.00 5.87  ? 37   PHE A CB  1 
ATOM   290   C  CG  . PHE A  1 37  ? 68.305  20.533  75.007  1.00 6.54  ? 37   PHE A CG  1 
ATOM   291   C  CD1 . PHE A  1 37  ? 67.693  19.299  74.883  1.00 5.14  ? 37   PHE A CD1 1 
ATOM   292   C  CD2 . PHE A  1 37  ? 69.557  20.649  75.636  1.00 8.01  ? 37   PHE A CD2 1 
ATOM   293   C  CE1 . PHE A  1 37  ? 68.286  18.134  75.438  1.00 11.40 ? 37   PHE A CE1 1 
ATOM   294   C  CE2 . PHE A  1 37  ? 70.149  19.512  76.190  1.00 12.26 ? 37   PHE A CE2 1 
ATOM   295   C  CZ  . PHE A  1 37  ? 69.510  18.265  76.071  1.00 4.07  ? 37   PHE A CZ  1 
ATOM   296   N  N   . TYR A  1 38  ? 67.125  22.612  70.776  1.00 7.34  ? 38   TYR A N   1 
ATOM   297   C  CA  . TYR A  1 38  ? 66.813  23.679  69.846  1.00 6.58  ? 38   TYR A CA  1 
ATOM   298   C  C   . TYR A  1 38  ? 65.442  24.212  70.207  1.00 7.27  ? 38   TYR A C   1 
ATOM   299   O  O   . TYR A  1 38  ? 65.231  25.423  70.128  1.00 8.20  ? 38   TYR A O   1 
ATOM   300   C  CB  . TYR A  1 38  ? 66.769  23.133  68.391  1.00 7.41  ? 38   TYR A CB  1 
ATOM   301   C  CG  . TYR A  1 38  ? 68.131  22.631  67.902  1.00 9.44  ? 38   TYR A CG  1 
ATOM   302   C  CD1 . TYR A  1 38  ? 69.207  23.523  67.774  1.00 9.41  ? 38   TYR A CD1 1 
ATOM   303   C  CD2 . TYR A  1 38  ? 68.320  21.301  67.540  1.00 9.99  ? 38   TYR A CD2 1 
ATOM   304   C  CE1 . TYR A  1 38  ? 70.430  23.121  67.326  1.00 11.19 ? 38   TYR A CE1 1 
ATOM   305   C  CE2 . TYR A  1 38  ? 69.556  20.871  67.075  1.00 11.42 ? 38   TYR A CE2 1 
ATOM   306   C  CZ  . TYR A  1 38  ? 70.607  21.789  66.978  1.00 10.64 ? 38   TYR A CZ  1 
ATOM   307   O  OH  . TYR A  1 38  ? 71.828  21.386  66.530  1.00 8.02  ? 38   TYR A OH  1 
ATOM   308   N  N   . VAL A  1 39  ? 64.520  23.315  70.605  1.00 7.74  ? 39   VAL A N   1 
ATOM   309   C  CA  . VAL A  1 39  ? 63.230  23.758  71.163  1.00 7.70  ? 39   VAL A CA  1 
ATOM   310   C  C   . VAL A  1 39  ? 63.033  23.075  72.495  1.00 8.01  ? 39   VAL A C   1 
ATOM   311   O  O   . VAL A  1 39  ? 63.275  21.854  72.633  1.00 6.59  ? 39   VAL A O   1 
ATOM   312   C  CB  . VAL A  1 39  ? 62.022  23.406  70.243  1.00 6.99  ? 39   VAL A CB  1 
ATOM   313   C  CG1 . VAL A  1 39  ? 60.747  23.881  70.884  1.00 9.30  ? 39   VAL A CG1 1 
ATOM   314   C  CG2 . VAL A  1 39  ? 62.164  24.050  68.837  1.00 7.97  ? 39   VAL A CG2 1 
ATOM   315   N  N   . THR A  1 40  ? 62.642  23.847  73.510  1.00 8.20  ? 40   THR A N   1 
ATOM   316   C  CA  . THR A  1 40  ? 62.530  23.270  74.864  1.00 7.26  ? 40   THR A CA  1 
ATOM   317   C  C   . THR A  1 40  ? 61.133  23.454  75.384  1.00 8.14  ? 40   THR A C   1 
ATOM   318   O  O   . THR A  1 40  ? 60.284  24.099  74.734  1.00 7.69  ? 40   THR A O   1 
ATOM   319   C  CB  . THR A  1 40  ? 63.476  23.978  75.873  1.00 9.14  ? 40   THR A CB  1 
ATOM   320   O  OG1 . THR A  1 40  ? 63.145  25.373  75.987  1.00 7.09  ? 40   THR A OG1 1 
ATOM   321   C  CG2 . THR A  1 40  ? 64.985  23.903  75.494  1.00 6.49  ? 40   THR A CG2 1 
ATOM   322   N  N   . GLY A  1 41  ? 60.850  22.900  76.571  1.00 7.55  ? 41   GLY A N   1 
ATOM   323   C  CA  . GLY A  1 41  ? 59.595  23.271  77.216  1.00 7.97  ? 41   GLY A CA  1 
ATOM   324   C  C   . GLY A  1 41  ? 59.374  24.795  77.383  1.00 7.50  ? 41   GLY A C   1 
ATOM   325   O  O   . GLY A  1 41  ? 58.339  25.372  76.903  1.00 9.15  ? 41   GLY A O   1 
ATOM   326   N  N   . PRO A  1 42  ? 60.228  25.479  78.130  1.00 7.51  ? 42   PRO A N   1 
ATOM   327   C  CA  . PRO A  1 42  ? 60.048  26.940  78.276  1.00 8.55  ? 42   PRO A CA  1 
ATOM   328   C  C   . PRO A  1 42  ? 59.907  27.648  76.912  1.00 8.36  ? 42   PRO A C   1 
ATOM   329   O  O   . PRO A  1 42  ? 59.083  28.544  76.791  1.00 9.39  ? 42   PRO A O   1 
ATOM   330   C  CB  . PRO A  1 42  ? 61.341  27.366  78.971  1.00 7.81  ? 42   PRO A CB  1 
ATOM   331   C  CG  . PRO A  1 42  ? 61.641  26.163  79.879  1.00 8.82  ? 42   PRO A CG  1 
ATOM   332   C  CD  . PRO A  1 42  ? 61.347  24.971  78.954  1.00 7.84  ? 42   PRO A CD  1 
ATOM   333   N  N   . SER A  1 43  ? 60.672  27.246  75.884  1.00 9.33  ? 43   SER A N   1 
ATOM   334   C  CA  . SER A  1 43  ? 60.647  28.024  74.645  1.00 9.33  ? 43   SER A CA  1 
ATOM   335   C  C   . SER A  1 43  ? 59.410  27.799  73.816  1.00 9.40  ? 43   SER A C   1 
ATOM   336   O  O   . SER A  1 43  ? 59.055  28.679  72.996  1.00 10.76 ? 43   SER A O   1 
ATOM   337   C  CB  . SER A  1 43  ? 61.908  27.832  73.758  1.00 8.04  ? 43   SER A CB  1 
ATOM   338   O  OG  . SER A  1 43  ? 61.916  26.589  73.047  1.00 8.26  ? 43   SER A OG  1 
ATOM   339   N  N   . SER A  1 44  ? 58.757  26.645  74.023  1.00 8.87  ? 44   SER A N   1 
ATOM   340   C  CA  . SER A  1 44  ? 57.563  26.296  73.240  1.00 8.95  ? 44   SER A CA  1 
ATOM   341   C  C   . SER A  1 44  ? 56.282  26.367  74.083  1.00 8.33  ? 44   SER A C   1 
ATOM   342   O  O   . SER A  1 44  ? 55.212  25.970  73.601  1.00 6.86  ? 44   SER A O   1 
ATOM   343   C  CB  . SER A  1 44  ? 57.714  24.887  72.656  1.00 8.79  ? 44   SER A CB  1 
ATOM   344   O  OG  . SER A  1 44  ? 57.599  23.902  73.687  1.00 11.75 ? 44   SER A OG  1 
ATOM   345   N  N   . GLY A  1 45  ? 56.395  26.899  75.317  1.00 6.73  ? 45   GLY A N   1 
ATOM   346   C  CA  . GLY A  1 45  ? 55.291  26.848  76.274  1.00 7.61  ? 45   GLY A CA  1 
ATOM   347   C  C   . GLY A  1 45  ? 54.763  25.424  76.490  1.00 8.04  ? 45   GLY A C   1 
ATOM   348   O  O   . GLY A  1 45  ? 53.547  25.219  76.576  1.00 8.68  ? 45   GLY A O   1 
ATOM   349   N  N   . TYR A  1 46  ? 55.700  24.468  76.500  1.00 7.15  ? 46   TYR A N   1 
ATOM   350   C  CA  . TYR A  1 46  ? 55.498  23.074  76.908  1.00 8.77  ? 46   TYR A CA  1 
ATOM   351   C  C   . TYR A  1 46  ? 54.865  22.245  75.825  1.00 8.92  ? 46   TYR A C   1 
ATOM   352   O  O   . TYR A  1 46  ? 54.460  21.106  76.071  1.00 9.29  ? 46   TYR A O   1 
ATOM   353   C  CB  . TYR A  1 46  ? 54.845  22.955  78.329  1.00 9.10  ? 46   TYR A CB  1 
ATOM   354   C  CG  . TYR A  1 46  ? 55.782  23.633  79.271  1.00 8.48  ? 46   TYR A CG  1 
ATOM   355   C  CD1 . TYR A  1 46  ? 56.955  23.024  79.667  1.00 8.35  ? 46   TYR A CD1 1 
ATOM   356   C  CD2 . TYR A  1 46  ? 55.564  24.965  79.656  1.00 11.43 ? 46   TYR A CD2 1 
ATOM   357   C  CE1 . TYR A  1 46  ? 57.864  23.706  80.474  1.00 11.05 ? 46   TYR A CE1 1 
ATOM   358   C  CE2 . TYR A  1 46  ? 56.469  25.646  80.441  1.00 11.57 ? 46   TYR A CE2 1 
ATOM   359   C  CZ  . TYR A  1 46  ? 57.612  25.011  80.838  1.00 12.11 ? 46   TYR A CZ  1 
ATOM   360   O  OH  . TYR A  1 46  ? 58.487  25.716  81.617  1.00 16.61 ? 46   TYR A OH  1 
ATOM   361   N  N   . ALA A  1 47  ? 54.883  22.784  74.596  1.00 7.50  ? 47   ALA A N   1 
ATOM   362   C  CA  . ALA A  1 47  ? 54.201  22.132  73.490  1.00 8.09  ? 47   ALA A CA  1 
ATOM   363   C  C   . ALA A  1 47  ? 55.029  20.931  73.068  1.00 7.11  ? 47   ALA A C   1 
ATOM   364   O  O   . ALA A  1 47  ? 54.469  19.857  72.862  1.00 6.69  ? 47   ALA A O   1 
ATOM   365   C  CB  . ALA A  1 47  ? 53.972  23.095  72.307  1.00 6.74  ? 47   ALA A CB  1 
ATOM   366   N  N   . PHE A  1 48  ? 56.340  21.098  72.956  1.00 7.25  ? 48   PHE A N   1 
ATOM   367   C  CA  . PHE A  1 48  ? 57.211  19.970  72.492  1.00 7.86  ? 48   PHE A CA  1 
ATOM   368   C  C   . PHE A  1 48  ? 58.669  20.289  72.737  1.00 7.73  ? 48   PHE A C   1 
ATOM   369   O  O   . PHE A  1 48  ? 59.048  21.443  72.917  1.00 7.95  ? 48   PHE A O   1 
ATOM   370   C  CB  . PHE A  1 48  ? 57.033  19.584  70.958  1.00 6.43  ? 48   PHE A CB  1 
ATOM   371   C  CG  . PHE A  1 48  ? 56.873  20.757  70.023  1.00 7.89  ? 48   PHE A CG  1 
ATOM   372   C  CD1 . PHE A  1 48  ? 57.980  21.485  69.554  1.00 11.49 ? 48   PHE A CD1 1 
ATOM   373   C  CD2 . PHE A  1 48  ? 55.601  21.162  69.613  1.00 9.43  ? 48   PHE A CD2 1 
ATOM   374   C  CE1 . PHE A  1 48  ? 57.804  22.597  68.718  1.00 8.41  ? 48   PHE A CE1 1 
ATOM   375   C  CE2 . PHE A  1 48  ? 55.430  22.266  68.765  1.00 10.70 ? 48   PHE A CE2 1 
ATOM   376   C  CZ  . PHE A  1 48  ? 56.528  23.003  68.348  1.00 8.64  ? 48   PHE A CZ  1 
ATOM   377   N  N   . THR A  1 49  ? 59.515  19.257  72.655  1.00 8.57  ? 49   THR A N   1 
ATOM   378   C  CA  . THR A  1 49  ? 60.944  19.480  72.606  1.00 8.81  ? 49   THR A CA  1 
ATOM   379   C  C   . THR A  1 49  ? 61.443  18.997  71.241  1.00 9.57  ? 49   THR A C   1 
ATOM   380   O  O   . THR A  1 49  ? 60.961  18.023  70.726  1.00 7.88  ? 49   THR A O   1 
ATOM   381   C  CB  . THR A  1 49  ? 61.591  18.658  73.711  1.00 9.35  ? 49   THR A CB  1 
ATOM   382   O  OG1 . THR A  1 49  ? 61.143  19.156  74.997  1.00 12.40 ? 49   THR A OG1 1 
ATOM   383   C  CG2 . THR A  1 49  ? 63.141  18.822  73.725  1.00 7.70  ? 49   THR A CG2 1 
ATOM   384   N  N   . LEU A  1 50  ? 62.411  19.712  70.674  1.00 9.54  ? 50   LEU A N   1 
ATOM   385   C  CA  . LEU A  1 50  ? 63.086  19.263  69.442  1.00 8.29  ? 50   LEU A CA  1 
ATOM   386   C  C   . LEU A  1 50  ? 64.567  19.349  69.806  1.00 8.98  ? 50   LEU A C   1 
ATOM   387   O  O   . LEU A  1 50  ? 65.093  20.420  70.117  1.00 8.48  ? 50   LEU A O   1 
ATOM   388   C  CB  . LEU A  1 50  ? 62.758  20.223  68.281  1.00 7.49  ? 50   LEU A CB  1 
ATOM   389   C  CG  . LEU A  1 50  ? 63.108  19.680  66.884  1.00 8.19  ? 50   LEU A CG  1 
ATOM   390   C  CD1 . LEU A  1 50  ? 62.228  20.431  65.860  1.00 12.57 ? 50   LEU A CD1 1 
ATOM   391   C  CD2 . LEU A  1 50  ? 64.653  19.925  66.651  1.00 7.93  ? 50   LEU A CD2 1 
ATOM   392   N  N   . MET A  1 51  ? 65.233  18.203  69.817  1.00 10.40 ? 51   MET A N   1 
ATOM   393   C  CA  . MET A  1 51  ? 66.601  18.156  70.253  1.00 11.27 ? 51   MET A CA  1 
ATOM   394   C  C   . MET A  1 51  ? 67.449  17.379  69.251  1.00 11.40 ? 51   MET A C   1 
ATOM   395   O  O   . MET A  1 51  ? 66.935  16.542  68.492  1.00 12.50 ? 51   MET A O   1 
ATOM   396   C  CB  . MET A  1 51  ? 66.693  17.511  71.626  1.00 11.93 ? 51   MET A CB  1 
ATOM   397   C  CG  . MET A  1 51  ? 66.237  15.988  71.655  1.00 12.89 ? 51   MET A CG  1 
ATOM   398   S  SD  . MET A  1 51  ? 66.574  15.359  73.302  1.00 16.50 ? 51   MET A SD  1 
ATOM   399   C  CE  . MET A  1 51  ? 66.296  13.702  73.023  1.00 14.70 ? 51   MET A CE  1 
ATOM   400   N  N   . GLY A  1 52  ? 68.739  17.650  69.260  1.00 9.82  ? 52   GLY A N   1 
ATOM   401   C  CA  . GLY A  1 52  ? 69.628  16.912  68.381  1.00 10.44 ? 52   GLY A CA  1 
ATOM   402   C  C   . GLY A  1 52  ? 70.663  16.179  69.214  1.00 10.61 ? 52   GLY A C   1 
ATOM   403   O  O   . GLY A  1 52  ? 71.213  16.760  70.170  1.00 10.45 ? 52   GLY A O   1 
ATOM   404   N  N   . THR A  1 53  ? 70.980  14.950  68.842  1.00 9.22  ? 53   THR A N   1 
ATOM   405   C  CA  . THR A  1 53  ? 72.052  14.234  69.566  1.00 8.55  ? 53   THR A CA  1 
ATOM   406   C  C   . THR A  1 53  ? 73.088  13.846  68.535  1.00 9.44  ? 53   THR A C   1 
ATOM   407   O  O   . THR A  1 53  ? 72.733  13.200  67.563  1.00 10.01 ? 53   THR A O   1 
ATOM   408   C  CB  . THR A  1 53  ? 71.470  12.944  70.177  1.00 9.04  ? 53   THR A CB  1 
ATOM   409   O  OG1 . THR A  1 53  ? 70.380  13.270  71.047  1.00 10.98 ? 53   THR A OG1 1 
ATOM   410   C  CG2 . THR A  1 53  ? 72.499  12.181  71.106  1.00 5.41  ? 53   THR A CG2 1 
ATOM   411   N  N   . ASN A  1 54  ? 74.363  14.215  68.727  1.00 9.79  ? 54   ASN A N   1 
ATOM   412   C  CA  . ASN A  1 54  ? 75.413  13.770  67.826  1.00 9.32  ? 54   ASN A CA  1 
ATOM   413   C  C   . ASN A  1 54  ? 76.303  12.823  68.595  1.00 9.23  ? 54   ASN A C   1 
ATOM   414   O  O   . ASN A  1 54  ? 76.532  13.035  69.766  1.00 9.59  ? 54   ASN A O   1 
ATOM   415   C  CB  . ASN A  1 54  ? 76.188  14.967  67.273  1.00 8.67  ? 54   ASN A CB  1 
ATOM   416   C  CG  . ASN A  1 54  ? 75.346  15.774  66.285  1.00 11.13 ? 54   ASN A CG  1 
ATOM   417   O  OD1 . ASN A  1 54  ? 74.471  16.557  66.682  1.00 10.78 ? 54   ASN A OD1 1 
ATOM   418   N  ND2 . ASN A  1 54  ? 75.608  15.576  64.977  1.00 8.22  ? 54   ASN A ND2 1 
ATOM   419   N  N   . ALA A  1 55  ? 76.778  11.771  67.954  1.00 8.26  ? 55   ALA A N   1 
ATOM   420   C  CA  . ALA A  1 55  ? 77.538  10.743  68.699  1.00 9.32  ? 55   ALA A CA  1 
ATOM   421   C  C   . ALA A  1 55  ? 78.313  9.866   67.719  1.00 7.84  ? 55   ALA A C   1 
ATOM   422   O  O   . ALA A  1 55  ? 77.872  9.729   66.561  1.00 9.13  ? 55   ALA A O   1 
ATOM   423   C  CB  . ALA A  1 55  ? 76.535  9.857   69.483  1.00 6.28  ? 55   ALA A CB  1 
ATOM   424   N  N   . PRO A  1 56  ? 79.424  9.278   68.174  1.00 7.44  ? 56   PRO A N   1 
ATOM   425   C  CA  . PRO A  1 56  ? 80.178  8.304   67.369  1.00 6.34  ? 56   PRO A CA  1 
ATOM   426   C  C   . PRO A  1 56  ? 79.601  6.900   67.497  1.00 6.79  ? 56   PRO A C   1 
ATOM   427   O  O   . PRO A  1 56  ? 78.697  6.661   68.337  1.00 8.06  ? 56   PRO A O   1 
ATOM   428   C  CB  . PRO A  1 56  ? 81.576  8.314   68.022  1.00 5.65  ? 56   PRO A CB  1 
ATOM   429   C  CG  . PRO A  1 56  ? 81.239  8.522   69.493  1.00 5.95  ? 56   PRO A CG  1 
ATOM   430   C  CD  . PRO A  1 56  ? 80.112  9.583   69.440  1.00 5.37  ? 56   PRO A CD  1 
ATOM   431   N  N   . HIS A  1 57  ? 80.105  6.026   66.655  1.00 6.49  ? 57   HIS A N   1 
ATOM   432   C  CA  . HIS A  1 57  ? 79.806  4.580   66.741  1.00 7.41  ? 57   HIS A CA  1 
ATOM   433   C  C   . HIS A  1 57  ? 80.080  4.147   68.168  1.00 7.15  ? 57   HIS A C   1 
ATOM   434   O  O   . HIS A  1 57  ? 81.074  4.582   68.762  1.00 6.23  ? 57   HIS A O   1 
ATOM   435   C  CB  . HIS A  1 57  ? 80.762  3.767   65.862  1.00 7.17  ? 57   HIS A CB  1 
ATOM   436   C  CG  . HIS A  1 57  ? 80.681  2.303   66.127  1.00 8.21  ? 57   HIS A CG  1 
ATOM   437   N  ND1 . HIS A  1 57  ? 79.707  1.507   65.562  1.00 9.44  ? 57   HIS A ND1 1 
ATOM   438   C  CD2 . HIS A  1 57  ? 81.412  1.497   66.943  1.00 8.17  ? 57   HIS A CD2 1 
ATOM   439   C  CE1 . HIS A  1 57  ? 79.869  0.259   65.986  1.00 10.72 ? 57   HIS A CE1 1 
ATOM   440   N  NE2 . HIS A  1 57  ? 80.868  0.238   66.857  1.00 7.17  ? 57   HIS A NE2 1 
ATOM   441   N  N   . SER A  1 58  ? 79.214  3.286   68.699  1.00 8.16  ? 58   SER A N   1 
ATOM   442   C  CA  . SER A  1 58  ? 79.497  2.615   69.985  1.00 8.58  ? 58   SER A CA  1 
ATOM   443   C  C   . SER A  1 58  ? 79.167  1.145   69.793  1.00 8.99  ? 58   SER A C   1 
ATOM   444   O  O   . SER A  1 58  ? 78.227  0.795   69.082  1.00 8.92  ? 58   SER A O   1 
ATOM   445   C  CB  . SER A  1 58  ? 78.583  3.193   71.069  1.00 8.79  ? 58   SER A CB  1 
ATOM   446   O  OG  . SER A  1 58  ? 78.669  2.443   72.269  1.00 9.93  ? 58   SER A OG  1 
ATOM   447   N  N   . ASP A  1 59  ? 79.934  0.283   70.420  1.00 9.23  ? 59   ASP A N   1 
ATOM   448   C  CA  . ASP A  1 59  ? 79.593  -1.143  70.431  1.00 9.72  ? 59   ASP A CA  1 
ATOM   449   C  C   . ASP A  1 59  ? 78.554  -1.487  71.483  1.00 10.36 ? 59   ASP A C   1 
ATOM   450   O  O   . ASP A  1 59  ? 78.127  -2.653  71.572  1.00 11.23 ? 59   ASP A O   1 
ATOM   451   C  CB  . ASP A  1 59  ? 80.854  -1.970  70.692  1.00 10.84 ? 59   ASP A CB  1 
ATOM   452   C  CG  . ASP A  1 59  ? 81.820  -1.922  69.522  1.00 14.26 ? 59   ASP A CG  1 
ATOM   453   O  OD1 . ASP A  1 59  ? 81.357  -1.896  68.349  1.00 12.06 ? 59   ASP A OD1 1 
ATOM   454   O  OD2 . ASP A  1 59  ? 83.065  -1.856  69.697  1.00 18.60 ? 59   ASP A OD2 1 
ATOM   455   N  N   . ALA A  1 60  ? 78.176  -0.518  72.312  1.00 9.43  ? 60   ALA A N   1 
ATOM   456   C  CA  . ALA A  1 60  ? 77.209  -0.787  73.390  1.00 9.96  ? 60   ALA A CA  1 
ATOM   457   C  C   . ALA A  1 60  ? 75.877  -0.023  73.189  1.00 8.88  ? 60   ALA A C   1 
ATOM   458   O  O   . ALA A  1 60  ? 75.824  0.922   72.412  1.00 8.50  ? 60   ALA A O   1 
ATOM   459   C  CB  . ALA A  1 60  ? 77.830  -0.386  74.714  1.00 10.20 ? 60   ALA A CB  1 
ATOM   460   N  N   . LEU A  1 61  ? 74.827  -0.371  73.928  1.00 7.83  ? 61   LEU A N   1 
ATOM   461   C  CA  . LEU A  1 61  ? 73.575  0.423   73.811  1.00 9.42  ? 61   LEU A CA  1 
ATOM   462   C  C   . LEU A  1 61  ? 73.813  1.862   74.174  1.00 9.76  ? 61   LEU A C   1 
ATOM   463   O  O   . LEU A  1 61  ? 74.729  2.153   74.937  1.00 9.93  ? 61   LEU A O   1 
ATOM   464   C  CB  . LEU A  1 61  ? 72.487  -0.155  74.734  1.00 8.71  ? 61   LEU A CB  1 
ATOM   465   C  CG  . LEU A  1 61  ? 72.004  -1.556  74.428  1.00 10.13 ? 61   LEU A CG  1 
ATOM   466   C  CD1 . LEU A  1 61  ? 71.018  -1.949  75.522  1.00 9.11  ? 61   LEU A CD1 1 
ATOM   467   C  CD2 . LEU A  1 61  ? 71.312  -1.587  72.991  1.00 8.86  ? 61   LEU A CD2 1 
ATOM   468   N  N   . GLY A  1 62  ? 72.997  2.779   73.621  1.00 10.54 ? 62   GLY A N   1 
ATOM   469   C  CA  . GLY A  1 62  ? 73.145  4.183   73.914  1.00 10.06 ? 62   GLY A CA  1 
ATOM   470   C  C   . GLY A  1 62  ? 72.387  4.606   75.169  1.00 10.23 ? 62   GLY A C   1 
ATOM   471   O  O   . GLY A  1 62  ? 72.566  5.735   75.677  1.00 9.79  ? 62   GLY A O   1 
ATOM   472   N  N   . VAL A  1 63  ? 71.582  3.684   75.701  1.00 8.65  ? 63   VAL A N   1 
ATOM   473   C  CA  . VAL A  1 63  ? 70.818  3.939   76.918  1.00 8.40  ? 63   VAL A CA  1 
ATOM   474   C  C   . VAL A  1 63  ? 70.232  2.613   77.345  1.00 7.38  ? 63   VAL A C   1 
ATOM   475   O  O   . VAL A  1 63  ? 70.044  1.736   76.514  1.00 7.77  ? 63   VAL A O   1 
ATOM   476   C  CB  . VAL A  1 63  ? 69.654  5.000   76.645  1.00 9.11  ? 63   VAL A CB  1 
ATOM   477   C  CG1 . VAL A  1 63  ? 68.623  4.431   75.631  1.00 9.51  ? 63   VAL A CG1 1 
ATOM   478   C  CG2 . VAL A  1 63  ? 68.976  5.417   77.967  1.00 10.55 ? 63   VAL A CG2 1 
ATOM   479   N  N   . LEU A  1 64  ? 70.025  2.409   78.647  1.00 6.18  ? 64   LEU A N   1 
ATOM   480   C  CA  . LEU A  1 64  ? 69.384  1.199   79.053  1.00 6.44  ? 64   LEU A CA  1 
ATOM   481   C  C   . LEU A  1 64  ? 67.923  1.259   78.592  1.00 5.95  ? 64   LEU A C   1 
ATOM   482   O  O   . LEU A  1 64  ? 67.376  2.379   78.391  1.00 4.58  ? 64   LEU A O   1 
ATOM   483   C  CB  . LEU A  1 64  ? 69.510  0.998   80.575  1.00 6.76  ? 64   LEU A CB  1 
ATOM   484   C  CG  . LEU A  1 64  ? 70.902  0.552   80.976  1.00 9.19  ? 64   LEU A CG  1 
ATOM   485   C  CD1 . LEU A  1 64  ? 70.993  0.646   82.489  1.00 11.47 ? 64   LEU A CD1 1 
ATOM   486   C  CD2 . LEU A  1 64  ? 71.215  -0.902  80.477  1.00 9.98  ? 64   LEU A CD2 1 
ATOM   487   N  N   . PRO A  1 65  ? 67.290  0.085   78.377  1.00 5.11  ? 65   PRO A N   1 
ATOM   488   C  CA  . PRO A  1 65  ? 65.886  0.073   77.928  1.00 5.86  ? 65   PRO A CA  1 
ATOM   489   C  C   . PRO A  1 65  ? 64.969  0.721   78.979  1.00 7.21  ? 65   PRO A C   1 
ATOM   490   O  O   . PRO A  1 65  ? 65.190  0.533   80.207  1.00 6.71  ? 65   PRO A O   1 
ATOM   491   C  CB  . PRO A  1 65  ? 65.556  -1.427  77.860  1.00 4.91  ? 65   PRO A CB  1 
ATOM   492   C  CG  . PRO A  1 65  ? 66.923  -2.049  77.622  1.00 6.98  ? 65   PRO A CG  1 
ATOM   493   C  CD  . PRO A  1 65  ? 67.805  -1.278  78.596  1.00 4.63  ? 65   PRO A CD  1 
ATOM   494   N  N   . HIS A  1 66  ? 63.934  1.449   78.524  1.00 5.95  ? 66   HIS A N   1 
ATOM   495   C  CA  . HIS A  1 66  ? 63.147  2.225   79.453  1.00 5.39  ? 66   HIS A CA  1 
ATOM   496   C  C   . HIS A  1 66  ? 61.825  2.549   78.807  1.00 5.96  ? 66   HIS A C   1 
ATOM   497   O  O   . HIS A  1 66  ? 61.642  2.283   77.604  1.00 6.60  ? 66   HIS A O   1 
ATOM   498   C  CB  . HIS A  1 66  ? 63.953  3.497   79.846  1.00 4.82  ? 66   HIS A CB  1 
ATOM   499   C  CG  . HIS A  1 66  ? 64.229  4.424   78.700  1.00 6.13  ? 66   HIS A CG  1 
ATOM   500   N  ND1 . HIS A  1 66  ? 65.322  4.285   77.859  1.00 8.15  ? 66   HIS A ND1 1 
ATOM   501   C  CD2 . HIS A  1 66  ? 63.545  5.503   78.245  1.00 4.35  ? 66   HIS A CD2 1 
ATOM   502   C  CE1 . HIS A  1 66  ? 65.289  5.239   76.930  1.00 8.83  ? 66   HIS A CE1 1 
ATOM   503   N  NE2 . HIS A  1 66  ? 64.223  5.994   77.142  1.00 7.17  ? 66   HIS A NE2 1 
ATOM   504   N  N   . ILE A  1 67  ? 60.917  3.135   79.577  1.00 7.02  ? 67   ILE A N   1 
ATOM   505   C  CA  . ILE A  1 67  ? 59.668  3.678   79.088  1.00 7.62  ? 67   ILE A CA  1 
ATOM   506   C  C   . ILE A  1 67  ? 59.423  5.054   79.689  1.00 7.10  ? 67   ILE A C   1 
ATOM   507   O  O   . ILE A  1 67  ? 59.988  5.427   80.707  1.00 7.69  ? 67   ILE A O   1 
ATOM   508   C  CB  . ILE A  1 67  ? 58.360  2.808   79.370  1.00 9.80  ? 67   ILE A CB  1 
ATOM   509   C  CG1 . ILE A  1 67  ? 57.910  2.968   80.813  1.00 13.07 ? 67   ILE A CG1 1 
ATOM   510   C  CG2 . ILE A  1 67  ? 58.444  1.324   78.887  1.00 10.64 ? 67   ILE A CG2 1 
ATOM   511   C  CD1 . ILE A  1 67  ? 56.882  1.944   81.284  1.00 14.18 ? 67   ILE A CD1 1 
ATOM   512   N  N   . HIS A  1 68  ? 58.540  5.775   79.024  1.00 5.61  ? 68   HIS A N   1 
ATOM   513   C  CA  . HIS A  1 68  ? 58.007  7.051   79.475  1.00 6.52  ? 68   HIS A CA  1 
ATOM   514   C  C   . HIS A  1 68  ? 56.492  6.874   79.539  1.00 6.56  ? 68   HIS A C   1 
ATOM   515   O  O   . HIS A  1 68  ? 55.877  6.469   78.524  1.00 7.73  ? 68   HIS A O   1 
ATOM   516   C  CB  . HIS A  1 68  ? 58.300  8.104   78.413  1.00 6.23  ? 68   HIS A CB  1 
ATOM   517   C  CG  . HIS A  1 68  ? 59.738  8.158   78.015  1.00 9.05  ? 68   HIS A CG  1 
ATOM   518   N  ND1 . HIS A  1 68  ? 60.741  8.528   78.894  1.00 10.80 ? 68   HIS A ND1 1 
ATOM   519   C  CD2 . HIS A  1 68  ? 60.346  7.919   76.829  1.00 9.91  ? 68   HIS A CD2 1 
ATOM   520   C  CE1 . HIS A  1 68  ? 61.899  8.515   78.261  1.00 8.26  ? 68   HIS A CE1 1 
ATOM   521   N  NE2 . HIS A  1 68  ? 61.692  8.127   77.017  1.00 9.36  ? 68   HIS A NE2 1 
ATOM   522   N  N   . GLN A  1 69  ? 55.900  7.183   80.697  1.00 5.22  ? 69   GLN A N   1 
ATOM   523   C  CA  . GLN A  1 69  ? 54.438  7.082   80.842  1.00 5.91  ? 69   GLN A CA  1 
ATOM   524   C  C   . GLN A  1 69  ? 53.725  8.328   80.328  1.00 5.16  ? 69   GLN A C   1 
ATOM   525   O  O   . GLN A  1 69  ? 52.552  8.234   79.988  1.00 3.62  ? 69   GLN A O   1 
ATOM   526   C  CB  . GLN A  1 69  ? 54.019  6.781   82.274  1.00 6.63  ? 69   GLN A CB  1 
ATOM   527   C  CG  . GLN A  1 69  ? 54.531  5.441   82.749  1.00 9.50  ? 69   GLN A CG  1 
ATOM   528   C  CD  . GLN A  1 69  ? 54.070  5.101   84.154  1.00 14.30 ? 69   GLN A CD  1 
ATOM   529   O  OE1 . GLN A  1 69  ? 53.270  5.839   84.746  1.00 15.46 ? 69   GLN A OE1 1 
ATOM   530   N  NE2 . GLN A  1 69  ? 54.530  3.959   84.674  1.00 13.76 ? 69   GLN A NE2 1 
ATOM   531   N  N   . LYS A  1 70  ? 54.406  9.472   80.234  1.00 5.56  ? 70   LYS A N   1 
ATOM   532   C  CA  . LYS A  1 70  ? 53.682  10.697  79.860  1.00 7.26  ? 70   LYS A CA  1 
ATOM   533   C  C   . LYS A  1 70  ? 54.248  11.436  78.630  1.00 7.73  ? 70   LYS A C   1 
ATOM   534   O  O   . LYS A  1 70  ? 53.713  12.465  78.260  1.00 8.43  ? 70   LYS A O   1 
ATOM   535   C  CB  . LYS A  1 70  ? 53.616  11.678  81.017  1.00 8.28  ? 70   LYS A CB  1 
ATOM   536   C  CG  . LYS A  1 70  ? 52.899  11.233  82.282  1.00 11.34 ? 70   LYS A CG  1 
ATOM   537   C  CD  . LYS A  1 70  ? 53.028  12.362  83.318  1.00 15.77 ? 70   LYS A CD  1 
ATOM   538   C  CE  . LYS A  1 70  ? 52.372  12.017  84.627  1.00 20.71 ? 70   LYS A CE  1 
ATOM   539   N  NZ  . LYS A  1 70  ? 52.243  13.304  85.418  1.00 25.05 ? 70   LYS A NZ  1 
ATOM   540   N  N   . HIS A  1 71  ? 55.297  10.902  78.006  1.00 7.44  ? 71   HIS A N   1 
ATOM   541   C  CA  . HIS A  1 71  ? 55.904  11.532  76.853  1.00 7.76  ? 71   HIS A CA  1 
ATOM   542   C  C   . HIS A  1 71  ? 55.962  10.558  75.710  1.00 8.08  ? 71   HIS A C   1 
ATOM   543   O  O   . HIS A  1 71  ? 56.314  9.376   75.887  1.00 7.78  ? 71   HIS A O   1 
ATOM   544   C  CB  . HIS A  1 71  ? 57.356  12.007  77.154  1.00 7.06  ? 71   HIS A CB  1 
ATOM   545   C  CG  . HIS A  1 71  ? 57.423  13.086  78.181  1.00 8.43  ? 71   HIS A CG  1 
ATOM   546   N  ND1 . HIS A  1 71  ? 57.463  12.817  79.529  1.00 9.79  ? 71   HIS A ND1 1 
ATOM   547   C  CD2 . HIS A  1 71  ? 57.350  14.433  78.071  1.00 6.29  ? 71   HIS A CD2 1 
ATOM   548   C  CE1 . HIS A  1 71  ? 57.491  13.958  80.201  1.00 7.03  ? 71   HIS A CE1 1 
ATOM   549   N  NE2 . HIS A  1 71  ? 57.412  14.946  79.344  1.00 6.02  ? 71   HIS A NE2 1 
ATOM   550   N  N   . TYR A  1 72  ? 55.631  11.092  74.538  1.00 7.01  ? 72   TYR A N   1 
ATOM   551   C  CA  . TYR A  1 72  ? 55.748  10.422  73.256  1.00 8.01  ? 72   TYR A CA  1 
ATOM   552   C  C   . TYR A  1 72  ? 57.094  10.859  72.628  1.00 8.07  ? 72   TYR A C   1 
ATOM   553   O  O   . TYR A  1 72  ? 57.371  12.073  72.398  1.00 8.81  ? 72   TYR A O   1 
ATOM   554   C  CB  . TYR A  1 72  ? 54.555  10.850  72.375  1.00 8.15  ? 72   TYR A CB  1 
ATOM   555   C  CG  . TYR A  1 72  ? 54.217  10.000  71.143  1.00 6.48  ? 72   TYR A CG  1 
ATOM   556   C  CD1 . TYR A  1 72  ? 55.224  9.455   70.317  1.00 6.60  ? 72   TYR A CD1 1 
ATOM   557   C  CD2 . TYR A  1 72  ? 52.863  9.790   70.781  1.00 6.08  ? 72   TYR A CD2 1 
ATOM   558   C  CE1 . TYR A  1 72  ? 54.886  8.722   69.166  1.00 4.02  ? 72   TYR A CE1 1 
ATOM   559   C  CE2 . TYR A  1 72  ? 52.541  9.091   69.674  1.00 7.49  ? 72   TYR A CE2 1 
ATOM   560   C  CZ  . TYR A  1 72  ? 53.539  8.559   68.866  1.00 6.47  ? 72   TYR A CZ  1 
ATOM   561   O  OH  . TYR A  1 72  ? 53.162  7.839   67.777  1.00 6.47  ? 72   TYR A OH  1 
ATOM   562   N  N   . GLU A  1 73  ? 57.933  9.872   72.367  1.00 7.34  ? 73   GLU A N   1 
ATOM   563   C  CA  . GLU A  1 73  ? 59.249  10.093  71.746  1.00 7.91  ? 73   GLU A CA  1 
ATOM   564   C  C   . GLU A  1 73  ? 59.262  9.743   70.249  1.00 6.86  ? 73   GLU A C   1 
ATOM   565   O  O   . GLU A  1 73  ? 58.608  8.755   69.811  1.00 8.38  ? 73   GLU A O   1 
ATOM   566   C  CB  . GLU A  1 73  ? 60.332  9.282   72.473  1.00 7.78  ? 73   GLU A CB  1 
ATOM   567   C  CG  . GLU A  1 73  ? 60.634  9.916   73.812  1.00 14.62 ? 73   GLU A CG  1 
ATOM   568   C  CD  . GLU A  1 73  ? 61.923  9.490   74.431  1.00 22.45 ? 73   GLU A CD  1 
ATOM   569   O  OE1 . GLU A  1 73  ? 62.212  8.282   74.364  1.00 23.23 ? 73   GLU A OE1 1 
ATOM   570   O  OE2 . GLU A  1 73  ? 62.610  10.360  75.062  1.00 23.91 ? 73   GLU A OE2 1 
ATOM   571   N  N   . ASN A  1 74  ? 59.939  10.588  69.496  1.00 5.77  ? 74   ASN A N   1 
ATOM   572   C  CA  . ASN A  1 74  ? 60.051  10.480  68.056  1.00 7.57  ? 74   ASN A CA  1 
ATOM   573   C  C   . ASN A  1 74  ? 61.490  10.518  67.675  1.00 7.82  ? 74   ASN A C   1 
ATOM   574   O  O   . ASN A  1 74  ? 62.185  11.469  68.049  1.00 9.24  ? 74   ASN A O   1 
ATOM   575   C  CB  . ASN A  1 74  ? 59.304  11.606  67.351  1.00 5.42  ? 74   ASN A CB  1 
ATOM   576   C  CG  . ASN A  1 74  ? 57.810  11.506  67.571  1.00 7.01  ? 74   ASN A CG  1 
ATOM   577   O  OD1 . ASN A  1 74  ? 57.113  10.732  66.906  1.00 7.05  ? 74   ASN A OD1 1 
ATOM   578   N  ND2 . ASN A  1 74  ? 57.311  12.245  68.561  1.00 6.38  ? 74   ASN A ND2 1 
ATOM   579   N  N   . PHE A  1 75  ? 61.934  9.472   66.956  1.00 7.54  ? 75   PHE A N   1 
ATOM   580   C  CA  . PHE A  1 75  ? 63.332  9.352   66.564  1.00 8.12  ? 75   PHE A CA  1 
ATOM   581   C  C   . PHE A  1 75  ? 63.461  9.579   65.067  1.00 9.42  ? 75   PHE A C   1 
ATOM   582   O  O   . PHE A  1 75  ? 62.872  8.846   64.281  1.00 8.92  ? 75   PHE A O   1 
ATOM   583   C  CB  . PHE A  1 75  ? 63.856  7.929   66.847  1.00 8.96  ? 75   PHE A CB  1 
ATOM   584   C  CG  . PHE A  1 75  ? 64.085  7.640   68.334  1.00 8.88  ? 75   PHE A CG  1 
ATOM   585   C  CD1 . PHE A  1 75  ? 63.024  7.290   69.151  1.00 10.55 ? 75   PHE A CD1 1 
ATOM   586   C  CD2 . PHE A  1 75  ? 65.376  7.728   68.886  1.00 12.71 ? 75   PHE A CD2 1 
ATOM   587   C  CE1 . PHE A  1 75  ? 63.233  7.033   70.533  1.00 12.17 ? 75   PHE A CE1 1 
ATOM   588   C  CE2 . PHE A  1 75  ? 65.582  7.448   70.220  1.00 11.34 ? 75   PHE A CE2 1 
ATOM   589   C  CZ  . PHE A  1 75  ? 64.512  7.123   71.058  1.00 10.43 ? 75   PHE A CZ  1 
ATOM   590   N  N   . TYR A  1 76  ? 64.219  10.587  64.679  1.00 9.17  ? 76   TYR A N   1 
ATOM   591   C  CA  . TYR A  1 76  ? 64.470  10.874  63.261  1.00 10.36 ? 76   TYR A CA  1 
ATOM   592   C  C   . TYR A  1 76  ? 65.964  10.896  62.985  1.00 11.46 ? 76   TYR A C   1 
ATOM   593   O  O   . TYR A  1 76  ? 66.734  11.545  63.719  1.00 10.50 ? 76   TYR A O   1 
ATOM   594   C  CB  . TYR A  1 76  ? 63.926  12.252  62.913  1.00 9.14  ? 76   TYR A CB  1 
ATOM   595   C  CG  . TYR A  1 76  ? 63.988  12.557  61.430  1.00 9.19  ? 76   TYR A CG  1 
ATOM   596   C  CD1 . TYR A  1 76  ? 63.019  12.040  60.542  1.00 7.96  ? 76   TYR A CD1 1 
ATOM   597   C  CD2 . TYR A  1 76  ? 64.976  13.376  60.916  1.00 8.24  ? 76   TYR A CD2 1 
ATOM   598   C  CE1 . TYR A  1 76  ? 63.067  12.329  59.212  1.00 6.97  ? 76   TYR A CE1 1 
ATOM   599   C  CE2 . TYR A  1 76  ? 65.012  13.699  59.576  1.00 9.92  ? 76   TYR A CE2 1 
ATOM   600   C  CZ  . TYR A  1 76  ? 64.057  13.194  58.741  1.00 9.82  ? 76   TYR A CZ  1 
ATOM   601   O  OH  . TYR A  1 76  ? 64.156  13.509  57.413  1.00 9.46  ? 76   TYR A OH  1 
ATOM   602   N  N   . CYS A  1 77  ? 66.404  10.185  61.942  1.00 10.83 ? 77   CYS A N   1 
ATOM   603   C  CA  . CYS A  1 77  ? 67.842  10.154  61.647  1.00 9.74  ? 77   CYS A CA  1 
ATOM   604   C  C   . CYS A  1 77  ? 68.218  11.273  60.660  1.00 10.16 ? 77   CYS A C   1 
ATOM   605   O  O   . CYS A  1 77  ? 67.827  11.254  59.490  1.00 10.23 ? 77   CYS A O   1 
ATOM   606   C  CB  . CYS A  1 77  ? 68.230  8.765   61.071  1.00 9.60  ? 77   CYS A CB  1 
ATOM   607   S  SG  . CYS A  1 77  ? 70.006  8.707   60.776  1.00 9.13  ? 77   CYS A SG  1 
ATOM   608   N  N   . ASN A  1 78  ? 68.937  12.283  61.144  1.00 10.45 ? 78   ASN A N   1 
ATOM   609   C  CA  . ASN A  1 78  ? 69.383  13.408  60.319  1.00 11.59 ? 78   ASN A CA  1 
ATOM   610   C  C   . ASN A  1 78  ? 70.537  12.971  59.419  1.00 10.49 ? 78   ASN A C   1 
ATOM   611   O  O   . ASN A  1 78  ? 70.562  13.303  58.228  1.00 11.11 ? 78   ASN A O   1 
ATOM   612   C  CB  . ASN A  1 78  ? 69.711  14.613  61.252  1.00 13.95 ? 78   ASN A CB  1 
ATOM   613   C  CG  . ASN A  1 78  ? 70.412  15.770  60.542  1.00 19.78 ? 78   ASN A CG  1 
ATOM   614   O  OD1 . ASN A  1 78  ? 71.674  15.874  60.577  1.00 25.89 ? 78   ASN A OD1 1 
ATOM   615   N  ND2 . ASN A  1 78  ? 69.608  16.731  59.985  1.00 24.42 ? 78   ASN A ND2 1 
ATOM   616   N  N   . LYS A  1 79  ? 71.461  12.181  59.967  1.00 8.65  ? 79   LYS A N   1 
ATOM   617   C  CA  . LYS A  1 79  ? 72.603  11.637  59.218  1.00 7.52  ? 79   LYS A CA  1 
ATOM   618   C  C   . LYS A  1 79  ? 73.202  10.471  60.020  1.00 8.46  ? 79   LYS A C   1 
ATOM   619   O  O   . LYS A  1 79  ? 72.889  10.295  61.211  1.00 7.32  ? 79   LYS A O   1 
ATOM   620   C  CB  . LYS A  1 79  ? 73.707  12.683  58.905  1.00 7.84  ? 79   LYS A CB  1 
ATOM   621   C  CG  . LYS A  1 79  ? 74.273  13.427  60.103  1.00 9.84  ? 79   LYS A CG  1 
ATOM   622   C  CD  . LYS A  1 79  ? 75.522  14.221  59.741  1.00 5.68  ? 79   LYS A CD  1 
ATOM   623   C  CE  . LYS A  1 79  ? 75.849  15.208  60.875  1.00 10.44 ? 79   LYS A CE  1 
ATOM   624   N  NZ  . LYS A  1 79  ? 77.114  16.007  60.590  1.00 7.49  ? 79   LYS A NZ  1 
ATOM   625   N  N   . GLY A  1 80  ? 74.030  9.678   59.342  1.00 6.96  ? 80   GLY A N   1 
ATOM   626   C  CA  . GLY A  1 80  ? 74.641  8.495   59.927  1.00 7.42  ? 80   GLY A CA  1 
ATOM   627   C  C   . GLY A  1 80  ? 73.591  7.402   60.059  1.00 7.51  ? 80   GLY A C   1 
ATOM   628   O  O   . GLY A  1 80  ? 72.760  7.215   59.155  1.00 8.75  ? 80   GLY A O   1 
ATOM   629   N  N   . SER A  1 81  ? 73.626  6.681   61.168  1.00 7.06  ? 81   SER A N   1 
ATOM   630   C  CA  . SER A  1 81  ? 72.682  5.598   61.429  1.00 8.14  ? 81   SER A CA  1 
ATOM   631   C  C   . SER A  1 81  ? 72.744  5.171   62.906  1.00 8.31  ? 81   SER A C   1 
ATOM   632   O  O   . SER A  1 81  ? 73.831  5.231   63.594  1.00 8.68  ? 81   SER A O   1 
ATOM   633   C  CB  . SER A  1 81  ? 72.918  4.347   60.537  1.00 7.00  ? 81   SER A CB  1 
ATOM   634   O  OG  . SER A  1 81  ? 74.221  3.836   60.772  1.00 8.65  ? 81   SER A OG  1 
ATOM   635   N  N   . PHE A  1 82  ? 71.584  4.695   63.345  1.00 7.41  ? 82   PHE A N   1 
ATOM   636   C  CA  . PHE A  1 82  ? 71.417  4.180   64.706  1.00 8.58  ? 82   PHE A CA  1 
ATOM   637   C  C   . PHE A  1 82  ? 70.290  3.150   64.692  1.00 8.40  ? 82   PHE A C   1 
ATOM   638   O  O   . PHE A  1 82  ? 69.322  3.293   63.940  1.00 9.35  ? 82   PHE A O   1 
ATOM   639   C  CB  . PHE A  1 82  ? 71.197  5.307   65.719  1.00 9.01  ? 82   PHE A CB  1 
ATOM   640   C  CG  . PHE A  1 82  ? 69.902  6.085   65.521  1.00 8.74  ? 82   PHE A CG  1 
ATOM   641   C  CD1 . PHE A  1 82  ? 68.728  5.674   66.134  1.00 8.96  ? 82   PHE A CD1 1 
ATOM   642   C  CD2 . PHE A  1 82  ? 69.892  7.230   64.777  1.00 9.60  ? 82   PHE A CD2 1 
ATOM   643   C  CE1 . PHE A  1 82  ? 67.484  6.407   65.954  1.00 8.07  ? 82   PHE A CE1 1 
ATOM   644   C  CE2 . PHE A  1 82  ? 68.689  7.978   64.582  1.00 7.45  ? 82   PHE A CE2 1 
ATOM   645   C  CZ  . PHE A  1 82  ? 67.494  7.567   65.158  1.00 9.73  ? 82   PHE A CZ  1 
ATOM   646   N  N   . GLN A  1 83  ? 70.445  2.091   65.492  1.00 8.65  ? 83   GLN A N   1 
ATOM   647   C  CA  . GLN A  1 83  ? 69.384  1.087   65.623  1.00 7.15  ? 83   GLN A CA  1 
ATOM   648   C  C   . GLN A  1 83  ? 68.444  1.483   66.751  1.00 8.67  ? 83   GLN A C   1 
ATOM   649   O  O   . GLN A  1 83  ? 68.859  2.041   67.770  1.00 6.38  ? 83   GLN A O   1 
ATOM   650   C  CB  . GLN A  1 83  ? 69.990  -0.267  65.930  1.00 7.63  ? 83   GLN A CB  1 
ATOM   651   C  CG  . GLN A  1 83  ? 68.928  -1.424  65.957  1.00 7.82  ? 83   GLN A CG  1 
ATOM   652   C  CD  . GLN A  1 83  ? 69.495  -2.789  65.585  1.00 9.16  ? 83   GLN A CD  1 
ATOM   653   O  OE1 . GLN A  1 83  ? 68.734  -3.799  65.524  1.00 8.80  ? 83   GLN A OE1 1 
ATOM   654   N  NE2 . GLN A  1 83  ? 70.796  -2.856  65.351  1.00 3.81  ? 83   GLN A NE2 1 
ATOM   655   N  N   . LEU A  1 84  ? 67.167  1.190   66.545  1.00 7.08  ? 84   LEU A N   1 
ATOM   656   C  CA  . LEU A  1 84  ? 66.161  1.493   67.511  1.00 7.81  ? 84   LEU A CA  1 
ATOM   657   C  C   . LEU A  1 84  ? 65.382  0.199   67.773  1.00 7.34  ? 84   LEU A C   1 
ATOM   658   O  O   . LEU A  1 84  ? 65.070  -0.538  66.808  1.00 7.50  ? 84   LEU A O   1 
ATOM   659   C  CB  . LEU A  1 84  ? 65.254  2.563   66.914  1.00 7.61  ? 84   LEU A CB  1 
ATOM   660   C  CG  . LEU A  1 84  ? 64.031  2.871   67.764  1.00 9.22  ? 84   LEU A CG  1 
ATOM   661   C  CD1 . LEU A  1 84  ? 64.407  3.540   69.101  1.00 10.88 ? 84   LEU A CD1 1 
ATOM   662   C  CD2 . LEU A  1 84  ? 63.260  3.795   66.918  1.00 10.93 ? 84   LEU A CD2 1 
ATOM   663   N  N   . TRP A  1 85  ? 65.104  -0.103  69.053  1.00 7.32  ? 85   TRP A N   1 
ATOM   664   C  CA  . TRP A  1 85  ? 64.301  -1.301  69.404  1.00 5.75  ? 85   TRP A CA  1 
ATOM   665   C  C   . TRP A  1 85  ? 63.098  -0.799  70.167  1.00 6.76  ? 85   TRP A C   1 
ATOM   666   O  O   . TRP A  1 85  ? 63.210  0.145   70.926  1.00 4.90  ? 85   TRP A O   1 
ATOM   667   C  CB  . TRP A  1 85  ? 65.047  -2.211  70.367  1.00 6.11  ? 85   TRP A CB  1 
ATOM   668   C  CG  . TRP A  1 85  ? 66.282  -2.950  69.829  1.00 6.26  ? 85   TRP A CG  1 
ATOM   669   C  CD1 . TRP A  1 85  ? 66.356  -4.269  69.486  1.00 7.69  ? 85   TRP A CD1 1 
ATOM   670   C  CD2 . TRP A  1 85  ? 67.619  -2.428  69.692  1.00 7.44  ? 85   TRP A CD2 1 
ATOM   671   N  NE1 . TRP A  1 85  ? 67.638  -4.606  69.115  1.00 8.88  ? 85   TRP A NE1 1 
ATOM   672   C  CE2 . TRP A  1 85  ? 68.433  -3.488  69.204  1.00 4.66  ? 85   TRP A CE2 1 
ATOM   673   C  CE3 . TRP A  1 85  ? 68.208  -1.160  69.895  1.00 3.91  ? 85   TRP A CE3 1 
ATOM   674   C  CZ2 . TRP A  1 85  ? 69.807  -3.351  68.997  1.00 6.78  ? 85   TRP A CZ2 1 
ATOM   675   C  CZ3 . TRP A  1 85  ? 69.579  -1.002  69.633  1.00 5.04  ? 85   TRP A CZ3 1 
ATOM   676   C  CH2 . TRP A  1 85  ? 70.369  -2.114  69.207  1.00 6.42  ? 85   TRP A CH2 1 
ATOM   677   N  N   . ALA A  1 86  ? 61.948  -1.435  69.983  1.00 5.52  ? 86   ALA A N   1 
ATOM   678   C  CA  . ALA A  1 86  ? 60.756  -0.983  70.682  1.00 7.01  ? 86   ALA A CA  1 
ATOM   679   C  C   . ALA A  1 86  ? 59.842  -2.139  70.864  1.00 6.00  ? 86   ALA A C   1 
ATOM   680   O  O   . ALA A  1 86  ? 59.813  -2.989  70.002  1.00 7.16  ? 86   ALA A O   1 
ATOM   681   C  CB  . ALA A  1 86  ? 60.035  0.139   69.861  1.00 5.38  ? 86   ALA A CB  1 
ATOM   682   N  N   . GLN A  1 87  ? 59.046  -2.116  71.938  1.00 6.94  ? 87   GLN A N   1 
ATOM   683   C  CA  . GLN A  1 87  ? 57.983  -3.095  72.157  1.00 7.52  ? 87   GLN A CA  1 
ATOM   684   C  C   . GLN A  1 87  ? 56.852  -2.548  72.957  1.00 8.78  ? 87   GLN A C   1 
ATOM   685   O  O   . GLN A  1 87  ? 57.077  -1.901  73.966  1.00 9.57  ? 87   GLN A O   1 
ATOM   686   C  CB  . GLN A  1 87  ? 58.535  -4.323  72.919  1.00 7.89  ? 87   GLN A CB  1 
ATOM   687   C  CG  . GLN A  1 87  ? 57.481  -5.374  73.222  1.00 7.27  ? 87   GLN A CG  1 
ATOM   688   C  CD  . GLN A  1 87  ? 58.080  -6.643  73.782  1.00 13.16 ? 87   GLN A CD  1 
ATOM   689   O  OE1 . GLN A  1 87  ? 59.073  -6.618  74.500  1.00 16.10 ? 87   GLN A OE1 1 
ATOM   690   N  NE2 . GLN A  1 87  ? 57.456  -7.748  73.487  1.00 13.10 ? 87   GLN A NE2 1 
ATOM   691   N  N   . SER A  1 88  ? 55.635  -2.911  72.560  1.00 10.93 ? 88   SER A N   1 
ATOM   692   C  CA  . SER A  1 88  ? 54.433  -2.480  73.263  1.00 12.48 ? 88   SER A CA  1 
ATOM   693   C  C   . SER A  1 88  ? 53.751  -3.697  73.824  1.00 12.98 ? 88   SER A C   1 
ATOM   694   O  O   . SER A  1 88  ? 53.578  -4.691  73.129  1.00 11.88 ? 88   SER A O   1 
ATOM   695   C  CB  . SER A  1 88  ? 53.442  -1.764  72.328  1.00 12.43 ? 88   SER A CB  1 
ATOM   696   O  OG  . SER A  1 88  ? 52.242  -1.490  73.037  1.00 15.95 ? 88   SER A OG  1 
ATOM   697   N  N   . GLY A  1 89  ? 53.391  -3.611  75.100  1.00 14.42 ? 89   GLY A N   1 
ATOM   698   C  CA  . GLY A  1 89  ? 52.648  -4.641  75.784  1.00 16.36 ? 89   GLY A CA  1 
ATOM   699   C  C   . GLY A  1 89  ? 53.165  -6.009  75.436  1.00 18.86 ? 89   GLY A C   1 
ATOM   700   O  O   . GLY A  1 89  ? 54.380  -6.287  75.583  1.00 18.85 ? 89   GLY A O   1 
ATOM   701   N  N   . ASN A  1 90  ? 52.221  -6.821  74.935  1.00 20.67 ? 90   ASN A N   1 
ATOM   702   C  CA  . ASN A  1 90  ? 52.412  -8.204  74.501  1.00 22.68 ? 90   ASN A CA  1 
ATOM   703   C  C   . ASN A  1 90  ? 52.864  -8.384  73.034  1.00 21.84 ? 90   ASN A C   1 
ATOM   704   O  O   . ASN A  1 90  ? 53.060  -9.516  72.578  1.00 22.87 ? 90   ASN A O   1 
ATOM   705   C  CB  . ASN A  1 90  ? 51.096  -9.013  74.681  1.00 23.17 ? 90   ASN A CB  1 
ATOM   706   C  CG  . ASN A  1 90  ? 50.493  -8.896  76.089  1.00 26.79 ? 90   ASN A CG  1 
ATOM   707   O  OD1 . ASN A  1 90  ? 51.223  -8.912  77.102  1.00 28.84 ? 90   ASN A OD1 1 
ATOM   708   N  ND2 . ASN A  1 90  ? 49.144  -8.782  76.148  1.00 29.43 ? 90   ASN A ND2 1 
ATOM   709   N  N   . GLU A  1 91  ? 52.991  -7.289  72.297  1.00 20.23 ? 91   GLU A N   1 
ATOM   710   C  CA  . GLU A  1 91  ? 53.283  -7.382  70.893  1.00 17.57 ? 91   GLU A CA  1 
ATOM   711   C  C   . GLU A  1 91  ? 54.764  -7.822  70.694  1.00 16.53 ? 91   GLU A C   1 
ATOM   712   O  O   . GLU A  1 91  ? 55.651  -7.591  71.549  1.00 16.20 ? 91   GLU A O   1 
ATOM   713   C  CB  . GLU A  1 91  ? 52.945  -6.041  70.202  1.00 17.94 ? 91   GLU A CB  1 
ATOM   714   C  CG  . GLU A  1 91  ? 51.439  -5.712  70.074  1.00 19.73 ? 91   GLU A CG  1 
ATOM   715   C  CD  . GLU A  1 91  ? 51.146  -4.229  69.802  1.00 25.57 ? 91   GLU A CD  1 
ATOM   716   O  OE1 . GLU A  1 91  ? 51.971  -3.495  69.171  1.00 24.75 ? 91   GLU A OE1 1 
ATOM   717   O  OE2 . GLU A  1 91  ? 50.057  -3.772  70.238  1.00 31.62 ? 91   GLU A OE2 1 
ATOM   718   N  N   . THR A  1 92  ? 55.027  -8.455  69.555  1.00 13.04 ? 92   THR A N   1 
ATOM   719   C  CA  . THR A  1 92  ? 56.372  -8.794  69.120  1.00 9.91  ? 92   THR A CA  1 
ATOM   720   C  C   . THR A  1 92  ? 57.320  -7.590  69.205  1.00 9.53  ? 92   THR A C   1 
ATOM   721   O  O   . THR A  1 92  ? 56.955  -6.484  68.853  1.00 9.05  ? 92   THR A O   1 
ATOM   722   C  CB  . THR A  1 92  ? 56.253  -9.279  67.691  1.00 9.53  ? 92   THR A CB  1 
ATOM   723   O  OG1 . THR A  1 92  ? 55.465  -10.471 67.732  1.00 9.78  ? 92   THR A OG1 1 
ATOM   724   C  CG2 . THR A  1 92  ? 57.572  -9.727  67.167  1.00 6.78  ? 92   THR A CG2 1 
ATOM   725   N  N   . GLN A  1 93  ? 58.527  -7.819  69.726  1.00 8.96  ? 93   GLN A N   1 
ATOM   726   C  CA  . GLN A  1 93  ? 59.530  -6.764  69.760  1.00 8.19  ? 93   GLN A CA  1 
ATOM   727   C  C   . GLN A  1 93  ? 60.036  -6.510  68.328  1.00 8.03  ? 93   GLN A C   1 
ATOM   728   O  O   . GLN A  1 93  ? 60.275  -7.459  67.566  1.00 7.23  ? 93   GLN A O   1 
ATOM   729   C  CB  . GLN A  1 93  ? 60.690  -7.156  70.634  1.00 7.56  ? 93   GLN A CB  1 
ATOM   730   C  CG  . GLN A  1 93  ? 61.715  -6.002  70.780  1.00 8.97  ? 93   GLN A CG  1 
ATOM   731   C  CD  . GLN A  1 93  ? 63.052  -6.494  71.343  1.00 9.43  ? 93   GLN A CD  1 
ATOM   732   O  OE1 . GLN A  1 93  ? 64.086  -6.144  70.830  1.00 6.76  ? 93   GLN A OE1 1 
ATOM   733   N  NE2 . GLN A  1 93  ? 63.011  -7.325  72.399  1.00 11.17 ? 93   GLN A NE2 1 
ATOM   734   N  N   . GLN A  1 94  ? 60.180  -5.230  68.009  1.00 7.56  ? 94   GLN A N   1 
ATOM   735   C  CA  . GLN A  1 94  ? 60.582  -4.700  66.674  1.00 6.74  ? 94   GLN A CA  1 
ATOM   736   C  C   . GLN A  1 94  ? 61.862  -3.920  66.739  1.00 6.09  ? 94   GLN A C   1 
ATOM   737   O  O   . GLN A  1 94  ? 62.100  -3.179  67.714  1.00 5.64  ? 94   GLN A O   1 
ATOM   738   C  CB  . GLN A  1 94  ? 59.528  -3.735  66.120  1.00 6.93  ? 94   GLN A CB  1 
ATOM   739   C  CG  . GLN A  1 94  ? 58.147  -4.394  65.997  1.00 4.64  ? 94   GLN A CG  1 
ATOM   740   C  CD  . GLN A  1 94  ? 58.041  -5.270  64.761  1.00 9.21  ? 94   GLN A CD  1 
ATOM   741   O  OE1 . GLN A  1 94  ? 58.874  -5.179  63.853  1.00 8.70  ? 94   GLN A OE1 1 
ATOM   742   N  NE2 . GLN A  1 94  ? 57.039  -6.137  64.737  1.00 7.10  ? 94   GLN A NE2 1 
ATOM   743   N  N   . THR A  1 95  ? 62.713  -4.075  65.730  1.00 4.69  ? 95   THR A N   1 
ATOM   744   C  CA  . THR A  1 95  ? 63.903  -3.186  65.667  1.00 6.46  ? 95   THR A CA  1 
ATOM   745   C  C   . THR A  1 95  ? 64.257  -2.827  64.197  1.00 6.44  ? 95   THR A C   1 
ATOM   746   O  O   . THR A  1 95  ? 64.020  -3.640  63.287  1.00 6.39  ? 95   THR A O   1 
ATOM   747   C  CB  . THR A  1 95  ? 65.115  -3.815  66.410  1.00 5.66  ? 95   THR A CB  1 
ATOM   748   O  OG1 . THR A  1 95  ? 66.246  -2.915  66.385  1.00 7.55  ? 95   THR A OG1 1 
ATOM   749   C  CG2 . THR A  1 95  ? 65.608  -5.076  65.717  1.00 6.94  ? 95   THR A CG2 1 
ATOM   750   N  N   . ARG A  1 96  ? 64.826  -1.626  63.995  1.00 6.04  ? 96   ARG A N   1 
ATOM   751   C  CA  . ARG A  1 96  ? 65.226  -1.156  62.693  1.00 6.59  ? 96   ARG A CA  1 
ATOM   752   C  C   . ARG A  1 96  ? 66.519  -0.396  62.841  1.00 7.44  ? 96   ARG A C   1 
ATOM   753   O  O   . ARG A  1 96  ? 66.746  0.298   63.845  1.00 8.83  ? 96   ARG A O   1 
ATOM   754   C  CB  . ARG A  1 96  ? 64.218  -0.126  62.143  1.00 5.16  ? 96   ARG A CB  1 
ATOM   755   C  CG  . ARG A  1 96  ? 62.761  -0.683  61.947  1.00 5.53  ? 96   ARG A CG  1 
ATOM   756   C  CD  . ARG A  1 96  ? 62.621  -1.901  60.998  1.00 5.16  ? 96   ARG A CD  1 
ATOM   757   N  NE  . ARG A  1 96  ? 61.178  -2.163  60.872  1.00 8.83  ? 96   ARG A NE  1 
ATOM   758   C  CZ  . ARG A  1 96  ? 60.519  -2.968  61.683  1.00 7.73  ? 96   ARG A CZ  1 
ATOM   759   N  NH1 . ARG A  1 96  ? 61.197  -3.637  62.628  1.00 4.28  ? 96   ARG A NH1 1 
ATOM   760   N  NH2 . ARG A  1 96  ? 59.196  -3.089  61.567  1.00 8.15  ? 96   ARG A NH2 1 
ATOM   761   N  N   . VAL A  1 97  ? 67.342  -0.491  61.816  1.00 7.66  ? 97   VAL A N   1 
ATOM   762   C  CA  . VAL A  1 97  ? 68.461  0.407   61.699  1.00 8.19  ? 97   VAL A CA  1 
ATOM   763   C  C   . VAL A  1 97  ? 68.009  1.593   60.847  1.00 7.83  ? 97   VAL A C   1 
ATOM   764   O  O   . VAL A  1 97  ? 67.764  1.430   59.642  1.00 6.32  ? 97   VAL A O   1 
ATOM   765   C  CB  . VAL A  1 97  ? 69.661  -0.323  61.091  1.00 7.15  ? 97   VAL A CB  1 
ATOM   766   C  CG1 . VAL A  1 97  ? 70.882  0.648   61.054  1.00 9.45  ? 97   VAL A CG1 1 
ATOM   767   C  CG2 . VAL A  1 97  ? 70.040  -1.560  61.957  1.00 7.20  ? 97   VAL A CG2 1 
ATOM   768   N  N   . LEU A  1 98  ? 67.902  2.775   61.480  1.00 7.70  ? 98   LEU A N   1 
ATOM   769   C  CA  . LEU A  1 98  ? 67.534  4.016   60.805  1.00 9.51  ? 98   LEU A CA  1 
ATOM   770   C  C   . LEU A  1 98  ? 68.799  4.649   60.150  1.00 10.40 ? 98   LEU A C   1 
ATOM   771   O  O   . LEU A  1 98  ? 69.837  4.742   60.777  1.00 10.01 ? 98   LEU A O   1 
ATOM   772   C  CB  . LEU A  1 98  ? 66.919  5.022   61.802  1.00 9.69  ? 98   LEU A CB  1 
ATOM   773   C  CG  . LEU A  1 98  ? 65.468  4.679   62.204  1.00 10.13 ? 98   LEU A CG  1 
ATOM   774   C  CD1 . LEU A  1 98  ? 65.443  3.401   63.060  1.00 13.27 ? 98   LEU A CD1 1 
ATOM   775   C  CD2 . LEU A  1 98  ? 64.864  5.828   62.968  1.00 10.70 ? 98   LEU A CD2 1 
ATOM   776   N  N   . SER A  1 99  ? 68.730  4.961   58.867  1.00 9.45  ? 99   SER A N   1 
ATOM   777   C  CA  . SER A  1 99  ? 69.764  5.775   58.237  1.00 9.10  ? 99   SER A CA  1 
ATOM   778   C  C   . SER A  1 99  ? 69.102  7.102   57.877  1.00 9.60  ? 99   SER A C   1 
ATOM   779   O  O   . SER A  1 99  ? 68.005  7.392   58.331  1.00 9.20  ? 99   SER A O   1 
ATOM   780   C  CB  . SER A  1 99  ? 70.341  5.080   56.983  1.00 9.65  ? 99   SER A CB  1 
ATOM   781   O  OG  . SER A  1 99  ? 69.305  4.550   56.180  1.00 11.99 ? 99   SER A OG  1 
ATOM   782   N  N   . SER A  1 100 ? 69.765  7.928   57.082  1.00 9.66  ? 100  SER A N   1 
ATOM   783   C  CA  . SER A  1 100 ? 69.334  9.310   56.894  1.00 8.89  ? 100  SER A CA  1 
ATOM   784   C  C   . SER A  1 100 ? 67.922  9.379   56.367  1.00 9.30  ? 100  SER A C   1 
ATOM   785   O  O   . SER A  1 100 ? 67.581  8.757   55.337  1.00 8.91  ? 100  SER A O   1 
ATOM   786   C  CB  . SER A  1 100 ? 70.278  10.020  55.893  1.00 9.30  ? 100  SER A CB  1 
ATOM   787   O  OG  A SER A  1 100 ? 69.952  11.396  55.782  0.50 12.16 ? 100  SER A OG  1 
ATOM   788   O  OG  B SER A  1 100 ? 71.562  10.090  56.378  0.50 3.88  ? 100  SER A OG  1 
ATOM   789   N  N   . GLY A  1 101 ? 67.108  10.160  57.074  1.00 8.52  ? 101  GLY A N   1 
ATOM   790   C  CA  . GLY A  1 101 ? 65.744  10.429  56.677  1.00 7.92  ? 101  GLY A CA  1 
ATOM   791   C  C   . GLY A  1 101 ? 64.729  9.410   57.182  1.00 7.87  ? 101  GLY A C   1 
ATOM   792   O  O   . GLY A  1 101 ? 63.540  9.635   56.950  1.00 7.14  ? 101  GLY A O   1 
ATOM   793   N  N   . ASP A  1 102 ? 65.201  8.366   57.912  1.00 6.40  ? 102  ASP A N   1 
ATOM   794   C  CA  . ASP A  1 102 ? 64.315  7.333   58.484  1.00 7.81  ? 102  ASP A CA  1 
ATOM   795   C  C   . ASP A  1 102 ? 63.699  7.765   59.822  1.00 8.02  ? 102  ASP A C   1 
ATOM   796   O  O   . ASP A  1 102 ? 64.271  8.555   60.532  1.00 8.76  ? 102  ASP A O   1 
ATOM   797   C  CB  . ASP A  1 102 ? 65.104  6.048   58.742  1.00 8.48  ? 102  ASP A CB  1 
ATOM   798   C  CG  . ASP A  1 102 ? 65.506  5.328   57.473  1.00 9.43  ? 102  ASP A CG  1 
ATOM   799   O  OD1 . ASP A  1 102 ? 65.031  5.726   56.381  1.00 6.11  ? 102  ASP A OD1 1 
ATOM   800   O  OD2 . ASP A  1 102 ? 66.289  4.321   57.484  1.00 7.72  ? 102  ASP A OD2 1 
ATOM   801   N  N   . TYR A  1 103 ? 62.557  7.178   60.177  1.00 9.43  ? 103  TYR A N   1 
ATOM   802   C  CA  . TYR A  1 103 ? 61.762  7.673   61.286  1.00 9.20  ? 103  TYR A CA  1 
ATOM   803   C  C   . TYR A  1 103 ? 61.259  6.530   62.130  1.00 7.89  ? 103  TYR A C   1 
ATOM   804   O  O   . TYR A  1 103 ? 60.926  5.439   61.594  1.00 7.96  ? 103  TYR A O   1 
ATOM   805   C  CB  . TYR A  1 103 ? 60.570  8.520   60.764  1.00 8.45  ? 103  TYR A CB  1 
ATOM   806   C  CG  . TYR A  1 103 ? 59.538  8.730   61.837  1.00 8.30  ? 103  TYR A CG  1 
ATOM   807   C  CD1 . TYR A  1 103 ? 59.783  9.610   62.909  1.00 9.69  ? 103  TYR A CD1 1 
ATOM   808   C  CD2 . TYR A  1 103 ? 58.309  8.043   61.811  1.00 9.00  ? 103  TYR A CD2 1 
ATOM   809   C  CE1 . TYR A  1 103 ? 58.847  9.792   63.896  1.00 7.44  ? 103  TYR A CE1 1 
ATOM   810   C  CE2 . TYR A  1 103 ? 57.362  8.242   62.825  1.00 7.44  ? 103  TYR A CE2 1 
ATOM   811   C  CZ  . TYR A  1 103 ? 57.640  9.096   63.856  1.00 5.84  ? 103  TYR A CZ  1 
ATOM   812   O  OH  . TYR A  1 103 ? 56.694  9.283   64.847  1.00 8.50  ? 103  TYR A OH  1 
ATOM   813   N  N   . GLY A  1 104 ? 61.287  6.727   63.452  1.00 8.04  ? 104  GLY A N   1 
ATOM   814   C  CA  . GLY A  1 104 ? 60.771  5.712   64.362  1.00 5.50  ? 104  GLY A CA  1 
ATOM   815   C  C   . GLY A  1 104 ? 59.904  6.379   65.417  1.00 6.52  ? 104  GLY A C   1 
ATOM   816   O  O   . GLY A  1 104 ? 60.360  7.330   66.048  1.00 6.78  ? 104  GLY A O   1 
ATOM   817   N  N   . SER A  1 105 ? 58.688  5.868   65.618  1.00 6.53  ? 105  SER A N   1 
ATOM   818   C  CA  . SER A  1 105 ? 57.689  6.457   66.544  1.00 6.89  ? 105  SER A CA  1 
ATOM   819   C  C   . SER A  1 105 ? 57.659  5.603   67.789  1.00 7.54  ? 105  SER A C   1 
ATOM   820   O  O   . SER A  1 105 ? 57.474  4.389   67.687  1.00 5.86  ? 105  SER A O   1 
ATOM   821   C  CB  . SER A  1 105 ? 56.288  6.401   65.892  1.00 6.55  ? 105  SER A CB  1 
ATOM   822   O  OG  . SER A  1 105 ? 55.331  7.295   66.474  1.00 8.71  ? 105  SER A OG  1 
ATOM   823   N  N   . VAL A  1 106 ? 57.828  6.235   68.958  1.00 7.83  ? 106  VAL A N   1 
ATOM   824   C  CA  . VAL A  1 106 ? 57.748  5.510   70.236  1.00 8.11  ? 106  VAL A CA  1 
ATOM   825   C  C   . VAL A  1 106 ? 56.709  6.146   71.168  1.00 7.90  ? 106  VAL A C   1 
ATOM   826   O  O   . VAL A  1 106 ? 57.058  7.052   71.937  1.00 8.36  ? 106  VAL A O   1 
ATOM   827   C  CB  . VAL A  1 106 ? 59.157  5.445   70.920  1.00 8.21  ? 106  VAL A CB  1 
ATOM   828   C  CG1 . VAL A  1 106 ? 59.106  4.572   72.184  1.00 8.52  ? 106  VAL A CG1 1 
ATOM   829   C  CG2 . VAL A  1 106 ? 60.212  4.827   69.944  1.00 6.22  ? 106  VAL A CG2 1 
ATOM   830   N  N   . PRO A  1 107 ? 55.431  5.740   71.048  1.00 7.52  ? 107  PRO A N   1 
ATOM   831   C  CA  . PRO A  1 107 ? 54.381  6.225   71.937  1.00 7.75  ? 107  PRO A CA  1 
ATOM   832   C  C   . PRO A  1 107 ? 54.702  5.974   73.434  1.00 8.17  ? 107  PRO A C   1 
ATOM   833   O  O   . PRO A  1 107 ? 55.612  5.183   73.801  1.00 8.84  ? 107  PRO A O   1 
ATOM   834   C  CB  . PRO A  1 107 ? 53.125  5.379   71.531  1.00 7.72  ? 107  PRO A CB  1 
ATOM   835   C  CG  . PRO A  1 107 ? 53.403  5.000   70.041  1.00 6.89  ? 107  PRO A CG  1 
ATOM   836   C  CD  . PRO A  1 107 ? 54.923  4.790   70.045  1.00 6.98  ? 107  PRO A CD  1 
ATOM   837   N  N   . ARG A  1 108 ? 53.933  6.637   74.289  1.00 9.17  ? 108  ARG A N   1 
ATOM   838   C  CA  . ARG A  1 108 ? 53.927  6.356   75.736  1.00 8.60  ? 108  ARG A CA  1 
ATOM   839   C  C   . ARG A  1 108 ? 53.736  4.864   75.999  1.00 9.85  ? 108  ARG A C   1 
ATOM   840   O  O   . ARG A  1 108 ? 52.970  4.172   75.288  1.00 9.40  ? 108  ARG A O   1 
ATOM   841   C  CB  . ARG A  1 108 ? 52.849  7.172   76.442  1.00 9.50  ? 108  ARG A CB  1 
ATOM   842   C  CG  . ARG A  1 108 ? 53.015  8.704   76.278  1.00 7.77  ? 108  ARG A CG  1 
ATOM   843   C  CD  . ARG A  1 108 ? 51.763  9.511   76.652  1.00 6.82  ? 108  ARG A CD  1 
ATOM   844   N  NE  . ARG A  1 108 ? 50.596  9.267   75.761  1.00 8.39  ? 108  ARG A NE  1 
ATOM   845   C  CZ  . ARG A  1 108 ? 49.368  9.772   75.974  1.00 10.81 ? 108  ARG A CZ  1 
ATOM   846   N  NH1 . ARG A  1 108 ? 49.111  10.504  77.044  1.00 6.83  ? 108  ARG A NH1 1 
ATOM   847   N  NH2 . ARG A  1 108 ? 48.378  9.539   75.113  1.00 7.87  ? 108  ARG A NH2 1 
ATOM   848   N  N   . ASN A  1 109 ? 54.459  4.396   77.024  1.00 10.65 ? 109  ASN A N   1 
ATOM   849   C  CA  . ASN A  1 109 ? 54.456  3.026   77.535  1.00 11.72 ? 109  ASN A CA  1 
ATOM   850   C  C   . ASN A  1 109 ? 54.977  2.015   76.541  1.00 11.34 ? 109  ASN A C   1 
ATOM   851   O  O   . ASN A  1 109 ? 54.575  0.894   76.590  1.00 13.53 ? 109  ASN A O   1 
ATOM   852   C  CB  . ASN A  1 109 ? 53.091  2.560   78.067  1.00 12.40 ? 109  ASN A CB  1 
ATOM   853   C  CG  . ASN A  1 109 ? 52.626  3.361   79.258  1.00 15.79 ? 109  ASN A CG  1 
ATOM   854   O  OD1 . ASN A  1 109 ? 53.447  3.974   79.976  1.00 16.34 ? 109  ASN A OD1 1 
ATOM   855   N  ND2 . ASN A  1 109 ? 51.304  3.366   79.485  1.00 19.45 ? 109  ASN A ND2 1 
ATOM   856   N  N   . VAL A  1 110 ? 55.876  2.426   75.661  1.00 9.54  ? 110  VAL A N   1 
ATOM   857   C  CA  . VAL A  1 110 ? 56.553  1.502   74.767  1.00 7.79  ? 110  VAL A CA  1 
ATOM   858   C  C   . VAL A  1 110 ? 58.026  1.424   75.233  1.00 6.79  ? 110  VAL A C   1 
ATOM   859   O  O   . VAL A  1 110 ? 58.700  2.447   75.375  1.00 5.67  ? 110  VAL A O   1 
ATOM   860   C  CB  . VAL A  1 110 ? 56.460  2.049   73.300  1.00 8.49  ? 110  VAL A CB  1 
ATOM   861   C  CG1 . VAL A  1 110 ? 57.347  1.251   72.349  1.00 8.18  ? 110  VAL A CG1 1 
ATOM   862   C  CG2 . VAL A  1 110 ? 54.962  2.019   72.838  1.00 8.09  ? 110  VAL A CG2 1 
ATOM   863   N  N   . THR A  1 111 ? 58.502  0.209   75.493  1.00 7.19  ? 111  THR A N   1 
ATOM   864   C  CA  . THR A  1 111 ? 59.876  0.006   75.921  1.00 5.83  ? 111  THR A CA  1 
ATOM   865   C  C   . THR A  1 111 ? 60.800  0.235   74.731  1.00 7.12  ? 111  THR A C   1 
ATOM   866   O  O   . THR A  1 111 ? 60.535  -0.262  73.628  1.00 5.65  ? 111  THR A O   1 
ATOM   867   C  CB  . THR A  1 111 ? 59.993  -1.450  76.477  1.00 6.25  ? 111  THR A CB  1 
ATOM   868   O  OG1 . THR A  1 111 ? 59.203  -1.566  77.675  1.00 7.45  ? 111  THR A OG1 1 
ATOM   869   C  CG2 . THR A  1 111 ? 61.426  -1.751  76.930  1.00 5.37  ? 111  THR A CG2 1 
ATOM   870   N  N   . HIS A  1 112 ? 61.901  0.964   74.931  1.00 6.03  ? 112  HIS A N   1 
ATOM   871   C  CA  . HIS A  1 112 ? 62.781  1.238   73.804  1.00 7.16  ? 112  HIS A CA  1 
ATOM   872   C  C   . HIS A  1 112 ? 64.197  1.450   74.248  1.00 5.96  ? 112  HIS A C   1 
ATOM   873   O  O   . HIS A  1 112 ? 64.459  1.797   75.417  1.00 5.87  ? 112  HIS A O   1 
ATOM   874   C  CB  . HIS A  1 112 ? 62.360  2.497   73.008  1.00 5.82  ? 112  HIS A CB  1 
ATOM   875   C  CG  . HIS A  1 112 ? 62.172  3.712   73.863  1.00 7.39  ? 112  HIS A CG  1 
ATOM   876   N  ND1 . HIS A  1 112 ? 61.174  3.793   74.808  1.00 7.69  ? 112  HIS A ND1 1 
ATOM   877   C  CD2 . HIS A  1 112 ? 62.839  4.899   73.913  1.00 9.32  ? 112  HIS A CD2 1 
ATOM   878   C  CE1 . HIS A  1 112 ? 61.232  4.978   75.405  1.00 8.23  ? 112  HIS A CE1 1 
ATOM   879   N  NE2 . HIS A  1 112 ? 62.228  5.663   74.890  1.00 10.21 ? 112  HIS A NE2 1 
ATOM   880   N  N   . THR A  1 113 ? 65.117  1.277   73.304  1.00 6.24  ? 113  THR A N   1 
ATOM   881   C  CA  . THR A  1 113 ? 66.511  1.696   73.527  1.00 6.59  ? 113  THR A CA  1 
ATOM   882   C  C   . THR A  1 113 ? 67.099  1.920   72.118  1.00 6.43  ? 113  THR A C   1 
ATOM   883   O  O   . THR A  1 113 ? 66.421  1.623   71.139  1.00 6.98  ? 113  THR A O   1 
ATOM   884   C  CB  . THR A  1 113 ? 67.266  0.627   74.352  1.00 7.47  ? 113  THR A CB  1 
ATOM   885   O  OG1 . THR A  1 113 ? 68.651  0.987   74.390  1.00 9.11  ? 113  THR A OG1 1 
ATOM   886   C  CG2 . THR A  1 113 ? 67.291  -0.719  73.676  1.00 4.23  ? 113  THR A CG2 1 
ATOM   887   N  N   . PHE A  1 114 ? 68.309  2.447   72.020  1.00 6.68  ? 114  PHE A N   1 
ATOM   888   C  CA  . PHE A  1 114 ? 68.953  2.716   70.729  1.00 7.10  ? 114  PHE A CA  1 
ATOM   889   C  C   . PHE A  1 114 ? 70.464  2.443   70.816  1.00 8.01  ? 114  PHE A C   1 
ATOM   890   O  O   . PHE A  1 114 ? 71.016  2.292   71.912  1.00 7.93  ? 114  PHE A O   1 
ATOM   891   C  CB  . PHE A  1 114 ? 68.702  4.124   70.227  1.00 6.61  ? 114  PHE A CB  1 
ATOM   892   C  CG  . PHE A  1 114 ? 69.308  5.215   71.095  1.00 9.40  ? 114  PHE A CG  1 
ATOM   893   C  CD1 . PHE A  1 114 ? 70.638  5.673   70.882  1.00 8.59  ? 114  PHE A CD1 1 
ATOM   894   C  CD2 . PHE A  1 114 ? 68.564  5.766   72.147  1.00 7.69  ? 114  PHE A CD2 1 
ATOM   895   C  CE1 . PHE A  1 114 ? 71.198  6.670   71.714  1.00 8.57  ? 114  PHE A CE1 1 
ATOM   896   C  CE2 . PHE A  1 114 ? 69.125  6.745   73.008  1.00 10.97 ? 114  PHE A CE2 1 
ATOM   897   C  CZ  . PHE A  1 114 ? 70.425  7.186   72.792  1.00 10.74 ? 114  PHE A CZ  1 
ATOM   898   N  N   . GLN A  1 115 ? 71.111  2.342   69.654  1.00 7.15  ? 115  GLN A N   1 
ATOM   899   C  CA  . GLN A  1 115 ? 72.550  2.124   69.570  1.00 6.89  ? 115  GLN A CA  1 
ATOM   900   C  C   . GLN A  1 115 ? 73.096  2.881   68.367  1.00 6.88  ? 115  GLN A C   1 
ATOM   901   O  O   . GLN A  1 115 ? 72.601  2.723   67.242  1.00 6.78  ? 115  GLN A O   1 
ATOM   902   C  CB  . GLN A  1 115 ? 72.933  0.627   69.448  1.00 6.68  ? 115  GLN A CB  1 
ATOM   903   C  CG  . GLN A  1 115 ? 74.470  0.441   69.320  1.00 3.81  ? 115  GLN A CG  1 
ATOM   904   C  CD  . GLN A  1 115 ? 74.959  -1.009  69.632  1.00 15.61 ? 115  GLN A CD  1 
ATOM   905   O  OE1 . GLN A  1 115 ? 74.185  -1.837  70.144  1.00 16.42 ? 115  GLN A OE1 1 
ATOM   906   N  NE2 . GLN A  1 115 ? 76.229  -1.312  69.310  1.00 14.72 ? 115  GLN A NE2 1 
ATOM   907   N  N   . ILE A  1 116 ? 74.077  3.750   68.594  1.00 8.03  ? 116  ILE A N   1 
ATOM   908   C  CA  . ILE A  1 116 ? 74.666  4.495   67.482  1.00 7.68  ? 116  ILE A CA  1 
ATOM   909   C  C   . ILE A  1 116 ? 75.591  3.630   66.626  1.00 9.27  ? 116  ILE A C   1 
ATOM   910   O  O   . ILE A  1 116 ? 76.526  3.006   67.156  1.00 9.06  ? 116  ILE A O   1 
ATOM   911   C  CB  . ILE A  1 116 ? 75.500  5.705   68.011  1.00 8.29  ? 116  ILE A CB  1 
ATOM   912   C  CG1 . ILE A  1 116 ? 74.708  6.634   68.926  1.00 6.03  ? 116  ILE A CG1 1 
ATOM   913   C  CG2 . ILE A  1 116 ? 76.086  6.478   66.848  1.00 7.38  ? 116  ILE A CG2 1 
ATOM   914   C  CD1 . ILE A  1 116 ? 73.402  7.165   68.396  1.00 6.48  ? 116  ILE A CD1 1 
ATOM   915   N  N   . GLN A  1 117 ? 75.374  3.607   65.297  1.00 9.01  ? 117  GLN A N   1 
ATOM   916   C  CA  . GLN A  1 117 ? 76.173  2.742   64.411  1.00 9.73  ? 117  GLN A CA  1 
ATOM   917   C  C   . GLN A  1 117 ? 77.299  3.509   63.721  1.00 8.96  ? 117  GLN A C   1 
ATOM   918   O  O   . GLN A  1 117 ? 78.483  3.071   63.773  1.00 9.37  ? 117  GLN A O   1 
ATOM   919   C  CB  . GLN A  1 117 ? 75.297  2.061   63.341  1.00 9.89  ? 117  GLN A CB  1 
ATOM   920   C  CG  . GLN A  1 117 ? 76.130  1.318   62.209  1.00 16.71 ? 117  GLN A CG  1 
ATOM   921   C  CD  . GLN A  1 117 ? 75.219  0.546   61.244  1.00 27.58 ? 117  GLN A CD  1 
ATOM   922   O  OE1 . GLN A  1 117 ? 75.045  -0.664  61.411  1.00 33.98 ? 117  GLN A OE1 1 
ATOM   923   N  NE2 . GLN A  1 117 ? 74.614  1.246   60.253  1.00 27.08 ? 117  GLN A NE2 1 
ATOM   924   N  N   . ASP A  1 118 ? 76.967  4.622   63.054  1.00 7.55  ? 118  ASP A N   1 
ATOM   925   C  CA  . ASP A  1 118 ? 77.959  5.273   62.169  1.00 7.72  ? 118  ASP A CA  1 
ATOM   926   C  C   . ASP A  1 118 ? 78.711  6.425   62.847  1.00 7.14  ? 118  ASP A C   1 
ATOM   927   O  O   . ASP A  1 118 ? 78.200  7.027   63.783  1.00 7.47  ? 118  ASP A O   1 
ATOM   928   C  CB  . ASP A  1 118 ? 77.289  5.802   60.879  1.00 8.09  ? 118  ASP A CB  1 
ATOM   929   C  CG  . ASP A  1 118 ? 77.193  4.747   59.813  1.00 8.20  ? 118  ASP A CG  1 
ATOM   930   O  OD1 . ASP A  1 118 ? 78.070  3.842   59.723  1.00 7.67  ? 118  ASP A OD1 1 
ATOM   931   O  OD2 . ASP A  1 118 ? 76.240  4.755   59.014  1.00 13.04 ? 118  ASP A OD2 1 
ATOM   932   N  N   . PRO A  1 119 ? 79.933  6.695   62.413  1.00 6.70  ? 119  PRO A N   1 
ATOM   933   C  CA  . PRO A  1 119 ? 80.733  7.740   63.073  1.00 7.65  ? 119  PRO A CA  1 
ATOM   934   C  C   . PRO A  1 119 ? 80.046  9.077   63.099  1.00 8.06  ? 119  PRO A C   1 
ATOM   935   O  O   . PRO A  1 119 ? 80.247  9.745   64.070  1.00 10.74 ? 119  PRO A O   1 
ATOM   936   C  CB  . PRO A  1 119 ? 81.976  7.842   62.217  1.00 5.92  ? 119  PRO A CB  1 
ATOM   937   C  CG  . PRO A  1 119 ? 82.197  6.390   61.741  1.00 5.92  ? 119  PRO A CG  1 
ATOM   938   C  CD  . PRO A  1 119 ? 80.699  5.971   61.377  1.00 6.96  ? 119  PRO A CD  1 
ATOM   939   N  N   . ASP A  1 120 ? 79.355  9.503   62.041  1.00 7.57  ? 120  ASP A N   1 
ATOM   940   C  CA  . ASP A  1 120 ? 78.836  10.877  62.012  1.00 7.46  ? 120  ASP A CA  1 
ATOM   941   C  C   . ASP A  1 120 ? 77.305  10.787  62.129  1.00 7.29  ? 120  ASP A C   1 
ATOM   942   O  O   . ASP A  1 120 ? 76.559  11.181  61.211  1.00 6.55  ? 120  ASP A O   1 
ATOM   943   C  CB  . ASP A  1 120 ? 79.218  11.616  60.721  1.00 6.79  ? 120  ASP A CB  1 
ATOM   944   C  CG  . ASP A  1 120 ? 78.953  13.110  60.818  1.00 12.71 ? 120  ASP A CG  1 
ATOM   945   O  OD1 . ASP A  1 120 ? 78.646  13.548  61.934  1.00 10.70 ? 120  ASP A OD1 1 
ATOM   946   O  OD2 . ASP A  1 120 ? 78.973  13.896  59.834  1.00 14.51 ? 120  ASP A OD2 1 
ATOM   947   N  N   . THR A  1 121 ? 76.841  10.332  63.287  1.00 6.86  ? 121  THR A N   1 
ATOM   948   C  CA  . THR A  1 121 ? 75.406  10.056  63.427  1.00 8.26  ? 121  THR A CA  1 
ATOM   949   C  C   . THR A  1 121 ? 74.744  11.212  64.123  1.00 9.16  ? 121  THR A C   1 
ATOM   950   O  O   . THR A  1 121 ? 75.285  11.751  65.098  1.00 9.42  ? 121  THR A O   1 
ATOM   951   C  CB  . THR A  1 121 ? 75.185  8.754   64.193  1.00 8.22  ? 121  THR A CB  1 
ATOM   952   O  OG1 . THR A  1 121 ? 75.567  7.707   63.318  1.00 6.93  ? 121  THR A OG1 1 
ATOM   953   C  CG2 . THR A  1 121 ? 73.664  8.477   64.484  1.00 7.28  ? 121  THR A CG2 1 
ATOM   954   N  N   . GLU A  1 122 ? 73.598  11.615  63.579  1.00 7.53  ? 122  GLU A N   1 
ATOM   955   C  CA  . GLU A  1 122 ? 72.766  12.605  64.230  1.00 8.41  ? 122  GLU A CA  1 
ATOM   956   C  C   . GLU A  1 122 ? 71.302  12.126  64.368  1.00 9.88  ? 122  GLU A C   1 
ATOM   957   O  O   . GLU A  1 122 ? 70.667  11.791  63.384  1.00 10.88 ? 122  GLU A O   1 
ATOM   958   C  CB  . GLU A  1 122 ? 72.882  13.951  63.492  1.00 7.26  ? 122  GLU A CB  1 
ATOM   959   C  CG  . GLU A  1 122 ? 72.079  15.058  64.162  1.00 9.38  ? 122  GLU A CG  1 
ATOM   960   C  CD  . GLU A  1 122 ? 72.565  16.447  63.750  1.00 13.89 ? 122  GLU A CD  1 
ATOM   961   O  OE1 . GLU A  1 122 ? 73.695  16.545  63.178  1.00 14.49 ? 122  GLU A OE1 1 
ATOM   962   O  OE2 . GLU A  1 122 ? 71.811  17.430  63.961  1.00 15.24 ? 122  GLU A OE2 1 
ATOM   963   N  N   . MET A  1 123 ? 70.784  12.115  65.600  1.00 10.21 ? 123  MET A N   1 
ATOM   964   C  CA  . MET A  1 123 ? 69.365  11.817  65.875  1.00 11.78 ? 123  MET A CA  1 
ATOM   965   C  C   . MET A  1 123 ? 68.675  13.141  66.194  1.00 12.08 ? 123  MET A C   1 
ATOM   966   O  O   . MET A  1 123 ? 69.195  13.933  66.949  1.00 13.65 ? 123  MET A O   1 
ATOM   967   C  CB  . MET A  1 123 ? 69.243  10.956  67.125  1.00 11.80 ? 123  MET A CB  1 
ATOM   968   C  CG  . MET A  1 123 ? 70.375  9.992   67.311  1.00 11.06 ? 123  MET A CG  1 
ATOM   969   S  SD  . MET A  1 123 ? 70.342  9.181   68.996  1.00 21.47 ? 123  MET A SD  1 
ATOM   970   C  CE  . MET A  1 123 ? 68.711  8.575   68.963  1.00 11.69 ? 123  MET A CE  1 
ATOM   971   N  N   . THR A  1 124 ? 67.543  13.408  65.572  1.00 9.83  ? 124  THR A N   1 
ATOM   972   C  CA  . THR A  1 124 ? 66.717  14.526  66.004  1.00 9.97  ? 124  THR A CA  1 
ATOM   973   C  C   . THR A  1 124 ? 65.585  13.856  66.771  1.00 10.48 ? 124  THR A C   1 
ATOM   974   O  O   . THR A  1 124 ? 64.966  12.859  66.275  1.00 10.43 ? 124  THR A O   1 
ATOM   975   C  CB  . THR A  1 124 ? 66.204  15.274  64.808  1.00 10.16 ? 124  THR A CB  1 
ATOM   976   O  OG1 . THR A  1 124 ? 67.320  15.901  64.119  1.00 10.62 ? 124  THR A OG1 1 
ATOM   977   C  CG2 . THR A  1 124 ? 65.256  16.442  65.259  1.00 9.44  ? 124  THR A CG2 1 
ATOM   978   N  N   . GLY A  1 125 ? 65.387  14.303  67.998  1.00 10.12 ? 125  GLY A N   1 
ATOM   979   C  CA  . GLY A  1 125 ? 64.320  13.774  68.832  1.00 9.16  ? 125  GLY A CA  1 
ATOM   980   C  C   . GLY A  1 125 ? 63.248  14.838  68.933  1.00 9.24  ? 125  GLY A C   1 
ATOM   981   O  O   . GLY A  1 125 ? 63.556  16.015  69.185  1.00 10.66 ? 125  GLY A O   1 
ATOM   982   N  N   . VAL A  1 126 ? 61.993  14.436  68.716  1.00 9.14  ? 126  VAL A N   1 
ATOM   983   C  CA  . VAL A  1 126 ? 60.871  15.276  68.971  1.00 7.90  ? 126  VAL A CA  1 
ATOM   984   C  C   . VAL A  1 126 ? 60.072  14.605  70.074  1.00 9.13  ? 126  VAL A C   1 
ATOM   985   O  O   . VAL A  1 126 ? 59.588  13.465  69.917  1.00 8.24  ? 126  VAL A O   1 
ATOM   986   C  CB  . VAL A  1 126 ? 60.022  15.553  67.684  1.00 9.01  ? 126  VAL A CB  1 
ATOM   987   C  CG1 . VAL A  1 126 ? 58.771  16.393  67.959  1.00 7.95  ? 126  VAL A CG1 1 
ATOM   988   C  CG2 . VAL A  1 126 ? 60.881  16.201  66.591  1.00 8.19  ? 126  VAL A CG2 1 
ATOM   989   N  N   . ILE A  1 127 ? 59.906  15.315  71.190  1.00 9.09  ? 127  ILE A N   1 
ATOM   990   C  CA  . ILE A  1 127 ? 59.309  14.676  72.351  1.00 9.67  ? 127  ILE A CA  1 
ATOM   991   C  C   . ILE A  1 127 ? 58.119  15.506  72.742  1.00 9.17  ? 127  ILE A C   1 
ATOM   992   O  O   . ILE A  1 127 ? 58.231  16.724  72.840  1.00 8.96  ? 127  ILE A O   1 
ATOM   993   C  CB  . ILE A  1 127 ? 60.253  14.642  73.529  1.00 10.03 ? 127  ILE A CB  1 
ATOM   994   C  CG1 . ILE A  1 127 ? 61.584  13.959  73.157  1.00 14.27 ? 127  ILE A CG1 1 
ATOM   995   C  CG2 . ILE A  1 127 ? 59.591  13.787  74.719  1.00 10.98 ? 127  ILE A CG2 1 
ATOM   996   C  CD1 . ILE A  1 127 ? 62.732  14.355  74.111  1.00 18.62 ? 127  ILE A CD1 1 
ATOM   997   N  N   . VAL A  1 128 ? 57.007  14.850  73.008  1.00 8.59  ? 128  VAL A N   1 
ATOM   998   C  CA  . VAL A  1 128 ? 55.748  15.551  73.302  1.00 7.45  ? 128  VAL A CA  1 
ATOM   999   C  C   . VAL A  1 128 ? 55.153  15.007  74.587  1.00 8.26  ? 128  VAL A C   1 
ATOM   1000  O  O   . VAL A  1 128 ? 54.963  13.762  74.708  1.00 8.66  ? 128  VAL A O   1 
ATOM   1001  C  CB  . VAL A  1 128 ? 54.725  15.376  72.145  1.00 7.39  ? 128  VAL A CB  1 
ATOM   1002  C  CG1 . VAL A  1 128 ? 53.500  16.284  72.396  1.00 8.22  ? 128  VAL A CG1 1 
ATOM   1003  C  CG2 . VAL A  1 128 ? 55.387  15.835  70.776  1.00 5.21  ? 128  VAL A CG2 1 
ATOM   1004  N  N   . PRO A  1 129 ? 54.740  15.870  75.525  1.00 8.18  ? 129  PRO A N   1 
ATOM   1005  C  CA  . PRO A  1 129 ? 54.843  17.336  75.473  1.00 7.85  ? 129  PRO A CA  1 
ATOM   1006  C  C   . PRO A  1 129 ? 56.243  17.845  75.761  1.00 8.53  ? 129  PRO A C   1 
ATOM   1007  O  O   . PRO A  1 129 ? 57.114  17.031  75.986  1.00 9.17  ? 129  PRO A O   1 
ATOM   1008  C  CB  . PRO A  1 129 ? 53.853  17.780  76.607  1.00 7.49  ? 129  PRO A CB  1 
ATOM   1009  C  CG  . PRO A  1 129 ? 54.018  16.595  77.631  1.00 8.45  ? 129  PRO A CG  1 
ATOM   1010  C  CD  . PRO A  1 129 ? 54.009  15.403  76.724  1.00 6.24  ? 129  PRO A CD  1 
ATOM   1011  N  N   . GLY A  1 130 ? 56.474  19.171  75.781  1.00 9.53  ? 130  GLY A N   1 
ATOM   1012  C  CA  . GLY A  1 130 ? 57.813  19.671  76.035  1.00 8.72  ? 130  GLY A CA  1 
ATOM   1013  C  C   . GLY A  1 130 ? 58.218  19.617  77.524  1.00 10.29 ? 130  GLY A C   1 
ATOM   1014  O  O   . GLY A  1 130 ? 57.377  19.405  78.382  1.00 10.34 ? 130  GLY A O   1 
ATOM   1015  N  N   . GLY A  1 131 ? 59.509  19.771  77.827  1.00 10.00 ? 131  GLY A N   1 
ATOM   1016  C  CA  . GLY A  1 131 ? 59.986  19.796  79.224  1.00 10.10 ? 131  GLY A CA  1 
ATOM   1017  C  C   . GLY A  1 131 ? 60.720  18.507  79.624  1.00 10.89 ? 131  GLY A C   1 
ATOM   1018  O  O   . GLY A  1 131 ? 61.284  18.421  80.713  1.00 12.43 ? 131  GLY A O   1 
ATOM   1019  N  N   . PHE A  1 132 ? 60.728  17.503  78.753  1.00 9.97  ? 132  PHE A N   1 
ATOM   1020  C  CA  . PHE A  1 132 ? 61.377  16.239  79.091  1.00 9.34  ? 132  PHE A CA  1 
ATOM   1021  C  C   . PHE A  1 132 ? 62.886  16.475  79.238  1.00 10.82 ? 132  PHE A C   1 
ATOM   1022  O  O   . PHE A  1 132 ? 63.516  15.781  79.996  1.00 9.59  ? 132  PHE A O   1 
ATOM   1023  C  CB  . PHE A  1 132 ? 61.091  15.151  78.047  1.00 9.56  ? 132  PHE A CB  1 
ATOM   1024  C  CG  . PHE A  1 132 ? 61.741  13.828  78.370  1.00 10.70 ? 132  PHE A CG  1 
ATOM   1025  C  CD1 . PHE A  1 132 ? 61.160  12.969  79.311  1.00 8.73  ? 132  PHE A CD1 1 
ATOM   1026  C  CD2 . PHE A  1 132 ? 63.001  13.498  77.815  1.00 10.63 ? 132  PHE A CD2 1 
ATOM   1027  C  CE1 . PHE A  1 132 ? 61.773  11.729  79.648  1.00 10.74 ? 132  PHE A CE1 1 
ATOM   1028  C  CE2 . PHE A  1 132 ? 63.645  12.259  78.159  1.00 9.47  ? 132  PHE A CE2 1 
ATOM   1029  C  CZ  . PHE A  1 132 ? 63.029  11.386  79.069  1.00 10.24 ? 132  PHE A CZ  1 
ATOM   1030  N  N   . GLU A  1 133 ? 63.420  17.496  78.571  1.00 10.39 ? 133  GLU A N   1 
ATOM   1031  C  CA  . GLU A  1 133 ? 64.886  17.725  78.550  1.00 9.88  ? 133  GLU A CA  1 
ATOM   1032  C  C   . GLU A  1 133 ? 65.529  17.908  79.926  1.00 10.50 ? 133  GLU A C   1 
ATOM   1033  O  O   . GLU A  1 133 ? 66.742  17.730  80.067  1.00 9.04  ? 133  GLU A O   1 
ATOM   1034  C  CB  . GLU A  1 133 ? 65.271  18.874  77.589  1.00 9.71  ? 133  GLU A CB  1 
ATOM   1035  C  CG  . GLU A  1 133 ? 64.783  20.293  77.956  1.00 8.66  ? 133  GLU A CG  1 
ATOM   1036  C  CD  . GLU A  1 133 ? 63.309  20.552  77.622  1.00 8.11  ? 133  GLU A CD  1 
ATOM   1037  O  OE1 . GLU A  1 133 ? 62.632  19.650  77.092  1.00 8.87  ? 133  GLU A OE1 1 
ATOM   1038  O  OE2 . GLU A  1 133 ? 62.812  21.655  77.925  1.00 9.50  ? 133  GLU A OE2 1 
ATOM   1039  N  N   . ASP A  1 134 ? 64.733  18.243  80.957  1.00 10.35 ? 134  ASP A N   1 
ATOM   1040  C  CA  . ASP A  1 134 ? 65.309  18.299  82.294  1.00 10.20 ? 134  ASP A CA  1 
ATOM   1041  C  C   . ASP A  1 134 ? 66.123  17.054  82.588  1.00 10.78 ? 134  ASP A C   1 
ATOM   1042  O  O   . ASP A  1 134 ? 67.104  17.101  83.352  1.00 9.59  ? 134  ASP A O   1 
ATOM   1043  C  CB  . ASP A  1 134 ? 64.214  18.366  83.339  1.00 11.08 ? 134  ASP A CB  1 
ATOM   1044  C  CG  . ASP A  1 134 ? 63.590  19.715  83.424  1.00 13.86 ? 134  ASP A CG  1 
ATOM   1045  O  OD1 . ASP A  1 134 ? 64.088  20.658  82.770  1.00 12.47 ? 134  ASP A OD1 1 
ATOM   1046  O  OD2 . ASP A  1 134 ? 62.609  19.924  84.157  1.00 18.00 ? 134  ASP A OD2 1 
ATOM   1047  N  N   . LEU A  1 135 ? 65.663  15.921  82.035  1.00 9.57  ? 135  LEU A N   1 
ATOM   1048  C  CA  . LEU A  1 135 ? 66.294  14.655  82.272  1.00 9.81  ? 135  LEU A CA  1 
ATOM   1049  C  C   . LEU A  1 135 ? 67.706  14.738  81.748  1.00 8.73  ? 135  LEU A C   1 
ATOM   1050  O  O   . LEU A  1 135 ? 68.636  14.238  82.386  1.00 8.09  ? 135  LEU A O   1 
ATOM   1051  C  CB  . LEU A  1 135 ? 65.497  13.521  81.569  1.00 8.68  ? 135  LEU A CB  1 
ATOM   1052  C  CG  . LEU A  1 135 ? 65.968  12.053  81.497  1.00 12.64 ? 135  LEU A CG  1 
ATOM   1053  C  CD1 . LEU A  1 135 ? 67.055  11.829  80.449  1.00 15.73 ? 135  LEU A CD1 1 
ATOM   1054  C  CD2 . LEU A  1 135 ? 66.423  11.535  82.854  1.00 8.91  ? 135  LEU A CD2 1 
ATOM   1055  N  N   . PHE A  1 136 ? 67.873  15.354  80.569  1.00 8.22  ? 136  PHE A N   1 
ATOM   1056  C  CA  . PHE A  1 136 ? 69.244  15.469  80.002  1.00 8.35  ? 136  PHE A CA  1 
ATOM   1057  C  C   . PHE A  1 136 ? 70.092  16.491  80.688  1.00 7.31  ? 136  PHE A C   1 
ATOM   1058  O  O   . PHE A  1 136 ? 71.309  16.293  80.871  1.00 5.28  ? 136  PHE A O   1 
ATOM   1059  C  CB  . PHE A  1 136 ? 69.208  15.706  78.486  1.00 8.00  ? 136  PHE A CB  1 
ATOM   1060  C  CG  . PHE A  1 136 ? 68.519  14.596  77.750  1.00 8.36  ? 136  PHE A CG  1 
ATOM   1061  C  CD1 . PHE A  1 136 ? 69.153  13.363  77.584  1.00 10.37 ? 136  PHE A CD1 1 
ATOM   1062  C  CD2 . PHE A  1 136 ? 67.257  14.769  77.276  1.00 6.61  ? 136  PHE A CD2 1 
ATOM   1063  C  CE1 . PHE A  1 136 ? 68.529  12.312  76.909  1.00 9.62  ? 136  PHE A CE1 1 
ATOM   1064  C  CE2 . PHE A  1 136 ? 66.571  13.691  76.609  1.00 8.65  ? 136  PHE A CE2 1 
ATOM   1065  C  CZ  . PHE A  1 136 ? 67.237  12.457  76.434  1.00 8.98  ? 136  PHE A CZ  1 
ATOM   1066  N  N   . TYR A  1 137 ? 69.479  17.597  81.111  1.00 7.17  ? 137  TYR A N   1 
ATOM   1067  C  CA  . TYR A  1 137 ? 70.256  18.501  81.990  1.00 7.03  ? 137  TYR A CA  1 
ATOM   1068  C  C   . TYR A  1 137 ? 70.757  17.704  83.173  1.00 7.11  ? 137  TYR A C   1 
ATOM   1069  O  O   . TYR A  1 137 ? 71.960  17.686  83.469  1.00 7.58  ? 137  TYR A O   1 
ATOM   1070  C  CB  . TYR A  1 137 ? 69.406  19.645  82.520  1.00 7.12  ? 137  TYR A CB  1 
ATOM   1071  C  CG  . TYR A  1 137 ? 68.776  20.534  81.495  1.00 8.80  ? 137  TYR A CG  1 
ATOM   1072  C  CD1 . TYR A  1 137 ? 69.306  20.691  80.196  1.00 7.95  ? 137  TYR A CD1 1 
ATOM   1073  C  CD2 . TYR A  1 137 ? 67.609  21.249  81.829  1.00 10.63 ? 137  TYR A CD2 1 
ATOM   1074  C  CE1 . TYR A  1 137 ? 68.670  21.555  79.245  1.00 8.56  ? 137  TYR A CE1 1 
ATOM   1075  C  CE2 . TYR A  1 137 ? 66.993  22.081  80.900  1.00 7.22  ? 137  TYR A CE2 1 
ATOM   1076  C  CZ  . TYR A  1 137 ? 67.513  22.238  79.642  1.00 8.90  ? 137  TYR A CZ  1 
ATOM   1077  O  OH  . TYR A  1 137 ? 66.832  23.100  78.780  1.00 11.30 ? 137  TYR A OH  1 
ATOM   1078  N  N   . TYR A  1 138 ? 69.840  16.994  83.835  1.00 6.47  ? 138  TYR A N   1 
ATOM   1079  C  CA  . TYR A  1 138 ? 70.176  16.306  85.084  1.00 7.05  ? 138  TYR A CA  1 
ATOM   1080  C  C   . TYR A  1 138 ? 71.333  15.291  84.941  1.00 6.35  ? 138  TYR A C   1 
ATOM   1081  O  O   . TYR A  1 138 ? 72.339  15.372  85.664  1.00 5.51  ? 138  TYR A O   1 
ATOM   1082  C  CB  . TYR A  1 138 ? 68.920  15.591  85.557  1.00 6.78  ? 138  TYR A CB  1 
ATOM   1083  C  CG  . TYR A  1 138 ? 68.909  15.052  86.942  1.00 7.02  ? 138  TYR A CG  1 
ATOM   1084  C  CD1 . TYR A  1 138 ? 68.942  15.892  88.065  1.00 4.54  ? 138  TYR A CD1 1 
ATOM   1085  C  CD2 . TYR A  1 138 ? 68.737  13.669  87.152  1.00 3.44  ? 138  TYR A CD2 1 
ATOM   1086  C  CE1 . TYR A  1 138 ? 68.847  15.347  89.371  1.00 2.00  ? 138  TYR A CE1 1 
ATOM   1087  C  CE2 . TYR A  1 138 ? 68.660  13.128  88.454  1.00 5.77  ? 138  TYR A CE2 1 
ATOM   1088  C  CZ  . TYR A  1 138 ? 68.723  13.975  89.543  1.00 6.61  ? 138  TYR A CZ  1 
ATOM   1089  O  OH  . TYR A  1 138 ? 68.638  13.420  90.794  1.00 4.20  ? 138  TYR A OH  1 
ATOM   1090  N  N   . LEU A  1 139 ? 71.196  14.384  83.972  1.00 6.16  ? 139  LEU A N   1 
ATOM   1091  C  CA  . LEU A  1 139 ? 72.118  13.265  83.794  1.00 7.98  ? 139  LEU A CA  1 
ATOM   1092  C  C   . LEU A  1 139 ? 73.330  13.690  83.005  1.00 8.98  ? 139  LEU A C   1 
ATOM   1093  O  O   . LEU A  1 139 ? 74.374  13.035  83.070  1.00 8.85  ? 139  LEU A O   1 
ATOM   1094  C  CB  . LEU A  1 139 ? 71.448  12.153  83.011  1.00 8.09  ? 139  LEU A CB  1 
ATOM   1095  C  CG  . LEU A  1 139 ? 70.309  11.417  83.722  1.00 9.07  ? 139  LEU A CG  1 
ATOM   1096  C  CD1 . LEU A  1 139 ? 69.859  10.232  82.836  1.00 10.26 ? 139  LEU A CD1 1 
ATOM   1097  C  CD2 . LEU A  1 139 ? 70.790  10.979  85.086  1.00 6.39  ? 139  LEU A CD2 1 
ATOM   1098  N  N   . GLY A  1 140 ? 73.191  14.784  82.256  1.00 9.01  ? 140  GLY A N   1 
ATOM   1099  C  CA  . GLY A  1 140 ? 74.286  15.244  81.436  1.00 8.93  ? 140  GLY A CA  1 
ATOM   1100  C  C   . GLY A  1 140 ? 75.316  16.109  82.175  1.00 9.40  ? 140  GLY A C   1 
ATOM   1101  O  O   . GLY A  1 140 ? 75.125  16.508  83.362  1.00 8.88  ? 140  GLY A O   1 
ATOM   1102  N  N   . THR A  1 141 ? 76.429  16.370  81.486  1.00 7.25  ? 141  THR A N   1 
ATOM   1103  C  CA  . THR A  1 141 ? 77.433  17.332  81.990  1.00 7.56  ? 141  THR A CA  1 
ATOM   1104  C  C   . THR A  1 141 ? 77.450  18.539  81.062  1.00 6.71  ? 141  THR A C   1 
ATOM   1105  O  O   . THR A  1 141 ? 77.595  18.389  79.852  1.00 8.15  ? 141  THR A O   1 
ATOM   1106  C  CB  . THR A  1 141 ? 78.841  16.703  81.966  1.00 7.02  ? 141  THR A CB  1 
ATOM   1107  O  OG1 . THR A  1 141 ? 78.863  15.554  82.829  1.00 8.59  ? 141  THR A OG1 1 
ATOM   1108  C  CG2 . THR A  1 141 ? 79.881  17.672  82.568  1.00 6.83  ? 141  THR A CG2 1 
ATOM   1109  N  N   . ASN A  1 142 ? 77.340  19.730  81.613  1.00 6.34  ? 142  ASN A N   1 
ATOM   1110  C  CA  . ASN A  1 142 ? 77.343  20.939  80.797  1.00 8.13  ? 142  ASN A CA  1 
ATOM   1111  C  C   . ASN A  1 142 ? 78.523  20.945  79.793  1.00 8.22  ? 142  ASN A C   1 
ATOM   1112  O  O   . ASN A  1 142 ? 79.612  20.423  80.104  1.00 8.99  ? 142  ASN A O   1 
ATOM   1113  C  CB  . ASN A  1 142 ? 77.407  22.149  81.705  1.00 8.52  ? 142  ASN A CB  1 
ATOM   1114  C  CG  . ASN A  1 142 ? 78.745  22.313  82.337  1.00 11.46 ? 142  ASN A CG  1 
ATOM   1115  O  OD1 . ASN A  1 142 ? 79.583  23.110  81.854  1.00 10.71 ? 142  ASN A OD1 1 
ATOM   1116  N  ND2 . ASN A  1 142 ? 78.967  21.604  83.437  1.00 16.27 ? 142  ASN A ND2 1 
ATOM   1117  N  N   . ALA A  1 143 ? 78.268  21.395  78.569  1.00 7.20  ? 143  ALA A N   1 
ATOM   1118  C  CA  . ALA A  1 143 ? 79.324  21.447  77.551  1.00 8.27  ? 143  ALA A CA  1 
ATOM   1119  C  C   . ALA A  1 143 ? 79.389  22.873  76.989  1.00 8.22  ? 143  ALA A C   1 
ATOM   1120  O  O   . ALA A  1 143 ? 78.383  23.460  76.519  1.00 9.96  ? 143  ALA A O   1 
ATOM   1121  C  CB  . ALA A  1 143 ? 79.082  20.406  76.441  1.00 6.98  ? 143  ALA A CB  1 
ATOM   1122  N  N   . THR A  1 144 ? 80.552  23.447  77.108  1.00 7.28  ? 144  THR A N   1 
ATOM   1123  C  CA  . THR A  1 144 ? 80.806  24.765  76.551  1.00 9.36  ? 144  THR A CA  1 
ATOM   1124  C  C   . THR A  1 144 ? 80.913  24.664  75.006  1.00 7.49  ? 144  THR A C   1 
ATOM   1125  O  O   . THR A  1 144 ? 80.356  25.492  74.297  1.00 6.80  ? 144  THR A O   1 
ATOM   1126  C  CB  . THR A  1 144 ? 82.125  25.269  77.135  1.00 8.03  ? 144  THR A CB  1 
ATOM   1127  O  OG1 . THR A  1 144 ? 81.905  25.660  78.516  1.00 12.96 ? 144  THR A OG1 1 
ATOM   1128  C  CG2 . THR A  1 144 ? 82.536  26.519  76.466  1.00 12.37 ? 144  THR A CG2 1 
ATOM   1129  N  N   . ASP A  1 145 ? 81.710  23.706  74.541  1.00 7.97  ? 145  ASP A N   1 
ATOM   1130  C  CA  . ASP A  1 145 ? 81.925  23.433  73.119  1.00 8.28  ? 145  ASP A CA  1 
ATOM   1131  C  C   . ASP A  1 145 ? 82.143  24.722  72.322  1.00 8.07  ? 145  ASP A C   1 
ATOM   1132  O  O   . ASP A  1 145 ? 81.331  25.148  71.476  1.00 9.53  ? 145  ASP A O   1 
ATOM   1133  C  CB  . ASP A  1 145 ? 80.779  22.567  72.565  1.00 8.05  ? 145  ASP A CB  1 
ATOM   1134  C  CG  . ASP A  1 145 ? 81.100  22.002  71.175  1.00 8.98  ? 145  ASP A CG  1 
ATOM   1135  O  OD1 . ASP A  1 145 ? 82.241  22.252  70.637  1.00 6.12  ? 145  ASP A OD1 1 
ATOM   1136  O  OD2 . ASP A  1 145 ? 80.268  21.285  70.558  1.00 8.84  ? 145  ASP A OD2 1 
ATOM   1137  N  N   . THR A  1 146 ? 83.236  25.382  72.647  1.00 7.00  ? 146  THR A N   1 
ATOM   1138  C  CA  . THR A  1 146 ? 83.538  26.678  72.051  1.00 7.38  ? 146  THR A CA  1 
ATOM   1139  C  C   . THR A  1 146 ? 83.485  26.685  70.522  1.00 6.22  ? 146  THR A C   1 
ATOM   1140  O  O   . THR A  1 146 ? 82.982  27.648  69.932  1.00 4.92  ? 146  THR A O   1 
ATOM   1141  C  CB  . THR A  1 146 ? 84.919  27.148  72.488  1.00 6.42  ? 146  THR A CB  1 
ATOM   1142  O  OG1 . THR A  1 146 ? 84.954  27.234  73.925  1.00 9.25  ? 146  THR A OG1 1 
ATOM   1143  C  CG2 . THR A  1 146 ? 85.148  28.578  72.001  1.00 7.12  ? 146  THR A CG2 1 
ATOM   1144  N  N   . THR A  1 147 ? 84.015  25.625  69.915  1.00 6.43  ? 147  THR A N   1 
ATOM   1145  C  CA  . THR A  1 147 ? 84.129  25.556  68.449  1.00 7.19  ? 147  THR A CA  1 
ATOM   1146  C  C   . THR A  1 147 ? 82.851  25.093  67.761  1.00 7.99  ? 147  THR A C   1 
ATOM   1147  O  O   . THR A  1 147 ? 82.796  25.039  66.518  1.00 9.31  ? 147  THR A O   1 
ATOM   1148  C  CB  . THR A  1 147 ? 85.231  24.623  68.011  1.00 8.19  ? 147  THR A CB  1 
ATOM   1149  O  OG1 . THR A  1 147 ? 84.918  23.286  68.403  1.00 5.07  ? 147  THR A OG1 1 
ATOM   1150  C  CG2 . THR A  1 147 ? 86.617  24.966  68.645  1.00 5.41  ? 147  THR A CG2 1 
ATOM   1151  N  N   . HIS A  1 148 ? 81.831  24.773  68.550  1.00 6.75  ? 148  HIS A N   1 
ATOM   1152  C  CA  . HIS A  1 148 ? 80.601  24.196  68.019  1.00 9.19  ? 148  HIS A CA  1 
ATOM   1153  C  C   . HIS A  1 148 ? 80.801  22.877  67.247  1.00 8.54  ? 148  HIS A C   1 
ATOM   1154  O  O   . HIS A  1 148 ? 80.006  22.540  66.339  1.00 9.34  ? 148  HIS A O   1 
ATOM   1155  C  CB  . HIS A  1 148 ? 79.847  25.213  67.143  1.00 8.09  ? 148  HIS A CB  1 
ATOM   1156  C  CG  . HIS A  1 148 ? 79.453  26.454  67.856  1.00 10.01 ? 148  HIS A CG  1 
ATOM   1157  N  ND1 . HIS A  1 148 ? 80.325  27.510  68.046  1.00 14.38 ? 148  HIS A ND1 1 
ATOM   1158  C  CD2 . HIS A  1 148 ? 78.260  26.850  68.362  1.00 7.39  ? 148  HIS A CD2 1 
ATOM   1159  C  CE1 . HIS A  1 148 ? 79.681  28.499  68.648  1.00 12.19 ? 148  HIS A CE1 1 
ATOM   1160  N  NE2 . HIS A  1 148 ? 78.437  28.113  68.874  1.00 9.30  ? 148  HIS A NE2 1 
ATOM   1161  N  N   . THR A  1 149 ? 81.841  22.126  67.571  1.00 8.10  ? 149  THR A N   1 
ATOM   1162  C  CA  . THR A  1 149 ? 81.994  20.799  66.964  1.00 7.96  ? 149  THR A CA  1 
ATOM   1163  C  C   . THR A  1 149 ? 80.801  19.910  67.265  1.00 7.34  ? 149  THR A C   1 
ATOM   1164  O  O   . THR A  1 149 ? 80.202  19.993  68.383  1.00 7.55  ? 149  THR A O   1 
ATOM   1165  C  CB  . THR A  1 149 ? 83.314  20.172  67.375  1.00 7.71  ? 149  THR A CB  1 
ATOM   1166  O  OG1 . THR A  1 149 ? 83.577  19.045  66.532  1.00 8.49  ? 149  THR A OG1 1 
ATOM   1167  C  CG2 . THR A  1 149 ? 83.276  19.603  68.831  1.00 6.68  ? 149  THR A CG2 1 
ATOM   1168  N  N   . PRO A  1 150 ? 80.362  19.114  66.288  1.00 6.64  ? 150  PRO A N   1 
ATOM   1169  C  CA  . PRO A  1 150 ? 79.107  18.389  66.479  1.00 6.46  ? 150  PRO A CA  1 
ATOM   1170  C  C   . PRO A  1 150 ? 79.072  17.503  67.733  1.00 6.55  ? 150  PRO A C   1 
ATOM   1171  O  O   . PRO A  1 150 ? 78.038  17.464  68.413  1.00 6.57  ? 150  PRO A O   1 
ATOM   1172  C  CB  . PRO A  1 150 ? 78.989  17.572  65.200  1.00 5.44  ? 150  PRO A CB  1 
ATOM   1173  C  CG  . PRO A  1 150 ? 79.629  18.428  64.199  1.00 6.64  ? 150  PRO A CG  1 
ATOM   1174  C  CD  . PRO A  1 150 ? 80.903  18.937  64.918  1.00 7.46  ? 150  PRO A CD  1 
ATOM   1175  N  N   . TYR A  1 151 ? 80.154  16.780  67.990  1.00 6.70  ? 151  TYR A N   1 
ATOM   1176  C  CA  . TYR A  1 151 ? 80.318  16.087  69.256  1.00 7.97  ? 151  TYR A CA  1 
ATOM   1177  C  C   . TYR A  1 151 ? 81.805  16.141  69.631  1.00 9.91  ? 151  TYR A C   1 
ATOM   1178  O  O   . TYR A  1 151 ? 82.637  16.498  68.770  1.00 11.17 ? 151  TYR A O   1 
ATOM   1179  C  CB  . TYR A  1 151 ? 79.751  14.656  69.194  1.00 8.47  ? 151  TYR A CB  1 
ATOM   1180  C  CG  . TYR A  1 151 ? 80.445  13.672  68.252  1.00 9.41  ? 151  TYR A CG  1 
ATOM   1181  C  CD1 . TYR A  1 151 ? 81.721  13.154  68.529  1.00 9.37  ? 151  TYR A CD1 1 
ATOM   1182  C  CD2 . TYR A  1 151 ? 79.809  13.245  67.083  1.00 11.46 ? 151  TYR A CD2 1 
ATOM   1183  C  CE1 . TYR A  1 151 ? 82.338  12.252  67.653  1.00 9.96  ? 151  TYR A CE1 1 
ATOM   1184  C  CE2 . TYR A  1 151 ? 80.430  12.291  66.193  1.00 8.74  ? 151  TYR A CE2 1 
ATOM   1185  C  CZ  . TYR A  1 151 ? 81.659  11.822  66.480  1.00 11.04 ? 151  TYR A CZ  1 
ATOM   1186  O  OH  . TYR A  1 151 ? 82.204  10.897  65.597  1.00 10.30 ? 151  TYR A OH  1 
ATOM   1187  N  N   . ILE A  1 152 ? 82.143  15.841  70.892  1.00 9.04  ? 152  ILE A N   1 
ATOM   1188  C  CA  . ILE A  1 152 ? 83.531  15.951  71.350  1.00 11.04 ? 152  ILE A CA  1 
ATOM   1189  C  C   . ILE A  1 152 ? 84.328  14.726  70.885  1.00 12.30 ? 152  ILE A C   1 
ATOM   1190  O  O   . ILE A  1 152 ? 83.987  13.606  71.271  1.00 12.20 ? 152  ILE A O   1 
ATOM   1191  C  CB  . ILE A  1 152 ? 83.627  16.096  72.929  1.00 9.53  ? 152  ILE A CB  1 
ATOM   1192  C  CG1 . ILE A  1 152 ? 82.582  17.083  73.473  1.00 12.73 ? 152  ILE A CG1 1 
ATOM   1193  C  CG2 . ILE A  1 152 ? 85.059  16.550  73.400  1.00 13.43 ? 152  ILE A CG2 1 
ATOM   1194  C  CD1 . ILE A  1 152 ? 82.680  18.546  72.886  1.00 13.07 ? 152  ILE A CD1 1 
ATOM   1195  N  N   . PRO A  1 153 ? 85.375  14.922  70.070  1.00 14.11 ? 153  PRO A N   1 
ATOM   1196  C  CA  . PRO A  1 153 ? 86.142  13.790  69.499  1.00 16.10 ? 153  PRO A CA  1 
ATOM   1197  C  C   . PRO A  1 153 ? 86.742  12.851  70.574  1.00 18.73 ? 153  PRO A C   1 
ATOM   1198  O  O   . PRO A  1 153 ? 87.148  13.375  71.593  1.00 18.07 ? 153  PRO A O   1 
ATOM   1199  C  CB  . PRO A  1 153 ? 87.288  14.485  68.742  1.00 16.42 ? 153  PRO A CB  1 
ATOM   1200  C  CG  . PRO A  1 153 ? 86.871  15.862  68.555  1.00 15.31 ? 153  PRO A CG  1 
ATOM   1201  C  CD  . PRO A  1 153 ? 85.895  16.234  69.623  1.00 13.51 ? 153  PRO A CD  1 
ATOM   1202  N  N   . SER A  1 154 ? 86.786  11.527  70.351  1.00 22.22 ? 154  SER A N   1 
ATOM   1203  C  CA  . SER A  1 154 ? 87.489  10.580  71.279  1.00 25.79 ? 154  SER A CA  1 
ATOM   1204  C  C   . SER A  1 154 ? 87.911  9.252   70.646  1.00 26.37 ? 154  SER A C   1 
ATOM   1205  O  O   . SER A  1 154 ? 87.067  8.508   70.103  1.00 28.11 ? 154  SER A O   1 
ATOM   1206  C  CB  . SER A  1 154 ? 86.642  10.279  72.524  1.00 26.73 ? 154  SER A CB  1 
ATOM   1207  O  OG  . SER A  1 154 ? 86.622  11.401  73.411  1.00 31.03 ? 154  SER A OG  1 
ATOM   1208  N  N   . SER A  1 159 ? 83.487  -1.526  76.304  1.00 30.80 ? 159  SER A N   1 
ATOM   1209  C  CA  . SER A  1 159 ? 82.294  -0.696  76.042  1.00 30.09 ? 159  SER A CA  1 
ATOM   1210  C  C   . SER A  1 159 ? 81.064  -1.106  76.894  1.00 29.38 ? 159  SER A C   1 
ATOM   1211  O  O   . SER A  1 159 ? 80.346  -2.080  76.559  1.00 29.55 ? 159  SER A O   1 
ATOM   1212  C  CB  . SER A  1 159 ? 81.944  -0.721  74.543  1.00 30.12 ? 159  SER A CB  1 
ATOM   1213  O  OG  . SER A  1 159 ? 81.541  0.561   74.060  1.00 32.10 ? 159  SER A OG  1 
ATOM   1214  N  N   . SER A  1 160 ? 80.847  -0.356  77.985  1.00 27.25 ? 160  SER A N   1 
ATOM   1215  C  CA  . SER A  1 160 ? 79.597  -0.349  78.775  1.00 25.79 ? 160  SER A CA  1 
ATOM   1216  C  C   . SER A  1 160 ? 78.459  0.495   78.131  1.00 23.91 ? 160  SER A C   1 
ATOM   1217  O  O   . SER A  1 160 ? 78.726  1.429   77.349  1.00 22.79 ? 160  SER A O   1 
ATOM   1218  C  CB  . SER A  1 160 ? 79.874  0.233   80.172  1.00 26.02 ? 160  SER A CB  1 
ATOM   1219  O  OG  . SER A  1 160 ? 81.145  -0.186  80.647  1.00 30.20 ? 160  SER A OG  1 
ATOM   1220  N  N   . THR A  1 161 ? 77.204  0.168   78.460  1.00 21.66 ? 161  THR A N   1 
ATOM   1221  C  CA  . THR A  1 161 ? 76.051  0.958   78.003  1.00 19.90 ? 161  THR A CA  1 
ATOM   1222  C  C   . THR A  1 161 ? 76.227  2.416   78.425  1.00 19.34 ? 161  THR A C   1 
ATOM   1223  O  O   . THR A  1 161 ? 76.638  2.692   79.560  1.00 19.31 ? 161  THR A O   1 
ATOM   1224  C  CB  . THR A  1 161 ? 74.722  0.412   78.598  1.00 19.95 ? 161  THR A CB  1 
ATOM   1225  O  OG1 . THR A  1 161 ? 74.409  -0.877  78.032  1.00 19.81 ? 161  THR A OG1 1 
ATOM   1226  C  CG2 . THR A  1 161 ? 73.557  1.318   78.219  1.00 16.95 ? 161  THR A CG2 1 
ATOM   1227  N  N   . THR A  1 162 ? 75.897  3.329   77.523  1.00 17.79 ? 162  THR A N   1 
ATOM   1228  C  CA  . THR A  1 162 ? 76.013  4.767   77.766  1.00 16.62 ? 162  THR A CA  1 
ATOM   1229  C  C   . THR A  1 162 ? 74.859  5.241   78.656  1.00 15.47 ? 162  THR A C   1 
ATOM   1230  O  O   . THR A  1 162 ? 73.724  4.714   78.575  1.00 13.20 ? 162  THR A O   1 
ATOM   1231  C  CB  . THR A  1 162 ? 75.976  5.522   76.388  1.00 17.18 ? 162  THR A CB  1 
ATOM   1232  O  OG1 . THR A  1 162 ? 77.149  5.177   75.628  1.00 17.59 ? 162  THR A OG1 1 
ATOM   1233  C  CG2 . THR A  1 162 ? 76.092  7.029   76.555  1.00 17.12 ? 162  THR A CG2 1 
ATOM   1234  N  N   . GLY A  1 163 ? 75.138  6.234   79.502  1.00 14.62 ? 163  GLY A N   1 
ATOM   1235  C  CA  . GLY A  1 163 ? 74.074  6.900   80.242  1.00 13.41 ? 163  GLY A CA  1 
ATOM   1236  C  C   . GLY A  1 163 ? 74.019  6.277   81.624  1.00 13.70 ? 163  GLY A C   1 
ATOM   1237  O  O   . GLY A  1 163 ? 74.997  5.660   82.056  1.00 11.55 ? 163  GLY A O   1 
ATOM   1238  N  N   . PRO A  1 164 ? 72.879  6.414   82.317  1.00 13.84 ? 164  PRO A N   1 
ATOM   1239  C  CA  . PRO A  1 164 ? 72.781  5.918   83.704  1.00 14.13 ? 164  PRO A CA  1 
ATOM   1240  C  C   . PRO A  1 164 ? 72.997  4.387   83.788  1.00 15.12 ? 164  PRO A C   1 
ATOM   1241  O  O   . PRO A  1 164 ? 72.552  3.630   82.915  1.00 15.49 ? 164  PRO A O   1 
ATOM   1242  C  CB  . PRO A  1 164 ? 71.369  6.341   84.152  1.00 14.18 ? 164  PRO A CB  1 
ATOM   1243  C  CG  . PRO A  1 164 ? 70.602  6.706   82.884  1.00 13.86 ? 164  PRO A CG  1 
ATOM   1244  C  CD  . PRO A  1 164 ? 71.646  7.080   81.846  1.00 13.74 ? 164  PRO A CD  1 
ATOM   1245  N  N   . ASP A  1 165 ? 73.713  3.941   84.813  1.00 16.00 ? 165  ASP A N   1 
ATOM   1246  C  CA  . ASP A  1 165 ? 73.772  2.511   85.090  1.00 16.12 ? 165  ASP A CA  1 
ATOM   1247  C  C   . ASP A  1 165 ? 72.392  1.980   85.577  1.00 16.53 ? 165  ASP A C   1 
ATOM   1248  O  O   . ASP A  1 165 ? 71.454  2.772   85.783  1.00 15.25 ? 165  ASP A O   1 
ATOM   1249  C  CB  . ASP A  1 165 ? 74.914  2.185   86.052  1.00 15.64 ? 165  ASP A CB  1 
ATOM   1250  C  CG  . ASP A  1 165 ? 74.749  2.816   87.430  1.00 17.23 ? 165  ASP A CG  1 
ATOM   1251  O  OD1 . ASP A  1 165 ? 73.655  3.343   87.757  1.00 14.76 ? 165  ASP A OD1 1 
ATOM   1252  O  OD2 . ASP A  1 165 ? 75.689  2.816   88.262  1.00 16.79 ? 165  ASP A OD2 1 
ATOM   1253  N  N   . SER A  1 166 ? 72.273  0.664   85.765  1.00 16.39 ? 166  SER A N   1 
ATOM   1254  C  CA  . SER A  1 166 ? 70.960  0.062   86.039  1.00 17.39 ? 166  SER A CA  1 
ATOM   1255  C  C   . SER A  1 166 ? 70.345  0.566   87.361  1.00 17.32 ? 166  SER A C   1 
ATOM   1256  O  O   . SER A  1 166 ? 69.127  0.797   87.428  1.00 17.51 ? 166  SER A O   1 
ATOM   1257  C  CB  . SER A  1 166 ? 71.031  -1.463  85.980  1.00 16.45 ? 166  SER A CB  1 
ATOM   1258  O  OG  . SER A  1 166 ? 71.899  -1.960  86.986  1.00 19.19 ? 166  SER A OG  1 
ATOM   1259  N  N   . SER A  1 167 ? 71.198  0.749   88.377  1.00 17.34 ? 167  SER A N   1 
ATOM   1260  C  CA  . SER A  1 167 ? 70.811  1.363   89.651  1.00 17.67 ? 167  SER A CA  1 
ATOM   1261  C  C   . SER A  1 167 ? 70.237  2.773   89.455  1.00 17.22 ? 167  SER A C   1 
ATOM   1262  O  O   . SER A  1 167 ? 69.188  3.095   90.021  1.00 17.72 ? 167  SER A O   1 
ATOM   1263  C  CB  . SER A  1 167 ? 71.994  1.416   90.602  1.00 17.82 ? 167  SER A CB  1 
ATOM   1264  O  OG  . SER A  1 167 ? 72.298  0.119   91.056  1.00 19.80 ? 167  SER A OG  1 
ATOM   1265  N  N   . THR A  1 168 ? 70.899  3.599   88.642  1.00 16.74 ? 168  THR A N   1 
ATOM   1266  C  CA  . THR A  1 168 ? 70.505  5.002   88.485  1.00 16.34 ? 168  THR A CA  1 
ATOM   1267  C  C   . THR A  1 168 ? 69.234  5.151   87.662  1.00 16.39 ? 168  THR A C   1 
ATOM   1268  O  O   . THR A  1 168 ? 68.367  5.957   88.023  1.00 16.87 ? 168  THR A O   1 
ATOM   1269  C  CB  . THR A  1 168 ? 71.615  5.819   87.821  1.00 16.87 ? 168  THR A CB  1 
ATOM   1270  O  OG1 . THR A  1 168 ? 72.750  5.880   88.690  1.00 17.15 ? 168  THR A OG1 1 
ATOM   1271  C  CG2 . THR A  1 168 ? 71.167  7.318   87.625  1.00 17.09 ? 168  THR A CG2 1 
ATOM   1272  N  N   . ILE A  1 169 ? 69.120  4.410   86.549  1.00 14.89 ? 169  ILE A N   1 
ATOM   1273  C  CA  . ILE A  1 169 ? 67.936  4.544   85.695  1.00 13.92 ? 169  ILE A CA  1 
ATOM   1274  C  C   . ILE A  1 169 ? 66.593  4.071   86.325  1.00 13.44 ? 169  ILE A C   1 
ATOM   1275  O  O   . ILE A  1 169 ? 65.510  4.436   85.823  1.00 14.20 ? 169  ILE A O   1 
ATOM   1276  C  CB  . ILE A  1 169 ? 68.156  3.923   84.295  1.00 14.54 ? 169  ILE A CB  1 
ATOM   1277  C  CG1 . ILE A  1 169 ? 67.253  4.654   83.274  1.00 11.30 ? 169  ILE A CG1 1 
ATOM   1278  C  CG2 . ILE A  1 169 ? 67.962  2.385   84.365  1.00 13.85 ? 169  ILE A CG2 1 
ATOM   1279  C  CD1 . ILE A  1 169 ? 67.575  4.379   81.814  1.00 12.24 ? 169  ILE A CD1 1 
ATOM   1280  N  N   . SER A  1 170 ? 66.685  3.296   87.403  1.00 12.33 ? 170  SER A N   1 
ATOM   1281  C  CA  . SER A  1 170 ? 65.539  2.819   88.210  1.00 12.14 ? 170  SER A CA  1 
ATOM   1282  C  C   . SER A  1 170 ? 65.047  3.848   89.250  1.00 12.00 ? 170  SER A C   1 
ATOM   1283  O  O   . SER A  1 170 ? 64.152  3.560   90.044  1.00 12.29 ? 170  SER A O   1 
ATOM   1284  C  CB  . SER A  1 170 ? 65.901  1.515   88.937  1.00 12.08 ? 170  SER A CB  1 
ATOM   1285  O  OG  . SER A  1 170 ? 66.125  0.436   88.020  1.00 13.17 ? 170  SER A OG  1 
ATOM   1286  N  N   . THR A  1 171 ? 65.566  5.067   89.168  1.00 11.06 ? 171  THR A N   1 
ATOM   1287  C  CA  . THR A  1 171 ? 65.476  6.075   90.228  1.00 10.62 ? 171  THR A CA  1 
ATOM   1288  C  C   . THR A  1 171 ? 64.883  7.420   89.682  1.00 9.28  ? 171  THR A C   1 
ATOM   1289  O  O   . THR A  1 171 ? 64.727  8.420   90.400  1.00 7.98  ? 171  THR A O   1 
ATOM   1290  C  CB  . THR A  1 171 ? 66.949  6.177   90.657  1.00 10.75 ? 171  THR A CB  1 
ATOM   1291  O  OG1 . THR A  1 171 ? 67.130  5.449   91.870  1.00 12.59 ? 171  THR A OG1 1 
ATOM   1292  C  CG2 . THR A  1 171 ? 67.432  7.503   90.870  1.00 9.02  ? 171  THR A CG2 1 
ATOM   1293  N  N   . LEU A  1 172 ? 64.504  7.367   88.409  1.00 7.22  ? 172  LEU A N   1 
ATOM   1294  C  CA  . LEU A  1 172 ? 64.260  8.566   87.594  1.00 6.52  ? 172  LEU A CA  1 
ATOM   1295  C  C   . LEU A  1 172 ? 62.778  8.785   87.265  1.00 5.83  ? 172  LEU A C   1 
ATOM   1296  O  O   . LEU A  1 172 ? 62.433  9.522   86.304  1.00 6.09  ? 172  LEU A O   1 
ATOM   1297  C  CB  . LEU A  1 172 ? 65.090  8.448   86.303  1.00 5.75  ? 172  LEU A CB  1 
ATOM   1298  C  CG  . LEU A  1 172 ? 66.641  8.525   86.451  1.00 4.67  ? 172  LEU A CG  1 
ATOM   1299  C  CD1 . LEU A  1 172 ? 67.264  8.496   85.121  1.00 6.00  ? 172  LEU A CD1 1 
ATOM   1300  C  CD2 . LEU A  1 172 ? 67.140  9.771   87.221  1.00 6.10  ? 172  LEU A CD2 1 
ATOM   1301  N  N   . GLN A  1 173 ? 61.904  8.199   88.086  1.00 5.93  ? 173  GLN A N   1 
ATOM   1302  C  CA  . GLN A  1 173 ? 60.437  8.328   87.842  1.00 7.15  ? 173  GLN A CA  1 
ATOM   1303  C  C   . GLN A  1 173 ? 59.982  9.785   87.770  1.00 5.95  ? 173  GLN A C   1 
ATOM   1304  O  O   . GLN A  1 173 ? 59.063  10.141  87.022  1.00 5.89  ? 173  GLN A O   1 
ATOM   1305  C  CB  . GLN A  1 173 ? 59.609  7.580   88.905  1.00 6.99  ? 173  GLN A CB  1 
ATOM   1306  C  CG  . GLN A  1 173 ? 59.734  6.093   88.856  1.00 13.43 ? 173  GLN A CG  1 
ATOM   1307  C  CD  . GLN A  1 173 ? 58.829  5.350   89.877  1.00 25.42 ? 173  GLN A CD  1 
ATOM   1308  O  OE1 . GLN A  1 173 ? 58.799  4.080   89.890  1.00 28.40 ? 173  GLN A OE1 1 
ATOM   1309  N  NE2 . GLN A  1 173 ? 58.089  6.121   90.738  1.00 27.89 ? 173  GLN A NE2 1 
ATOM   1310  N  N   . SER A  1 174 ? 60.657  10.649  88.512  1.00 5.33  ? 174  SER A N   1 
ATOM   1311  C  CA  . SER A  1 174 ? 60.315  12.056  88.512  1.00 5.02  ? 174  SER A CA  1 
ATOM   1312  C  C   . SER A  1 174 ? 60.504  12.676  87.117  1.00 5.85  ? 174  SER A C   1 
ATOM   1313  O  O   . SER A  1 174 ? 59.790  13.632  86.715  1.00 5.69  ? 174  SER A O   1 
ATOM   1314  C  CB  . SER A  1 174 ? 61.130  12.783  89.616  1.00 4.68  ? 174  SER A CB  1 
ATOM   1315  O  OG  . SER A  1 174 ? 60.990  14.196  89.535  1.00 6.76  ? 174  SER A OG  1 
ATOM   1316  N  N   . PHE A  1 175 ? 61.468  12.163  86.357  1.00 4.59  ? 175  PHE A N   1 
ATOM   1317  C  CA  . PHE A  1 175 ? 61.706  12.674  85.034  1.00 4.77  ? 175  PHE A CA  1 
ATOM   1318  C  C   . PHE A  1 175 ? 60.914  11.887  83.979  1.00 4.77  ? 175  PHE A C   1 
ATOM   1319  O  O   . PHE A  1 175 ? 61.153  12.007  82.792  1.00 5.48  ? 175  PHE A O   1 
ATOM   1320  C  CB  . PHE A  1 175 ? 63.206  12.624  84.710  1.00 4.70  ? 175  PHE A CB  1 
ATOM   1321  C  CG  . PHE A  1 175 ? 64.034  13.465  85.618  1.00 4.23  ? 175  PHE A CG  1 
ATOM   1322  C  CD1 . PHE A  1 175 ? 64.264  14.814  85.344  1.00 5.49  ? 175  PHE A CD1 1 
ATOM   1323  C  CD2 . PHE A  1 175 ? 64.550  12.927  86.781  1.00 2.81  ? 175  PHE A CD2 1 
ATOM   1324  C  CE1 . PHE A  1 175 ? 65.070  15.589  86.219  1.00 2.08  ? 175  PHE A CE1 1 
ATOM   1325  C  CE2 . PHE A  1 175 ? 65.305  13.705  87.659  1.00 5.34  ? 175  PHE A CE2 1 
ATOM   1326  C  CZ  . PHE A  1 175 ? 65.567  15.041  87.365  1.00 2.00  ? 175  PHE A CZ  1 
ATOM   1327  N  N   . ASP A  1 176 ? 59.969  11.076  84.422  1.00 4.45  ? 176  ASP A N   1 
ATOM   1328  C  CA  . ASP A  1 176 ? 59.170  10.251  83.498  1.00 4.81  ? 176  ASP A CA  1 
ATOM   1329  C  C   . ASP A  1 176 ? 60.006  9.220   82.738  1.00 5.08  ? 176  ASP A C   1 
ATOM   1330  O  O   . ASP A  1 176 ? 59.767  8.969   81.562  1.00 4.48  ? 176  ASP A O   1 
ATOM   1331  C  CB  . ASP A  1 176 ? 58.349  11.075  82.506  1.00 5.02  ? 176  ASP A CB  1 
ATOM   1332  C  CG  . ASP A  1 176 ? 57.266  10.235  81.818  1.00 4.73  ? 176  ASP A CG  1 
ATOM   1333  O  OD1 . ASP A  1 176 ? 56.741  9.347   82.478  1.00 5.99  ? 176  ASP A OD1 1 
ATOM   1334  O  OD2 . ASP A  1 176 ? 56.890  10.385  80.655  1.00 5.08  ? 176  ASP A OD2 1 
ATOM   1335  N  N   . VAL A  1 177 ? 60.965  8.642   83.450  1.00 4.46  ? 177  VAL A N   1 
ATOM   1336  C  CA  . VAL A  1 177 ? 61.769  7.559   82.942  1.00 4.74  ? 177  VAL A CA  1 
ATOM   1337  C  C   . VAL A  1 177 ? 61.602  6.384   83.854  1.00 4.37  ? 177  VAL A C   1 
ATOM   1338  O  O   . VAL A  1 177 ? 61.797  6.505   85.062  1.00 5.27  ? 177  VAL A O   1 
ATOM   1339  C  CB  . VAL A  1 177 ? 63.274  7.919   82.939  1.00 5.86  ? 177  VAL A CB  1 
ATOM   1340  C  CG1 . VAL A  1 177 ? 64.127  6.688   82.463  1.00 5.14  ? 177  VAL A CG1 1 
ATOM   1341  C  CG2 . VAL A  1 177 ? 63.519  9.143   82.011  1.00 4.16  ? 177  VAL A CG2 1 
ATOM   1342  N  N   . TYR A  1 178 ? 61.300  5.214   83.279  1.00 5.26  ? 178  TYR A N   1 
ATOM   1343  C  CA  . TYR A  1 178 ? 61.069  4.031   84.096  1.00 5.56  ? 178  TYR A CA  1 
ATOM   1344  C  C   . TYR A  1 178 ? 61.851  2.918   83.479  1.00 5.99  ? 178  TYR A C   1 
ATOM   1345  O  O   . TYR A  1 178 ? 61.697  2.651   82.307  1.00 6.50  ? 178  TYR A O   1 
ATOM   1346  C  CB  . TYR A  1 178 ? 59.587  3.623   84.077  1.00 5.82  ? 178  TYR A CB  1 
ATOM   1347  C  CG  . TYR A  1 178 ? 58.688  4.637   84.729  1.00 4.62  ? 178  TYR A CG  1 
ATOM   1348  C  CD1 . TYR A  1 178 ? 58.235  5.747   84.013  1.00 6.51  ? 178  TYR A CD1 1 
ATOM   1349  C  CD2 . TYR A  1 178 ? 58.298  4.489   86.074  1.00 6.28  ? 178  TYR A CD2 1 
ATOM   1350  C  CE1 . TYR A  1 178 ? 57.438  6.740   84.633  1.00 6.63  ? 178  TYR A CE1 1 
ATOM   1351  C  CE2 . TYR A  1 178 ? 57.474  5.479   86.701  1.00 8.07  ? 178  TYR A CE2 1 
ATOM   1352  C  CZ  . TYR A  1 178 ? 57.061  6.592   85.946  1.00 9.10  ? 178  TYR A CZ  1 
ATOM   1353  O  OH  . TYR A  1 178 ? 56.277  7.568   86.504  1.00 7.88  ? 178  TYR A OH  1 
ATOM   1354  N  N   . ALA A  1 179 ? 62.671  2.281   84.293  1.00 7.07  ? 179  ALA A N   1 
ATOM   1355  C  CA  . ALA A  1 179 ? 63.567  1.212   83.851  1.00 7.38  ? 179  ALA A CA  1 
ATOM   1356  C  C   . ALA A  1 179 ? 62.765  0.016   83.372  1.00 8.04  ? 179  ALA A C   1 
ATOM   1357  O  O   . ALA A  1 179 ? 61.755  -0.320  83.984  1.00 7.41  ? 179  ALA A O   1 
ATOM   1358  C  CB  . ALA A  1 179 ? 64.391  0.787   84.985  1.00 6.50  ? 179  ALA A CB  1 
ATOM   1359  N  N   . GLU A  1 180 ? 63.245  -0.624  82.307  1.00 7.62  ? 180  GLU A N   1 
ATOM   1360  C  CA  . GLU A  1 180 ? 62.758  -1.941  81.886  1.00 8.46  ? 180  GLU A CA  1 
ATOM   1361  C  C   . GLU A  1 180 ? 63.931  -2.882  81.757  1.00 9.68  ? 180  GLU A C   1 
ATOM   1362  O  O   . GLU A  1 180 ? 64.349  -3.207  80.649  1.00 8.75  ? 180  GLU A O   1 
ATOM   1363  C  CB  . GLU A  1 180 ? 62.033  -1.839  80.535  1.00 8.36  ? 180  GLU A CB  1 
ATOM   1364  C  CG  . GLU A  1 180 ? 60.797  -0.963  80.587  1.00 9.62  ? 180  GLU A CG  1 
ATOM   1365  C  CD  . GLU A  1 180 ? 59.674  -1.512  81.464  1.00 17.10 ? 180  GLU A CD  1 
ATOM   1366  O  OE1 . GLU A  1 180 ? 59.588  -2.747  81.698  1.00 19.99 ? 180  GLU A OE1 1 
ATOM   1367  O  OE2 . GLU A  1 180 ? 58.842  -0.687  81.899  1.00 22.84 ? 180  GLU A OE2 1 
ATOM   1368  N  N   . LEU A  1 181 ? 64.396  -3.403  82.880  1.00 10.86 ? 181  LEU A N   1 
ATOM   1369  C  CA  . LEU A  1 181 ? 65.661  -4.105  82.895  1.00 13.03 ? 181  LEU A CA  1 
ATOM   1370  C  C   . LEU A  1 181 ? 65.522  -5.575  82.414  1.00 13.78 ? 181  LEU A C   1 
ATOM   1371  O  O   . LEU A  1 181 ? 66.526  -6.238  82.105  1.00 14.05 ? 181  LEU A O   1 
ATOM   1372  C  CB  . LEU A  1 181 ? 66.256  -3.992  84.308  1.00 14.29 ? 181  LEU A CB  1 
ATOM   1373  C  CG  . LEU A  1 181 ? 67.290  -2.892  84.680  1.00 15.88 ? 181  LEU A CG  1 
ATOM   1374  C  CD1 . LEU A  1 181 ? 67.401  -1.656  83.787  1.00 17.09 ? 181  LEU A CD1 1 
ATOM   1375  C  CD2 . LEU A  1 181 ? 67.147  -2.471  86.141  1.00 17.84 ? 181  LEU A CD2 1 
ATOM   1376  N  N   . SER A  1 182 ? 64.280  -6.069  82.354  1.00 13.26 ? 182  SER A N   1 
ATOM   1377  C  CA  . SER A  1 182 ? 63.965  -7.359  81.757  1.00 12.80 ? 182  SER A CA  1 
ATOM   1378  C  C   . SER A  1 182 ? 63.936  -7.299  80.235  1.00 11.55 ? 182  SER A C   1 
ATOM   1379  O  O   . SER A  1 182 ? 63.795  -8.349  79.612  1.00 11.05 ? 182  SER A O   1 
ATOM   1380  C  CB  . SER A  1 182 ? 62.586  -7.865  82.229  1.00 13.50 ? 182  SER A CB  1 
ATOM   1381  O  OG  . SER A  1 182 ? 61.513  -7.268  81.468  1.00 18.68 ? 182  SER A OG  1 
ATOM   1382  N  N   . PHE A  1 183 ? 63.976  -6.094  79.644  1.00 8.93  ? 183  PHE A N   1 
ATOM   1383  C  CA  . PHE A  1 183 ? 63.979  -5.985  78.188  1.00 8.64  ? 183  PHE A CA  1 
ATOM   1384  C  C   . PHE A  1 183 ? 65.305  -6.484  77.620  1.00 7.95  ? 183  PHE A C   1 
ATOM   1385  O  O   . PHE A  1 183 ? 66.376  -6.020  78.040  1.00 6.30  ? 183  PHE A O   1 
ATOM   1386  C  CB  . PHE A  1 183 ? 63.714  -4.556  77.744  1.00 8.07  ? 183  PHE A CB  1 
ATOM   1387  C  CG  . PHE A  1 183 ? 63.502  -4.391  76.262  1.00 8.44  ? 183  PHE A CG  1 
ATOM   1388  C  CD1 . PHE A  1 183 ? 62.269  -4.712  75.670  1.00 10.97 ? 183  PHE A CD1 1 
ATOM   1389  C  CD2 . PHE A  1 183 ? 64.510  -3.842  75.458  1.00 6.65  ? 183  PHE A CD2 1 
ATOM   1390  C  CE1 . PHE A  1 183 ? 62.070  -4.512  74.331  1.00 7.50  ? 183  PHE A CE1 1 
ATOM   1391  C  CE2 . PHE A  1 183 ? 64.327  -3.674  74.096  1.00 7.35  ? 183  PHE A CE2 1 
ATOM   1392  C  CZ  . PHE A  1 183 ? 63.095  -3.976  73.531  1.00 10.75 ? 183  PHE A CZ  1 
ATOM   1393  N  N   . THR A  1 184 ? 65.232  -7.420  76.661  1.00 7.18  ? 184  THR A N   1 
ATOM   1394  C  CA  . THR A  1 184 ? 66.444  -7.849  75.952  1.00 6.77  ? 184  THR A CA  1 
ATOM   1395  C  C   . THR A  1 184 ? 66.361  -7.457  74.481  1.00 6.02  ? 184  THR A C   1 
ATOM   1396  O  O   . THR A  1 184 ? 65.532  -8.019  73.734  1.00 6.55  ? 184  THR A O   1 
ATOM   1397  C  CB  . THR A  1 184 ? 66.699  -9.352  76.091  1.00 6.87  ? 184  THR A CB  1 
ATOM   1398  O  OG1 . THR A  1 184 ? 66.894  -9.751  77.471  1.00 9.29  ? 184  THR A OG1 1 
ATOM   1399  C  CG2 . THR A  1 184 ? 68.060  -9.713  75.413  1.00 7.90  ? 184  THR A CG2 1 
ATOM   1400  N  N   . PRO A  1 185 ? 67.132  -6.453  74.052  1.00 4.70  ? 185  PRO A N   1 
ATOM   1401  C  CA  . PRO A  1 185 ? 67.139  -6.059  72.618  1.00 5.62  ? 185  PRO A CA  1 
ATOM   1402  C  C   . PRO A  1 185 ? 67.416  -7.240  71.711  1.00 5.94  ? 185  PRO A C   1 
ATOM   1403  O  O   . PRO A  1 185 ? 68.338  -8.028  72.008  1.00 6.75  ? 185  PRO A O   1 
ATOM   1404  C  CB  . PRO A  1 185 ? 68.241  -4.982  72.517  1.00 6.06  ? 185  PRO A CB  1 
ATOM   1405  C  CG  . PRO A  1 185 ? 68.234  -4.336  73.974  1.00 5.24  ? 185  PRO A CG  1 
ATOM   1406  C  CD  . PRO A  1 185 ? 68.034  -5.612  74.872  1.00 6.17  ? 185  PRO A CD  1 
ATOM   1407  N  N   . ARG A  1 186 ? 66.573  -7.439  70.694  1.00 6.04  ? 186  ARG A N   1 
ATOM   1408  C  CA  . ARG A  1 186 ? 66.708  -8.679  69.902  1.00 6.78  ? 186  ARG A CA  1 
ATOM   1409  C  C   . ARG A  1 186 ? 67.981  -8.584  69.063  1.00 7.57  ? 186  ARG A C   1 
ATOM   1410  O  O   . ARG A  1 186 ? 68.412  -7.483  68.707  1.00 7.89  ? 186  ARG A O   1 
ATOM   1411  C  CB  . ARG A  1 186 ? 65.476  -8.927  69.003  1.00 6.62  ? 186  ARG A CB  1 
ATOM   1412  C  CG  . ARG A  1 186 ? 65.048  -7.832  68.031  1.00 6.63  ? 186  ARG A CG  1 
ATOM   1413  C  CD  . ARG A  1 186 ? 63.707  -8.194  67.326  1.00 7.76  ? 186  ARG A CD  1 
ATOM   1414  N  NE  . ARG A  1 186 ? 63.739  -9.594  66.898  1.00 7.03  ? 186  ARG A NE  1 
ATOM   1415  C  CZ  . ARG A  1 186 ? 62.684  -10.394 66.914  1.00 7.13  ? 186  ARG A CZ  1 
ATOM   1416  N  NH1 . ARG A  1 186 ? 61.497  -9.906  67.297  1.00 5.82  ? 186  ARG A NH1 1 
ATOM   1417  N  NH2 . ARG A  1 186 ? 62.794  -11.632 66.478  1.00 7.02  ? 186  ARG A NH2 1 
ATOM   1418  N  N   . THR A  1 187 ? 68.592  -9.725  68.763  1.00 6.90  ? 187  THR A N   1 
ATOM   1419  C  CA  . THR A  1 187 ? 69.898  -9.704  68.142  1.00 8.20  ? 187  THR A CA  1 
ATOM   1420  C  C   . THR A  1 187 ? 69.928  -10.524 66.853  1.00 8.74  ? 187  THR A C   1 
ATOM   1421  O  O   . THR A  1 187 ? 70.959  -11.136 66.504  1.00 8.90  ? 187  THR A O   1 
ATOM   1422  C  CB  . THR A  1 187 ? 70.972  -10.196 69.122  1.00 8.86  ? 187  THR A CB  1 
ATOM   1423  O  OG1 . THR A  1 187 ? 70.616  -11.473 69.677  1.00 7.93  ? 187  THR A OG1 1 
ATOM   1424  C  CG2 . THR A  1 187 ? 71.085  -9.254  70.351  1.00 10.99 ? 187  THR A CG2 1 
ATOM   1425  N  N   . ASP A  1 188 ? 68.794  -10.524 66.155  1.00 7.64  ? 188  ASP A N   1 
ATOM   1426  C  CA  . ASP A  1 188 ? 68.688  -11.286 64.905  1.00 7.33  ? 188  ASP A CA  1 
ATOM   1427  C  C   . ASP A  1 188 ? 68.460  -10.333 63.729  1.00 6.79  ? 188  ASP A C   1 
ATOM   1428  O  O   . ASP A  1 188 ? 67.844  -10.692 62.727  1.00 7.95  ? 188  ASP A O   1 
ATOM   1429  C  CB  . ASP A  1 188 ? 67.602  -12.407 64.997  1.00 6.18  ? 188  ASP A CB  1 
ATOM   1430  C  CG  . ASP A  1 188 ? 66.202  -11.895 65.389  1.00 6.63  ? 188  ASP A CG  1 
ATOM   1431  O  OD1 . ASP A  1 188 ? 66.035  -10.751 65.867  1.00 8.09  ? 188  ASP A OD1 1 
ATOM   1432  O  OD2 . ASP A  1 188 ? 65.166  -12.573 65.232  1.00 9.62  ? 188  ASP A OD2 1 
ATOM   1433  N  N   . THR A  1 189 ? 68.940  -9.104  63.874  1.00 6.50  ? 189  THR A N   1 
ATOM   1434  C  CA  . THR A  1 189 ? 68.890  -8.099  62.822  1.00 5.94  ? 189  THR A CA  1 
ATOM   1435  C  C   . THR A  1 189 ? 69.541  -8.626  61.566  1.00 6.98  ? 189  THR A C   1 
ATOM   1436  O  O   . THR A  1 189 ? 70.659  -9.233  61.631  1.00 5.62  ? 189  THR A O   1 
ATOM   1437  C  CB  . THR A  1 189 ? 69.652  -6.826  63.290  1.00 6.20  ? 189  THR A CB  1 
ATOM   1438  O  OG1 . THR A  1 189 ? 69.237  -6.522  64.640  1.00 9.26  ? 189  THR A OG1 1 
ATOM   1439  C  CG2 . THR A  1 189 ? 69.213  -5.631  62.481  1.00 3.22  ? 189  THR A CG2 1 
ATOM   1440  N  N   . VAL A  1 190 ? 68.853  -8.431  60.435  1.00 6.27  ? 190  VAL A N   1 
ATOM   1441  C  CA  . VAL A  1 190 ? 69.442  -8.742  59.133  1.00 7.56  ? 190  VAL A CA  1 
ATOM   1442  C  C   . VAL A  1 190 ? 68.925  -7.687  58.187  1.00 8.31  ? 190  VAL A C   1 
ATOM   1443  O  O   . VAL A  1 190 ? 67.728  -7.299  58.289  1.00 9.57  ? 190  VAL A O   1 
ATOM   1444  C  CB  . VAL A  1 190 ? 68.996  -10.128 58.593  1.00 6.58  ? 190  VAL A CB  1 
ATOM   1445  C  CG1 . VAL A  1 190 ? 69.665  -10.386 57.236  1.00 5.76  ? 190  VAL A CG1 1 
ATOM   1446  C  CG2 . VAL A  1 190 ? 69.258  -11.291 59.571  1.00 11.41 ? 190  VAL A CG2 1 
ATOM   1447  N  N   . ASN A  1 191 ? 69.791  -7.130  57.318  1.00 8.18  ? 191  ASN A N   1 
ATOM   1448  C  CA  . ASN A  1 191 ? 69.383  -5.975  56.478  1.00 8.20  ? 191  ASN A CA  1 
ATOM   1449  C  C   . ASN A  1 191 ? 68.712  -4.857  57.223  1.00 9.03  ? 191  ASN A C   1 
ATOM   1450  O  O   . ASN A  1 191 ? 67.760  -4.235  56.710  1.00 8.32  ? 191  ASN A O   1 
ATOM   1451  C  CB  . ASN A  1 191 ? 68.493  -6.415  55.307  1.00 7.81  ? 191  ASN A CB  1 
ATOM   1452  C  CG  . ASN A  1 191 ? 69.179  -7.468  54.422  1.00 10.17 ? 191  ASN A CG  1 
ATOM   1453  O  OD1 . ASN A  1 191 ? 70.415  -7.514  54.355  1.00 9.73  ? 191  ASN A OD1 1 
ATOM   1454  N  ND2 . ASN A  1 191 ? 68.380  -8.324  53.768  1.00 8.90  ? 191  ASN A ND2 1 
ATOM   1455  N  N   . GLY A  1 192 ? 69.199  -4.549  58.436  1.00 9.11  ? 192  GLY A N   1 
ATOM   1456  C  CA  . GLY A  1 192 ? 68.650  -3.411  59.142  1.00 7.10  ? 192  GLY A CA  1 
ATOM   1457  C  C   . GLY A  1 192 ? 67.295  -3.651  59.822  1.00 7.44  ? 192  GLY A C   1 
ATOM   1458  O  O   . GLY A  1 192 ? 66.684  -2.682  60.268  1.00 5.85  ? 192  GLY A O   1 
ATOM   1459  N  N   . THR A  1 193 ? 66.805  -4.904  59.905  1.00 7.12  ? 193  THR A N   1 
ATOM   1460  C  CA  . THR A  1 193 ? 65.482  -5.114  60.542  1.00 7.11  ? 193  THR A CA  1 
ATOM   1461  C  C   . THR A  1 193 ? 65.382  -6.444  61.238  1.00 7.62  ? 193  THR A C   1 
ATOM   1462  O  O   . THR A  1 193 ? 66.087  -7.373  60.883  1.00 7.23  ? 193  THR A O   1 
ATOM   1463  C  CB  . THR A  1 193 ? 64.301  -4.919  59.494  1.00 8.05  ? 193  THR A CB  1 
ATOM   1464  O  OG1 . THR A  1 193 ? 63.045  -4.856  60.196  1.00 6.48  ? 193  THR A OG1 1 
ATOM   1465  C  CG2 . THR A  1 193 ? 64.163  -6.181  58.550  1.00 6.67  ? 193  THR A CG2 1 
ATOM   1466  N  N   . ALA A  1 194 ? 64.560  -6.520  62.294  1.00 7.94  ? 194  ALA A N   1 
ATOM   1467  C  CA  . ALA A  1 194 ? 64.082  -7.787  62.853  1.00 6.62  ? 194  ALA A CA  1 
ATOM   1468  C  C   . ALA A  1 194 ? 62.680  -7.481  63.470  1.00 7.20  ? 194  ALA A C   1 
ATOM   1469  O  O   . ALA A  1 194 ? 62.468  -6.343  63.944  1.00 7.63  ? 194  ALA A O   1 
ATOM   1470  C  CB  . ALA A  1 194 ? 65.038  -8.355  63.964  1.00 5.47  ? 194  ALA A CB  1 
ATOM   1471  N  N   . PRO A  1 195 ? 61.747  -8.461  63.492  1.00 6.00  ? 195  PRO A N   1 
ATOM   1472  C  CA  . PRO A  1 195 ? 61.969  -9.805  62.936  1.00 7.30  ? 195  PRO A CA  1 
ATOM   1473  C  C   . PRO A  1 195 ? 61.954  -9.764  61.396  1.00 7.72  ? 195  PRO A C   1 
ATOM   1474  O  O   . PRO A  1 195 ? 61.765  -8.696  60.789  1.00 6.28  ? 195  PRO A O   1 
ATOM   1475  C  CB  . PRO A  1 195 ? 60.796  -10.639 63.519  1.00 7.03  ? 195  PRO A CB  1 
ATOM   1476  C  CG  . PRO A  1 195 ? 59.702  -9.661  63.819  1.00 4.45  ? 195  PRO A CG  1 
ATOM   1477  C  CD  . PRO A  1 195 ? 60.398  -8.314  64.075  1.00 6.53  ? 195  PRO A CD  1 
ATOM   1478  N  N   . ALA A  1 196 ? 62.224  -10.906 60.771  1.00 8.74  ? 196  ALA A N   1 
ATOM   1479  C  CA  . ALA A  1 196 ? 62.434  -10.926 59.332  1.00 9.46  ? 196  ALA A CA  1 
ATOM   1480  C  C   . ALA A  1 196 ? 61.147  -10.542 58.574  1.00 11.02 ? 196  ALA A C   1 
ATOM   1481  O  O   . ALA A  1 196 ? 61.223  -9.949  57.495  1.00 11.41 ? 196  ALA A O   1 
ATOM   1482  C  CB  . ALA A  1 196 ? 62.901  -12.246 58.926  1.00 11.11 ? 196  ALA A CB  1 
ATOM   1483  N  N   . ASN A  1 197 ? 59.988  -10.880 59.140  1.00 11.64 ? 197  ASN A N   1 
ATOM   1484  C  CA  . ASN A  1 197 ? 58.701  -10.576 58.527  1.00 12.28 ? 197  ASN A CA  1 
ATOM   1485  C  C   . ASN A  1 197 ? 58.228  -9.127  58.651  1.00 12.23 ? 197  ASN A C   1 
ATOM   1486  O  O   . ASN A  1 197 ? 57.078  -8.874  59.080  1.00 14.09 ? 197  ASN A O   1 
ATOM   1487  C  CB  . ASN A  1 197 ? 57.629  -11.472 59.151  1.00 13.31 ? 197  ASN A CB  1 
ATOM   1488  C  CG  . ASN A  1 197 ? 56.357  -11.552 58.291  1.00 19.54 ? 197  ASN A CG  1 
ATOM   1489  O  OD1 . ASN A  1 197 ? 56.436  -11.550 57.045  1.00 23.20 ? 197  ASN A OD1 1 
ATOM   1490  N  ND2 . ASN A  1 197 ? 55.184  -11.674 58.946  1.00 23.96 ? 197  ASN A ND2 1 
ATOM   1491  N  N   . THR A  1 198 ? 59.096  -8.181  58.326  1.00 10.41 ? 198  THR A N   1 
ATOM   1492  C  CA  . THR A  1 198 ? 58.789  -6.744  58.374  1.00 8.06  ? 198  THR A CA  1 
ATOM   1493  C  C   . THR A  1 198 ? 59.240  -6.123  57.074  1.00 7.35  ? 198  THR A C   1 
ATOM   1494  O  O   . THR A  1 198 ? 59.963  -6.772  56.287  1.00 6.75  ? 198  THR A O   1 
ATOM   1495  C  CB  . THR A  1 198 ? 59.628  -6.075  59.547  1.00 8.90  ? 198  THR A CB  1 
ATOM   1496  O  OG1 . THR A  1 198 ? 61.013  -6.492  59.451  1.00 8.29  ? 198  THR A OG1 1 
ATOM   1497  C  CG2 . THR A  1 198 ? 59.146  -6.535  60.916  1.00 6.29  ? 198  THR A CG2 1 
ATOM   1498  N  N   . VAL A  1 199 ? 58.914  -4.839  56.867  1.00 7.03  ? 199  VAL A N   1 
ATOM   1499  C  CA  . VAL A  1 199 ? 59.284  -4.111  55.657  1.00 5.79  ? 199  VAL A CA  1 
ATOM   1500  C  C   . VAL A  1 199 ? 60.114  -2.885  56.050  1.00 5.75  ? 199  VAL A C   1 
ATOM   1501  O  O   . VAL A  1 199 ? 59.656  -2.049  56.788  1.00 6.41  ? 199  VAL A O   1 
ATOM   1502  C  CB  . VAL A  1 199 ? 57.973  -3.553  54.934  1.00 6.38  ? 199  VAL A CB  1 
ATOM   1503  C  CG1 . VAL A  1 199 ? 58.282  -2.850  53.612  1.00 5.07  ? 199  VAL A CG1 1 
ATOM   1504  C  CG2 . VAL A  1 199 ? 56.952  -4.700  54.706  1.00 8.84  ? 199  VAL A CG2 1 
ATOM   1505  N  N   . TRP A  1 200 ? 61.325  -2.806  55.515  1.00 5.29  ? 200  TRP A N   1 
ATOM   1506  C  CA  . TRP A  1 200 ? 62.277  -1.754  55.876  1.00 6.00  ? 200  TRP A CA  1 
ATOM   1507  C  C   . TRP A  1 200 ? 63.198  -1.508  54.680  1.00 5.46  ? 200  TRP A C   1 
ATOM   1508  O  O   . TRP A  1 200 ? 64.158  -2.299  54.411  1.00 7.08  ? 200  TRP A O   1 
ATOM   1509  C  CB  . TRP A  1 200 ? 63.116  -2.214  57.122  1.00 5.61  ? 200  TRP A CB  1 
ATOM   1510  C  CG  . TRP A  1 200 ? 63.861  -1.053  57.707  1.00 5.26  ? 200  TRP A CG  1 
ATOM   1511  C  CD1 . TRP A  1 200 ? 65.229  -0.926  57.895  1.00 5.14  ? 200  TRP A CD1 1 
ATOM   1512  C  CD2 . TRP A  1 200 ? 63.281  0.176   58.133  1.00 6.50  ? 200  TRP A CD2 1 
ATOM   1513  N  NE1 . TRP A  1 200 ? 65.510  0.324   58.430  1.00 6.79  ? 200  TRP A NE1 1 
ATOM   1514  C  CE2 . TRP A  1 200 ? 64.341  1.013   58.596  1.00 6.45  ? 200  TRP A CE2 1 
ATOM   1515  C  CE3 . TRP A  1 200 ? 61.957  0.663   58.205  1.00 5.95  ? 200  TRP A CE3 1 
ATOM   1516  C  CZ2 . TRP A  1 200 ? 64.108  2.294   59.096  1.00 6.29  ? 200  TRP A CZ2 1 
ATOM   1517  C  CZ3 . TRP A  1 200 ? 61.741  1.929   58.715  1.00 7.64  ? 200  TRP A CZ3 1 
ATOM   1518  C  CH2 . TRP A  1 200 ? 62.792  2.718   59.163  1.00 8.52  ? 200  TRP A CH2 1 
ATOM   1519  N  N   . HIS A  1 201 ? 62.916  -0.433  53.952  1.00 5.71  ? 201  HIS A N   1 
ATOM   1520  C  CA  . HIS A  1 201 ? 63.643  -0.023  52.746  1.00 7.33  ? 201  HIS A CA  1 
ATOM   1521  C  C   . HIS A  1 201 ? 63.352  -0.929  51.560  1.00 8.96  ? 201  HIS A C   1 
ATOM   1522  O  O   . HIS A  1 201 ? 64.065  -0.848  50.533  1.00 9.76  ? 201  HIS A O   1 
ATOM   1523  C  CB  . HIS A  1 201 ? 65.171  0.146   52.981  1.00 7.10  ? 201  HIS A CB  1 
ATOM   1524  C  CG  . HIS A  1 201 ? 65.505  1.363   53.778  1.00 6.61  ? 201  HIS A CG  1 
ATOM   1525  N  ND1 . HIS A  1 201 ? 65.612  2.626   53.218  1.00 8.76  ? 201  HIS A ND1 1 
ATOM   1526  C  CD2 . HIS A  1 201 ? 65.664  1.529   55.116  1.00 7.63  ? 201  HIS A CD2 1 
ATOM   1527  C  CE1 . HIS A  1 201 ? 65.873  3.505   54.180  1.00 8.94  ? 201  HIS A CE1 1 
ATOM   1528  N  NE2 . HIS A  1 201 ? 65.892  2.862   55.338  1.00 6.50  ? 201  HIS A NE2 1 
ATOM   1529  N  N   . THR A  1 202 ? 62.303  -1.747  51.702  1.00 8.41  ? 202  THR A N   1 
ATOM   1530  C  CA  . THR A  1 202 ? 61.911  -2.697  50.665  1.00 9.82  ? 202  THR A CA  1 
ATOM   1531  C  C   . THR A  1 202 ? 60.454  -2.570  50.185  1.00 10.32 ? 202  THR A C   1 
ATOM   1532  O  O   . THR A  1 202 ? 59.997  -3.372  49.368  1.00 10.38 ? 202  THR A O   1 
ATOM   1533  C  CB  . THR A  1 202 ? 62.170  -4.152  51.140  1.00 10.34 ? 202  THR A CB  1 
ATOM   1534  O  OG1 . THR A  1 202 ? 61.354  -4.430  52.300  1.00 8.76  ? 202  THR A OG1 1 
ATOM   1535  C  CG2 . THR A  1 202 ? 63.683  -4.375  51.574  1.00 10.91 ? 202  THR A CG2 1 
ATOM   1536  N  N   . GLY A  1 203 ? 59.712  -1.602  50.695  1.00 8.90  ? 203  GLY A N   1 
ATOM   1537  C  CA  . GLY A  1 203 ? 58.294  -1.559  50.392  1.00 9.07  ? 203  GLY A CA  1 
ATOM   1538  C  C   . GLY A  1 203 ? 57.647  -0.476  51.243  1.00 8.58  ? 203  GLY A C   1 
ATOM   1539  O  O   . GLY A  1 203 ? 58.336  0.148   52.087  1.00 7.87  ? 203  GLY A O   1 
ATOM   1540  N  N   . ALA A  1 204 ? 56.354  -0.220  51.004  1.00 8.43  ? 204  ALA A N   1 
ATOM   1541  C  CA  . ALA A  1 204 ? 55.639  0.833   51.722  1.00 8.56  ? 204  ALA A CA  1 
ATOM   1542  C  C   . ALA A  1 204 ? 55.528  0.529   53.248  1.00 8.03  ? 204  ALA A C   1 
ATOM   1543  O  O   . ALA A  1 204 ? 55.372  -0.652  53.689  1.00 8.91  ? 204  ALA A O   1 
ATOM   1544  C  CB  . ALA A  1 204 ? 54.222  1.060   51.091  1.00 9.34  ? 204  ALA A CB  1 
ATOM   1545  N  N   . ASN A  1 205 ? 55.620  1.587   54.048  1.00 7.43  ? 205  ASN A N   1 
ATOM   1546  C  CA  . ASN A  1 205 ? 55.410  1.503   55.505  1.00 8.86  ? 205  ASN A CA  1 
ATOM   1547  C  C   . ASN A  1 205 ? 54.128  2.276   55.823  1.00 9.33  ? 205  ASN A C   1 
ATOM   1548  O  O   . ASN A  1 205 ? 53.959  3.388   55.345  1.00 10.34 ? 205  ASN A O   1 
ATOM   1549  C  CB  . ASN A  1 205 ? 56.524  2.210   56.257  1.00 7.73  ? 205  ASN A CB  1 
ATOM   1550  C  CG  . ASN A  1 205 ? 57.863  1.536   56.082  1.00 11.74 ? 205  ASN A CG  1 
ATOM   1551  O  OD1 . ASN A  1 205 ? 58.842  2.172   55.716  1.00 8.13  ? 205  ASN A OD1 1 
ATOM   1552  N  ND2 . ASN A  1 205 ? 57.895  0.216   56.283  1.00 7.85  ? 205  ASN A ND2 1 
ATOM   1553  N  N   . ALA A  1 206 ? 53.269  1.701   56.641  1.00 7.69  ? 206  ALA A N   1 
ATOM   1554  C  CA  . ALA A  1 206 ? 52.050  2.372   57.089  1.00 8.66  ? 206  ALA A CA  1 
ATOM   1555  C  C   . ALA A  1 206 ? 52.301  2.950   58.487  1.00 9.17  ? 206  ALA A C   1 
ATOM   1556  O  O   . ALA A  1 206 ? 53.184  2.470   59.230  1.00 8.74  ? 206  ALA A O   1 
ATOM   1557  C  CB  . ALA A  1 206 ? 50.839  1.323   57.144  1.00 8.65  ? 206  ALA A CB  1 
ATOM   1558  N  N   . LEU A  1 207 ? 51.551  3.985   58.836  1.00 8.58  ? 207  LEU A N   1 
ATOM   1559  C  CA  . LEU A  1 207 ? 51.548  4.466   60.236  1.00 8.70  ? 207  LEU A CA  1 
ATOM   1560  C  C   . LEU A  1 207 ? 50.757  3.431   61.033  1.00 8.77  ? 207  LEU A C   1 
ATOM   1561  O  O   . LEU A  1 207 ? 49.946  2.696   60.459  1.00 8.75  ? 207  LEU A O   1 
ATOM   1562  C  CB  . LEU A  1 207 ? 50.889  5.863   60.362  1.00 7.41  ? 207  LEU A CB  1 
ATOM   1563  C  CG  . LEU A  1 207 ? 51.748  7.077   59.974  1.00 10.05 ? 207  LEU A CG  1 
ATOM   1564  C  CD1 . LEU A  1 207 ? 52.001  7.128   58.504  1.00 10.94 ? 207  LEU A CD1 1 
ATOM   1565  C  CD2 . LEU A  1 207 ? 51.002  8.353   60.419  1.00 8.60  ? 207  LEU A CD2 1 
ATOM   1566  N  N   . ALA A  1 208 ? 50.966  3.366   62.359  1.00 7.57  ? 208  ALA A N   1 
ATOM   1567  C  CA  . ALA A  1 208 ? 50.229  2.339   63.110  1.00 7.83  ? 208  ALA A CA  1 
ATOM   1568  C  C   . ALA A  1 208 ? 48.745  2.646   63.020  1.00 7.25  ? 208  ALA A C   1 
ATOM   1569  O  O   . ALA A  1 208 ? 48.349  3.830   62.907  1.00 6.25  ? 208  ALA A O   1 
ATOM   1570  C  CB  . ALA A  1 208 ? 50.689  2.304   64.552  1.00 8.69  ? 208  ALA A CB  1 
ATOM   1571  N  N   . SER A  1 209 ? 47.938  1.588   63.076  1.00 5.64  ? 209  SER A N   1 
ATOM   1572  C  CA  . SER A  1 209 ? 46.489  1.719   62.979  1.00 5.95  ? 209  SER A CA  1 
ATOM   1573  C  C   . SER A  1 209 ? 45.834  2.424   64.179  1.00 6.15  ? 209  SER A C   1 
ATOM   1574  O  O   . SER A  1 209 ? 44.732  2.930   64.061  1.00 5.32  ? 209  SER A O   1 
ATOM   1575  C  CB  . SER A  1 209 ? 45.881  0.334   62.810  1.00 6.04  ? 209  SER A CB  1 
ATOM   1576  O  OG  . SER A  1 209 ? 46.363  -0.206  61.598  1.00 6.36  ? 209  SER A OG  1 
ATOM   1577  N  N   . THR A  1 210 ? 46.523  2.487   65.326  1.00 6.35  ? 210  THR A N   1 
ATOM   1578  C  CA  . THR A  1 210 ? 45.990  3.169   66.505  1.00 7.05  ? 210  THR A CA  1 
ATOM   1579  C  C   . THR A  1 210 ? 47.129  3.662   67.409  1.00 7.62  ? 210  THR A C   1 
ATOM   1580  O  O   . THR A  1 210 ? 48.291  3.328   67.143  1.00 7.78  ? 210  THR A O   1 
ATOM   1581  C  CB  . THR A  1 210 ? 44.985  2.277   67.260  1.00 6.77  ? 210  THR A CB  1 
ATOM   1582  O  OG1 . THR A  1 210 ? 44.211  3.069   68.183  1.00 5.78  ? 210  THR A OG1 1 
ATOM   1583  C  CG2 . THR A  1 210 ? 45.692  1.183   68.112  1.00 8.52  ? 210  THR A CG2 1 
ATOM   1584  N  N   . ALA A  1 211 ? 46.795  4.395   68.472  1.00 7.05  ? 211  ALA A N   1 
ATOM   1585  C  CA  . ALA A  1 211 ? 47.816  4.965   69.344  1.00 8.06  ? 211  ALA A CA  1 
ATOM   1586  C  C   . ALA A  1 211 ? 48.401  3.866   70.211  1.00 8.09  ? 211  ALA A C   1 
ATOM   1587  O  O   . ALA A  1 211 ? 47.725  2.856   70.461  1.00 9.30  ? 211  ALA A O   1 
ATOM   1588  C  CB  . ALA A  1 211 ? 47.221  6.123   70.243  1.00 7.16  ? 211  ALA A CB  1 
ATOM   1589  N  N   . GLY A  1 212 ? 49.632  4.052   70.669  1.00 7.92  ? 212  GLY A N   1 
ATOM   1590  C  CA  . GLY A  1 212 ? 50.207  3.132   71.646  1.00 8.66  ? 212  GLY A CA  1 
ATOM   1591  C  C   . GLY A  1 212 ? 51.169  2.109   71.062  1.00 9.12  ? 212  GLY A C   1 
ATOM   1592  O  O   . GLY A  1 212 ? 51.887  1.449   71.796  1.00 10.53 ? 212  GLY A O   1 
ATOM   1593  N  N   . ASP A  1 213 ? 51.167  1.938   69.744  1.00 8.99  ? 213  ASP A N   1 
ATOM   1594  C  CA  . ASP A  1 213 ? 52.037  0.953   69.078  1.00 10.09 ? 213  ASP A CA  1 
ATOM   1595  C  C   . ASP A  1 213 ? 53.196  1.657   68.395  1.00 9.65  ? 213  ASP A C   1 
ATOM   1596  O  O   . ASP A  1 213 ? 52.983  2.656   67.708  1.00 9.55  ? 213  ASP A O   1 
ATOM   1597  C  CB  . ASP A  1 213 ? 51.261  0.193   68.009  1.00 9.74  ? 213  ASP A CB  1 
ATOM   1598  C  CG  . ASP A  1 213 ? 50.156  -0.652  68.605  1.00 14.13 ? 213  ASP A CG  1 
ATOM   1599  O  OD1 . ASP A  1 213 ? 50.390  -1.223  69.696  1.00 13.17 ? 213  ASP A OD1 1 
ATOM   1600  O  OD2 . ASP A  1 213 ? 49.033  -0.765  68.065  1.00 15.26 ? 213  ASP A OD2 1 
ATOM   1601  N  N   . PRO A  1 214 ? 54.410  1.132   68.549  1.00 8.61  ? 214  PRO A N   1 
ATOM   1602  C  CA  . PRO A  1 214 ? 55.534  1.703   67.836  1.00 8.34  ? 214  PRO A CA  1 
ATOM   1603  C  C   . PRO A  1 214 ? 55.388  1.394   66.359  1.00 7.34  ? 214  PRO A C   1 
ATOM   1604  O  O   . PRO A  1 214 ? 54.642  0.438   65.978  1.00 5.28  ? 214  PRO A O   1 
ATOM   1605  C  CB  . PRO A  1 214 ? 56.728  0.946   68.452  1.00 8.72  ? 214  PRO A CB  1 
ATOM   1606  C  CG  . PRO A  1 214 ? 56.113  -0.451  68.711  1.00 7.70  ? 214  PRO A CG  1 
ATOM   1607  C  CD  . PRO A  1 214 ? 54.803  -0.045  69.375  1.00 9.15  ? 214  PRO A CD  1 
ATOM   1608  N  N   . TYR A  1 215 ? 56.018  2.219   65.520  1.00 6.69  ? 215  TYR A N   1 
ATOM   1609  C  CA  . TYR A  1 215 ? 56.079  1.931   64.078  1.00 7.00  ? 215  TYR A CA  1 
ATOM   1610  C  C   . TYR A  1 215 ? 57.214  2.699   63.477  1.00 7.75  ? 215  TYR A C   1 
ATOM   1611  O  O   . TYR A  1 215 ? 57.712  3.639   64.117  1.00 8.73  ? 215  TYR A O   1 
ATOM   1612  C  CB  . TYR A  1 215 ? 54.741  2.247   63.366  1.00 6.47  ? 215  TYR A CB  1 
ATOM   1613  C  CG  . TYR A  1 215 ? 54.273  3.681   63.557  1.00 5.14  ? 215  TYR A CG  1 
ATOM   1614  C  CD1 . TYR A  1 215 ? 53.591  4.048   64.725  1.00 6.75  ? 215  TYR A CD1 1 
ATOM   1615  C  CD2 . TYR A  1 215 ? 54.546  4.656   62.615  1.00 6.57  ? 215  TYR A CD2 1 
ATOM   1616  C  CE1 . TYR A  1 215 ? 53.149  5.365   64.925  1.00 4.68  ? 215  TYR A CE1 1 
ATOM   1617  C  CE2 . TYR A  1 215 ? 54.081  5.993   62.793  1.00 7.30  ? 215  TYR A CE2 1 
ATOM   1618  C  CZ  . TYR A  1 215 ? 53.411  6.320   63.966  1.00 9.83  ? 215  TYR A CZ  1 
ATOM   1619  O  OH  . TYR A  1 215 ? 52.977  7.606   64.179  1.00 7.00  ? 215  TYR A OH  1 
ATOM   1620  N  N   . PHE A  1 216 ? 57.645  2.296   62.271  1.00 8.39  ? 216  PHE A N   1 
ATOM   1621  C  CA  . PHE A  1 216 ? 58.831  2.892   61.637  1.00 8.10  ? 216  PHE A CA  1 
ATOM   1622  C  C   . PHE A  1 216 ? 58.542  3.253   60.204  1.00 8.54  ? 216  PHE A C   1 
ATOM   1623  O  O   . PHE A  1 216 ? 57.842  2.507   59.508  1.00 9.30  ? 216  PHE A O   1 
ATOM   1624  C  CB  . PHE A  1 216 ? 60.017  1.937   61.695  1.00 7.38  ? 216  PHE A CB  1 
ATOM   1625  C  CG  . PHE A  1 216 ? 60.202  1.307   63.053  1.00 8.22  ? 216  PHE A CG  1 
ATOM   1626  C  CD1 . PHE A  1 216 ? 59.359  0.285   63.476  1.00 8.25  ? 216  PHE A CD1 1 
ATOM   1627  C  CD2 . PHE A  1 216 ? 61.231  1.758   63.910  1.00 9.85  ? 216  PHE A CD2 1 
ATOM   1628  C  CE1 . PHE A  1 216 ? 59.546  -0.272  64.755  1.00 10.86 ? 216  PHE A CE1 1 
ATOM   1629  C  CE2 . PHE A  1 216 ? 61.444  1.166   65.167  1.00 8.39  ? 216  PHE A CE2 1 
ATOM   1630  C  CZ  . PHE A  1 216 ? 60.595  0.160   65.571  1.00 10.83 ? 216  PHE A CZ  1 
ATOM   1631  N  N   . ILE A  1 217 ? 59.099  4.371   59.758  1.00 8.95  ? 217  ILE A N   1 
ATOM   1632  C  CA  . ILE A  1 217 ? 58.893  4.769   58.372  1.00 8.89  ? 217  ILE A CA  1 
ATOM   1633  C  C   . ILE A  1 217 ? 60.250  5.034   57.758  1.00 7.69  ? 217  ILE A C   1 
ATOM   1634  O  O   . ILE A  1 217 ? 60.989  5.922   58.181  1.00 9.48  ? 217  ILE A O   1 
ATOM   1635  C  CB  . ILE A  1 217 ? 57.920  5.996   58.242  1.00 7.53  ? 217  ILE A CB  1 
ATOM   1636  C  CG1 . ILE A  1 217 ? 56.492  5.617   58.716  1.00 8.39  ? 217  ILE A CG1 1 
ATOM   1637  C  CG2 . ILE A  1 217 ? 57.817  6.458   56.719  1.00 9.46  ? 217  ILE A CG2 1 
ATOM   1638  C  CD1 . ILE A  1 217 ? 55.626  6.869   58.957  1.00 17.23 ? 217  ILE A CD1 1 
ATOM   1639  N  N   . ALA A  1 218 ? 60.572  4.268   56.732  1.00 8.51  ? 218  ALA A N   1 
ATOM   1640  C  CA  . ALA A  1 218 ? 61.849  4.466   56.044  1.00 8.52  ? 218  ALA A CA  1 
ATOM   1641  C  C   . ALA A  1 218 ? 61.690  5.618   55.050  1.00 8.82  ? 218  ALA A C   1 
ATOM   1642  O  O   . ALA A  1 218 ? 60.621  5.792   54.503  1.00 7.65  ? 218  ALA A O   1 
ATOM   1643  C  CB  . ALA A  1 218 ? 62.222  3.189   55.276  1.00 7.95  ? 218  ALA A CB  1 
ATOM   1644  N  N   . ASN A  1 219 ? 62.788  6.311   54.758  1.00 8.04  ? 219  ASN A N   1 
ATOM   1645  C  CA  . ASN A  1 219 ? 62.782  7.546   53.989  1.00 9.57  ? 219  ASN A CA  1 
ATOM   1646  C  C   . ASN A  1 219 ? 62.155  7.338   52.612  1.00 8.84  ? 219  ASN A C   1 
ATOM   1647  O  O   . ASN A  1 219 ? 62.700  6.611   51.764  1.00 8.68  ? 219  ASN A O   1 
ATOM   1648  C  CB  . ASN A  1 219 ? 64.253  8.011   53.826  1.00 8.75  ? 219  ASN A CB  1 
ATOM   1649  C  CG  . ASN A  1 219 ? 64.372  9.379   53.182  1.00 13.66 ? 219  ASN A CG  1 
ATOM   1650  O  OD1 . ASN A  1 219 ? 63.411  10.131  53.109  1.00 13.39 ? 219  ASN A OD1 1 
ATOM   1651  N  ND2 . ASN A  1 219 ? 65.565  9.694   52.693  1.00 18.27 ? 219  ASN A ND2 1 
ATOM   1652  N  N   . GLY A  1 220 ? 61.036  8.015   52.379  1.00 10.21 ? 220  GLY A N   1 
ATOM   1653  C  CA  . GLY A  1 220 ? 60.370  7.989   51.090  1.00 9.27  ? 220  GLY A CA  1 
ATOM   1654  C  C   . GLY A  1 220 ? 59.312  6.914   50.977  1.00 9.54  ? 220  GLY A C   1 
ATOM   1655  O  O   . GLY A  1 220 ? 58.618  6.829   49.961  1.00 9.36  ? 220  GLY A O   1 
ATOM   1656  N  N   . TRP A  1 221 ? 59.206  6.050   51.978  1.00 8.90  ? 221  TRP A N   1 
ATOM   1657  C  CA  . TRP A  1 221 ? 58.383  4.840   51.812  1.00 8.40  ? 221  TRP A CA  1 
ATOM   1658  C  C   . TRP A  1 221 ? 56.998  4.940   52.511  1.00 9.57  ? 221  TRP A C   1 
ATOM   1659  O  O   . TRP A  1 221 ? 56.205  3.992   52.448  1.00 8.25  ? 221  TRP A O   1 
ATOM   1660  C  CB  . TRP A  1 221 ? 59.127  3.637   52.357  1.00 9.56  ? 221  TRP A CB  1 
ATOM   1661  C  CG  . TRP A  1 221 ? 60.294  3.163   51.527  1.00 9.59  ? 221  TRP A CG  1 
ATOM   1662  C  CD1 . TRP A  1 221 ? 61.624  3.368   51.771  1.00 7.05  ? 221  TRP A CD1 1 
ATOM   1663  C  CD2 . TRP A  1 221 ? 60.216  2.364   50.334  1.00 7.64  ? 221  TRP A CD2 1 
ATOM   1664  N  NE1 . TRP A  1 221 ? 62.377  2.733   50.809  1.00 7.88  ? 221  TRP A NE1 1 
ATOM   1665  C  CE2 . TRP A  1 221 ? 61.538  2.091   49.927  1.00 7.67  ? 221  TRP A CE2 1 
ATOM   1666  C  CE3 . TRP A  1 221 ? 59.150  1.839   49.580  1.00 7.68  ? 221  TRP A CE3 1 
ATOM   1667  C  CZ2 . TRP A  1 221 ? 61.838  1.316   48.784  1.00 8.24  ? 221  TRP A CZ2 1 
ATOM   1668  C  CZ3 . TRP A  1 221 ? 59.442  1.064   48.442  1.00 8.50  ? 221  TRP A CZ3 1 
ATOM   1669  C  CH2 . TRP A  1 221 ? 60.781  0.801   48.069  1.00 11.01 ? 221  TRP A CH2 1 
ATOM   1670  N  N   . GLY A  1 222 ? 56.753  6.028   53.247  1.00 8.79  ? 222  GLY A N   1 
ATOM   1671  C  CA  . GLY A  1 222 ? 55.484  6.155   53.955  1.00 9.81  ? 222  GLY A CA  1 
ATOM   1672  C  C   . GLY A  1 222 ? 54.446  6.825   53.051  1.00 9.34  ? 222  GLY A C   1 
ATOM   1673  O  O   . GLY A  1 222 ? 54.775  7.166   51.928  1.00 9.74  ? 222  GLY A O   1 
ATOM   1674  N  N   . PRO A  1 223 ? 53.208  7.020   53.510  1.00 9.38  ? 223  PRO A N   1 
ATOM   1675  C  CA  . PRO A  1 223 ? 52.193  7.656   52.655  1.00 9.76  ? 223  PRO A CA  1 
ATOM   1676  C  C   . PRO A  1 223 ? 52.578  9.124   52.439  1.00 9.91  ? 223  PRO A C   1 
ATOM   1677  O  O   . PRO A  1 223 ? 53.224  9.695   53.310  1.00 9.97  ? 223  PRO A O   1 
ATOM   1678  C  CB  . PRO A  1 223 ? 50.908  7.596   53.490  1.00 10.22 ? 223  PRO A CB  1 
ATOM   1679  C  CG  . PRO A  1 223 ? 51.343  7.358   54.901  1.00 11.34 ? 223  PRO A CG  1 
ATOM   1680  C  CD  . PRO A  1 223 ? 52.695  6.673   54.854  1.00 10.92 ? 223  PRO A CD  1 
ATOM   1681  N  N   . LYS A  1 224 ? 52.143  9.696   51.326  1.00 9.65  ? 224  LYS A N   1 
ATOM   1682  C  CA  . LYS A  1 224 ? 52.486  11.053  50.950  1.00 8.46  ? 224  LYS A CA  1 
ATOM   1683  C  C   . LYS A  1 224 ? 51.238  11.669  50.343  1.00 8.31  ? 224  LYS A C   1 
ATOM   1684  O  O   . LYS A  1 224 ? 50.365  10.963  49.786  1.00 6.85  ? 224  LYS A O   1 
ATOM   1685  C  CB  . LYS A  1 224 ? 53.611  11.054  49.899  1.00 7.72  ? 224  LYS A CB  1 
ATOM   1686  C  CG  . LYS A  1 224 ? 54.992  10.563  50.437  1.00 9.17  ? 224  LYS A CG  1 
ATOM   1687  C  CD  . LYS A  1 224 ? 56.034  10.270  49.287  1.00 8.53  ? 224  LYS A CD  1 
ATOM   1688  C  CE  . LYS A  1 224 ? 55.763  8.927   48.615  1.00 10.92 ? 224  LYS A CE  1 
ATOM   1689  N  NZ  . LYS A  1 224 ? 56.064  7.750   49.576  1.00 8.71  ? 224  LYS A NZ  1 
ATOM   1690  N  N   . TYR A  1 225 ? 51.192  12.991  50.426  1.00 6.86  ? 225  TYR A N   1 
ATOM   1691  C  CA  . TYR A  1 225 ? 50.117  13.813  49.897  1.00 6.83  ? 225  TYR A CA  1 
ATOM   1692  C  C   . TYR A  1 225 ? 50.762  14.981  49.153  1.00 7.31  ? 225  TYR A C   1 
ATOM   1693  O  O   . TYR A  1 225 ? 51.689  15.596  49.688  1.00 8.86  ? 225  TYR A O   1 
ATOM   1694  C  CB  . TYR A  1 225 ? 49.205  14.335  51.067  1.00 7.18  ? 225  TYR A CB  1 
ATOM   1695  C  CG  . TYR A  1 225 ? 48.646  13.158  51.844  1.00 11.08 ? 225  TYR A CG  1 
ATOM   1696  C  CD1 . TYR A  1 225 ? 49.446  12.489  52.787  1.00 12.00 ? 225  TYR A CD1 1 
ATOM   1697  C  CD2 . TYR A  1 225 ? 47.332  12.644  51.580  1.00 14.43 ? 225  TYR A CD2 1 
ATOM   1698  C  CE1 . TYR A  1 225 ? 48.976  11.366  53.483  1.00 15.07 ? 225  TYR A CE1 1 
ATOM   1699  C  CE2 . TYR A  1 225 ? 46.836  11.479  52.295  1.00 16.24 ? 225  TYR A CE2 1 
ATOM   1700  C  CZ  . TYR A  1 225 ? 47.692  10.861  53.240  1.00 18.68 ? 225  TYR A CZ  1 
ATOM   1701  O  OH  . TYR A  1 225 ? 47.351  9.709   53.970  1.00 22.57 ? 225  TYR A OH  1 
ATOM   1702  N  N   . LEU A  1 226 ? 50.283  15.274  47.948  1.00 6.78  ? 226  LEU A N   1 
ATOM   1703  C  CA  . LEU A  1 226 ? 50.689  16.452  47.167  1.00 7.77  ? 226  LEU A CA  1 
ATOM   1704  C  C   . LEU A  1 226 ? 49.728  17.593  47.389  1.00 6.67  ? 226  LEU A C   1 
ATOM   1705  O  O   . LEU A  1 226 ? 48.537  17.456  47.164  1.00 6.45  ? 226  LEU A O   1 
ATOM   1706  C  CB  . LEU A  1 226 ? 50.687  16.168  45.671  1.00 5.77  ? 226  LEU A CB  1 
ATOM   1707  C  CG  . LEU A  1 226 ? 51.253  17.243  44.709  1.00 7.27  ? 226  LEU A CG  1 
ATOM   1708  C  CD1 . LEU A  1 226 ? 52.775  17.521  44.986  1.00 3.13  ? 226  LEU A CD1 1 
ATOM   1709  C  CD2 . LEU A  1 226 ? 51.009  16.799  43.233  1.00 5.83  ? 226  LEU A CD2 1 
ATOM   1710  N  N   . ASN A  1 227 ? 50.256  18.715  47.837  1.00 7.31  ? 227  ASN A N   1 
ATOM   1711  C  CA  . ASN A  1 227 ? 49.426  19.917  47.840  1.00 7.20  ? 227  ASN A CA  1 
ATOM   1712  C  C   . ASN A  1 227 ? 49.896  20.855  46.721  1.00 6.30  ? 227  ASN A C   1 
ATOM   1713  O  O   . ASN A  1 227 ? 51.097  21.143  46.638  1.00 7.73  ? 227  ASN A O   1 
ATOM   1714  C  CB  . ASN A  1 227 ? 49.501  20.593  49.224  1.00 6.25  ? 227  ASN A CB  1 
ATOM   1715  C  CG  . ASN A  1 227 ? 48.610  21.778  49.299  1.00 10.24 ? 227  ASN A CG  1 
ATOM   1716  O  OD1 . ASN A  1 227 ? 48.902  22.831  48.688  1.00 6.63  ? 227  ASN A OD1 1 
ATOM   1717  N  ND2 . ASN A  1 227 ? 47.456  21.623  49.988  1.00 11.15 ? 227  ASN A ND2 1 
ATOM   1718  N  N   . SER A  1 228 ? 48.973  21.378  45.922  1.00 6.06  ? 228  SER A N   1 
ATOM   1719  C  CA  . SER A  1 228 ? 49.293  22.167  44.722  1.00 6.74  ? 228  SER A CA  1 
ATOM   1720  C  C   . SER A  1 228 ? 48.869  23.641  44.851  1.00 6.99  ? 228  SER A C   1 
ATOM   1721  O  O   . SER A  1 228 ? 48.887  24.384  43.890  1.00 5.69  ? 228  SER A O   1 
ATOM   1722  C  CB  . SER A  1 228 ? 48.661  21.516  43.469  1.00 6.43  ? 228  SER A CB  1 
ATOM   1723  O  OG  . SER A  1 228 ? 49.178  20.175  43.348  1.00 10.76 ? 228  SER A OG  1 
ATOM   1724  N  N   . GLN A  1 229 ? 48.510  24.048  46.050  1.00 7.79  ? 229  GLN A N   1 
ATOM   1725  C  CA  . GLN A  1 229 ? 47.874  25.363  46.242  1.00 9.45  ? 229  GLN A CA  1 
ATOM   1726  C  C   . GLN A  1 229 ? 48.885  26.522  46.223  1.00 9.40  ? 229  GLN A C   1 
ATOM   1727  O  O   . GLN A  1 229 ? 48.543  27.656  45.819  1.00 8.78  ? 229  GLN A O   1 
ATOM   1728  C  CB  . GLN A  1 229 ? 47.054  25.368  47.555  1.00 9.90  ? 229  GLN A CB  1 
ATOM   1729  C  CG  . GLN A  1 229 ? 46.040  26.593  47.712  1.00 17.96 ? 229  GLN A CG  1 
ATOM   1730  C  CD  . GLN A  1 229 ? 44.984  26.768  46.584  1.00 27.65 ? 229  GLN A CD  1 
ATOM   1731  O  OE1 . GLN A  1 229 ? 43.900  26.142  46.613  1.00 28.75 ? 229  GLN A OE1 1 
ATOM   1732  N  NE2 . GLN A  1 229 ? 45.271  27.679  45.628  1.00 29.91 ? 229  GLN A NE2 1 
ATOM   1733  N  N   . TYR A  1 230 ? 50.117  26.251  46.673  1.00 8.35  ? 230  TYR A N   1 
ATOM   1734  C  CA  . TYR A  1 230 ? 51.111  27.316  46.837  1.00 9.11  ? 230  TYR A CA  1 
ATOM   1735  C  C   . TYR A  1 230 ? 52.430  26.859  46.220  1.00 9.79  ? 230  TYR A C   1 
ATOM   1736  O  O   . TYR A  1 230 ? 53.469  26.840  46.887  1.00 12.30 ? 230  TYR A O   1 
ATOM   1737  C  CB  . TYR A  1 230 ? 51.261  27.652  48.353  1.00 9.06  ? 230  TYR A CB  1 
ATOM   1738  C  CG  . TYR A  1 230 ? 49.966  27.615  49.154  1.00 7.23  ? 230  TYR A CG  1 
ATOM   1739  C  CD1 . TYR A  1 230 ? 49.029  28.659  49.065  1.00 9.73  ? 230  TYR A CD1 1 
ATOM   1740  C  CD2 . TYR A  1 230 ? 49.675  26.529  50.002  1.00 9.96  ? 230  TYR A CD2 1 
ATOM   1741  C  CE1 . TYR A  1 230 ? 47.802  28.631  49.792  1.00 7.61  ? 230  TYR A CE1 1 
ATOM   1742  C  CE2 . TYR A  1 230 ? 48.461  26.483  50.777  1.00 7.99  ? 230  TYR A CE2 1 
ATOM   1743  C  CZ  . TYR A  1 230 ? 47.545  27.550  50.658  1.00 9.95  ? 230  TYR A CZ  1 
ATOM   1744  O  OH  . TYR A  1 230 ? 46.385  27.473  51.389  1.00 11.48 ? 230  TYR A OH  1 
ATOM   1745  N  N   . GLY A  1 231 ? 52.406  26.453  44.954  1.00 9.49  ? 231  GLY A N   1 
ATOM   1746  C  CA  . GLY A  1 231 ? 53.537  25.705  44.393  1.00 8.79  ? 231  GLY A CA  1 
ATOM   1747  C  C   . GLY A  1 231 ? 53.302  24.278  44.808  1.00 7.98  ? 231  GLY A C   1 
ATOM   1748  O  O   . GLY A  1 231 ? 52.186  23.962  45.233  1.00 7.96  ? 231  GLY A O   1 
ATOM   1749  N  N   . TYR A  1 232 ? 54.314  23.403  44.735  1.00 7.64  ? 232  TYR A N   1 
ATOM   1750  C  CA  . TYR A  1 232 ? 54.051  22.015  45.111  1.00 6.53  ? 232  TYR A CA  1 
ATOM   1751  C  C   . TYR A  1 232 ? 54.658  21.719  46.435  1.00 6.99  ? 232  TYR A C   1 
ATOM   1752  O  O   . TYR A  1 232 ? 55.819  22.086  46.700  1.00 4.98  ? 232  TYR A O   1 
ATOM   1753  C  CB  . TYR A  1 232 ? 54.628  21.034  44.081  1.00 5.83  ? 232  TYR A CB  1 
ATOM   1754  C  CG  . TYR A  1 232 ? 53.869  20.960  42.776  1.00 6.45  ? 232  TYR A CG  1 
ATOM   1755  C  CD1 . TYR A  1 232 ? 52.520  20.551  42.734  1.00 5.34  ? 232  TYR A CD1 1 
ATOM   1756  C  CD2 . TYR A  1 232 ? 54.514  21.285  41.554  1.00 4.77  ? 232  TYR A CD2 1 
ATOM   1757  C  CE1 . TYR A  1 232 ? 51.844  20.477  41.508  1.00 6.33  ? 232  TYR A CE1 1 
ATOM   1758  C  CE2 . TYR A  1 232 ? 53.849  21.215  40.333  1.00 7.01  ? 232  TYR A CE2 1 
ATOM   1759  C  CZ  . TYR A  1 232 ? 52.529  20.797  40.310  1.00 8.21  ? 232  TYR A CZ  1 
ATOM   1760  O  OH  . TYR A  1 232 ? 51.879  20.764  39.107  1.00 7.15  ? 232  TYR A OH  1 
ATOM   1761  N  N   . GLN A  1 233 ? 53.894  21.025  47.269  1.00 5.98  ? 233  GLN A N   1 
ATOM   1762  C  CA  . GLN A  1 233 ? 54.422  20.586  48.561  1.00 7.71  ? 233  GLN A CA  1 
ATOM   1763  C  C   . GLN A  1 233 ? 53.974  19.168  48.809  1.00 7.40  ? 233  GLN A C   1 
ATOM   1764  O  O   . GLN A  1 233 ? 52.842  18.836  48.556  1.00 8.12  ? 233  GLN A O   1 
ATOM   1765  C  CB  . GLN A  1 233 ? 53.958  21.494  49.700  1.00 6.98  ? 233  GLN A CB  1 
ATOM   1766  C  CG  . GLN A  1 233 ? 54.520  22.919  49.537  1.00 8.18  ? 233  GLN A CG  1 
ATOM   1767  C  CD  . GLN A  1 233 ? 54.102  23.824  50.671  1.00 10.39 ? 233  GLN A CD  1 
ATOM   1768  O  OE1 . GLN A  1 233 ? 54.702  23.778  51.725  1.00 7.03  ? 233  GLN A OE1 1 
ATOM   1769  N  NE2 . GLN A  1 233 ? 53.078  24.655  50.448  1.00 4.88  ? 233  GLN A NE2 1 
ATOM   1770  N  N   . ILE A  1 234 ? 54.889  18.335  49.263  1.00 7.70  ? 234  ILE A N   1 
ATOM   1771  C  CA  . ILE A  1 234 ? 54.575  16.942  49.534  1.00 8.18  ? 234  ILE A CA  1 
ATOM   1772  C  C   . ILE A  1 234 ? 54.734  16.692  51.018  1.00 8.27  ? 234  ILE A C   1 
ATOM   1773  O  O   . ILE A  1 234 ? 55.852  16.835  51.569  1.00 7.88  ? 234  ILE A O   1 
ATOM   1774  C  CB  . ILE A  1 234 ? 55.537  16.010  48.753  1.00 8.06  ? 234  ILE A CB  1 
ATOM   1775  C  CG1 . ILE A  1 234 ? 55.350  16.187  47.238  1.00 7.90  ? 234  ILE A CG1 1 
ATOM   1776  C  CG2 . ILE A  1 234 ? 55.303  14.518  49.148  1.00 8.35  ? 234  ILE A CG2 1 
ATOM   1777  C  CD1 . ILE A  1 234 ? 56.545  15.475  46.410  1.00 7.94  ? 234  ILE A CD1 1 
ATOM   1778  N  N   . VAL A  1 235 ? 53.634  16.336  51.663  1.00 6.69  ? 235  VAL A N   1 
ATOM   1779  C  CA  . VAL A  1 235 ? 53.674  16.056  53.087  1.00 7.66  ? 235  VAL A CA  1 
ATOM   1780  C  C   . VAL A  1 235 ? 53.839  14.546  53.274  1.00 7.13  ? 235  VAL A C   1 
ATOM   1781  O  O   . VAL A  1 235 ? 53.123  13.768  52.666  1.00 7.36  ? 235  VAL A O   1 
ATOM   1782  C  CB  . VAL A  1 235 ? 52.391  16.507  53.838  1.00 8.65  ? 235  VAL A CB  1 
ATOM   1783  C  CG1 . VAL A  1 235 ? 52.510  16.169  55.411  1.00 2.95  ? 235  VAL A CG1 1 
ATOM   1784  C  CG2 . VAL A  1 235 ? 52.091  17.984  53.609  1.00 8.54  ? 235  VAL A CG2 1 
ATOM   1785  N  N   . ALA A  1 236 ? 54.804  14.132  54.077  1.00 8.32  ? 236  ALA A N   1 
ATOM   1786  C  CA  . ALA A  1 236 ? 54.918  12.704  54.426  1.00 6.74  ? 236  ALA A CA  1 
ATOM   1787  C  C   . ALA A  1 236 ? 54.563  12.594  55.900  1.00 7.58  ? 236  ALA A C   1 
ATOM   1788  O  O   . ALA A  1 236 ? 55.384  12.913  56.740  1.00 7.91  ? 236  ALA A O   1 
ATOM   1789  C  CB  . ALA A  1 236 ? 56.349  12.212  54.150  1.00 6.85  ? 236  ALA A CB  1 
ATOM   1790  N  N   . PRO A  1 237 ? 53.328  12.240  56.260  1.00 8.22  ? 237  PRO A N   1 
ATOM   1791  C  CA  . PRO A  1 237 ? 52.975  12.183  57.697  1.00 8.97  ? 237  PRO A CA  1 
ATOM   1792  C  C   . PRO A  1 237 ? 53.757  11.159  58.495  1.00 9.37  ? 237  PRO A C   1 
ATOM   1793  O  O   . PRO A  1 237 ? 53.942  10.039  58.001  1.00 8.72  ? 237  PRO A O   1 
ATOM   1794  C  CB  . PRO A  1 237 ? 51.484  11.777  57.664  1.00 8.52  ? 237  PRO A CB  1 
ATOM   1795  C  CG  . PRO A  1 237 ? 51.000  12.425  56.372  1.00 9.78  ? 237  PRO A CG  1 
ATOM   1796  C  CD  . PRO A  1 237 ? 52.144  12.052  55.387  1.00 7.51  ? 237  PRO A CD  1 
ATOM   1797  N  N   . PHE A  1 238 ? 54.197  11.532  59.698  1.00 9.02  ? 238  PHE A N   1 
ATOM   1798  C  CA  . PHE A  1 238 ? 54.769  10.574  60.614  1.00 9.16  ? 238  PHE A CA  1 
ATOM   1799  C  C   . PHE A  1 238 ? 53.844  10.320  61.815  1.00 9.01  ? 238  PHE A C   1 
ATOM   1800  O  O   . PHE A  1 238 ? 53.711  9.167   62.264  1.00 9.08  ? 238  PHE A O   1 
ATOM   1801  C  CB  . PHE A  1 238 ? 56.121  11.048  61.131  1.00 8.58  ? 238  PHE A CB  1 
ATOM   1802  C  CG  . PHE A  1 238 ? 57.219  11.060  60.123  1.00 7.94  ? 238  PHE A CG  1 
ATOM   1803  C  CD1 . PHE A  1 238 ? 57.161  10.333  58.950  1.00 9.54  ? 238  PHE A CD1 1 
ATOM   1804  C  CD2 . PHE A  1 238 ? 58.318  11.884  60.351  1.00 10.88 ? 238  PHE A CD2 1 
ATOM   1805  C  CE1 . PHE A  1 238 ? 58.214  10.335  58.059  1.00 8.98  ? 238  PHE A CE1 1 
ATOM   1806  C  CE2 . PHE A  1 238 ? 59.403  11.904  59.461  1.00 12.02 ? 238  PHE A CE2 1 
ATOM   1807  C  CZ  . PHE A  1 238 ? 59.348  11.122  58.301  1.00 8.28  ? 238  PHE A CZ  1 
ATOM   1808  N  N   . VAL A  1 239 ? 53.211  11.381  62.311  1.00 7.69  ? 239  VAL A N   1 
ATOM   1809  C  CA  . VAL A  1 239 ? 52.237  11.295  63.392  1.00 7.49  ? 239  VAL A CA  1 
ATOM   1810  C  C   . VAL A  1 239 ? 51.017  12.108  62.998  1.00 8.34  ? 239  VAL A C   1 
ATOM   1811  O  O   . VAL A  1 239 ? 51.146  13.287  62.583  1.00 9.71  ? 239  VAL A O   1 
ATOM   1812  C  CB  . VAL A  1 239 ? 52.840  11.811  64.758  1.00 7.10  ? 239  VAL A CB  1 
ATOM   1813  C  CG1 . VAL A  1 239 ? 51.753  11.819  65.841  1.00 8.58  ? 239  VAL A CG1 1 
ATOM   1814  C  CG2 . VAL A  1 239 ? 54.050  10.912  65.173  1.00 7.79  ? 239  VAL A CG2 1 
ATOM   1815  N  N   . THR A  1 240 ? 49.848  11.479  63.103  1.00 8.49  ? 240  THR A N   1 
ATOM   1816  C  CA  . THR A  1 240 ? 48.567  12.161  62.882  1.00 8.46  ? 240  THR A CA  1 
ATOM   1817  C  C   . THR A  1 240 ? 47.766  12.020  64.141  1.00 8.15  ? 240  THR A C   1 
ATOM   1818  O  O   . THR A  1 240 ? 48.223  11.386  65.121  1.00 9.33  ? 240  THR A O   1 
ATOM   1819  C  CB  . THR A  1 240 ? 47.725  11.479  61.721  1.00 8.79  ? 240  THR A CB  1 
ATOM   1820  O  OG1 . THR A  1 240 ? 47.267  10.158  62.140  1.00 7.42  ? 240  THR A OG1 1 
ATOM   1821  C  CG2 . THR A  1 240 ? 48.548  11.307  60.435  1.00 7.34  ? 240  THR A CG2 1 
ATOM   1822  N  N   . ALA A  1 241 ? 46.538  12.524  64.091  1.00 8.71  ? 241  ALA A N   1 
ATOM   1823  C  CA  . ALA A  1 241 ? 45.624  12.504  65.230  1.00 8.49  ? 241  ALA A CA  1 
ATOM   1824  C  C   . ALA A  1 241 ? 45.413  11.072  65.736  1.00 8.60  ? 241  ALA A C   1 
ATOM   1825  O  O   . ALA A  1 241 ? 45.231  10.842  66.923  1.00 9.38  ? 241  ALA A O   1 
ATOM   1826  C  CB  . ALA A  1 241 ? 44.300  13.132  64.846  1.00 10.33 ? 241  ALA A CB  1 
ATOM   1827  N  N   . THR A  1 242 ? 45.418  10.135  64.820  1.00 8.29  ? 242  THR A N   1 
ATOM   1828  C  CA  . THR A  1 242 ? 45.184  8.732   65.122  1.00 9.90  ? 242  THR A CA  1 
ATOM   1829  C  C   . THR A  1 242 ? 46.206  8.241   66.155  1.00 8.99  ? 242  THR A C   1 
ATOM   1830  O  O   . THR A  1 242 ? 45.821  7.617   67.161  1.00 9.47  ? 242  THR A O   1 
ATOM   1831  C  CB  . THR A  1 242 ? 45.267  7.906   63.845  1.00 8.76  ? 242  THR A CB  1 
ATOM   1832  O  OG1 . THR A  1 242 ? 44.144  8.221   63.011  1.00 11.99 ? 242  THR A OG1 1 
ATOM   1833  C  CG2 . THR A  1 242 ? 45.099  6.416   64.128  1.00 10.10 ? 242  THR A CG2 1 
ATOM   1834  N  N   . GLN A  1 243 ? 47.470  8.575   65.921  1.00 8.26  ? 243  GLN A N   1 
ATOM   1835  C  CA  . GLN A  1 243 ? 48.573  8.114   66.775  1.00 8.70  ? 243  GLN A CA  1 
ATOM   1836  C  C   . GLN A  1 243 ? 48.800  9.036   67.979  1.00 9.76  ? 243  GLN A C   1 
ATOM   1837  O  O   . GLN A  1 243 ? 49.129  8.550   69.089  1.00 8.80  ? 243  GLN A O   1 
ATOM   1838  C  CB  . GLN A  1 243 ? 49.882  7.942   65.958  1.00 8.20  ? 243  GLN A CB  1 
ATOM   1839  C  CG  . GLN A  1 243 ? 49.794  6.920   64.815  1.00 6.28  ? 243  GLN A CG  1 
ATOM   1840  C  CD  . GLN A  1 243 ? 49.134  7.492   63.594  1.00 8.84  ? 243  GLN A CD  1 
ATOM   1841  O  OE1 . GLN A  1 243 ? 49.152  8.704   63.389  1.00 7.08  ? 243  GLN A OE1 1 
ATOM   1842  N  NE2 . GLN A  1 243 ? 48.556  6.625   62.768  1.00 6.38  ? 243  GLN A NE2 1 
ATOM   1843  N  N   . ALA A  1 244 ? 48.654  10.356  67.755  1.00 8.88  ? 244  ALA A N   1 
ATOM   1844  C  CA  . ALA A  1 244 ? 48.808  11.345  68.821  1.00 9.23  ? 244  ALA A CA  1 
ATOM   1845  C  C   . ALA A  1 244 ? 47.707  11.272  69.905  1.00 9.94  ? 244  ALA A C   1 
ATOM   1846  O  O   . ALA A  1 244 ? 48.016  11.328  71.085  1.00 10.16 ? 244  ALA A O   1 
ATOM   1847  C  CB  . ALA A  1 244 ? 48.922  12.772  68.258  1.00 7.19  ? 244  ALA A CB  1 
ATOM   1848  N  N   . GLN A  1 245 ? 46.441  11.146  69.505  1.00 9.75  ? 245  GLN A N   1 
ATOM   1849  C  CA  . GLN A  1 245 ? 45.326  11.280  70.456  1.00 11.52 ? 245  GLN A CA  1 
ATOM   1850  C  C   . GLN A  1 245 ? 45.489  12.484  71.378  1.00 10.93 ? 245  GLN A C   1 
ATOM   1851  O  O   . GLN A  1 245 ? 45.724  13.571  70.898  1.00 9.82  ? 245  GLN A O   1 
ATOM   1852  C  CB  . GLN A  1 245 ? 45.062  9.987   71.243  1.00 11.57 ? 245  GLN A CB  1 
ATOM   1853  C  CG  . GLN A  1 245 ? 44.576  8.843   70.371  1.00 16.17 ? 245  GLN A CG  1 
ATOM   1854  C  CD  . GLN A  1 245 ? 43.185  9.064   69.772  1.00 23.35 ? 245  GLN A CD  1 
ATOM   1855  O  OE1 . GLN A  1 245 ? 42.150  8.617   70.342  1.00 25.82 ? 245  GLN A OE1 1 
ATOM   1856  N  NE2 . GLN A  1 245 ? 43.142  9.730   68.602  1.00 23.53 ? 245  GLN A NE2 1 
ATOM   1857  N  N   . ASP A  1 246 ? 45.434  12.275  72.695  1.00 11.12 ? 246  ASP A N   1 
ATOM   1858  C  CA  . ASP A  1 246 ? 45.455  13.375  73.619  1.00 11.18 ? 246  ASP A CA  1 
ATOM   1859  C  C   . ASP A  1 246 ? 46.779  14.090  73.717  1.00 11.15 ? 246  ASP A C   1 
ATOM   1860  O  O   . ASP A  1 246 ? 46.785  15.209  74.216  1.00 10.41 ? 246  ASP A O   1 
ATOM   1861  C  CB  . ASP A  1 246 ? 44.955  12.918  74.998  1.00 12.00 ? 246  ASP A CB  1 
ATOM   1862  C  CG  . ASP A  1 246 ? 45.921  11.941  75.637  1.00 15.14 ? 246  ASP A CG  1 
ATOM   1863  O  OD1 . ASP A  1 246 ? 46.055  10.876  75.030  1.00 13.72 ? 246  ASP A OD1 1 
ATOM   1864  O  OD2 . ASP A  1 246 ? 46.634  12.180  76.648  1.00 18.32 ? 246  ASP A OD2 1 
ATOM   1865  N  N   . THR A  1 247 ? 47.902  13.514  73.201  1.00 10.00 ? 247  THR A N   1 
ATOM   1866  C  CA  . THR A  1 247 ? 49.146  14.288  73.075  1.00 10.26 ? 247  THR A CA  1 
ATOM   1867  C  C   . THR A  1 247 ? 49.053  15.422  72.042  1.00 10.28 ? 247  THR A C   1 
ATOM   1868  O  O   . THR A  1 247 ? 49.832  16.370  72.107  1.00 10.80 ? 247  THR A O   1 
ATOM   1869  C  CB  . THR A  1 247 ? 50.400  13.399  72.842  1.00 11.28 ? 247  THR A CB  1 
ATOM   1870  O  OG1 . THR A  1 247 ? 50.329  12.782  71.538  1.00 9.86  ? 247  THR A OG1 1 
ATOM   1871  C  CG2 . THR A  1 247 ? 50.405  12.229  73.856  1.00 10.46 ? 247  THR A CG2 1 
ATOM   1872  N  N   . ASN A  1 248 ? 48.098  15.330  71.102  1.00 10.73 ? 248  ASN A N   1 
ATOM   1873  C  CA  . ASN A  1 248 ? 47.582  16.506  70.416  1.00 10.70 ? 248  ASN A CA  1 
ATOM   1874  C  C   . ASN A  1 248 ? 48.676  17.264  69.655  1.00 9.58  ? 248  ASN A C   1 
ATOM   1875  O  O   . ASN A  1 248 ? 49.040  18.420  69.998  1.00 10.27 ? 248  ASN A O   1 
ATOM   1876  C  CB  . ASN A  1 248 ? 46.949  17.420  71.459  1.00 10.81 ? 248  ASN A CB  1 
ATOM   1877  C  CG  . ASN A  1 248 ? 46.238  18.619  70.851  1.00 14.42 ? 248  ASN A CG  1 
ATOM   1878  O  OD1 . ASN A  1 248 ? 45.756  18.558  69.722  1.00 12.68 ? 248  ASN A OD1 1 
ATOM   1879  N  ND2 . ASN A  1 248 ? 46.144  19.711  71.653  1.00 12.98 ? 248  ASN A ND2 1 
ATOM   1880  N  N   . TYR A  1 249 ? 49.221  16.597  68.649  1.00 9.05  ? 249  TYR A N   1 
ATOM   1881  C  CA  . TYR A  1 249 ? 50.260  17.164  67.829  1.00 8.02  ? 249  TYR A CA  1 
ATOM   1882  C  C   . TYR A  1 249 ? 50.309  16.415  66.517  1.00 9.10  ? 249  TYR A C   1 
ATOM   1883  O  O   . TYR A  1 249 ? 49.693  15.336  66.380  1.00 7.85  ? 249  TYR A O   1 
ATOM   1884  C  CB  . TYR A  1 249 ? 51.615  17.067  68.540  1.00 6.91  ? 249  TYR A CB  1 
ATOM   1885  C  CG  . TYR A  1 249 ? 52.313  15.709  68.564  1.00 7.96  ? 249  TYR A CG  1 
ATOM   1886  C  CD1 . TYR A  1 249 ? 51.935  14.726  69.470  1.00 9.68  ? 249  TYR A CD1 1 
ATOM   1887  C  CD2 . TYR A  1 249 ? 53.390  15.444  67.707  1.00 8.98  ? 249  TYR A CD2 1 
ATOM   1888  C  CE1 . TYR A  1 249 ? 52.599  13.478  69.499  1.00 8.33  ? 249  TYR A CE1 1 
ATOM   1889  C  CE2 . TYR A  1 249 ? 54.056  14.222  67.716  1.00 10.37 ? 249  TYR A CE2 1 
ATOM   1890  C  CZ  . TYR A  1 249 ? 53.658  13.245  68.612  1.00 7.24  ? 249  TYR A CZ  1 
ATOM   1891  O  OH  . TYR A  1 249 ? 54.356  12.085  68.678  1.00 9.02  ? 249  TYR A OH  1 
ATOM   1892  N  N   . THR A  1 250 ? 51.090  16.949  65.571  1.00 8.90  ? 250  THR A N   1 
ATOM   1893  C  CA  . THR A  1 250 ? 51.372  16.210  64.348  1.00 8.78  ? 250  THR A CA  1 
ATOM   1894  C  C   . THR A  1 250 ? 52.843  16.381  64.073  1.00 9.10  ? 250  THR A C   1 
ATOM   1895  O  O   . THR A  1 250 ? 53.494  17.343  64.553  1.00 8.48  ? 250  THR A O   1 
ATOM   1896  C  CB  . THR A  1 250 ? 50.607  16.760  63.130  1.00 10.00 ? 250  THR A CB  1 
ATOM   1897  O  OG1 . THR A  1 250 ? 50.803  18.188  63.062  1.00 9.16  ? 250  THR A OG1 1 
ATOM   1898  C  CG2 . THR A  1 250 ? 49.037  16.533  63.264  1.00 8.32  ? 250  THR A CG2 1 
ATOM   1899  N  N   . LEU A  1 251 ? 53.334  15.478  63.240  1.00 8.82  ? 251  LEU A N   1 
ATOM   1900  C  CA  . LEU A  1 251 ? 54.750  15.395  62.903  1.00 9.46  ? 251  LEU A CA  1 
ATOM   1901  C  C   . LEU A  1 251 ? 54.808  14.852  61.457  1.00 8.70  ? 251  LEU A C   1 
ATOM   1902  O  O   . LEU A  1 251 ? 54.073  13.905  61.111  1.00 8.17  ? 251  LEU A O   1 
ATOM   1903  C  CB  . LEU A  1 251 ? 55.501  14.406  63.861  1.00 8.37  ? 251  LEU A CB  1 
ATOM   1904  C  CG  . LEU A  1 251 ? 57.009  14.345  63.634  1.00 9.13  ? 251  LEU A CG  1 
ATOM   1905  C  CD1 . LEU A  1 251 ? 57.719  15.652  64.026  1.00 8.92  ? 251  LEU A CD1 1 
ATOM   1906  C  CD2 . LEU A  1 251 ? 57.648  13.215  64.422  1.00 12.19 ? 251  LEU A CD2 1 
ATOM   1907  N  N   . SER A  1 252 ? 55.663  15.443  60.611  1.00 7.70  ? 252  SER A N   1 
ATOM   1908  C  CA  . SER A  1 252 ? 55.779  14.922  59.243  1.00 8.40  ? 252  SER A CA  1 
ATOM   1909  C  C   . SER A  1 252 ? 57.073  15.483  58.647  1.00 8.56  ? 252  SER A C   1 
ATOM   1910  O  O   . SER A  1 252 ? 57.761  16.318  59.286  1.00 8.70  ? 252  SER A O   1 
ATOM   1911  C  CB  . SER A  1 252 ? 54.590  15.436  58.445  1.00 7.61  ? 252  SER A CB  1 
ATOM   1912  O  OG  . SER A  1 252 ? 54.647  16.857  58.447  1.00 11.55 ? 252  SER A OG  1 
ATOM   1913  N  N   . THR A  1 253 ? 57.387  15.081  57.410  1.00 7.82  ? 253  THR A N   1 
ATOM   1914  C  CA  . THR A  1 253 ? 58.220  15.981  56.631  1.00 7.57  ? 253  THR A CA  1 
ATOM   1915  C  C   . THR A  1 253 ? 57.383  16.725  55.601  1.00 7.31  ? 253  THR A C   1 
ATOM   1916  O  O   . THR A  1 253 ? 56.329  16.235  55.165  1.00 7.62  ? 253  THR A O   1 
ATOM   1917  C  CB  . THR A  1 253 ? 59.380  15.271  55.904  1.00 7.52  ? 253  THR A CB  1 
ATOM   1918  O  OG1 . THR A  1 253 ? 58.872  14.261  55.045  1.00 8.27  ? 253  THR A OG1 1 
ATOM   1919  C  CG2 . THR A  1 253 ? 60.255  14.556  56.902  1.00 3.42  ? 253  THR A CG2 1 
ATOM   1920  N  N   . ILE A  1 254 ? 57.818  17.948  55.269  1.00 7.07  ? 254  ILE A N   1 
ATOM   1921  C  CA  . ILE A  1 254 ? 57.243  18.673  54.149  1.00 5.07  ? 254  ILE A CA  1 
ATOM   1922  C  C   . ILE A  1 254 ? 58.369  18.923  53.125  1.00 6.34  ? 254  ILE A C   1 
ATOM   1923  O  O   . ILE A  1 254 ? 59.415  19.473  53.461  1.00 5.47  ? 254  ILE A O   1 
ATOM   1924  C  CB  . ILE A  1 254 ? 56.666  20.023  54.642  1.00 6.05  ? 254  ILE A CB  1 
ATOM   1925  C  CG1 . ILE A  1 254 ? 55.652  19.774  55.788  1.00 5.34  ? 254  ILE A CG1 1 
ATOM   1926  C  CG2 . ILE A  1 254 ? 55.969  20.782  53.490  1.00 3.99  ? 254  ILE A CG2 1 
ATOM   1927  C  CD1 . ILE A  1 254 ? 55.053  21.007  56.368  1.00 4.98  ? 254  ILE A CD1 1 
ATOM   1928  N  N   . SER A  1 255 ? 58.139  18.527  51.878  1.00 6.31  ? 255  SER A N   1 
ATOM   1929  C  CA  . SER A  1 255 ? 59.072  18.779  50.779  1.00 6.27  ? 255  SER A CA  1 
ATOM   1930  C  C   . SER A  1 255 ? 58.447  19.873  49.941  1.00 6.66  ? 255  SER A C   1 
ATOM   1931  O  O   . SER A  1 255 ? 57.216  19.970  49.843  1.00 7.80  ? 255  SER A O   1 
ATOM   1932  C  CB  . SER A  1 255 ? 59.272  17.563  49.906  1.00 6.63  ? 255  SER A CB  1 
ATOM   1933  O  OG  . SER A  1 255 ? 59.769  16.491  50.702  1.00 6.08  ? 255  SER A OG  1 
ATOM   1934  N  N   . MET A  1 256 ? 59.269  20.720  49.357  1.00 5.81  ? 256  MET A N   1 
ATOM   1935  C  CA  . MET A  1 256 ? 58.717  21.923  48.728  1.00 6.86  ? 256  MET A CA  1 
ATOM   1936  C  C   . MET A  1 256 ? 59.442  22.199  47.460  1.00 7.42  ? 256  MET A C   1 
ATOM   1937  O  O   . MET A  1 256 ? 60.686  22.063  47.415  1.00 7.79  ? 256  MET A O   1 
ATOM   1938  C  CB  . MET A  1 256 ? 58.968  23.126  49.627  1.00 7.45  ? 256  MET A CB  1 
ATOM   1939  C  CG  . MET A  1 256 ? 58.421  22.999  51.049  1.00 9.30  ? 256  MET A CG  1 
ATOM   1940  S  SD  . MET A  1 256 ? 59.283  24.278  52.055  1.00 13.73 ? 256  MET A SD  1 
ATOM   1941  C  CE  . MET A  1 256 ? 58.865  23.543  53.678  1.00 14.27 ? 256  MET A CE  1 
ATOM   1942  N  N   . SER A  1 257 ? 58.690  22.700  46.454  1.00 7.09  ? 257  SER A N   1 
ATOM   1943  C  CA  . SER A  1 257 ? 59.242  23.317  45.260  1.00 4.95  ? 257  SER A CA  1 
ATOM   1944  C  C   . SER A  1 257 ? 59.435  24.823  45.546  1.00 5.38  ? 257  SER A C   1 
ATOM   1945  O  O   . SER A  1 257 ? 59.150  25.257  46.631  1.00 6.02  ? 257  SER A O   1 
ATOM   1946  C  CB  . SER A  1 257 ? 58.255  23.185  44.088  1.00 5.93  ? 257  SER A CB  1 
ATOM   1947  O  OG  . SER A  1 257 ? 57.135  24.075  44.259  1.00 4.93  ? 257  SER A OG  1 
ATOM   1948  N  N   . THR A  1 258 ? 59.942  25.596  44.593  1.00 4.03  ? 258  THR A N   1 
ATOM   1949  C  CA  . THR A  1 258 ? 59.906  27.056  44.683  1.00 6.51  ? 258  THR A CA  1 
ATOM   1950  C  C   . THR A  1 258 ? 58.443  27.445  44.511  1.00 5.60  ? 258  THR A C   1 
ATOM   1951  O  O   . THR A  1 258 ? 57.604  26.626  44.097  1.00 4.43  ? 258  THR A O   1 
ATOM   1952  C  CB  . THR A  1 258 ? 60.725  27.719  43.572  1.00 6.72  ? 258  THR A CB  1 
ATOM   1953  O  OG1 . THR A  1 258 ? 60.332  27.110  42.340  1.00 8.24  ? 258  THR A OG1 1 
ATOM   1954  C  CG2 . THR A  1 258 ? 62.222  27.372  43.745  1.00 8.83  ? 258  THR A CG2 1 
ATOM   1955  N  N   . THR A  1 259 ? 58.165  28.680  44.853  1.00 5.69  ? 259  THR A N   1 
ATOM   1956  C  CA  . THR A  1 259 ? 56.867  29.272  44.659  1.00 7.96  ? 259  THR A CA  1 
ATOM   1957  C  C   . THR A  1 259 ? 56.900  30.022  43.317  1.00 8.64  ? 259  THR A C   1 
ATOM   1958  O  O   . THR A  1 259 ? 57.748  30.852  43.116  1.00 9.14  ? 259  THR A O   1 
ATOM   1959  C  CB  . THR A  1 259 ? 56.555  30.256  45.818  1.00 6.86  ? 259  THR A CB  1 
ATOM   1960  O  OG1 . THR A  1 259 ? 56.465  29.521  47.026  1.00 9.72  ? 259  THR A OG1 1 
ATOM   1961  C  CG2 . THR A  1 259 ? 55.132  30.853  45.621  1.00 5.82  ? 259  THR A CG2 1 
ATOM   1962  N  N   . PRO A  1 260 ? 56.005  29.678  42.401  1.00 9.78  ? 260  PRO A N   1 
ATOM   1963  C  CA  . PRO A  1 260 ? 55.942  30.336  41.093  1.00 11.21 ? 260  PRO A CA  1 
ATOM   1964  C  C   . PRO A  1 260 ? 55.614  31.816  41.282  1.00 13.00 ? 260  PRO A C   1 
ATOM   1965  O  O   . PRO A  1 260 ? 54.925  32.209  42.238  1.00 11.48 ? 260  PRO A O   1 
ATOM   1966  C  CB  . PRO A  1 260 ? 54.798  29.608  40.361  1.00 10.27 ? 260  PRO A CB  1 
ATOM   1967  C  CG  . PRO A  1 260 ? 54.616  28.303  41.075  1.00 9.63  ? 260  PRO A CG  1 
ATOM   1968  C  CD  . PRO A  1 260 ? 55.018  28.578  42.534  1.00 9.86  ? 260  PRO A CD  1 
ATOM   1969  N  N   . SER A  1 261 ? 56.159  32.641  40.399  1.00 15.09 ? 261  SER A N   1 
ATOM   1970  C  CA  . SER A  1 261 ? 56.073  34.098  40.557  1.00 17.08 ? 261  SER A CA  1 
ATOM   1971  C  C   . SER A  1 261 ? 54.617  34.593  40.537  1.00 17.57 ? 261  SER A C   1 
ATOM   1972  O  O   . SER A  1 261 ? 54.336  35.703  40.997  1.00 19.40 ? 261  SER A O   1 
ATOM   1973  C  CB  . SER A  1 261 ? 56.836  34.787  39.426  1.00 17.82 ? 261  SER A CB  1 
ATOM   1974  O  OG  . SER A  1 261 ? 56.213  34.409  38.204  1.00 20.25 ? 261  SER A OG  1 
ATOM   1975  N  N   . THR A  1 262 ? 53.707  33.779  40.005  1.00 17.05 ? 262  THR A N   1 
ATOM   1976  C  CA  . THR A  1 262 ? 52.289  34.145  39.956  1.00 17.08 ? 262  THR A CA  1 
ATOM   1977  C  C   . THR A  1 262 ? 51.461  33.670  41.174  1.00 16.58 ? 262  THR A C   1 
ATOM   1978  O  O   . THR A  1 262 ? 50.210  33.821  41.176  1.00 16.40 ? 262  THR A O   1 
ATOM   1979  C  CB  . THR A  1 262 ? 51.636  33.526  38.721  1.00 17.61 ? 262  THR A CB  1 
ATOM   1980  O  OG1 . THR A  1 262 ? 51.885  32.107  38.728  1.00 18.69 ? 262  THR A OG1 1 
ATOM   1981  C  CG2 . THR A  1 262 ? 52.295  34.037  37.429  1.00 18.78 ? 262  THR A CG2 1 
ATOM   1982  N  N   . VAL A  1 263 ? 52.126  33.057  42.152  1.00 13.55 ? 263  VAL A N   1 
ATOM   1983  C  CA  . VAL A  1 263 ? 51.480  32.562  43.338  1.00 13.14 ? 263  VAL A CA  1 
ATOM   1984  C  C   . VAL A  1 263 ? 51.981  33.407  44.472  1.00 13.15 ? 263  VAL A C   1 
ATOM   1985  O  O   . VAL A  1 263 ? 53.195  33.563  44.646  1.00 12.69 ? 263  VAL A O   1 
ATOM   1986  C  CB  . VAL A  1 263 ? 51.900  31.109  43.656  1.00 13.33 ? 263  VAL A CB  1 
ATOM   1987  C  CG1 . VAL A  1 263 ? 51.148  30.652  44.860  1.00 15.86 ? 263  VAL A CG1 1 
ATOM   1988  C  CG2 . VAL A  1 263 ? 51.591  30.183  42.484  1.00 16.16 ? 263  VAL A CG2 1 
ATOM   1989  N  N   . THR A  1 264 ? 51.066  33.915  45.286  1.00 11.61 ? 264  THR A N   1 
ATOM   1990  C  CA  . THR A  1 264 ? 51.488  34.650  46.436  1.00 12.53 ? 264  THR A CA  1 
ATOM   1991  C  C   . THR A  1 264 ? 51.841  33.652  47.545  1.00 11.67 ? 264  THR A C   1 
ATOM   1992  O  O   . THR A  1 264 ? 51.120  32.683  47.813  1.00 12.16 ? 264  THR A O   1 
ATOM   1993  C  CB  . THR A  1 264 ? 50.404  35.628  46.879  1.00 12.69 ? 264  THR A CB  1 
ATOM   1994  O  OG1 . THR A  1 264 ? 50.159  36.567  45.815  1.00 13.56 ? 264  THR A OG1 1 
ATOM   1995  C  CG2 . THR A  1 264 ? 50.934  36.458  47.995  1.00 14.64 ? 264  THR A CG2 1 
ATOM   1996  N  N   . VAL A  1 265 ? 52.981  33.863  48.166  1.00 10.99 ? 265  VAL A N   1 
ATOM   1997  C  CA  . VAL A  1 265 ? 53.362  32.992  49.284  1.00 8.94  ? 265  VAL A CA  1 
ATOM   1998  C  C   . VAL A  1 265 ? 52.330  33.258  50.377  1.00 8.75  ? 265  VAL A C   1 
ATOM   1999  O  O   . VAL A  1 265 ? 52.126  34.426  50.756  1.00 9.11  ? 265  VAL A O   1 
ATOM   2000  C  CB  . VAL A  1 265 ? 54.779  33.325  49.787  1.00 10.36 ? 265  VAL A CB  1 
ATOM   2001  C  CG1 . VAL A  1 265 ? 55.126  32.483  51.023  1.00 7.36  ? 265  VAL A CG1 1 
ATOM   2002  C  CG2 . VAL A  1 265 ? 55.841  33.061  48.684  1.00 7.82  ? 265  VAL A CG2 1 
ATOM   2003  N  N   . PRO A  1 266 ? 51.630  32.227  50.845  1.00 7.96  ? 266  PRO A N   1 
ATOM   2004  C  CA  . PRO A  1 266 ? 50.575  32.447  51.836  1.00 8.08  ? 266  PRO A CA  1 
ATOM   2005  C  C   . PRO A  1 266 ? 51.107  32.825  53.229  1.00 7.12  ? 266  PRO A C   1 
ATOM   2006  O  O   . PRO A  1 266 ? 52.238  32.440  53.616  1.00 5.66  ? 266  PRO A O   1 
ATOM   2007  C  CB  . PRO A  1 266 ? 49.862  31.093  51.894  1.00 9.14  ? 266  PRO A CB  1 
ATOM   2008  C  CG  . PRO A  1 266 ? 50.989  30.074  51.634  1.00 10.58 ? 266  PRO A CG  1 
ATOM   2009  C  CD  . PRO A  1 266 ? 51.792  30.789  50.506  1.00 9.47  ? 266  PRO A CD  1 
ATOM   2010  N  N   . THR A  1 267 ? 50.269  33.535  53.981  1.00 7.32  ? 267  THR A N   1 
ATOM   2011  C  CA  . THR A  1 267 ? 50.511  33.765  55.435  1.00 9.12  ? 267  THR A CA  1 
ATOM   2012  C  C   . THR A  1 267 ? 49.748  32.706  56.250  1.00 8.81  ? 267  THR A C   1 
ATOM   2013  O  O   . THR A  1 267 ? 48.616  32.364  55.906  1.00 9.01  ? 267  THR A O   1 
ATOM   2014  C  CB  . THR A  1 267 ? 50.056  35.183  55.803  1.00 10.40 ? 267  THR A CB  1 
ATOM   2015  O  OG1 . THR A  1 267 ? 50.903  36.119  55.104  1.00 13.01 ? 267  THR A OG1 1 
ATOM   2016  C  CG2 . THR A  1 267 ? 50.271  35.515  57.344  1.00 10.61 ? 267  THR A CG2 1 
ATOM   2017  N  N   . TRP A  1 268 ? 50.380  32.188  57.311  1.00 6.87  ? 268  TRP A N   1 
ATOM   2018  C  CA  . TRP A  1 268 ? 49.762  31.230  58.228  1.00 6.42  ? 268  TRP A CA  1 
ATOM   2019  C  C   . TRP A  1 268 ? 49.737  31.786  59.639  1.00 5.42  ? 268  TRP A C   1 
ATOM   2020  O  O   . TRP A  1 268 ? 50.683  32.435  60.058  1.00 7.12  ? 268  TRP A O   1 
ATOM   2021  C  CB  . TRP A  1 268 ? 50.600  29.921  58.236  1.00 4.68  ? 268  TRP A CB  1 
ATOM   2022  C  CG  . TRP A  1 268 ? 50.732  29.269  56.870  1.00 9.61  ? 268  TRP A CG  1 
ATOM   2023  C  CD1 . TRP A  1 268 ? 51.757  29.420  55.959  1.00 8.08  ? 268  TRP A CD1 1 
ATOM   2024  C  CD2 . TRP A  1 268 ? 49.817  28.356  56.285  1.00 7.76  ? 268  TRP A CD2 1 
ATOM   2025  N  NE1 . TRP A  1 268 ? 51.526  28.645  54.857  1.00 7.95  ? 268  TRP A NE1 1 
ATOM   2026  C  CE2 . TRP A  1 268 ? 50.349  27.970  55.027  1.00 8.95  ? 268  TRP A CE2 1 
ATOM   2027  C  CE3 . TRP A  1 268 ? 48.640  27.751  56.726  1.00 6.63  ? 268  TRP A CE3 1 
ATOM   2028  C  CZ2 . TRP A  1 268 ? 49.700  27.051  54.178  1.00 7.48  ? 268  TRP A CZ2 1 
ATOM   2029  C  CZ3 . TRP A  1 268 ? 47.983  26.841  55.865  1.00 7.22  ? 268  TRP A CZ3 1 
ATOM   2030  C  CH2 . TRP A  1 268 ? 48.527  26.509  54.614  1.00 9.72  ? 268  TRP A CH2 1 
ATOM   2031  N  N   . SER A  1 269 ? 48.683  31.491  60.399  1.00 6.01  ? 269  SER A N   1 
ATOM   2032  C  CA  . SER A  1 269 ? 48.689  31.718  61.834  1.00 6.01  ? 269  SER A CA  1 
ATOM   2033  C  C   . SER A  1 269 ? 47.819  30.643  62.448  1.00 6.24  ? 269  SER A C   1 
ATOM   2034  O  O   . SER A  1 269 ? 46.601  30.565  62.175  1.00 3.88  ? 269  SER A O   1 
ATOM   2035  C  CB  . SER A  1 269 ? 48.116  33.118  62.141  1.00 7.21  ? 269  SER A CB  1 
ATOM   2036  O  OG  . SER A  1 269 ? 47.884  33.281  63.535  1.00 10.83 ? 269  SER A OG  1 
ATOM   2037  N  N   . PHE A  1 270 ? 48.443  29.781  63.245  1.00 6.04  ? 270  PHE A N   1 
ATOM   2038  C  CA  . PHE A  1 270 ? 47.797  28.590  63.785  1.00 7.01  ? 270  PHE A CA  1 
ATOM   2039  C  C   . PHE A  1 270 ? 47.490  28.742  65.236  1.00 8.31  ? 270  PHE A C   1 
ATOM   2040  O  O   . PHE A  1 270 ? 48.142  29.516  65.939  1.00 11.01 ? 270  PHE A O   1 
ATOM   2041  C  CB  . PHE A  1 270 ? 48.737  27.372  63.647  1.00 7.20  ? 270  PHE A CB  1 
ATOM   2042  C  CG  . PHE A  1 270 ? 48.973  26.982  62.220  1.00 9.43  ? 270  PHE A CG  1 
ATOM   2043  C  CD1 . PHE A  1 270 ? 47.993  26.274  61.524  1.00 6.16  ? 270  PHE A CD1 1 
ATOM   2044  C  CD2 . PHE A  1 270 ? 50.140  27.375  61.569  1.00 10.31 ? 270  PHE A CD2 1 
ATOM   2045  C  CE1 . PHE A  1 270 ? 48.184  25.909  60.192  1.00 10.20 ? 270  PHE A CE1 1 
ATOM   2046  C  CE2 . PHE A  1 270 ? 50.326  27.040  60.240  1.00 11.07 ? 270  PHE A CE2 1 
ATOM   2047  C  CZ  . PHE A  1 270 ? 49.354  26.293  59.552  1.00 9.07  ? 270  PHE A CZ  1 
ATOM   2048  N  N   . PRO A  1 271 ? 46.559  27.958  65.745  1.00 8.75  ? 271  PRO A N   1 
ATOM   2049  C  CA  . PRO A  1 271 ? 46.317  27.977  67.193  1.00 9.18  ? 271  PRO A CA  1 
ATOM   2050  C  C   . PRO A  1 271 ? 47.560  27.556  68.015  1.00 8.62  ? 271  PRO A C   1 
ATOM   2051  O  O   . PRO A  1 271 ? 47.804  28.131  69.067  1.00 9.31  ? 271  PRO A O   1 
ATOM   2052  C  CB  . PRO A  1 271 ? 45.193  26.951  67.370  1.00 9.05  ? 271  PRO A CB  1 
ATOM   2053  C  CG  . PRO A  1 271 ? 44.493  26.926  66.002  1.00 9.31  ? 271  PRO A CG  1 
ATOM   2054  C  CD  . PRO A  1 271 ? 45.687  26.992  65.032  1.00 9.11  ? 271  PRO A CD  1 
ATOM   2055  N  N   . GLY A  1 272 ? 48.309  26.583  67.533  1.00 9.45  ? 272  GLY A N   1 
ATOM   2056  C  CA  . GLY A  1 272 ? 49.342  25.944  68.349  1.00 8.49  ? 272  GLY A CA  1 
ATOM   2057  C  C   . GLY A  1 272 ? 50.699  26.278  67.802  1.00 8.93  ? 272  GLY A C   1 
ATOM   2058  O  O   . GLY A  1 272 ? 50.824  26.617  66.617  1.00 9.10  ? 272  GLY A O   1 
ATOM   2059  N  N   . ALA A  1 273 ? 51.707  26.206  68.679  1.00 6.47  ? 273  ALA A N   1 
ATOM   2060  C  CA  . ALA A  1 273 ? 53.077  26.428  68.288  1.00 7.35  ? 273  ALA A CA  1 
ATOM   2061  C  C   . ALA A  1 273 ? 53.490  25.371  67.219  1.00 8.03  ? 273  ALA A C   1 
ATOM   2062  O  O   . ALA A  1 273 ? 52.848  24.295  67.130  1.00 8.83  ? 273  ALA A O   1 
ATOM   2063  C  CB  . ALA A  1 273 ? 53.975  26.331  69.495  1.00 6.93  ? 273  ALA A CB  1 
ATOM   2064  N  N   . CYS A  1 274 ? 54.444  25.728  66.343  1.00 7.65  ? 274  CYS A N   1 
ATOM   2065  C  CA  . CYS A  1 274 ? 55.031  24.771  65.405  1.00 7.42  ? 274  CYS A CA  1 
ATOM   2066  C  C   . CYS A  1 274 ? 56.495  25.072  65.169  1.00 7.71  ? 274  CYS A C   1 
ATOM   2067  O  O   . CYS A  1 274 ? 56.999  26.128  65.552  1.00 7.82  ? 274  CYS A O   1 
ATOM   2068  C  CB  . CYS A  1 274 ? 54.273  24.684  64.075  1.00 8.15  ? 274  CYS A CB  1 
ATOM   2069  S  SG  . CYS A  1 274 ? 54.353  26.177  63.059  1.00 8.97  ? 274  CYS A SG  1 
ATOM   2070  N  N   . ALA A  1 275 ? 57.190  24.118  64.578  1.00 8.04  ? 275  ALA A N   1 
ATOM   2071  C  CA  . ALA A  1 275 ? 58.620  24.281  64.330  1.00 9.30  ? 275  ALA A CA  1 
ATOM   2072  C  C   . ALA A  1 275 ? 59.006  23.383  63.206  1.00 9.57  ? 275  ALA A C   1 
ATOM   2073  O  O   . ALA A  1 275 ? 58.355  22.347  62.925  1.00 9.22  ? 275  ALA A O   1 
ATOM   2074  C  CB  . ALA A  1 275 ? 59.473  23.950  65.609  1.00 9.67  ? 275  ALA A CB  1 
ATOM   2075  N  N   . PHE A  1 276 ? 60.082  23.767  62.546  1.00 9.83  ? 276  PHE A N   1 
ATOM   2076  C  CA  . PHE A  1 276 ? 60.701  22.828  61.640  1.00 10.51 ? 276  PHE A CA  1 
ATOM   2077  C  C   . PHE A  1 276 ? 62.210  22.884  61.634  1.00 10.50 ? 276  PHE A C   1 
ATOM   2078  O  O   . PHE A  1 276 ? 62.831  23.889  61.991  1.00 9.80  ? 276  PHE A O   1 
ATOM   2079  C  CB  . PHE A  1 276 ? 60.182  22.979  60.208  1.00 10.43 ? 276  PHE A CB  1 
ATOM   2080  C  CG  . PHE A  1 276 ? 60.426  24.320  59.599  1.00 9.75  ? 276  PHE A CG  1 
ATOM   2081  C  CD1 . PHE A  1 276 ? 61.620  24.569  58.885  1.00 13.04 ? 276  PHE A CD1 1 
ATOM   2082  C  CD2 . PHE A  1 276 ? 59.422  25.300  59.660  1.00 11.02 ? 276  PHE A CD2 1 
ATOM   2083  C  CE1 . PHE A  1 276 ? 61.841  25.810  58.268  1.00 11.82 ? 276  PHE A CE1 1 
ATOM   2084  C  CE2 . PHE A  1 276 ? 59.634  26.585  59.060  1.00 12.91 ? 276  PHE A CE2 1 
ATOM   2085  C  CZ  . PHE A  1 276 ? 60.838  26.809  58.341  1.00 11.68 ? 276  PHE A CZ  1 
ATOM   2086  N  N   . GLN A  1 277 ? 62.784  21.765  61.225  1.00 10.25 ? 277  GLN A N   1 
ATOM   2087  C  CA  . GLN A  1 277 ? 64.194  21.722  61.005  1.00 10.05 ? 277  GLN A CA  1 
ATOM   2088  C  C   . GLN A  1 277 ? 64.424  21.299  59.587  1.00 8.15  ? 277  GLN A C   1 
ATOM   2089  O  O   . GLN A  1 277 ? 63.929  20.253  59.112  1.00 9.47  ? 277  GLN A O   1 
ATOM   2090  C  CB  . GLN A  1 277 ? 64.861  20.693  61.944  1.00 8.31  ? 277  GLN A CB  1 
ATOM   2091  C  CG  . GLN A  1 277 ? 66.344  20.594  61.744  1.00 9.04  ? 277  GLN A CG  1 
ATOM   2092  C  CD  . GLN A  1 277 ? 67.023  19.441  62.581  1.00 12.01 ? 277  GLN A CD  1 
ATOM   2093  O  OE1 . GLN A  1 277 ? 66.667  18.268  62.436  1.00 14.12 ? 277  GLN A OE1 1 
ATOM   2094  N  NE2 . GLN A  1 277 ? 68.027  19.800  63.412  1.00 11.86 ? 277  GLN A NE2 1 
ATOM   2095  N  N   . VAL A  1 278 ? 65.219  22.092  58.916  1.00 9.05  ? 278  VAL A N   1 
ATOM   2096  C  CA  . VAL A  1 278 ? 65.575  21.826  57.523  1.00 8.85  ? 278  VAL A CA  1 
ATOM   2097  C  C   . VAL A  1 278 ? 66.480  20.618  57.456  1.00 9.63  ? 278  VAL A C   1 
ATOM   2098  O  O   . VAL A  1 278 ? 67.483  20.533  58.182  1.00 8.12  ? 278  VAL A O   1 
ATOM   2099  C  CB  . VAL A  1 278 ? 66.298  23.022  56.901  1.00 9.22  ? 278  VAL A CB  1 
ATOM   2100  C  CG1 . VAL A  1 278 ? 66.738  22.718  55.414  1.00 7.47  ? 278  VAL A CG1 1 
ATOM   2101  C  CG2 . VAL A  1 278 ? 65.364  24.305  56.978  1.00 7.98  ? 278  VAL A CG2 1 
ATOM   2102  N  N   . GLN A  1 279 ? 66.154  19.733  56.528  1.00 8.90  ? 279  GLN A N   1 
ATOM   2103  C  CA  . GLN A  1 279 ? 66.956  18.513  56.333  1.00 10.29 ? 279  GLN A CA  1 
ATOM   2104  C  C   . GLN A  1 279 ? 67.778  18.721  55.048  1.00 11.23 ? 279  GLN A C   1 
ATOM   2105  O  O   . GLN A  1 279 ? 68.998  18.515  55.029  1.00 10.78 ? 279  GLN A O   1 
ATOM   2106  C  CB  . GLN A  1 279 ? 65.998  17.281  56.192  1.00 8.39  ? 279  GLN A CB  1 
ATOM   2107  C  CG  . GLN A  1 279 ? 65.191  16.943  57.448  1.00 9.95  ? 279  GLN A CG  1 
ATOM   2108  C  CD  . GLN A  1 279 ? 66.070  16.981  58.752  1.00 7.97  ? 279  GLN A CD  1 
ATOM   2109  O  OE1 . GLN A  1 279 ? 67.125  16.317  58.814  1.00 10.48 ? 279  GLN A OE1 1 
ATOM   2110  N  NE2 . GLN A  1 279 ? 65.651  17.731  59.733  1.00 7.42  ? 279  GLN A NE2 1 
ATOM   2111  N  N   . GLU A  1 280 ? 67.111  19.224  53.995  1.00 10.49 ? 280  GLU A N   1 
ATOM   2112  C  CA  . GLU A  1 280 ? 67.755  19.413  52.699  1.00 11.73 ? 280  GLU A CA  1 
ATOM   2113  C  C   . GLU A  1 280 ? 67.228  20.739  52.137  1.00 9.99  ? 280  GLU A C   1 
ATOM   2114  O  O   . GLU A  1 280 ? 66.037  21.037  52.315  1.00 9.38  ? 280  GLU A O   1 
ATOM   2115  C  CB  . GLU A  1 280 ? 67.346  18.264  51.734  1.00 11.25 ? 280  GLU A CB  1 
ATOM   2116  C  CG  . GLU A  1 280 ? 68.139  18.356  50.435  1.00 16.80 ? 280  GLU A CG  1 
ATOM   2117  C  CD  . GLU A  1 280 ? 67.705  17.305  49.396  1.00 18.34 ? 280  GLU A CD  1 
ATOM   2118  O  OE1 . GLU A  1 280 ? 66.835  16.406  49.710  1.00 11.68 ? 280  GLU A OE1 1 
ATOM   2119  O  OE2 . GLU A  1 280 ? 68.202  17.435  48.250  1.00 18.13 ? 280  GLU A OE2 1 
ATOM   2120  N  N   . GLY A  1 281 ? 68.084  21.533  51.475  1.00 8.64  ? 281  GLY A N   1 
ATOM   2121  C  CA  . GLY A  1 281 ? 67.597  22.713  50.805  1.00 6.06  ? 281  GLY A CA  1 
ATOM   2122  C  C   . GLY A  1 281 ? 67.776  24.026  51.573  1.00 7.29  ? 281  GLY A C   1 
ATOM   2123  O  O   . GLY A  1 281 ? 68.592  24.115  52.507  1.00 6.16  ? 281  GLY A O   1 
ATOM   2124  N  N   . ARG A  1 282 ? 67.001  25.041  51.197  1.00 4.93  ? 282  ARG A N   1 
ATOM   2125  C  CA  . ARG A  1 282 ? 67.233  26.385  51.691  1.00 6.01  ? 282  ARG A CA  1 
ATOM   2126  C  C   . ARG A  1 282 ? 65.835  26.969  51.781  1.00 7.38  ? 282  ARG A C   1 
ATOM   2127  O  O   . ARG A  1 282 ? 65.171  27.172  50.747  1.00 7.70  ? 282  ARG A O   1 
ATOM   2128  C  CB  . ARG A  1 282 ? 68.085  27.164  50.653  1.00 6.20  ? 282  ARG A CB  1 
ATOM   2129  C  CG  . ARG A  1 282 ? 69.485  26.544  50.485  1.00 5.22  ? 282  ARG A CG  1 
ATOM   2130  C  CD  . ARG A  1 282 ? 70.427  27.388  49.684  1.00 8.53  ? 282  ARG A CD  1 
ATOM   2131  N  NE  . ARG A  1 282 ? 69.958  27.540  48.309  1.00 11.70 ? 282  ARG A NE  1 
ATOM   2132  C  CZ  . ARG A  1 282 ? 69.646  28.678  47.687  1.00 13.00 ? 282  ARG A CZ  1 
ATOM   2133  N  NH1 . ARG A  1 282 ? 69.689  29.849  48.291  1.00 7.91  ? 282  ARG A NH1 1 
ATOM   2134  N  NH2 . ARG A  1 282 ? 69.296  28.635  46.406  1.00 12.83 ? 282  ARG A NH2 1 
ATOM   2135  N  N   . VAL A  1 283 ? 65.360  27.166  53.011  1.00 6.00  ? 283  VAL A N   1 
ATOM   2136  C  CA  . VAL A  1 283 ? 63.987  27.588  53.222  1.00 7.92  ? 283  VAL A CA  1 
ATOM   2137  C  C   . VAL A  1 283 ? 64.024  28.931  53.909  1.00 7.06  ? 283  VAL A C   1 
ATOM   2138  O  O   . VAL A  1 283 ? 64.670  29.104  54.943  1.00 9.18  ? 283  VAL A O   1 
ATOM   2139  C  CB  . VAL A  1 283 ? 63.222  26.569  54.095  1.00 8.17  ? 283  VAL A CB  1 
ATOM   2140  C  CG1 . VAL A  1 283 ? 61.792  27.035  54.408  1.00 9.53  ? 283  VAL A CG1 1 
ATOM   2141  C  CG2 . VAL A  1 283 ? 63.204  25.212  53.381  1.00 9.64  ? 283  VAL A CG2 1 
ATOM   2142  N  N   . VAL A  1 284 ? 63.242  29.843  53.375  1.00 7.54  ? 284  VAL A N   1 
ATOM   2143  C  CA  . VAL A  1 284 ? 63.203  31.189  53.905  1.00 7.56  ? 284  VAL A CA  1 
ATOM   2144  C  C   . VAL A  1 284 ? 61.954  31.293  54.821  1.00 8.75  ? 284  VAL A C   1 
ATOM   2145  O  O   . VAL A  1 284 ? 60.821  30.954  54.386  1.00 8.38  ? 284  VAL A O   1 
ATOM   2146  C  CB  . VAL A  1 284 ? 63.080  32.194  52.784  1.00 6.96  ? 284  VAL A CB  1 
ATOM   2147  C  CG1 . VAL A  1 284 ? 62.794  33.566  53.391  1.00 9.06  ? 284  VAL A CG1 1 
ATOM   2148  C  CG2 . VAL A  1 284 ? 64.385  32.293  51.964  1.00 10.86 ? 284  VAL A CG2 1 
ATOM   2149  N  N   . VAL A  1 285 ? 62.142  31.769  56.048  1.00 7.18  ? 285  VAL A N   1 
ATOM   2150  C  CA  . VAL A  1 285 ? 61.002  31.957  56.944  1.00 8.95  ? 285  VAL A CA  1 
ATOM   2151  C  C   . VAL A  1 285 ? 60.877  33.423  57.351  1.00 8.21  ? 285  VAL A C   1 
ATOM   2152  O  O   . VAL A  1 285 ? 61.914  34.109  57.628  1.00 8.21  ? 285  VAL A O   1 
ATOM   2153  C  CB  . VAL A  1 285 ? 61.114  30.961  58.163  1.00 9.53  ? 285  VAL A CB  1 
ATOM   2154  C  CG1 . VAL A  1 285 ? 62.131  31.487  59.215  1.00 9.94  ? 285  VAL A CG1 1 
ATOM   2155  C  CG2 . VAL A  1 285 ? 59.716  30.622  58.713  1.00 13.57 ? 285  VAL A CG2 1 
ATOM   2156  N  N   . GLN A  1 286 ? 59.644  33.954  57.300  1.00 6.01  ? 286  GLN A N   1 
ATOM   2157  C  CA  . GLN A  1 286 ? 59.423  35.352  57.672  1.00 7.11  ? 286  GLN A CA  1 
ATOM   2158  C  C   . GLN A  1 286 ? 58.377  35.371  58.751  1.00 5.87  ? 286  GLN A C   1 
ATOM   2159  O  O   . GLN A  1 286 ? 57.211  35.192  58.454  1.00 5.11  ? 286  GLN A O   1 
ATOM   2160  C  CB  . GLN A  1 286 ? 58.941  36.186  56.500  1.00 7.07  ? 286  GLN A CB  1 
ATOM   2161  C  CG  . GLN A  1 286 ? 58.923  37.693  56.821  1.00 11.38 ? 286  GLN A CG  1 
ATOM   2162  C  CD  . GLN A  1 286 ? 58.305  38.507  55.710  1.00 17.95 ? 286  GLN A CD  1 
ATOM   2163  O  OE1 . GLN A  1 286 ? 58.297  38.077  54.547  1.00 20.09 ? 286  GLN A OE1 1 
ATOM   2164  N  NE2 . GLN A  1 286 ? 57.763  39.672  56.056  1.00 12.89 ? 286  GLN A NE2 1 
ATOM   2165  N  N   . ILE A  1 287 ? 58.790  35.585  59.988  1.00 5.64  ? 287  ILE A N   1 
ATOM   2166  C  CA  . ILE A  1 287 ? 57.915  35.348  61.150  1.00 6.47  ? 287  ILE A CA  1 
ATOM   2167  C  C   . ILE A  1 287 ? 57.666  36.661  61.809  1.00 7.09  ? 287  ILE A C   1 
ATOM   2168  O  O   . ILE A  1 287 ? 58.619  37.393  62.043  1.00 7.65  ? 287  ILE A O   1 
ATOM   2169  C  CB  . ILE A  1 287 ? 58.604  34.446  62.188  1.00 7.50  ? 287  ILE A CB  1 
ATOM   2170  C  CG1 . ILE A  1 287 ? 59.100  33.150  61.550  1.00 8.64  ? 287  ILE A CG1 1 
ATOM   2171  C  CG2 . ILE A  1 287 ? 57.655  34.194  63.432  1.00 4.89  ? 287  ILE A CG2 1 
ATOM   2172  C  CD1 . ILE A  1 287 ? 60.105  32.366  62.441  1.00 13.94 ? 287  ILE A CD1 1 
ATOM   2173  N  N   . GLY A  1 288 ? 56.390  36.977  62.090  1.00 6.77  ? 288  GLY A N   1 
ATOM   2174  C  CA  . GLY A  1 288 ? 56.062  38.237  62.769  1.00 7.94  ? 288  GLY A CA  1 
ATOM   2175  C  C   . GLY A  1 288 ? 56.608  39.456  62.012  1.00 8.28  ? 288  GLY A C   1 
ATOM   2176  O  O   . GLY A  1 288 ? 56.429  39.568  60.801  1.00 9.01  ? 288  GLY A O   1 
ATOM   2177  N  N   . ASP A  1 289 ? 57.295  40.360  62.720  1.00 8.58  ? 289  ASP A N   1 
ATOM   2178  C  CA  . ASP A  1 289 ? 57.891  41.543  62.104  1.00 10.07 ? 289  ASP A CA  1 
ATOM   2179  C  C   . ASP A  1 289 ? 59.379  41.416  61.819  1.00 9.99  ? 289  ASP A C   1 
ATOM   2180  O  O   . ASP A  1 289 ? 60.022  42.403  61.444  1.00 9.39  ? 289  ASP A O   1 
ATOM   2181  C  CB  . ASP A  1 289 ? 57.703  42.764  63.001  1.00 10.20 ? 289  ASP A CB  1 
ATOM   2182  C  CG  A ASP A  1 289 ? 58.015  42.462  64.477  0.50 10.79 ? 289  ASP A CG  1 
ATOM   2183  C  CG  B ASP A  1 289 ? 56.296  43.298  62.956  0.50 10.21 ? 289  ASP A CG  1 
ATOM   2184  O  OD1 A ASP A  1 289 ? 58.966  41.683  64.792  0.50 15.84 ? 289  ASP A OD1 1 
ATOM   2185  O  OD1 B ASP A  1 289 ? 55.700  43.416  61.857  0.50 10.96 ? 289  ASP A OD1 1 
ATOM   2186  O  OD2 A ASP A  1 289 ? 57.340  42.932  65.402  0.50 14.24 ? 289  ASP A OD2 1 
ATOM   2187  O  OD2 B ASP A  1 289 ? 55.723  43.610  64.000  0.50 10.22 ? 289  ASP A OD2 1 
ATOM   2188  N  N   . TYR A  1 290 ? 59.902  40.211  62.011  1.00 8.85  ? 290  TYR A N   1 
ATOM   2189  C  CA  . TYR A  1 290 ? 61.313  39.902  61.817  1.00 8.83  ? 290  TYR A CA  1 
ATOM   2190  C  C   . TYR A  1 290 ? 61.684  39.733  60.331  1.00 8.37  ? 290  TYR A C   1 
ATOM   2191  O  O   . TYR A  1 290 ? 60.813  39.502  59.498  1.00 9.46  ? 290  TYR A O   1 
ATOM   2192  C  CB  . TYR A  1 290 ? 61.604  38.607  62.570  1.00 8.47  ? 290  TYR A CB  1 
ATOM   2193  C  CG  . TYR A  1 290 ? 61.664  38.755  64.059  1.00 9.97  ? 290  TYR A CG  1 
ATOM   2194  C  CD1 . TYR A  1 290 ? 62.733  39.412  64.676  1.00 15.05 ? 290  TYR A CD1 1 
ATOM   2195  C  CD2 . TYR A  1 290 ? 60.655  38.243  64.865  1.00 11.28 ? 290  TYR A CD2 1 
ATOM   2196  C  CE1 . TYR A  1 290 ? 62.800  39.516  66.072  1.00 18.15 ? 290  TYR A CE1 1 
ATOM   2197  C  CE2 . TYR A  1 290 ? 60.706  38.333  66.230  1.00 15.00 ? 290  TYR A CE2 1 
ATOM   2198  C  CZ  . TYR A  1 290 ? 61.774  38.974  66.837  1.00 17.37 ? 290  TYR A CZ  1 
ATOM   2199  O  OH  . TYR A  1 290 ? 61.793  39.078  68.204  1.00 19.50 ? 290  TYR A OH  1 
ATOM   2200  N  N   . ALA A  1 291 ? 62.973  39.829  60.006  1.00 7.62  ? 291  ALA A N   1 
ATOM   2201  C  CA  . ALA A  1 291 ? 63.451  39.664  58.635  1.00 7.74  ? 291  ALA A CA  1 
ATOM   2202  C  C   . ALA A  1 291 ? 63.240  38.272  58.115  1.00 7.77  ? 291  ALA A C   1 
ATOM   2203  O  O   . ALA A  1 291 ? 63.470  37.311  58.841  1.00 7.07  ? 291  ALA A O   1 
ATOM   2204  C  CB  . ALA A  1 291 ? 64.938  39.967  58.532  1.00 7.63  ? 291  ALA A CB  1 
ATOM   2205  N  N   . ALA A  1 292 ? 62.888  38.196  56.832  1.00 7.91  ? 292  ALA A N   1 
ATOM   2206  C  CA  . ALA A  1 292 ? 62.898  36.935  56.099  1.00 9.41  ? 292  ALA A CA  1 
ATOM   2207  C  C   . ALA A  1 292 ? 64.308  36.321  56.278  1.00 9.03  ? 292  ALA A C   1 
ATOM   2208  O  O   . ALA A  1 292 ? 65.295  36.983  55.993  1.00 11.32 ? 292  ALA A O   1 
ATOM   2209  C  CB  . ALA A  1 292 ? 62.609  37.216  54.669  1.00 9.06  ? 292  ALA A CB  1 
ATOM   2210  N  N   . THR A  1 293 ? 64.410  35.104  56.790  1.00 9.26  ? 293  THR A N   1 
ATOM   2211  C  CA  . THR A  1 293 ? 65.709  34.520  57.121  1.00 8.16  ? 293  THR A CA  1 
ATOM   2212  C  C   . THR A  1 293 ? 65.805  33.160  56.441  1.00 8.35  ? 293  THR A C   1 
ATOM   2213  O  O   . THR A  1 293 ? 64.844  32.328  56.507  1.00 5.93  ? 293  THR A O   1 
ATOM   2214  C  CB  . THR A  1 293 ? 65.792  34.390  58.675  1.00 9.33  ? 293  THR A CB  1 
ATOM   2215  O  OG1 . THR A  1 293 ? 65.752  35.708  59.261  1.00 11.54 ? 293  THR A OG1 1 
ATOM   2216  C  CG2 . THR A  1 293 ? 67.112  33.830  59.132  1.00 10.59 ? 293  THR A CG2 1 
ATOM   2217  N  N   . GLU A  1 294 ? 66.947  32.886  55.813  1.00 6.13  ? 294  GLU A N   1 
ATOM   2218  C  CA  . GLU A  1 294 ? 67.110  31.633  55.092  1.00 7.07  ? 294  GLU A CA  1 
ATOM   2219  C  C   . GLU A  1 294 ? 67.799  30.594  56.001  1.00 8.19  ? 294  GLU A C   1 
ATOM   2220  O  O   . GLU A  1 294 ? 68.836  30.889  56.594  1.00 7.49  ? 294  GLU A O   1 
ATOM   2221  C  CB  . GLU A  1 294 ? 67.990  31.860  53.840  1.00 7.29  ? 294  GLU A CB  1 
ATOM   2222  C  CG  . GLU A  1 294 ? 67.971  30.668  52.892  1.00 11.58 ? 294  GLU A CG  1 
ATOM   2223  C  CD  . GLU A  1 294 ? 68.813  30.918  51.644  1.00 17.18 ? 294  GLU A CD  1 
ATOM   2224  O  OE1 . GLU A  1 294 ? 68.487  31.830  50.828  1.00 23.95 ? 294  GLU A OE1 1 
ATOM   2225  O  OE2 . GLU A  1 294 ? 69.822  30.218  51.491  1.00 15.31 ? 294  GLU A OE2 1 
ATOM   2226  N  N   . LEU A  1 295 ? 67.212  29.407  56.082  1.00 8.03  ? 295  LEU A N   1 
ATOM   2227  C  CA  . LEU A  1 295 ? 67.716  28.302  56.913  1.00 8.85  ? 295  LEU A CA  1 
ATOM   2228  C  C   . LEU A  1 295 ? 68.294  27.241  56.000  1.00 10.08 ? 295  LEU A C   1 
ATOM   2229  O  O   . LEU A  1 295 ? 67.666  26.880  54.983  1.00 11.19 ? 295  LEU A O   1 
ATOM   2230  C  CB  . LEU A  1 295 ? 66.560  27.650  57.685  1.00 9.55  ? 295  LEU A CB  1 
ATOM   2231  C  CG  . LEU A  1 295 ? 66.284  28.324  59.041  1.00 14.25 ? 295  LEU A CG  1 
ATOM   2232  C  CD1 . LEU A  1 295 ? 65.731  29.725  58.817  1.00 13.22 ? 295  LEU A CD1 1 
ATOM   2233  C  CD2 . LEU A  1 295 ? 65.319  27.453  59.943  1.00 16.04 ? 295  LEU A CD2 1 
ATOM   2234  N  N   . GLY A  1 296 ? 69.434  26.712  56.399  1.00 9.96  ? 296  GLY A N   1 
ATOM   2235  C  CA  . GLY A  1 296 ? 70.081  25.579  55.756  1.00 9.01  ? 296  GLY A CA  1 
ATOM   2236  C  C   . GLY A  1 296 ? 70.030  24.321  56.616  1.00 9.20  ? 296  GLY A C   1 
ATOM   2237  O  O   . GLY A  1 296 ? 69.281  24.257  57.592  1.00 8.83  ? 296  GLY A O   1 
ATOM   2238  N  N   . SER A  1 297 ? 70.791  23.297  56.250  1.00 8.90  ? 297  SER A N   1 
ATOM   2239  C  CA  . SER A  1 297 ? 70.638  22.025  56.952  1.00 10.84 ? 297  SER A CA  1 
ATOM   2240  C  C   . SER A  1 297 ? 70.805  22.084  58.468  1.00 10.32 ? 297  SER A C   1 
ATOM   2241  O  O   . SER A  1 297 ? 71.722  22.727  59.008  1.00 7.88  ? 297  SER A O   1 
ATOM   2242  C  CB  . SER A  1 297 ? 71.518  20.922  56.366  1.00 12.28 ? 297  SER A CB  1 
ATOM   2243  O  OG  . SER A  1 297 ? 72.844  21.331  56.377  1.00 16.52 ? 297  SER A OG  1 
ATOM   2244  N  N   . GLY A  1 298 ? 69.838  21.447  59.133  1.00 9.79  ? 298  GLY A N   1 
ATOM   2245  C  CA  . GLY A  1 298 ? 69.865  21.334  60.580  1.00 7.92  ? 298  GLY A CA  1 
ATOM   2246  C  C   . GLY A  1 298 ? 69.347  22.577  61.256  1.00 8.52  ? 298  GLY A C   1 
ATOM   2247  O  O   . GLY A  1 298 ? 69.155  22.562  62.456  1.00 8.03  ? 298  GLY A O   1 
ATOM   2248  N  N   . ASP A  1 299 ? 69.130  23.678  60.522  1.00 8.90  ? 299  ASP A N   1 
ATOM   2249  C  CA  . ASP A  1 299 ? 68.674  24.903  61.189  1.00 8.07  ? 299  ASP A CA  1 
ATOM   2250  C  C   . ASP A  1 299 ? 67.189  24.783  61.597  1.00 8.38  ? 299  ASP A C   1 
ATOM   2251  O  O   . ASP A  1 299 ? 66.419  24.105  60.913  1.00 7.48  ? 299  ASP A O   1 
ATOM   2252  C  CB  . ASP A  1 299 ? 68.782  26.143  60.295  1.00 8.32  ? 299  ASP A CB  1 
ATOM   2253  C  CG  . ASP A  1 299 ? 70.187  26.547  59.962  1.00 6.74  ? 299  ASP A CG  1 
ATOM   2254  O  OD1 . ASP A  1 299 ? 71.179  26.134  60.618  1.00 10.72 ? 299  ASP A OD1 1 
ATOM   2255  O  OD2 . ASP A  1 299 ? 70.425  27.305  58.980  1.00 9.33  ? 299  ASP A OD2 1 
ATOM   2256  N  N   . VAL A  1 300 ? 66.788  25.454  62.685  1.00 8.33  ? 300  VAL A N   1 
ATOM   2257  C  CA  . VAL A  1 300 ? 65.420  25.272  63.239  1.00 7.06  ? 300  VAL A CA  1 
ATOM   2258  C  C   . VAL A  1 300 ? 64.706  26.602  63.342  1.00 7.33  ? 300  VAL A C   1 
ATOM   2259  O  O   . VAL A  1 300 ? 65.294  27.599  63.764  1.00 6.96  ? 300  VAL A O   1 
ATOM   2260  C  CB  . VAL A  1 300 ? 65.521  24.639  64.677  1.00 6.87  ? 300  VAL A CB  1 
ATOM   2261  C  CG1 . VAL A  1 300 ? 64.122  24.531  65.392  1.00 9.05  ? 300  VAL A CG1 1 
ATOM   2262  C  CG2 . VAL A  1 300 ? 66.192  23.260  64.527  1.00 5.26  ? 300  VAL A CG2 1 
ATOM   2263  N  N   . ALA A  1 301 ? 63.442  26.622  62.931  1.00 7.46  ? 301  ALA A N   1 
ATOM   2264  C  CA  . ALA A  1 301 ? 62.632  27.802  63.120  1.00 6.36  ? 301  ALA A CA  1 
ATOM   2265  C  C   . ALA A  1 301 ? 61.491  27.460  64.081  1.00 8.37  ? 301  ALA A C   1 
ATOM   2266  O  O   . ALA A  1 301 ? 60.911  26.385  63.947  1.00 7.70  ? 301  ALA A O   1 
ATOM   2267  C  CB  . ALA A  1 301 ? 62.082  28.274  61.760  1.00 5.69  ? 301  ALA A CB  1 
ATOM   2268  N  N   . PHE A  1 302 ? 61.157  28.376  65.015  1.00 8.26  ? 302  PHE A N   1 
ATOM   2269  C  CA  . PHE A  1 302 ? 60.055  28.097  65.960  1.00 7.65  ? 302  PHE A CA  1 
ATOM   2270  C  C   . PHE A  1 302 ? 59.061  29.242  65.873  1.00 6.66  ? 302  PHE A C   1 
ATOM   2271  O  O   . PHE A  1 302 ? 59.459  30.427  65.911  1.00 5.31  ? 302  PHE A O   1 
ATOM   2272  C  CB  . PHE A  1 302 ? 60.581  27.916  67.427  1.00 7.17  ? 302  PHE A CB  1 
ATOM   2273  C  CG  . PHE A  1 302 ? 59.468  27.862  68.402  1.00 6.75  ? 302  PHE A CG  1 
ATOM   2274  C  CD1 . PHE A  1 302 ? 58.777  26.677  68.588  1.00 7.34  ? 302  PHE A CD1 1 
ATOM   2275  C  CD2 . PHE A  1 302 ? 59.009  29.048  69.011  1.00 9.10  ? 302  PHE A CD2 1 
ATOM   2276  C  CE1 . PHE A  1 302 ? 57.709  26.627  69.478  1.00 7.46  ? 302  PHE A CE1 1 
ATOM   2277  C  CE2 . PHE A  1 302 ? 57.963  29.056  69.854  1.00 8.09  ? 302  PHE A CE2 1 
ATOM   2278  C  CZ  . PHE A  1 302 ? 57.256  27.833  70.086  1.00 7.00  ? 302  PHE A CZ  1 
ATOM   2279  N  N   . ILE A  1 303 ? 57.787  28.896  65.662  1.00 6.03  ? 303  ILE A N   1 
ATOM   2280  C  CA  . ILE A  1 303 ? 56.724  29.901  65.597  1.00 5.89  ? 303  ILE A CA  1 
ATOM   2281  C  C   . ILE A  1 303 ? 55.676  29.683  66.672  1.00 6.54  ? 303  ILE A C   1 
ATOM   2282  O  O   . ILE A  1 303 ? 54.933  28.675  66.624  1.00 7.43  ? 303  ILE A O   1 
ATOM   2283  C  CB  . ILE A  1 303 ? 56.047  29.906  64.200  1.00 5.32  ? 303  ILE A CB  1 
ATOM   2284  C  CG1 . ILE A  1 303 ? 57.062  30.010  63.054  1.00 6.92  ? 303  ILE A CG1 1 
ATOM   2285  C  CG2 . ILE A  1 303 ? 55.055  31.045  64.085  1.00 6.08  ? 303  ILE A CG2 1 
ATOM   2286  C  CD1 . ILE A  1 303 ? 57.675  28.723  62.609  1.00 7.65  ? 303  ILE A CD1 1 
ATOM   2287  N  N   . PRO A  1 304 ? 55.532  30.634  67.595  1.00 7.73  ? 304  PRO A N   1 
ATOM   2288  C  CA  . PRO A  1 304 ? 54.472  30.547  68.596  1.00 8.40  ? 304  PRO A CA  1 
ATOM   2289  C  C   . PRO A  1 304 ? 53.070  30.460  67.912  1.00 8.34  ? 304  PRO A C   1 
ATOM   2290  O  O   . PRO A  1 304 ? 52.816  31.017  66.823  1.00 6.74  ? 304  PRO A O   1 
ATOM   2291  C  CB  . PRO A  1 304 ? 54.578  31.888  69.353  1.00 8.68  ? 304  PRO A CB  1 
ATOM   2292  C  CG  . PRO A  1 304 ? 55.936  32.398  69.076  1.00 10.69 ? 304  PRO A CG  1 
ATOM   2293  C  CD  . PRO A  1 304 ? 56.286  31.909  67.684  1.00 8.56  ? 304  PRO A CD  1 
ATOM   2294  N  N   . GLY A  1 305 ? 52.140  29.773  68.571  1.00 7.64  ? 305  GLY A N   1 
ATOM   2295  C  CA  . GLY A  1 305 ? 50.771  29.868  68.126  1.00 8.16  ? 305  GLY A CA  1 
ATOM   2296  C  C   . GLY A  1 305 ? 50.316  31.312  68.093  1.00 7.82  ? 305  GLY A C   1 
ATOM   2297  O  O   . GLY A  1 305 ? 50.713  32.097  68.933  1.00 6.65  ? 305  GLY A O   1 
ATOM   2298  N  N   . GLY A  1 306 ? 49.460  31.656  67.148  1.00 7.12  ? 306  GLY A N   1 
ATOM   2299  C  CA  . GLY A  1 306 ? 48.892  32.995  67.098  1.00 7.23  ? 306  GLY A CA  1 
ATOM   2300  C  C   . GLY A  1 306 ? 49.848  33.992  66.439  1.00 7.61  ? 306  GLY A C   1 
ATOM   2301  O  O   . GLY A  1 306 ? 49.493  35.176  66.312  1.00 8.61  ? 306  GLY A O   1 
ATOM   2302  N  N   . VAL A  1 307 ? 51.030  33.542  65.997  1.00 6.59  ? 307  VAL A N   1 
ATOM   2303  C  CA  . VAL A  1 307 ? 51.968  34.468  65.333  1.00 6.39  ? 307  VAL A CA  1 
ATOM   2304  C  C   . VAL A  1 307 ? 51.978  34.218  63.807  1.00 6.07  ? 307  VAL A C   1 
ATOM   2305  O  O   . VAL A  1 307 ? 52.128  33.078  63.363  1.00 6.82  ? 307  VAL A O   1 
ATOM   2306  C  CB  . VAL A  1 307 ? 53.404  34.370  65.946  1.00 6.37  ? 307  VAL A CB  1 
ATOM   2307  C  CG1 . VAL A  1 307 ? 54.451  35.142  65.057  1.00 4.95  ? 307  VAL A CG1 1 
ATOM   2308  C  CG2 . VAL A  1 307 ? 53.447  34.938  67.377  1.00 4.22  ? 307  VAL A CG2 1 
ATOM   2309  N  N   . GLU A  1 308 ? 51.858  35.268  63.022  1.00 6.37  ? 308  GLU A N   1 
ATOM   2310  C  CA  . GLU A  1 308 ? 51.784  35.138  61.560  1.00 6.66  ? 308  GLU A CA  1 
ATOM   2311  C  C   . GLU A  1 308 ? 53.146  34.801  61.000  1.00 7.04  ? 308  GLU A C   1 
ATOM   2312  O  O   . GLU A  1 308 ? 54.163  35.375  61.431  1.00 6.51  ? 308  GLU A O   1 
ATOM   2313  C  CB  . GLU A  1 308 ? 51.405  36.477  60.895  1.00 8.54  ? 308  GLU A CB  1 
ATOM   2314  C  CG  . GLU A  1 308 ? 50.036  36.992  61.140  1.00 12.96 ? 308  GLU A CG  1 
ATOM   2315  C  CD  . GLU A  1 308 ? 49.727  38.240  60.288  1.00 22.55 ? 308  GLU A CD  1 
ATOM   2316  O  OE1 . GLU A  1 308 ? 50.400  39.296  60.432  1.00 27.35 ? 308  GLU A OE1 1 
ATOM   2317  O  OE2 . GLU A  1 308 ? 48.803  38.180  59.450  1.00 23.54 ? 308  GLU A OE2 1 
ATOM   2318  N  N   . PHE A  1 309 ? 53.178  33.916  60.015  1.00 5.41  ? 309  PHE A N   1 
ATOM   2319  C  CA  . PHE A  1 309 ? 54.438  33.663  59.310  1.00 8.26  ? 309  PHE A CA  1 
ATOM   2320  C  C   . PHE A  1 309 ? 54.257  33.217  57.849  1.00 8.97  ? 309  PHE A C   1 
ATOM   2321  O  O   . PHE A  1 309 ? 53.196  32.705  57.472  1.00 9.56  ? 309  PHE A O   1 
ATOM   2322  C  CB  . PHE A  1 309 ? 55.309  32.655  60.059  1.00 7.10  ? 309  PHE A CB  1 
ATOM   2323  C  CG  . PHE A  1 309 ? 54.795  31.212  60.013  1.00 7.85  ? 309  PHE A CG  1 
ATOM   2324  C  CD1 . PHE A  1 309 ? 53.696  30.813  60.771  1.00 7.40  ? 309  PHE A CD1 1 
ATOM   2325  C  CD2 . PHE A  1 309 ? 55.461  30.268  59.233  1.00 9.68  ? 309  PHE A CD2 1 
ATOM   2326  C  CE1 . PHE A  1 309 ? 53.261  29.500  60.784  1.00 13.20 ? 309  PHE A CE1 1 
ATOM   2327  C  CE2 . PHE A  1 309 ? 55.007  28.907  59.211  1.00 12.07 ? 309  PHE A CE2 1 
ATOM   2328  C  CZ  . PHE A  1 309 ? 53.918  28.532  60.002  1.00 12.99 ? 309  PHE A CZ  1 
ATOM   2329  N  N   . LYS A  1 310 ? 55.312  33.391  57.065  1.00 9.03  ? 310  LYS A N   1 
ATOM   2330  C  CA  . LYS A  1 310 ? 55.353  32.934  55.681  1.00 9.32  ? 310  LYS A CA  1 
ATOM   2331  C  C   . LYS A  1 310 ? 56.608  32.114  55.606  1.00 9.92  ? 310  LYS A C   1 
ATOM   2332  O  O   . LYS A  1 310 ? 57.633  32.408  56.305  1.00 9.07  ? 310  LYS A O   1 
ATOM   2333  C  CB  . LYS A  1 310 ? 55.539  34.110  54.682  1.00 9.48  ? 310  LYS A CB  1 
ATOM   2334  C  CG  . LYS A  1 310 ? 54.441  35.143  54.673  1.00 14.22 ? 310  LYS A CG  1 
ATOM   2335  C  CD  . LYS A  1 310 ? 54.680  36.132  53.503  1.00 13.15 ? 310  LYS A CD  1 
ATOM   2336  C  CE  . LYS A  1 310 ? 53.589  37.206  53.439  1.00 20.12 ? 310  LYS A CE  1 
ATOM   2337  N  NZ  . LYS A  1 310 ? 54.116  38.399  52.650  1.00 20.89 ? 310  LYS A NZ  1 
ATOM   2338  N  N   . TYR A  1 311 ? 56.550  31.055  54.799  1.00 7.99  ? 311  TYR A N   1 
ATOM   2339  C  CA  . TYR A  1 311 ? 57.794  30.399  54.437  1.00 7.89  ? 311  TYR A CA  1 
ATOM   2340  C  C   . TYR A  1 311 ? 57.745  30.025  52.938  1.00 7.97  ? 311  TYR A C   1 
ATOM   2341  O  O   . TYR A  1 311 ? 56.660  29.847  52.345  1.00 7.36  ? 311  TYR A O   1 
ATOM   2342  C  CB  . TYR A  1 311 ? 58.011  29.144  55.288  1.00 8.78  ? 311  TYR A CB  1 
ATOM   2343  C  CG  . TYR A  1 311 ? 56.986  28.065  54.927  1.00 7.62  ? 311  TYR A CG  1 
ATOM   2344  C  CD1 . TYR A  1 311 ? 55.694  28.106  55.470  1.00 6.40  ? 311  TYR A CD1 1 
ATOM   2345  C  CD2 . TYR A  1 311 ? 57.308  27.049  54.023  1.00 8.08  ? 311  TYR A CD2 1 
ATOM   2346  C  CE1 . TYR A  1 311 ? 54.702  27.127  55.108  1.00 10.09 ? 311  TYR A CE1 1 
ATOM   2347  C  CE2 . TYR A  1 311 ? 56.337  26.045  53.661  1.00 7.77  ? 311  TYR A CE2 1 
ATOM   2348  C  CZ  . TYR A  1 311 ? 55.046  26.114  54.222  1.00 8.65  ? 311  TYR A CZ  1 
ATOM   2349  O  OH  . TYR A  1 311 ? 54.121  25.171  53.852  1.00 8.95  ? 311  TYR A OH  1 
ATOM   2350  N  N   . TYR A  1 312 ? 58.907  29.837  52.336  1.00 6.21  ? 312  TYR A N   1 
ATOM   2351  C  CA  . TYR A  1 312 ? 58.992  29.351  50.964  1.00 7.58  ? 312  TYR A CA  1 
ATOM   2352  C  C   . TYR A  1 312 ? 60.402  28.796  50.747  1.00 8.49  ? 312  TYR A C   1 
ATOM   2353  O  O   . TYR A  1 312 ? 61.335  29.119  51.505  1.00 8.48  ? 312  TYR A O   1 
ATOM   2354  C  CB  . TYR A  1 312 ? 58.709  30.463  49.941  1.00 8.35  ? 312  TYR A CB  1 
ATOM   2355  C  CG  . TYR A  1 312 ? 59.727  31.586  49.960  1.00 8.81  ? 312  TYR A CG  1 
ATOM   2356  C  CD1 . TYR A  1 312 ? 60.917  31.496  49.210  1.00 9.26  ? 312  TYR A CD1 1 
ATOM   2357  C  CD2 . TYR A  1 312 ? 59.513  32.723  50.704  1.00 10.72 ? 312  TYR A CD2 1 
ATOM   2358  C  CE1 . TYR A  1 312 ? 61.852  32.551  49.214  1.00 11.38 ? 312  TYR A CE1 1 
ATOM   2359  C  CE2 . TYR A  1 312 ? 60.453  33.789  50.707  1.00 9.92  ? 312  TYR A CE2 1 
ATOM   2360  C  CZ  . TYR A  1 312 ? 61.594  33.686  49.944  1.00 9.53  ? 312  TYR A CZ  1 
ATOM   2361  O  OH  . TYR A  1 312 ? 62.533  34.708  49.969  1.00 14.51 ? 312  TYR A OH  1 
ATOM   2362  N  N   . SER A  1 313 ? 60.543  27.955  49.725  1.00 8.84  ? 313  SER A N   1 
ATOM   2363  C  CA  . SER A  1 313 ? 61.827  27.314  49.439  1.00 8.79  ? 313  SER A CA  1 
ATOM   2364  C  C   . SER A  1 313 ? 62.588  28.140  48.400  1.00 8.84  ? 313  SER A C   1 
ATOM   2365  O  O   . SER A  1 313 ? 62.075  28.460  47.314  1.00 8.81  ? 313  SER A O   1 
ATOM   2366  C  CB  . SER A  1 313 ? 61.624  25.868  48.961  1.00 9.75  ? 313  SER A CB  1 
ATOM   2367  O  OG  . SER A  1 313 ? 62.880  25.326  48.530  1.00 10.49 ? 313  SER A OG  1 
ATOM   2368  N  N   . GLU A  1 314 ? 63.817  28.533  48.733  1.00 8.27  ? 314  GLU A N   1 
ATOM   2369  C  CA  . GLU A  1 314 ? 64.610  29.267  47.768  1.00 8.03  ? 314  GLU A CA  1 
ATOM   2370  C  C   . GLU A  1 314 ? 65.337  28.207  46.919  1.00 7.90  ? 314  GLU A C   1 
ATOM   2371  O  O   . GLU A  1 314 ? 65.628  28.414  45.742  1.00 7.63  ? 314  GLU A O   1 
ATOM   2372  C  CB  . GLU A  1 314 ? 65.572  30.188  48.531  1.00 9.30  ? 314  GLU A CB  1 
ATOM   2373  C  CG  . GLU A  1 314 ? 66.501  30.973  47.654  1.00 15.73 ? 314  GLU A CG  1 
ATOM   2374  C  CD  . GLU A  1 314 ? 65.788  32.097  46.932  1.00 20.32 ? 314  GLU A CD  1 
ATOM   2375  O  OE1 . GLU A  1 314 ? 64.732  32.536  47.413  1.00 18.72 ? 314  GLU A OE1 1 
ATOM   2376  O  OE2 . GLU A  1 314 ? 66.311  32.544  45.891  1.00 25.05 ? 314  GLU A OE2 1 
ATOM   2377  N  N   . ALA A  1 315 ? 65.588  27.038  47.509  1.00 5.70  ? 315  ALA A N   1 
ATOM   2378  C  CA  . ALA A  1 315 ? 66.166  25.949  46.723  1.00 6.49  ? 315  ALA A CA  1 
ATOM   2379  C  C   . ALA A  1 315 ? 65.057  25.339  45.861  1.00 6.86  ? 315  ALA A C   1 
ATOM   2380  O  O   . ALA A  1 315 ? 63.878  25.371  46.224  1.00 7.27  ? 315  ALA A O   1 
ATOM   2381  C  CB  . ALA A  1 315 ? 66.774  24.870  47.628  1.00 6.50  ? 315  ALA A CB  1 
ATOM   2382  N  N   . TYR A  1 316 ? 65.441  24.802  44.715  1.00 7.06  ? 316  TYR A N   1 
ATOM   2383  C  CA  . TYR A  1 316 ? 64.506  24.111  43.842  1.00 7.16  ? 316  TYR A CA  1 
ATOM   2384  C  C   . TYR A  1 316 ? 63.729  22.945  44.458  1.00 7.89  ? 316  TYR A C   1 
ATOM   2385  O  O   . TYR A  1 316 ? 62.569  22.694  44.039  1.00 8.83  ? 316  TYR A O   1 
ATOM   2386  C  CB  . TYR A  1 316 ? 65.228  23.670  42.565  1.00 5.16  ? 316  TYR A CB  1 
ATOM   2387  C  CG  . TYR A  1 316 ? 65.546  24.835  41.658  1.00 6.01  ? 316  TYR A CG  1 
ATOM   2388  C  CD1 . TYR A  1 316 ? 64.557  25.760  41.266  1.00 2.96  ? 316  TYR A CD1 1 
ATOM   2389  C  CD2 . TYR A  1 316 ? 66.835  25.013  41.177  1.00 4.22  ? 316  TYR A CD2 1 
ATOM   2390  C  CE1 . TYR A  1 316 ? 64.876  26.800  40.407  1.00 3.96  ? 316  TYR A CE1 1 
ATOM   2391  C  CE2 . TYR A  1 316 ? 67.157  26.033  40.321  1.00 4.44  ? 316  TYR A CE2 1 
ATOM   2392  C  CZ  . TYR A  1 316 ? 66.174  26.923  39.946  1.00 6.58  ? 316  TYR A CZ  1 
ATOM   2393  O  OH  . TYR A  1 316 ? 66.566  27.912  39.129  1.00 5.57  ? 316  TYR A OH  1 
ATOM   2394  N  N   . PHE A  1 317 ? 64.350  22.254  45.429  1.00 7.97  ? 317  PHE A N   1 
ATOM   2395  C  CA  . PHE A  1 317 ? 63.686  21.249  46.278  1.00 7.57  ? 317  PHE A CA  1 
ATOM   2396  C  C   . PHE A  1 317 ? 64.236  21.416  47.703  1.00 8.49  ? 317  PHE A C   1 
ATOM   2397  O  O   . PHE A  1 317 ? 65.466  21.560  47.881  1.00 9.49  ? 317  PHE A O   1 
ATOM   2398  C  CB  . PHE A  1 317 ? 63.977  19.858  45.759  1.00 8.00  ? 317  PHE A CB  1 
ATOM   2399  C  CG  . PHE A  1 317 ? 63.417  18.726  46.600  1.00 8.95  ? 317  PHE A CG  1 
ATOM   2400  C  CD1 . PHE A  1 317 ? 64.171  18.182  47.669  1.00 9.86  ? 317  PHE A CD1 1 
ATOM   2401  C  CD2 . PHE A  1 317 ? 62.188  18.146  46.277  1.00 10.16 ? 317  PHE A CD2 1 
ATOM   2402  C  CE1 . PHE A  1 317 ? 63.704  17.124  48.396  1.00 8.51  ? 317  PHE A CE1 1 
ATOM   2403  C  CE2 . PHE A  1 317 ? 61.676  17.098  47.023  1.00 10.17 ? 317  PHE A CE2 1 
ATOM   2404  C  CZ  . PHE A  1 317 ? 62.415  16.580  48.082  1.00 9.26  ? 317  PHE A CZ  1 
ATOM   2405  N  N   . SER A  1 318 ? 63.350  21.504  48.697  1.00 6.12  ? 318  SER A N   1 
ATOM   2406  C  CA  . SER A  1 318 ? 63.763  21.485  50.104  1.00 6.68  ? 318  SER A CA  1 
ATOM   2407  C  C   . SER A  1 318 ? 62.895  20.445  50.837  1.00 7.66  ? 318  SER A C   1 
ATOM   2408  O  O   . SER A  1 318 ? 61.785  20.100  50.344  1.00 8.17  ? 318  SER A O   1 
ATOM   2409  C  CB  . SER A  1 318 ? 63.612  22.872  50.764  1.00 6.54  ? 318  SER A CB  1 
ATOM   2410  O  OG  . SER A  1 318 ? 64.428  23.839  50.137  1.00 6.25  ? 318  SER A OG  1 
ATOM   2411  N  N   . LYS A  1 319 ? 63.408  19.863  51.944  1.00 7.33  ? 319  LYS A N   1 
ATOM   2412  C  CA  . LYS A  1 319 ? 62.612  18.936  52.783  1.00 9.23  ? 319  LYS A CA  1 
ATOM   2413  C  C   . LYS A  1 319 ? 62.878  19.372  54.223  1.00 10.68 ? 319  LYS A C   1 
ATOM   2414  O  O   . LYS A  1 319 ? 64.048  19.648  54.562  1.00 11.42 ? 319  LYS A O   1 
ATOM   2415  C  CB  . LYS A  1 319 ? 63.019  17.456  52.605  1.00 8.66  ? 319  LYS A CB  1 
ATOM   2416  C  CG  . LYS A  1 319 ? 62.213  16.460  53.471  1.00 11.00 ? 319  LYS A CG  1 
ATOM   2417  C  CD  . LYS A  1 319 ? 62.576  14.963  53.204  1.00 10.61 ? 319  LYS A CD  1 
ATOM   2418  C  CE  . LYS A  1 319 ? 63.932  14.653  53.847  1.00 17.25 ? 319  LYS A CE  1 
ATOM   2419  N  NZ  . LYS A  1 319 ? 64.235  13.146  53.693  1.00 11.69 ? 319  LYS A NZ  1 
ATOM   2420  N  N   . VAL A  1 320 ? 61.830  19.451  55.048  1.00 10.17 ? 320  VAL A N   1 
ATOM   2421  C  CA  . VAL A  1 320 ? 62.004  19.904  56.440  1.00 9.14  ? 320  VAL A CA  1 
ATOM   2422  C  C   . VAL A  1 320 ? 61.282  18.862  57.278  1.00 10.22 ? 320  VAL A C   1 
ATOM   2423  O  O   . VAL A  1 320 ? 60.354  18.210  56.772  1.00 9.63  ? 320  VAL A O   1 
ATOM   2424  C  CB  . VAL A  1 320 ? 61.388  21.300  56.743  1.00 10.36 ? 320  VAL A CB  1 
ATOM   2425  C  CG1 . VAL A  1 320 ? 61.976  22.422  55.848  1.00 6.72  ? 320  VAL A CG1 1 
ATOM   2426  C  CG2 . VAL A  1 320 ? 59.840  21.315  56.665  1.00 6.42  ? 320  VAL A CG2 1 
ATOM   2427  N  N   . LEU A  1 321 ? 61.715  18.713  58.536  1.00 9.47  ? 321  LEU A N   1 
ATOM   2428  C  CA  . LEU A  1 321 ? 61.006  17.921  59.530  1.00 9.67  ? 321  LEU A CA  1 
ATOM   2429  C  C   . LEU A  1 321 ? 60.141  18.934  60.287  1.00 9.68  ? 321  LEU A C   1 
ATOM   2430  O  O   . LEU A  1 321 ? 60.639  19.969  60.738  1.00 11.01 ? 321  LEU A O   1 
ATOM   2431  C  CB  . LEU A  1 321 ? 62.036  17.211  60.466  1.00 9.82  ? 321  LEU A CB  1 
ATOM   2432  C  CG  . LEU A  1 321 ? 61.393  16.410  61.598  1.00 10.02 ? 321  LEU A CG  1 
ATOM   2433  C  CD1 . LEU A  1 321 ? 60.661  15.190  61.103  1.00 9.70  ? 321  LEU A CD1 1 
ATOM   2434  C  CD2 . LEU A  1 321 ? 62.509  16.095  62.691  1.00 10.35 ? 321  LEU A CD2 1 
ATOM   2435  N  N   . PHE A  1 322 ? 58.864  18.636  60.416  1.00 8.86  ? 322  PHE A N   1 
ATOM   2436  C  CA  . PHE A  1 322 ? 57.901  19.628  60.829  1.00 8.91  ? 322  PHE A CA  1 
ATOM   2437  C  C   . PHE A  1 322 ? 57.135  19.080  62.014  1.00 10.19 ? 322  PHE A C   1 
ATOM   2438  O  O   . PHE A  1 322 ? 56.608  17.944  61.936  1.00 9.24  ? 322  PHE A O   1 
ATOM   2439  C  CB  . PHE A  1 322 ? 56.908  19.957  59.663  1.00 7.71  ? 322  PHE A CB  1 
ATOM   2440  C  CG  . PHE A  1 322 ? 55.809  20.826  60.118  1.00 10.50 ? 322  PHE A CG  1 
ATOM   2441  C  CD1 . PHE A  1 322 ? 56.010  22.204  60.267  1.00 7.06  ? 322  PHE A CD1 1 
ATOM   2442  C  CD2 . PHE A  1 322 ? 54.641  20.258  60.598  1.00 10.27 ? 322  PHE A CD2 1 
ATOM   2443  C  CE1 . PHE A  1 322 ? 54.994  23.003  60.787  1.00 8.51  ? 322  PHE A CE1 1 
ATOM   2444  C  CE2 . PHE A  1 322 ? 53.663  21.058  61.118  1.00 6.91  ? 322  PHE A CE2 1 
ATOM   2445  C  CZ  . PHE A  1 322 ? 53.861  22.427  61.221  1.00 7.06  ? 322  PHE A CZ  1 
ATOM   2446  N  N   . VAL A  1 323 ? 56.980  19.891  63.073  1.00 9.32  ? 323  VAL A N   1 
ATOM   2447  C  CA  . VAL A  1 323 ? 56.116  19.480  64.217  1.00 8.29  ? 323  VAL A CA  1 
ATOM   2448  C  C   . VAL A  1 323 ? 55.147  20.603  64.566  1.00 8.53  ? 323  VAL A C   1 
ATOM   2449  O  O   . VAL A  1 323 ? 55.528  21.789  64.488  1.00 9.15  ? 323  VAL A O   1 
ATOM   2450  C  CB  . VAL A  1 323 ? 56.986  19.042  65.458  1.00 6.25  ? 323  VAL A CB  1 
ATOM   2451  C  CG1 . VAL A  1 323 ? 57.899  20.224  65.884  1.00 7.22  ? 323  VAL A CG1 1 
ATOM   2452  C  CG2 . VAL A  1 323 ? 56.128  18.554  66.649  1.00 5.42  ? 323  VAL A CG2 1 
ATOM   2453  N  N   . SER A  1 324 ? 53.901  20.240  64.918  1.00 8.65  ? 324  SER A N   1 
ATOM   2454  C  CA  . SER A  1 324 ? 52.889  21.212  65.319  1.00 9.10  ? 324  SER A CA  1 
ATOM   2455  C  C   . SER A  1 324 ? 52.114  20.723  66.539  1.00 8.63  ? 324  SER A C   1 
ATOM   2456  O  O   . SER A  1 324 ? 51.760  19.518  66.606  1.00 8.08  ? 324  SER A O   1 
ATOM   2457  C  CB  . SER A  1 324 ? 51.864  21.349  64.201  1.00 8.41  ? 324  SER A CB  1 
ATOM   2458  O  OG  . SER A  1 324 ? 50.766  22.115  64.675  1.00 13.03 ? 324  SER A OG  1 
ATOM   2459  N  N   . SER A  1 325 ? 51.827  21.629  67.471  1.00 7.18  ? 325  SER A N   1 
ATOM   2460  C  CA  . SER A  1 325 ? 50.923  21.393  68.595  1.00 8.07  ? 325  SER A CA  1 
ATOM   2461  C  C   . SER A  1 325 ? 49.505  21.623  68.079  1.00 8.68  ? 325  SER A C   1 
ATOM   2462  O  O   . SER A  1 325 ? 49.243  22.663  67.425  1.00 9.33  ? 325  SER A O   1 
ATOM   2463  C  CB  . SER A  1 325 ? 51.231  22.389  69.762  1.00 7.27  ? 325  SER A CB  1 
ATOM   2464  O  OG  . SER A  1 325 ? 50.259  22.254  70.834  1.00 9.59  ? 325  SER A OG  1 
ATOM   2465  N  N   . GLY A  1 326 ? 48.579  20.697  68.360  1.00 9.88  ? 326  GLY A N   1 
ATOM   2466  C  CA  . GLY A  1 326 ? 47.237  20.814  67.819  1.00 9.61  ? 326  GLY A CA  1 
ATOM   2467  C  C   . GLY A  1 326 ? 46.956  19.737  66.785  1.00 11.59 ? 326  GLY A C   1 
ATOM   2468  O  O   . GLY A  1 326 ? 47.846  18.966  66.374  1.00 11.98 ? 326  GLY A O   1 
ATOM   2469  N  N   . SER A  1 327 ? 45.708  19.642  66.369  1.00 12.08 ? 327  SER A N   1 
ATOM   2470  C  CA  . SER A  1 327 ? 45.381  18.612  65.401  1.00 13.97 ? 327  SER A CA  1 
ATOM   2471  C  C   . SER A  1 327 ? 45.328  19.224  63.972  1.00 13.83 ? 327  SER A C   1 
ATOM   2472  O  O   . SER A  1 327 ? 45.230  18.491  63.005  1.00 15.50 ? 327  SER A O   1 
ATOM   2473  C  CB  . SER A  1 327 ? 44.084  17.924  65.796  1.00 12.59 ? 327  SER A CB  1 
ATOM   2474  O  OG  . SER A  1 327 ? 43.054  18.904  65.828  1.00 17.79 ? 327  SER A OG  1 
ATOM   2475  N  N   . ASP A  1 328 ? 45.465  20.551  63.851  1.00 13.97 ? 328  ASP A N   1 
ATOM   2476  C  CA  . ASP A  1 328 ? 45.221  21.225  62.577  1.00 13.97 ? 328  ASP A CA  1 
ATOM   2477  C  C   . ASP A  1 328 ? 46.345  22.155  62.158  1.00 12.00 ? 328  ASP A C   1 
ATOM   2478  O  O   . ASP A  1 328 ? 46.100  23.273  61.662  1.00 10.90 ? 328  ASP A O   1 
ATOM   2479  C  CB  . ASP A  1 328 ? 43.948  22.085  62.684  1.00 15.56 ? 328  ASP A CB  1 
ATOM   2480  C  CG  . ASP A  1 328 ? 42.715  21.274  62.890  1.00 22.99 ? 328  ASP A CG  1 
ATOM   2481  O  OD1 . ASP A  1 328 ? 42.638  20.161  62.305  1.00 31.60 ? 328  ASP A OD1 1 
ATOM   2482  O  OD2 . ASP A  1 328 ? 41.752  21.688  63.606  1.00 32.00 ? 328  ASP A OD2 1 
ATOM   2483  N  N   . GLY A  1 329 ? 47.574  21.712  62.358  1.00 10.56 ? 329  GLY A N   1 
ATOM   2484  C  CA  . GLY A  1 329 ? 48.716  22.520  61.976  1.00 10.21 ? 329  GLY A CA  1 
ATOM   2485  C  C   . GLY A  1 329 ? 48.979  22.440  60.490  1.00 9.76  ? 329  GLY A C   1 
ATOM   2486  O  O   . GLY A  1 329 ? 48.212  21.817  59.712  1.00 7.07  ? 329  GLY A O   1 
ATOM   2487  N  N   . LEU A  1 330 ? 50.094  23.064  60.107  1.00 9.49  ? 330  LEU A N   1 
ATOM   2488  C  CA  . LEU A  1 330 ? 50.468  23.225  58.700  1.00 8.34  ? 330  LEU A CA  1 
ATOM   2489  C  C   . LEU A  1 330 ? 50.424  21.912  57.912  1.00 8.69  ? 330  LEU A C   1 
ATOM   2490  O  O   . LEU A  1 330 ? 49.773  21.870  56.882  1.00 9.47  ? 330  LEU A O   1 
ATOM   2491  C  CB  . LEU A  1 330 ? 51.861  23.856  58.614  1.00 8.42  ? 330  LEU A CB  1 
ATOM   2492  C  CG  . LEU A  1 330 ? 52.469  23.997  57.213  1.00 9.81  ? 330  LEU A CG  1 
ATOM   2493  C  CD1 . LEU A  1 330 ? 51.598  24.987  56.366  1.00 7.51  ? 330  LEU A CD1 1 
ATOM   2494  C  CD2 . LEU A  1 330 ? 53.935  24.494  57.292  1.00 10.14 ? 330  LEU A CD2 1 
ATOM   2495  N  N   . ASP A  1 331 ? 51.091  20.850  58.385  1.00 8.20  ? 331  ASP A N   1 
ATOM   2496  C  CA  . ASP A  1 331 ? 51.103  19.602  57.628  1.00 8.52  ? 331  ASP A CA  1 
ATOM   2497  C  C   . ASP A  1 331 ? 49.722  19.064  57.372  1.00 8.77  ? 331  ASP A C   1 
ATOM   2498  O  O   . ASP A  1 331 ? 49.389  18.774  56.246  1.00 8.37  ? 331  ASP A O   1 
ATOM   2499  C  CB  . ASP A  1 331 ? 52.074  18.537  58.200  1.00 8.13  ? 331  ASP A CB  1 
ATOM   2500  C  CG  . ASP A  1 331 ? 51.759  18.169  59.630  1.00 8.23  ? 331  ASP A CG  1 
ATOM   2501  O  OD1 . ASP A  1 331 ? 50.935  18.855  60.274  1.00 7.95  ? 331  ASP A OD1 1 
ATOM   2502  O  OD2 . ASP A  1 331 ? 52.290  17.189  60.198  1.00 13.93 ? 331  ASP A OD2 1 
ATOM   2503  N  N   . GLN A  1 332 ? 48.859  19.038  58.394  1.00 9.15  ? 332  GLN A N   1 
ATOM   2504  C  CA  . GLN A  1 332 ? 47.509  18.532  58.213  1.00 10.82 ? 332  GLN A CA  1 
ATOM   2505  C  C   . GLN A  1 332 ? 46.637  19.424  57.305  1.00 10.10 ? 332  GLN A C   1 
ATOM   2506  O  O   . GLN A  1 332 ? 45.799  18.946  56.519  1.00 9.18  ? 332  GLN A O   1 
ATOM   2507  C  CB  . GLN A  1 332 ? 46.841  18.385  59.599  1.00 10.93 ? 332  GLN A CB  1 
ATOM   2508  C  CG  . GLN A  1 332 ? 45.487  17.696  59.514  1.00 17.77 ? 332  GLN A CG  1 
ATOM   2509  C  CD  . GLN A  1 332 ? 45.668  16.254  59.101  1.00 21.52 ? 332  GLN A CD  1 
ATOM   2510  O  OE1 . GLN A  1 332 ? 44.954  15.757  58.227  1.00 26.96 ? 332  GLN A OE1 1 
ATOM   2511  N  NE2 . GLN A  1 332 ? 46.670  15.610  59.664  1.00 19.44 ? 332  GLN A NE2 1 
ATOM   2512  N  N   . ASN A  1 333 ? 46.828  20.724  57.412  1.00 9.72  ? 333  ASN A N   1 
ATOM   2513  C  CA  . ASN A  1 333 ? 46.160  21.676  56.534  1.00 8.05  ? 333  ASN A CA  1 
ATOM   2514  C  C   . ASN A  1 333 ? 46.555  21.370  55.075  1.00 8.28  ? 333  ASN A C   1 
ATOM   2515  O  O   . ASN A  1 333 ? 45.693  21.280  54.201  1.00 8.53  ? 333  ASN A O   1 
ATOM   2516  C  CB  . ASN A  1 333 ? 46.627  23.134  56.906  1.00 9.00  ? 333  ASN A CB  1 
ATOM   2517  C  CG  A ASN A  1 333 ? 45.574  23.961  57.614  0.50 8.90  ? 333  ASN A CG  1 
ATOM   2518  C  CG  B ASN A  1 333 ? 45.836  24.199  56.218  0.50 2.00  ? 333  ASN A CG  1 
ATOM   2519  O  OD1 A ASN A  1 333 ? 44.770  24.715  56.994  0.50 12.31 ? 333  ASN A OD1 1 
ATOM   2520  O  OD1 B ASN A  1 333 ? 45.896  24.309  55.015  0.50 4.59  ? 333  ASN A OD1 1 
ATOM   2521  N  ND2 A ASN A  1 333 ? 45.585  23.871  58.929  0.50 10.18 ? 333  ASN A ND2 1 
ATOM   2522  N  ND2 B ASN A  1 333 ? 45.095  25.019  56.985  0.50 7.73  ? 333  ASN A ND2 1 
ATOM   2523  N  N   . LEU A  1 334 ? 47.858  21.176  54.803  1.00 7.47  ? 334  LEU A N   1 
ATOM   2524  C  CA  . LEU A  1 334 ? 48.284  20.891  53.420  1.00 6.25  ? 334  LEU A CA  1 
ATOM   2525  C  C   . LEU A  1 334 ? 47.736  19.522  52.952  1.00 6.66  ? 334  LEU A C   1 
ATOM   2526  O  O   . LEU A  1 334 ? 47.370  19.364  51.795  1.00 6.77  ? 334  LEU A O   1 
ATOM   2527  C  CB  . LEU A  1 334 ? 49.816  20.905  53.276  1.00 5.35  ? 334  LEU A CB  1 
ATOM   2528  C  CG  . LEU A  1 334 ? 50.448  22.292  53.554  1.00 5.02  ? 334  LEU A CG  1 
ATOM   2529  C  CD1 . LEU A  1 334 ? 51.976  22.224  53.662  1.00 6.59  ? 334  LEU A CD1 1 
ATOM   2530  C  CD2 . LEU A  1 334 ? 50.010  23.338  52.481  1.00 6.12  ? 334  LEU A CD2 1 
ATOM   2531  N  N   . VAL A  1 335 ? 47.690  18.545  53.852  1.00 7.40  ? 335  VAL A N   1 
ATOM   2532  C  CA  . VAL A  1 335 ? 47.122  17.226  53.508  1.00 7.82  ? 335  VAL A CA  1 
ATOM   2533  C  C   . VAL A  1 335 ? 45.680  17.402  53.135  1.00 8.20  ? 335  VAL A C   1 
ATOM   2534  O  O   . VAL A  1 335 ? 45.240  16.972  52.041  1.00 7.86  ? 335  VAL A O   1 
ATOM   2535  C  CB  . VAL A  1 335 ? 47.232  16.227  54.688  1.00 8.85  ? 335  VAL A CB  1 
ATOM   2536  C  CG1 . VAL A  1 335 ? 46.411  14.936  54.427  1.00 7.29  ? 335  VAL A CG1 1 
ATOM   2537  C  CG2 . VAL A  1 335 ? 48.686  15.887  54.916  1.00 6.53  ? 335  VAL A CG2 1 
ATOM   2538  N  N   . ASN A  1 336 ? 44.932  18.044  54.021  1.00 6.64  ? 336  ASN A N   1 
ATOM   2539  C  CA  . ASN A  1 336 ? 43.509  18.176  53.795  1.00 8.19  ? 336  ASN A CA  1 
ATOM   2540  C  C   . ASN A  1 336 ? 43.193  18.902  52.501  1.00 8.56  ? 336  ASN A C   1 
ATOM   2541  O  O   . ASN A  1 336 ? 42.162  18.630  51.862  1.00 7.90  ? 336  ASN A O   1 
ATOM   2542  C  CB  . ASN A  1 336 ? 42.840  18.924  54.959  1.00 8.96  ? 336  ASN A CB  1 
ATOM   2543  C  CG  . ASN A  1 336 ? 42.775  18.104  56.244  1.00 12.28 ? 336  ASN A CG  1 
ATOM   2544  O  OD1 . ASN A  1 336 ? 42.955  16.884  56.249  1.00 20.15 ? 336  ASN A OD1 1 
ATOM   2545  N  ND2 . ASN A  1 336 ? 42.463  18.769  57.329  1.00 18.26 ? 336  ASN A ND2 1 
ATOM   2546  N  N   . GLY A  1 337 ? 44.005  19.909  52.176  1.00 8.04  ? 337  GLY A N   1 
ATOM   2547  C  CA  . GLY A  1 337 ? 43.832  20.627  50.926  1.00 8.04  ? 337  GLY A CA  1 
ATOM   2548  C  C   . GLY A  1 337 ? 44.448  19.963  49.672  1.00 8.58  ? 337  GLY A C   1 
ATOM   2549  O  O   . GLY A  1 337 ? 44.280  20.504  48.585  1.00 8.74  ? 337  GLY A O   1 
ATOM   2550  N  N   . GLY A  1 338 ? 45.117  18.809  49.802  1.00 8.78  ? 338  GLY A N   1 
ATOM   2551  C  CA  . GLY A  1 338 ? 45.832  18.158  48.689  1.00 8.74  ? 338  GLY A CA  1 
ATOM   2552  C  C   . GLY A  1 338 ? 45.216  16.801  48.311  1.00 9.73  ? 338  GLY A C   1 
ATOM   2553  O  O   . GLY A  1 338 ? 44.008  16.599  48.448  1.00 9.31  ? 338  GLY A O   1 
ATOM   2554  N  N   . GLU A  1 339 ? 46.037  15.886  47.819  1.00 9.46  ? 339  GLU A N   1 
ATOM   2555  C  CA  . GLU A  1 339 ? 45.543  14.607  47.288  1.00 10.26 ? 339  GLU A CA  1 
ATOM   2556  C  C   . GLU A  1 339 ? 46.615  13.588  47.666  1.00 9.68  ? 339  GLU A C   1 
ATOM   2557  O  O   . GLU A  1 339 ? 47.768  13.945  47.874  1.00 9.67  ? 339  GLU A O   1 
ATOM   2558  C  CB  . GLU A  1 339 ? 45.389  14.653  45.741  1.00 10.11 ? 339  GLU A CB  1 
ATOM   2559  C  CG  . GLU A  1 339 ? 46.747  14.892  45.010  1.00 12.85 ? 339  GLU A CG  1 
ATOM   2560  C  CD  . GLU A  1 339 ? 46.610  15.188  43.499  1.00 19.29 ? 339  GLU A CD  1 
ATOM   2561  O  OE1 . GLU A  1 339 ? 45.892  14.441  42.797  1.00 19.23 ? 339  GLU A OE1 1 
ATOM   2562  O  OE2 . GLU A  1 339 ? 47.178  16.192  43.004  1.00 18.23 ? 339  GLU A OE2 1 
ATOM   2563  N  N   . GLU A  1 340 ? 46.224  12.337  47.750  1.00 8.35  ? 340  GLU A N   1 
ATOM   2564  C  CA  . GLU A  1 340 ? 47.167  11.217  47.859  1.00 9.80  ? 340  GLU A CA  1 
ATOM   2565  C  C   . GLU A  1 340 ? 48.180  11.279  46.721  1.00 8.68  ? 340  GLU A C   1 
ATOM   2566  O  O   . GLU A  1 340 ? 47.845  11.647  45.603  1.00 6.41  ? 340  GLU A O   1 
ATOM   2567  C  CB  . GLU A  1 340 ? 46.378  9.893   47.726  1.00 9.24  ? 340  GLU A CB  1 
ATOM   2568  C  CG  . GLU A  1 340 ? 45.843  9.517   49.099  1.00 15.86 ? 340  GLU A CG  1 
ATOM   2569  C  CD  . GLU A  1 340 ? 44.813  8.380   49.107  1.00 23.62 ? 340  GLU A CD  1 
ATOM   2570  O  OE1 . GLU A  1 340 ? 44.653  7.680   48.071  1.00 25.06 ? 340  GLU A OE1 1 
ATOM   2571  O  OE2 . GLU A  1 340 ? 44.124  8.237   50.147  1.00 24.22 ? 340  GLU A OE2 1 
ATOM   2572  N  N   . TRP A  1 341 ? 49.413  10.897  46.994  1.00 8.06  ? 341  TRP A N   1 
ATOM   2573  C  CA  . TRP A  1 341 ? 50.441  11.083  46.004  1.00 9.59  ? 341  TRP A CA  1 
ATOM   2574  C  C   . TRP A  1 341 ? 51.458  9.997   46.170  1.00 9.79  ? 341  TRP A C   1 
ATOM   2575  O  O   . TRP A  1 341 ? 51.826  9.653   47.298  1.00 10.98 ? 341  TRP A O   1 
ATOM   2576  C  CB  . TRP A  1 341 ? 51.095  12.429  46.267  1.00 9.84  ? 341  TRP A CB  1 
ATOM   2577  C  CG  . TRP A  1 341 ? 52.151  12.805  45.231  1.00 10.81 ? 341  TRP A CG  1 
ATOM   2578  C  CD1 . TRP A  1 341 ? 53.474  13.052  45.460  1.00 9.75  ? 341  TRP A CD1 1 
ATOM   2579  C  CD2 . TRP A  1 341 ? 51.933  13.021  43.831  1.00 12.92 ? 341  TRP A CD2 1 
ATOM   2580  N  NE1 . TRP A  1 341 ? 54.102  13.390  44.286  1.00 13.27 ? 341  TRP A NE1 1 
ATOM   2581  C  CE2 . TRP A  1 341 ? 53.180  13.379  43.267  1.00 13.39 ? 341  TRP A CE2 1 
ATOM   2582  C  CE3 . TRP A  1 341 ? 50.807  12.954  42.997  1.00 10.39 ? 341  TRP A CE3 1 
ATOM   2583  C  CZ2 . TRP A  1 341 ? 53.330  13.657  41.910  1.00 13.41 ? 341  TRP A CZ2 1 
ATOM   2584  C  CZ3 . TRP A  1 341 ? 50.950  13.245  41.635  1.00 12.43 ? 341  TRP A CZ3 1 
ATOM   2585  C  CH2 . TRP A  1 341 ? 52.213  13.582  41.114  1.00 13.41 ? 341  TRP A CH2 1 
ATOM   2586  N  N   . SER A  1 342 ? 51.949  9.444   45.071  1.00 10.05 ? 342  SER A N   1 
ATOM   2587  C  CA  . SER A  1 342 ? 52.876  8.338   45.228  1.00 10.94 ? 342  SER A CA  1 
ATOM   2588  C  C   . SER A  1 342 ? 54.338  8.555   44.928  1.00 11.03 ? 342  SER A C   1 
ATOM   2589  O  O   . SER A  1 342 ? 55.073  7.556   44.704  1.00 13.59 ? 342  SER A O   1 
ATOM   2590  C  CB  . SER A  1 342 ? 52.401  7.139   44.391  1.00 12.57 ? 342  SER A CB  1 
ATOM   2591  O  OG  A SER A  1 342 ? 52.144  7.619   43.083  0.50 10.13 ? 342  SER A OG  1 
ATOM   2592  O  OG  B SER A  1 342 ? 51.234  6.594   44.990  0.50 14.07 ? 342  SER A OG  1 
ATOM   2593  N  N   . SER A  1 343 ? 54.801  9.781   44.954  1.00 8.97  ? 343  SER A N   1 
ATOM   2594  C  CA  . SER A  1 343 ? 56.211  10.023  44.655  1.00 8.73  ? 343  SER A CA  1 
ATOM   2595  C  C   . SER A  1 343 ? 56.800  10.957  45.677  1.00 9.11  ? 343  SER A C   1 
ATOM   2596  O  O   . SER A  1 343 ? 56.110  11.824  46.196  1.00 8.97  ? 343  SER A O   1 
ATOM   2597  C  CB  . SER A  1 343 ? 56.361  10.680  43.256  1.00 7.69  ? 343  SER A CB  1 
ATOM   2598  O  OG  . SER A  1 343 ? 57.770  10.826  42.896  1.00 8.50  ? 343  SER A OG  1 
ATOM   2599  N  N   . VAL A  1 344 ? 58.100  10.823  45.899  1.00 7.77  ? 344  VAL A N   1 
ATOM   2600  C  CA  . VAL A  1 344 ? 58.853  11.850  46.639  1.00 7.85  ? 344  VAL A CA  1 
ATOM   2601  C  C   . VAL A  1 344 ? 59.136  13.075  45.790  1.00 8.10  ? 344  VAL A C   1 
ATOM   2602  O  O   . VAL A  1 344 ? 59.604  14.034  46.328  1.00 8.30  ? 344  VAL A O   1 
ATOM   2603  C  CB  . VAL A  1 344 ? 60.199  11.273  47.180  1.00 9.16  ? 344  VAL A CB  1 
ATOM   2604  C  CG1 . VAL A  1 344 ? 59.881  10.242  48.243  1.00 7.50  ? 344  VAL A CG1 1 
ATOM   2605  C  CG2 . VAL A  1 344 ? 61.053  10.702  46.044  1.00 8.01  ? 344  VAL A CG2 1 
ATOM   2606  N  N   . SER A  1 345 ? 58.898  13.013  44.462  1.00 8.37  ? 345  SER A N   1 
ATOM   2607  C  CA  . SER A  1 345 ? 59.054  14.157  43.581  1.00 7.82  ? 345  SER A CA  1 
ATOM   2608  C  C   . SER A  1 345 ? 57.698  14.723  43.259  1.00 7.81  ? 345  SER A C   1 
ATOM   2609  O  O   . SER A  1 345 ? 56.721  13.974  43.169  1.00 7.82  ? 345  SER A O   1 
ATOM   2610  C  CB  . SER A  1 345 ? 59.649  13.711  42.237  1.00 8.14  ? 345  SER A CB  1 
ATOM   2611  O  OG  . SER A  1 345 ? 61.044  13.683  42.374  1.00 14.78 ? 345  SER A OG  1 
ATOM   2612  N  N   . PHE A  1 346 ? 57.663  16.031  42.995  1.00 6.43  ? 346  PHE A N   1 
ATOM   2613  C  CA  . PHE A  1 346 ? 56.434  16.676  42.537  1.00 6.92  ? 346  PHE A CA  1 
ATOM   2614  C  C   . PHE A  1 346 ? 56.361  16.721  41.008  1.00 7.17  ? 346  PHE A C   1 
ATOM   2615  O  O   . PHE A  1 346 ? 57.344  16.316  40.347  1.00 8.20  ? 346  PHE A O   1 
ATOM   2616  C  CB  . PHE A  1 346 ? 56.274  18.048  43.190  1.00 8.06  ? 346  PHE A CB  1 
ATOM   2617  C  CG  . PHE A  1 346 ? 57.524  18.876  43.167  1.00 7.58  ? 346  PHE A CG  1 
ATOM   2618  C  CD1 . PHE A  1 346 ? 57.869  19.566  42.020  1.00 8.27  ? 346  PHE A CD1 1 
ATOM   2619  C  CD2 . PHE A  1 346 ? 58.302  19.027  44.321  1.00 8.27  ? 346  PHE A CD2 1 
ATOM   2620  C  CE1 . PHE A  1 346 ? 59.022  20.411  42.005  1.00 5.43  ? 346  PHE A CE1 1 
ATOM   2621  C  CE2 . PHE A  1 346 ? 59.456  19.843  44.289  1.00 10.42 ? 346  PHE A CE2 1 
ATOM   2622  C  CZ  . PHE A  1 346 ? 59.831  20.471  43.116  1.00 9.17  ? 346  PHE A CZ  1 
ATOM   2623  N  N   . PRO A  1 347 ? 55.220  17.096  40.404  1.00 6.28  ? 347  PRO A N   1 
ATOM   2624  C  CA  . PRO A  1 347 ? 55.155  17.111  38.932  1.00 6.82  ? 347  PRO A CA  1 
ATOM   2625  C  C   . PRO A  1 347 ? 56.135  18.062  38.286  1.00 6.82  ? 347  PRO A C   1 
ATOM   2626  O  O   . PRO A  1 347 ? 56.539  19.075  38.907  1.00 7.53  ? 347  PRO A O   1 
ATOM   2627  C  CB  . PRO A  1 347 ? 53.705  17.565  38.607  1.00 6.92  ? 347  PRO A CB  1 
ATOM   2628  C  CG  . PRO A  1 347 ? 52.916  17.343  39.906  1.00 6.92  ? 347  PRO A CG  1 
ATOM   2629  C  CD  . PRO A  1 347 ? 53.928  17.447  41.044  1.00 5.72  ? 347  PRO A CD  1 
ATOM   2630  N  N   . ALA A  1 348 ? 56.528  17.712  37.060  1.00 5.71  ? 348  ALA A N   1 
ATOM   2631  C  CA  . ALA A  1 348 ? 57.470  18.472  36.255  1.00 6.15  ? 348  ALA A CA  1 
ATOM   2632  C  C   . ALA A  1 348 ? 56.873  19.793  35.702  1.00 6.26  ? 348  ALA A C   1 
ATOM   2633  O  O   . ALA A  1 348 ? 57.612  20.671  35.261  1.00 6.94  ? 348  ALA A O   1 
ATOM   2634  C  CB  . ALA A  1 348 ? 57.955  17.626  35.095  1.00 5.78  ? 348  ALA A CB  1 
ATOM   2635  N  N   . ASP A  1 349 ? 55.541  19.909  35.707  1.00 6.49  ? 349  ASP A N   1 
ATOM   2636  C  CA  . ASP A  1 349 ? 54.872  21.128  35.218  1.00 6.91  ? 349  ASP A CA  1 
ATOM   2637  C  C   . ASP A  1 349 ? 53.985  21.745  36.266  1.00 6.59  ? 349  ASP A C   1 
ATOM   2638  O  O   . ASP A  1 349 ? 53.413  21.040  37.079  1.00 6.04  ? 349  ASP A O   1 
ATOM   2639  C  CB  . ASP A  1 349 ? 54.049  20.832  33.958  1.00 7.10  ? 349  ASP A CB  1 
ATOM   2640  C  CG  . ASP A  1 349 ? 54.821  20.003  32.950  1.00 10.85 ? 349  ASP A CG  1 
ATOM   2641  O  OD1 . ASP A  1 349 ? 55.788  20.510  32.321  1.00 10.73 ? 349  ASP A OD1 1 
ATOM   2642  O  OD2 . ASP A  1 349 ? 54.511  18.843  32.721  1.00 16.32 ? 349  ASP A OD2 1 
ATOM   2643  N  N   . TRP A  1 350 ? 53.833  23.071  36.225  1.00 8.74  ? 350  TRP A N   1 
ATOM   2644  C  CA  . TRP A  1 350 ? 52.912  23.752  37.145  1.00 10.43 ? 350  TRP A CA  1 
ATOM   2645  C  C   . TRP A  1 350 ? 51.440  23.463  36.808  1.00 11.42 ? 350  TRP A C   1 
ATOM   2646  O  O   . TRP A  1 350 ? 51.098  23.105  35.682  1.00 10.92 ? 350  TRP A O   1 
ATOM   2647  C  CB  . TRP A  1 350 ? 53.130  25.274  37.149  1.00 11.12 ? 350  TRP A CB  1 
ATOM   2648  C  CG  . TRP A  1 350 ? 54.567  25.699  37.523  1.00 12.33 ? 350  TRP A CG  1 
ATOM   2649  C  CD1 . TRP A  1 350 ? 55.471  26.343  36.713  1.00 12.72 ? 350  TRP A CD1 1 
ATOM   2650  C  CD2 . TRP A  1 350 ? 55.236  25.485  38.775  1.00 12.09 ? 350  TRP A CD2 1 
ATOM   2651  N  NE1 . TRP A  1 350 ? 56.655  26.535  37.389  1.00 10.79 ? 350  TRP A NE1 1 
ATOM   2652  C  CE2 . TRP A  1 350 ? 56.544  26.038  38.656  1.00 11.86 ? 350  TRP A CE2 1 
ATOM   2653  C  CE3 . TRP A  1 350 ? 54.865  24.901  39.998  1.00 11.81 ? 350  TRP A CE3 1 
ATOM   2654  C  CZ2 . TRP A  1 350 ? 57.470  26.035  39.711  1.00 10.18 ? 350  TRP A CZ2 1 
ATOM   2655  C  CZ3 . TRP A  1 350 ? 55.821  24.858  41.057  1.00 9.10  ? 350  TRP A CZ3 1 
ATOM   2656  C  CH2 . TRP A  1 350 ? 57.100  25.429  40.888  1.00 12.99 ? 350  TRP A CH2 1 
ATOM   2657  O  OXT . TRP A  1 350 ? 50.594  23.628  37.690  1.00 14.06 ? 350  TRP A OXT 1 
ATOM   2658  N  N   . SER B  1 3   ? 66.575  2.649   4.101   1.00 30.65 ? 3    SER B N   1 
ATOM   2659  C  CA  . SER B  1 3   ? 67.119  3.513   5.213   1.00 30.81 ? 3    SER B CA  1 
ATOM   2660  C  C   . SER B  1 3   ? 68.067  4.621   4.681   1.00 29.13 ? 3    SER B C   1 
ATOM   2661  O  O   . SER B  1 3   ? 69.017  4.334   3.938   1.00 29.68 ? 3    SER B O   1 
ATOM   2662  C  CB  . SER B  1 3   ? 67.810  2.656   6.273   1.00 31.12 ? 3    SER B CB  1 
ATOM   2663  O  OG  . SER B  1 3   ? 68.076  3.407   7.451   1.00 34.46 ? 3    SER B OG  1 
ATOM   2664  N  N   . SER B  1 4   ? 67.762  5.879   5.032   1.00 26.73 ? 4    SER B N   1 
ATOM   2665  C  CA  . SER B  1 4   ? 68.465  7.050   4.477   1.00 23.45 ? 4    SER B CA  1 
ATOM   2666  C  C   . SER B  1 4   ? 69.644  7.509   5.326   1.00 20.21 ? 4    SER B C   1 
ATOM   2667  O  O   . SER B  1 4   ? 69.554  7.739   6.549   1.00 18.45 ? 4    SER B O   1 
ATOM   2668  C  CB  . SER B  1 4   ? 67.501  8.254   4.241   1.00 24.19 ? 4    SER B CB  1 
ATOM   2669  O  OG  . SER B  1 4   ? 68.195  9.388   3.672   1.00 23.38 ? 4    SER B OG  1 
ATOM   2670  N  N   . LEU B  1 5   ? 70.749  7.703   4.623   1.00 18.10 ? 5    LEU B N   1 
ATOM   2671  C  CA  . LEU B  1 5   ? 71.935  8.215   5.223   1.00 15.09 ? 5    LEU B CA  1 
ATOM   2672  C  C   . LEU B  1 5   ? 71.764  9.654   5.642   1.00 13.28 ? 5    LEU B C   1 
ATOM   2673  O  O   . LEU B  1 5   ? 72.561  10.157  6.417   1.00 12.17 ? 5    LEU B O   1 
ATOM   2674  C  CB  . LEU B  1 5   ? 73.041  8.178   4.180   1.00 15.40 ? 5    LEU B CB  1 
ATOM   2675  C  CG  . LEU B  1 5   ? 73.611  6.797   4.004   1.00 16.19 ? 5    LEU B CG  1 
ATOM   2676  C  CD1 . LEU B  1 5   ? 74.347  6.700   2.642   1.00 14.17 ? 5    LEU B CD1 1 
ATOM   2677  C  CD2 . LEU B  1 5   ? 74.508  6.507   5.191   1.00 14.69 ? 5    LEU B CD2 1 
ATOM   2678  N  N   . ILE B  1 6   ? 70.792  10.342  5.041   1.00 11.98 ? 6    ILE B N   1 
ATOM   2679  C  CA  . ILE B  1 6   ? 70.869  11.814  4.968   1.00 10.30 ? 6    ILE B CA  1 
ATOM   2680  C  C   . ILE B  1 6   ? 70.444  12.448  6.290   1.00 9.90  ? 6    ILE B C   1 
ATOM   2681  O  O   . ILE B  1 6   ? 69.383  12.103  6.792   1.00 8.63  ? 6    ILE B O   1 
ATOM   2682  C  CB  . ILE B  1 6   ? 69.986  12.379  3.788   1.00 11.51 ? 6    ILE B CB  1 
ATOM   2683  C  CG1 . ILE B  1 6   ? 70.401  11.768  2.442   1.00 12.19 ? 6    ILE B CG1 1 
ATOM   2684  C  CG2 . ILE B  1 6   ? 70.034  13.941  3.732   1.00 11.11 ? 6    ILE B CG2 1 
ATOM   2685  C  CD1 . ILE B  1 6   ? 71.427  12.590  1.725   1.00 15.22 ? 6    ILE B CD1 1 
ATOM   2686  N  N   . VAL B  1 7   ? 71.254  13.380  6.836   1.00 8.20  ? 7    VAL B N   1 
ATOM   2687  C  CA  . VAL B  1 7   ? 70.882  14.139  8.023   1.00 8.21  ? 7    VAL B CA  1 
ATOM   2688  C  C   . VAL B  1 7   ? 71.088  15.638  7.781   1.00 9.65  ? 7    VAL B C   1 
ATOM   2689  O  O   . VAL B  1 7   ? 71.886  16.020  6.918   1.00 9.36  ? 7    VAL B O   1 
ATOM   2690  C  CB  . VAL B  1 7   ? 71.733  13.697  9.228   1.00 8.04  ? 7    VAL B CB  1 
ATOM   2691  C  CG1 . VAL B  1 7   ? 71.406  12.219  9.603   1.00 5.21  ? 7    VAL B CG1 1 
ATOM   2692  C  CG2 . VAL B  1 7   ? 73.254  13.842  8.882   1.00 8.49  ? 7    VAL B CG2 1 
ATOM   2693  N  N   . GLU B  1 8   ? 70.406  16.473  8.570   1.00 10.62 ? 8    GLU B N   1 
ATOM   2694  C  CA  . GLU B  1 8   ? 70.491  17.951  8.441   1.00 8.67  ? 8    GLU B CA  1 
ATOM   2695  C  C   . GLU B  1 8   ? 71.554  18.556  9.414   1.00 8.15  ? 8    GLU B C   1 
ATOM   2696  O  O   . GLU B  1 8   ? 72.029  19.687  9.242   1.00 7.54  ? 8    GLU B O   1 
ATOM   2697  C  CB  . GLU B  1 8   ? 69.057  18.516  8.679   1.00 9.32  ? 8    GLU B CB  1 
ATOM   2698  C  CG  A GLU B  1 8   ? 68.800  19.999  8.443   0.50 6.33  ? 8    GLU B CG  1 
ATOM   2699  C  CG  B GLU B  1 8   ? 68.001  18.069  7.680   0.50 9.27  ? 8    GLU B CG  1 
ATOM   2700  C  CD  A GLU B  1 8   ? 69.241  20.508  7.078   0.50 6.53  ? 8    GLU B CD  1 
ATOM   2701  C  CD  B GLU B  1 8   ? 68.325  18.407  6.234   0.50 10.44 ? 8    GLU B CD  1 
ATOM   2702  O  OE1 A GLU B  1 8   ? 69.279  19.707  6.112   0.50 6.24  ? 8    GLU B OE1 1 
ATOM   2703  O  OE1 B GLU B  1 8   ? 68.778  19.541  5.971   0.50 11.78 ? 8    GLU B OE1 1 
ATOM   2704  O  OE2 A GLU B  1 8   ? 69.534  21.718  6.974   0.50 2.00  ? 8    GLU B OE2 1 
ATOM   2705  O  OE2 B GLU B  1 8   ? 68.125  17.532  5.358   0.50 8.02  ? 8    GLU B OE2 1 
ATOM   2706  N  N   . ASP B  1 9   ? 71.870  17.804  10.473  1.00 8.42  ? 9    ASP B N   1 
ATOM   2707  C  CA  . ASP B  1 9   ? 72.909  18.160  11.451  1.00 8.05  ? 9    ASP B CA  1 
ATOM   2708  C  C   . ASP B  1 9   ? 73.662  16.873  11.713  1.00 8.83  ? 9    ASP B C   1 
ATOM   2709  O  O   . ASP B  1 9   ? 73.067  15.788  11.589  1.00 9.35  ? 9    ASP B O   1 
ATOM   2710  C  CB  . ASP B  1 9   ? 72.288  18.650  12.773  1.00 9.89  ? 9    ASP B CB  1 
ATOM   2711  C  CG  . ASP B  1 9   ? 71.496  19.936  12.574  1.00 9.17  ? 9    ASP B CG  1 
ATOM   2712  O  OD1 . ASP B  1 9   ? 70.291  19.796  12.271  1.00 9.69  ? 9    ASP B OD1 1 
ATOM   2713  O  OD2 . ASP B  1 9   ? 71.982  21.106  12.615  1.00 9.46  ? 9    ASP B OD2 1 
ATOM   2714  N  N   . ALA B  1 10  ? 74.935  16.981  12.063  1.00 8.36  ? 10   ALA B N   1 
ATOM   2715  C  CA  . ALA B  1 10  ? 75.737  15.782  12.309  1.00 9.53  ? 10   ALA B CA  1 
ATOM   2716  C  C   . ALA B  1 10  ? 75.175  15.070  13.530  1.00 9.76  ? 10   ALA B C   1 
ATOM   2717  O  O   . ALA B  1 10  ? 74.677  15.727  14.453  1.00 9.37  ? 10   ALA B O   1 
ATOM   2718  C  CB  . ALA B  1 10  ? 77.169  16.126  12.512  1.00 8.66  ? 10   ALA B CB  1 
ATOM   2719  N  N   . PRO B  1 11  ? 75.181  13.742  13.509  1.00 9.60  ? 11   PRO B N   1 
ATOM   2720  C  CA  . PRO B  1 11  ? 74.583  12.982  14.613  1.00 9.40  ? 11   PRO B CA  1 
ATOM   2721  C  C   . PRO B  1 11  ? 75.301  13.180  15.944  1.00 9.53  ? 11   PRO B C   1 
ATOM   2722  O  O   . PRO B  1 11  ? 76.469  13.681  15.982  1.00 9.37  ? 11   PRO B O   1 
ATOM   2723  C  CB  . PRO B  1 11  ? 74.570  11.541  14.096  1.00 9.62  ? 11   PRO B CB  1 
ATOM   2724  C  CG  . PRO B  1 11  ? 74.692  11.704  12.558  1.00 10.73 ? 11   PRO B CG  1 
ATOM   2725  C  CD  . PRO B  1 11  ? 75.573  12.883  12.372  1.00 9.23  ? 11   PRO B CD  1 
ATOM   2726  N  N   . ASP B  1 12  ? 74.602  12.850  17.035  1.00 9.05  ? 12   ASP B N   1 
ATOM   2727  C  CA  . ASP B  1 12  ? 75.200  12.993  18.365  1.00 9.79  ? 12   ASP B CA  1 
ATOM   2728  C  C   . ASP B  1 12  ? 75.927  11.703  18.788  1.00 9.94  ? 12   ASP B C   1 
ATOM   2729  O  O   . ASP B  1 12  ? 76.314  11.553  19.958  1.00 10.70 ? 12   ASP B O   1 
ATOM   2730  C  CB  . ASP B  1 12  ? 74.164  13.476  19.429  1.00 9.61  ? 12   ASP B CB  1 
ATOM   2731  C  CG  . ASP B  1 12  ? 73.067  12.446  19.727  1.00 12.62 ? 12   ASP B CG  1 
ATOM   2732  O  OD1 . ASP B  1 12  ? 73.119  11.292  19.247  1.00 6.28  ? 12   ASP B OD1 1 
ATOM   2733  O  OD2 . ASP B  1 12  ? 72.090  12.727  20.464  1.00 13.48 ? 12   ASP B OD2 1 
ATOM   2734  N  N   . HIS B  1 13  ? 76.111  10.789  17.826  1.00 8.88  ? 13   HIS B N   1 
ATOM   2735  C  CA  . HIS B  1 13  ? 76.796  9.493   18.039  1.00 8.50  ? 13   HIS B CA  1 
ATOM   2736  C  C   . HIS B  1 13  ? 77.328  9.007   16.669  1.00 8.80  ? 13   HIS B C   1 
ATOM   2737  O  O   . HIS B  1 13  ? 77.006  9.574   15.602  1.00 8.31  ? 13   HIS B O   1 
ATOM   2738  C  CB  . HIS B  1 13  ? 75.864  8.440   18.622  1.00 8.19  ? 13   HIS B CB  1 
ATOM   2739  C  CG  . HIS B  1 13  ? 74.733  8.094   17.703  1.00 8.02  ? 13   HIS B CG  1 
ATOM   2740  N  ND1 . HIS B  1 13  ? 73.709  8.980   17.424  1.00 10.88 ? 13   HIS B ND1 1 
ATOM   2741  C  CD2 . HIS B  1 13  ? 74.491  6.993   16.964  1.00 4.72  ? 13   HIS B CD2 1 
ATOM   2742  C  CE1 . HIS B  1 13  ? 72.869  8.422   16.569  1.00 11.14 ? 13   HIS B CE1 1 
ATOM   2743  N  NE2 . HIS B  1 13  ? 73.335  7.227   16.254  1.00 8.81  ? 13   HIS B NE2 1 
ATOM   2744  N  N   . VAL B  1 14  ? 78.124  7.938   16.710  1.00 8.96  ? 14   VAL B N   1 
ATOM   2745  C  CA  . VAL B  1 14  ? 78.738  7.396   15.517  1.00 9.02  ? 14   VAL B CA  1 
ATOM   2746  C  C   . VAL B  1 14  ? 77.755  6.536   14.709  1.00 8.44  ? 14   VAL B C   1 
ATOM   2747  O  O   . VAL B  1 14  ? 77.125  5.636   15.277  1.00 8.13  ? 14   VAL B O   1 
ATOM   2748  C  CB  . VAL B  1 14  ? 80.029  6.658   15.887  1.00 9.33  ? 14   VAL B CB  1 
ATOM   2749  C  CG1 . VAL B  1 14  ? 80.567  5.872   14.682  1.00 8.71  ? 14   VAL B CG1 1 
ATOM   2750  C  CG2 . VAL B  1 14  ? 81.075  7.714   16.317  1.00 8.74  ? 14   VAL B CG2 1 
ATOM   2751  N  N   . ARG B  1 15  ? 77.590  6.861   13.413  1.00 6.44  ? 15   ARG B N   1 
ATOM   2752  C  CA  . ARG B  1 15  ? 76.738  6.053   12.518  1.00 6.59  ? 15   ARG B CA  1 
ATOM   2753  C  C   . ARG B  1 15  ? 77.070  6.512   11.100  1.00 6.74  ? 15   ARG B C   1 
ATOM   2754  O  O   . ARG B  1 15  ? 77.597  7.624   10.917  1.00 6.98  ? 15   ARG B O   1 
ATOM   2755  C  CB  . ARG B  1 15  ? 75.259  6.317   12.817  1.00 5.24  ? 15   ARG B CB  1 
ATOM   2756  C  CG  . ARG B  1 15  ? 74.906  7.841   12.816  1.00 4.82  ? 15   ARG B CG  1 
ATOM   2757  C  CD  . ARG B  1 15  ? 73.405  8.088   12.507  1.00 6.59  ? 15   ARG B CD  1 
ATOM   2758  N  NE  . ARG B  1 15  ? 73.177  7.990   11.075  1.00 6.92  ? 15   ARG B NE  1 
ATOM   2759  C  CZ  . ARG B  1 15  ? 72.089  8.408   10.437  1.00 11.09 ? 15   ARG B CZ  1 
ATOM   2760  N  NH1 . ARG B  1 15  ? 71.109  9.014   11.113  1.00 10.14 ? 15   ARG B NH1 1 
ATOM   2761  N  NH2 . ARG B  1 15  ? 72.008  8.257   9.109   1.00 10.12 ? 15   ARG B NH2 1 
ATOM   2762  N  N   . PRO B  1 16  ? 76.794  5.678   10.088  1.00 6.30  ? 16   PRO B N   1 
ATOM   2763  C  CA  . PRO B  1 16  ? 76.939  6.148   8.697   1.00 5.38  ? 16   PRO B CA  1 
ATOM   2764  C  C   . PRO B  1 16  ? 76.008  7.356   8.477   1.00 6.42  ? 16   PRO B C   1 
ATOM   2765  O  O   . PRO B  1 16  ? 74.850  7.319   8.929   1.00 6.40  ? 16   PRO B O   1 
ATOM   2766  C  CB  . PRO B  1 16  ? 76.457  4.973   7.872   1.00 6.25  ? 16   PRO B CB  1 
ATOM   2767  C  CG  . PRO B  1 16  ? 76.724  3.710   8.822   1.00 6.25  ? 16   PRO B CG  1 
ATOM   2768  C  CD  . PRO B  1 16  ? 76.304  4.287   10.190  1.00 6.55  ? 16   PRO B CD  1 
ATOM   2769  N  N   . TYR B  1 17  ? 76.484  8.379   7.794   1.00 6.37  ? 17   TYR B N   1 
ATOM   2770  C  CA  . TYR B  1 17  ? 75.601  9.476   7.364   1.00 6.99  ? 17   TYR B CA  1 
ATOM   2771  C  C   . TYR B  1 17  ? 76.113  10.249  6.168   1.00 6.73  ? 17   TYR B C   1 
ATOM   2772  O  O   . TYR B  1 17  ? 77.330  10.207  5.850   1.00 4.85  ? 17   TYR B O   1 
ATOM   2773  C  CB  . TYR B  1 17  ? 75.281  10.436  8.516   1.00 6.57  ? 17   TYR B CB  1 
ATOM   2774  C  CG  . TYR B  1 17  ? 76.405  11.345  9.028   1.00 8.65  ? 17   TYR B CG  1 
ATOM   2775  C  CD1 . TYR B  1 17  ? 77.287  10.901  10.026  1.00 5.16  ? 17   TYR B CD1 1 
ATOM   2776  C  CD2 . TYR B  1 17  ? 76.553  12.650  8.544   1.00 6.46  ? 17   TYR B CD2 1 
ATOM   2777  C  CE1 . TYR B  1 17  ? 78.256  11.710  10.551  1.00 2.57  ? 17   TYR B CE1 1 
ATOM   2778  C  CE2 . TYR B  1 17  ? 77.560  13.510  9.083   1.00 7.77  ? 17   TYR B CE2 1 
ATOM   2779  C  CZ  . TYR B  1 17  ? 78.390  13.017  10.083  1.00 6.60  ? 17   TYR B CZ  1 
ATOM   2780  O  OH  . TYR B  1 17  ? 79.362  13.790  10.631  1.00 7.04  ? 17   TYR B OH  1 
ATOM   2781  N  N   . VAL B  1 18  ? 75.177  10.946  5.508   1.00 4.76  ? 18   VAL B N   1 
ATOM   2782  C  CA  . VAL B  1 18  ? 75.532  11.959  4.490   1.00 6.07  ? 18   VAL B CA  1 
ATOM   2783  C  C   . VAL B  1 18  ? 74.890  13.262  4.880   1.00 6.72  ? 18   VAL B C   1 
ATOM   2784  O  O   . VAL B  1 18  ? 73.712  13.282  5.285   1.00 5.21  ? 18   VAL B O   1 
ATOM   2785  C  CB  . VAL B  1 18  ? 75.072  11.489  3.057   1.00 6.48  ? 18   VAL B CB  1 
ATOM   2786  C  CG1 . VAL B  1 18  ? 75.101  12.649  1.977   1.00 7.68  ? 18   VAL B CG1 1 
ATOM   2787  C  CG2 . VAL B  1 18  ? 75.951  10.333  2.594   1.00 6.10  ? 18   VAL B CG2 1 
ATOM   2788  N  N   . ILE B  1 19  ? 75.635  14.349  4.780   1.00 7.46  ? 19   ILE B N   1 
ATOM   2789  C  CA  . ILE B  1 19  ? 75.076  15.666  5.100   1.00 7.18  ? 19   ILE B CA  1 
ATOM   2790  C  C   . ILE B  1 19  ? 75.345  16.591  3.903   1.00 7.56  ? 19   ILE B C   1 
ATOM   2791  O  O   . ILE B  1 19  ? 76.490  16.738  3.422   1.00 6.92  ? 19   ILE B O   1 
ATOM   2792  C  CB  . ILE B  1 19  ? 75.618  16.240  6.488   1.00 7.13  ? 19   ILE B CB  1 
ATOM   2793  C  CG1 . ILE B  1 19  ? 75.057  17.631  6.834   1.00 8.08  ? 19   ILE B CG1 1 
ATOM   2794  C  CG2 . ILE B  1 19  ? 77.177  16.307  6.571   1.00 4.24  ? 19   ILE B CG2 1 
ATOM   2795  C  CD1 . ILE B  1 19  ? 75.123  17.976  8.413   1.00 5.09  ? 19   ILE B CD1 1 
ATOM   2796  N  N   . ARG B  1 20  ? 74.279  17.231  3.438   1.00 7.26  ? 20   ARG B N   1 
ATOM   2797  C  CA  . ARG B  1 20  ? 74.334  17.909  2.145   1.00 7.08  ? 20   ARG B CA  1 
ATOM   2798  C  C   . ARG B  1 20  ? 75.021  19.229  2.389   1.00 7.95  ? 20   ARG B C   1 
ATOM   2799  O  O   . ARG B  1 20  ? 74.943  19.755  3.494   1.00 8.88  ? 20   ARG B O   1 
ATOM   2800  C  CB  . ARG B  1 20  ? 72.912  18.144  1.594   1.00 5.56  ? 20   ARG B CB  1 
ATOM   2801  C  CG  . ARG B  1 20  ? 72.120  16.874  1.179   1.00 5.62  ? 20   ARG B CG  1 
ATOM   2802  C  CD  . ARG B  1 20  ? 72.793  16.070  0.077   1.00 8.49  ? 20   ARG B CD  1 
ATOM   2803  N  NE  . ARG B  1 20  ? 71.890  15.116  -0.579  1.00 5.79  ? 20   ARG B NE  1 
ATOM   2804  C  CZ  . ARG B  1 20  ? 72.188  14.370  -1.628  1.00 8.17  ? 20   ARG B CZ  1 
ATOM   2805  N  NH1 . ARG B  1 20  ? 73.397  14.389  -2.219  1.00 7.44  ? 20   ARG B NH1 1 
ATOM   2806  N  NH2 . ARG B  1 20  ? 71.257  13.548  -2.077  1.00 6.51  ? 20   ARG B NH2 1 
ATOM   2807  N  N   . HIS B  1 21  ? 75.707  19.746  1.369   1.00 7.73  ? 21   HIS B N   1 
ATOM   2808  C  CA  . HIS B  1 21  ? 76.397  21.042  1.426   1.00 7.56  ? 21   HIS B CA  1 
ATOM   2809  C  C   . HIS B  1 21  ? 75.392  22.102  1.890   1.00 8.03  ? 21   HIS B C   1 
ATOM   2810  O  O   . HIS B  1 21  ? 74.262  22.122  1.413   1.00 6.87  ? 21   HIS B O   1 
ATOM   2811  C  CB  . HIS B  1 21  ? 76.875  21.434  0.016   1.00 6.25  ? 21   HIS B CB  1 
ATOM   2812  C  CG  . HIS B  1 21  ? 77.958  22.499  0.006   1.00 10.05 ? 21   HIS B CG  1 
ATOM   2813  N  ND1 . HIS B  1 21  ? 78.198  23.312  -1.085  1.00 12.71 ? 21   HIS B ND1 1 
ATOM   2814  C  CD2 . HIS B  1 21  ? 78.895  22.830  0.921   1.00 11.27 ? 21   HIS B CD2 1 
ATOM   2815  C  CE1 . HIS B  1 21  ? 79.232  24.093  -0.848  1.00 11.66 ? 21   HIS B CE1 1 
ATOM   2816  N  NE2 . HIS B  1 21  ? 79.677  23.823  0.371   1.00 11.34 ? 21   HIS B NE2 1 
ATOM   2817  N  N   . TYR B  1 22  ? 75.816  22.956  2.811   1.00 6.89  ? 22   TYR B N   1 
ATOM   2818  C  CA  . TYR B  1 22  ? 74.954  23.994  3.396   1.00 7.93  ? 22   TYR B CA  1 
ATOM   2819  C  C   . TYR B  1 22  ? 73.749  23.533  4.225   1.00 7.01  ? 22   TYR B C   1 
ATOM   2820  O  O   . TYR B  1 22  ? 72.796  24.326  4.455   1.00 7.72  ? 22   TYR B O   1 
ATOM   2821  C  CB  . TYR B  1 22  ? 74.460  24.956  2.320   1.00 5.99  ? 22   TYR B CB  1 
ATOM   2822  C  CG  . TYR B  1 22  ? 75.566  25.537  1.474   1.00 9.41  ? 22   TYR B CG  1 
ATOM   2823  C  CD1 . TYR B  1 22  ? 76.643  26.240  2.065   1.00 8.63  ? 22   TYR B CD1 1 
ATOM   2824  C  CD2 . TYR B  1 22  ? 75.539  25.382  0.089   1.00 9.16  ? 22   TYR B CD2 1 
ATOM   2825  C  CE1 . TYR B  1 22  ? 77.659  26.781  1.284   1.00 9.91  ? 22   TYR B CE1 1 
ATOM   2826  C  CE2 . TYR B  1 22  ? 76.547  25.933  -0.717  1.00 11.88 ? 22   TYR B CE2 1 
ATOM   2827  C  CZ  . TYR B  1 22  ? 77.587  26.651  -0.108  1.00 10.95 ? 22   TYR B CZ  1 
ATOM   2828  O  OH  . TYR B  1 22  ? 78.579  27.193  -0.885  1.00 12.73 ? 22   TYR B OH  1 
ATOM   2829  N  N   . SER B  1 23  ? 73.791  22.299  4.701   1.00 7.51  ? 23   SER B N   1 
ATOM   2830  C  CA  . SER B  1 23  ? 72.793  21.835  5.695   1.00 8.24  ? 23   SER B CA  1 
ATOM   2831  C  C   . SER B  1 23  ? 72.995  22.635  6.948   1.00 8.01  ? 23   SER B C   1 
ATOM   2832  O  O   . SER B  1 23  ? 74.090  23.206  7.161   1.00 6.73  ? 23   SER B O   1 
ATOM   2833  C  CB  . SER B  1 23  ? 72.991  20.348  6.038   1.00 8.96  ? 23   SER B CB  1 
ATOM   2834  O  OG  . SER B  1 23  ? 72.725  19.561  4.913   1.00 8.80  ? 23   SER B OG  1 
ATOM   2835  N  N   . HIS B  1 24  ? 71.950  22.697  7.771   1.00 6.99  ? 24   HIS B N   1 
ATOM   2836  C  CA  . HIS B  1 24  ? 72.060  23.431  8.998   1.00 7.04  ? 24   HIS B CA  1 
ATOM   2837  C  C   . HIS B  1 24  ? 73.356  23.151  9.771   1.00 6.08  ? 24   HIS B C   1 
ATOM   2838  O  O   . HIS B  1 24  ? 74.087  24.091  10.091  1.00 7.69  ? 24   HIS B O   1 
ATOM   2839  C  CB  . HIS B  1 24  ? 70.849  23.228  9.902   1.00 6.69  ? 24   HIS B CB  1 
ATOM   2840  C  CG  . HIS B  1 24  ? 70.886  24.136  11.083  1.00 6.97  ? 24   HIS B CG  1 
ATOM   2841  N  ND1 . HIS B  1 24  ? 71.106  23.674  12.355  1.00 4.45  ? 24   HIS B ND1 1 
ATOM   2842  C  CD2 . HIS B  1 24  ? 70.848  25.495  11.169  1.00 8.01  ? 24   HIS B CD2 1 
ATOM   2843  C  CE1 . HIS B  1 24  ? 71.145  24.700  13.191  1.00 7.00  ? 24   HIS B CE1 1 
ATOM   2844  N  NE2 . HIS B  1 24  ? 70.973  25.814  12.499  1.00 7.50  ? 24   HIS B NE2 1 
ATOM   2845  N  N   . ALA B  1 25  ? 73.663  21.882  10.035  1.00 5.86  ? 25   ALA B N   1 
ATOM   2846  C  CA  . ALA B  1 25  ? 74.940  21.480  10.632  1.00 5.36  ? 25   ALA B CA  1 
ATOM   2847  C  C   . ALA B  1 25  ? 75.272  22.263  11.881  1.00 7.00  ? 25   ALA B C   1 
ATOM   2848  O  O   . ALA B  1 25  ? 76.414  22.695  12.065  1.00 6.34  ? 25   ALA B O   1 
ATOM   2849  C  CB  . ALA B  1 25  ? 76.106  21.619  9.618   1.00 6.12  ? 25   ALA B CB  1 
ATOM   2850  N  N   . ARG B  1 26  ? 74.278  22.488  12.735  1.00 8.08  ? 26   ARG B N   1 
ATOM   2851  C  CA  . ARG B  1 26  ? 74.536  23.170  13.983  1.00 9.83  ? 26   ARG B CA  1 
ATOM   2852  C  C   . ARG B  1 26  ? 75.175  24.533  13.802  1.00 9.18  ? 26   ARG B C   1 
ATOM   2853  O  O   . ARG B  1 26  ? 76.000  24.928  14.617  1.00 9.00  ? 26   ARG B O   1 
ATOM   2854  C  CB  . ARG B  1 26  ? 75.405  22.238  14.883  1.00 11.93 ? 26   ARG B CB  1 
ATOM   2855  C  CG  . ARG B  1 26  ? 74.711  21.874  16.185  1.00 17.79 ? 26   ARG B CG  1 
ATOM   2856  C  CD  . ARG B  1 26  ? 75.530  20.974  17.121  1.00 28.59 ? 26   ARG B CD  1 
ATOM   2857  N  NE  . ARG B  1 26  ? 74.962  19.623  17.412  1.00 36.06 ? 26   ARG B NE  1 
ATOM   2858  C  CZ  . ARG B  1 26  ? 73.959  19.343  18.280  1.00 40.11 ? 26   ARG B CZ  1 
ATOM   2859  N  NH1 . ARG B  1 26  ? 73.325  20.330  18.929  1.00 39.17 ? 26   ARG B NH1 1 
ATOM   2860  N  NH2 . ARG B  1 26  ? 73.580  18.061  18.488  1.00 39.25 ? 26   ARG B NH2 1 
ATOM   2861  N  N   . ALA B  1 27  ? 74.766  25.264  12.754  1.00 8.72  ? 27   ALA B N   1 
ATOM   2862  C  CA  . ALA B  1 27  ? 75.418  26.517  12.329  1.00 8.64  ? 27   ALA B CA  1 
ATOM   2863  C  C   . ALA B  1 27  ? 75.517  27.593  13.408  1.00 7.22  ? 27   ALA B C   1 
ATOM   2864  O  O   . ALA B  1 27  ? 74.550  27.849  14.154  1.00 7.31  ? 27   ALA B O   1 
ATOM   2865  C  CB  . ALA B  1 27  ? 74.659  27.092  11.149  1.00 8.22  ? 27   ALA B CB  1 
ATOM   2866  N  N   . VAL B  1 28  ? 76.655  28.268  13.430  1.00 7.55  ? 28   VAL B N   1 
ATOM   2867  C  CA  . VAL B  1 28  ? 76.817  29.484  14.195  1.00 7.34  ? 28   VAL B CA  1 
ATOM   2868  C  C   . VAL B  1 28  ? 77.480  30.555  13.318  1.00 7.51  ? 28   VAL B C   1 
ATOM   2869  O  O   . VAL B  1 28  ? 78.182  30.238  12.326  1.00 9.28  ? 28   VAL B O   1 
ATOM   2870  C  CB  . VAL B  1 28  ? 77.704  29.326  15.454  1.00 6.63  ? 28   VAL B CB  1 
ATOM   2871  C  CG1 . VAL B  1 28  ? 77.152  28.305  16.384  1.00 7.20  ? 28   VAL B CG1 1 
ATOM   2872  C  CG2 . VAL B  1 28  ? 79.210  29.031  15.074  1.00 5.96  ? 28   VAL B CG2 1 
ATOM   2873  N  N   . THR B  1 29  ? 77.301  31.801  13.707  1.00 6.93  ? 29   THR B N   1 
ATOM   2874  C  CA  . THR B  1 29  ? 78.073  32.865  13.090  1.00 6.86  ? 29   THR B CA  1 
ATOM   2875  C  C   . THR B  1 29  ? 79.046  33.462  14.079  1.00 7.07  ? 29   THR B C   1 
ATOM   2876  O  O   . THR B  1 29  ? 78.762  33.514  15.293  1.00 6.96  ? 29   THR B O   1 
ATOM   2877  C  CB  . THR B  1 29  ? 77.159  33.974  12.525  1.00 6.41  ? 29   THR B CB  1 
ATOM   2878  O  OG1 . THR B  1 29  ? 76.341  34.530  13.571  1.00 8.13  ? 29   THR B OG1 1 
ATOM   2879  C  CG2 . THR B  1 29  ? 76.181  33.424  11.499  1.00 5.59  ? 29   THR B CG2 1 
ATOM   2880  N  N   . VAL B  1 30  ? 80.183  33.927  13.563  1.00 6.69  ? 30   VAL B N   1 
ATOM   2881  C  CA  . VAL B  1 30  ? 81.118  34.718  14.344  1.00 8.42  ? 30   VAL B CA  1 
ATOM   2882  C  C   . VAL B  1 30  ? 81.320  35.914  13.481  1.00 9.25  ? 30   VAL B C   1 
ATOM   2883  O  O   . VAL B  1 30  ? 81.999  35.822  12.442  1.00 8.46  ? 30   VAL B O   1 
ATOM   2884  C  CB  . VAL B  1 30  ? 82.517  33.992  14.505  1.00 8.28  ? 30   VAL B CB  1 
ATOM   2885  C  CG1 . VAL B  1 30  ? 83.444  34.890  15.275  1.00 8.29  ? 30   VAL B CG1 1 
ATOM   2886  C  CG2 . VAL B  1 30  ? 82.339  32.675  15.217  1.00 9.44  ? 30   VAL B CG2 1 
ATOM   2887  N  N   . ASP B  1 31  ? 80.637  37.006  13.823  1.00 9.78  ? 31   ASP B N   1 
ATOM   2888  C  CA  . ASP B  1 31  ? 80.620  38.201  12.984  1.00 9.88  ? 31   ASP B CA  1 
ATOM   2889  C  C   . ASP B  1 31  ? 80.104  37.808  11.593  1.00 9.30  ? 31   ASP B C   1 
ATOM   2890  O  O   . ASP B  1 31  ? 79.017  37.240  11.496  1.00 9.65  ? 31   ASP B O   1 
ATOM   2891  C  CB  . ASP B  1 31  ? 82.002  38.957  13.021  1.00 10.44 ? 31   ASP B CB  1 
ATOM   2892  C  CG  . ASP B  1 31  ? 82.471  39.280  14.466  1.00 14.86 ? 31   ASP B CG  1 
ATOM   2893  O  OD1 . ASP B  1 31  ? 81.683  39.877  15.264  1.00 15.10 ? 31   ASP B OD1 1 
ATOM   2894  O  OD2 . ASP B  1 31  ? 83.614  38.978  14.905  1.00 17.92 ? 31   ASP B OD2 1 
ATOM   2895  N  N   . THR B  1 32  ? 80.842  38.051  10.510  1.00 7.99  ? 32   THR B N   1 
ATOM   2896  C  CA  . THR B  1 32  ? 80.287  37.687  9.217   1.00 8.48  ? 32   THR B CA  1 
ATOM   2897  C  C   . THR B  1 32  ? 80.456  36.248  8.790   1.00 8.62  ? 32   THR B C   1 
ATOM   2898  O  O   . THR B  1 32  ? 79.859  35.860  7.775   1.00 8.21  ? 32   THR B O   1 
ATOM   2899  C  CB  . THR B  1 32  ? 80.859  38.553  8.108   1.00 9.06  ? 32   THR B CB  1 
ATOM   2900  O  OG1 . THR B  1 32  ? 82.284  38.414  8.140   1.00 6.44  ? 32   THR B OG1 1 
ATOM   2901  C  CG2 . THR B  1 32  ? 80.545  39.993  8.390   1.00 7.25  ? 32   THR B CG2 1 
ATOM   2902  N  N   . GLN B  1 33  ? 81.312  35.503  9.495   1.00 7.27  ? 33   GLN B N   1 
ATOM   2903  C  CA  . GLN B  1 33  ? 81.600  34.106  9.159   1.00 7.95  ? 33   GLN B CA  1 
ATOM   2904  C  C   . GLN B  1 33  ? 80.525  33.153  9.649   1.00 8.71  ? 33   GLN B C   1 
ATOM   2905  O  O   . GLN B  1 33  ? 80.039  33.293  10.774  1.00 9.81  ? 33   GLN B O   1 
ATOM   2906  C  CB  . GLN B  1 33  ? 82.925  33.684  9.775   1.00 6.37  ? 33   GLN B CB  1 
ATOM   2907  C  CG  . GLN B  1 33  ? 84.009  34.692  9.541   1.00 5.75  ? 33   GLN B CG  1 
ATOM   2908  C  CD  . GLN B  1 33  ? 85.251  34.425  10.401  1.00 10.38 ? 33   GLN B CD  1 
ATOM   2909  O  OE1 . GLN B  1 33  ? 85.198  33.660  11.395  1.00 10.73 ? 33   GLN B OE1 1 
ATOM   2910  N  NE2 . GLN B  1 33  ? 86.354  35.057  10.036  1.00 9.14  ? 33   GLN B NE2 1 
ATOM   2911  N  N   . LEU B  1 34  ? 80.130  32.217  8.802   1.00 8.67  ? 34   LEU B N   1 
ATOM   2912  C  CA  . LEU B  1 34  ? 79.129  31.228  9.169   1.00 8.96  ? 34   LEU B CA  1 
ATOM   2913  C  C   . LEU B  1 34  ? 79.820  29.875  9.140   1.00 8.44  ? 34   LEU B C   1 
ATOM   2914  O  O   . LEU B  1 34  ? 80.393  29.497  8.109   1.00 7.89  ? 34   LEU B O   1 
ATOM   2915  C  CB  . LEU B  1 34  ? 77.957  31.229  8.186   1.00 9.03  ? 34   LEU B CB  1 
ATOM   2916  C  CG  . LEU B  1 34  ? 76.730  30.463  8.708   1.00 10.54 ? 34   LEU B CG  1 
ATOM   2917  C  CD1 . LEU B  1 34  ? 75.528  30.980  7.996   1.00 14.03 ? 34   LEU B CD1 1 
ATOM   2918  C  CD2 . LEU B  1 34  ? 76.859  28.932  8.518   1.00 11.13 ? 34   LEU B CD2 1 
ATOM   2919  N  N   . TYR B  1 35  ? 79.776  29.168  10.271  1.00 7.99  ? 35   TYR B N   1 
ATOM   2920  C  CA  . TYR B  1 35  ? 80.477  27.879  10.458  1.00 7.26  ? 35   TYR B CA  1 
ATOM   2921  C  C   . TYR B  1 35  ? 79.471  26.796  10.456  1.00 7.49  ? 35   TYR B C   1 
ATOM   2922  O  O   . TYR B  1 35  ? 78.442  26.935  11.104  1.00 8.29  ? 35   TYR B O   1 
ATOM   2923  C  CB  . TYR B  1 35  ? 81.174  27.832  11.822  1.00 6.76  ? 35   TYR B CB  1 
ATOM   2924  C  CG  . TYR B  1 35  ? 82.419  28.699  11.867  1.00 7.41  ? 35   TYR B CG  1 
ATOM   2925  C  CD1 . TYR B  1 35  ? 82.312  30.060  12.033  1.00 6.16  ? 35   TYR B CD1 1 
ATOM   2926  C  CD2 . TYR B  1 35  ? 83.683  28.143  11.750  1.00 9.54  ? 35   TYR B CD2 1 
ATOM   2927  C  CE1 . TYR B  1 35  ? 83.442  30.885  12.056  1.00 9.39  ? 35   TYR B CE1 1 
ATOM   2928  C  CE2 . TYR B  1 35  ? 84.806  28.935  11.766  1.00 7.40  ? 35   TYR B CE2 1 
ATOM   2929  C  CZ  . TYR B  1 35  ? 84.682  30.283  11.920  1.00 8.53  ? 35   TYR B CZ  1 
ATOM   2930  O  OH  . TYR B  1 35  ? 85.820  31.035  11.913  1.00 9.46  ? 35   TYR B OH  1 
ATOM   2931  N  N   . ARG B  1 36  ? 79.762  25.687  9.765   1.00 8.15  ? 36   ARG B N   1 
ATOM   2932  C  CA  . ARG B  1 36  ? 78.856  24.532  9.687   1.00 7.27  ? 36   ARG B CA  1 
ATOM   2933  C  C   . ARG B  1 36  ? 79.674  23.285  10.103  1.00 7.78  ? 36   ARG B C   1 
ATOM   2934  O  O   . ARG B  1 36  ? 80.812  23.074  9.621   1.00 7.73  ? 36   ARG B O   1 
ATOM   2935  C  CB  . ARG B  1 36  ? 78.295  24.346  8.275   1.00 7.19  ? 36   ARG B CB  1 
ATOM   2936  C  CG  . ARG B  1 36  ? 77.123  25.285  7.948   1.00 8.32  ? 36   ARG B CG  1 
ATOM   2937  C  CD  . ARG B  1 36  ? 76.573  25.139  6.517   1.00 3.89  ? 36   ARG B CD  1 
ATOM   2938  N  NE  . ARG B  1 36  ? 75.455  26.023  6.243   1.00 5.02  ? 36   ARG B NE  1 
ATOM   2939  C  CZ  . ARG B  1 36  ? 75.586  27.206  5.702   1.00 7.25  ? 36   ARG B CZ  1 
ATOM   2940  N  NH1 . ARG B  1 36  ? 76.792  27.644  5.344   1.00 6.73  ? 36   ARG B NH1 1 
ATOM   2941  N  NH2 . ARG B  1 36  ? 74.515  27.953  5.503   1.00 7.11  ? 36   ARG B NH2 1 
ATOM   2942  N  N   . PHE B  1 37  ? 79.121  22.462  10.991  1.00 6.34  ? 37   PHE B N   1 
ATOM   2943  C  CA  . PHE B  1 37  ? 79.932  21.389  11.595  1.00 7.46  ? 37   PHE B CA  1 
ATOM   2944  C  C   . PHE B  1 37  ? 79.504  20.061  10.977  1.00 7.33  ? 37   PHE B C   1 
ATOM   2945  O  O   . PHE B  1 37  ? 78.618  19.374  11.504  1.00 6.41  ? 37   PHE B O   1 
ATOM   2946  C  CB  . PHE B  1 37  ? 79.760  21.469  13.133  1.00 7.55  ? 37   PHE B CB  1 
ATOM   2947  C  CG  . PHE B  1 37  ? 80.096  22.846  13.649  1.00 10.86 ? 37   PHE B CG  1 
ATOM   2948  C  CD1 . PHE B  1 37  ? 81.430  23.257  13.770  1.00 11.35 ? 37   PHE B CD1 1 
ATOM   2949  C  CD2 . PHE B  1 37  ? 79.090  23.784  13.863  1.00 10.85 ? 37   PHE B CD2 1 
ATOM   2950  C  CE1 . PHE B  1 37  ? 81.739  24.572  14.166  1.00 10.16 ? 37   PHE B CE1 1 
ATOM   2951  C  CE2 . PHE B  1 37  ? 79.405  25.083  14.258  1.00 11.67 ? 37   PHE B CE2 1 
ATOM   2952  C  CZ  . PHE B  1 37  ? 80.726  25.467  14.445  1.00 9.48  ? 37   PHE B CZ  1 
ATOM   2953  N  N   . TYR B  1 38  ? 80.068  19.749  9.809   1.00 6.12  ? 38   TYR B N   1 
ATOM   2954  C  CA  . TYR B  1 38  ? 79.569  18.603  9.051   1.00 6.08  ? 38   TYR B CA  1 
ATOM   2955  C  C   . TYR B  1 38  ? 79.944  17.278  9.753   1.00 5.90  ? 38   TYR B C   1 
ATOM   2956  O  O   . TYR B  1 38  ? 79.193  16.273  9.717   1.00 7.82  ? 38   TYR B O   1 
ATOM   2957  C  CB  . TYR B  1 38  ? 80.145  18.637  7.600   1.00 4.23  ? 38   TYR B CB  1 
ATOM   2958  C  CG  . TYR B  1 38  ? 79.625  19.797  6.762   1.00 9.46  ? 38   TYR B CG  1 
ATOM   2959  C  CD1 . TYR B  1 38  ? 78.262  19.914  6.474   1.00 10.89 ? 38   TYR B CD1 1 
ATOM   2960  C  CD2 . TYR B  1 38  ? 80.497  20.736  6.210   1.00 8.45  ? 38   TYR B CD2 1 
ATOM   2961  C  CE1 . TYR B  1 38  ? 77.783  20.972  5.702   1.00 10.49 ? 38   TYR B CE1 1 
ATOM   2962  C  CE2 . TYR B  1 38  ? 80.006  21.805  5.428   1.00 10.36 ? 38   TYR B CE2 1 
ATOM   2963  C  CZ  . TYR B  1 38  ? 78.673  21.883  5.159   1.00 8.98  ? 38   TYR B CZ  1 
ATOM   2964  O  OH  . TYR B  1 38  ? 78.229  22.932  4.400   1.00 10.98 ? 38   TYR B OH  1 
ATOM   2965  N  N   . VAL B  1 39  ? 81.132  17.257  10.351  1.00 5.60  ? 39   VAL B N   1 
ATOM   2966  C  CA  . VAL B  1 39  ? 81.513  16.153  11.219  1.00 6.12  ? 39   VAL B CA  1 
ATOM   2967  C  C   . VAL B  1 39  ? 82.028  16.747  12.525  1.00 6.17  ? 39   VAL B C   1 
ATOM   2968  O  O   . VAL B  1 39  ? 82.933  17.589  12.504  1.00 5.74  ? 39   VAL B O   1 
ATOM   2969  C  CB  . VAL B  1 39  ? 82.648  15.315  10.608  1.00 5.97  ? 39   VAL B CB  1 
ATOM   2970  C  CG1 . VAL B  1 39  ? 82.973  14.081  11.493  1.00 5.32  ? 39   VAL B CG1 1 
ATOM   2971  C  CG2 . VAL B  1 39  ? 82.290  14.849  9.188   1.00 6.85  ? 39   VAL B CG2 1 
ATOM   2972  N  N   . THR B  1 40  ? 81.526  16.212  13.638  1.00 6.64  ? 40   THR B N   1 
ATOM   2973  C  CA  . THR B  1 40  ? 81.897  16.652  14.990  1.00 7.37  ? 40   THR B CA  1 
ATOM   2974  C  C   . THR B  1 40  ? 82.668  15.595  15.776  1.00 8.37  ? 40   THR B C   1 
ATOM   2975  O  O   . THR B  1 40  ? 82.859  14.479  15.299  1.00 9.34  ? 40   THR B O   1 
ATOM   2976  C  CB  . THR B  1 40  ? 80.649  17.040  15.760  1.00 7.69  ? 40   THR B CB  1 
ATOM   2977  O  OG1 . THR B  1 40  ? 79.764  15.894  15.857  1.00 7.15  ? 40   THR B OG1 1 
ATOM   2978  C  CG2 . THR B  1 40  ? 79.865  18.157  14.979  1.00 6.93  ? 40   THR B CG2 1 
ATOM   2979  N  N   . GLY B  1 41  ? 83.090  15.935  16.994  1.00 8.70  ? 41   GLY B N   1 
ATOM   2980  C  CA  . GLY B  1 41  ? 83.596  14.950  17.946  1.00 8.84  ? 41   GLY B CA  1 
ATOM   2981  C  C   . GLY B  1 41  ? 82.585  13.832  18.173  1.00 8.59  ? 41   GLY B C   1 
ATOM   2982  O  O   . GLY B  1 41  ? 82.885  12.673  17.909  1.00 9.77  ? 41   GLY B O   1 
ATOM   2983  N  N   . PRO B  1 42  ? 81.389  14.145  18.660  1.00 8.74  ? 42   PRO B N   1 
ATOM   2984  C  CA  . PRO B  1 42  ? 80.376  13.100  18.836  1.00 8.35  ? 42   PRO B CA  1 
ATOM   2985  C  C   . PRO B  1 42  ? 80.057  12.272  17.562  1.00 9.24  ? 42   PRO B C   1 
ATOM   2986  O  O   . PRO B  1 42  ? 79.934  11.030  17.655  1.00 9.09  ? 42   PRO B O   1 
ATOM   2987  C  CB  . PRO B  1 42  ? 79.145  13.883  19.338  1.00 8.12  ? 42   PRO B CB  1 
ATOM   2988  C  CG  . PRO B  1 42  ? 79.761  15.123  20.104  1.00 8.06  ? 42   PRO B CG  1 
ATOM   2989  C  CD  . PRO B  1 42  ? 80.901  15.470  19.115  1.00 8.60  ? 42   PRO B CD  1 
ATOM   2990  N  N   . SER B  1 43  ? 79.949  12.918  16.396  1.00 8.32  ? 43   SER B N   1 
ATOM   2991  C  CA  . SER B  1 43  ? 79.594  12.187  15.186  1.00 8.93  ? 43   SER B CA  1 
ATOM   2992  C  C   . SER B  1 43  ? 80.744  11.311  14.659  1.00 8.08  ? 43   SER B C   1 
ATOM   2993  O  O   . SER B  1 43  ? 80.515  10.290  14.000  1.00 9.16  ? 43   SER B O   1 
ATOM   2994  C  CB  . SER B  1 43  ? 79.087  13.118  14.105  1.00 5.46  ? 43   SER B CB  1 
ATOM   2995  O  OG  . SER B  1 43  ? 80.133  13.700  13.353  1.00 8.04  ? 43   SER B OG  1 
ATOM   2996  N  N   . SER B  1 44  ? 81.971  11.683  14.984  1.00 7.12  ? 44   SER B N   1 
ATOM   2997  C  CA  . SER B  1 44  ? 83.101  10.882  14.555  1.00 6.65  ? 44   SER B CA  1 
ATOM   2998  C  C   . SER B  1 44  ? 83.801  10.073  15.649  1.00 7.85  ? 44   SER B C   1 
ATOM   2999  O  O   . SER B  1 44  ? 84.874  9.466   15.387  1.00 8.57  ? 44   SER B O   1 
ATOM   3000  C  CB  . SER B  1 44  ? 84.121  11.815  13.897  1.00 8.49  ? 44   SER B CB  1 
ATOM   3001  O  OG  . SER B  1 44  ? 84.918  12.441  14.902  1.00 8.86  ? 44   SER B OG  1 
ATOM   3002  N  N   . GLY B  1 45  ? 83.226  9.994   16.855  1.00 6.98  ? 45   GLY B N   1 
ATOM   3003  C  CA  . GLY B  1 45  ? 83.876  9.285   17.948  1.00 7.03  ? 45   GLY B CA  1 
ATOM   3004  C  C   . GLY B  1 45  ? 85.202  9.936   18.292  1.00 7.84  ? 45   GLY B C   1 
ATOM   3005  O  O   . GLY B  1 45  ? 86.179  9.268   18.702  1.00 8.04  ? 45   GLY B O   1 
ATOM   3006  N  N   . TYR B  1 46  ? 85.218  11.256  18.105  1.00 7.57  ? 46   TYR B N   1 
ATOM   3007  C  CA  . TYR B  1 46  ? 86.325  12.142  18.486  1.00 8.92  ? 46   TYR B CA  1 
ATOM   3008  C  C   . TYR B  1 46  ? 87.555  12.035  17.612  1.00 9.59  ? 46   TYR B C   1 
ATOM   3009  O  O   . TYR B  1 46  ? 88.596  12.675  17.909  1.00 9.72  ? 46   TYR B O   1 
ATOM   3010  C  CB  . TYR B  1 46  ? 86.638  12.054  19.988  1.00 8.25  ? 46   TYR B CB  1 
ATOM   3011  C  CG  . TYR B  1 46  ? 85.354  12.118  20.742  1.00 9.98  ? 46   TYR B CG  1 
ATOM   3012  C  CD1 . TYR B  1 46  ? 84.736  13.324  20.990  1.00 6.54  ? 46   TYR B CD1 1 
ATOM   3013  C  CD2 . TYR B  1 46  ? 84.708  10.934  21.145  1.00 7.03  ? 46   TYR B CD2 1 
ATOM   3014  C  CE1 . TYR B  1 46  ? 83.529  13.357  21.654  1.00 7.83  ? 46   TYR B CE1 1 
ATOM   3015  C  CE2 . TYR B  1 46  ? 83.542  10.959  21.793  1.00 7.73  ? 46   TYR B CE2 1 
ATOM   3016  C  CZ  . TYR B  1 46  ? 82.953  12.163  22.043  1.00 8.04  ? 46   TYR B CZ  1 
ATOM   3017  O  OH  . TYR B  1 46  ? 81.759  12.154  22.649  1.00 10.12 ? 46   TYR B OH  1 
ATOM   3018  N  N   . ALA B  1 47  ? 87.415  11.294  16.504  1.00 8.95  ? 47   ALA B N   1 
ATOM   3019  C  CA  . ALA B  1 47  ? 88.476  11.199  15.502  1.00 10.22 ? 47   ALA B CA  1 
ATOM   3020  C  C   . ALA B  1 47  ? 88.880  12.513  14.821  1.00 9.17  ? 47   ALA B C   1 
ATOM   3021  O  O   . ALA B  1 47  ? 90.074  12.810  14.702  1.00 9.72  ? 47   ALA B O   1 
ATOM   3022  C  CB  . ALA B  1 47  ? 88.081  10.178  14.422  1.00 10.30 ? 47   ALA B CB  1 
ATOM   3023  N  N   . PHE B  1 48  ? 87.899  13.276  14.340  1.00 7.10  ? 48   PHE B N   1 
ATOM   3024  C  CA  . PHE B  1 48  ? 88.187  14.501  13.583  1.00 8.09  ? 48   PHE B CA  1 
ATOM   3025  C  C   . PHE B  1 48  ? 86.951  15.373  13.492  1.00 6.67  ? 48   PHE B C   1 
ATOM   3026  O  O   . PHE B  1 48  ? 85.806  14.905  13.663  1.00 8.04  ? 48   PHE B O   1 
ATOM   3027  C  CB  . PHE B  1 48  ? 88.787  14.248  12.165  1.00 7.87  ? 48   PHE B CB  1 
ATOM   3028  C  CG  . PHE B  1 48  ? 88.038  13.233  11.356  1.00 10.23 ? 48   PHE B CG  1 
ATOM   3029  C  CD1 . PHE B  1 48  ? 86.835  13.574  10.679  1.00 10.10 ? 48   PHE B CD1 1 
ATOM   3030  C  CD2 . PHE B  1 48  ? 88.530  11.937  11.255  1.00 9.46  ? 48   PHE B CD2 1 
ATOM   3031  C  CE1 . PHE B  1 48  ? 86.136  12.580  9.940   1.00 8.66  ? 48   PHE B CE1 1 
ATOM   3032  C  CE2 . PHE B  1 48  ? 87.798  10.931  10.545  1.00 11.18 ? 48   PHE B CE2 1 
ATOM   3033  C  CZ  . PHE B  1 48  ? 86.630  11.250  9.922   1.00 6.35  ? 48   PHE B CZ  1 
ATOM   3034  N  N   . THR B  1 49  ? 87.195  16.627  13.222  1.00 6.89  ? 49   THR B N   1 
ATOM   3035  C  CA  . THR B  1 49  ? 86.148  17.589  12.927  1.00 7.47  ? 49   THR B CA  1 
ATOM   3036  C  C   . THR B  1 49  ? 86.305  18.068  11.490  1.00 8.15  ? 49   THR B C   1 
ATOM   3037  O  O   . THR B  1 49  ? 87.420  18.427  11.086  1.00 8.07  ? 49   THR B O   1 
ATOM   3038  C  CB  . THR B  1 49  ? 86.334  18.777  13.847  1.00 7.71  ? 49   THR B CB  1 
ATOM   3039  O  OG1 . THR B  1 49  ? 85.985  18.401  15.183  1.00 7.18  ? 49   THR B OG1 1 
ATOM   3040  C  CG2 . THR B  1 49  ? 85.370  19.942  13.499  1.00 5.01  ? 49   THR B CG2 1 
ATOM   3041  N  N   . LEU B  1 50  ? 85.201  18.105  10.736  1.00 8.55  ? 50   LEU B N   1 
ATOM   3042  C  CA  . LEU B  1 50  ? 85.199  18.657  9.407   1.00 8.66  ? 50   LEU B CA  1 
ATOM   3043  C  C   . LEU B  1 50  ? 84.167  19.765  9.365   1.00 9.85  ? 50   LEU B C   1 
ATOM   3044  O  O   . LEU B  1 50  ? 82.945  19.517  9.545   1.00 9.17  ? 50   LEU B O   1 
ATOM   3045  C  CB  . LEU B  1 50  ? 84.883  17.580  8.370   1.00 8.28  ? 50   LEU B CB  1 
ATOM   3046  C  CG  . LEU B  1 50  ? 85.226  17.938  6.911   1.00 7.64  ? 50   LEU B CG  1 
ATOM   3047  C  CD1 . LEU B  1 50  ? 85.395  16.638  6.069   1.00 11.62 ? 50   LEU B CD1 1 
ATOM   3048  C  CD2 . LEU B  1 50  ? 84.116  18.796  6.336   1.00 8.99  ? 50   LEU B CD2 1 
ATOM   3049  N  N   . MET B  1 51  ? 84.644  20.984  9.186   1.00 8.85  ? 51   MET B N   1 
ATOM   3050  C  CA  . MET B  1 51  ? 83.728  22.117  9.184   1.00 10.12 ? 51   MET B CA  1 
ATOM   3051  C  C   . MET B  1 51  ? 83.848  22.984  7.935   1.00 10.54 ? 51   MET B C   1 
ATOM   3052  O  O   . MET B  1 51  ? 84.925  23.064  7.302   1.00 12.03 ? 51   MET B O   1 
ATOM   3053  C  CB  . MET B  1 51  ? 83.937  22.982  10.426  1.00 8.19  ? 51   MET B CB  1 
ATOM   3054  C  CG  . MET B  1 51  ? 85.338  23.550  10.577  1.00 14.34 ? 51   MET B CG  1 
ATOM   3055  S  SD  . MET B  1 51  ? 85.409  24.465  12.151  1.00 17.41 ? 51   MET B SD  1 
ATOM   3056  C  CE  . MET B  1 51  ? 86.794  25.446  11.862  1.00 17.33 ? 51   MET B CE  1 
ATOM   3057  N  N   . GLY B  1 52  ? 82.740  23.642  7.591   1.00 10.29 ? 52   GLY B N   1 
ATOM   3058  C  CA  . GLY B  1 52  ? 82.741  24.629  6.522   1.00 9.42  ? 52   GLY B CA  1 
ATOM   3059  C  C   . GLY B  1 52  ? 82.652  26.048  7.114   1.00 9.62  ? 52   GLY B C   1 
ATOM   3060  O  O   . GLY B  1 52  ? 81.977  26.217  8.090   1.00 11.22 ? 52   GLY B O   1 
ATOM   3061  N  N   . THR B  1 53  ? 83.395  27.022  6.603   1.00 8.24  ? 53   THR B N   1 
ATOM   3062  C  CA  . THR B  1 53  ? 83.208  28.427  7.023   1.00 8.26  ? 53   THR B CA  1 
ATOM   3063  C  C   . THR B  1 53  ? 82.945  29.173  5.716   1.00 7.79  ? 53   THR B C   1 
ATOM   3064  O  O   . THR B  1 53  ? 83.799  29.159  4.813   1.00 7.08  ? 53   THR B O   1 
ATOM   3065  C  CB  . THR B  1 53  ? 84.497  28.951  7.669   1.00 9.42  ? 53   THR B CB  1 
ATOM   3066  O  OG1 . THR B  1 53  ? 84.830  28.101  8.763   1.00 9.96  ? 53   THR B OG1 1 
ATOM   3067  C  CG2 . THR B  1 53  ? 84.326  30.346  8.336   1.00 5.66  ? 53   THR B CG2 1 
ATOM   3068  N  N   . ASN B  1 54  ? 81.797  29.834  5.592   1.00 8.29  ? 54   ASN B N   1 
ATOM   3069  C  CA  . ASN B  1 54  ? 81.549  30.676  4.414   1.00 7.00  ? 54   ASN B CA  1 
ATOM   3070  C  C   . ASN B  1 54  ? 81.602  32.106  4.905   1.00 8.13  ? 54   ASN B C   1 
ATOM   3071  O  O   . ASN B  1 54  ? 81.103  32.406  6.018   1.00 8.40  ? 54   ASN B O   1 
ATOM   3072  C  CB  . ASN B  1 54  ? 80.175  30.314  3.809   1.00 6.83  ? 54   ASN B CB  1 
ATOM   3073  C  CG  . ASN B  1 54  ? 80.200  28.982  3.122   1.00 10.01 ? 54   ASN B CG  1 
ATOM   3074  O  OD1 . ASN B  1 54  ? 80.184  27.943  3.759   1.00 12.22 ? 54   ASN B OD1 1 
ATOM   3075  N  ND2 . ASN B  1 54  ? 80.335  29.009  1.829   1.00 11.29 ? 54   ASN B ND2 1 
ATOM   3076  N  N   . ALA B  1 55  ? 82.180  33.020  4.116   1.00 7.95  ? 55   ALA B N   1 
ATOM   3077  C  CA  . ALA B  1 55  ? 82.290  34.395  4.608   1.00 7.21  ? 55   ALA B CA  1 
ATOM   3078  C  C   . ALA B  1 55  ? 82.620  35.344  3.485   1.00 7.36  ? 55   ALA B C   1 
ATOM   3079  O  O   . ALA B  1 55  ? 83.188  34.918  2.435   1.00 7.29  ? 55   ALA B O   1 
ATOM   3080  C  CB  . ALA B  1 55  ? 83.406  34.460  5.676   1.00 6.65  ? 55   ALA B CB  1 
ATOM   3081  N  N   . PRO B  1 56  ? 82.234  36.621  3.654   1.00 6.55  ? 56   PRO B N   1 
ATOM   3082  C  CA  . PRO B  1 56  ? 82.525  37.624  2.640   1.00 6.16  ? 56   PRO B CA  1 
ATOM   3083  C  C   . PRO B  1 56  ? 83.932  38.222  2.800   1.00 7.25  ? 56   PRO B C   1 
ATOM   3084  O  O   . PRO B  1 56  ? 84.694  37.904  3.742   1.00 7.60  ? 56   PRO B O   1 
ATOM   3085  C  CB  . PRO B  1 56  ? 81.455  38.708  2.915   1.00 5.08  ? 56   PRO B CB  1 
ATOM   3086  C  CG  . PRO B  1 56  ? 81.384  38.707  4.416   1.00 6.10  ? 56   PRO B CG  1 
ATOM   3087  C  CD  . PRO B  1 56  ? 81.406  37.165  4.762   1.00 6.55  ? 56   PRO B CD  1 
ATOM   3088  N  N   . HIS B  1 57  ? 84.284  39.080  1.857   1.00 7.03  ? 57   HIS B N   1 
ATOM   3089  C  CA  . HIS B  1 57  ? 85.561  39.748  1.893   1.00 7.97  ? 57   HIS B CA  1 
ATOM   3090  C  C   . HIS B  1 57  ? 85.650  40.515  3.218   1.00 9.00  ? 57   HIS B C   1 
ATOM   3091  O  O   . HIS B  1 57  ? 84.647  41.110  3.636   1.00 7.99  ? 57   HIS B O   1 
ATOM   3092  C  CB  . HIS B  1 57  ? 85.664  40.774  0.751   1.00 7.44  ? 57   HIS B CB  1 
ATOM   3093  C  CG  . HIS B  1 57  ? 86.804  41.739  0.928   1.00 10.27 ? 57   HIS B CG  1 
ATOM   3094  N  ND1 . HIS B  1 57  ? 88.104  41.419  0.603   1.00 9.54  ? 57   HIS B ND1 1 
ATOM   3095  C  CD2 . HIS B  1 57  ? 86.842  42.999  1.425   1.00 12.20 ? 57   HIS B CD2 1 
ATOM   3096  C  CE1 . HIS B  1 57  ? 88.891  42.453  0.856   1.00 11.08 ? 57   HIS B CE1 1 
ATOM   3097  N  NE2 . HIS B  1 57  ? 88.154  43.420  1.370   1.00 10.44 ? 57   HIS B NE2 1 
ATOM   3098  N  N   . SER B  1 58  ? 86.834  40.524  3.853   1.00 8.18  ? 58   SER B N   1 
ATOM   3099  C  CA  . SER B  1 58  ? 87.057  41.441  4.984   1.00 9.14  ? 58   SER B CA  1 
ATOM   3100  C  C   . SER B  1 58  ? 88.382  42.145  4.823   1.00 10.00 ? 58   SER B C   1 
ATOM   3101  O  O   . SER B  1 58  ? 89.353  41.529  4.329   1.00 10.10 ? 58   SER B O   1 
ATOM   3102  C  CB  . SER B  1 58  ? 87.098  40.673  6.305   1.00 9.44  ? 58   SER B CB  1 
ATOM   3103  O  OG  . SER B  1 58  ? 87.291  41.596  7.382   1.00 10.74 ? 58   SER B OG  1 
ATOM   3104  N  N   . ASP B  1 59  ? 88.461  43.396  5.258   1.00 10.75 ? 59   ASP B N   1 
ATOM   3105  C  CA  . ASP B  1 59  ? 89.741  44.122  5.277   1.00 11.65 ? 59   ASP B CA  1 
ATOM   3106  C  C   . ASP B  1 59  ? 90.566  43.816  6.522   1.00 12.83 ? 59   ASP B C   1 
ATOM   3107  O  O   . ASP B  1 59  ? 91.666  44.406  6.708   1.00 12.63 ? 59   ASP B O   1 
ATOM   3108  C  CB  . ASP B  1 59  ? 89.534  45.629  5.206   1.00 12.94 ? 59   ASP B CB  1 
ATOM   3109  C  CG  . ASP B  1 59  ? 88.863  46.038  3.934   1.00 16.86 ? 59   ASP B CG  1 
ATOM   3110  O  OD1 . ASP B  1 59  ? 89.184  45.426  2.879   1.00 19.08 ? 59   ASP B OD1 1 
ATOM   3111  O  OD2 . ASP B  1 59  ? 87.994  46.940  3.895   1.00 18.71 ? 59   ASP B OD2 1 
ATOM   3112  N  N   . ALA B  1 60  ? 90.061  42.896  7.352   1.00 13.05 ? 60   ALA B N   1 
ATOM   3113  C  CA  . ALA B  1 60  ? 90.676  42.645  8.641   1.00 12.91 ? 60   ALA B CA  1 
ATOM   3114  C  C   . ALA B  1 60  ? 90.920  41.162  8.793   1.00 12.32 ? 60   ALA B C   1 
ATOM   3115  O  O   . ALA B  1 60  ? 90.257  40.351  8.138   1.00 11.99 ? 60   ALA B O   1 
ATOM   3116  C  CB  . ALA B  1 60  ? 89.774  43.160  9.758   1.00 12.59 ? 60   ALA B CB  1 
ATOM   3117  N  N   . LEU B  1 61  ? 91.885  40.800  9.629   1.00 11.65 ? 61   LEU B N   1 
ATOM   3118  C  CA  . LEU B  1 61  ? 92.066  39.379  9.910   1.00 10.29 ? 61   LEU B CA  1 
ATOM   3119  C  C   . LEU B  1 61  ? 90.768  38.707  10.288  1.00 10.09 ? 61   LEU B C   1 
ATOM   3120  O  O   . LEU B  1 61  ? 89.847  39.362  10.835  1.00 8.07  ? 61   LEU B O   1 
ATOM   3121  C  CB  . LEU B  1 61  ? 93.096  39.193  11.011  1.00 10.96 ? 61   LEU B CB  1 
ATOM   3122  C  CG  . LEU B  1 61  ? 94.536  39.639  10.728  1.00 8.17  ? 61   LEU B CG  1 
ATOM   3123  C  CD1 . LEU B  1 61  ? 95.354  39.281  11.967  1.00 9.34  ? 61   LEU B CD1 1 
ATOM   3124  C  CD2 . LEU B  1 61  ? 95.086  38.962  9.468   1.00 9.62  ? 61   LEU B CD2 1 
ATOM   3125  N  N   . GLY B  1 62  ? 90.694  37.397  9.996   1.00 8.86  ? 62   GLY B N   1 
ATOM   3126  C  CA  . GLY B  1 62  ? 89.531  36.601  10.304  1.00 8.41  ? 62   GLY B CA  1 
ATOM   3127  C  C   . GLY B  1 62  ? 89.601  36.006  11.697  1.00 8.41  ? 62   GLY B C   1 
ATOM   3128  O  O   . GLY B  1 62  ? 88.646  35.443  12.181  1.00 7.14  ? 62   GLY B O   1 
ATOM   3129  N  N   . VAL B  1 63  ? 90.754  36.163  12.350  1.00 8.84  ? 63   VAL B N   1 
ATOM   3130  C  CA  . VAL B  1 63  ? 90.926  35.684  13.720  1.00 7.68  ? 63   VAL B CA  1 
ATOM   3131  C  C   . VAL B  1 63  ? 92.249  36.211  14.197  1.00 8.16  ? 63   VAL B C   1 
ATOM   3132  O  O   . VAL B  1 63  ? 93.130  36.494  13.382  1.00 7.85  ? 63   VAL B O   1 
ATOM   3133  C  CB  . VAL B  1 63  ? 90.927  34.171  13.789  1.00 5.86  ? 63   VAL B CB  1 
ATOM   3134  C  CG1 . VAL B  1 63  ? 92.047  33.579  12.934  1.00 7.81  ? 63   VAL B CG1 1 
ATOM   3135  C  CG2 . VAL B  1 63  ? 91.023  33.719  15.276  1.00 7.36  ? 63   VAL B CG2 1 
ATOM   3136  N  N   . LEU B  1 64  ? 92.400  36.360  15.505  1.00 8.25  ? 64   LEU B N   1 
ATOM   3137  C  CA  . LEU B  1 64  ? 93.687  36.857  15.994  1.00 9.26  ? 64   LEU B CA  1 
ATOM   3138  C  C   . LEU B  1 64  ? 94.685  35.706  15.952  1.00 8.88  ? 64   LEU B C   1 
ATOM   3139  O  O   . LEU B  1 64  ? 94.301  34.540  16.040  1.00 9.63  ? 64   LEU B O   1 
ATOM   3140  C  CB  . LEU B  1 64  ? 93.557  37.498  17.387  1.00 10.36 ? 64   LEU B CB  1 
ATOM   3141  C  CG  . LEU B  1 64  ? 93.016  38.944  17.414  1.00 12.98 ? 64   LEU B CG  1 
ATOM   3142  C  CD1 . LEU B  1 64  ? 92.550  39.328  18.859  1.00 13.53 ? 64   LEU B CD1 1 
ATOM   3143  C  CD2 . LEU B  1 64  ? 94.009  40.015  16.827  1.00 15.29 ? 64   LEU B CD2 1 
ATOM   3144  N  N   . PRO B  1 65  ? 95.956  36.010  15.720  1.00 8.76  ? 65   PRO B N   1 
ATOM   3145  C  CA  . PRO B  1 65  ? 96.972  34.953  15.627  1.00 7.87  ? 65   PRO B CA  1 
ATOM   3146  C  C   . PRO B  1 65  ? 97.022  34.090  16.884  1.00 7.04  ? 65   PRO B C   1 
ATOM   3147  O  O   . PRO B  1 65  ? 96.961  34.587  18.016  1.00 8.65  ? 65   PRO B O   1 
ATOM   3148  C  CB  . PRO B  1 65  ? 98.285  35.732  15.485  1.00 7.10  ? 65   PRO B CB  1 
ATOM   3149  C  CG  . PRO B  1 65  ? 97.898  37.116  15.069  1.00 8.80  ? 65   PRO B CG  1 
ATOM   3150  C  CD  . PRO B  1 65  ? 96.525  37.362  15.535  1.00 8.26  ? 65   PRO B CD  1 
ATOM   3151  N  N   . HIS B  1 66  ? 97.135  32.791  16.682  1.00 7.47  ? 66   HIS B N   1 
ATOM   3152  C  CA  . HIS B  1 66  ? 97.092  31.803  17.781  1.00 6.73  ? 66   HIS B CA  1 
ATOM   3153  C  C   . HIS B  1 66  ? 97.817  30.524  17.423  1.00 6.76  ? 66   HIS B C   1 
ATOM   3154  O  O   . HIS B  1 66  ? 98.201  30.317  16.250  1.00 6.18  ? 66   HIS B O   1 
ATOM   3155  C  CB  . HIS B  1 66  ? 95.629  31.434  18.128  1.00 7.01  ? 66   HIS B CB  1 
ATOM   3156  C  CG  . HIS B  1 66  ? 94.865  30.851  16.980  1.00 6.82  ? 66   HIS B CG  1 
ATOM   3157  N  ND1 . HIS B  1 66  ? 94.284  31.635  16.013  1.00 7.18  ? 66   HIS B ND1 1 
ATOM   3158  C  CD2 . HIS B  1 66  ? 94.596  29.564  16.637  1.00 4.65  ? 66   HIS B CD2 1 
ATOM   3159  C  CE1 . HIS B  1 66  ? 93.667  30.854  15.132  1.00 7.93  ? 66   HIS B CE1 1 
ATOM   3160  N  NE2 . HIS B  1 66  ? 93.860  29.592  15.485  1.00 6.65  ? 66   HIS B NE2 1 
ATOM   3161  N  N   . ILE B  1 67  ? 97.955  29.652  18.430  1.00 6.28  ? 67   ILE B N   1 
ATOM   3162  C  CA  . ILE B  1 67  ? 98.556  28.317  18.298  1.00 7.82  ? 67   ILE B CA  1 
ATOM   3163  C  C   . ILE B  1 67  ? 97.625  27.310  18.956  1.00 7.87  ? 67   ILE B C   1 
ATOM   3164  O  O   . ILE B  1 67  ? 96.931  27.658  19.908  1.00 8.41  ? 67   ILE B O   1 
ATOM   3165  C  CB  . ILE B  1 67  ? 99.909  28.299  19.053  1.00 9.24  ? 67   ILE B CB  1 
ATOM   3166  C  CG1 . ILE B  1 67  ? 101.104 28.344  18.138  1.00 9.42  ? 67   ILE B CG1 1 
ATOM   3167  C  CG2 . ILE B  1 67  ? 100.050 27.116  20.041  1.00 11.40 ? 67   ILE B CG2 1 
ATOM   3168  C  CD1 . ILE B  1 67  ? 102.338 28.747  18.910  1.00 15.15 ? 67   ILE B CD1 1 
ATOM   3169  N  N   . HIS B  1 68  ? 97.628  26.063  18.470  1.00 7.70  ? 68   HIS B N   1 
ATOM   3170  C  CA  . HIS B  1 68  ? 97.053  24.909  19.190  1.00 7.58  ? 68   HIS B CA  1 
ATOM   3171  C  C   . HIS B  1 68  ? 98.197  24.000  19.580  1.00 8.06  ? 68   HIS B C   1 
ATOM   3172  O  O   . HIS B  1 68  ? 99.085  23.737  18.748  1.00 8.46  ? 68   HIS B O   1 
ATOM   3173  C  CB  . HIS B  1 68  ? 96.057  24.127  18.279  1.00 6.18  ? 68   HIS B CB  1 
ATOM   3174  C  CG  . HIS B  1 68  ? 95.177  25.028  17.490  1.00 7.82  ? 68   HIS B CG  1 
ATOM   3175  N  ND1 . HIS B  1 68  ? 94.129  25.711  18.063  1.00 8.79  ? 68   HIS B ND1 1 
ATOM   3176  C  CD2 . HIS B  1 68  ? 95.215  25.412  16.191  1.00 10.93 ? 68   HIS B CD2 1 
ATOM   3177  C  CE1 . HIS B  1 68  ? 93.527  26.442  17.142  1.00 10.75 ? 68   HIS B CE1 1 
ATOM   3178  N  NE2 . HIS B  1 68  ? 94.171  26.289  16.001  1.00 13.07 ? 68   HIS B NE2 1 
ATOM   3179  N  N   . GLN B  1 69  ? 98.210  23.535  20.836  1.00 7.94  ? 69   GLN B N   1 
ATOM   3180  C  CA  . GLN B  1 69  ? 99.276  22.625  21.267  1.00 7.69  ? 69   GLN B CA  1 
ATOM   3181  C  C   . GLN B  1 69  ? 98.889  21.166  21.002  1.00 7.25  ? 69   GLN B C   1 
ATOM   3182  O  O   . GLN B  1 69  ? 99.747  20.289  20.924  1.00 7.49  ? 69   GLN B O   1 
ATOM   3183  C  CB  . GLN B  1 69  ? 99.545  22.810  22.753  1.00 8.16  ? 69   GLN B CB  1 
ATOM   3184  C  CG  . GLN B  1 69  ? 100.167 24.154  23.035  1.00 9.07  ? 69   GLN B CG  1 
ATOM   3185  C  CD  . GLN B  1 69  ? 100.570 24.352  24.483  1.00 11.53 ? 69   GLN B CD  1 
ATOM   3186  O  OE1 . GLN B  1 69  ? 100.612 23.407  25.287  1.00 9.83  ? 69   GLN B OE1 1 
ATOM   3187  N  NE2 . GLN B  1 69  ? 100.894 25.596  24.814  1.00 14.02 ? 69   GLN B NE2 1 
ATOM   3188  N  N   . LYS B  1 70  ? 97.603  20.907  20.845  1.00 7.69  ? 70   LYS B N   1 
ATOM   3189  C  CA  . LYS B  1 70  ? 97.135  19.521  20.768  1.00 8.19  ? 70   LYS B CA  1 
ATOM   3190  C  C   . LYS B  1 70  ? 96.262  19.219  19.543  1.00 8.64  ? 70   LYS B C   1 
ATOM   3191  O  O   . LYS B  1 70  ? 95.767  18.080  19.377  1.00 9.33  ? 70   LYS B O   1 
ATOM   3192  C  CB  . LYS B  1 70  ? 96.352  19.195  22.072  1.00 9.48  ? 70   LYS B CB  1 
ATOM   3193  C  CG  . LYS B  1 70  ? 97.174  19.212  23.380  1.00 10.64 ? 70   LYS B CG  1 
ATOM   3194  C  CD  . LYS B  1 70  ? 96.239  18.846  24.526  1.00 19.80 ? 70   LYS B CD  1 
ATOM   3195  C  CE  . LYS B  1 70  ? 96.960  18.779  25.869  1.00 27.00 ? 70   LYS B CE  1 
ATOM   3196  N  NZ  . LYS B  1 70  ? 96.022  19.236  26.984  1.00 29.62 ? 70   LYS B NZ  1 
ATOM   3197  N  N   . HIS B  1 71  ? 96.036  20.202  18.683  1.00 6.40  ? 71   HIS B N   1 
ATOM   3198  C  CA  . HIS B  1 71  ? 95.246  19.914  17.507  1.00 7.96  ? 71   HIS B CA  1 
ATOM   3199  C  C   . HIS B  1 71  ? 96.013  20.261  16.259  1.00 8.14  ? 71   HIS B C   1 
ATOM   3200  O  O   . HIS B  1 71  ? 96.731  21.255  16.206  1.00 9.52  ? 71   HIS B O   1 
ATOM   3201  C  CB  . HIS B  1 71  ? 93.887  20.674  17.509  1.00 6.86  ? 71   HIS B CB  1 
ATOM   3202  C  CG  . HIS B  1 71  ? 92.943  20.236  18.582  1.00 5.33  ? 71   HIS B CG  1 
ATOM   3203  N  ND1 . HIS B  1 71  ? 93.036  20.672  19.889  1.00 7.28  ? 71   HIS B ND1 1 
ATOM   3204  C  CD2 . HIS B  1 71  ? 91.839  19.437  18.531  1.00 9.53  ? 71   HIS B CD2 1 
ATOM   3205  C  CE1 . HIS B  1 71  ? 92.041  20.162  20.598  1.00 7.11  ? 71   HIS B CE1 1 
ATOM   3206  N  NE2 . HIS B  1 71  ? 91.306  19.401  19.801  1.00 10.53 ? 71   HIS B NE2 1 
ATOM   3207  N  N   . TYR B  1 72  ? 95.851  19.440  15.240  1.00 9.14  ? 72   TYR B N   1 
ATOM   3208  C  CA  . TYR B  1 72  ? 96.451  19.739  13.933  1.00 9.49  ? 72   TYR B CA  1 
ATOM   3209  C  C   . TYR B  1 72  ? 95.346  20.318  13.071  1.00 10.03 ? 72   TYR B C   1 
ATOM   3210  O  O   . TYR B  1 72  ? 94.245  19.718  12.968  1.00 9.35  ? 72   TYR B O   1 
ATOM   3211  C  CB  . TYR B  1 72  ? 96.989  18.444  13.385  1.00 9.53  ? 72   TYR B CB  1 
ATOM   3212  C  CG  . TYR B  1 72  ? 97.977  18.502  12.213  1.00 7.77  ? 72   TYR B CG  1 
ATOM   3213  C  CD1 . TYR B  1 72  ? 97.768  19.341  11.113  1.00 5.62  ? 72   TYR B CD1 1 
ATOM   3214  C  CD2 . TYR B  1 72  ? 99.117  17.674  12.226  1.00 6.93  ? 72   TYR B CD2 1 
ATOM   3215  C  CE1 . TYR B  1 72  ? 98.641  19.359  10.039  1.00 8.55  ? 72   TYR B CE1 1 
ATOM   3216  C  CE2 . TYR B  1 72  ? 99.998  17.673  11.169  1.00 8.04  ? 72   TYR B CE2 1 
ATOM   3217  C  CZ  . TYR B  1 72  ? 99.766  18.510  10.077  1.00 10.03 ? 72   TYR B CZ  1 
ATOM   3218  O  OH  . TYR B  1 72  ? 100.646 18.499  9.028   1.00 9.71  ? 72   TYR B OH  1 
ATOM   3219  N  N   . GLU B  1 73  ? 95.624  21.488  12.498  1.00 8.62  ? 73   GLU B N   1 
ATOM   3220  C  CA  . GLU B  1 73  ? 94.642  22.229  11.700  1.00 10.56 ? 73   GLU B CA  1 
ATOM   3221  C  C   . GLU B  1 73  ? 94.962  22.135  10.200  1.00 10.16 ? 73   GLU B C   1 
ATOM   3222  O  O   . GLU B  1 73  ? 96.112  22.239  9.765   1.00 10.84 ? 73   GLU B O   1 
ATOM   3223  C  CB  . GLU B  1 73  ? 94.597  23.679  12.143  1.00 12.58 ? 73   GLU B CB  1 
ATOM   3224  C  CG  . GLU B  1 73  ? 93.223  24.297  12.165  1.00 19.79 ? 73   GLU B CG  1 
ATOM   3225  C  CD  . GLU B  1 73  ? 93.006  25.205  13.363  1.00 29.47 ? 73   GLU B CD  1 
ATOM   3226  O  OE1 . GLU B  1 73  ? 93.769  26.214  13.489  1.00 29.04 ? 73   GLU B OE1 1 
ATOM   3227  O  OE2 . GLU B  1 73  ? 92.047  24.948  14.176  1.00 30.94 ? 73   GLU B OE2 1 
ATOM   3228  N  N   . ASN B  1 74  ? 93.939  21.902  9.415   1.00 8.58  ? 74   ASN B N   1 
ATOM   3229  C  CA  . ASN B  1 74  ? 94.102  21.834  7.972   1.00 7.45  ? 74   ASN B CA  1 
ATOM   3230  C  C   . ASN B  1 74  ? 93.177  22.809  7.293   1.00 7.34  ? 74   ASN B C   1 
ATOM   3231  O  O   . ASN B  1 74  ? 91.972  22.753  7.520   1.00 7.68  ? 74   ASN B O   1 
ATOM   3232  C  CB  . ASN B  1 74  ? 93.767  20.436  7.511   1.00 5.61  ? 74   ASN B CB  1 
ATOM   3233  C  CG  . ASN B  1 74  ? 94.766  19.406  8.080   1.00 9.13  ? 74   ASN B CG  1 
ATOM   3234  O  OD1 . ASN B  1 74  ? 95.852  19.302  7.582   1.00 7.81  ? 74   ASN B OD1 1 
ATOM   3235  N  ND2 . ASN B  1 74  ? 94.420  18.743  9.184   1.00 9.86  ? 74   ASN B ND2 1 
ATOM   3236  N  N   . PHE B  1 75  ? 93.712  23.667  6.426   1.00 8.19  ? 75   PHE B N   1 
ATOM   3237  C  CA  . PHE B  1 75  ? 92.897  24.695  5.735   1.00 8.92  ? 75   PHE B CA  1 
ATOM   3238  C  C   . PHE B  1 75  ? 92.766  24.313  4.300   1.00 9.23  ? 75   PHE B C   1 
ATOM   3239  O  O   . PHE B  1 75  ? 93.782  24.134  3.623   1.00 10.28 ? 75   PHE B O   1 
ATOM   3240  C  CB  . PHE B  1 75  ? 93.570  26.066  5.806   1.00 9.44  ? 75   PHE B CB  1 
ATOM   3241  C  CG  . PHE B  1 75  ? 93.564  26.637  7.174   1.00 11.70 ? 75   PHE B CG  1 
ATOM   3242  C  CD1 . PHE B  1 75  ? 94.468  26.173  8.150   1.00 12.22 ? 75   PHE B CD1 1 
ATOM   3243  C  CD2 . PHE B  1 75  ? 92.658  27.613  7.500   1.00 10.51 ? 75   PHE B CD2 1 
ATOM   3244  C  CE1 . PHE B  1 75  ? 94.422  26.682  9.462   1.00 9.59  ? 75   PHE B CE1 1 
ATOM   3245  C  CE2 . PHE B  1 75  ? 92.618  28.140  8.799   1.00 11.24 ? 75   PHE B CE2 1 
ATOM   3246  C  CZ  . PHE B  1 75  ? 93.515  27.683  9.768   1.00 11.73 ? 75   PHE B CZ  1 
ATOM   3247  N  N   . TYR B  1 76  ? 91.534  24.125  3.838   1.00 8.80  ? 76   TYR B N   1 
ATOM   3248  C  CA  . TYR B  1 76  ? 91.305  23.759  2.436   1.00 9.54  ? 76   TYR B CA  1 
ATOM   3249  C  C   . TYR B  1 76  ? 90.339  24.815  1.860   1.00 10.37 ? 76   TYR B C   1 
ATOM   3250  O  O   . TYR B  1 76  ? 89.306  25.122  2.458   1.00 10.77 ? 76   TYR B O   1 
ATOM   3251  C  CB  . TYR B  1 76  ? 90.692  22.365  2.329   1.00 9.35  ? 76   TYR B CB  1 
ATOM   3252  C  CG  . TYR B  1 76  ? 90.571  21.876  0.891   1.00 8.33  ? 76   TYR B CG  1 
ATOM   3253  C  CD1 . TYR B  1 76  ? 91.665  21.363  0.199   1.00 12.69 ? 76   TYR B CD1 1 
ATOM   3254  C  CD2 . TYR B  1 76  ? 89.341  21.921  0.243   1.00 10.68 ? 76   TYR B CD2 1 
ATOM   3255  C  CE1 . TYR B  1 76  ? 91.518  20.906  -1.144  1.00 11.84 ? 76   TYR B CE1 1 
ATOM   3256  C  CE2 . TYR B  1 76  ? 89.176  21.493  -1.075  1.00 11.42 ? 76   TYR B CE2 1 
ATOM   3257  C  CZ  . TYR B  1 76  ? 90.255  21.002  -1.761  1.00 10.05 ? 76   TYR B CZ  1 
ATOM   3258  O  OH  . TYR B  1 76  ? 90.016  20.580  -3.061  1.00 10.91 ? 76   TYR B OH  1 
ATOM   3259  N  N   . CYS B  1 77  ? 90.690  25.382  0.720   1.00 10.14 ? 77   CYS B N   1 
ATOM   3260  C  CA  . CYS B  1 77  ? 89.821  26.361  0.078   1.00 9.31  ? 77   CYS B CA  1 
ATOM   3261  C  C   . CYS B  1 77  ? 88.894  25.657  -0.911  1.00 9.32  ? 77   CYS B C   1 
ATOM   3262  O  O   . CYS B  1 77  ? 89.311  25.202  -1.994  1.00 10.69 ? 77   CYS B O   1 
ATOM   3263  C  CB  . CYS B  1 77  ? 90.678  27.390  -0.667  1.00 8.79  ? 77   CYS B CB  1 
ATOM   3264  S  SG  . CYS B  1 77  ? 89.647  28.651  -1.436  1.00 10.09 ? 77   CYS B SG  1 
ATOM   3265  N  N   . ASN B  1 78  ? 87.626  25.594  -0.574  1.00 9.11  ? 78   ASN B N   1 
ATOM   3266  C  CA  . ASN B  1 78  ? 86.622  25.039  -1.478  1.00 9.19  ? 78   ASN B CA  1 
ATOM   3267  C  C   . ASN B  1 78  ? 86.365  25.991  -2.631  1.00 9.96  ? 78   ASN B C   1 
ATOM   3268  O  O   . ASN B  1 78  ? 86.247  25.527  -3.765  1.00 9.60  ? 78   ASN B O   1 
ATOM   3269  C  CB  . ASN B  1 78  ? 85.353  24.817  -0.696  1.00 10.72 ? 78   ASN B CB  1 
ATOM   3270  C  CG  A ASN B  1 78  ? 85.601  24.038  0.491   0.50 11.19 ? 78   ASN B CG  1 
ATOM   3271  C  CG  B ASN B  1 78  ? 84.205  24.347  -1.519  0.50 11.89 ? 78   ASN B CG  1 
ATOM   3272  O  OD1 A ASN B  1 78  ? 85.876  24.609  1.532   0.50 12.37 ? 78   ASN B OD1 1 
ATOM   3273  O  OD1 B ASN B  1 78  ? 84.190  23.205  -2.000  0.50 15.82 ? 78   ASN B OD1 1 
ATOM   3274  N  ND2 A ASN B  1 78  ? 85.640  22.705  0.341   0.50 12.44 ? 78   ASN B ND2 1 
ATOM   3275  N  ND2 B ASN B  1 78  ? 83.185  25.197  -1.635  0.50 14.46 ? 78   ASN B ND2 1 
ATOM   3276  N  N   . LYS B  1 79  ? 86.246  27.290  -2.331  1.00 8.81  ? 79   LYS B N   1 
ATOM   3277  C  CA  . LYS B  1 79  ? 85.993  28.300  -3.362  1.00 7.30  ? 79   LYS B CA  1 
ATOM   3278  C  C   . LYS B  1 79  ? 86.401  29.629  -2.833  1.00 7.31  ? 79   LYS B C   1 
ATOM   3279  O  O   . LYS B  1 79  ? 86.596  29.782  -1.613  1.00 5.98  ? 79   LYS B O   1 
ATOM   3280  C  CB  . LYS B  1 79  ? 84.525  28.410  -3.841  1.00 8.16  ? 79   LYS B CB  1 
ATOM   3281  C  CG  . LYS B  1 79  ? 83.442  28.482  -2.750  1.00 4.87  ? 79   LYS B CG  1 
ATOM   3282  C  CD  . LYS B  1 79  ? 82.110  28.831  -3.397  1.00 6.92  ? 79   LYS B CD  1 
ATOM   3283  C  CE  . LYS B  1 79  ? 80.982  28.879  -2.352  1.00 7.98  ? 79   LYS B CE  1 
ATOM   3284  N  NZ  . LYS B  1 79  ? 79.631  29.031  -2.920  1.00 6.82  ? 79   LYS B NZ  1 
ATOM   3285  N  N   . GLY B  1 80  ? 86.464  30.607  -3.728  1.00 6.38  ? 80   GLY B N   1 
ATOM   3286  C  CA  . GLY B  1 80  ? 86.879  31.955  -3.323  1.00 6.97  ? 80   GLY B CA  1 
ATOM   3287  C  C   . GLY B  1 80  ? 88.350  31.955  -2.973  1.00 8.51  ? 80   GLY B C   1 
ATOM   3288  O  O   . GLY B  1 80  ? 89.135  31.334  -3.671  1.00 8.31  ? 80   GLY B O   1 
ATOM   3289  N  N   . SER B  1 81  ? 88.752  32.725  -1.942  1.00 8.86  ? 81   SER B N   1 
ATOM   3290  C  CA  . SER B  1 81  ? 90.144  32.733  -1.547  1.00 8.67  ? 81   SER B CA  1 
ATOM   3291  C  C   . SER B  1 81  ? 90.340  33.370  -0.206  1.00 8.36  ? 81   SER B C   1 
ATOM   3292  O  O   . SER B  1 81  ? 89.599  34.277  0.204   1.00 8.09  ? 81   SER B O   1 
ATOM   3293  C  CB  . SER B  1 81  ? 91.012  33.480  -2.583  1.00 9.20  ? 81   SER B CB  1 
ATOM   3294  O  OG  . SER B  1 81  ? 90.531  34.799  -2.783  1.00 7.79  ? 81   SER B OG  1 
ATOM   3295  N  N   . PHE B  1 82  ? 91.396  32.950  0.455   1.00 6.80  ? 82   PHE B N   1 
ATOM   3296  C  CA  . PHE B  1 82  ? 91.692  33.536  1.724   1.00 7.50  ? 82   PHE B CA  1 
ATOM   3297  C  C   . PHE B  1 82  ? 93.183  33.424  1.915   1.00 6.99  ? 82   PHE B C   1 
ATOM   3298  O  O   . PHE B  1 82  ? 93.791  32.466  1.412   1.00 6.31  ? 82   PHE B O   1 
ATOM   3299  C  CB  . PHE B  1 82  ? 90.876  32.836  2.845   1.00 7.22  ? 82   PHE B CB  1 
ATOM   3300  C  CG  . PHE B  1 82  ? 91.158  31.358  3.004   1.00 7.19  ? 82   PHE B CG  1 
ATOM   3301  C  CD1 . PHE B  1 82  ? 92.245  30.935  3.755   1.00 5.68  ? 82   PHE B CD1 1 
ATOM   3302  C  CD2 . PHE B  1 82  ? 90.352  30.401  2.410   1.00 8.45  ? 82   PHE B CD2 1 
ATOM   3303  C  CE1 . PHE B  1 82  ? 92.530  29.581  3.951   1.00 8.59  ? 82   PHE B CE1 1 
ATOM   3304  C  CE2 . PHE B  1 82  ? 90.626  29.038  2.545   1.00 9.41  ? 82   PHE B CE2 1 
ATOM   3305  C  CZ  . PHE B  1 82  ? 91.728  28.613  3.341   1.00 10.83 ? 82   PHE B CZ  1 
ATOM   3306  N  N   . GLN B  1 83  ? 93.751  34.399  2.607   1.00 7.42  ? 83   GLN B N   1 
ATOM   3307  C  CA  . GLN B  1 83  ? 95.206  34.383  2.934   1.00 8.18  ? 83   GLN B CA  1 
ATOM   3308  C  C   . GLN B  1 83  ? 95.419  33.637  4.236   1.00 9.84  ? 83   GLN B C   1 
ATOM   3309  O  O   . GLN B  1 83  ? 94.625  33.769  5.177   1.00 10.45 ? 83   GLN B O   1 
ATOM   3310  C  CB  . GLN B  1 83  ? 95.765  35.796  3.074   1.00 7.62  ? 83   GLN B CB  1 
ATOM   3311  C  CG  . GLN B  1 83  ? 97.300  35.803  3.252   1.00 8.08  ? 83   GLN B CG  1 
ATOM   3312  C  CD  . GLN B  1 83  ? 98.037  37.023  2.637   1.00 10.29 ? 83   GLN B CD  1 
ATOM   3313  O  OE1 . GLN B  1 83  ? 99.282  37.084  2.696   1.00 9.22  ? 83   GLN B OE1 1 
ATOM   3314  N  NE2 . GLN B  1 83  ? 97.304  37.970  2.077   1.00 8.08  ? 83   GLN B NE2 1 
ATOM   3315  N  N   . LEU B  1 84  ? 96.439  32.784  4.265   1.00 9.58  ? 84   LEU B N   1 
ATOM   3316  C  CA  . LEU B  1 84  ? 96.813  32.078  5.470   1.00 9.44  ? 84   LEU B CA  1 
ATOM   3317  C  C   . LEU B  1 84  ? 98.269  32.468  5.822   1.00 9.51  ? 84   LEU B C   1 
ATOM   3318  O  O   . LEU B  1 84  ? 99.121  32.539  4.930   1.00 8.64  ? 84   LEU B O   1 
ATOM   3319  C  CB  . LEU B  1 84  ? 96.666  30.570  5.247   1.00 8.88  ? 84   LEU B CB  1 
ATOM   3320  C  CG  . LEU B  1 84  ? 97.134  29.620  6.326   1.00 9.32  ? 84   LEU B CG  1 
ATOM   3321  C  CD1 . LEU B  1 84  ? 96.257  29.745  7.629   1.00 7.34  ? 84   LEU B CD1 1 
ATOM   3322  C  CD2 . LEU B  1 84  ? 97.069  28.227  5.723   1.00 9.64  ? 84   LEU B CD2 1 
ATOM   3323  N  N   . TRP B  1 85  ? 98.525  32.783  7.105   1.00 9.35  ? 85   TRP B N   1 
ATOM   3324  C  CA  . TRP B  1 85  ? 99.887  33.012  7.608   1.00 7.71  ? 85   TRP B CA  1 
ATOM   3325  C  C   . TRP B  1 85  ? 100.253 31.904  8.601   1.00 8.05  ? 85   TRP B C   1 
ATOM   3326  O  O   . TRP B  1 85  ? 99.390  31.416  9.354   1.00 8.63  ? 85   TRP B O   1 
ATOM   3327  C  CB  . TRP B  1 85  ? 100.043 34.366  8.320   1.00 6.43  ? 85   TRP B CB  1 
ATOM   3328  C  CG  . TRP B  1 85  ? 99.893  35.583  7.485   1.00 7.47  ? 85   TRP B CG  1 
ATOM   3329  C  CD1 . TRP B  1 85  ? 100.893 36.406  7.053   1.00 8.35  ? 85   TRP B CD1 1 
ATOM   3330  C  CD2 . TRP B  1 85  ? 98.662  36.200  7.067   1.00 7.47  ? 85   TRP B CD2 1 
ATOM   3331  N  NE1 . TRP B  1 85  ? 100.374 37.475  6.355   1.00 5.70  ? 85   TRP B NE1 1 
ATOM   3332  C  CE2 . TRP B  1 85  ? 99.002  37.375  6.356   1.00 7.89  ? 85   TRP B CE2 1 
ATOM   3333  C  CE3 . TRP B  1 85  ? 97.314  35.870  7.212   1.00 6.25  ? 85   TRP B CE3 1 
ATOM   3334  C  CZ2 . TRP B  1 85  ? 98.038  38.241  5.820   1.00 7.96  ? 85   TRP B CZ2 1 
ATOM   3335  C  CZ3 . TRP B  1 85  ? 96.355  36.703  6.677   1.00 3.90  ? 85   TRP B CZ3 1 
ATOM   3336  C  CH2 . TRP B  1 85  ? 96.718  37.879  5.964   1.00 5.84  ? 85   TRP B CH2 1 
ATOM   3337  N  N   . ALA B  1 86  ? 101.518 31.522  8.628   1.00 7.16  ? 86   ALA B N   1 
ATOM   3338  C  CA  . ALA B  1 86  ? 101.920 30.426  9.516   1.00 6.79  ? 86   ALA B CA  1 
ATOM   3339  C  C   . ALA B  1 86  ? 103.400 30.505  9.889   1.00 6.45  ? 86   ALA B C   1 
ATOM   3340  O  O   . ALA B  1 86  ? 104.249 30.803  9.049   1.00 5.38  ? 86   ALA B O   1 
ATOM   3341  C  CB  . ALA B  1 86  ? 101.545 29.083  8.882   1.00 7.19  ? 86   ALA B CB  1 
ATOM   3342  N  N   . GLN B  1 87  ? 103.716 30.286  11.166  1.00 5.92  ? 87   GLN B N   1 
ATOM   3343  C  CA  . GLN B  1 87  ? 105.113 30.258  11.574  1.00 5.59  ? 87   GLN B CA  1 
ATOM   3344  C  C   . GLN B  1 87  ? 105.370 29.196  12.629  1.00 6.47  ? 87   GLN B C   1 
ATOM   3345  O  O   . GLN B  1 87  ? 104.661 29.118  13.607  1.00 6.06  ? 87   GLN B O   1 
ATOM   3346  C  CB  . GLN B  1 87  ? 105.581 31.634  12.067  1.00 6.12  ? 87   GLN B CB  1 
ATOM   3347  C  CG  . GLN B  1 87  ? 107.017 31.704  12.389  1.00 4.82  ? 87   GLN B CG  1 
ATOM   3348  C  CD  . GLN B  1 87  ? 107.425 33.075  12.906  1.00 9.73  ? 87   GLN B CD  1 
ATOM   3349  O  OE1 . GLN B  1 87  ? 106.618 33.757  13.571  1.00 10.62 ? 87   GLN B OE1 1 
ATOM   3350  N  NE2 . GLN B  1 87  ? 108.678 33.478  12.637  1.00 9.22  ? 87   GLN B NE2 1 
ATOM   3351  N  N   . SER B  1 88  ? 106.399 28.381  12.395  1.00 6.59  ? 88   SER B N   1 
ATOM   3352  C  CA  . SER B  1 88  ? 106.887 27.426  13.411  1.00 6.71  ? 88   SER B CA  1 
ATOM   3353  C  C   . SER B  1 88  ? 108.133 28.010  14.076  1.00 7.30  ? 88   SER B C   1 
ATOM   3354  O  O   . SER B  1 88  ? 109.118 28.263  13.389  1.00 6.92  ? 88   SER B O   1 
ATOM   3355  C  CB  . SER B  1 88  ? 107.267 26.105  12.762  1.00 4.84  ? 88   SER B CB  1 
ATOM   3356  O  OG  . SER B  1 88  ? 107.890 25.319  13.771  1.00 6.98  ? 88   SER B OG  1 
ATOM   3357  N  N   . GLY B  1 89  ? 108.066 28.248  15.384  1.00 6.15  ? 89   GLY B N   1 
ATOM   3358  C  CA  . GLY B  1 89  ? 109.202 28.715  16.152  1.00 9.70  ? 89   GLY B CA  1 
ATOM   3359  C  C   . GLY B  1 89  ? 109.804 30.002  15.598  1.00 9.54  ? 89   GLY B C   1 
ATOM   3360  O  O   . GLY B  1 89  ? 109.115 31.021  15.436  1.00 8.79  ? 89   GLY B O   1 
ATOM   3361  N  N   . ASN B  1 90  ? 111.083 29.933  15.295  1.00 9.95  ? 90   ASN B N   1 
ATOM   3362  C  CA  . ASN B  1 90  ? 111.822 31.066  14.730  1.00 11.35 ? 90   ASN B CA  1 
ATOM   3363  C  C   . ASN B  1 90  ? 112.102 30.888  13.244  1.00 11.00 ? 90   ASN B C   1 
ATOM   3364  O  O   . ASN B  1 90  ? 112.928 31.613  12.664  1.00 11.96 ? 90   ASN B O   1 
ATOM   3365  C  CB  . ASN B  1 90  ? 113.131 31.283  15.517  1.00 11.89 ? 90   ASN B CB  1 
ATOM   3366  C  CG  . ASN B  1 90  ? 114.047 30.068  15.490  1.00 16.83 ? 90   ASN B CG  1 
ATOM   3367  O  OD1 . ASN B  1 90  ? 114.143 29.351  14.456  1.00 22.58 ? 90   ASN B OD1 1 
ATOM   3368  N  ND2 . ASN B  1 90  ? 114.782 29.833  16.632  1.00 19.75 ? 90   ASN B ND2 1 
ATOM   3369  N  N   . GLU B  1 91  ? 111.436 29.919  12.621  1.00 9.54  ? 91   GLU B N   1 
ATOM   3370  C  CA  . GLU B  1 91  ? 111.616 29.732  11.204  1.00 9.09  ? 91   GLU B CA  1 
ATOM   3371  C  C   . GLU B  1 91  ? 110.927 30.871  10.494  1.00 8.01  ? 91   GLU B C   1 
ATOM   3372  O  O   . GLU B  1 91  ? 110.048 31.530  11.038  1.00 8.79  ? 91   GLU B O   1 
ATOM   3373  C  CB  . GLU B  1 91  ? 111.010 28.433  10.711  1.00 9.52  ? 91   GLU B CB  1 
ATOM   3374  C  CG  . GLU B  1 91  ? 111.607 27.162  11.266  1.00 11.40 ? 91   GLU B CG  1 
ATOM   3375  C  CD  . GLU B  1 91  ? 110.706 25.990  10.923  1.00 16.69 ? 91   GLU B CD  1 
ATOM   3376  O  OE1 . GLU B  1 91  ? 109.912 26.104  9.961   1.00 23.17 ? 91   GLU B OE1 1 
ATOM   3377  O  OE2 . GLU B  1 91  ? 110.769 24.978  11.607  1.00 16.17 ? 91   GLU B OE2 1 
ATOM   3378  N  N   . THR B  1 92  ? 111.309 31.092  9.256   1.00 5.74  ? 92   THR B N   1 
ATOM   3379  C  CA  . THR B  1 92  ? 110.782 32.250  8.526   1.00 4.47  ? 92   THR B CA  1 
ATOM   3380  C  C   . THR B  1 92  ? 109.249 32.176  8.454   1.00 4.79  ? 92   THR B C   1 
ATOM   3381  O  O   . THR B  1 92  ? 108.675 31.126  8.137   1.00 3.89  ? 92   THR B O   1 
ATOM   3382  C  CB  . THR B  1 92  ? 111.334 32.238  7.129   1.00 2.79  ? 92   THR B CB  1 
ATOM   3383  O  OG1 . THR B  1 92  ? 112.750 32.423  7.204   1.00 4.26  ? 92   THR B OG1 1 
ATOM   3384  C  CG2 . THR B  1 92  ? 110.738 33.428  6.291   1.00 3.57  ? 92   THR B CG2 1 
ATOM   3385  N  N   . GLN B  1 93  ? 108.570 33.281  8.731   1.00 4.53  ? 93   GLN B N   1 
ATOM   3386  C  CA  . GLN B  1 93  ? 107.086 33.225  8.610   1.00 5.86  ? 93   GLN B CA  1 
ATOM   3387  C  C   . GLN B  1 93  ? 106.666 33.054  7.134   1.00 6.05  ? 93   GLN B C   1 
ATOM   3388  O  O   . GLN B  1 93  ? 107.234 33.706  6.235   1.00 6.43  ? 93   GLN B O   1 
ATOM   3389  C  CB  . GLN B  1 93  ? 106.487 34.516  9.210   1.00 6.06  ? 93   GLN B CB  1 
ATOM   3390  C  CG  . GLN B  1 93  ? 104.971 34.555  9.195   1.00 4.83  ? 93   GLN B CG  1 
ATOM   3391  C  CD  . GLN B  1 93  ? 104.409 35.967  9.372   1.00 5.26  ? 93   GLN B CD  1 
ATOM   3392  O  OE1 . GLN B  1 93  ? 103.468 36.328  8.694   1.00 7.59  ? 93   GLN B OE1 1 
ATOM   3393  N  NE2 . GLN B  1 93  ? 104.958 36.734  10.312  1.00 6.16  ? 93   GLN B NE2 1 
ATOM   3394  N  N   . GLN B  1 94  ? 105.657 32.205  6.877   1.00 5.81  ? 94   GLN B N   1 
ATOM   3395  C  CA  . GLN B  1 94  ? 105.227 31.941  5.527   1.00 6.97  ? 94   GLN B CA  1 
ATOM   3396  C  C   . GLN B  1 94  ? 103.773 32.395  5.356   1.00 6.37  ? 94   GLN B C   1 
ATOM   3397  O  O   . GLN B  1 94  ? 102.975 32.299  6.278   1.00 6.41  ? 94   GLN B O   1 
ATOM   3398  C  CB  . GLN B  1 94  ? 105.233 30.426  5.284   1.00 7.31  ? 94   GLN B CB  1 
ATOM   3399  C  CG  . GLN B  1 94  ? 106.627 29.780  5.341   1.00 9.20  ? 94   GLN B CG  1 
ATOM   3400  C  CD  . GLN B  1 94  ? 107.498 30.170  4.143   1.00 10.66 ? 94   GLN B CD  1 
ATOM   3401  O  OE1 . GLN B  1 94  ? 106.974 30.511  3.089   1.00 10.57 ? 94   GLN B OE1 1 
ATOM   3402  N  NE2 . GLN B  1 94  ? 108.811 30.125  4.306   1.00 9.83  ? 94   GLN B NE2 1 
ATOM   3403  N  N   . THR B  1 95  ? 103.439 32.913  4.191   1.00 6.74  ? 95   THR B N   1 
ATOM   3404  C  CA  . THR B  1 95  ? 102.030 33.161  3.928   1.00 7.13  ? 95   THR B CA  1 
ATOM   3405  C  C   . THR B  1 95  ? 101.671 32.827  2.482   1.00 7.20  ? 95   THR B C   1 
ATOM   3406  O  O   . THR B  1 95  ? 102.488 33.030  1.601   1.00 7.04  ? 95   THR B O   1 
ATOM   3407  C  CB  . THR B  1 95  ? 101.664 34.606  4.298   1.00 5.95  ? 95   THR B CB  1 
ATOM   3408  O  OG1 . THR B  1 95  ? 100.254 34.788  4.048   1.00 7.41  ? 95   THR B OG1 1 
ATOM   3409  C  CG2 . THR B  1 95  ? 102.303 35.599  3.361   1.00 6.73  ? 95   THR B CG2 1 
ATOM   3410  N  N   . ARG B  1 96  ? 100.445 32.330  2.239   1.00 8.41  ? 96   ARG B N   1 
ATOM   3411  C  CA  . ARG B  1 96  ? 99.966  32.041  0.876   1.00 8.53  ? 96   ARG B CA  1 
ATOM   3412  C  C   . ARG B  1 96  ? 98.524  32.505  0.793   1.00 8.24  ? 96   ARG B C   1 
ATOM   3413  O  O   . ARG B  1 96  ? 97.805  32.517  1.817   1.00 6.81  ? 96   ARG B O   1 
ATOM   3414  C  CB  . ARG B  1 96  ? 99.959  30.525  0.562   1.00 7.62  ? 96   ARG B CB  1 
ATOM   3415  C  CG  . ARG B  1 96  ? 101.334 29.857  0.819   1.00 8.11  ? 96   ARG B CG  1 
ATOM   3416  C  CD  . ARG B  1 96  ? 102.373 30.190  -0.278  1.00 10.12 ? 96   ARG B CD  1 
ATOM   3417  N  NE  . ARG B  1 96  ? 103.568 29.380  -0.102  1.00 6.86  ? 96   ARG B NE  1 
ATOM   3418  C  CZ  . ARG B  1 96  ? 104.573 29.661  0.747   1.00 9.82  ? 96   ARG B CZ  1 
ATOM   3419  N  NH1 . ARG B  1 96  ? 104.594 30.771  1.479   1.00 9.43  ? 96   ARG B NH1 1 
ATOM   3420  N  NH2 . ARG B  1 96  ? 105.569 28.806  0.841   1.00 9.77  ? 96   ARG B NH2 1 
ATOM   3421  N  N   . VAL B  1 97  ? 98.123  32.889  -0.400  1.00 7.57  ? 97   VAL B N   1 
ATOM   3422  C  CA  . VAL B  1 97  ? 96.720  33.192  -0.618  1.00 8.86  ? 97   VAL B CA  1 
ATOM   3423  C  C   . VAL B  1 97  ? 96.144  31.948  -1.276  1.00 8.02  ? 97   VAL B C   1 
ATOM   3424  O  O   . VAL B  1 97  ? 96.557  31.567  -2.399  1.00 8.64  ? 97   VAL B O   1 
ATOM   3425  C  CB  . VAL B  1 97  ? 96.544  34.370  -1.527  1.00 8.16  ? 97   VAL B CB  1 
ATOM   3426  C  CG1 . VAL B  1 97  ? 95.005  34.599  -1.787  1.00 9.68  ? 97   VAL B CG1 1 
ATOM   3427  C  CG2 . VAL B  1 97  ? 97.207  35.639  -0.913  1.00 9.84  ? 97   VAL B CG2 1 
ATOM   3428  N  N   . LEU B  1 98  ? 95.208  31.311  -0.600  1.00 7.86  ? 98   LEU B N   1 
ATOM   3429  C  CA  . LEU B  1 98  ? 94.730  30.045  -1.110  1.00 8.25  ? 98   LEU B CA  1 
ATOM   3430  C  C   . LEU B  1 98  ? 93.510  30.341  -1.968  1.00 8.76  ? 98   LEU B C   1 
ATOM   3431  O  O   . LEU B  1 98  ? 92.648  31.047  -1.542  1.00 9.15  ? 98   LEU B O   1 
ATOM   3432  C  CB  . LEU B  1 98  ? 94.391  29.078  0.034   1.00 8.76  ? 98   LEU B CB  1 
ATOM   3433  C  CG  . LEU B  1 98  ? 95.574  28.389  0.779   1.00 8.02  ? 98   LEU B CG  1 
ATOM   3434  C  CD1 . LEU B  1 98  ? 96.309  29.364  1.676   1.00 12.45 ? 98   LEU B CD1 1 
ATOM   3435  C  CD2 . LEU B  1 98  ? 94.928  27.257  1.651   1.00 11.45 ? 98   LEU B CD2 1 
ATOM   3436  N  N   . SER B  1 99  ? 93.447  29.774  -3.181  1.00 9.67  ? 99   SER B N   1 
ATOM   3437  C  CA  . SER B  1 99  ? 92.256  29.868  -3.993  1.00 8.33  ? 99   SER B CA  1 
ATOM   3438  C  C   . SER B  1 99  ? 91.758  28.431  -4.148  1.00 9.16  ? 99   SER B C   1 
ATOM   3439  O  O   . SER B  1 99  ? 92.259  27.507  -3.487  1.00 9.61  ? 99   SER B O   1 
ATOM   3440  C  CB  . SER B  1 99  ? 92.566  30.518  -5.366  1.00 7.53  ? 99   SER B CB  1 
ATOM   3441  O  OG  . SER B  1 99  ? 93.666  29.822  -5.986  1.00 8.63  ? 99   SER B OG  1 
ATOM   3442  N  N   . SER B  1 100 ? 90.726  28.260  -4.974  1.00 8.25  ? 100  SER B N   1 
ATOM   3443  C  CA  . SER B  1 100 ? 89.991  26.993  -5.026  1.00 8.05  ? 100  SER B CA  1 
ATOM   3444  C  C   . SER B  1 100 ? 90.865  25.762  -5.187  1.00 8.57  ? 100  SER B C   1 
ATOM   3445  O  O   . SER B  1 100 ? 91.679  25.669  -6.145  1.00 8.96  ? 100  SER B O   1 
ATOM   3446  C  CB  . SER B  1 100 ? 89.045  27.008  -6.206  1.00 7.81  ? 100  SER B CB  1 
ATOM   3447  O  OG  A SER B  1 100 ? 88.080  25.988  -6.018  0.50 10.76 ? 100  SER B OG  1 
ATOM   3448  O  OG  B SER B  1 100 ? 87.954  27.891  -6.068  0.50 4.40  ? 100  SER B OG  1 
ATOM   3449  N  N   . GLY B  1 101 ? 90.713  24.785  -4.295  1.00 7.80  ? 101  GLY B N   1 
ATOM   3450  C  CA  . GLY B  1 101 ? 91.507  23.596  -4.421  1.00 7.89  ? 101  GLY B CA  1 
ATOM   3451  C  C   . GLY B  1 101 ? 92.860  23.627  -3.693  1.00 8.88  ? 101  GLY B C   1 
ATOM   3452  O  O   . GLY B  1 101 ? 93.557  22.621  -3.636  1.00 8.66  ? 101  GLY B O   1 
ATOM   3453  N  N   . ASP B  1 102 ? 93.240  24.773  -3.147  1.00 9.22  ? 102  ASP B N   1 
ATOM   3454  C  CA  . ASP B  1 102 ? 94.535  24.930  -2.487  1.00 9.10  ? 102  ASP B CA  1 
ATOM   3455  C  C   . ASP B  1 102 ? 94.493  24.463  -1.039  1.00 8.68  ? 102  ASP B C   1 
ATOM   3456  O  O   . ASP B  1 102 ? 93.442  24.532  -0.409  1.00 9.60  ? 102  ASP B O   1 
ATOM   3457  C  CB  . ASP B  1 102 ? 94.934  26.394  -2.463  1.00 9.67  ? 102  ASP B CB  1 
ATOM   3458  C  CG  . ASP B  1 102 ? 95.343  26.959  -3.834  1.00 10.50 ? 102  ASP B CG  1 
ATOM   3459  O  OD1 . ASP B  1 102 ? 95.401  26.225  -4.842  1.00 8.32  ? 102  ASP B OD1 1 
ATOM   3460  O  OD2 . ASP B  1 102 ? 95.637  28.178  -3.986  1.00 9.41  ? 102  ASP B OD2 1 
ATOM   3461  N  N   . TYR B  1 103 ? 95.657  24.133  -0.464  1.00 8.91  ? 103  TYR B N   1 
ATOM   3462  C  CA  . TYR B  1 103 ? 95.676  23.493  0.853   1.00 8.50  ? 103  TYR B CA  1 
ATOM   3463  C  C   . TYR B  1 103 ? 96.782  24.066  1.710   1.00 8.79  ? 103  TYR B C   1 
ATOM   3464  O  O   . TYR B  1 103 ? 97.878  24.312  1.192   1.00 7.64  ? 103  TYR B O   1 
ATOM   3465  C  CB  . TYR B  1 103 ? 95.881  21.989  0.681   1.00 9.05  ? 103  TYR B CB  1 
ATOM   3466  C  CG  . TYR B  1 103 ? 96.264  21.300  1.964   1.00 10.60 ? 103  TYR B CG  1 
ATOM   3467  C  CD1 . TYR B  1 103 ? 95.309  21.113  2.986   1.00 8.92  ? 103  TYR B CD1 1 
ATOM   3468  C  CD2 . TYR B  1 103 ? 97.577  20.868  2.178   1.00 10.30 ? 103  TYR B CD2 1 
ATOM   3469  C  CE1 . TYR B  1 103 ? 95.646  20.505  4.182   1.00 11.01 ? 103  TYR B CE1 1 
ATOM   3470  C  CE2 . TYR B  1 103 ? 97.935  20.252  3.377   1.00 12.01 ? 103  TYR B CE2 1 
ATOM   3471  C  CZ  . TYR B  1 103 ? 96.963  20.070  4.377   1.00 10.58 ? 103  TYR B CZ  1 
ATOM   3472  O  OH  . TYR B  1 103 ? 97.330  19.435  5.536   1.00 12.42 ? 103  TYR B OH  1 
ATOM   3473  N  N   . GLY B  1 104 ? 96.462  24.353  2.986   1.00 7.62  ? 104  GLY B N   1 
ATOM   3474  C  CA  . GLY B  1 104 ? 97.462  24.769  3.959   1.00 8.55  ? 104  GLY B CA  1 
ATOM   3475  C  C   . GLY B  1 104 ? 97.480  23.869  5.191   1.00 8.63  ? 104  GLY B C   1 
ATOM   3476  O  O   . GLY B  1 104 ? 96.437  23.591  5.803   1.00 9.71  ? 104  GLY B O   1 
ATOM   3477  N  N   . SER B  1 105 ? 98.672  23.378  5.556   1.00 8.35  ? 105  SER B N   1 
ATOM   3478  C  CA  . SER B  1 105 ? 98.792  22.486  6.701   1.00 7.69  ? 105  SER B CA  1 
ATOM   3479  C  C   . SER B  1 105 ? 99.390  23.237  7.881   1.00 8.49  ? 105  SER B C   1 
ATOM   3480  O  O   . SER B  1 105 ? 100.444 23.888  7.741   1.00 7.07  ? 105  SER B O   1 
ATOM   3481  C  CB  . SER B  1 105 ? 99.749  21.375  6.341   1.00 6.70  ? 105  SER B CB  1 
ATOM   3482  O  OG  . SER B  1 105 ? 99.499  20.301  7.180   1.00 10.82 ? 105  SER B OG  1 
ATOM   3483  N  N   . VAL B  1 106 ? 98.738  23.117  9.043   1.00 8.20  ? 106  VAL B N   1 
ATOM   3484  C  CA  . VAL B  1 106 ? 99.145  23.842  10.255  1.00 8.06  ? 106  VAL B CA  1 
ATOM   3485  C  C   . VAL B  1 106 ? 99.258  22.824  11.414  1.00 7.76  ? 106  VAL B C   1 
ATOM   3486  O  O   . VAL B  1 106 ? 98.281  22.576  12.178  1.00 7.53  ? 106  VAL B O   1 
ATOM   3487  C  CB  . VAL B  1 106 ? 98.126  24.951  10.557  1.00 8.95  ? 106  VAL B CB  1 
ATOM   3488  C  CG1 . VAL B  1 106 ? 98.472  25.751  11.807  1.00 8.88  ? 106  VAL B CG1 1 
ATOM   3489  C  CG2 . VAL B  1 106 ? 97.986  25.916  9.353   1.00 7.91  ? 106  VAL B CG2 1 
ATOM   3490  N  N   . PRO B  1 107 ? 100.428 22.187  11.522  1.00 6.75  ? 107  PRO B N   1 
ATOM   3491  C  CA  . PRO B  1 107 ? 100.709 21.297  12.663  1.00 6.81  ? 107  PRO B CA  1 
ATOM   3492  C  C   . PRO B  1 107 ? 100.542 22.006  14.021  1.00 6.86  ? 107  PRO B C   1 
ATOM   3493  O  O   . PRO B  1 107 ? 100.368 23.253  14.113  1.00 7.27  ? 107  PRO B O   1 
ATOM   3494  C  CB  . PRO B  1 107 ? 102.157 20.832  12.439  1.00 5.95  ? 107  PRO B CB  1 
ATOM   3495  C  CG  . PRO B  1 107 ? 102.494 21.142  10.931  1.00 6.53  ? 107  PRO B CG  1 
ATOM   3496  C  CD  . PRO B  1 107 ? 101.542 22.249  10.541  1.00 7.07  ? 107  PRO B CD  1 
ATOM   3497  N  N   . ARG B  1 108 ? 100.522 21.201  15.063  1.00 6.96  ? 108  ARG B N   1 
ATOM   3498  C  CA  . ARG B  1 108 ? 100.515 21.693  16.423  1.00 7.75  ? 108  ARG B CA  1 
ATOM   3499  C  C   . ARG B  1 108 ? 101.686 22.636  16.609  1.00 8.28  ? 108  ARG B C   1 
ATOM   3500  O  O   . ARG B  1 108 ? 102.750 22.433  16.022  1.00 8.59  ? 108  ARG B O   1 
ATOM   3501  C  CB  . ARG B  1 108 ? 100.641 20.547  17.429  1.00 8.47  ? 108  ARG B CB  1 
ATOM   3502  C  CG  . ARG B  1 108 ? 99.425  19.576  17.395  1.00 9.63  ? 108  ARG B CG  1 
ATOM   3503  C  CD  . ARG B  1 108 ? 99.665  18.289  18.140  1.00 10.50 ? 108  ARG B CD  1 
ATOM   3504  N  NE  . ARG B  1 108 ? 100.601 17.442  17.401  1.00 7.55  ? 108  ARG B NE  1 
ATOM   3505  C  CZ  . ARG B  1 108 ? 100.982 16.209  17.782  1.00 11.76 ? 108  ARG B CZ  1 
ATOM   3506  N  NH1 . ARG B  1 108 ? 100.522 15.695  18.900  1.00 5.77  ? 108  ARG B NH1 1 
ATOM   3507  N  NH2 . ARG B  1 108 ? 101.853 15.494  17.052  1.00 8.47  ? 108  ARG B NH2 1 
ATOM   3508  N  N   . ASN B  1 109 ? 101.470 23.655  17.433  1.00 8.99  ? 109  ASN B N   1 
ATOM   3509  C  CA  . ASN B  1 109 ? 102.509 24.617  17.847  1.00 8.75  ? 109  ASN B CA  1 
ATOM   3510  C  C   . ASN B  1 109 ? 102.987 25.459  16.687  1.00 9.59  ? 109  ASN B C   1 
ATOM   3511  O  O   . ASN B  1 109 ? 104.169 25.769  16.605  1.00 9.75  ? 109  ASN B O   1 
ATOM   3512  C  CB  . ASN B  1 109 ? 103.699 23.907  18.457  1.00 10.18 ? 109  ASN B CB  1 
ATOM   3513  C  CG  . ASN B  1 109 ? 103.414 23.422  19.856  1.00 11.33 ? 109  ASN B CG  1 
ATOM   3514  O  OD1 . ASN B  1 109 ? 102.436 23.855  20.488  1.00 11.04 ? 109  ASN B OD1 1 
ATOM   3515  N  ND2 . ASN B  1 109 ? 104.243 22.501  20.333  1.00 14.45 ? 109  ASN B ND2 1 
ATOM   3516  N  N   . VAL B  1 110 ? 102.081 25.789  15.773  1.00 7.03  ? 110  VAL B N   1 
ATOM   3517  C  CA  . VAL B  1 110 ? 102.402 26.700  14.679  1.00 7.50  ? 110  VAL B CA  1 
ATOM   3518  C  C   . VAL B  1 110 ? 101.491 27.879  14.769  1.00 7.23  ? 110  VAL B C   1 
ATOM   3519  O  O   . VAL B  1 110 ? 100.270 27.729  14.748  1.00 5.75  ? 110  VAL B O   1 
ATOM   3520  C  CB  . VAL B  1 110 ? 102.194 26.048  13.296  1.00 6.77  ? 110  VAL B CB  1 
ATOM   3521  C  CG1 . VAL B  1 110 ? 102.288 27.079  12.164  1.00 5.55  ? 110  VAL B CG1 1 
ATOM   3522  C  CG2 . VAL B  1 110 ? 103.212 24.928  13.071  1.00 7.58  ? 110  VAL B CG2 1 
ATOM   3523  N  N   . THR B  1 111 ? 102.078 29.060  14.889  1.00 6.42  ? 111  THR B N   1 
ATOM   3524  C  CA  . THR B  1 111 ? 101.270 30.274  14.961  1.00 8.19  ? 111  THR B CA  1 
ATOM   3525  C  C   . THR B  1 111 ? 100.622 30.539  13.622  1.00 7.91  ? 111  THR B C   1 
ATOM   3526  O  O   . THR B  1 111 ? 101.275 30.441  12.587  1.00 7.00  ? 111  THR B O   1 
ATOM   3527  C  CB  . THR B  1 111 ? 102.169 31.443  15.295  1.00 8.23  ? 111  THR B CB  1 
ATOM   3528  O  OG1 . THR B  1 111 ? 102.814 31.161  16.520  1.00 8.69  ? 111  THR B OG1 1 
ATOM   3529  C  CG2 . THR B  1 111 ? 101.334 32.741  15.574  1.00 8.66  ? 111  THR B CG2 1 
ATOM   3530  N  N   . HIS B  1 112 ? 99.354  30.930  13.624  1.00 7.13  ? 112  HIS B N   1 
ATOM   3531  C  CA  . HIS B  1 112 ? 98.669  31.119  12.369  1.00 6.43  ? 112  HIS B CA  1 
ATOM   3532  C  C   . HIS B  1 112 ? 97.492  32.089  12.481  1.00 7.29  ? 112  HIS B C   1 
ATOM   3533  O  O   . HIS B  1 112 ? 96.953  32.351  13.587  1.00 5.59  ? 112  HIS B O   1 
ATOM   3534  C  CB  . HIS B  1 112 ? 98.202  29.756  11.773  1.00 7.15  ? 112  HIS B CB  1 
ATOM   3535  C  CG  . HIS B  1 112 ? 97.286  28.988  12.667  1.00 7.95  ? 112  HIS B CG  1 
ATOM   3536  N  ND1 . HIS B  1 112 ? 97.727  28.375  13.821  1.00 7.61  ? 112  HIS B ND1 1 
ATOM   3537  C  CD2 . HIS B  1 112 ? 95.955  28.709  12.572  1.00 7.01  ? 112  HIS B CD2 1 
ATOM   3538  C  CE1 . HIS B  1 112 ? 96.712  27.757  14.402  1.00 6.30  ? 112  HIS B CE1 1 
ATOM   3539  N  NE2 . HIS B  1 112 ? 95.629  27.958  13.676  1.00 7.32  ? 112  HIS B NE2 1 
ATOM   3540  N  N   . THR B  1 113 ? 97.093  32.613  11.332  1.00 7.21  ? 113  THR B N   1 
ATOM   3541  C  CA  . THR B  1 113 ? 95.877  33.406  11.240  1.00 7.71  ? 113  THR B CA  1 
ATOM   3542  C  C   . THR B  1 113 ? 95.422  33.385  9.776   1.00 8.27  ? 113  THR B C   1 
ATOM   3543  O  O   . THR B  1 113 ? 96.169  32.907  8.932   1.00 6.56  ? 113  THR B O   1 
ATOM   3544  C  CB  . THR B  1 113 ? 96.041  34.829  11.785  1.00 8.61  ? 113  THR B CB  1 
ATOM   3545  O  OG1 . THR B  1 113 ? 94.861  35.586  11.464  1.00 7.53  ? 113  THR B OG1 1 
ATOM   3546  C  CG2 . THR B  1 113 ? 97.201  35.571  11.125  1.00 6.91  ? 113  THR B CG2 1 
ATOM   3547  N  N   . PHE B  1 114 ? 94.217  33.879  9.469   1.00 7.15  ? 114  PHE B N   1 
ATOM   3548  C  CA  . PHE B  1 114 ? 93.811  33.913  8.083   1.00 7.45  ? 114  PHE B CA  1 
ATOM   3549  C  C   . PHE B  1 114 ? 93.034  35.200  7.822   1.00 6.97  ? 114  PHE B C   1 
ATOM   3550  O  O   . PHE B  1 114 ? 92.597  35.879  8.769   1.00 7.24  ? 114  PHE B O   1 
ATOM   3551  C  CB  . PHE B  1 114 ? 92.973  32.629  7.705   1.00 5.62  ? 114  PHE B CB  1 
ATOM   3552  C  CG  . PHE B  1 114 ? 91.702  32.495  8.503   1.00 7.99  ? 114  PHE B CG  1 
ATOM   3553  C  CD1 . PHE B  1 114 ? 90.523  33.151  8.099   1.00 8.44  ? 114  PHE B CD1 1 
ATOM   3554  C  CD2 . PHE B  1 114 ? 91.703  31.829  9.718   1.00 6.31  ? 114  PHE B CD2 1 
ATOM   3555  C  CE1 . PHE B  1 114 ? 89.326  33.038  8.824   1.00 8.74  ? 114  PHE B CE1 1 
ATOM   3556  C  CE2 . PHE B  1 114 ? 90.525  31.756  10.504  1.00 6.20  ? 114  PHE B CE2 1 
ATOM   3557  C  CZ  . PHE B  1 114 ? 89.342  32.369  10.079  1.00 5.21  ? 114  PHE B CZ  1 
ATOM   3558  N  N   . GLN B  1 115 ? 92.807  35.509  6.540   1.00 8.19  ? 115  GLN B N   1 
ATOM   3559  C  CA  . GLN B  1 115 ? 91.975  36.652  6.140   1.00 7.03  ? 115  GLN B CA  1 
ATOM   3560  C  C   . GLN B  1 115 ? 91.186  36.309  4.881   1.00 9.48  ? 115  GLN B C   1 
ATOM   3561  O  O   . GLN B  1 115 ? 91.763  35.834  3.874   1.00 8.61  ? 115  GLN B O   1 
ATOM   3562  C  CB  . GLN B  1 115 ? 92.834  37.941  5.942   1.00 8.34  ? 115  GLN B CB  1 
ATOM   3563  C  CG  . GLN B  1 115 ? 91.995  39.214  5.611   1.00 6.48  ? 115  GLN B CG  1 
ATOM   3564  C  CD  . GLN B  1 115 ? 92.755  40.526  5.703   1.00 14.14 ? 115  GLN B CD  1 
ATOM   3565  O  OE1 . GLN B  1 115 ? 93.648  40.686  6.559   1.00 20.35 ? 115  GLN B OE1 1 
ATOM   3566  N  NE2 . GLN B  1 115 ? 92.357  41.511  4.881   1.00 13.46 ? 115  GLN B NE2 1 
ATOM   3567  N  N   . ILE B  1 116 ? 89.883  36.636  4.895   1.00 8.98  ? 116  ILE B N   1 
ATOM   3568  C  CA  . ILE B  1 116 ? 88.994  36.262  3.799   1.00 8.61  ? 116  ILE B CA  1 
ATOM   3569  C  C   . ILE B  1 116 ? 89.099  37.289  2.690   1.00 9.16  ? 116  ILE B C   1 
ATOM   3570  O  O   . ILE B  1 116 ? 88.923  38.501  2.965   1.00 10.58 ? 116  ILE B O   1 
ATOM   3571  C  CB  . ILE B  1 116 ? 87.527  36.220  4.258   1.00 9.06  ? 116  ILE B CB  1 
ATOM   3572  C  CG1 . ILE B  1 116 ? 87.337  35.250  5.459   1.00 8.58  ? 116  ILE B CG1 1 
ATOM   3573  C  CG2 . ILE B  1 116 ? 86.667  35.865  3.068   1.00 9.05  ? 116  ILE B CG2 1 
ATOM   3574  C  CD1 . ILE B  1 116 ? 87.591  33.654  5.156   1.00 11.08 ? 116  ILE B CD1 1 
ATOM   3575  N  N   . GLN B  1 117 ? 89.382  36.835  1.470   1.00 8.34  ? 117  GLN B N   1 
ATOM   3576  C  CA  . GLN B  1 117 ? 89.618  37.751  0.343   1.00 10.18 ? 117  GLN B CA  1 
ATOM   3577  C  C   . GLN B  1 117 ? 88.385  37.924  -0.557  1.00 9.45  ? 117  GLN B C   1 
ATOM   3578  O  O   . GLN B  1 117 ? 87.953  39.007  -0.723  1.00 8.97  ? 117  GLN B O   1 
ATOM   3579  C  CB  . GLN B  1 117 ? 90.828  37.315  -0.522  1.00 11.21 ? 117  GLN B CB  1 
ATOM   3580  C  CG  . GLN B  1 117 ? 91.039  38.204  -1.771  1.00 17.79 ? 117  GLN B CG  1 
ATOM   3581  C  CD  . GLN B  1 117 ? 92.307  37.906  -2.634  1.00 27.46 ? 117  GLN B CD  1 
ATOM   3582  O  OE1 . GLN B  1 117 ? 93.375  38.551  -2.452  1.00 30.13 ? 117  GLN B OE1 1 
ATOM   3583  N  NE2 . GLN B  1 117 ? 92.162  36.997  -3.626  1.00 27.35 ? 117  GLN B NE2 1 
ATOM   3584  N  N   . ASP B  1 118 ? 87.831  36.856  -1.116  1.00 8.26  ? 118  ASP B N   1 
ATOM   3585  C  CA  . ASP B  1 118 ? 86.814  37.036  -2.137  1.00 8.08  ? 118  ASP B CA  1 
ATOM   3586  C  C   . ASP B  1 118 ? 85.402  36.908  -1.534  1.00 7.22  ? 118  ASP B C   1 
ATOM   3587  O  O   . ASP B  1 118 ? 85.247  36.281  -0.488  1.00 7.62  ? 118  ASP B O   1 
ATOM   3588  C  CB  . ASP B  1 118 ? 86.988  35.959  -3.202  1.00 8.67  ? 118  ASP B CB  1 
ATOM   3589  C  CG  . ASP B  1 118 ? 88.030  36.302  -4.220  1.00 10.36 ? 118  ASP B CG  1 
ATOM   3590  O  OD1 . ASP B  1 118 ? 88.164  37.476  -4.601  1.00 10.45 ? 118  ASP B OD1 1 
ATOM   3591  O  OD2 . ASP B  1 118 ? 88.755  35.425  -4.709  1.00 12.03 ? 118  ASP B OD2 1 
ATOM   3592  N  N   . PRO B  1 119 ? 84.401  37.487  -2.189  1.00 8.53  ? 119  PRO B N   1 
ATOM   3593  C  CA  . PRO B  1 119 ? 83.016  37.501  -1.691  1.00 9.58  ? 119  PRO B CA  1 
ATOM   3594  C  C   . PRO B  1 119 ? 82.419  36.155  -1.436  1.00 10.10 ? 119  PRO B C   1 
ATOM   3595  O  O   . PRO B  1 119 ? 81.688  36.021  -0.456  1.00 10.36 ? 119  PRO B O   1 
ATOM   3596  C  CB  . PRO B  1 119 ? 82.266  38.177  -2.829  1.00 10.08 ? 119  PRO B CB  1 
ATOM   3597  C  CG  . PRO B  1 119 ? 83.346  39.186  -3.305  1.00 10.96 ? 119  PRO B CG  1 
ATOM   3598  C  CD  . PRO B  1 119 ? 84.513  38.275  -3.440  1.00 8.15  ? 119  PRO B CD  1 
ATOM   3599  N  N   . ASP B  1 120 ? 82.759  35.160  -2.261  1.00 8.80  ? 120  ASP B N   1 
ATOM   3600  C  CA  . ASP B  1 120 ? 82.121  33.864  -2.110  1.00 9.07  ? 120  ASP B CA  1 
ATOM   3601  C  C   . ASP B  1 120 ? 83.180  32.842  -1.640  1.00 8.90  ? 120  ASP B C   1 
ATOM   3602  O  O   . ASP B  1 120 ? 83.473  31.881  -2.327  1.00 11.00 ? 120  ASP B O   1 
ATOM   3603  C  CB  . ASP B  1 120 ? 81.454  33.427  -3.433  1.00 8.94  ? 120  ASP B CB  1 
ATOM   3604  C  CG  . ASP B  1 120 ? 80.457  32.242  -3.237  1.00 10.36 ? 120  ASP B CG  1 
ATOM   3605  O  OD1 . ASP B  1 120 ? 80.104  31.951  -2.083  1.00 11.11 ? 120  ASP B OD1 1 
ATOM   3606  O  OD2 . ASP B  1 120 ? 79.989  31.524  -4.152  1.00 13.45 ? 120  ASP B OD2 1 
ATOM   3607  N  N   . THR B  1 121 ? 83.743  33.063  -0.462  1.00 7.97  ? 121  THR B N   1 
ATOM   3608  C  CA  . THR B  1 121 ? 84.834  32.220  0.021   1.00 6.40  ? 121  THR B CA  1 
ATOM   3609  C  C   . THR B  1 121 ? 84.304  31.131  0.878   1.00 7.97  ? 121  THR B C   1 
ATOM   3610  O  O   . THR B  1 121 ? 83.391  31.353  1.678   1.00 7.03  ? 121  THR B O   1 
ATOM   3611  C  CB  . THR B  1 121 ? 85.847  33.077  0.742   1.00 7.59  ? 121  THR B CB  1 
ATOM   3612  O  OG1 . THR B  1 121 ? 86.424  33.991  -0.220  1.00 8.20  ? 121  THR B OG1 1 
ATOM   3613  C  CG2 . THR B  1 121 ? 87.028  32.213  1.256   1.00 4.17  ? 121  THR B CG2 1 
ATOM   3614  N  N   . GLU B  1 122 ? 84.829  29.915  0.704   1.00 7.44  ? 122  GLU B N   1 
ATOM   3615  C  CA  . GLU B  1 122 ? 84.462  28.830  1.601   1.00 8.29  ? 122  GLU B CA  1 
ATOM   3616  C  C   . GLU B  1 122 ? 85.722  28.058  1.965   1.00 9.05  ? 122  GLU B C   1 
ATOM   3617  O  O   . GLU B  1 122 ? 86.516  27.670  1.071   1.00 10.13 ? 122  GLU B O   1 
ATOM   3618  C  CB  . GLU B  1 122 ? 83.437  27.883  0.940   1.00 8.04  ? 122  GLU B CB  1 
ATOM   3619  C  CG  . GLU B  1 122 ? 83.043  26.742  1.865   1.00 7.88  ? 122  GLU B CG  1 
ATOM   3620  C  CD  . GLU B  1 122 ? 81.883  25.936  1.279   1.00 12.98 ? 122  GLU B CD  1 
ATOM   3621  O  OE1 . GLU B  1 122 ? 81.190  26.433  0.342   1.00 14.72 ? 122  GLU B OE1 1 
ATOM   3622  O  OE2 . GLU B  1 122 ? 81.615  24.835  1.777   1.00 15.76 ? 122  GLU B OE2 1 
ATOM   3623  N  N   . MET B  1 123 ? 85.950  27.949  3.274   1.00 9.37  ? 123  MET B N   1 
ATOM   3624  C  CA  . MET B  1 123 ? 87.063  27.210  3.850   1.00 12.03 ? 123  MET B CA  1 
ATOM   3625  C  C   . MET B  1 123 ? 86.497  25.887  4.384   1.00 11.95 ? 123  MET B C   1 
ATOM   3626  O  O   . MET B  1 123 ? 85.492  25.877  5.084   1.00 13.59 ? 123  MET B O   1 
ATOM   3627  C  CB  . MET B  1 123 ? 87.664  28.017  5.017   1.00 11.54 ? 123  MET B CB  1 
ATOM   3628  C  CG  . MET B  1 123 ? 87.714  29.548  4.837   1.00 14.58 ? 123  MET B CG  1 
ATOM   3629  S  SD  . MET B  1 123 ? 88.144  30.317  6.504   1.00 23.09 ? 123  MET B SD  1 
ATOM   3630  C  CE  . MET B  1 123 ? 89.527  29.383  6.946   1.00 14.57 ? 123  MET B CE  1 
ATOM   3631  N  N   . THR B  1 124 ? 87.160  24.783  4.103   1.00 13.01 ? 124  THR B N   1 
ATOM   3632  C  CA  . THR B  1 124 ? 86.864  23.549  4.778   1.00 12.38 ? 124  THR B CA  1 
ATOM   3633  C  C   . THR B  1 124 ? 88.025  23.341  5.733   1.00 11.94 ? 124  THR B C   1 
ATOM   3634  O  O   . THR B  1 124 ? 89.199  23.295  5.311   1.00 11.63 ? 124  THR B O   1 
ATOM   3635  C  CB  . THR B  1 124 ? 86.724  22.399  3.773   1.00 13.29 ? 124  THR B CB  1 
ATOM   3636  O  OG1 . THR B  1 124 ? 85.551  22.607  2.979   1.00 12.85 ? 124  THR B OG1 1 
ATOM   3637  C  CG2 . THR B  1 124 ? 86.424  21.095  4.504   1.00 13.48 ? 124  THR B CG2 1 
ATOM   3638  N  N   . GLY B  1 125 ? 87.704  23.240  7.031   1.00 11.14 ? 125  GLY B N   1 
ATOM   3639  C  CA  . GLY B  1 125 ? 88.727  23.009  8.048   1.00 9.69  ? 125  GLY B CA  1 
ATOM   3640  C  C   . GLY B  1 125 ? 88.661  21.553  8.505   1.00 10.45 ? 125  GLY B C   1 
ATOM   3641  O  O   . GLY B  1 125 ? 87.565  21.016  8.762   1.00 8.33  ? 125  GLY B O   1 
ATOM   3642  N  N   . VAL B  1 126 ? 89.808  20.895  8.562   1.00 8.83  ? 126  VAL B N   1 
ATOM   3643  C  CA  . VAL B  1 126 ? 89.813  19.517  9.044   1.00 8.64  ? 126  VAL B CA  1 
ATOM   3644  C  C   . VAL B  1 126 ? 90.722  19.539  10.244  1.00 9.36  ? 126  VAL B C   1 
ATOM   3645  O  O   . VAL B  1 126 ? 91.884  19.953  10.121  1.00 8.84  ? 126  VAL B O   1 
ATOM   3646  C  CB  . VAL B  1 126 ? 90.335  18.554  7.992   1.00 8.22  ? 126  VAL B CB  1 
ATOM   3647  C  CG1 . VAL B  1 126 ? 90.505  17.192  8.616   1.00 7.21  ? 126  VAL B CG1 1 
ATOM   3648  C  CG2 . VAL B  1 126 ? 89.360  18.476  6.780   1.00 8.15  ? 126  VAL B CG2 1 
ATOM   3649  N  N   . ILE B  1 127 ? 90.178  19.214  11.424  1.00 7.68  ? 127  ILE B N   1 
ATOM   3650  C  CA  . ILE B  1 127 ? 90.937  19.382  12.670  1.00 8.88  ? 127  ILE B CA  1 
ATOM   3651  C  C   . ILE B  1 127 ? 91.005  18.027  13.375  1.00 8.36  ? 127  ILE B C   1 
ATOM   3652  O  O   . ILE B  1 127 ? 90.004  17.299  13.489  1.00 8.39  ? 127  ILE B O   1 
ATOM   3653  C  CB  . ILE B  1 127 ? 90.285  20.482  13.588  1.00 8.58  ? 127  ILE B CB  1 
ATOM   3654  C  CG1 . ILE B  1 127 ? 90.161  21.794  12.789  1.00 12.94 ? 127  ILE B CG1 1 
ATOM   3655  C  CG2 . ILE B  1 127 ? 91.121  20.793  14.880  1.00 6.85  ? 127  ILE B CG2 1 
ATOM   3656  C  CD1 . ILE B  1 127 ? 88.741  22.278  12.738  1.00 19.21 ? 127  ILE B CD1 1 
ATOM   3657  N  N   . VAL B  1 128 ? 92.208  17.673  13.798  1.00 8.31  ? 128  VAL B N   1 
ATOM   3658  C  CA  . VAL B  1 128 ? 92.451  16.395  14.420  1.00 8.44  ? 128  VAL B CA  1 
ATOM   3659  C  C   . VAL B  1 128 ? 93.149  16.622  15.766  1.00 7.82  ? 128  VAL B C   1 
ATOM   3660  O  O   . VAL B  1 128 ? 94.127  17.397  15.811  1.00 8.89  ? 128  VAL B O   1 
ATOM   3661  C  CB  . VAL B  1 128 ? 93.355  15.516  13.535  1.00 8.75  ? 128  VAL B CB  1 
ATOM   3662  C  CG1 . VAL B  1 128 ? 93.405  14.085  14.145  1.00 8.74  ? 128  VAL B CG1 1 
ATOM   3663  C  CG2 . VAL B  1 128 ? 92.829  15.459  12.147  1.00 7.76  ? 128  VAL B CG2 1 
ATOM   3664  N  N   . PRO B  1 129 ? 92.678  16.007  16.856  1.00 7.74  ? 129  PRO B N   1 
ATOM   3665  C  CA  . PRO B  1 129 ? 91.484  15.158  16.907  1.00 7.23  ? 129  PRO B CA  1 
ATOM   3666  C  C   . PRO B  1 129 ? 90.194  15.958  16.878  1.00 8.42  ? 129  PRO B C   1 
ATOM   3667  O  O   . PRO B  1 129 ? 90.235  17.186  16.834  1.00 7.87  ? 129  PRO B O   1 
ATOM   3668  C  CB  . PRO B  1 129 ? 91.629  14.423  18.269  1.00 6.94  ? 129  PRO B CB  1 
ATOM   3669  C  CG  . PRO B  1 129 ? 92.355  15.396  19.104  1.00 9.41  ? 129  PRO B CG  1 
ATOM   3670  C  CD  . PRO B  1 129 ? 93.346  16.085  18.165  1.00 7.83  ? 129  PRO B CD  1 
ATOM   3671  N  N   . GLY B  1 130 ? 89.054  15.249  16.927  1.00 8.36  ? 130  GLY B N   1 
ATOM   3672  C  CA  . GLY B  1 130 ? 87.753  15.863  16.799  1.00 7.42  ? 130  GLY B CA  1 
ATOM   3673  C  C   . GLY B  1 130 ? 87.273  16.462  18.119  1.00 8.41  ? 130  GLY B C   1 
ATOM   3674  O  O   . GLY B  1 130 ? 87.904  16.245  19.184  1.00 6.39  ? 130  GLY B O   1 
ATOM   3675  N  N   . GLY B  1 131 ? 86.192  17.243  18.048  1.00 6.18  ? 131  GLY B N   1 
ATOM   3676  C  CA  . GLY B  1 131 ? 85.647  17.884  19.233  1.00 8.71  ? 131  GLY B CA  1 
ATOM   3677  C  C   . GLY B  1 131 ? 86.122  19.342  19.386  1.00 10.28 ? 131  GLY B C   1 
ATOM   3678  O  O   . GLY B  1 131 ? 85.605  20.061  20.239  1.00 9.85  ? 131  GLY B O   1 
ATOM   3679  N  N   . PHE B  1 132 ? 87.056  19.785  18.524  1.00 10.30 ? 132  PHE B N   1 
ATOM   3680  C  CA  . PHE B  1 132 ? 87.567  21.159  18.541  1.00 10.45 ? 132  PHE B CA  1 
ATOM   3681  C  C   . PHE B  1 132 ? 86.419  22.181  18.402  1.00 9.39  ? 132  PHE B C   1 
ATOM   3682  O  O   . PHE B  1 132 ? 86.500  23.269  18.939  1.00 9.30  ? 132  PHE B O   1 
ATOM   3683  C  CB  . PHE B  1 132 ? 88.619  21.392  17.433  1.00 11.35 ? 132  PHE B CB  1 
ATOM   3684  C  CG  . PHE B  1 132 ? 89.276  22.722  17.515  1.00 13.63 ? 132  PHE B CG  1 
ATOM   3685  C  CD1 . PHE B  1 132 ? 90.235  22.983  18.484  1.00 12.74 ? 132  PHE B CD1 1 
ATOM   3686  C  CD2 . PHE B  1 132 ? 88.840  23.772  16.690  1.00 17.97 ? 132  PHE B CD2 1 
ATOM   3687  C  CE1 . PHE B  1 132 ? 90.799  24.256  18.602  1.00 14.48 ? 132  PHE B CE1 1 
ATOM   3688  C  CE2 . PHE B  1 132 ? 89.412  25.058  16.800  1.00 16.40 ? 132  PHE B CE2 1 
ATOM   3689  C  CZ  . PHE B  1 132 ? 90.361  25.306  17.773  1.00 16.36 ? 132  PHE B CZ  1 
ATOM   3690  N  N   . GLU B  1 133 ? 85.336  21.789  17.736  1.00 8.86  ? 133  GLU B N   1 
ATOM   3691  C  CA  . GLU B  1 133 ? 84.206  22.699  17.495  1.00 9.10  ? 133  GLU B CA  1 
ATOM   3692  C  C   . GLU B  1 133 ? 83.533  23.307  18.755  1.00 9.14  ? 133  GLU B C   1 
ATOM   3693  O  O   . GLU B  1 133 ? 82.782  24.314  18.666  1.00 8.74  ? 133  GLU B O   1 
ATOM   3694  C  CB  . GLU B  1 133 ? 83.162  22.018  16.623  1.00 9.24  ? 133  GLU B CB  1 
ATOM   3695  C  CG  . GLU B  1 133 ? 82.384  20.900  17.296  1.00 11.50 ? 133  GLU B CG  1 
ATOM   3696  C  CD  . GLU B  1 133 ? 83.153  19.579  17.282  1.00 11.48 ? 133  GLU B CD  1 
ATOM   3697  O  OE1 . GLU B  1 133 ? 84.261  19.506  16.666  1.00 13.71 ? 133  GLU B OE1 1 
ATOM   3698  O  OE2 . GLU B  1 133 ? 82.668  18.613  17.894  1.00 10.42 ? 133  GLU B OE2 1 
ATOM   3699  N  N   . ASP B  1 134 ? 83.796  22.732  19.927  1.00 6.02  ? 134  ASP B N   1 
ATOM   3700  C  CA  . ASP B  1 134 ? 83.252  23.330  21.144  1.00 6.70  ? 134  ASP B CA  1 
ATOM   3701  C  C   . ASP B  1 134 ? 83.648  24.816  21.238  1.00 6.72  ? 134  ASP B C   1 
ATOM   3702  O  O   . ASP B  1 134 ? 82.906  25.585  21.816  1.00 5.49  ? 134  ASP B O   1 
ATOM   3703  C  CB  . ASP B  1 134 ? 83.822  22.676  22.389  1.00 6.81  ? 134  ASP B CB  1 
ATOM   3704  C  CG  . ASP B  1 134 ? 83.220  21.318  22.678  1.00 7.71  ? 134  ASP B CG  1 
ATOM   3705  O  OD1 . ASP B  1 134 ? 82.194  20.992  22.057  1.00 11.25 ? 134  ASP B OD1 1 
ATOM   3706  O  OD2 . ASP B  1 134 ? 83.687  20.567  23.581  1.00 8.81  ? 134  ASP B OD2 1 
ATOM   3707  N  N   . LEU B  1 135 ? 84.826  25.159  20.722  1.00 5.62  ? 135  LEU B N   1 
ATOM   3708  C  CA  . LEU B  1 135 ? 85.344  26.531  20.695  1.00 7.91  ? 135  LEU B CA  1 
ATOM   3709  C  C   . LEU B  1 135 ? 84.305  27.466  20.024  1.00 6.86  ? 135  LEU B C   1 
ATOM   3710  O  O   . LEU B  1 135 ? 83.955  28.531  20.563  1.00 6.09  ? 135  LEU B O   1 
ATOM   3711  C  CB  . LEU B  1 135 ? 86.678  26.608  19.932  1.00 8.33  ? 135  LEU B CB  1 
ATOM   3712  C  CG  . LEU B  1 135 ? 87.133  28.096  19.717  1.00 7.24  ? 135  LEU B CG  1 
ATOM   3713  C  CD1 . LEU B  1 135 ? 87.557  28.758  20.976  1.00 7.75  ? 135  LEU B CD1 1 
ATOM   3714  C  CD2 . LEU B  1 135 ? 88.262  28.168  18.677  1.00 10.10 ? 135  LEU B CD2 1 
ATOM   3715  N  N   . PHE B  1 136 ? 83.782  27.031  18.892  1.00 7.73  ? 136  PHE B N   1 
ATOM   3716  C  CA  . PHE B  1 136 ? 82.858  27.863  18.093  1.00 7.66  ? 136  PHE B CA  1 
ATOM   3717  C  C   . PHE B  1 136 ? 81.449  27.911  18.676  1.00 8.24  ? 136  PHE B C   1 
ATOM   3718  O  O   . PHE B  1 136 ? 80.739  28.892  18.481  1.00 9.21  ? 136  PHE B O   1 
ATOM   3719  C  CB  . PHE B  1 136 ? 82.843  27.406  16.630  1.00 8.02  ? 136  PHE B CB  1 
ATOM   3720  C  CG  . PHE B  1 136 ? 84.211  27.444  15.986  1.00 9.67  ? 136  PHE B CG  1 
ATOM   3721  C  CD1 . PHE B  1 136 ? 84.762  28.662  15.565  1.00 9.67  ? 136  PHE B CD1 1 
ATOM   3722  C  CD2 . PHE B  1 136 ? 84.958  26.291  15.829  1.00 9.81  ? 136  PHE B CD2 1 
ATOM   3723  C  CE1 . PHE B  1 136 ? 86.060  28.746  14.991  1.00 9.78  ? 136  PHE B CE1 1 
ATOM   3724  C  CE2 . PHE B  1 136 ? 86.261  26.363  15.237  1.00 10.59 ? 136  PHE B CE2 1 
ATOM   3725  C  CZ  . PHE B  1 136 ? 86.815  27.625  14.850  1.00 9.69  ? 136  PHE B CZ  1 
ATOM   3726  N  N   . TYR B  1 137 ? 81.036  26.862  19.398  1.00 8.79  ? 137  TYR B N   1 
ATOM   3727  C  CA  . TYR B  1 137 ? 79.753  26.897  20.085  1.00 9.23  ? 137  TYR B CA  1 
ATOM   3728  C  C   . TYR B  1 137 ? 79.804  28.040  21.087  1.00 9.37  ? 137  TYR B C   1 
ATOM   3729  O  O   . TYR B  1 137 ? 78.828  28.780  21.256  1.00 9.99  ? 137  TYR B O   1 
ATOM   3730  C  CB  . TYR B  1 137 ? 79.475  25.580  20.807  1.00 8.01  ? 137  TYR B CB  1 
ATOM   3731  C  CG  . TYR B  1 137 ? 79.402  24.386  19.890  1.00 10.76 ? 137  TYR B CG  1 
ATOM   3732  C  CD1 . TYR B  1 137 ? 79.196  24.540  18.530  1.00 9.77  ? 137  TYR B CD1 1 
ATOM   3733  C  CD2 . TYR B  1 137 ? 79.538  23.090  20.409  1.00 9.43  ? 137  TYR B CD2 1 
ATOM   3734  C  CE1 . TYR B  1 137 ? 79.141  23.440  17.695  1.00 14.33 ? 137  TYR B CE1 1 
ATOM   3735  C  CE2 . TYR B  1 137 ? 79.468  21.983  19.595  1.00 11.34 ? 137  TYR B CE2 1 
ATOM   3736  C  CZ  . TYR B  1 137 ? 79.246  22.159  18.243  1.00 12.36 ? 137  TYR B CZ  1 
ATOM   3737  O  OH  . TYR B  1 137 ? 79.163  21.072  17.434  1.00 9.55  ? 137  TYR B OH  1 
ATOM   3738  N  N   . TYR B  1 138 ? 80.986  28.202  21.703  1.00 8.92  ? 138  TYR B N   1 
ATOM   3739  C  CA  . TYR B  1 138 ? 81.241  29.314  22.609  1.00 9.63  ? 138  TYR B CA  1 
ATOM   3740  C  C   . TYR B  1 138 ? 81.336  30.695  21.892  1.00 8.05  ? 138  TYR B C   1 
ATOM   3741  O  O   . TYR B  1 138 ? 80.584  31.597  22.223  1.00 8.62  ? 138  TYR B O   1 
ATOM   3742  C  CB  . TYR B  1 138 ? 82.498  29.061  23.453  1.00 8.71  ? 138  TYR B CB  1 
ATOM   3743  C  CG  . TYR B  1 138 ? 82.926  30.284  24.265  1.00 9.33  ? 138  TYR B CG  1 
ATOM   3744  C  CD1 . TYR B  1 138 ? 81.991  30.991  25.025  1.00 12.55 ? 138  TYR B CD1 1 
ATOM   3745  C  CD2 . TYR B  1 138 ? 84.229  30.758  24.239  1.00 13.60 ? 138  TYR B CD2 1 
ATOM   3746  C  CE1 . TYR B  1 138 ? 82.335  32.090  25.780  1.00 11.23 ? 138  TYR B CE1 1 
ATOM   3747  C  CE2 . TYR B  1 138 ? 84.611  31.913  25.025  1.00 8.37  ? 138  TYR B CE2 1 
ATOM   3748  C  CZ  . TYR B  1 138 ? 83.655  32.552  25.760  1.00 12.34 ? 138  TYR B CZ  1 
ATOM   3749  O  OH  . TYR B  1 138 ? 83.965  33.669  26.537  1.00 16.11 ? 138  TYR B OH  1 
ATOM   3750  N  N   . LEU B  1 139 ? 82.257  30.831  20.940  1.00 8.25  ? 139  LEU B N   1 
ATOM   3751  C  CA  . LEU B  1 139 ? 82.476  32.111  20.229  1.00 8.58  ? 139  LEU B CA  1 
ATOM   3752  C  C   . LEU B  1 139 ? 81.308  32.536  19.370  1.00 8.75  ? 139  LEU B C   1 
ATOM   3753  O  O   . LEU B  1 139 ? 81.079  33.735  19.218  1.00 8.71  ? 139  LEU B O   1 
ATOM   3754  C  CB  . LEU B  1 139 ? 83.703  32.054  19.309  1.00 7.32  ? 139  LEU B CB  1 
ATOM   3755  C  CG  . LEU B  1 139 ? 85.027  31.844  20.045  1.00 9.04  ? 139  LEU B CG  1 
ATOM   3756  C  CD1 . LEU B  1 139 ? 86.143  31.604  19.023  1.00 12.02 ? 139  LEU B CD1 1 
ATOM   3757  C  CD2 . LEU B  1 139 ? 85.370  32.983  21.003  1.00 12.00 ? 139  LEU B CD2 1 
ATOM   3758  N  N   . GLY B  1 140 ? 80.598  31.560  18.811  1.00 7.89  ? 140  GLY B N   1 
ATOM   3759  C  CA  . GLY B  1 140 ? 79.580  31.845  17.812  1.00 8.33  ? 140  GLY B CA  1 
ATOM   3760  C  C   . GLY B  1 140 ? 78.176  32.017  18.348  1.00 9.20  ? 140  GLY B C   1 
ATOM   3761  O  O   . GLY B  1 140 ? 77.903  31.655  19.489  1.00 8.33  ? 140  GLY B O   1 
ATOM   3762  N  N   . THR B  1 141 ? 77.301  32.593  17.525  1.00 7.81  ? 141  THR B N   1 
ATOM   3763  C  CA  . THR B  1 141 ? 75.902  32.731  17.852  1.00 8.40  ? 141  THR B CA  1 
ATOM   3764  C  C   . THR B  1 141 ? 75.093  31.789  16.982  1.00 8.61  ? 141  THR B C   1 
ATOM   3765  O  O   . THR B  1 141 ? 75.235  31.811  15.755  1.00 7.19  ? 141  THR B O   1 
ATOM   3766  C  CB  . THR B  1 141 ? 75.511  34.182  17.589  1.00 8.52  ? 141  THR B CB  1 
ATOM   3767  O  OG1 . THR B  1 141 ? 76.320  34.998  18.441  1.00 6.56  ? 141  THR B OG1 1 
ATOM   3768  C  CG2 . THR B  1 141 ? 74.078  34.446  18.026  1.00 11.48 ? 141  THR B CG2 1 
ATOM   3769  N  N   . ASN B  1 142 ? 74.264  30.946  17.601  1.00 7.96  ? 142  ASN B N   1 
ATOM   3770  C  CA  . ASN B  1 142 ? 73.511  30.010  16.798  1.00 8.10  ? 142  ASN B CA  1 
ATOM   3771  C  C   . ASN B  1 142 ? 72.785  30.771  15.689  1.00 8.95  ? 142  ASN B C   1 
ATOM   3772  O  O   . ASN B  1 142 ? 72.245  31.893  15.911  1.00 8.97  ? 142  ASN B O   1 
ATOM   3773  C  CB  . ASN B  1 142 ? 72.475  29.265  17.633  1.00 8.44  ? 142  ASN B CB  1 
ATOM   3774  C  CG  . ASN B  1 142 ? 73.073  28.323  18.669  1.00 10.64 ? 142  ASN B CG  1 
ATOM   3775  O  OD1 . ASN B  1 142 ? 74.266  28.046  18.685  1.00 9.74  ? 142  ASN B OD1 1 
ATOM   3776  N  ND2 . ASN B  1 142 ? 72.202  27.860  19.575  1.00 15.64 ? 142  ASN B ND2 1 
ATOM   3777  N  N   . ALA B  1 143 ? 72.731  30.157  14.510  1.00 8.32  ? 143  ALA B N   1 
ATOM   3778  C  CA  . ALA B  1 143 ? 72.070  30.744  13.348  1.00 9.00  ? 143  ALA B CA  1 
ATOM   3779  C  C   . ALA B  1 143 ? 70.990  29.771  12.893  1.00 8.35  ? 143  ALA B C   1 
ATOM   3780  O  O   . ALA B  1 143 ? 71.297  28.630  12.581  1.00 8.42  ? 143  ALA B O   1 
ATOM   3781  C  CB  . ALA B  1 143 ? 73.100  30.914  12.219  1.00 9.27  ? 143  ALA B CB  1 
ATOM   3782  N  N   . THR B  1 144 ? 69.749  30.218  12.805  1.00 8.35  ? 144  THR B N   1 
ATOM   3783  C  CA  . THR B  1 144 ? 68.678  29.355  12.243  1.00 8.58  ? 144  THR B CA  1 
ATOM   3784  C  C   . THR B  1 144 ? 68.916  29.167  10.717  1.00 8.25  ? 144  THR B C   1 
ATOM   3785  O  O   . THR B  1 144 ? 68.740  28.077  10.160  1.00 7.97  ? 144  THR B O   1 
ATOM   3786  C  CB  . THR B  1 144 ? 67.388  30.065  12.497  1.00 8.97  ? 144  THR B CB  1 
ATOM   3787  O  OG1 . THR B  1 144 ? 67.202  30.078  13.927  1.00 12.56 ? 144  THR B OG1 1 
ATOM   3788  C  CG2 . THR B  1 144 ? 66.178  29.286  11.961  1.00 10.05 ? 144  THR B CG2 1 
ATOM   3789  N  N   . ASP B  1 145 ? 69.282  30.259  10.062  1.00 7.12  ? 145  ASP B N   1 
ATOM   3790  C  CA  . ASP B  1 145 ? 69.451  30.299  8.593   1.00 6.89  ? 145  ASP B CA  1 
ATOM   3791  C  C   . ASP B  1 145 ? 68.429  29.393  7.881   1.00 7.33  ? 145  ASP B C   1 
ATOM   3792  O  O   . ASP B  1 145 ? 68.793  28.328  7.327   1.00 7.96  ? 145  ASP B O   1 
ATOM   3793  C  CB  . ASP B  1 145 ? 70.871  29.839  8.250   1.00 7.08  ? 145  ASP B CB  1 
ATOM   3794  C  CG  . ASP B  1 145 ? 71.185  30.040  6.788   1.00 6.01  ? 145  ASP B CG  1 
ATOM   3795  O  OD1 . ASP B  1 145 ? 70.340  30.587  6.024   1.00 6.17  ? 145  ASP B OD1 1 
ATOM   3796  O  OD2 . ASP B  1 145 ? 72.251  29.708  6.334   1.00 7.04  ? 145  ASP B OD2 1 
ATOM   3797  N  N   . THR B  1 146 ? 67.156  29.809  7.923   1.00 6.66  ? 146  THR B N   1 
ATOM   3798  C  CA  . THR B  1 146 ? 66.029  29.072  7.331   1.00 8.24  ? 146  THR B CA  1 
ATOM   3799  C  C   . THR B  1 146 ? 66.244  28.706  5.876   1.00 8.40  ? 146  THR B C   1 
ATOM   3800  O  O   . THR B  1 146 ? 65.925  27.583  5.441   1.00 8.22  ? 146  THR B O   1 
ATOM   3801  C  CB  . THR B  1 146 ? 64.759  29.955  7.425   1.00 8.33  ? 146  THR B CB  1 
ATOM   3802  O  OG1 . THR B  1 146 ? 64.475  30.179  8.814   1.00 7.97  ? 146  THR B OG1 1 
ATOM   3803  C  CG2 . THR B  1 146 ? 63.515  29.225  6.872   1.00 10.11 ? 146  THR B CG2 1 
ATOM   3804  N  N   . THR B  1 147 ? 66.818  29.633  5.129   1.00 8.61  ? 147  THR B N   1 
ATOM   3805  C  CA  . THR B  1 147 ? 66.960  29.409  3.690   1.00 8.32  ? 147  THR B CA  1 
ATOM   3806  C  C   . THR B  1 147 ? 68.209  28.650  3.323   1.00 7.45  ? 147  THR B C   1 
ATOM   3807  O  O   . THR B  1 147 ? 68.420  28.347  2.132   1.00 7.73  ? 147  THR B O   1 
ATOM   3808  C  CB  . THR B  1 147 ? 66.948  30.704  2.941   1.00 6.56  ? 147  THR B CB  1 
ATOM   3809  O  OG1 . THR B  1 147 ? 68.143  31.466  3.269   1.00 8.09  ? 147  THR B OG1 1 
ATOM   3810  C  CG2 . THR B  1 147 ? 65.699  31.546  3.347   1.00 5.51  ? 147  THR B CG2 1 
ATOM   3811  N  N   . HIS B  1 148 ? 69.077  28.424  4.298   1.00 7.59  ? 148  HIS B N   1 
ATOM   3812  C  CA  . HIS B  1 148 ? 70.364  27.735  4.045   1.00 8.41  ? 148  HIS B CA  1 
ATOM   3813  C  C   . HIS B  1 148 ? 71.295  28.594  3.154   1.00 8.46  ? 148  HIS B C   1 
ATOM   3814  O  O   . HIS B  1 148 ? 72.146  28.075  2.449   1.00 10.27 ? 148  HIS B O   1 
ATOM   3815  C  CB  . HIS B  1 148 ? 70.187  26.343  3.408   1.00 8.05  ? 148  HIS B CB  1 
ATOM   3816  C  CG  . HIS B  1 148 ? 69.308  25.411  4.188   1.00 9.10  ? 148  HIS B CG  1 
ATOM   3817  N  ND1 . HIS B  1 148 ? 69.807  24.306  4.858   1.00 10.07 ? 148  HIS B ND1 1 
ATOM   3818  C  CD2 . HIS B  1 148 ? 67.960  25.388  4.366   1.00 6.61  ? 148  HIS B CD2 1 
ATOM   3819  C  CE1 . HIS B  1 148 ? 68.805  23.675  5.455   1.00 6.62  ? 148  HIS B CE1 1 
ATOM   3820  N  NE2 . HIS B  1 148 ? 67.672  24.290  5.140   1.00 12.17 ? 148  HIS B NE2 1 
ATOM   3821  N  N   . THR B  1 149 ? 71.151  29.909  3.189   1.00 8.18  ? 149  THR B N   1 
ATOM   3822  C  CA  . THR B  1 149 ? 72.051  30.727  2.435   1.00 8.13  ? 149  THR B CA  1 
ATOM   3823  C  C   . THR B  1 149 ? 73.477  30.438  2.929   1.00 7.97  ? 149  THR B C   1 
ATOM   3824  O  O   . THR B  1 149 ? 73.657  30.128  4.124   1.00 6.48  ? 149  THR B O   1 
ATOM   3825  C  CB  . THR B  1 149 ? 71.607  32.202  2.490   1.00 8.30  ? 149  THR B CB  1 
ATOM   3826  O  OG1 . THR B  1 149 ? 72.366  32.970  1.571   1.00 8.01  ? 149  THR B OG1 1 
ATOM   3827  C  CG2 . THR B  1 149 ? 71.856  32.852  3.881   1.00 9.50  ? 149  THR B CG2 1 
ATOM   3828  N  N   . PRO B  1 150 ? 74.467  30.456  2.028   1.00 8.23  ? 150  PRO B N   1 
ATOM   3829  C  CA  . PRO B  1 150 ? 75.845  30.116  2.436   1.00 7.90  ? 150  PRO B CA  1 
ATOM   3830  C  C   . PRO B  1 150 ? 76.351  30.941  3.606   1.00 8.08  ? 150  PRO B C   1 
ATOM   3831  O  O   . PRO B  1 150 ? 76.919  30.335  4.503   1.00 7.68  ? 150  PRO B O   1 
ATOM   3832  C  CB  . PRO B  1 150 ? 76.666  30.331  1.165   1.00 7.40  ? 150  PRO B CB  1 
ATOM   3833  C  CG  . PRO B  1 150 ? 75.699  29.969  0.072   1.00 9.24  ? 150  PRO B CG  1 
ATOM   3834  C  CD  . PRO B  1 150 ? 74.380  30.686  0.570   1.00 7.43  ? 150  PRO B CD  1 
ATOM   3835  N  N   . TYR B  1 151 ? 76.140  32.262  3.606   1.00 7.53  ? 151  TYR B N   1 
ATOM   3836  C  CA  . TYR B  1 151 ? 76.384  33.044  4.816   1.00 7.78  ? 151  TYR B CA  1 
ATOM   3837  C  C   . TYR B  1 151 ? 75.371  34.173  4.863   1.00 8.32  ? 151  TYR B C   1 
ATOM   3838  O  O   . TYR B  1 151 ? 74.739  34.462  3.842   1.00 6.72  ? 151  TYR B O   1 
ATOM   3839  C  CB  . TYR B  1 151 ? 77.843  33.565  4.854   1.00 7.64  ? 151  TYR B CB  1 
ATOM   3840  C  CG  . TYR B  1 151 ? 78.271  34.485  3.693   1.00 8.55  ? 151  TYR B CG  1 
ATOM   3841  C  CD1 . TYR B  1 151 ? 77.913  35.850  3.681   1.00 5.07  ? 151  TYR B CD1 1 
ATOM   3842  C  CD2 . TYR B  1 151 ? 79.077  34.008  2.670   1.00 6.20  ? 151  TYR B CD2 1 
ATOM   3843  C  CE1 . TYR B  1 151 ? 78.326  36.677  2.690   1.00 8.04  ? 151  TYR B CE1 1 
ATOM   3844  C  CE2 . TYR B  1 151 ? 79.521  34.851  1.628   1.00 6.57  ? 151  TYR B CE2 1 
ATOM   3845  C  CZ  . TYR B  1 151 ? 79.139  36.177  1.656   1.00 9.05  ? 151  TYR B CZ  1 
ATOM   3846  O  OH  . TYR B  1 151 ? 79.561  37.023  0.677   1.00 7.80  ? 151  TYR B OH  1 
ATOM   3847  N  N   . ILE B  1 152 ? 75.222  34.823  6.024   1.00 8.35  ? 152  ILE B N   1 
ATOM   3848  C  CA  . ILE B  1 152 ? 74.215  35.866  6.174   1.00 9.96  ? 152  ILE B CA  1 
ATOM   3849  C  C   . ILE B  1 152 ? 74.705  37.141  5.515   1.00 11.87 ? 152  ILE B C   1 
ATOM   3850  O  O   . ILE B  1 152 ? 75.727  37.659  5.909   1.00 9.79  ? 152  ILE B O   1 
ATOM   3851  C  CB  . ILE B  1 152 ? 73.913  36.176  7.687   1.00 10.07 ? 152  ILE B CB  1 
ATOM   3852  C  CG1 . ILE B  1 152 ? 73.813  34.901  8.508   1.00 8.82  ? 152  ILE B CG1 1 
ATOM   3853  C  CG2 . ILE B  1 152 ? 72.642  37.073  7.797   1.00 10.37 ? 152  ILE B CG2 1 
ATOM   3854  C  CD1 . ILE B  1 152 ? 72.625  34.004  8.118   1.00 10.16 ? 152  ILE B CD1 1 
ATOM   3855  N  N   . PRO B  1 153 ? 73.973  37.624  4.512   1.00 13.39 ? 153  PRO B N   1 
ATOM   3856  C  CA  . PRO B  1 153 ? 74.361  38.817  3.762   1.00 17.00 ? 153  PRO B CA  1 
ATOM   3857  C  C   . PRO B  1 153 ? 74.414  40.094  4.627   1.00 20.26 ? 153  PRO B C   1 
ATOM   3858  O  O   . PRO B  1 153 ? 73.546  40.280  5.463   1.00 20.46 ? 153  PRO B O   1 
ATOM   3859  C  CB  . PRO B  1 153 ? 73.280  38.928  2.662   1.00 17.07 ? 153  PRO B CB  1 
ATOM   3860  C  CG  . PRO B  1 153 ? 72.227  37.959  2.985   1.00 14.84 ? 153  PRO B CG  1 
ATOM   3861  C  CD  . PRO B  1 153 ? 72.730  37.015  4.015   1.00 13.06 ? 153  PRO B CD  1 
ATOM   3862  N  N   . SER B  1 154 ? 75.470  40.896  4.442   1.00 23.71 ? 154  SER B N   1 
ATOM   3863  C  CA  . SER B  1 154 ? 75.633  42.198  5.113   1.00 27.39 ? 154  SER B CA  1 
ATOM   3864  C  C   . SER B  1 154 ? 76.223  43.252  4.154   1.00 27.97 ? 154  SER B C   1 
ATOM   3865  O  O   . SER B  1 154 ? 76.425  42.985  2.944   1.00 29.41 ? 154  SER B O   1 
ATOM   3866  C  CB  . SER B  1 154 ? 76.489  42.062  6.393   1.00 27.75 ? 154  SER B CB  1 
ATOM   3867  O  OG  . SER B  1 154 ? 75.740  41.417  7.433   1.00 31.38 ? 154  SER B OG  1 
ATOM   3868  N  N   . SER B  1 159 ? 85.823  47.555  11.052  1.00 30.50 ? 159  SER B N   1 
ATOM   3869  C  CA  . SER B  1 159 ? 86.815  46.575  10.604  1.00 30.52 ? 159  SER B CA  1 
ATOM   3870  C  C   . SER B  1 159 ? 87.869  46.202  11.670  1.00 29.48 ? 159  SER B C   1 
ATOM   3871  O  O   . SER B  1 159 ? 89.104  46.319  11.477  1.00 29.40 ? 159  SER B O   1 
ATOM   3872  C  CB  . SER B  1 159 ? 87.435  46.955  9.248   1.00 30.81 ? 159  SER B CB  1 
ATOM   3873  O  OG  . SER B  1 159 ? 87.142  45.923  8.294   1.00 32.72 ? 159  SER B OG  1 
ATOM   3874  N  N   . SER B  1 160 ? 87.337  45.757  12.805  1.00 28.03 ? 160  SER B N   1 
ATOM   3875  C  CA  . SER B  1 160 ? 88.100  45.060  13.820  1.00 26.68 ? 160  SER B CA  1 
ATOM   3876  C  C   . SER B  1 160 ? 88.297  43.655  13.291  1.00 24.88 ? 160  SER B C   1 
ATOM   3877  O  O   . SER B  1 160 ? 87.460  43.129  12.530  1.00 24.10 ? 160  SER B O   1 
ATOM   3878  C  CB  . SER B  1 160 ? 87.302  44.986  15.136  1.00 27.15 ? 160  SER B CB  1 
ATOM   3879  O  OG  . SER B  1 160 ? 87.903  45.762  16.172  1.00 29.56 ? 160  SER B OG  1 
ATOM   3880  N  N   . THR B  1 161 ? 89.398  43.042  13.698  1.00 22.99 ? 161  THR B N   1 
ATOM   3881  C  CA  . THR B  1 161 ? 89.602  41.609  13.486  1.00 21.20 ? 161  THR B CA  1 
ATOM   3882  C  C   . THR B  1 161 ? 88.325  40.871  13.886  1.00 20.12 ? 161  THR B C   1 
ATOM   3883  O  O   . THR B  1 161 ? 87.677  41.219  14.884  1.00 19.54 ? 161  THR B O   1 
ATOM   3884  C  CB  . THR B  1 161 ? 90.796  41.171  14.337  1.00 21.80 ? 161  THR B CB  1 
ATOM   3885  O  OG1 . THR B  1 161 ? 91.974  41.877  13.886  1.00 21.25 ? 161  THR B OG1 1 
ATOM   3886  C  CG2 . THR B  1 161 ? 91.089  39.684  14.180  1.00 20.75 ? 161  THR B CG2 1 
ATOM   3887  N  N   . THR B  1 162 ? 87.935  39.881  13.084  1.00 18.37 ? 162  THR B N   1 
ATOM   3888  C  CA  . THR B  1 162 ? 86.739  39.094  13.359  1.00 16.42 ? 162  THR B CA  1 
ATOM   3889  C  C   . THR B  1 162 ? 87.023  38.190  14.564  1.00 16.16 ? 162  THR B C   1 
ATOM   3890  O  O   . THR B  1 162 ? 88.165  37.788  14.798  1.00 14.94 ? 162  THR B O   1 
ATOM   3891  C  CB  . THR B  1 162 ? 86.332  38.254  12.113  1.00 16.90 ? 162  THR B CB  1 
ATOM   3892  O  OG1 . THR B  1 162 ? 85.938  39.121  11.034  1.00 16.44 ? 162  THR B OG1 1 
ATOM   3893  C  CG2 . THR B  1 162 ? 85.089  37.450  12.400  1.00 14.16 ? 162  THR B CG2 1 
ATOM   3894  N  N   . GLY B  1 163 ? 85.970  37.907  15.329  1.00 15.96 ? 163  GLY B N   1 
ATOM   3895  C  CA  . GLY B  1 163 ? 86.056  37.045  16.478  1.00 15.80 ? 163  GLY B CA  1 
ATOM   3896  C  C   . GLY B  1 163 ? 86.405  37.778  17.742  1.00 15.73 ? 163  GLY B C   1 
ATOM   3897  O  O   . GLY B  1 163 ? 86.189  39.008  17.872  1.00 16.39 ? 163  GLY B O   1 
ATOM   3898  N  N   . PRO B  1 164 ? 86.946  37.027  18.693  1.00 15.51 ? 164  PRO B N   1 
ATOM   3899  C  CA  . PRO B  1 164 ? 87.282  37.584  20.007  1.00 15.66 ? 164  PRO B CA  1 
ATOM   3900  C  C   . PRO B  1 164 ? 88.368  38.668  19.923  1.00 16.31 ? 164  PRO B C   1 
ATOM   3901  O  O   . PRO B  1 164 ? 89.277  38.609  19.063  1.00 15.96 ? 164  PRO B O   1 
ATOM   3902  C  CB  . PRO B  1 164 ? 87.773  36.346  20.779  1.00 15.17 ? 164  PRO B CB  1 
ATOM   3903  C  CG  . PRO B  1 164 ? 88.294  35.426  19.726  1.00 15.29 ? 164  PRO B CG  1 
ATOM   3904  C  CD  . PRO B  1 164 ? 87.261  35.588  18.613  1.00 15.30 ? 164  PRO B CD  1 
ATOM   3905  N  N   . ASP B  1 165 ? 88.246  39.666  20.804  1.00 17.41 ? 165  ASP B N   1 
ATOM   3906  C  CA  . ASP B  1 165 ? 89.250  40.707  20.959  1.00 17.63 ? 165  ASP B CA  1 
ATOM   3907  C  C   . ASP B  1 165 ? 90.473  40.117  21.658  1.00 17.80 ? 165  ASP B C   1 
ATOM   3908  O  O   . ASP B  1 165 ? 90.482  38.931  22.020  1.00 18.44 ? 165  ASP B O   1 
ATOM   3909  C  CB  . ASP B  1 165 ? 88.682  41.950  21.699  1.00 17.79 ? 165  ASP B CB  1 
ATOM   3910  C  CG  . ASP B  1 165 ? 88.136  41.639  23.106  1.00 18.01 ? 165  ASP B CG  1 
ATOM   3911  O  OD1 . ASP B  1 165 ? 88.649  40.720  23.788  1.00 16.45 ? 165  ASP B OD1 1 
ATOM   3912  O  OD2 . ASP B  1 165 ? 87.195  42.305  23.622  1.00 17.30 ? 165  ASP B OD2 1 
ATOM   3913  N  N   . SER B  1 166 ? 91.510  40.924  21.836  1.00 17.82 ? 166  SER B N   1 
ATOM   3914  C  CA  . SER B  1 166 ? 92.772  40.409  22.359  1.00 18.54 ? 166  SER B CA  1 
ATOM   3915  C  C   . SER B  1 166 ? 92.611  39.904  23.802  1.00 18.65 ? 166  SER B C   1 
ATOM   3916  O  O   . SER B  1 166 ? 93.169  38.850  24.151  1.00 17.91 ? 166  SER B O   1 
ATOM   3917  C  CB  . SER B  1 166 ? 93.908  41.436  22.190  1.00 18.36 ? 166  SER B CB  1 
ATOM   3918  O  OG  . SER B  1 166 ? 93.564  42.670  22.790  1.00 20.71 ? 166  SER B OG  1 
ATOM   3919  N  N   . SER B  1 167 ? 91.826  40.626  24.616  1.00 19.54 ? 167  SER B N   1 
ATOM   3920  C  CA  . SER B  1 167 ? 91.470  40.163  25.968  1.00 20.24 ? 167  SER B CA  1 
ATOM   3921  C  C   . SER B  1 167 ? 90.850  38.764  25.925  1.00 20.74 ? 167  SER B C   1 
ATOM   3922  O  O   . SER B  1 167 ? 91.288  37.863  26.646  1.00 21.78 ? 167  SER B O   1 
ATOM   3923  C  CB  . SER B  1 167 ? 90.483  41.115  26.644  1.00 20.21 ? 167  SER B CB  1 
ATOM   3924  O  OG  . SER B  1 167 ? 91.140  42.249  27.180  1.00 21.15 ? 167  SER B OG  1 
ATOM   3925  N  N   . THR B  1 168 ? 89.855  38.576  25.057  1.00 20.86 ? 168  THR B N   1 
ATOM   3926  C  CA  . THR B  1 168 ? 89.010  37.368  25.082  1.00 20.56 ? 168  THR B CA  1 
ATOM   3927  C  C   . THR B  1 168 ? 89.775  36.160  24.552  1.00 20.19 ? 168  THR B C   1 
ATOM   3928  O  O   . THR B  1 168 ? 89.730  35.079  25.161  1.00 20.08 ? 168  THR B O   1 
ATOM   3929  C  CB  . THR B  1 168 ? 87.688  37.604  24.301  1.00 20.77 ? 168  THR B CB  1 
ATOM   3930  O  OG1 . THR B  1 168 ? 86.963  38.713  24.887  1.00 21.01 ? 168  THR B OG1 1 
ATOM   3931  C  CG2 . THR B  1 168 ? 86.733  36.407  24.405  1.00 20.82 ? 168  THR B CG2 1 
ATOM   3932  N  N   . ILE B  1 169 ? 90.484  36.359  23.428  1.00 19.58 ? 169  ILE B N   1 
ATOM   3933  C  CA  . ILE B  1 169 ? 91.247  35.285  22.785  1.00 18.24 ? 169  ILE B CA  1 
ATOM   3934  C  C   . ILE B  1 169 ? 92.391  34.781  23.687  1.00 18.25 ? 169  ILE B C   1 
ATOM   3935  O  O   . ILE B  1 169 ? 92.922  33.684  23.459  1.00 18.30 ? 169  ILE B O   1 
ATOM   3936  C  CB  . ILE B  1 169 ? 91.729  35.639  21.301  1.00 18.19 ? 169  ILE B CB  1 
ATOM   3937  C  CG1 . ILE B  1 169 ? 91.839  34.341  20.458  1.00 16.85 ? 169  ILE B CG1 1 
ATOM   3938  C  CG2 . ILE B  1 169 ? 93.052  36.436  21.312  1.00 17.02 ? 169  ILE B CG2 1 
ATOM   3939  C  CD1 . ILE B  1 169 ? 92.119  34.510  18.951  1.00 14.04 ? 169  ILE B CD1 1 
ATOM   3940  N  N   . SER B  1 170 ? 92.738  35.576  24.712  1.00 17.61 ? 170  SER B N   1 
ATOM   3941  C  CA  . SER B  1 170 ? 93.686  35.153  25.742  1.00 17.39 ? 170  SER B CA  1 
ATOM   3942  C  C   . SER B  1 170 ? 93.034  34.309  26.868  1.00 17.00 ? 170  SER B C   1 
ATOM   3943  O  O   . SER B  1 170 ? 93.716  33.948  27.822  1.00 17.32 ? 170  SER B O   1 
ATOM   3944  C  CB  . SER B  1 170 ? 94.428  36.379  26.334  1.00 17.01 ? 170  SER B CB  1 
ATOM   3945  O  OG  . SER B  1 170 ? 95.290  36.965  25.362  1.00 17.12 ? 170  SER B OG  1 
ATOM   3946  N  N   . THR B  1 171 ? 91.738  34.006  26.745  1.00 16.72 ? 171  THR B N   1 
ATOM   3947  C  CA  . THR B  1 171 ? 90.958  33.346  27.811  1.00 16.44 ? 171  THR B CA  1 
ATOM   3948  C  C   . THR B  1 171 ? 90.526  31.905  27.440  1.00 14.82 ? 171  THR B C   1 
ATOM   3949  O  O   . THR B  1 171 ? 89.774  31.253  28.195  1.00 14.48 ? 171  THR B O   1 
ATOM   3950  C  CB  . THR B  1 171 ? 89.736  34.226  28.211  1.00 16.30 ? 171  THR B CB  1 
ATOM   3951  O  OG1 . THR B  1 171 ? 90.196  35.407  28.890  1.00 18.66 ? 171  THR B OG1 1 
ATOM   3952  C  CG2 . THR B  1 171 ? 88.925  33.583  29.347  1.00 19.43 ? 171  THR B CG2 1 
ATOM   3953  N  N   . LEU B  1 172 ? 91.123  31.417  26.346  1.00 11.27 ? 172  LEU B N   1 
ATOM   3954  C  CA  . LEU B  1 172 ? 90.680  30.322  25.504  1.00 8.17  ? 172  LEU B CA  1 
ATOM   3955  C  C   . LEU B  1 172 ? 91.612  29.105  25.521  1.00 6.44  ? 172  LEU B C   1 
ATOM   3956  O  O   . LEU B  1 172 ? 91.441  28.182  24.725  1.00 4.37  ? 172  LEU B O   1 
ATOM   3957  C  CB  . LEU B  1 172 ? 90.597  30.813  24.040  1.00 8.32  ? 172  LEU B CB  1 
ATOM   3958  C  CG  . LEU B  1 172 ? 89.508  31.805  23.620  1.00 8.46  ? 172  LEU B CG  1 
ATOM   3959  C  CD1 . LEU B  1 172 ? 89.235  31.600  22.142  1.00 9.63  ? 172  LEU B CD1 1 
ATOM   3960  C  CD2 . LEU B  1 172 ? 88.199  31.627  24.438  1.00 11.16 ? 172  LEU B CD2 1 
ATOM   3961  N  N   . GLN B  1 173 ? 92.549  29.075  26.455  1.00 5.17  ? 173  GLN B N   1 
ATOM   3962  C  CA  . GLN B  1 173 ? 93.495  27.971  26.544  1.00 6.03  ? 173  GLN B CA  1 
ATOM   3963  C  C   . GLN B  1 173 ? 92.774  26.653  26.804  1.00 5.36  ? 173  GLN B C   1 
ATOM   3964  O  O   . GLN B  1 173 ? 93.283  25.600  26.435  1.00 4.16  ? 173  GLN B O   1 
ATOM   3965  C  CB  . GLN B  1 173 ? 94.518  28.259  27.650  1.00 6.93  ? 173  GLN B CB  1 
ATOM   3966  C  CG  . GLN B  1 173 ? 95.417  29.406  27.243  1.00 10.14 ? 173  GLN B CG  1 
ATOM   3967  C  CD  . GLN B  1 173 ? 96.245  29.988  28.359  1.00 19.10 ? 173  GLN B CD  1 
ATOM   3968  O  OE1 . GLN B  1 173 ? 97.476  29.886  28.338  1.00 19.76 ? 173  GLN B OE1 1 
ATOM   3969  N  NE2 . GLN B  1 173 ? 95.594  30.667  29.299  1.00 22.51 ? 173  GLN B NE2 1 
ATOM   3970  N  N   . SER B  1 174 ? 91.621  26.699  27.489  1.00 3.92  ? 174  SER B N   1 
ATOM   3971  C  CA  . SER B  1 174 ? 90.880  25.452  27.728  1.00 4.79  ? 174  SER B CA  1 
ATOM   3972  C  C   . SER B  1 174 ? 90.371  24.799  26.467  1.00 4.42  ? 174  SER B C   1 
ATOM   3973  O  O   . SER B  1 174 ? 90.151  23.589  26.444  1.00 4.72  ? 174  SER B O   1 
ATOM   3974  C  CB  . SER B  1 174 ? 89.749  25.668  28.719  1.00 3.68  ? 174  SER B CB  1 
ATOM   3975  O  OG  . SER B  1 174 ? 90.341  25.903  29.978  1.00 9.58  ? 174  SER B OG  1 
ATOM   3976  N  N   . PHE B  1 175 ? 90.209  25.594  25.411  1.00 3.60  ? 175  PHE B N   1 
ATOM   3977  C  CA  . PHE B  1 175 ? 89.806  25.070  24.124  1.00 3.62  ? 175  PHE B CA  1 
ATOM   3978  C  C   . PHE B  1 175 ? 91.022  24.766  23.261  1.00 4.19  ? 175  PHE B C   1 
ATOM   3979  O  O   . PHE B  1 175 ? 90.874  24.480  22.070  1.00 4.51  ? 175  PHE B O   1 
ATOM   3980  C  CB  . PHE B  1 175 ? 88.939  26.099  23.380  1.00 2.85  ? 175  PHE B CB  1 
ATOM   3981  C  CG  . PHE B  1 175 ? 87.568  26.298  23.971  1.00 2.10  ? 175  PHE B CG  1 
ATOM   3982  C  CD1 . PHE B  1 175 ? 86.633  25.271  23.959  1.00 3.10  ? 175  PHE B CD1 1 
ATOM   3983  C  CD2 . PHE B  1 175 ? 87.225  27.500  24.540  1.00 2.00  ? 175  PHE B CD2 1 
ATOM   3984  C  CE1 . PHE B  1 175 ? 85.369  25.462  24.504  1.00 2.00  ? 175  PHE B CE1 1 
ATOM   3985  C  CE2 . PHE B  1 175 ? 85.979  27.707  25.072  1.00 4.54  ? 175  PHE B CE2 1 
ATOM   3986  C  CZ  . PHE B  1 175 ? 85.039  26.667  25.053  1.00 4.17  ? 175  PHE B CZ  1 
ATOM   3987  N  N   . ASP B  1 176 ? 92.223  24.836  23.850  1.00 4.83  ? 176  ASP B N   1 
ATOM   3988  C  CA  . ASP B  1 176 ? 93.467  24.582  23.084  1.00 4.37  ? 176  ASP B CA  1 
ATOM   3989  C  C   . ASP B  1 176 ? 93.720  25.690  22.071  1.00 3.89  ? 176  ASP B C   1 
ATOM   3990  O  O   . ASP B  1 176 ? 94.196  25.444  20.967  1.00 3.45  ? 176  ASP B O   1 
ATOM   3991  C  CB  . ASP B  1 176 ? 93.501  23.187  22.417  1.00 4.98  ? 176  ASP B CB  1 
ATOM   3992  C  CG  . ASP B  1 176 ? 94.893  22.823  21.873  1.00 4.35  ? 176  ASP B CG  1 
ATOM   3993  O  OD1 . ASP B  1 176 ? 95.892  23.226  22.508  1.00 5.15  ? 176  ASP B OD1 1 
ATOM   3994  O  OD2 . ASP B  1 176 ? 95.077  22.191  20.815  1.00 3.90  ? 176  ASP B OD2 1 
ATOM   3995  N  N   . VAL B  1 177 ? 93.387  26.919  22.478  1.00 3.73  ? 177  VAL B N   1 
ATOM   3996  C  CA  . VAL B  1 177 ? 93.680  28.094  21.676  1.00 3.15  ? 177  VAL B CA  1 
ATOM   3997  C  C   . VAL B  1 177 ? 94.563  29.020  22.509  1.00 2.63  ? 177  VAL B C   1 
ATOM   3998  O  O   . VAL B  1 177 ? 94.157  29.456  23.583  1.00 3.23  ? 177  VAL B O   1 
ATOM   3999  C  CB  . VAL B  1 177 ? 92.394  28.853  21.203  1.00 2.30  ? 177  VAL B CB  1 
ATOM   4000  C  CG1 . VAL B  1 177 ? 92.839  30.133  20.460  1.00 2.54  ? 177  VAL B CG1 1 
ATOM   4001  C  CG2 . VAL B  1 177 ? 91.540  27.974  20.273  1.00 2.00  ? 177  VAL B CG2 1 
ATOM   4002  N  N   . TYR B  1 178 ? 95.789  29.273  22.043  1.00 3.25  ? 178  TYR B N   1 
ATOM   4003  C  CA  . TYR B  1 178 ? 96.783  30.067  22.801  1.00 3.90  ? 178  TYR B CA  1 
ATOM   4004  C  C   . TYR B  1 178 ? 97.083  31.319  22.007  1.00 4.06  ? 178  TYR B C   1 
ATOM   4005  O  O   . TYR B  1 178 ? 97.620  31.217  20.923  1.00 2.38  ? 178  TYR B O   1 
ATOM   4006  C  CB  . TYR B  1 178 ? 98.097  29.259  23.026  1.00 4.04  ? 178  TYR B CB  1 
ATOM   4007  C  CG  . TYR B  1 178 ? 97.886  28.099  23.961  1.00 3.97  ? 178  TYR B CG  1 
ATOM   4008  C  CD1 . TYR B  1 178 ? 97.378  26.881  23.489  1.00 5.48  ? 178  TYR B CD1 1 
ATOM   4009  C  CD2 . TYR B  1 178 ? 98.079  28.243  25.327  1.00 3.07  ? 178  TYR B CD2 1 
ATOM   4010  C  CE1 . TYR B  1 178 ? 97.125  25.821  24.373  1.00 2.41  ? 178  TYR B CE1 1 
ATOM   4011  C  CE2 . TYR B  1 178 ? 97.833  27.176  26.218  1.00 8.13  ? 178  TYR B CE2 1 
ATOM   4012  C  CZ  . TYR B  1 178 ? 97.349  25.966  25.699  1.00 4.34  ? 178  TYR B CZ  1 
ATOM   4013  O  OH  . TYR B  1 178 ? 97.099  24.898  26.543  1.00 7.44  ? 178  TYR B OH  1 
ATOM   4014  N  N   . ALA B  1 179 ? 96.739  32.485  22.549  1.00 4.45  ? 179  ALA B N   1 
ATOM   4015  C  CA  . ALA B  1 179 ? 96.947  33.723  21.811  1.00 5.30  ? 179  ALA B CA  1 
ATOM   4016  C  C   . ALA B  1 179 ? 98.433  33.982  21.560  1.00 5.80  ? 179  ALA B C   1 
ATOM   4017  O  O   . ALA B  1 179 ? 99.276  33.642  22.375  1.00 4.46  ? 179  ALA B O   1 
ATOM   4018  C  CB  . ALA B  1 179 ? 96.325  34.895  22.538  1.00 3.93  ? 179  ALA B CB  1 
ATOM   4019  N  N   . GLU B  1 180 ? 98.733  34.585  20.408  1.00 6.71  ? 180  GLU B N   1 
ATOM   4020  C  CA  . GLU B  1 180 ? 100.082 34.990  20.049  1.00 8.39  ? 180  GLU B CA  1 
ATOM   4021  C  C   . GLU B  1 180 ? 99.949  36.434  19.573  1.00 9.18  ? 180  GLU B C   1 
ATOM   4022  O  O   . GLU B  1 180 ? 100.027 36.719  18.380  1.00 8.52  ? 180  GLU B O   1 
ATOM   4023  C  CB  . GLU B  1 180 ? 100.609 34.085  18.926  1.00 9.64  ? 180  GLU B CB  1 
ATOM   4024  C  CG  . GLU B  1 180 ? 100.925 32.672  19.367  1.00 9.01  ? 180  GLU B CG  1 
ATOM   4025  C  CD  . GLU B  1 180 ? 102.097 32.632  20.334  1.00 15.69 ? 180  GLU B CD  1 
ATOM   4026  O  OE1 . GLU B  1 180 ? 102.954 33.555  20.346  1.00 18.21 ? 180  GLU B OE1 1 
ATOM   4027  O  OE2 . GLU B  1 180 ? 102.143 31.689  21.130  1.00 19.06 ? 180  GLU B OE2 1 
ATOM   4028  N  N   . LEU B  1 181 ? 99.717  37.338  20.529  1.00 10.77 ? 181  LEU B N   1 
ATOM   4029  C  CA  . LEU B  1 181 ? 99.349  38.724  20.222  1.00 11.79 ? 181  LEU B CA  1 
ATOM   4030  C  C   . LEU B  1 181 ? 100.519 39.556  19.650  1.00 11.87 ? 181  LEU B C   1 
ATOM   4031  O  O   . LEU B  1 181 ? 100.290 40.557  18.955  1.00 11.62 ? 181  LEU B O   1 
ATOM   4032  C  CB  . LEU B  1 181 ? 98.698  39.411  21.437  1.00 12.21 ? 181  LEU B CB  1 
ATOM   4033  C  CG  . LEU B  1 181 ? 97.321  38.865  21.865  1.00 13.60 ? 181  LEU B CG  1 
ATOM   4034  C  CD1 . LEU B  1 181 ? 96.808  39.564  23.095  1.00 17.73 ? 181  LEU B CD1 1 
ATOM   4035  C  CD2 . LEU B  1 181 ? 96.258  38.895  20.738  1.00 16.96 ? 181  LEU B CD2 1 
ATOM   4036  N  N   . SER B  1 182 ? 101.755 39.113  19.891  1.00 11.16 ? 182  SER B N   1 
ATOM   4037  C  CA  . SER B  1 182 ? 102.924 39.780  19.318  1.00 10.66 ? 182  SER B CA  1 
ATOM   4038  C  C   . SER B  1 182 ? 103.242 39.386  17.840  1.00 10.33 ? 182  SER B C   1 
ATOM   4039  O  O   . SER B  1 182 ? 104.158 39.959  17.231  1.00 10.17 ? 182  SER B O   1 
ATOM   4040  C  CB  . SER B  1 182 ? 104.126 39.501  20.200  1.00 11.54 ? 182  SER B CB  1 
ATOM   4041  O  OG  . SER B  1 182 ? 104.552 38.170  19.956  1.00 13.64 ? 182  SER B OG  1 
ATOM   4042  N  N   . PHE B  1 183 ? 102.494 38.428  17.280  1.00 8.67  ? 183  PHE B N   1 
ATOM   4043  C  CA  . PHE B  1 183 ? 102.692 37.972  15.889  1.00 8.13  ? 183  PHE B CA  1 
ATOM   4044  C  C   . PHE B  1 183 ? 102.236 39.072  14.956  1.00 8.08  ? 183  PHE B C   1 
ATOM   4045  O  O   . PHE B  1 183 ? 101.154 39.585  15.124  1.00 8.03  ? 183  PHE B O   1 
ATOM   4046  C  CB  . PHE B  1 183 ? 101.835 36.735  15.632  1.00 7.80  ? 183  PHE B CB  1 
ATOM   4047  C  CG  . PHE B  1 183 ? 102.049 36.073  14.286  1.00 7.08  ? 183  PHE B CG  1 
ATOM   4048  C  CD1 . PHE B  1 183 ? 103.162 35.250  14.048  1.00 6.77  ? 183  PHE B CD1 1 
ATOM   4049  C  CD2 . PHE B  1 183 ? 101.125 36.245  13.244  1.00 4.31  ? 183  PHE B CD2 1 
ATOM   4050  C  CE1 . PHE B  1 183 ? 103.306 34.591  12.794  1.00 2.00  ? 183  PHE B CE1 1 
ATOM   4051  C  CE2 . PHE B  1 183 ? 101.271 35.597  12.034  1.00 2.47  ? 183  PHE B CE2 1 
ATOM   4052  C  CZ  . PHE B  1 183 ? 102.368 34.759  11.798  1.00 2.65  ? 183  PHE B CZ  1 
ATOM   4053  N  N   . THR B  1 184 ? 103.070 39.438  13.988  1.00 8.19  ? 184  THR B N   1 
ATOM   4054  C  CA  . THR B  1 184 ? 102.764 40.466  13.018  1.00 7.26  ? 184  THR B CA  1 
ATOM   4055  C  C   . THR B  1 184 ? 102.750 39.731  11.693  1.00 6.70  ? 184  THR B C   1 
ATOM   4056  O  O   . THR B  1 184 ? 103.844 39.391  11.186  1.00 7.02  ? 184  THR B O   1 
ATOM   4057  C  CB  . THR B  1 184 ? 103.875 41.525  13.000  1.00 8.17  ? 184  THR B CB  1 
ATOM   4058  O  OG1 . THR B  1 184 ? 103.957 42.200  14.262  1.00 9.14  ? 184  THR B OG1 1 
ATOM   4059  C  CG2 . THR B  1 184 ? 103.535 42.642  12.035  1.00 9.20  ? 184  THR B CG2 1 
ATOM   4060  N  N   . PRO B  1 185 ? 101.561 39.467  11.115  1.00 5.49  ? 185  PRO B N   1 
ATOM   4061  C  CA  . PRO B  1 185 ? 101.473 38.779  9.818   1.00 5.25  ? 185  PRO B CA  1 
ATOM   4062  C  C   . PRO B  1 185 ? 102.235 39.607  8.788   1.00 4.59  ? 185  PRO B C   1 
ATOM   4063  O  O   . PRO B  1 185 ? 102.073 40.841  8.750   1.00 3.02  ? 185  PRO B O   1 
ATOM   4064  C  CB  . PRO B  1 185 ? 99.960  38.799  9.472   1.00 4.17  ? 185  PRO B CB  1 
ATOM   4065  C  CG  . PRO B  1 185 ? 99.296  38.870  10.767  1.00 4.37  ? 185  PRO B CG  1 
ATOM   4066  C  CD  . PRO B  1 185 ? 100.208 39.761  11.649  1.00 6.38  ? 185  PRO B CD  1 
ATOM   4067  N  N   . ARG B  1 186 ? 103.032 38.940  7.965   1.00 2.70  ? 186  ARG B N   1 
ATOM   4068  C  CA  . ARG B  1 186 ? 103.896 39.681  7.052   1.00 4.61  ? 186  ARG B CA  1 
ATOM   4069  C  C   . ARG B  1 186 ? 103.089 40.435  5.989   1.00 5.23  ? 186  ARG B C   1 
ATOM   4070  O  O   . ARG B  1 186 ? 102.019 40.001  5.609   1.00 3.97  ? 186  ARG B O   1 
ATOM   4071  C  CB  . ARG B  1 186 ? 104.971 38.783  6.440   1.00 4.29  ? 186  ARG B CB  1 
ATOM   4072  C  CG  . ARG B  1 186 ? 104.468 37.493  5.743   1.00 2.00  ? 186  ARG B CG  1 
ATOM   4073  C  CD  . ARG B  1 186 ? 105.595 36.587  5.140   1.00 5.58  ? 186  ARG B CD  1 
ATOM   4074  N  NE  . ARG B  1 186 ? 106.743 37.396  4.719   1.00 5.59  ? 186  ARG B NE  1 
ATOM   4075  C  CZ  . ARG B  1 186 ? 108.006 37.290  5.150   1.00 7.88  ? 186  ARG B CZ  1 
ATOM   4076  N  NH1 . ARG B  1 186 ? 108.403 36.310  5.983   1.00 8.18  ? 186  ARG B NH1 1 
ATOM   4077  N  NH2 . ARG B  1 186 ? 108.885 38.180  4.718   1.00 2.58  ? 186  ARG B NH2 1 
ATOM   4078  N  N   . THR B  1 187 ? 103.598 41.583  5.545   1.00 6.83  ? 187  THR B N   1 
ATOM   4079  C  CA  . THR B  1 187 ? 102.833 42.436  4.633   1.00 9.05  ? 187  THR B CA  1 
ATOM   4080  C  C   . THR B  1 187 ? 103.583 42.712  3.330   1.00 9.69  ? 187  THR B C   1 
ATOM   4081  O  O   . THR B  1 187 ? 103.446 43.803  2.771   1.00 10.85 ? 187  THR B O   1 
ATOM   4082  C  CB  . THR B  1 187 ? 102.578 43.775  5.302   1.00 10.35 ? 187  THR B CB  1 
ATOM   4083  O  OG1 . THR B  1 187 ? 103.837 44.385  5.616   1.00 10.14 ? 187  THR B OG1 1 
ATOM   4084  C  CG2 . THR B  1 187 ? 101.906 43.604  6.686   1.00 12.49 ? 187  THR B CG2 1 
ATOM   4085  N  N   . ASP B  1 188 ? 104.400 41.746  2.885   1.00 8.24  ? 188  ASP B N   1 
ATOM   4086  C  CA  . ASP B  1 188 ? 105.153 41.828  1.637   1.00 6.81  ? 188  ASP B CA  1 
ATOM   4087  C  C   . ASP B  1 188 ? 104.698 40.754  0.660   1.00 4.85  ? 188  ASP B C   1 
ATOM   4088  O  O   . ASP B  1 188 ? 105.448 40.303  -0.190  1.00 3.59  ? 188  ASP B O   1 
ATOM   4089  C  CB  . ASP B  1 188 ? 106.657 41.708  1.910   1.00 6.92  ? 188  ASP B CB  1 
ATOM   4090  C  CG  . ASP B  1 188 ? 107.029 40.433  2.699   1.00 9.83  ? 188  ASP B CG  1 
ATOM   4091  O  OD1 . ASP B  1 188 ? 106.146 39.629  3.167   1.00 7.01  ? 188  ASP B OD1 1 
ATOM   4092  O  OD2 . ASP B  1 188 ? 108.220 40.160  2.913   1.00 8.48  ? 188  ASP B OD2 1 
ATOM   4093  N  N   . THR B  1 189 ? 103.433 40.356  0.759   1.00 4.81  ? 189  THR B N   1 
ATOM   4094  C  CA  . THR B  1 189 ? 102.842 39.405  -0.190  1.00 4.74  ? 189  THR B CA  1 
ATOM   4095  C  C   . THR B  1 189 ? 102.927 39.995  -1.615  1.00 4.83  ? 189  THR B C   1 
ATOM   4096  O  O   . THR B  1 189 ? 102.646 41.180  -1.811  1.00 5.24  ? 189  THR B O   1 
ATOM   4097  C  CB  . THR B  1 189 ? 101.377 39.171  0.169   1.00 4.35  ? 189  THR B CB  1 
ATOM   4098  O  OG1 . THR B  1 189 ? 101.240 39.017  1.589   1.00 7.21  ? 189  THR B OG1 1 
ATOM   4099  C  CG2 . THR B  1 189 ? 100.884 37.878  -0.385  1.00 5.97  ? 189  THR B CG2 1 
ATOM   4100  N  N   . VAL B  1 190 ? 103.319 39.155  -2.565  1.00 5.50  ? 190  VAL B N   1 
ATOM   4101  C  CA  . VAL B  1 190 ? 103.359 39.448  -3.995  1.00 6.35  ? 190  VAL B CA  1 
ATOM   4102  C  C   . VAL B  1 190 ? 102.953 38.164  -4.715  1.00 6.62  ? 190  VAL B C   1 
ATOM   4103  O  O   . VAL B  1 190 ? 103.409 37.077  -4.360  1.00 7.96  ? 190  VAL B O   1 
ATOM   4104  C  CB  . VAL B  1 190 ? 104.779 39.789  -4.482  1.00 5.35  ? 190  VAL B CB  1 
ATOM   4105  C  CG1 . VAL B  1 190 ? 104.727 40.148  -5.983  1.00 6.65  ? 190  VAL B CG1 1 
ATOM   4106  C  CG2 . VAL B  1 190 ? 105.452 40.965  -3.614  1.00 9.32  ? 190  VAL B CG2 1 
ATOM   4107  N  N   . ASN B  1 191 ? 102.086 38.256  -5.712  1.00 7.06  ? 191  ASN B N   1 
ATOM   4108  C  CA  . ASN B  1 191 ? 101.545 37.042  -6.356  1.00 6.93  ? 191  ASN B CA  1 
ATOM   4109  C  C   . ASN B  1 191 ? 101.054 35.969  -5.388  1.00 7.63  ? 191  ASN B C   1 
ATOM   4110  O  O   . ASN B  1 191 ? 101.203 34.737  -5.668  1.00 5.78  ? 191  ASN B O   1 
ATOM   4111  C  CB  . ASN B  1 191 ? 102.573 36.432  -7.388  1.00 7.47  ? 191  ASN B CB  1 
ATOM   4112  C  CG  . ASN B  1 191 ? 102.937 37.393  -8.550  1.00 8.29  ? 191  ASN B CG  1 
ATOM   4113  O  OD1 . ASN B  1 191 ? 102.166 38.321  -8.904  1.00 7.39  ? 191  ASN B OD1 1 
ATOM   4114  N  ND2 . ASN B  1 191 ? 104.150 37.178  -9.125  1.00 10.28 ? 191  ASN B ND2 1 
ATOM   4115  N  N   . GLY B  1 192 ? 100.452 36.407  -4.262  1.00 6.77  ? 192  GLY B N   1 
ATOM   4116  C  CA  . GLY B  1 192 ? 99.800  35.499  -3.340  1.00 5.86  ? 192  GLY B CA  1 
ATOM   4117  C  C   . GLY B  1 192 ? 100.783 34.678  -2.516  1.00 5.39  ? 192  GLY B C   1 
ATOM   4118  O  O   . GLY B  1 192 ? 100.429 33.652  -1.922  1.00 6.04  ? 192  GLY B O   1 
ATOM   4119  N  N   . THR B  1 193 ? 102.041 35.122  -2.479  1.00 5.67  ? 193  THR B N   1 
ATOM   4120  C  CA  . THR B  1 193 ? 102.963 34.474  -1.560  1.00 5.09  ? 193  THR B CA  1 
ATOM   4121  C  C   . THR B  1 193 ? 103.990 35.423  -0.981  1.00 4.83  ? 193  THR B C   1 
ATOM   4122  O  O   . THR B  1 193 ? 104.296 36.470  -1.586  1.00 2.60  ? 193  THR B O   1 
ATOM   4123  C  CB  . THR B  1 193 ? 103.619 33.239  -2.274  1.00 4.81  ? 193  THR B CB  1 
ATOM   4124  O  OG1 . THR B  1 193 ? 104.383 32.497  -1.312  1.00 6.40  ? 193  THR B OG1 1 
ATOM   4125  C  CG2 . THR B  1 193 ? 104.628 33.708  -3.338  1.00 5.29  ? 193  THR B CG2 1 
ATOM   4126  N  N   . ALA B  1 194 ? 104.518 35.025  0.190   1.00 4.18  ? 194  ALA B N   1 
ATOM   4127  C  CA  . ALA B  1 194 ? 105.713 35.601  0.802   1.00 5.22  ? 194  ALA B CA  1 
ATOM   4128  C  C   . ALA B  1 194 ? 106.321 34.602  1.798   1.00 5.60  ? 194  ALA B C   1 
ATOM   4129  O  O   . ALA B  1 194 ? 105.595 33.756  2.357   1.00 5.04  ? 194  ALA B O   1 
ATOM   4130  C  CB  . ALA B  1 194 ? 105.411 36.951  1.485   1.00 2.00  ? 194  ALA B CB  1 
ATOM   4131  N  N   . PRO B  1 195 ? 107.644 34.648  1.995   1.00 5.33  ? 195  PRO B N   1 
ATOM   4132  C  CA  . PRO B  1 195 ? 108.532 35.555  1.290   1.00 7.21  ? 195  PRO B CA  1 
ATOM   4133  C  C   . PRO B  1 195 ? 108.789 35.099  -0.160  1.00 8.62  ? 195  PRO B C   1 
ATOM   4134  O  O   . PRO B  1 195 ? 108.181 34.150  -0.686  1.00 9.60  ? 195  PRO B O   1 
ATOM   4135  C  CB  . PRO B  1 195 ? 109.821 35.470  2.146   1.00 7.19  ? 195  PRO B CB  1 
ATOM   4136  C  CG  . PRO B  1 195 ? 109.858 33.987  2.561   1.00 5.57  ? 195  PRO B CG  1 
ATOM   4137  C  CD  . PRO B  1 195 ? 108.386 33.729  2.888   1.00 6.78  ? 195  PRO B CD  1 
ATOM   4138  N  N   . ALA B  1 196 ? 109.695 35.807  -0.803  1.00 11.36 ? 196  ALA B N   1 
ATOM   4139  C  CA  . ALA B  1 196 ? 109.967 35.666  -2.232  1.00 12.60 ? 196  ALA B CA  1 
ATOM   4140  C  C   . ALA B  1 196 ? 110.532 34.306  -2.671  1.00 14.11 ? 196  ALA B C   1 
ATOM   4141  O  O   . ALA B  1 196 ? 110.186 33.812  -3.754  1.00 15.18 ? 196  ALA B O   1 
ATOM   4142  C  CB  . ALA B  1 196 ? 110.907 36.802  -2.655  1.00 12.05 ? 196  ALA B CB  1 
ATOM   4143  N  N   . ASN B  1 197 ? 111.361 33.678  -1.841  1.00 14.96 ? 197  ASN B N   1 
ATOM   4144  C  CA  . ASN B  1 197 ? 111.936 32.373  -2.238  1.00 16.07 ? 197  ASN B CA  1 
ATOM   4145  C  C   . ASN B  1 197 ? 111.001 31.212  -1.996  1.00 16.19 ? 197  ASN B C   1 
ATOM   4146  O  O   . ASN B  1 197 ? 111.392 30.205  -1.398  1.00 18.90 ? 197  ASN B O   1 
ATOM   4147  C  CB  . ASN B  1 197 ? 113.357 32.130  -1.634  1.00 16.65 ? 197  ASN B CB  1 
ATOM   4148  C  CG  . ASN B  1 197 ? 113.375 31.993  -0.067  1.00 18.18 ? 197  ASN B CG  1 
ATOM   4149  O  OD1 . ASN B  1 197 ? 112.366 32.202  0.630   1.00 18.29 ? 197  ASN B OD1 1 
ATOM   4150  N  ND2 . ASN B  1 197 ? 114.553 31.627  0.472   1.00 19.50 ? 197  ASN B ND2 1 
ATOM   4151  N  N   . THR B  1 198 ? 109.755 31.343  -2.453  1.00 14.59 ? 198  THR B N   1 
ATOM   4152  C  CA  . THR B  1 198 ? 108.741 30.310  -2.207  1.00 12.34 ? 198  THR B CA  1 
ATOM   4153  C  C   . THR B  1 198 ? 108.069 29.922  -3.515  1.00 12.25 ? 198  THR B C   1 
ATOM   4154  O  O   . THR B  1 198 ? 108.078 30.719  -4.466  1.00 12.71 ? 198  THR B O   1 
ATOM   4155  C  CB  . THR B  1 198 ? 107.655 30.785  -1.219  1.00 11.69 ? 198  THR B CB  1 
ATOM   4156  O  OG1 . THR B  1 198 ? 107.039 31.984  -1.698  1.00 9.41  ? 198  THR B OG1 1 
ATOM   4157  C  CG2 . THR B  1 198 ? 108.249 31.129  0.169   1.00 9.71  ? 198  THR B CG2 1 
ATOM   4158  N  N   . VAL B  1 199 ? 107.431 28.752  -3.532  1.00 11.39 ? 199  VAL B N   1 
ATOM   4159  C  CA  . VAL B  1 199 ? 106.828 28.241  -4.766  1.00 10.98 ? 199  VAL B CA  1 
ATOM   4160  C  C   . VAL B  1 199 ? 105.322 28.152  -4.590  1.00 10.84 ? 199  VAL B C   1 
ATOM   4161  O  O   . VAL B  1 199 ? 104.838 27.349  -3.786  1.00 10.05 ? 199  VAL B O   1 
ATOM   4162  C  CB  . VAL B  1 199 ? 107.412 26.845  -5.170  1.00 11.52 ? 199  VAL B CB  1 
ATOM   4163  C  CG1 . VAL B  1 199 ? 106.698 26.291  -6.392  1.00 12.26 ? 199  VAL B CG1 1 
ATOM   4164  C  CG2 . VAL B  1 199 ? 108.930 26.936  -5.425  1.00 10.88 ? 199  VAL B CG2 1 
ATOM   4165  N  N   . TRP B  1 200 ? 104.589 28.953  -5.363  1.00 9.97  ? 200  TRP B N   1 
ATOM   4166  C  CA  . TRP B  1 200 ? 103.124 29.023  -5.201  1.00 10.24 ? 200  TRP B CA  1 
ATOM   4167  C  C   . TRP B  1 200 ? 102.351 29.215  -6.514  1.00 9.17  ? 200  TRP B C   1 
ATOM   4168  O  O   . TRP B  1 200 ? 102.280 30.320  -7.076  1.00 9.32  ? 200  TRP B O   1 
ATOM   4169  C  CB  . TRP B  1 200 ? 102.735 30.121  -4.173  1.00 9.97  ? 200  TRP B CB  1 
ATOM   4170  C  CG  . TRP B  1 200 ? 101.299 29.978  -3.685  1.00 10.63 ? 200  TRP B CG  1 
ATOM   4171  C  CD1 . TRP B  1 200 ? 100.290 30.914  -3.773  1.00 7.32  ? 200  TRP B CD1 1 
ATOM   4172  C  CD2 . TRP B  1 200 ? 100.722 28.822  -3.028  1.00 6.04  ? 200  TRP B CD2 1 
ATOM   4173  N  NE1 . TRP B  1 200 ? 99.135  30.404  -3.215  1.00 9.32  ? 200  TRP B NE1 1 
ATOM   4174  C  CE2 . TRP B  1 200 ? 99.367  29.125  -2.761  1.00 8.70  ? 200  TRP B CE2 1 
ATOM   4175  C  CE3 . TRP B  1 200 ? 101.216 27.543  -2.665  1.00 8.20  ? 200  TRP B CE3 1 
ATOM   4176  C  CZ2 . TRP B  1 200 ? 98.485  28.204  -2.155  1.00 10.11 ? 200  TRP B CZ2 1 
ATOM   4177  C  CZ3 . TRP B  1 200 ? 100.334 26.613  -2.031  1.00 4.89  ? 200  TRP B CZ3 1 
ATOM   4178  C  CH2 . TRP B  1 200 ? 98.980  26.972  -1.783  1.00 7.38  ? 200  TRP B CH2 1 
ATOM   4179  N  N   . HIS B  1 201 ? 101.799 28.097  -6.977  1.00 8.70  ? 201  HIS B N   1 
ATOM   4180  C  CA  . HIS B  1 201 ? 101.122 27.979  -8.256  1.00 8.40  ? 201  HIS B CA  1 
ATOM   4181  C  C   . HIS B  1 201 ? 102.103 28.185  -9.406  1.00 9.42  ? 201  HIS B C   1 
ATOM   4182  O  O   . HIS B  1 201 ? 101.676 28.518  -10.496 1.00 8.49  ? 201  HIS B O   1 
ATOM   4183  C  CB  . HIS B  1 201 ? 99.988  28.994  -8.367  1.00 8.29  ? 201  HIS B CB  1 
ATOM   4184  C  CG  . HIS B  1 201 ? 98.772  28.617  -7.576  1.00 5.71  ? 201  HIS B CG  1 
ATOM   4185  N  ND1 . HIS B  1 201 ? 97.727  27.905  -8.114  1.00 7.28  ? 201  HIS B ND1 1 
ATOM   4186  C  CD2 . HIS B  1 201 ? 98.404  28.935  -6.312  1.00 8.85  ? 201  HIS B CD2 1 
ATOM   4187  C  CE1 . HIS B  1 201 ? 96.781  27.749  -7.198  1.00 5.96  ? 201  HIS B CE1 1 
ATOM   4188  N  NE2 . HIS B  1 201 ? 97.177  28.355  -6.089  1.00 8.79  ? 201  HIS B NE2 1 
ATOM   4189  N  N   . THR B  1 202 ? 103.402 28.011  -9.139  1.00 9.26  ? 202  THR B N   1 
ATOM   4190  C  CA  . THR B  1 202 ? 104.437 28.159  -10.188 1.00 10.81 ? 202  THR B CA  1 
ATOM   4191  C  C   . THR B  1 202 ? 105.367 26.959  -10.232 1.00 10.59 ? 202  THR B C   1 
ATOM   4192  O  O   . THR B  1 202 ? 106.400 26.981  -10.936 1.00 10.47 ? 202  THR B O   1 
ATOM   4193  C  CB  . THR B  1 202 ? 105.331 29.379  -9.908  1.00 10.38 ? 202  THR B CB  1 
ATOM   4194  O  OG1 . THR B  1 202 ? 105.860 29.258  -8.588  1.00 12.96 ? 202  THR B OG1 1 
ATOM   4195  C  CG2 . THR B  1 202 ? 104.506 30.697  -9.848  1.00 12.00 ? 202  THR B CG2 1 
ATOM   4196  N  N   . GLY B  1 203 ? 105.069 25.935  -9.462  1.00 9.31  ? 203  GLY B N   1 
ATOM   4197  C  CA  . GLY B  1 203 ? 105.984 24.803  -9.415  1.00 9.67  ? 203  GLY B CA  1 
ATOM   4198  C  C   . GLY B  1 203 ? 105.545 23.770  -8.395  1.00 10.22 ? 203  GLY B C   1 
ATOM   4199  O  O   . GLY B  1 203 ? 104.572 23.974  -7.654  1.00 9.35  ? 203  GLY B O   1 
ATOM   4200  N  N   . ALA B  1 204 ? 106.277 22.673  -8.330  1.00 10.25 ? 204  ALA B N   1 
ATOM   4201  C  CA  . ALA B  1 204 ? 105.863 21.544  -7.478  1.00 11.62 ? 204  ALA B CA  1 
ATOM   4202  C  C   . ALA B  1 204 ? 105.919 21.946  -5.997  1.00 11.39 ? 204  ALA B C   1 
ATOM   4203  O  O   . ALA B  1 204 ? 106.853 22.667  -5.580  1.00 11.96 ? 204  ALA B O   1 
ATOM   4204  C  CB  . ALA B  1 204 ? 106.794 20.338  -7.709  1.00 12.09 ? 204  ALA B CB  1 
ATOM   4205  N  N   . ASN B  1 205 ? 104.945 21.465  -5.219  1.00 10.99 ? 205  ASN B N   1 
ATOM   4206  C  CA  . ASN B  1 205 ? 105.018 21.603  -3.749  1.00 11.56 ? 205  ASN B CA  1 
ATOM   4207  C  C   . ASN B  1 205 ? 105.202 20.242  -3.112  1.00 12.36 ? 205  ASN B C   1 
ATOM   4208  O  O   . ASN B  1 205 ? 104.418 19.336  -3.380  1.00 13.40 ? 205  ASN B O   1 
ATOM   4209  C  CB  . ASN B  1 205 ? 103.756 22.221  -3.160  1.00 10.25 ? 205  ASN B CB  1 
ATOM   4210  C  CG  . ASN B  1 205 ? 103.478 23.631  -3.684  1.00 9.93  ? 205  ASN B CG  1 
ATOM   4211  O  OD1 . ASN B  1 205 ? 102.371 23.927  -4.115  1.00 10.70 ? 205  ASN B OD1 1 
ATOM   4212  N  ND2 . ASN B  1 205 ? 104.489 24.507  -3.668  1.00 4.11  ? 205  ASN B ND2 1 
ATOM   4213  N  N   . ALA B  1 206 ? 106.210 20.108  -2.274  1.00 10.36 ? 206  ALA B N   1 
ATOM   4214  C  CA  . ALA B  1 206 ? 106.377 18.906  -1.486  1.00 11.55 ? 206  ALA B CA  1 
ATOM   4215  C  C   . ALA B  1 206 ? 105.665 19.029  -0.107  1.00 12.52 ? 206  ALA B C   1 
ATOM   4216  O  O   . ALA B  1 206 ? 105.544 20.130  0.449   1.00 11.52 ? 206  ALA B O   1 
ATOM   4217  C  CB  . ALA B  1 206 ? 107.861 18.622  -1.293  1.00 11.21 ? 206  ALA B CB  1 
ATOM   4218  N  N   . LEU B  1 207 ? 105.204 17.901  0.428   1.00 12.50 ? 207  LEU B N   1 
ATOM   4219  C  CA  . LEU B  1 207 ? 104.842 17.808  1.859   1.00 14.13 ? 207  LEU B CA  1 
ATOM   4220  C  C   . LEU B  1 207 ? 106.105 18.071  2.723   1.00 13.83 ? 207  LEU B C   1 
ATOM   4221  O  O   . LEU B  1 207 ? 107.225 17.667  2.341   1.00 15.21 ? 207  LEU B O   1 
ATOM   4222  C  CB  . LEU B  1 207 ? 104.229 16.435  2.162   1.00 14.60 ? 207  LEU B CB  1 
ATOM   4223  C  CG  . LEU B  1 207 ? 102.711 16.324  1.858   1.00 16.51 ? 207  LEU B CG  1 
ATOM   4224  C  CD1 . LEU B  1 207 ? 102.445 16.417  0.381   1.00 18.92 ? 207  LEU B CD1 1 
ATOM   4225  C  CD2 . LEU B  1 207 ? 102.118 15.020  2.377   1.00 17.24 ? 207  LEU B CD2 1 
ATOM   4226  N  N   . ALA B  1 208 ? 105.962 18.756  3.859   1.00 13.19 ? 208  ALA B N   1 
ATOM   4227  C  CA  . ALA B  1 208 ? 107.113 18.969  4.741   1.00 13.42 ? 208  ALA B CA  1 
ATOM   4228  C  C   . ALA B  1 208 ? 107.656 17.642  5.233   1.00 14.45 ? 208  ALA B C   1 
ATOM   4229  O  O   . ALA B  1 208 ? 106.898 16.795  5.693   1.00 14.11 ? 208  ALA B O   1 
ATOM   4230  C  CB  . ALA B  1 208 ? 106.741 19.834  5.917   1.00 14.11 ? 208  ALA B CB  1 
ATOM   4231  N  N   . SER B  1 209 ? 108.967 17.449  5.184   1.00 14.86 ? 209  SER B N   1 
ATOM   4232  C  CA  . SER B  1 209 ? 109.473 16.209  5.751   1.00 17.35 ? 209  SER B CA  1 
ATOM   4233  C  C   . SER B  1 209 ? 109.789 16.355  7.204   1.00 18.24 ? 209  SER B C   1 
ATOM   4234  O  O   . SER B  1 209 ? 110.122 15.364  7.871   1.00 21.30 ? 209  SER B O   1 
ATOM   4235  C  CB  . SER B  1 209 ? 110.750 15.781  5.067   1.00 17.39 ? 209  SER B CB  1 
ATOM   4236  O  OG  . SER B  1 209 ? 111.681 16.855  5.141   1.00 17.14 ? 209  SER B OG  1 
ATOM   4237  N  N   . THR B  1 210 ? 109.768 17.578  7.702   1.00 17.53 ? 210  THR B N   1 
ATOM   4238  C  CA  . THR B  1 210 ? 110.037 17.819  9.117   1.00 17.37 ? 210  THR B CA  1 
ATOM   4239  C  C   . THR B  1 210 ? 108.708 17.975  9.834   1.00 16.76 ? 210  THR B C   1 
ATOM   4240  O  O   . THR B  1 210 ? 107.871 18.796  9.416   1.00 16.72 ? 210  THR B O   1 
ATOM   4241  C  CB  . THR B  1 210 ? 110.882 19.104  9.255   1.00 17.68 ? 210  THR B CB  1 
ATOM   4242  O  OG1 . THR B  1 210 ? 112.162 18.927  8.617   1.00 20.25 ? 210  THR B OG1 1 
ATOM   4243  C  CG2 . THR B  1 210 ? 111.209 19.415  10.740  1.00 17.70 ? 210  THR B CG2 1 
ATOM   4244  N  N   . ALA B  1 211 ? 108.494 17.227  10.916  1.00 15.90 ? 211  ALA B N   1 
ATOM   4245  C  CA  . ALA B  1 211 ? 107.229 17.325  11.621  1.00 14.59 ? 211  ALA B CA  1 
ATOM   4246  C  C   . ALA B  1 211 ? 107.216 18.670  12.353  1.00 13.21 ? 211  ALA B C   1 
ATOM   4247  O  O   . ALA B  1 211 ? 108.268 19.161  12.784  1.00 12.44 ? 211  ALA B O   1 
ATOM   4248  C  CB  . ALA B  1 211 ? 107.071 16.177  12.591  1.00 15.40 ? 211  ALA B CB  1 
ATOM   4249  N  N   . GLY B  1 212 ? 106.031 19.269  12.439  1.00 11.40 ? 212  GLY B N   1 
ATOM   4250  C  CA  . GLY B  1 212 ? 105.870 20.558  13.082  1.00 10.25 ? 212  GLY B CA  1 
ATOM   4251  C  C   . GLY B  1 212 ? 105.967 21.737  12.143  1.00 9.43  ? 212  GLY B C   1 
ATOM   4252  O  O   . GLY B  1 212 ? 105.629 22.854  12.559  1.00 10.12 ? 212  GLY B O   1 
ATOM   4253  N  N   . ASP B  1 213 ? 106.426 21.539  10.903  1.00 7.63  ? 213  ASP B N   1 
ATOM   4254  C  CA  . ASP B  1 213 ? 106.516 22.667  9.990   1.00 7.10  ? 213  ASP B CA  1 
ATOM   4255  C  C   . ASP B  1 213 ? 105.251 22.830  9.168   1.00 7.59  ? 213  ASP B C   1 
ATOM   4256  O  O   . ASP B  1 213 ? 104.725 21.852  8.655   1.00 7.28  ? 213  ASP B O   1 
ATOM   4257  C  CB  . ASP B  1 213 ? 107.667 22.482  9.017   1.00 7.39  ? 213  ASP B CB  1 
ATOM   4258  C  CG  . ASP B  1 213 ? 109.025 22.706  9.668   1.00 8.95  ? 213  ASP B CG  1 
ATOM   4259  O  OD1 . ASP B  1 213 ? 109.112 22.970  10.888  1.00 8.88  ? 213  ASP B OD1 1 
ATOM   4260  O  OD2 . ASP B  1 213 ? 110.063 22.658  9.001   1.00 11.78 ? 213  ASP B OD2 1 
ATOM   4261  N  N   . PRO B  1 214 ? 104.785 24.067  8.997   1.00 6.58  ? 214  PRO B N   1 
ATOM   4262  C  CA  . PRO B  1 214 ? 103.646 24.304  8.121   1.00 7.08  ? 214  PRO B CA  1 
ATOM   4263  C  C   . PRO B  1 214 ? 104.115 24.097  6.686   1.00 7.19  ? 214  PRO B C   1 
ATOM   4264  O  O   . PRO B  1 214 ? 105.340 24.238  6.387   1.00 6.39  ? 214  PRO B O   1 
ATOM   4265  C  CB  . PRO B  1 214 ? 103.335 25.776  8.382   1.00 7.94  ? 214  PRO B CB  1 
ATOM   4266  C  CG  . PRO B  1 214 ? 104.616 26.362  8.753   1.00 6.38  ? 214  PRO B CG  1 
ATOM   4267  C  CD  . PRO B  1 214 ? 105.323 25.316  9.574   1.00 7.44  ? 214  PRO B CD  1 
ATOM   4268  N  N   . TYR B  1 215 ? 103.182 23.761  5.808   1.00 6.98  ? 215  TYR B N   1 
ATOM   4269  C  CA  . TYR B  1 215 ? 103.478 23.654  4.374   1.00 7.51  ? 215  TYR B CA  1 
ATOM   4270  C  C   . TYR B  1 215 ? 102.185 23.827  3.576   1.00 8.35  ? 215  TYR B C   1 
ATOM   4271  O  O   . TYR B  1 215 ? 101.064 23.765  4.152   1.00 9.54  ? 215  TYR B O   1 
ATOM   4272  C  CB  . TYR B  1 215 ? 104.123 22.319  4.045   1.00 7.14  ? 215  TYR B CB  1 
ATOM   4273  C  CG  . TYR B  1 215 ? 103.300 21.105  4.460   1.00 8.45  ? 215  TYR B CG  1 
ATOM   4274  C  CD1 . TYR B  1 215 ? 103.358 20.610  5.786   1.00 9.69  ? 215  TYR B CD1 1 
ATOM   4275  C  CD2 . TYR B  1 215 ? 102.535 20.402  3.528   1.00 7.69  ? 215  TYR B CD2 1 
ATOM   4276  C  CE1 . TYR B  1 215 ? 102.631 19.471  6.151   1.00 10.32 ? 215  TYR B CE1 1 
ATOM   4277  C  CE2 . TYR B  1 215 ? 101.775 19.302  3.892   1.00 8.59  ? 215  TYR B CE2 1 
ATOM   4278  C  CZ  . TYR B  1 215 ? 101.843 18.811  5.212   1.00 11.38 ? 215  TYR B CZ  1 
ATOM   4279  O  OH  . TYR B  1 215 ? 101.095 17.673  5.588   1.00 6.82  ? 215  TYR B OH  1 
ATOM   4280  N  N   . PHE B  1 216 ? 102.330 24.147  2.289   1.00 6.74  ? 216  PHE B N   1 
ATOM   4281  C  CA  . PHE B  1 216 ? 101.184 24.530  1.513   1.00 6.65  ? 216  PHE B CA  1 
ATOM   4282  C  C   . PHE B  1 216 ? 101.241 23.775  0.182   1.00 7.57  ? 216  PHE B C   1 
ATOM   4283  O  O   . PHE B  1 216 ? 102.291 23.695  -0.432  1.00 7.19  ? 216  PHE B O   1 
ATOM   4284  C  CB  . PHE B  1 216 ? 101.130 26.036  1.279   1.00 6.46  ? 216  PHE B CB  1 
ATOM   4285  C  CG  . PHE B  1 216 ? 101.360 26.861  2.507   1.00 7.58  ? 216  PHE B CG  1 
ATOM   4286  C  CD1 . PHE B  1 216 ? 102.648 27.114  2.943   1.00 6.27  ? 216  PHE B CD1 1 
ATOM   4287  C  CD2 . PHE B  1 216 ? 100.271 27.452  3.207   1.00 6.92  ? 216  PHE B CD2 1 
ATOM   4288  C  CE1 . PHE B  1 216 ? 102.890 27.911  4.068   1.00 5.29  ? 216  PHE B CE1 1 
ATOM   4289  C  CE2 . PHE B  1 216 ? 100.521 28.259  4.365   1.00 8.17  ? 216  PHE B CE2 1 
ATOM   4290  C  CZ  . PHE B  1 216 ? 101.824 28.456  4.791   1.00 5.64  ? 216  PHE B CZ  1 
ATOM   4291  N  N   . ILE B  1 217 ? 100.111 23.203  -0.235  1.00 7.06  ? 217  ILE B N   1 
ATOM   4292  C  CA  . ILE B  1 217 ? 100.032 22.610  -1.565  1.00 8.03  ? 217  ILE B CA  1 
ATOM   4293  C  C   . ILE B  1 217 ? 98.998  23.312  -2.433  1.00 9.35  ? 217  ILE B C   1 
ATOM   4294  O  O   . ILE B  1 217 ? 97.779  23.270  -2.145  1.00 7.51  ? 217  ILE B O   1 
ATOM   4295  C  CB  . ILE B  1 217 ? 99.697  21.113  -1.425  1.00 8.33  ? 217  ILE B CB  1 
ATOM   4296  C  CG1 . ILE B  1 217 ? 100.740 20.508  -0.488  1.00 10.47 ? 217  ILE B CG1 1 
ATOM   4297  C  CG2 . ILE B  1 217 ? 99.689  20.404  -2.804  1.00 5.38  ? 217  ILE B CG2 1 
ATOM   4298  C  CD1 . ILE B  1 217 ? 100.355 19.101  -0.049  1.00 17.27 ? 217  ILE B CD1 1 
ATOM   4299  N  N   . ALA B  1 218 ? 99.484  23.893  -3.534  1.00 8.16  ? 218  ALA B N   1 
ATOM   4300  C  CA  . ALA B  1 218 ? 98.601  24.579  -4.465  1.00 7.57  ? 218  ALA B CA  1 
ATOM   4301  C  C   . ALA B  1 218 ? 97.913  23.531  -5.331  1.00 6.91  ? 218  ALA B C   1 
ATOM   4302  O  O   . ALA B  1 218 ? 98.529  22.507  -5.626  1.00 6.34  ? 218  ALA B O   1 
ATOM   4303  C  CB  . ALA B  1 218 ? 99.404  25.617  -5.348  1.00 6.44  ? 218  ALA B CB  1 
ATOM   4304  N  N   . ASN B  1 219 ? 96.648  23.782  -5.731  1.00 5.58  ? 219  ASN B N   1 
ATOM   4305  C  CA  . ASN B  1 219 ? 95.840  22.782  -6.466  1.00 7.48  ? 219  ASN B CA  1 
ATOM   4306  C  C   . ASN B  1 219 ? 96.578  22.173  -7.666  1.00 7.21  ? 219  ASN B C   1 
ATOM   4307  O  O   . ASN B  1 219 ? 96.901  22.888  -8.613  1.00 8.37  ? 219  ASN B O   1 
ATOM   4308  C  CB  . ASN B  1 219 ? 94.553  23.459  -6.987  1.00 8.66  ? 219  ASN B CB  1 
ATOM   4309  C  CG  . ASN B  1 219 ? 93.520  22.455  -7.481  1.00 8.63  ? 219  ASN B CG  1 
ATOM   4310  O  OD1 . ASN B  1 219 ? 93.616  21.273  -7.192  1.00 14.29 ? 219  ASN B OD1 1 
ATOM   4311  N  ND2 . ASN B  1 219 ? 92.546  22.919  -8.221  1.00 11.67 ? 219  ASN B ND2 1 
ATOM   4312  N  N   . GLY B  1 220 ? 96.875  20.871  -7.629  1.00 7.76  ? 220  GLY B N   1 
ATOM   4313  C  CA  . GLY B  1 220 ? 97.453  20.205  -8.795  1.00 7.09  ? 220  GLY B CA  1 
ATOM   4314  C  C   . GLY B  1 220 ? 98.954  20.053  -8.670  1.00 7.98  ? 220  GLY B C   1 
ATOM   4315  O  O   . GLY B  1 220 ? 99.589  19.328  -9.448  1.00 6.45  ? 220  GLY B O   1 
ATOM   4316  N  N   . TRP B  1 221 ? 99.549  20.728  -7.687  1.00 7.76  ? 221  TRP B N   1 
ATOM   4317  C  CA  . TRP B  1 221 ? 100.989 20.837  -7.688  1.00 7.41  ? 221  TRP B CA  1 
ATOM   4318  C  C   . TRP B  1 221 ? 101.726 19.898  -6.722  1.00 8.14  ? 221  TRP B C   1 
ATOM   4319  O  O   . TRP B  1 221 ? 102.983 19.914  -6.693  1.00 7.49  ? 221  TRP B O   1 
ATOM   4320  C  CB  . TRP B  1 221 ? 101.409 22.288  -7.371  1.00 7.77  ? 221  TRP B CB  1 
ATOM   4321  C  CG  . TRP B  1 221 ? 101.110 23.274  -8.503  1.00 7.83  ? 221  TRP B CG  1 
ATOM   4322  C  CD1 . TRP B  1 221 ? 100.051 24.146  -8.572  1.00 7.56  ? 221  TRP B CD1 1 
ATOM   4323  C  CD2 . TRP B  1 221 ? 101.896 23.513  -9.692  1.00 7.24  ? 221  TRP B CD2 1 
ATOM   4324  N  NE1 . TRP B  1 221 ? 100.139 24.909  -9.711  1.00 8.08  ? 221  TRP B NE1 1 
ATOM   4325  C  CE2 . TRP B  1 221 ? 101.250 24.536  -10.422 1.00 7.68  ? 221  TRP B CE2 1 
ATOM   4326  C  CE3 . TRP B  1 221 ? 103.070 22.949  -10.223 1.00 7.04  ? 221  TRP B CE3 1 
ATOM   4327  C  CZ2 . TRP B  1 221 ? 101.748 25.031  -11.644 1.00 9.31  ? 221  TRP B CZ2 1 
ATOM   4328  C  CZ3 . TRP B  1 221 ? 103.567 23.439  -11.461 1.00 9.09  ? 221  TRP B CZ3 1 
ATOM   4329  C  CH2 . TRP B  1 221 ? 102.905 24.478  -12.144 1.00 7.08  ? 221  TRP B CH2 1 
ATOM   4330  N  N   . GLY B  1 222 ? 100.976 19.135  -5.922  1.00 8.00  ? 222  GLY B N   1 
ATOM   4331  C  CA  . GLY B  1 222 ? 101.586 18.283  -4.906  1.00 8.32  ? 222  GLY B CA  1 
ATOM   4332  C  C   . GLY B  1 222 ? 101.943 16.948  -5.512  1.00 8.92  ? 222  GLY B C   1 
ATOM   4333  O  O   . GLY B  1 222 ? 101.715 16.726  -6.714  1.00 8.76  ? 222  GLY B O   1 
ATOM   4334  N  N   . PRO B  1 223 ? 102.493 16.047  -4.703  1.00 8.94  ? 223  PRO B N   1 
ATOM   4335  C  CA  . PRO B  1 223 ? 102.765 14.667  -5.147  1.00 9.41  ? 223  PRO B CA  1 
ATOM   4336  C  C   . PRO B  1 223 ? 101.456 13.919  -5.464  1.00 8.03  ? 223  PRO B C   1 
ATOM   4337  O  O   . PRO B  1 223 ? 100.462 14.194  -4.783  1.00 6.65  ? 223  PRO B O   1 
ATOM   4338  C  CB  . PRO B  1 223 ? 103.475 14.035  -3.946  1.00 9.76  ? 223  PRO B CB  1 
ATOM   4339  C  CG  . PRO B  1 223 ? 103.113 14.937  -2.794  1.00 10.84 ? 223  PRO B CG  1 
ATOM   4340  C  CD  . PRO B  1 223 ? 102.975 16.308  -3.344  1.00 9.27  ? 223  PRO B CD  1 
ATOM   4341  N  N   . LYS B  1 224 ? 101.463 13.037  -6.485  1.00 7.44  ? 224  LYS B N   1 
ATOM   4342  C  CA  . LYS B  1 224 ? 100.251 12.289  -6.863  1.00 8.07  ? 224  LYS B CA  1 
ATOM   4343  C  C   . LYS B  1 224 ? 100.596 10.844  -7.157  1.00 7.58  ? 224  LYS B C   1 
ATOM   4344  O  O   . LYS B  1 224 ? 101.765 10.528  -7.494  1.00 8.58  ? 224  LYS B O   1 
ATOM   4345  C  CB  . LYS B  1 224 ? 99.544  12.930  -8.129  1.00 8.54  ? 224  LYS B CB  1 
ATOM   4346  C  CG  . LYS B  1 224 ? 99.171  14.383  -7.920  1.00 7.26  ? 224  LYS B CG  1 
ATOM   4347  C  CD  . LYS B  1 224 ? 98.803  15.139  -9.275  1.00 5.22  ? 224  LYS B CD  1 
ATOM   4348  C  CE  . LYS B  1 224 ? 100.017 15.529  -9.998  1.00 6.19  ? 224  LYS B CE  1 
ATOM   4349  N  NZ  . LYS B  1 224 ? 100.635 16.724  -9.312  1.00 6.61  ? 224  LYS B NZ  1 
ATOM   4350  N  N   . TYR B  1 225 ? 99.625  9.967   -6.941  1.00 7.56  ? 225  TYR B N   1 
ATOM   4351  C  CA  . TYR B  1 225 ? 99.810  8.554   -7.170  1.00 7.87  ? 225  TYR B CA  1 
ATOM   4352  C  C   . TYR B  1 225 ? 98.599  8.078   -7.947  1.00 8.07  ? 225  TYR B C   1 
ATOM   4353  O  O   . TYR B  1 225 ? 97.458  8.393   -7.598  1.00 7.14  ? 225  TYR B O   1 
ATOM   4354  C  CB  . TYR B  1 225 ? 99.938  7.746   -5.868  1.00 9.76  ? 225  TYR B CB  1 
ATOM   4355  C  CG  . TYR B  1 225 ? 101.049 8.260   -5.035  1.00 13.23 ? 225  TYR B CG  1 
ATOM   4356  C  CD1 . TYR B  1 225 ? 100.908 9.491   -4.401  1.00 20.16 ? 225  TYR B CD1 1 
ATOM   4357  C  CD2 . TYR B  1 225 ? 102.257 7.608   -4.942  1.00 20.96 ? 225  TYR B CD2 1 
ATOM   4358  C  CE1 . TYR B  1 225 ? 101.918 10.033  -3.661  1.00 24.60 ? 225  TYR B CE1 1 
ATOM   4359  C  CE2 . TYR B  1 225 ? 103.296 8.144   -4.160  1.00 21.33 ? 225  TYR B CE2 1 
ATOM   4360  C  CZ  . TYR B  1 225 ? 103.104 9.370   -3.547  1.00 21.79 ? 225  TYR B CZ  1 
ATOM   4361  O  OH  . TYR B  1 225 ? 104.088 9.985   -2.766  1.00 27.52 ? 225  TYR B OH  1 
ATOM   4362  N  N   . LEU B  1 226 ? 98.885  7.335   -9.022  1.00 6.88  ? 226  LEU B N   1 
ATOM   4363  C  CA  . LEU B  1 226 ? 97.829  6.715   -9.822  1.00 5.48  ? 226  LEU B CA  1 
ATOM   4364  C  C   . LEU B  1 226 ? 97.587  5.272   -9.361  1.00 5.20  ? 226  LEU B C   1 
ATOM   4365  O  O   . LEU B  1 226 ? 98.486  4.451   -9.336  1.00 7.10  ? 226  LEU B O   1 
ATOM   4366  C  CB  . LEU B  1 226 ? 98.205  6.723   -11.303 1.00 5.21  ? 226  LEU B CB  1 
ATOM   4367  C  CG  . LEU B  1 226 ? 97.127  6.132   -12.260 1.00 6.22  ? 226  LEU B CG  1 
ATOM   4368  C  CD1 . LEU B  1 226 ? 95.791  6.947   -12.388 1.00 6.08  ? 226  LEU B CD1 1 
ATOM   4369  C  CD2 . LEU B  1 226 ? 97.807  5.910   -13.641 1.00 9.06  ? 226  LEU B CD2 1 
ATOM   4370  N  N   . ASN B  1 227 ? 96.361  4.972   -8.999  1.00 5.81  ? 227  ASN B N   1 
ATOM   4371  C  CA  . ASN B  1 227 ? 95.990  3.623   -8.683  1.00 5.20  ? 227  ASN B CA  1 
ATOM   4372  C  C   . ASN B  1 227 ? 95.080  3.140   -9.804  1.00 6.54  ? 227  ASN B C   1 
ATOM   4373  O  O   . ASN B  1 227 ? 94.163  3.868   -10.251 1.00 6.48  ? 227  ASN B O   1 
ATOM   4374  C  CB  . ASN B  1 227 ? 95.247  3.615   -7.357  1.00 5.80  ? 227  ASN B CB  1 
ATOM   4375  C  CG  . ASN B  1 227 ? 94.882  2.221   -6.915  1.00 6.46  ? 227  ASN B CG  1 
ATOM   4376  O  OD1 . ASN B  1 227 ? 93.988  1.588   -7.485  1.00 8.20  ? 227  ASN B OD1 1 
ATOM   4377  N  ND2 . ASN B  1 227 ? 95.620  1.706   -5.950  1.00 7.69  ? 227  ASN B ND2 1 
ATOM   4378  N  N   . SER B  1 228 ? 95.372  1.950   -10.324 1.00 6.27  ? 228  SER B N   1 
ATOM   4379  C  CA  . SER B  1 228 ? 94.641  1.455   -11.488 1.00 7.75  ? 228  SER B CA  1 
ATOM   4380  C  C   . SER B  1 228 ? 93.882  0.191   -11.132 1.00 8.28  ? 228  SER B C   1 
ATOM   4381  O  O   . SER B  1 228 ? 93.448  -0.523  -12.061 1.00 8.35  ? 228  SER B O   1 
ATOM   4382  C  CB  . SER B  1 228 ? 95.656  1.100   -12.597 1.00 8.76  ? 228  SER B CB  1 
ATOM   4383  O  OG  . SER B  1 228 ? 96.436  2.267   -12.857 1.00 14.10 ? 228  SER B OG  1 
ATOM   4384  N  N   . GLN B  1 229 ? 93.689  -0.095  -9.839  1.00 8.30  ? 229  GLN B N   1 
ATOM   4385  C  CA  . GLN B  1 229 ? 93.105  -1.401  -9.470  1.00 8.41  ? 229  GLN B CA  1 
ATOM   4386  C  C   . GLN B  1 229 ? 91.599  -1.485  -9.723  1.00 9.79  ? 229  GLN B C   1 
ATOM   4387  O  O   . GLN B  1 229 ? 91.071  -2.570  -9.963  1.00 10.41 ? 229  GLN B O   1 
ATOM   4388  C  CB  . GLN B  1 229 ? 93.412  -1.797  -8.008  1.00 8.69  ? 229  GLN B CB  1 
ATOM   4389  C  CG  . GLN B  1 229 ? 94.905  -1.957  -7.668  1.00 11.87 ? 229  GLN B CG  1 
ATOM   4390  C  CD  . GLN B  1 229 ? 95.199  -2.133  -6.137  1.00 16.41 ? 229  GLN B CD  1 
ATOM   4391  O  OE1 . GLN B  1 229 ? 95.063  -1.177  -5.311  1.00 15.19 ? 229  GLN B OE1 1 
ATOM   4392  N  NE2 . GLN B  1 229 ? 95.635  -3.343  -5.775  1.00 19.19 ? 229  GLN B NE2 1 
ATOM   4393  N  N   . TYR B  1 230 ? 90.898  -0.355  -9.614  1.00 8.61  ? 230  TYR B N   1 
ATOM   4394  C  CA  . TYR B  1 230 ? 89.439  -0.369  -9.690  1.00 8.91  ? 230  TYR B CA  1 
ATOM   4395  C  C   . TYR B  1 230 ? 89.036  0.803   -10.549 1.00 7.75  ? 230  TYR B C   1 
ATOM   4396  O  O   . TYR B  1 230 ? 88.480  1.767   -10.035 1.00 10.24 ? 230  TYR B O   1 
ATOM   4397  C  CB  . TYR B  1 230 ? 88.825  -0.234  -8.283  1.00 9.06  ? 230  TYR B CB  1 
ATOM   4398  C  CG  . TYR B  1 230 ? 89.308  -1.271  -7.338  1.00 11.61 ? 230  TYR B CG  1 
ATOM   4399  C  CD1 . TYR B  1 230 ? 88.887  -2.594  -7.473  1.00 11.51 ? 230  TYR B CD1 1 
ATOM   4400  C  CD2 . TYR B  1 230 ? 90.241  -0.958  -6.335  1.00 12.38 ? 230  TYR B CD2 1 
ATOM   4401  C  CE1 . TYR B  1 230 ? 89.355  -3.583  -6.645  1.00 14.14 ? 230  TYR B CE1 1 
ATOM   4402  C  CE2 . TYR B  1 230 ? 90.726  -1.955  -5.479  1.00 11.77 ? 230  TYR B CE2 1 
ATOM   4403  C  CZ  . TYR B  1 230 ? 90.265  -3.247  -5.631  1.00 16.81 ? 230  TYR B CZ  1 
ATOM   4404  O  OH  . TYR B  1 230 ? 90.724  -4.249  -4.815  1.00 20.63 ? 230  TYR B OH  1 
ATOM   4405  N  N   . GLY B  1 231 ? 89.364  0.765   -11.833 1.00 6.28  ? 231  GLY B N   1 
ATOM   4406  C  CA  . GLY B  1 231 ? 89.326  1.995   -12.624 1.00 6.14  ? 231  GLY B CA  1 
ATOM   4407  C  C   . GLY B  1 231 ? 90.503  2.858   -12.248 1.00 7.45  ? 231  GLY B C   1 
ATOM   4408  O  O   . GLY B  1 231 ? 91.466  2.374   -11.600 1.00 7.52  ? 231  GLY B O   1 
ATOM   4409  N  N   . TYR B  1 232 ? 90.479  4.122   -12.657 1.00 6.44  ? 232  TYR B N   1 
ATOM   4410  C  CA  . TYR B  1 232 ? 91.594  4.986   -12.288 1.00 7.36  ? 232  TYR B CA  1 
ATOM   4411  C  C   . TYR B  1 232 ? 91.301  5.960   -11.149 1.00 7.68  ? 232  TYR B C   1 
ATOM   4412  O  O   . TYR B  1 232 ? 90.287  6.677   -11.142 1.00 7.70  ? 232  TYR B O   1 
ATOM   4413  C  CB  . TYR B  1 232 ? 92.065  5.802   -13.480 1.00 6.94  ? 232  TYR B CB  1 
ATOM   4414  C  CG  . TYR B  1 232 ? 92.772  5.047   -14.574 1.00 8.47  ? 232  TYR B CG  1 
ATOM   4415  C  CD1 . TYR B  1 232 ? 93.926  4.280   -14.329 1.00 6.30  ? 232  TYR B CD1 1 
ATOM   4416  C  CD2 . TYR B  1 232 ? 92.325  5.146   -15.895 1.00 7.01  ? 232  TYR B CD2 1 
ATOM   4417  C  CE1 . TYR B  1 232 ? 94.595  3.632   -15.379 1.00 4.68  ? 232  TYR B CE1 1 
ATOM   4418  C  CE2 . TYR B  1 232 ? 92.979  4.492   -16.930 1.00 8.18  ? 232  TYR B CE2 1 
ATOM   4419  C  CZ  . TYR B  1 232 ? 94.118  3.724   -16.663 1.00 8.34  ? 232  TYR B CZ  1 
ATOM   4420  O  OH  . TYR B  1 232 ? 94.792  3.116   -17.710 1.00 6.66  ? 232  TYR B OH  1 
ATOM   4421  N  N   . GLN B  1 233 ? 92.227  6.021   -10.200 1.00 7.09  ? 233  GLN B N   1 
ATOM   4422  C  CA  . GLN B  1 233 ? 92.059  6.911   -9.068  1.00 6.78  ? 233  GLN B CA  1 
ATOM   4423  C  C   . GLN B  1 233 ? 93.390  7.598   -8.809  1.00 7.49  ? 233  GLN B C   1 
ATOM   4424  O  O   . GLN B  1 233 ? 94.448  6.966   -8.842  1.00 8.95  ? 233  GLN B O   1 
ATOM   4425  C  CB  . GLN B  1 233 ? 91.576  6.143   -7.831  1.00 6.66  ? 233  GLN B CB  1 
ATOM   4426  C  CG  . GLN B  1 233 ? 90.065  5.659   -8.006  1.00 4.93  ? 233  GLN B CG  1 
ATOM   4427  C  CD  . GLN B  1 233 ? 89.627  4.909   -6.794  1.00 11.01 ? 233  GLN B CD  1 
ATOM   4428  O  OE1 . GLN B  1 233 ? 89.649  3.650   -6.734  1.00 14.50 ? 233  GLN B OE1 1 
ATOM   4429  N  NE2 . GLN B  1 233 ? 89.201  5.640   -5.841  1.00 5.13  ? 233  GLN B NE2 1 
ATOM   4430  N  N   . ILE B  1 234 ? 93.336  8.891   -8.613  1.00 7.13  ? 234  ILE B N   1 
ATOM   4431  C  CA  . ILE B  1 234 ? 94.573  9.628   -8.374  1.00 7.19  ? 234  ILE B CA  1 
ATOM   4432  C  C   . ILE B  1 234 ? 94.470  10.199  -6.983  1.00 8.05  ? 234  ILE B C   1 
ATOM   4433  O  O   . ILE B  1 234 ? 93.613  11.050  -6.715  1.00 9.36  ? 234  ILE B O   1 
ATOM   4434  C  CB  . ILE B  1 234 ? 94.776  10.764  -9.377  1.00 6.68  ? 234  ILE B CB  1 
ATOM   4435  C  CG1 . ILE B  1 234 ? 94.818  10.225  -10.843 1.00 7.97  ? 234  ILE B CG1 1 
ATOM   4436  C  CG2 . ILE B  1 234 ? 96.052  11.579  -9.002  1.00 8.73  ? 234  ILE B CG2 1 
ATOM   4437  C  CD1 . ILE B  1 234 ? 94.855  11.373  -11.888 1.00 6.96  ? 234  ILE B CD1 1 
ATOM   4438  N  N   . VAL B  1 235 ? 95.359  9.728   -6.101  1.00 8.63  ? 235  VAL B N   1 
ATOM   4439  C  CA  . VAL B  1 235 ? 95.484  10.298  -4.754  1.00 8.46  ? 235  VAL B CA  1 
ATOM   4440  C  C   . VAL B  1 235 ? 96.529  11.440  -4.700  1.00 9.17  ? 235  VAL B C   1 
ATOM   4441  O  O   . VAL B  1 235 ? 97.646  11.256  -5.171  1.00 8.65  ? 235  VAL B O   1 
ATOM   4442  C  CB  . VAL B  1 235 ? 95.901  9.256   -3.718  1.00 8.12  ? 235  VAL B CB  1 
ATOM   4443  C  CG1 . VAL B  1 235 ? 95.910  9.902   -2.344  1.00 8.38  ? 235  VAL B CG1 1 
ATOM   4444  C  CG2 . VAL B  1 235 ? 94.979  7.998   -3.767  1.00 8.62  ? 235  VAL B CG2 1 
ATOM   4445  N  N   . ALA B  1 236 ? 96.131  12.622  -4.196  1.00 9.41  ? 236  ALA B N   1 
ATOM   4446  C  CA  . ALA B  1 236 ? 97.078  13.682  -3.920  1.00 10.73 ? 236  ALA B CA  1 
ATOM   4447  C  C   . ALA B  1 236 ? 97.188  13.814  -2.379  1.00 10.18 ? 236  ALA B C   1 
ATOM   4448  O  O   . ALA B  1 236 ? 96.349  14.480  -1.788  1.00 9.14  ? 236  ALA B O   1 
ATOM   4449  C  CB  . ALA B  1 236 ? 96.570  15.030  -4.518  1.00 10.31 ? 236  ALA B CB  1 
ATOM   4450  N  N   . PRO B  1 237 ? 98.210  13.224  -1.754  1.00 8.82  ? 237  PRO B N   1 
ATOM   4451  C  CA  . PRO B  1 237 ? 98.366  13.322  -0.290  1.00 9.85  ? 237  PRO B CA  1 
ATOM   4452  C  C   . PRO B  1 237 ? 98.558  14.749  0.182   1.00 9.55  ? 237  PRO B C   1 
ATOM   4453  O  O   . PRO B  1 237 ? 99.243  15.486  -0.510  1.00 10.39 ? 237  PRO B O   1 
ATOM   4454  C  CB  . PRO B  1 237 ? 99.634  12.548  -0.015  1.00 7.48  ? 237  PRO B CB  1 
ATOM   4455  C  CG  . PRO B  1 237 ? 99.618  11.500  -1.134  1.00 10.48 ? 237  PRO B CG  1 
ATOM   4456  C  CD  . PRO B  1 237 ? 99.230  12.369  -2.371  1.00 8.84  ? 237  PRO B CD  1 
ATOM   4457  N  N   . PHE B  1 238 ? 97.917  15.110  1.293   1.00 9.12  ? 238  PHE B N   1 
ATOM   4458  C  CA  . PHE B  1 238 ? 98.119  16.417  1.947   1.00 9.41  ? 238  PHE B CA  1 
ATOM   4459  C  C   . PHE B  1 238 ? 98.793  16.124  3.292   1.00 8.05  ? 238  PHE B C   1 
ATOM   4460  O  O   . PHE B  1 238 ? 99.689  16.871  3.731   1.00 8.69  ? 238  PHE B O   1 
ATOM   4461  C  CB  . PHE B  1 238 ? 96.768  17.149  2.195   1.00 8.78  ? 238  PHE B CB  1 
ATOM   4462  C  CG  . PHE B  1 238 ? 96.086  17.674  0.950   1.00 12.06 ? 238  PHE B CG  1 
ATOM   4463  C  CD1 . PHE B  1 238 ? 96.804  17.888  -0.238  1.00 12.70 ? 238  PHE B CD1 1 
ATOM   4464  C  CD2 . PHE B  1 238 ? 94.711  18.015  0.998   1.00 12.16 ? 238  PHE B CD2 1 
ATOM   4465  C  CE1 . PHE B  1 238 ? 96.190  18.387  -1.373  1.00 11.65 ? 238  PHE B CE1 1 
ATOM   4466  C  CE2 . PHE B  1 238 ? 94.048  18.547  -0.145  1.00 10.73 ? 238  PHE B CE2 1 
ATOM   4467  C  CZ  . PHE B  1 238 ? 94.805  18.720  -1.352  1.00 12.48 ? 238  PHE B CZ  1 
ATOM   4468  N  N   . VAL B  1 239 ? 98.299  15.087  3.985   1.00 7.29  ? 239  VAL B N   1 
ATOM   4469  C  CA  . VAL B  1 239 ? 98.924  14.620  5.252   1.00 7.97  ? 239  VAL B CA  1 
ATOM   4470  C  C   . VAL B  1 239 ? 99.167  13.124  5.227   1.00 8.35  ? 239  VAL B C   1 
ATOM   4471  O  O   . VAL B  1 239 ? 98.283  12.368  4.828   1.00 7.85  ? 239  VAL B O   1 
ATOM   4472  C  CB  . VAL B  1 239 ? 98.064  14.930  6.493   1.00 8.45  ? 239  VAL B CB  1 
ATOM   4473  C  CG1 . VAL B  1 239 ? 98.740  14.419  7.792   1.00 4.55  ? 239  VAL B CG1 1 
ATOM   4474  C  CG2 . VAL B  1 239 ? 97.778  16.441  6.595   1.00 7.16  ? 239  VAL B CG2 1 
ATOM   4475  N  N   . THR B  1 240 ? 100.384 12.724  5.613   1.00 8.40  ? 240  THR B N   1 
ATOM   4476  C  CA  . THR B  1 240 ? 100.784 11.343  5.728   1.00 8.71  ? 240  THR B CA  1 
ATOM   4477  C  C   . THR B  1 240 ? 101.299 11.149  7.135   1.00 9.15  ? 240  THR B C   1 
ATOM   4478  O  O   . THR B  1 240 ? 101.396 12.108  7.894   1.00 8.43  ? 240  THR B O   1 
ATOM   4479  C  CB  . THR B  1 240 ? 101.922 10.953  4.719   1.00 8.81  ? 240  THR B CB  1 
ATOM   4480  O  OG1 . THR B  1 240 ? 103.154 11.653  5.038   1.00 11.30 ? 240  THR B OG1 1 
ATOM   4481  C  CG2 . THR B  1 240 ? 101.562 11.444  3.334   1.00 7.86  ? 240  THR B CG2 1 
ATOM   4482  N  N   . ALA B  1 241 ? 101.658 9.900   7.468   1.00 10.20 ? 241  ALA B N   1 
ATOM   4483  C  CA  . ALA B  1 241 ? 102.284 9.593   8.769   1.00 10.11 ? 241  ALA B CA  1 
ATOM   4484  C  C   . ALA B  1 241 ? 103.498 10.470  9.099   1.00 10.40 ? 241  ALA B C   1 
ATOM   4485  O  O   . ALA B  1 241 ? 103.670 10.901  10.246  1.00 8.65  ? 241  ALA B O   1 
ATOM   4486  C  CB  . ALA B  1 241 ? 102.630 8.065   8.909   1.00 10.23 ? 241  ALA B CB  1 
ATOM   4487  N  N   . THR B  1 242 ? 104.309 10.792  8.096   1.00 10.15 ? 242  THR B N   1 
ATOM   4488  C  CA  . THR B  1 242 ? 105.438 11.681  8.346   1.00 10.56 ? 242  THR B CA  1 
ATOM   4489  C  C   . THR B  1 242 ? 104.990 12.952  9.076   1.00 9.64  ? 242  THR B C   1 
ATOM   4490  O  O   . THR B  1 242 ? 105.656 13.388  10.027  1.00 9.01  ? 242  THR B O   1 
ATOM   4491  C  CB  . THR B  1 242 ? 106.149 12.080  7.053   1.00 10.75 ? 242  THR B CB  1 
ATOM   4492  O  OG1 . THR B  1 242 ? 106.797 10.938  6.494   1.00 16.94 ? 242  THR B OG1 1 
ATOM   4493  C  CG2 . THR B  1 242 ? 107.364 13.060  7.347   1.00 9.66  ? 242  THR B CG2 1 
ATOM   4494  N  N   . GLN B  1 243 ? 103.880 13.557  8.612   1.00 8.61  ? 243  GLN B N   1 
ATOM   4495  C  CA  . GLN B  1 243 ? 103.469 14.851  9.167   1.00 8.83  ? 243  GLN B CA  1 
ATOM   4496  C  C   . GLN B  1 243 ? 102.543 14.672  10.392  1.00 8.50  ? 243  GLN B C   1 
ATOM   4497  O  O   . GLN B  1 243 ? 102.630 15.411  11.372  1.00 8.76  ? 243  GLN B O   1 
ATOM   4498  C  CB  . GLN B  1 243 ? 102.773 15.681  8.076   1.00 8.69  ? 243  GLN B CB  1 
ATOM   4499  C  CG  . GLN B  1 243 ? 103.722 16.047  6.913   1.00 8.71  ? 243  GLN B CG  1 
ATOM   4500  C  CD  . GLN B  1 243 ? 103.854 14.927  5.869   1.00 12.63 ? 243  GLN B CD  1 
ATOM   4501  O  OE1 . GLN B  1 243 ? 102.934 14.113  5.683   1.00 12.33 ? 243  GLN B OE1 1 
ATOM   4502  N  NE2 . GLN B  1 243 ? 105.008 14.863  5.226   1.00 8.41  ? 243  GLN B NE2 1 
ATOM   4503  N  N   . ALA B  1 244 ? 101.653 13.685  10.332  1.00 8.90  ? 244  ALA B N   1 
ATOM   4504  C  CA  . ALA B  1 244 ? 100.640 13.530  11.379  1.00 8.89  ? 244  ALA B CA  1 
ATOM   4505  C  C   . ALA B  1 244 ? 101.253 13.044  12.684  1.00 8.29  ? 244  ALA B C   1 
ATOM   4506  O  O   . ALA B  1 244 ? 100.763 13.377  13.731  1.00 6.82  ? 244  ALA B O   1 
ATOM   4507  C  CB  . ALA B  1 244 ? 99.522  12.550  10.918  1.00 9.60  ? 244  ALA B CB  1 
ATOM   4508  N  N   . GLN B  1 245 ? 102.311 12.228  12.589  1.00 8.86  ? 245  GLN B N   1 
ATOM   4509  C  CA  . GLN B  1 245 ? 102.906 11.503  13.722  1.00 9.01  ? 245  GLN B CA  1 
ATOM   4510  C  C   . GLN B  1 245 ? 101.802 10.872  14.612  1.00 8.72  ? 245  GLN B C   1 
ATOM   4511  O  O   . GLN B  1 245 ? 100.897 10.178  14.099  1.00 8.42  ? 245  GLN B O   1 
ATOM   4512  C  CB  . GLN B  1 245 ? 103.887 12.367  14.535  1.00 8.79  ? 245  GLN B CB  1 
ATOM   4513  C  CG  . GLN B  1 245 ? 104.878 13.263  13.783  1.00 12.93 ? 245  GLN B CG  1 
ATOM   4514  C  CD  . GLN B  1 245 ? 105.536 14.309  14.753  1.00 19.98 ? 245  GLN B CD  1 
ATOM   4515  O  OE1 . GLN B  1 245 ? 104.916 15.349  15.136  1.00 20.32 ? 245  GLN B OE1 1 
ATOM   4516  N  NE2 . GLN B  1 245 ? 106.754 14.001  15.200  1.00 20.91 ? 245  GLN B NE2 1 
ATOM   4517  N  N   . ASP B  1 246 ? 101.836 11.172  15.901  1.00 7.70  ? 246  ASP B N   1 
ATOM   4518  C  CA  . ASP B  1 246 ? 100.855 10.661  16.830  1.00 8.06  ? 246  ASP B CA  1 
ATOM   4519  C  C   . ASP B  1 246 ? 99.407  11.121  16.623  1.00 7.87  ? 246  ASP B C   1 
ATOM   4520  O  O   . ASP B  1 246 ? 98.514  10.468  17.155  1.00 8.53  ? 246  ASP B O   1 
ATOM   4521  C  CB  . ASP B  1 246 ? 101.307 10.909  18.272  1.00 8.13  ? 246  ASP B CB  1 
ATOM   4522  C  CG  . ASP B  1 246 ? 101.522 12.379  18.566  1.00 9.90  ? 246  ASP B CG  1 
ATOM   4523  O  OD1 . ASP B  1 246 ? 102.455 12.958  17.968  1.00 9.53  ? 246  ASP B OD1 1 
ATOM   4524  O  OD2 . ASP B  1 246 ? 100.793 13.029  19.356  1.00 6.60  ? 246  ASP B OD2 1 
ATOM   4525  N  N   . THR B  1 247 ? 99.151  12.239  15.919  1.00 7.74  ? 247  THR B N   1 
ATOM   4526  C  CA  . THR B  1 247 ? 97.762  12.586  15.590  1.00 8.25  ? 247  THR B CA  1 
ATOM   4527  C  C   . THR B  1 247 ? 97.061  11.556  14.701  1.00 8.75  ? 247  THR B C   1 
ATOM   4528  O  O   . THR B  1 247 ? 95.831  11.543  14.674  1.00 9.17  ? 247  THR B O   1 
ATOM   4529  C  CB  . THR B  1 247 ? 97.581  14.031  15.026  1.00 8.91  ? 247  THR B CB  1 
ATOM   4530  O  OG1 . THR B  1 247 ? 98.265  14.178  13.768  1.00 5.96  ? 247  THR B OG1 1 
ATOM   4531  C  CG2 . THR B  1 247 ? 98.223  15.061  15.968  1.00 10.49 ? 247  THR B CG2 1 
ATOM   4532  N  N   . ASN B  1 248 ? 97.835  10.693  14.025  1.00 8.61  ? 248  ASN B N   1 
ATOM   4533  C  CA  . ASN B  1 248 ? 97.370  9.369   13.564  1.00 9.50  ? 248  ASN B CA  1 
ATOM   4534  C  C   . ASN B  1 248 ? 96.188  9.461   12.612  1.00 9.70  ? 248  ASN B C   1 
ATOM   4535  O  O   . ASN B  1 248 ? 95.102  8.916   12.869  1.00 9.03  ? 248  ASN B O   1 
ATOM   4536  C  CB  . ASN B  1 248 ? 97.056  8.497   14.780  1.00 10.32 ? 248  ASN B CB  1 
ATOM   4537  C  CG  . ASN B  1 248 ? 96.686  7.044   14.434  1.00 9.65  ? 248  ASN B CG  1 
ATOM   4538  O  OD1 . ASN B  1 248 ? 97.138  6.472   13.411  1.00 10.66 ? 248  ASN B OD1 1 
ATOM   4539  N  ND2 . ASN B  1 248 ? 95.828  6.462   15.297  1.00 10.72 ? 248  ASN B ND2 1 
ATOM   4540  N  N   . TYR B  1 249 ? 96.422  10.187  11.512  1.00 8.96  ? 249  TYR B N   1 
ATOM   4541  C  CA  . TYR B  1 249 ? 95.456  10.323  10.452  1.00 8.10  ? 249  TYR B CA  1 
ATOM   4542  C  C   . TYR B  1 249 ? 96.125  10.605  9.111   1.00 7.36  ? 249  TYR B C   1 
ATOM   4543  O  O   . TYR B  1 249 ? 97.335  10.933  9.069   1.00 7.61  ? 249  TYR B O   1 
ATOM   4544  C  CB  . TYR B  1 249 ? 94.499  11.474  10.778  1.00 7.19  ? 249  TYR B CB  1 
ATOM   4545  C  CG  . TYR B  1 249 ? 95.048  12.846  10.521  1.00 8.51  ? 249  TYR B CG  1 
ATOM   4546  C  CD1 . TYR B  1 249 ? 95.912  13.459  11.437  1.00 9.90  ? 249  TYR B CD1 1 
ATOM   4547  C  CD2 . TYR B  1 249 ? 94.666  13.574  9.385   1.00 5.95  ? 249  TYR B CD2 1 
ATOM   4548  C  CE1 . TYR B  1 249 ? 96.381  14.754  11.218  1.00 7.26  ? 249  TYR B CE1 1 
ATOM   4549  C  CE2 . TYR B  1 249 ? 95.141  14.899  9.173   1.00 6.31  ? 249  TYR B CE2 1 
ATOM   4550  C  CZ  . TYR B  1 249 ? 95.971  15.471  10.106  1.00 6.57  ? 249  TYR B CZ  1 
ATOM   4551  O  OH  . TYR B  1 249 ? 96.482  16.749  9.932   1.00 7.76  ? 249  TYR B OH  1 
ATOM   4552  N  N   . THR B  1 250 ? 95.333  10.513  8.036   1.00 8.10  ? 250  THR B N   1 
ATOM   4553  C  CA  . THR B  1 250 ? 95.765  10.951  6.715   1.00 7.80  ? 250  THR B CA  1 
ATOM   4554  C  C   . THR B  1 250 ? 94.724  11.866  6.100   1.00 9.60  ? 250  THR B C   1 
ATOM   4555  O  O   . THR B  1 250 ? 93.539  11.818  6.466   1.00 9.39  ? 250  THR B O   1 
ATOM   4556  C  CB  . THR B  1 250 ? 95.997  9.786   5.774   1.00 10.06 ? 250  THR B CB  1 
ATOM   4557  O  OG1 . THR B  1 250 ? 94.807  8.966   5.746   1.00 11.19 ? 250  THR B OG1 1 
ATOM   4558  C  CG2 . THR B  1 250 ? 97.123  8.878   6.285   1.00 6.32  ? 250  THR B CG2 1 
ATOM   4559  N  N   . LEU B  1 251 ? 95.181  12.701  5.151   1.00 8.35  ? 251  LEU B N   1 
ATOM   4560  C  CA  . LEU B  1 251 ? 94.316  13.650  4.493   1.00 9.23  ? 251  LEU B CA  1 
ATOM   4561  C  C   . LEU B  1 251 ? 94.815  13.745  3.051   1.00 8.57  ? 251  LEU B C   1 
ATOM   4562  O  O   . LEU B  1 251 ? 96.017  13.753  2.833   1.00 7.65  ? 251  LEU B O   1 
ATOM   4563  C  CB  . LEU B  1 251 ? 94.411  14.988  5.201   1.00 7.70  ? 251  LEU B CB  1 
ATOM   4564  C  CG  . LEU B  1 251 ? 93.578  16.117  4.614   1.00 8.80  ? 251  LEU B CG  1 
ATOM   4565  C  CD1 . LEU B  1 251 ? 91.980  15.894  4.824   1.00 5.96  ? 251  LEU B CD1 1 
ATOM   4566  C  CD2 . LEU B  1 251 ? 94.019  17.462  5.162   1.00 9.91  ? 251  LEU B CD2 1 
ATOM   4567  N  N   . SER B  1 252 ? 93.898  13.785  2.073   1.00 8.51  ? 252  SER B N   1 
ATOM   4568  C  CA  . SER B  1 252 ? 94.318  13.803  0.661   1.00 9.19  ? 252  SER B CA  1 
ATOM   4569  C  C   . SER B  1 252 ? 93.110  14.241  -0.161  1.00 9.55  ? 252  SER B C   1 
ATOM   4570  O  O   . SER B  1 252 ? 92.020  14.376  0.405   1.00 11.15 ? 252  SER B O   1 
ATOM   4571  C  CB  . SER B  1 252 ? 94.731  12.386  0.245   1.00 9.28  ? 252  SER B CB  1 
ATOM   4572  O  OG  . SER B  1 252 ? 93.581  11.556  0.349   1.00 11.27 ? 252  SER B OG  1 
ATOM   4573  N  N   . THR B  1 253 ? 93.299  14.501  -1.467  1.00 8.64  ? 253  THR B N   1 
ATOM   4574  C  CA  . THR B  1 253 ? 92.171  14.345  -2.386  1.00 9.00  ? 253  THR B CA  1 
ATOM   4575  C  C   . THR B  1 253 ? 92.277  13.012  -3.169  1.00 7.93  ? 253  THR B C   1 
ATOM   4576  O  O   . THR B  1 253 ? 93.382  12.474  -3.379  1.00 9.95  ? 253  THR B O   1 
ATOM   4577  C  CB  . THR B  1 253 ? 91.997  15.531  -3.389  1.00 8.39  ? 253  THR B CB  1 
ATOM   4578  O  OG1 . THR B  1 253 ? 93.212  15.734  -4.176  1.00 9.58  ? 253  THR B OG1 1 
ATOM   4579  C  CG2 . THR B  1 253 ? 91.797  16.870  -2.678  1.00 5.71  ? 253  THR B CG2 1 
ATOM   4580  N  N   . ILE B  1 254 ? 91.128  12.491  -3.576  1.00 8.78  ? 254  ILE B N   1 
ATOM   4581  C  CA  . ILE B  1 254 ? 91.087  11.295  -4.444  1.00 7.99  ? 254  ILE B CA  1 
ATOM   4582  C  C   . ILE B  1 254 ? 90.262  11.746  -5.630  1.00 8.83  ? 254  ILE B C   1 
ATOM   4583  O  O   . ILE B  1 254 ? 89.140  12.261  -5.469  1.00 8.83  ? 254  ILE B O   1 
ATOM   4584  C  CB  . ILE B  1 254 ? 90.448  10.094  -3.726  1.00 9.19  ? 254  ILE B CB  1 
ATOM   4585  C  CG1 . ILE B  1 254 ? 91.171  9.805   -2.413  1.00 5.76  ? 254  ILE B CG1 1 
ATOM   4586  C  CG2 . ILE B  1 254 ? 90.367  8.832   -4.663  1.00 8.17  ? 254  ILE B CG2 1 
ATOM   4587  C  CD1 . ILE B  1 254 ? 90.430  8.754   -1.448  1.00 6.80  ? 254  ILE B CD1 1 
ATOM   4588  N  N   . SER B  1 255 ? 90.866  11.661  -6.808  1.00 8.82  ? 255  SER B N   1 
ATOM   4589  C  CA  . SER B  1 255 ? 90.171  11.896  -8.043  1.00 7.72  ? 255  SER B CA  1 
ATOM   4590  C  C   . SER B  1 255 ? 89.831  10.575  -8.651  1.00 8.46  ? 255  SER B C   1 
ATOM   4591  O  O   . SER B  1 255 ? 90.591  9.637   -8.472  1.00 8.94  ? 255  SER B O   1 
ATOM   4592  C  CB  . SER B  1 255 ? 91.043  12.663  -9.002  1.00 9.06  ? 255  SER B CB  1 
ATOM   4593  O  OG  . SER B  1 255 ? 91.427  13.896  -8.392  1.00 8.18  ? 255  SER B OG  1 
ATOM   4594  N  N   . MET B  1 256 ? 88.680  10.503  -9.320  1.00 8.53  ? 256  MET B N   1 
ATOM   4595  C  CA  . MET B  1 256 ? 88.134  9.196   -9.751  1.00 8.13  ? 256  MET B CA  1 
ATOM   4596  C  C   . MET B  1 256 ? 87.653  9.234   -11.185 1.00 7.38  ? 256  MET B C   1 
ATOM   4597  O  O   . MET B  1 256 ? 86.963  10.179  -11.567 1.00 8.05  ? 256  MET B O   1 
ATOM   4598  C  CB  . MET B  1 256 ? 86.926  8.842   -8.905  1.00 7.18  ? 256  MET B CB  1 
ATOM   4599  C  CG  . MET B  1 256 ? 87.259  8.756   -7.405  1.00 12.90 ? 256  MET B CG  1 
ATOM   4600  S  SD  . MET B  1 256 ? 85.679  8.783   -6.555  1.00 13.14 ? 256  MET B SD  1 
ATOM   4601  C  CE  . MET B  1 256 ? 86.307  9.128   -4.895  1.00 13.31 ? 256  MET B CE  1 
ATOM   4602  N  N   . SER B  1 257 ? 87.947  8.174   -11.932 1.00 5.40  ? 257  SER B N   1 
ATOM   4603  C  CA  . SER B  1 257 ? 87.321  7.916   -13.225 1.00 6.26  ? 257  SER B CA  1 
ATOM   4604  C  C   . SER B  1 257 ? 86.054  7.106   -12.964 1.00 7.57  ? 257  SER B C   1 
ATOM   4605  O  O   . SER B  1 257 ? 85.809  6.674   -11.806 1.00 8.78  ? 257  SER B O   1 
ATOM   4606  C  CB  . SER B  1 257 ? 88.259  7.021   -14.044 1.00 6.45  ? 257  SER B CB  1 
ATOM   4607  O  OG  . SER B  1 257 ? 88.161  5.651   -13.593 1.00 8.10  ? 257  SER B OG  1 
ATOM   4608  N  N   . THR B  1 258 ? 85.272  6.790   -14.007 1.00 8.32  ? 258  THR B N   1 
ATOM   4609  C  CA  . THR B  1 258 ? 84.251  5.737   -13.827 1.00 8.04  ? 258  THR B CA  1 
ATOM   4610  C  C   . THR B  1 258 ? 84.855  4.357   -13.651 1.00 8.47  ? 258  THR B C   1 
ATOM   4611  O  O   . THR B  1 258 ? 86.015  4.139   -13.873 1.00 7.11  ? 258  THR B O   1 
ATOM   4612  C  CB  . THR B  1 258 ? 83.275  5.702   -14.996 1.00 9.37  ? 258  THR B CB  1 
ATOM   4613  O  OG1 . THR B  1 258 ? 84.005  5.551   -16.218 1.00 9.67  ? 258  THR B OG1 1 
ATOM   4614  C  CG2 . THR B  1 258 ? 82.596  7.082   -15.125 1.00 7.79  ? 258  THR B CG2 1 
ATOM   4615  N  N   . THR B  1 259 ? 84.019  3.412   -13.268 1.00 8.52  ? 259  THR B N   1 
ATOM   4616  C  CA  . THR B  1 259 ? 84.467  2.061   -13.029 1.00 9.05  ? 259  THR B CA  1 
ATOM   4617  C  C   . THR B  1 259 ? 84.197  1.332   -14.339 1.00 9.70  ? 259  THR B C   1 
ATOM   4618  O  O   . THR B  1 259 ? 83.053  1.287   -14.754 1.00 10.29 ? 259  THR B O   1 
ATOM   4619  C  CB  . THR B  1 259 ? 83.633  1.440   -11.883 1.00 9.77  ? 259  THR B CB  1 
ATOM   4620  O  OG1 . THR B  1 259 ? 83.872  2.160   -10.650 1.00 10.02 ? 259  THR B OG1 1 
ATOM   4621  C  CG2 . THR B  1 259 ? 84.152  0.001   -11.599 1.00 9.87  ? 259  THR B CG2 1 
ATOM   4622  N  N   . PRO B  1 260 ? 85.231  0.777   -14.990 1.00 8.82  ? 260  PRO B N   1 
ATOM   4623  C  CA  . PRO B  1 260 ? 85.093  0.229   -16.346 1.00 8.37  ? 260  PRO B CA  1 
ATOM   4624  C  C   . PRO B  1 260 ? 84.607  -1.217  -16.506 1.00 7.30  ? 260  PRO B C   1 
ATOM   4625  O  O   . PRO B  1 260 ? 84.379  -1.956  -15.528 1.00 5.55  ? 260  PRO B O   1 
ATOM   4626  C  CB  . PRO B  1 260 ? 86.500  0.384   -16.930 1.00 7.83  ? 260  PRO B CB  1 
ATOM   4627  C  CG  . PRO B  1 260 ? 87.420  0.160   -15.689 1.00 9.00  ? 260  PRO B CG  1 
ATOM   4628  C  CD  . PRO B  1 260 ? 86.627  0.705   -14.497 1.00 9.44  ? 260  PRO B CD  1 
ATOM   4629  N  N   . SER B  1 261 ? 84.405  -1.586  -17.766 1.00 6.36  ? 261  SER B N   1 
ATOM   4630  C  CA  . SER B  1 261 ? 83.949  -2.957  -18.136 1.00 6.20  ? 261  SER B CA  1 
ATOM   4631  C  C   . SER B  1 261 ? 84.824  -4.022  -17.417 1.00 6.03  ? 261  SER B C   1 
ATOM   4632  O  O   . SER B  1 261 ? 86.053  -3.901  -17.411 1.00 4.45  ? 261  SER B O   1 
ATOM   4633  C  CB  . SER B  1 261 ? 84.083  -3.106  -19.657 1.00 7.08  ? 261  SER B CB  1 
ATOM   4634  O  OG  . SER B  1 261 ? 83.763  -4.397  -20.130 1.00 3.93  ? 261  SER B OG  1 
ATOM   4635  N  N   . THR B  1 262 ? 84.151  -5.029  -16.836 1.00 5.81  ? 262  THR B N   1 
ATOM   4636  C  CA  . THR B  1 262 ? 84.691  -6.159  -16.062 1.00 6.46  ? 262  THR B CA  1 
ATOM   4637  C  C   . THR B  1 262 ? 85.019  -5.845  -14.609 1.00 6.70  ? 262  THR B C   1 
ATOM   4638  O  O   . THR B  1 262 ? 85.190  -6.778  -13.812 1.00 6.84  ? 262  THR B O   1 
ATOM   4639  C  CB  . THR B  1 262 ? 85.938  -6.886  -16.686 1.00 6.65  ? 262  THR B CB  1 
ATOM   4640  O  OG1 . THR B  1 262 ? 87.089  -6.034  -16.532 1.00 4.88  ? 262  THR B OG1 1 
ATOM   4641  C  CG2 . THR B  1 262 ? 85.762  -7.172  -18.215 1.00 6.97  ? 262  THR B CG2 1 
ATOM   4642  N  N   . VAL B  1 263 ? 85.151  -4.565  -14.276 1.00 7.24  ? 263  VAL B N   1 
ATOM   4643  C  CA  . VAL B  1 263 ? 85.480  -4.181  -12.906 1.00 8.65  ? 263  VAL B CA  1 
ATOM   4644  C  C   . VAL B  1 263 ? 84.217  -3.966  -12.050 1.00 9.40  ? 263  VAL B C   1 
ATOM   4645  O  O   . VAL B  1 263 ? 83.290  -3.239  -12.446 1.00 7.11  ? 263  VAL B O   1 
ATOM   4646  C  CB  . VAL B  1 263 ? 86.395  -2.913  -12.861 1.00 8.57  ? 263  VAL B CB  1 
ATOM   4647  C  CG1 . VAL B  1 263 ? 86.752  -2.586  -11.417 1.00 13.33 ? 263  VAL B CG1 1 
ATOM   4648  C  CG2 . VAL B  1 263 ? 87.673  -3.225  -13.622 1.00 9.74  ? 263  VAL B CG2 1 
ATOM   4649  N  N   . THR B  1 264 ? 84.193  -4.589  -10.869 1.00 8.72  ? 264  THR B N   1 
ATOM   4650  C  CA  . THR B  1 264 ? 83.086  -4.411  -9.925  1.00 9.39  ? 264  THR B CA  1 
ATOM   4651  C  C   . THR B  1 264 ? 83.554  -3.404  -8.879  1.00 9.84  ? 264  THR B C   1 
ATOM   4652  O  O   . THR B  1 264 ? 84.722  -3.415  -8.471  1.00 11.47 ? 264  THR B O   1 
ATOM   4653  C  CB  . THR B  1 264 ? 82.786  -5.804  -9.275  1.00 9.89  ? 264  THR B CB  1 
ATOM   4654  O  OG1 . THR B  1 264 ? 82.327  -6.701  -10.295 1.00 11.09 ? 264  THR B OG1 1 
ATOM   4655  C  CG2 . THR B  1 264 ? 81.639  -5.734  -8.228  1.00 9.96  ? 264  THR B CG2 1 
ATOM   4656  N  N   . VAL B  1 265 ? 82.675  -2.507  -8.462  1.00 9.73  ? 265  VAL B N   1 
ATOM   4657  C  CA  . VAL B  1 265 ? 83.030  -1.517  -7.445  1.00 9.12  ? 265  VAL B CA  1 
ATOM   4658  C  C   . VAL B  1 265 ? 83.384  -2.318  -6.206  1.00 8.73  ? 265  VAL B C   1 
ATOM   4659  O  O   . VAL B  1 265 ? 82.603  -3.186  -5.795  1.00 7.65  ? 265  VAL B O   1 
ATOM   4660  C  CB  . VAL B  1 265 ? 81.810  -0.607  -7.140  1.00 9.79  ? 265  VAL B CB  1 
ATOM   4661  C  CG1 . VAL B  1 265 ? 82.116  0.263   -5.946  1.00 10.90 ? 265  VAL B CG1 1 
ATOM   4662  C  CG2 . VAL B  1 265 ? 81.439  0.234   -8.411  1.00 7.75  ? 265  VAL B CG2 1 
ATOM   4663  N  N   . PRO B  1 266 ? 84.576  -2.107  -5.643  1.00 8.32  ? 266  PRO B N   1 
ATOM   4664  C  CA  . PRO B  1 266 ? 84.995  -2.927  -4.515  1.00 10.35 ? 266  PRO B CA  1 
ATOM   4665  C  C   . PRO B  1 266 ? 84.303  -2.539  -3.214  1.00 10.43 ? 266  PRO B C   1 
ATOM   4666  O  O   . PRO B  1 266 ? 83.727  -1.465  -3.075  1.00 11.15 ? 266  PRO B O   1 
ATOM   4667  C  CB  . PRO B  1 266 ? 86.492  -2.644  -4.422  1.00 9.89  ? 266  PRO B CB  1 
ATOM   4668  C  CG  . PRO B  1 266 ? 86.585  -1.266  -4.941  1.00 10.04 ? 266  PRO B CG  1 
ATOM   4669  C  CD  . PRO B  1 266 ? 85.616  -1.150  -6.059  1.00 9.51  ? 266  PRO B CD  1 
ATOM   4670  N  N   . THR B  1 267 ? 84.380  -3.417  -2.241  1.00 10.61 ? 267  THR B N   1 
ATOM   4671  C  CA  . THR B  1 267 ? 83.876  -3.075  -0.909  1.00 10.85 ? 267  THR B CA  1 
ATOM   4672  C  C   . THR B  1 267 ? 85.080  -2.847  0.012   1.00 10.62 ? 267  THR B C   1 
ATOM   4673  O  O   . THR B  1 267 ? 86.013  -3.654  0.023   1.00 11.01 ? 267  THR B O   1 
ATOM   4674  C  CB  . THR B  1 267 ? 83.032  -4.253  -0.410  1.00 11.20 ? 267  THR B CB  1 
ATOM   4675  O  OG1 . THR B  1 267 ? 81.865  -4.349  -1.235  1.00 12.73 ? 267  THR B OG1 1 
ATOM   4676  C  CG2 . THR B  1 267 ? 82.495  -4.008  1.041   1.00 9.61  ? 267  THR B CG2 1 
ATOM   4677  N  N   . TRP B  1 268 ? 85.045  -1.775  0.788   1.00 10.44 ? 268  TRP B N   1 
ATOM   4678  C  CA  . TRP B  1 268 ? 86.140  -1.386  1.694   1.00 10.50 ? 268  TRP B CA  1 
ATOM   4679  C  C   . TRP B  1 268 ? 85.727  -1.480  3.179   1.00 10.33 ? 268  TRP B C   1 
ATOM   4680  O  O   . TRP B  1 268 ? 84.559  -1.274  3.521   1.00 9.77  ? 268  TRP B O   1 
ATOM   4681  C  CB  . TRP B  1 268 ? 86.551  0.075   1.406   1.00 9.81  ? 268  TRP B CB  1 
ATOM   4682  C  CG  . TRP B  1 268 ? 87.118  0.283   0.004   1.00 9.91  ? 268  TRP B CG  1 
ATOM   4683  C  CD1 . TRP B  1 268 ? 86.453  0.825   -1.091  1.00 8.75  ? 268  TRP B CD1 1 
ATOM   4684  C  CD2 . TRP B  1 268 ? 88.425  -0.077  -0.470  1.00 6.73  ? 268  TRP B CD2 1 
ATOM   4685  N  NE1 . TRP B  1 268 ? 87.275  0.824   -2.199  1.00 8.28  ? 268  TRP B NE1 1 
ATOM   4686  C  CE2 . TRP B  1 268 ? 88.485  0.265   -1.858  1.00 9.40  ? 268  TRP B CE2 1 
ATOM   4687  C  CE3 . TRP B  1 268 ? 89.543  -0.684  0.119   1.00 9.22  ? 268  TRP B CE3 1 
ATOM   4688  C  CZ2 . TRP B  1 268 ? 89.637  0.059   -2.645  1.00 8.81  ? 268  TRP B CZ2 1 
ATOM   4689  C  CZ3 . TRP B  1 268 ? 90.700  -0.876  -0.671  1.00 6.71  ? 268  TRP B CZ3 1 
ATOM   4690  C  CH2 . TRP B  1 268 ? 90.730  -0.509  -2.028  1.00 6.78  ? 268  TRP B CH2 1 
ATOM   4691  N  N   . SER B  1 269 ? 86.700  -1.745  4.052   1.00 9.86  ? 269  SER B N   1 
ATOM   4692  C  CA  . SER B  1 269 ? 86.501  -1.585  5.481   1.00 10.47 ? 269  SER B CA  1 
ATOM   4693  C  C   . SER B  1 269 ? 87.825  -1.237  6.102   1.00 10.05 ? 269  SER B C   1 
ATOM   4694  O  O   . SER B  1 269 ? 88.859  -1.824  5.717   1.00 9.01  ? 269  SER B O   1 
ATOM   4695  C  CB  . SER B  1 269 ? 85.994  -2.892  6.078   1.00 10.35 ? 269  SER B CB  1 
ATOM   4696  O  OG  . SER B  1 269 ? 85.365  -2.518  7.262   1.00 19.20 ? 269  SER B OG  1 
ATOM   4697  N  N   . PHE B  1 270 ? 87.831  -0.239  6.995   1.00 9.16  ? 270  PHE B N   1 
ATOM   4698  C  CA  . PHE B  1 270 ? 89.057  0.213   7.666   1.00 10.06 ? 270  PHE B CA  1 
ATOM   4699  C  C   . PHE B  1 270 ? 88.784  0.419   9.159   1.00 10.15 ? 270  PHE B C   1 
ATOM   4700  O  O   . PHE B  1 270 ? 87.647  0.724   9.523   1.00 11.37 ? 270  PHE B O   1 
ATOM   4701  C  CB  . PHE B  1 270 ? 89.582  1.477   7.011   1.00 9.45  ? 270  PHE B CB  1 
ATOM   4702  C  CG  . PHE B  1 270 ? 90.032  1.276   5.583   1.00 11.69 ? 270  PHE B CG  1 
ATOM   4703  C  CD1 . PHE B  1 270 ? 91.294  0.779   5.308   1.00 10.21 ? 270  PHE B CD1 1 
ATOM   4704  C  CD2 . PHE B  1 270 ? 89.202  1.610   4.525   1.00 11.78 ? 270  PHE B CD2 1 
ATOM   4705  C  CE1 . PHE B  1 270 ? 91.716  0.576   4.006   1.00 11.15 ? 270  PHE B CE1 1 
ATOM   4706  C  CE2 . PHE B  1 270 ? 89.623  1.406   3.226   1.00 11.95 ? 270  PHE B CE2 1 
ATOM   4707  C  CZ  . PHE B  1 270 ? 90.867  0.900   2.972   1.00 10.86 ? 270  PHE B CZ  1 
ATOM   4708  N  N   . PRO B  1 271 ? 89.779  0.240   10.028  1.00 9.81  ? 271  PRO B N   1 
ATOM   4709  C  CA  . PRO B  1 271 ? 89.528  0.314   11.477  1.00 9.73  ? 271  PRO B CA  1 
ATOM   4710  C  C   . PRO B  1 271 ? 89.170  1.715   11.949  1.00 9.13  ? 271  PRO B C   1 
ATOM   4711  O  O   . PRO B  1 271 ? 88.355  1.851   12.864  1.00 9.48  ? 271  PRO B O   1 
ATOM   4712  C  CB  . PRO B  1 271 ? 90.850  -0.203  12.141  1.00 10.87 ? 271  PRO B CB  1 
ATOM   4713  C  CG  . PRO B  1 271 ? 91.926  -0.106  11.052  1.00 11.49 ? 271  PRO B CG  1 
ATOM   4714  C  CD  . PRO B  1 271 ? 91.194  -0.034  9.707   1.00 10.90 ? 271  PRO B CD  1 
ATOM   4715  N  N   . GLY B  1 272 ? 89.721  2.740   11.322  1.00 7.94  ? 272  GLY B N   1 
ATOM   4716  C  CA  . GLY B  1 272 ? 89.350  4.097   11.701  1.00 8.74  ? 272  GLY B CA  1 
ATOM   4717  C  C   . GLY B  1 272 ? 88.203  4.703   10.898  1.00 7.49  ? 272  GLY B C   1 
ATOM   4718  O  O   . GLY B  1 272 ? 88.046  4.448   9.687   1.00 7.46  ? 272  GLY B O   1 
ATOM   4719  N  N   . ALA B  1 273 ? 87.470  5.633   11.521  1.00 7.20  ? 273  ALA B N   1 
ATOM   4720  C  CA  . ALA B  1 273 ? 86.493  6.401   10.765  1.00 6.24  ? 273  ALA B CA  1 
ATOM   4721  C  C   . ALA B  1 273 ? 87.143  7.094   9.592   1.00 7.17  ? 273  ALA B C   1 
ATOM   4722  O  O   . ALA B  1 273 ? 88.342  7.439   9.660   1.00 6.88  ? 273  ALA B O   1 
ATOM   4723  C  CB  . ALA B  1 273 ? 85.841  7.450   11.653  1.00 5.84  ? 273  ALA B CB  1 
ATOM   4724  N  N   . CYS B  1 274 ? 86.321  7.449   8.590   1.00 6.44  ? 274  CYS B N   1 
ATOM   4725  C  CA  . CYS B  1 274 ? 86.764  8.267   7.494   1.00 7.72  ? 274  CYS B CA  1 
ATOM   4726  C  C   . CYS B  1 274 ? 85.612  9.086   6.972   1.00 8.46  ? 274  CYS B C   1 
ATOM   4727  O  O   . CYS B  1 274 ? 84.428  8.858   7.333   1.00 7.75  ? 274  CYS B O   1 
ATOM   4728  C  CB  . CYS B  1 274 ? 87.491  7.504   6.357   1.00 7.20  ? 274  CYS B CB  1 
ATOM   4729  S  SG  . CYS B  1 274 ? 86.489  6.337   5.433   1.00 10.68 ? 274  CYS B SG  1 
ATOM   4730  N  N   . ALA B  1 275 ? 85.971  10.074  6.160   1.00 8.69  ? 275  ALA B N   1 
ATOM   4731  C  CA  . ALA B  1 275 ? 84.964  10.934  5.574   1.00 7.87  ? 275  ALA B CA  1 
ATOM   4732  C  C   . ALA B  1 275 ? 85.481  11.579  4.312   1.00 9.18  ? 275  ALA B C   1 
ATOM   4733  O  O   . ALA B  1 275 ? 86.685  11.728  4.112   1.00 9.52  ? 275  ALA B O   1 
ATOM   4734  C  CB  . ALA B  1 275 ? 84.524  12.017  6.590   1.00 8.45  ? 275  ALA B CB  1 
ATOM   4735  N  N   . PHE B  1 276 ? 84.540  12.019  3.483   1.00 9.26  ? 276  PHE B N   1 
ATOM   4736  C  CA  . PHE B  1 276 ? 84.942  12.798  2.337   1.00 9.85  ? 276  PHE B CA  1 
ATOM   4737  C  C   . PHE B  1 276 ? 83.918  13.860  2.022   1.00 8.17  ? 276  PHE B C   1 
ATOM   4738  O  O   . PHE B  1 276 ? 82.720  13.712  2.322   1.00 5.84  ? 276  PHE B O   1 
ATOM   4739  C  CB  . PHE B  1 276 ? 85.355  11.892  1.134   1.00 8.68  ? 276  PHE B CB  1 
ATOM   4740  C  CG  . PHE B  1 276 ? 84.220  11.067  0.520   1.00 10.87 ? 276  PHE B CG  1 
ATOM   4741  C  CD1 . PHE B  1 276 ? 83.329  11.630  -0.415  1.00 10.61 ? 276  PHE B CD1 1 
ATOM   4742  C  CD2 . PHE B  1 276 ? 84.064  9.716   0.854   1.00 11.54 ? 276  PHE B CD2 1 
ATOM   4743  C  CE1 . PHE B  1 276 ? 82.302  10.859  -0.975  1.00 11.74 ? 276  PHE B CE1 1 
ATOM   4744  C  CE2 . PHE B  1 276 ? 83.034  8.937   0.278   1.00 10.33 ? 276  PHE B CE2 1 
ATOM   4745  C  CZ  . PHE B  1 276 ? 82.162  9.518   -0.638  1.00 10.82 ? 276  PHE B CZ  1 
ATOM   4746  N  N   . GLN B  1 277 ? 84.428  14.919  1.430   1.00 8.50  ? 277  GLN B N   1 
ATOM   4747  C  CA  . GLN B  1 277 ? 83.617  15.986  0.895   1.00 9.35  ? 277  GLN B CA  1 
ATOM   4748  C  C   . GLN B  1 277 ? 83.885  16.056  -0.606  1.00 9.43  ? 277  GLN B C   1 
ATOM   4749  O  O   . GLN B  1 277 ? 85.059  16.213  -1.061  1.00 9.97  ? 277  GLN B O   1 
ATOM   4750  C  CB  . GLN B  1 277 ? 83.950  17.335  1.567   1.00 9.71  ? 277  GLN B CB  1 
ATOM   4751  C  CG  . GLN B  1 277 ? 83.019  18.439  1.061   1.00 7.91  ? 277  GLN B CG  1 
ATOM   4752  C  CD  . GLN B  1 277 ? 83.318  19.842  1.578   1.00 11.29 ? 277  GLN B CD  1 
ATOM   4753  O  OE1 . GLN B  1 277 ? 84.408  20.361  1.382   1.00 12.08 ? 277  GLN B OE1 1 
ATOM   4754  N  NE2 . GLN B  1 277 ? 82.310  20.483  2.188   1.00 10.06 ? 277  GLN B NE2 1 
ATOM   4755  N  N   . VAL B  1 278 ? 82.827  15.873  -1.382  1.00 10.03 ? 278  VAL B N   1 
ATOM   4756  C  CA  . VAL B  1 278 ? 82.904  16.067  -2.841  1.00 9.77  ? 278  VAL B CA  1 
ATOM   4757  C  C   . VAL B  1 278 ? 83.320  17.490  -3.161  1.00 10.03 ? 278  VAL B C   1 
ATOM   4758  O  O   . VAL B  1 278 ? 82.726  18.487  -2.670  1.00 8.18  ? 278  VAL B O   1 
ATOM   4759  C  CB  . VAL B  1 278 ? 81.598  15.705  -3.551  1.00 10.41 ? 278  VAL B CB  1 
ATOM   4760  C  CG1 . VAL B  1 278 ? 81.710  15.999  -5.081  1.00 7.30  ? 278  VAL B CG1 1 
ATOM   4761  C  CG2 . VAL B  1 278 ? 81.258  14.195  -3.243  1.00 10.10 ? 278  VAL B CG2 1 
ATOM   4762  N  N   . GLN B  1 279 ? 84.343  17.594  -4.012  1.00 8.67  ? 279  GLN B N   1 
ATOM   4763  C  CA  . GLN B  1 279 ? 84.718  18.904  -4.507  1.00 10.14 ? 279  GLN B CA  1 
ATOM   4764  C  C   . GLN B  1 279 ? 84.175  19.105  -5.902  1.00 11.66 ? 279  GLN B C   1 
ATOM   4765  O  O   . GLN B  1 279 ? 83.606  20.153  -6.151  1.00 11.61 ? 279  GLN B O   1 
ATOM   4766  C  CB  . GLN B  1 279 ? 86.210  19.106  -4.482  1.00 8.64  ? 279  GLN B CB  1 
ATOM   4767  C  CG  . GLN B  1 279 ? 86.757  18.793  -3.082  1.00 11.34 ? 279  GLN B CG  1 
ATOM   4768  C  CD  . GLN B  1 279 ? 86.199  19.757  -2.040  1.00 13.09 ? 279  GLN B CD  1 
ATOM   4769  O  OE1 . GLN B  1 279 ? 86.098  20.974  -2.304  1.00 7.89  ? 279  GLN B OE1 1 
ATOM   4770  N  NE2 . GLN B  1 279 ? 85.779  19.212  -0.885  1.00 10.39 ? 279  GLN B NE2 1 
ATOM   4771  N  N   . GLU B  1 280 ? 84.312  18.086  -6.773  1.00 10.11 ? 280  GLU B N   1 
ATOM   4772  C  CA  . GLU B  1 280 ? 83.871  18.214  -8.168  1.00 10.94 ? 280  GLU B CA  1 
ATOM   4773  C  C   . GLU B  1 280 ? 83.237  16.877  -8.528  1.00 10.20 ? 280  GLU B C   1 
ATOM   4774  O  O   . GLU B  1 280 ? 83.707  15.866  -8.092  1.00 10.21 ? 280  GLU B O   1 
ATOM   4775  C  CB  . GLU B  1 280 ? 85.075  18.479  -9.094  1.00 10.87 ? 280  GLU B CB  1 
ATOM   4776  C  CG  . GLU B  1 280 ? 84.733  18.341  -10.598 1.00 16.31 ? 280  GLU B CG  1 
ATOM   4777  C  CD  . GLU B  1 280 ? 85.892  18.704  -11.513 1.00 19.06 ? 280  GLU B CD  1 
ATOM   4778  O  OE1 . GLU B  1 280 ? 87.064  18.906  -11.012 1.00 14.67 ? 280  GLU B OE1 1 
ATOM   4779  O  OE2 . GLU B  1 280 ? 85.605  18.809  -12.718 1.00 20.54 ? 280  GLU B OE2 1 
ATOM   4780  N  N   . GLY B  1 281 ? 82.170  16.876  -9.309  1.00 10.24 ? 281  GLY B N   1 
ATOM   4781  C  CA  . GLY B  1 281 ? 81.702  15.597  -9.813  1.00 8.40  ? 281  GLY B CA  1 
ATOM   4782  C  C   . GLY B  1 281 ? 80.522  15.022  -9.054  1.00 7.98  ? 281  GLY B C   1 
ATOM   4783  O  O   . GLY B  1 281 ? 79.814  15.717  -8.328  1.00 6.14  ? 281  GLY B O   1 
ATOM   4784  N  N   . ARG B  1 282 ? 80.332  13.713  -9.195  1.00 7.62  ? 282  ARG B N   1 
ATOM   4785  C  CA  . ARG B  1 282 ? 79.105  13.065  -8.726  1.00 7.38  ? 282  ARG B CA  1 
ATOM   4786  C  C   . ARG B  1 282 ? 79.513  11.687  -8.243  1.00 7.12  ? 282  ARG B C   1 
ATOM   4787  O  O   . ARG B  1 282 ? 79.960  10.845  -9.026  1.00 7.25  ? 282  ARG B O   1 
ATOM   4788  C  CB  . ARG B  1 282 ? 78.005  12.980  -9.812  1.00 6.65  ? 282  ARG B CB  1 
ATOM   4789  C  CG  . ARG B  1 282 ? 77.665  14.324  -10.515 1.00 9.66  ? 282  ARG B CG  1 
ATOM   4790  C  CD  . ARG B  1 282 ? 76.410  14.230  -11.371 1.00 8.44  ? 282  ARG B CD  1 
ATOM   4791  N  NE  . ARG B  1 282 ? 76.665  13.502  -12.613 1.00 11.73 ? 282  ARG B NE  1 
ATOM   4792  C  CZ  . ARG B  1 282 ? 76.028  12.429  -13.026 1.00 9.85  ? 282  ARG B CZ  1 
ATOM   4793  N  NH1 . ARG B  1 282 ? 75.069  11.891  -12.283 1.00 8.64  ? 282  ARG B NH1 1 
ATOM   4794  N  NH2 . ARG B  1 282 ? 76.347  11.879  -14.201 1.00 8.58  ? 282  ARG B NH2 1 
ATOM   4795  N  N   . VAL B  1 283 ? 79.381  11.466  -6.942  1.00 6.00  ? 283  VAL B N   1 
ATOM   4796  C  CA  . VAL B  1 283 ? 79.978  10.257  -6.350  1.00 7.10  ? 283  VAL B CA  1 
ATOM   4797  C  C   . VAL B  1 283 ? 78.916  9.523   -5.574  1.00 7.16  ? 283  VAL B C   1 
ATOM   4798  O  O   . VAL B  1 283 ? 78.264  10.101  -4.676  1.00 8.41  ? 283  VAL B O   1 
ATOM   4799  C  CB  . VAL B  1 283 ? 81.115  10.597  -5.369  1.00 6.73  ? 283  VAL B CB  1 
ATOM   4800  C  CG1 . VAL B  1 283 ? 81.739  9.294   -4.696  1.00 5.47  ? 283  VAL B CG1 1 
ATOM   4801  C  CG2 . VAL B  1 283 ? 82.241  11.416  -6.094  1.00 8.63  ? 283  VAL B CG2 1 
ATOM   4802  N  N   . VAL B  1 284 ? 78.752  8.244   -5.877  1.00 7.01  ? 284  VAL B N   1 
ATOM   4803  C  CA  . VAL B  1 284 ? 77.778  7.414   -5.185  1.00 6.44  ? 284  VAL B CA  1 
ATOM   4804  C  C   . VAL B  1 284 ? 78.482  6.702   -4.045  1.00 9.24  ? 284  VAL B C   1 
ATOM   4805  O  O   . VAL B  1 284 ? 79.505  6.058   -4.271  1.00 7.50  ? 284  VAL B O   1 
ATOM   4806  C  CB  . VAL B  1 284 ? 77.155  6.368   -6.159  1.00 8.07  ? 284  VAL B CB  1 
ATOM   4807  C  CG1 . VAL B  1 284 ? 76.217  5.320   -5.398  1.00 3.21  ? 284  VAL B CG1 1 
ATOM   4808  C  CG2 . VAL B  1 284 ? 76.424  7.059   -7.319  1.00 7.38  ? 284  VAL B CG2 1 
ATOM   4809  N  N   . VAL B  1 285 ? 77.925  6.817   -2.834  1.00 9.64  ? 285  VAL B N   1 
ATOM   4810  C  CA  . VAL B  1 285 ? 78.421  6.065   -1.682  1.00 9.91  ? 285  VAL B CA  1 
ATOM   4811  C  C   . VAL B  1 285 ? 77.313  5.149   -1.153  1.00 9.24  ? 285  VAL B C   1 
ATOM   4812  O  O   . VAL B  1 285 ? 76.106  5.468   -1.167  1.00 10.14 ? 285  VAL B O   1 
ATOM   4813  C  CB  . VAL B  1 285 ? 78.964  7.049   -0.585  1.00 10.52 ? 285  VAL B CB  1 
ATOM   4814  C  CG1 . VAL B  1 285 ? 77.792  7.670   0.235   1.00 9.75  ? 285  VAL B CG1 1 
ATOM   4815  C  CG2 . VAL B  1 285 ? 79.971  6.382   0.314   1.00 10.51 ? 285  VAL B CG2 1 
ATOM   4816  N  N   . GLN B  1 286 ? 77.724  3.985   -0.696  1.00 8.79  ? 286  GLN B N   1 
ATOM   4817  C  CA  . GLN B  1 286 ? 76.824  3.026   -0.094  1.00 8.74  ? 286  GLN B CA  1 
ATOM   4818  C  C   . GLN B  1 286 ? 77.536  2.540   1.159   1.00 9.13  ? 286  GLN B C   1 
ATOM   4819  O  O   . GLN B  1 286 ? 78.626  1.997   1.061   1.00 8.50  ? 286  GLN B O   1 
ATOM   4820  C  CB  . GLN B  1 286 ? 76.509  1.885   -1.066  1.00 8.70  ? 286  GLN B CB  1 
ATOM   4821  C  CG  . GLN B  1 286 ? 75.712  0.726   -0.355  1.00 11.70 ? 286  GLN B CG  1 
ATOM   4822  C  CD  . GLN B  1 286 ? 75.130  -0.304  -1.316  1.00 17.00 ? 286  GLN B CD  1 
ATOM   4823  O  OE1 . GLN B  1 286 ? 74.372  -1.195  -0.892  1.00 17.34 ? 286  GLN B OE1 1 
ATOM   4824  N  NE2 . GLN B  1 286 ? 75.433  -0.169  -2.595  1.00 14.89 ? 286  GLN B NE2 1 
ATOM   4825  N  N   . ILE B  1 287 ? 76.949  2.836   2.321   1.00 8.88  ? 287  ILE B N   1 
ATOM   4826  C  CA  . ILE B  1 287 ? 77.544  2.572   3.619   1.00 8.33  ? 287  ILE B CA  1 
ATOM   4827  C  C   . ILE B  1 287 ? 76.677  1.662   4.461   1.00 8.70  ? 287  ILE B C   1 
ATOM   4828  O  O   . ILE B  1 287 ? 75.485  1.913   4.663   1.00 7.30  ? 287  ILE B O   1 
ATOM   4829  C  CB  . ILE B  1 287 ? 77.813  3.884   4.391   1.00 8.29  ? 287  ILE B CB  1 
ATOM   4830  C  CG1 . ILE B  1 287 ? 78.435  4.939   3.474   1.00 8.48  ? 287  ILE B CG1 1 
ATOM   4831  C  CG2 . ILE B  1 287 ? 78.773  3.591   5.581   1.00 6.49  ? 287  ILE B CG2 1 
ATOM   4832  C  CD1 . ILE B  1 287 ? 78.397  6.380   4.021   1.00 7.63  ? 287  ILE B CD1 1 
ATOM   4833  N  N   . GLY B  1 288 ? 77.272  0.552   4.900   1.00 8.78  ? 288  GLY B N   1 
ATOM   4834  C  CA  . GLY B  1 288 ? 76.603  -0.363  5.804   1.00 9.66  ? 288  GLY B CA  1 
ATOM   4835  C  C   . GLY B  1 288 ? 75.360  -0.882  5.140   1.00 9.90  ? 288  GLY B C   1 
ATOM   4836  O  O   . GLY B  1 288 ? 75.384  -1.240  3.974   1.00 11.06 ? 288  GLY B O   1 
ATOM   4837  N  N   . ASP B  1 289 ? 74.270  -0.890  5.896   1.00 10.19 ? 289  ASP B N   1 
ATOM   4838  C  CA  . ASP B  1 289 ? 72.960  -1.349  5.419   1.00 11.51 ? 289  ASP B CA  1 
ATOM   4839  C  C   . ASP B  1 289 ? 72.067  -0.263  4.836   1.00 10.10 ? 289  ASP B C   1 
ATOM   4840  O  O   . ASP B  1 289 ? 70.892  -0.511  4.548   1.00 10.27 ? 289  ASP B O   1 
ATOM   4841  C  CB  . ASP B  1 289 ? 72.212  -2.048  6.554   1.00 11.80 ? 289  ASP B CB  1 
ATOM   4842  C  CG  . ASP B  1 289 ? 72.773  -3.444  6.855   1.00 17.61 ? 289  ASP B CG  1 
ATOM   4843  O  OD1 . ASP B  1 289 ? 73.165  -4.204  5.900   1.00 22.08 ? 289  ASP B OD1 1 
ATOM   4844  O  OD2 . ASP B  1 289 ? 72.829  -3.865  8.040   1.00 21.43 ? 289  ASP B OD2 1 
ATOM   4845  N  N   . TYR B  1 290 ? 72.620  0.930   4.657   1.00 10.04 ? 290  TYR B N   1 
ATOM   4846  C  CA  . TYR B  1 290 ? 71.863  2.046   4.113   1.00 9.03  ? 290  TYR B CA  1 
ATOM   4847  C  C   . TYR B  1 290 ? 71.718  2.081   2.590   1.00 9.41  ? 290  TYR B C   1 
ATOM   4848  O  O   . TYR B  1 290 ? 72.542  1.539   1.827   1.00 8.77  ? 290  TYR B O   1 
ATOM   4849  C  CB  . TYR B  1 290 ? 72.542  3.341   4.552   1.00 8.82  ? 290  TYR B CB  1 
ATOM   4850  C  CG  . TYR B  1 290 ? 72.406  3.637   6.031   1.00 9.14  ? 290  TYR B CG  1 
ATOM   4851  C  CD1 . TYR B  1 290 ? 73.249  3.031   6.966   1.00 7.17  ? 290  TYR B CD1 1 
ATOM   4852  C  CD2 . TYR B  1 290 ? 71.474  4.566   6.491   1.00 4.89  ? 290  TYR B CD2 1 
ATOM   4853  C  CE1 . TYR B  1 290 ? 73.156  3.328   8.333   1.00 7.75  ? 290  TYR B CE1 1 
ATOM   4854  C  CE2 . TYR B  1 290 ? 71.375  4.864   7.876   1.00 9.25  ? 290  TYR B CE2 1 
ATOM   4855  C  CZ  . TYR B  1 290 ? 72.221  4.242   8.774   1.00 9.48  ? 290  TYR B CZ  1 
ATOM   4856  O  OH  . TYR B  1 290 ? 72.152  4.527   10.133  1.00 15.62 ? 290  TYR B OH  1 
ATOM   4857  N  N   . ALA B  1 291 ? 70.705  2.807   2.141   1.00 10.21 ? 291  ALA B N   1 
ATOM   4858  C  CA  . ALA B  1 291 ? 70.483  2.988   0.716   1.00 10.67 ? 291  ALA B CA  1 
ATOM   4859  C  C   . ALA B  1 291 ? 71.620  3.851   0.162   1.00 10.45 ? 291  ALA B C   1 
ATOM   4860  O  O   . ALA B  1 291 ? 72.073  4.773   0.842   1.00 10.01 ? 291  ALA B O   1 
ATOM   4861  C  CB  . ALA B  1 291 ? 69.096  3.671   0.463   1.00 10.50 ? 291  ALA B CB  1 
ATOM   4862  N  N   . ALA B  1 292 ? 72.089  3.524   -1.048  1.00 9.81  ? 292  ALA B N   1 
ATOM   4863  C  CA  . ALA B  1 292 ? 73.083  4.309   -1.763  1.00 10.82 ? 292  ALA B CA  1 
ATOM   4864  C  C   . ALA B  1 292 ? 72.545  5.742   -2.002  1.00 12.04 ? 292  ALA B C   1 
ATOM   4865  O  O   . ALA B  1 292 ? 71.334  5.922   -2.117  1.00 12.24 ? 292  ALA B O   1 
ATOM   4866  C  CB  . ALA B  1 292 ? 73.441  3.640   -3.084  1.00 10.85 ? 292  ALA B CB  1 
ATOM   4867  N  N   . THR B  1 293 ? 73.458  6.717   -2.038  1.00 11.24 ? 293  THR B N   1 
ATOM   4868  C  CA  . THR B  1 293 ? 73.154  8.126   -2.160  1.00 11.10 ? 293  THR B CA  1 
ATOM   4869  C  C   . THR B  1 293 ? 74.185  8.728   -3.103  1.00 10.32 ? 293  THR B C   1 
ATOM   4870  O  O   . THR B  1 293 ? 75.385  8.512   -2.971  1.00 8.53  ? 293  THR B O   1 
ATOM   4871  C  CB  . THR B  1 293 ? 73.287  8.790   -0.784  1.00 12.46 ? 293  THR B CB  1 
ATOM   4872  O  OG1 . THR B  1 293 ? 72.138  8.473   -0.025  1.00 18.34 ? 293  THR B OG1 1 
ATOM   4873  C  CG2 . THR B  1 293 ? 73.266  10.344  -0.826  1.00 13.28 ? 293  THR B CG2 1 
ATOM   4874  N  N   . GLU B  1 294 ? 73.717  9.533   -4.040  1.00 11.14 ? 294  GLU B N   1 
ATOM   4875  C  CA  . GLU B  1 294 ? 74.629  10.233  -4.910  1.00 11.22 ? 294  GLU B CA  1 
ATOM   4876  C  C   . GLU B  1 294 ? 74.964  11.594  -4.287  1.00 11.65 ? 294  GLU B C   1 
ATOM   4877  O  O   . GLU B  1 294 ? 74.062  12.389  -3.984  1.00 11.36 ? 294  GLU B O   1 
ATOM   4878  C  CB  . GLU B  1 294 ? 73.996  10.455  -6.300  1.00 12.81 ? 294  GLU B CB  1 
ATOM   4879  C  CG  . GLU B  1 294 ? 75.092  10.796  -7.318  1.00 12.30 ? 294  GLU B CG  1 
ATOM   4880  C  CD  . GLU B  1 294 ? 74.561  11.027  -8.728  1.00 15.61 ? 294  GLU B CD  1 
ATOM   4881  O  OE1 . GLU B  1 294 ? 74.058  10.063  -9.339  1.00 20.69 ? 294  GLU B OE1 1 
ATOM   4882  O  OE2 . GLU B  1 294 ? 74.646  12.174  -9.219  1.00 18.24 ? 294  GLU B OE2 1 
ATOM   4883  N  N   . LEU B  1 295 ? 76.245  11.879  -4.152  1.00 10.39 ? 295  LEU B N   1 
ATOM   4884  C  CA  . LEU B  1 295 ? 76.668  13.151  -3.558  1.00 11.02 ? 295  LEU B CA  1 
ATOM   4885  C  C   . LEU B  1 295 ? 77.149  14.107  -4.597  1.00 10.60 ? 295  LEU B C   1 
ATOM   4886  O  O   . LEU B  1 295 ? 77.792  13.679  -5.527  1.00 10.72 ? 295  LEU B O   1 
ATOM   4887  C  CB  . LEU B  1 295 ? 77.845  12.900  -2.617  1.00 10.78 ? 295  LEU B CB  1 
ATOM   4888  C  CG  . LEU B  1 295 ? 77.459  12.488  -1.182  1.00 15.09 ? 295  LEU B CG  1 
ATOM   4889  C  CD1 . LEU B  1 295 ? 77.101  11.037  -1.138  1.00 14.50 ? 295  LEU B CD1 1 
ATOM   4890  C  CD2 . LEU B  1 295 ? 78.673  12.759  -0.245  1.00 16.45 ? 295  LEU B CD2 1 
ATOM   4891  N  N   . GLY B  1 296 ? 76.906  15.408  -4.405  1.00 9.84  ? 296  GLY B N   1 
ATOM   4892  C  CA  . GLY B  1 296 ? 77.415  16.431  -5.324  1.00 9.46  ? 296  GLY B CA  1 
ATOM   4893  C  C   . GLY B  1 296 ? 78.288  17.460  -4.612  1.00 9.45  ? 296  GLY B C   1 
ATOM   4894  O  O   . GLY B  1 296 ? 78.701  17.192  -3.491  1.00 7.32  ? 296  GLY B O   1 
ATOM   4895  N  N   . SER B  1 297 ? 78.563  18.628  -5.221  1.00 8.50  ? 297  SER B N   1 
ATOM   4896  C  CA  . SER B  1 297 ? 79.621  19.490  -4.611  1.00 9.95  ? 297  SER B CA  1 
ATOM   4897  C  C   . SER B  1 297 ? 79.320  19.846  -3.164  1.00 8.04  ? 297  SER B C   1 
ATOM   4898  O  O   . SER B  1 297 ? 78.176  20.207  -2.835  1.00 8.64  ? 297  SER B O   1 
ATOM   4899  C  CB  . SER B  1 297 ? 79.919  20.777  -5.393  1.00 10.79 ? 297  SER B CB  1 
ATOM   4900  O  OG  . SER B  1 297 ? 78.723  21.224  -5.917  1.00 12.38 ? 297  SER B OG  1 
ATOM   4901  N  N   . GLY B  1 298 ? 80.341  19.679  -2.314  1.00 7.14  ? 298  GLY B N   1 
ATOM   4902  C  CA  . GLY B  1 298 ? 80.253  20.100  -0.929  1.00 5.89  ? 298  GLY B CA  1 
ATOM   4903  C  C   . GLY B  1 298 ? 79.544  19.120  -0.022  1.00 8.11  ? 298  GLY B C   1 
ATOM   4904  O  O   . GLY B  1 298 ? 79.552  19.317  1.196   1.00 6.58  ? 298  GLY B O   1 
ATOM   4905  N  N   . ASP B  1 299 ? 78.913  18.083  -0.605  1.00 7.41  ? 299  ASP B N   1 
ATOM   4906  C  CA  . ASP B  1 299 ? 78.231  17.078  0.201   1.00 7.52  ? 299  ASP B CA  1 
ATOM   4907  C  C   . ASP B  1 299 ? 79.314  16.224  0.922   1.00 7.70  ? 299  ASP B C   1 
ATOM   4908  O  O   . ASP B  1 299 ? 80.385  15.966  0.365   1.00 7.36  ? 299  ASP B O   1 
ATOM   4909  C  CB  . ASP B  1 299 ? 77.442  16.135  -0.690  1.00 6.85  ? 299  ASP B CB  1 
ATOM   4910  C  CG  . ASP B  1 299 ? 76.178  16.767  -1.308  1.00 7.46  ? 299  ASP B CG  1 
ATOM   4911  O  OD1 . ASP B  1 299 ? 75.726  17.876  -0.904  1.00 5.29  ? 299  ASP B OD1 1 
ATOM   4912  O  OD2 . ASP B  1 299 ? 75.545  16.157  -2.217  1.00 6.71  ? 299  ASP B OD2 1 
ATOM   4913  N  N   . VAL B  1 300 ? 78.989  15.764  2.127   1.00 6.22  ? 300  VAL B N   1 
ATOM   4914  C  CA  . VAL B  1 300 ? 79.955  15.060  2.986   1.00 7.71  ? 300  VAL B CA  1 
ATOM   4915  C  C   . VAL B  1 300 ? 79.410  13.709  3.354   1.00 7.67  ? 300  VAL B C   1 
ATOM   4916  O  O   . VAL B  1 300 ? 78.266  13.594  3.777   1.00 8.62  ? 300  VAL B O   1 
ATOM   4917  C  CB  . VAL B  1 300 ? 80.194  15.841  4.291   1.00 7.82  ? 300  VAL B CB  1 
ATOM   4918  C  CG1 . VAL B  1 300 ? 81.198  15.089  5.205   1.00 8.57  ? 300  VAL B CG1 1 
ATOM   4919  C  CG2 . VAL B  1 300 ? 80.723  17.257  3.946   1.00 6.80  ? 300  VAL B CG2 1 
ATOM   4920  N  N   . ALA B  1 301 ? 80.229  12.682  3.170   1.00 7.33  ? 301  ALA B N   1 
ATOM   4921  C  CA  . ALA B  1 301 ? 79.908  11.371  3.628   1.00 6.82  ? 301  ALA B CA  1 
ATOM   4922  C  C   . ALA B  1 301 ? 80.801  10.934  4.778   1.00 7.06  ? 301  ALA B C   1 
ATOM   4923  O  O   . ALA B  1 301 ? 82.011  11.161  4.769   1.00 9.07  ? 301  ALA B O   1 
ATOM   4924  C  CB  . ALA B  1 301 ? 79.990  10.361  2.461   1.00 6.70  ? 301  ALA B CB  1 
ATOM   4925  N  N   . PHE B  1 302 ? 80.188  10.336  5.789   1.00 5.88  ? 302  PHE B N   1 
ATOM   4926  C  CA  . PHE B  1 302 ? 80.936  9.861   6.932   1.00 6.05  ? 302  PHE B CA  1 
ATOM   4927  C  C   . PHE B  1 302 ? 80.756  8.366   7.127   1.00 6.03  ? 302  PHE B C   1 
ATOM   4928  O  O   . PHE B  1 302 ? 79.613  7.864   7.117   1.00 6.61  ? 302  PHE B O   1 
ATOM   4929  C  CB  . PHE B  1 302 ? 80.528  10.588  8.214   1.00 6.38  ? 302  PHE B CB  1 
ATOM   4930  C  CG  . PHE B  1 302 ? 81.210  10.036  9.438   1.00 6.40  ? 302  PHE B CG  1 
ATOM   4931  C  CD1 . PHE B  1 302 ? 82.488  10.453  9.773   1.00 4.14  ? 302  PHE B CD1 1 
ATOM   4932  C  CD2 . PHE B  1 302 ? 80.581  9.092   10.247  1.00 4.43  ? 302  PHE B CD2 1 
ATOM   4933  C  CE1 . PHE B  1 302 ? 83.123  9.942   10.912  1.00 4.64  ? 302  PHE B CE1 1 
ATOM   4934  C  CE2 . PHE B  1 302 ? 81.228  8.548   11.363  1.00 6.03  ? 302  PHE B CE2 1 
ATOM   4935  C  CZ  . PHE B  1 302 ? 82.509  9.000   11.707  1.00 2.43  ? 302  PHE B CZ  1 
ATOM   4936  N  N   . ILE B  1 303 ? 81.879  7.665   7.300   1.00 6.47  ? 303  ILE B N   1 
ATOM   4937  C  CA  . ILE B  1 303 ? 81.921  6.207   7.424   1.00 7.48  ? 303  ILE B CA  1 
ATOM   4938  C  C   . ILE B  1 303 ? 82.621  5.769   8.730   1.00 6.32  ? 303  ILE B C   1 
ATOM   4939  O  O   . ILE B  1 303 ? 83.814  5.939   8.847   1.00 5.80  ? 303  ILE B O   1 
ATOM   4940  C  CB  . ILE B  1 303 ? 82.730  5.591   6.193   1.00 9.79  ? 303  ILE B CB  1 
ATOM   4941  C  CG1 . ILE B  1 303 ? 82.055  5.909   4.876   1.00 10.00 ? 303  ILE B CG1 1 
ATOM   4942  C  CG2 . ILE B  1 303 ? 82.750  4.071   6.306   1.00 8.51  ? 303  ILE B CG2 1 
ATOM   4943  C  CD1 . ILE B  1 303 ? 82.788  6.806   4.031   1.00 14.64 ? 303  ILE B CD1 1 
ATOM   4944  N  N   . PRO B  1 304 ? 81.883  5.222   9.698   1.00 7.18  ? 304  PRO B N   1 
ATOM   4945  C  CA  . PRO B  1 304 ? 82.478  4.722   10.939  1.00 6.35  ? 304  PRO B CA  1 
ATOM   4946  C  C   . PRO B  1 304 ? 83.560  3.674   10.670  1.00 7.22  ? 304  PRO B C   1 
ATOM   4947  O  O   . PRO B  1 304 ? 83.389  2.870   9.732   1.00 7.42  ? 304  PRO B O   1 
ATOM   4948  C  CB  . PRO B  1 304 ? 81.295  4.005   11.629  1.00 7.10  ? 304  PRO B CB  1 
ATOM   4949  C  CG  . PRO B  1 304 ? 80.036  4.756   11.138  1.00 6.86  ? 304  PRO B CG  1 
ATOM   4950  C  CD  . PRO B  1 304 ? 80.401  5.087   9.688   1.00 6.07  ? 304  PRO B CD  1 
ATOM   4951  N  N   . GLY B  1 305 ? 84.573  3.640   11.528  1.00 6.98  ? 305  GLY B N   1 
ATOM   4952  C  CA  . GLY B  1 305 ? 85.541  2.569   11.582  1.00 6.96  ? 305  GLY B CA  1 
ATOM   4953  C  C   . GLY B  1 305 ? 84.861  1.226   11.655  1.00 8.23  ? 305  GLY B C   1 
ATOM   4954  O  O   . GLY B  1 305 ? 83.915  1.024   12.455  1.00 7.10  ? 305  GLY B O   1 
ATOM   4955  N  N   . GLY B  1 306 ? 85.314  0.320   10.802  1.00 8.06  ? 306  GLY B N   1 
ATOM   4956  C  CA  . GLY B  1 306 ? 84.844  -1.044  10.819  1.00 8.60  ? 306  GLY B CA  1 
ATOM   4957  C  C   . GLY B  1 306 ? 83.535  -1.282  10.076  1.00 9.21  ? 306  GLY B C   1 
ATOM   4958  O  O   . GLY B  1 306 ? 82.989  -2.398  10.146  1.00 10.16 ? 306  GLY B O   1 
ATOM   4959  N  N   . VAL B  1 307 ? 82.998  -0.269  9.415   1.00 7.68  ? 307  VAL B N   1 
ATOM   4960  C  CA  . VAL B  1 307 ? 81.761  -0.445  8.655   1.00 7.30  ? 307  VAL B CA  1 
ATOM   4961  C  C   . VAL B  1 307 ? 82.100  -0.551  7.151   1.00 7.12  ? 307  VAL B C   1 
ATOM   4962  O  O   . VAL B  1 307 ? 82.982  0.114   6.670   1.00 8.99  ? 307  VAL B O   1 
ATOM   4963  C  CB  . VAL B  1 307 ? 80.765  0.708   8.916   1.00 7.31  ? 307  VAL B CB  1 
ATOM   4964  C  CG1 . VAL B  1 307 ? 79.596  0.739   7.872   1.00 7.34  ? 307  VAL B CG1 1 
ATOM   4965  C  CG2 . VAL B  1 307 ? 80.270  0.735   10.384  1.00 6.58  ? 307  VAL B CG2 1 
ATOM   4966  N  N   . GLU B  1 308 ? 81.425  -1.421  6.410   1.00 7.23  ? 308  GLU B N   1 
ATOM   4967  C  CA  . GLU B  1 308 ? 81.790  -1.658  5.008   1.00 6.94  ? 308  GLU B CA  1 
ATOM   4968  C  C   . GLU B  1 308 ? 81.181  -0.548  4.151   1.00 7.06  ? 308  GLU B C   1 
ATOM   4969  O  O   . GLU B  1 308 ? 80.132  0.013   4.476   1.00 6.68  ? 308  GLU B O   1 
ATOM   4970  C  CB  . GLU B  1 308 ? 81.291  -3.032  4.503   1.00 8.62  ? 308  GLU B CB  1 
ATOM   4971  C  CG  . GLU B  1 308 ? 81.933  -4.225  5.216   1.00 10.87 ? 308  GLU B CG  1 
ATOM   4972  C  CD  . GLU B  1 308 ? 81.627  -5.573  4.563   1.00 22.05 ? 308  GLU B CD  1 
ATOM   4973  O  OE1 . GLU B  1 308 ? 80.455  -5.840  4.221   1.00 24.66 ? 308  GLU B OE1 1 
ATOM   4974  O  OE2 . GLU B  1 308 ? 82.569  -6.391  4.413   1.00 25.38 ? 308  GLU B OE2 1 
ATOM   4975  N  N   . PHE B  1 309 ? 81.839  -0.233  3.043   1.00 7.05  ? 309  PHE B N   1 
ATOM   4976  C  CA  . PHE B  1 309 ? 81.338  0.807   2.191   1.00 7.59  ? 309  PHE B CA  1 
ATOM   4977  C  C   . PHE B  1 309 ? 81.876  0.576   0.788   1.00 8.14  ? 309  PHE B C   1 
ATOM   4978  O  O   . PHE B  1 309 ? 82.889  -0.097  0.599   1.00 7.25  ? 309  PHE B O   1 
ATOM   4979  C  CB  . PHE B  1 309 ? 81.689  2.211   2.732   1.00 7.55  ? 309  PHE B CB  1 
ATOM   4980  C  CG  . PHE B  1 309 ? 83.163  2.550   2.701   1.00 9.78  ? 309  PHE B CG  1 
ATOM   4981  C  CD1 . PHE B  1 309 ? 84.032  2.098   3.714   1.00 9.60  ? 309  PHE B CD1 1 
ATOM   4982  C  CD2 . PHE B  1 309 ? 83.673  3.367   1.667   1.00 9.76  ? 309  PHE B CD2 1 
ATOM   4983  C  CE1 . PHE B  1 309 ? 85.389  2.486   3.687   1.00 12.02 ? 309  PHE B CE1 1 
ATOM   4984  C  CE2 . PHE B  1 309 ? 85.002  3.736   1.609   1.00 10.14 ? 309  PHE B CE2 1 
ATOM   4985  C  CZ  . PHE B  1 309 ? 85.874  3.314   2.594   1.00 10.80 ? 309  PHE B CZ  1 
ATOM   4986  N  N   . LYS B  1 310 ? 81.140  1.105   -0.176  1.00 7.03  ? 310  LYS B N   1 
ATOM   4987  C  CA  . LYS B  1 310 ? 81.535  1.112   -1.563  1.00 8.72  ? 310  LYS B CA  1 
ATOM   4988  C  C   . LYS B  1 310 ? 81.298  2.556   -2.023  1.00 8.08  ? 310  LYS B C   1 
ATOM   4989  O  O   . LYS B  1 310 ? 80.300  3.178   -1.633  1.00 8.19  ? 310  LYS B O   1 
ATOM   4990  C  CB  . LYS B  1 310 ? 80.597  0.273   -2.420  1.00 7.73  ? 310  LYS B CB  1 
ATOM   4991  C  CG  . LYS B  1 310 ? 80.490  -1.158  -2.150  1.00 12.75 ? 310  LYS B CG  1 
ATOM   4992  C  CD  . LYS B  1 310 ? 79.393  -1.713  -3.096  1.00 13.38 ? 310  LYS B CD  1 
ATOM   4993  C  CE  . LYS B  1 310 ? 79.109  -3.138  -2.779  1.00 19.13 ? 310  LYS B CE  1 
ATOM   4994  N  NZ  . LYS B  1 310 ? 78.327  -3.783  -3.886  1.00 22.29 ? 310  LYS B NZ  1 
ATOM   4995  N  N   . TYR B  1 311 ? 82.173  3.054   -2.888  1.00 6.90  ? 311  TYR B N   1 
ATOM   4996  C  CA  . TYR B  1 311 ? 81.904  4.318   -3.572  1.00 8.58  ? 311  TYR B CA  1 
ATOM   4997  C  C   . TYR B  1 311 ? 82.308  4.185   -5.045  1.00 8.02  ? 311  TYR B C   1 
ATOM   4998  O  O   . TYR B  1 311 ? 83.116  3.345   -5.411  1.00 7.96  ? 311  TYR B O   1 
ATOM   4999  C  CB  . TYR B  1 311 ? 82.648  5.497   -2.899  1.00 8.67  ? 311  TYR B CB  1 
ATOM   5000  C  CG  . TYR B  1 311 ? 84.142  5.344   -3.073  1.00 9.97  ? 311  TYR B CG  1 
ATOM   5001  C  CD1 . TYR B  1 311 ? 84.859  4.497   -2.229  1.00 10.82 ? 311  TYR B CD1 1 
ATOM   5002  C  CD2 . TYR B  1 311 ? 84.827  5.961   -4.146  1.00 10.65 ? 311  TYR B CD2 1 
ATOM   5003  C  CE1 . TYR B  1 311 ? 86.244  4.273   -2.400  1.00 11.80 ? 311  TYR B CE1 1 
ATOM   5004  C  CE2 . TYR B  1 311 ? 86.233  5.731   -4.324  1.00 10.60 ? 311  TYR B CE2 1 
ATOM   5005  C  CZ  . TYR B  1 311 ? 86.915  4.912   -3.437  1.00 11.83 ? 311  TYR B CZ  1 
ATOM   5006  O  OH  . TYR B  1 311 ? 88.252  4.652   -3.561  1.00 10.28 ? 311  TYR B OH  1 
ATOM   5007  N  N   . TYR B  1 312 ? 81.752  5.021   -5.916  1.00 7.29  ? 312  TYR B N   1 
ATOM   5008  C  CA  . TYR B  1 312 ? 82.197  5.021   -7.297  1.00 6.70  ? 312  TYR B CA  1 
ATOM   5009  C  C   . TYR B  1 312 ? 81.795  6.356   -7.898  1.00 7.50  ? 312  TYR B C   1 
ATOM   5010  O  O   . TYR B  1 312 ? 80.886  7.053   -7.369  1.00 6.04  ? 312  TYR B O   1 
ATOM   5011  C  CB  . TYR B  1 312 ? 81.596  3.835   -8.100  1.00 6.32  ? 312  TYR B CB  1 
ATOM   5012  C  CG  . TYR B  1 312 ? 80.082  3.850   -8.247  1.00 7.82  ? 312  TYR B CG  1 
ATOM   5013  C  CD1 . TYR B  1 312 ? 79.458  4.561   -9.297  1.00 9.42  ? 312  TYR B CD1 1 
ATOM   5014  C  CD2 . TYR B  1 312 ? 79.261  3.100   -7.375  1.00 8.25  ? 312  TYR B CD2 1 
ATOM   5015  C  CE1 . TYR B  1 312 ? 78.049  4.572   -9.450  1.00 8.49  ? 312  TYR B CE1 1 
ATOM   5016  C  CE2 . TYR B  1 312 ? 77.879  3.117   -7.525  1.00 10.62 ? 312  TYR B CE2 1 
ATOM   5017  C  CZ  . TYR B  1 312 ? 77.281  3.828   -8.571  1.00 11.76 ? 312  TYR B CZ  1 
ATOM   5018  O  OH  . TYR B  1 312 ? 75.890  3.813   -8.684  1.00 12.89 ? 312  TYR B OH  1 
ATOM   5019  N  N   . SER B  1 313 ? 82.486  6.741   -8.966  1.00 7.01  ? 313  SER B N   1 
ATOM   5020  C  CA  . SER B  1 313 ? 82.100  7.980   -9.612  1.00 8.44  ? 313  SER B CA  1 
ATOM   5021  C  C   . SER B  1 313 ? 81.011  7.751   -10.695 1.00 9.02  ? 313  SER B C   1 
ATOM   5022  O  O   . SER B  1 313 ? 81.235  7.001   -11.624 1.00 8.54  ? 313  SER B O   1 
ATOM   5023  C  CB  . SER B  1 313 ? 83.337  8.658   -10.181 1.00 7.53  ? 313  SER B CB  1 
ATOM   5024  O  OG  . SER B  1 313 ? 82.917  9.853   -10.790 1.00 7.61  ? 313  SER B OG  1 
ATOM   5025  N  N   . GLU B  1 314 ? 79.858  8.413   -10.584 1.00 9.04  ? 314  GLU B N   1 
ATOM   5026  C  CA  . GLU B  1 314 ? 78.961  8.536   -11.713 1.00 10.42 ? 314  GLU B CA  1 
ATOM   5027  C  C   . GLU B  1 314 ? 79.458  9.512   -12.775 1.00 10.39 ? 314  GLU B C   1 
ATOM   5028  O  O   . GLU B  1 314 ? 79.216  9.314   -13.977 1.00 10.71 ? 314  GLU B O   1 
ATOM   5029  C  CB  . GLU B  1 314 ? 77.580  9.048   -11.271 1.00 11.93 ? 314  GLU B CB  1 
ATOM   5030  C  CG  . GLU B  1 314 ? 76.611  7.960   -10.989 1.00 18.32 ? 314  GLU B CG  1 
ATOM   5031  C  CD  . GLU B  1 314 ? 76.334  7.093   -12.210 1.00 25.54 ? 314  GLU B CD  1 
ATOM   5032  O  OE1 . GLU B  1 314 ? 75.828  7.592   -13.242 1.00 27.07 ? 314  GLU B OE1 1 
ATOM   5033  O  OE2 . GLU B  1 314 ? 76.619  5.897   -12.123 1.00 28.90 ? 314  GLU B OE2 1 
ATOM   5034  N  N   . ALA B  1 315 ? 80.103  10.591  -12.344 1.00 9.53  ? 315  ALA B N   1 
ATOM   5035  C  CA  . ALA B  1 315 ? 80.615  11.576  -13.268 1.00 9.37  ? 315  ALA B CA  1 
ATOM   5036  C  C   . ALA B  1 315 ? 81.834  10.995  -13.922 1.00 8.85  ? 315  ALA B C   1 
ATOM   5037  O  O   . ALA B  1 315 ? 82.450  10.095  -13.368 1.00 9.06  ? 315  ALA B O   1 
ATOM   5038  C  CB  . ALA B  1 315 ? 80.977  12.901  -12.539 1.00 9.66  ? 315  ALA B CB  1 
ATOM   5039  N  N   . TYR B  1 316 ? 82.186  11.496  -15.114 1.00 7.49  ? 316  TYR B N   1 
ATOM   5040  C  CA  . TYR B  1 316 ? 83.373  11.007  -15.790 1.00 7.47  ? 316  TYR B CA  1 
ATOM   5041  C  C   . TYR B  1 316 ? 84.664  11.314  -15.043 1.00 7.93  ? 316  TYR B C   1 
ATOM   5042  O  O   . TYR B  1 316 ? 85.686  10.605  -15.214 1.00 9.21  ? 316  TYR B O   1 
ATOM   5043  C  CB  . TYR B  1 316 ? 83.452  11.483  -17.242 1.00 5.57  ? 316  TYR B CB  1 
ATOM   5044  C  CG  . TYR B  1 316 ? 82.390  10.857  -18.158 1.00 6.21  ? 316  TYR B CG  1 
ATOM   5045  C  CD1 . TYR B  1 316 ? 82.273  9.470   -18.273 1.00 4.46  ? 316  TYR B CD1 1 
ATOM   5046  C  CD2 . TYR B  1 316 ? 81.547  11.649  -18.899 1.00 2.71  ? 316  TYR B CD2 1 
ATOM   5047  C  CE1 . TYR B  1 316 ? 81.316  8.872   -19.118 1.00 6.75  ? 316  TYR B CE1 1 
ATOM   5048  C  CE2 . TYR B  1 316 ? 80.553  11.077  -19.722 1.00 2.00  ? 316  TYR B CE2 1 
ATOM   5049  C  CZ  . TYR B  1 316 ? 80.466  9.668   -19.833 1.00 5.66  ? 316  TYR B CZ  1 
ATOM   5050  O  OH  . TYR B  1 316 ? 79.552  9.030   -20.672 1.00 8.29  ? 316  TYR B OH  1 
ATOM   5051  N  N   . PHE B  1 317 ? 84.629  12.347  -14.211 1.00 7.53  ? 317  PHE B N   1 
ATOM   5052  C  CA  . PHE B  1 317 ? 85.771  12.633  -13.355 1.00 6.79  ? 317  PHE B CA  1 
ATOM   5053  C  C   . PHE B  1 317 ? 85.183  13.301  -12.117 1.00 8.00  ? 317  PHE B C   1 
ATOM   5054  O  O   . PHE B  1 317 ? 84.269  14.142  -12.263 1.00 7.94  ? 317  PHE B O   1 
ATOM   5055  C  CB  . PHE B  1 317 ? 86.702  13.575  -14.055 1.00 6.33  ? 317  PHE B CB  1 
ATOM   5056  C  CG  . PHE B  1 317 ? 87.780  14.176  -13.155 1.00 5.83  ? 317  PHE B CG  1 
ATOM   5057  C  CD1 . PHE B  1 317 ? 87.534  15.338  -12.387 1.00 10.40 ? 317  PHE B CD1 1 
ATOM   5058  C  CD2 . PHE B  1 317 ? 89.048  13.634  -13.143 1.00 10.82 ? 317  PHE B CD2 1 
ATOM   5059  C  CE1 . PHE B  1 317 ? 88.560  15.928  -11.585 1.00 7.81  ? 317  PHE B CE1 1 
ATOM   5060  C  CE2 . PHE B  1 317 ? 90.109  14.220  -12.336 1.00 7.88  ? 317  PHE B CE2 1 
ATOM   5061  C  CZ  . PHE B  1 317 ? 89.850  15.327  -11.549 1.00 12.56 ? 317  PHE B CZ  1 
ATOM   5062  N  N   . SER B  1 318 ? 85.606  12.844  -10.933 1.00 6.82  ? 318  SER B N   1 
ATOM   5063  C  CA  . SER B  1 318 ? 85.187  13.445  -9.644  1.00 8.32  ? 318  SER B CA  1 
ATOM   5064  C  C   . SER B  1 318 ? 86.438  13.630  -8.799  1.00 9.05  ? 318  SER B C   1 
ATOM   5065  O  O   . SER B  1 318 ? 87.410  12.880  -9.001  1.00 9.74  ? 318  SER B O   1 
ATOM   5066  C  CB  . SER B  1 318 ? 84.208  12.459  -8.933  1.00 7.66  ? 318  SER B CB  1 
ATOM   5067  O  OG  . SER B  1 318 ? 82.949  12.476  -9.637  1.00 9.22  ? 318  SER B OG  1 
ATOM   5068  N  N   . LYS B  1 319 ? 86.407  14.608  -7.872  1.00 8.56  ? 319  LYS B N   1 
ATOM   5069  C  CA  . LYS B  1 319 ? 87.514  14.841  -6.962  1.00 8.35  ? 319  LYS B CA  1 
ATOM   5070  C  C   . LYS B  1 319 ? 86.860  15.054  -5.629  1.00 7.76  ? 319  LYS B C   1 
ATOM   5071  O  O   . LYS B  1 319 ? 85.926  15.879  -5.517  1.00 6.96  ? 319  LYS B O   1 
ATOM   5072  C  CB  . LYS B  1 319 ? 88.360  16.071  -7.351  1.00 8.14  ? 319  LYS B CB  1 
ATOM   5073  C  CG  . LYS B  1 319 ? 89.556  16.299  -6.441  1.00 7.88  ? 319  LYS B CG  1 
ATOM   5074  C  CD  . LYS B  1 319 ? 90.426  17.588  -6.717  1.00 9.29  ? 319  LYS B CD  1 
ATOM   5075  C  CE  . LYS B  1 319 ? 89.656  18.883  -6.523  1.00 13.73 ? 319  LYS B CE  1 
ATOM   5076  N  NZ  . LYS B  1 319 ? 90.600  20.040  -6.823  1.00 16.06 ? 319  LYS B NZ  1 
ATOM   5077  N  N   . VAL B  1 320 ? 87.344  14.325  -4.629  1.00 6.79  ? 320  VAL B N   1 
ATOM   5078  C  CA  . VAL B  1 320 ? 86.869  14.497  -3.221  1.00 6.49  ? 320  VAL B CA  1 
ATOM   5079  C  C   . VAL B  1 320 ? 88.042  14.839  -2.282  1.00 7.25  ? 320  VAL B C   1 
ATOM   5080  O  O   . VAL B  1 320 ? 89.191  14.466  -2.552  1.00 8.66  ? 320  VAL B O   1 
ATOM   5081  C  CB  . VAL B  1 320 ? 86.145  13.268  -2.688  1.00 5.52  ? 320  VAL B CB  1 
ATOM   5082  C  CG1 . VAL B  1 320 ? 85.034  12.806  -3.671  1.00 5.73  ? 320  VAL B CG1 1 
ATOM   5083  C  CG2 . VAL B  1 320 ? 87.136  12.057  -2.344  1.00 4.96  ? 320  VAL B CG2 1 
ATOM   5084  N  N   . LEU B  1 321 ? 87.740  15.573  -1.215  1.00 5.88  ? 321  LEU B N   1 
ATOM   5085  C  CA  . LEU B  1 321 ? 88.632  15.766  -0.083  1.00 7.32  ? 321  LEU B CA  1 
ATOM   5086  C  C   . LEU B  1 321 ? 88.361  14.630  0.909   1.00 6.58  ? 321  LEU B C   1 
ATOM   5087  O  O   . LEU B  1 321 ? 87.230  14.404  1.292   1.00 7.49  ? 321  LEU B O   1 
ATOM   5088  C  CB  . LEU B  1 321 ? 88.358  17.104  0.593   1.00 8.17  ? 321  LEU B CB  1 
ATOM   5089  C  CG  . LEU B  1 321 ? 89.297  17.384  1.786   1.00 10.75 ? 321  LEU B CG  1 
ATOM   5090  C  CD1 . LEU B  1 321 ? 90.721  17.647  1.287   1.00 8.87  ? 321  LEU B CD1 1 
ATOM   5091  C  CD2 . LEU B  1 321 ? 88.696  18.654  2.420   1.00 7.94  ? 321  LEU B CD2 1 
ATOM   5092  N  N   . PHE B  1 322 ? 89.405  13.938  1.335   1.00 6.83  ? 322  PHE B N   1 
ATOM   5093  C  CA  . PHE B  1 322 ? 89.245  12.661  2.055   1.00 6.70  ? 322  PHE B CA  1 
ATOM   5094  C  C   . PHE B  1 322 ? 90.066  12.714  3.325   1.00 9.03  ? 322  PHE B C   1 
ATOM   5095  O  O   . PHE B  1 322 ? 91.221  13.182  3.309   1.00 8.84  ? 322  PHE B O   1 
ATOM   5096  C  CB  . PHE B  1 322 ? 89.724  11.507  1.188   1.00 8.21  ? 322  PHE B CB  1 
ATOM   5097  C  CG  . PHE B  1 322 ? 89.766  10.223  1.917   1.00 7.29  ? 322  PHE B CG  1 
ATOM   5098  C  CD1 . PHE B  1 322 ? 88.576  9.489   2.085   1.00 8.51  ? 322  PHE B CD1 1 
ATOM   5099  C  CD2 . PHE B  1 322 ? 90.918  9.787   2.527   1.00 11.30 ? 322  PHE B CD2 1 
ATOM   5100  C  CE1 . PHE B  1 322 ? 88.578  8.289   2.838   1.00 8.02  ? 322  PHE B CE1 1 
ATOM   5101  C  CE2 . PHE B  1 322 ? 90.939  8.566   3.294   1.00 9.47  ? 322  PHE B CE2 1 
ATOM   5102  C  CZ  . PHE B  1 322 ? 89.761  7.838   3.430   1.00 9.50  ? 322  PHE B CZ  1 
ATOM   5103  N  N   . VAL B  1 323 ? 89.467  12.288  4.442   1.00 8.85  ? 323  VAL B N   1 
ATOM   5104  C  CA  . VAL B  1 323 ? 90.174  12.277  5.738   1.00 8.89  ? 323  VAL B CA  1 
ATOM   5105  C  C   . VAL B  1 323 ? 89.926  10.924  6.348   1.00 8.80  ? 323  VAL B C   1 
ATOM   5106  O  O   . VAL B  1 323 ? 88.837  10.345  6.208   1.00 8.18  ? 323  VAL B O   1 
ATOM   5107  C  CB  . VAL B  1 323 ? 89.779  13.454  6.689   1.00 9.12  ? 323  VAL B CB  1 
ATOM   5108  C  CG1 . VAL B  1 323 ? 88.259  13.478  7.006   1.00 10.67 ? 323  VAL B CG1 1 
ATOM   5109  C  CG2 . VAL B  1 323 ? 90.622  13.473  8.030   1.00 10.93 ? 323  VAL B CG2 1 
ATOM   5110  N  N   . SER B  1 324 ? 90.969  10.384  6.973   1.00 7.65  ? 324  SER B N   1 
ATOM   5111  C  CA  . SER B  1 324 ? 90.878  9.094   7.633   1.00 7.54  ? 324  SER B CA  1 
ATOM   5112  C  C   . SER B  1 324 ? 91.649  9.071   8.926   1.00 8.18  ? 324  SER B C   1 
ATOM   5113  O  O   . SER B  1 324 ? 92.799  9.536   9.013   1.00 7.97  ? 324  SER B O   1 
ATOM   5114  C  CB  . SER B  1 324 ? 91.436  8.010   6.711   1.00 8.27  ? 324  SER B CB  1 
ATOM   5115  O  OG  . SER B  1 324 ? 91.787  6.867   7.420   1.00 8.77  ? 324  SER B OG  1 
ATOM   5116  N  N   . SER B  1 325 ? 91.025  8.502   9.942   1.00 7.90  ? 325  SER B N   1 
ATOM   5117  C  CA  . SER B  1 325 ? 91.720  8.206   11.176  1.00 9.08  ? 325  SER B CA  1 
ATOM   5118  C  C   . SER B  1 325 ? 92.501  6.874   11.065  1.00 9.43  ? 325  SER B C   1 
ATOM   5119  O  O   . SER B  1 325 ? 91.999  5.885   10.516  1.00 10.46 ? 325  SER B O   1 
ATOM   5120  C  CB  . SER B  1 325 ? 90.695  8.196   12.328  1.00 8.40  ? 325  SER B CB  1 
ATOM   5121  O  OG  . SER B  1 325 ? 91.334  7.852   13.533  1.00 11.07 ? 325  SER B OG  1 
ATOM   5122  N  N   . GLY B  1 326 ? 93.730  6.845   11.575  1.00 10.18 ? 326  GLY B N   1 
ATOM   5123  C  CA  . GLY B  1 326 ? 94.615  5.701   11.371  1.00 10.69 ? 326  GLY B CA  1 
ATOM   5124  C  C   . GLY B  1 326 ? 95.684  6.028   10.317  1.00 12.00 ? 326  GLY B C   1 
ATOM   5125  O  O   . GLY B  1 326 ? 95.612  7.052   9.609   1.00 10.87 ? 326  GLY B O   1 
ATOM   5126  N  N   . SER B  1 327 ? 96.712  5.180   10.204  1.00 11.98 ? 327  SER B N   1 
ATOM   5127  C  CA  . SER B  1 327 ? 97.763  5.471   9.228   1.00 12.96 ? 327  SER B CA  1 
ATOM   5128  C  C   . SER B  1 327 ? 97.564  4.731   7.904   1.00 12.42 ? 327  SER B C   1 
ATOM   5129  O  O   . SER B  1 327 ? 98.323  4.943   6.986   1.00 12.25 ? 327  SER B O   1 
ATOM   5130  C  CB  . SER B  1 327 ? 99.143  5.161   9.776   1.00 13.96 ? 327  SER B CB  1 
ATOM   5131  O  OG  . SER B  1 327 ? 99.164  3.841   10.320  1.00 14.58 ? 327  SER B OG  1 
ATOM   5132  N  N   . ASP B  1 328 ? 96.538  3.895   7.806   1.00 12.43 ? 328  ASP B N   1 
ATOM   5133  C  CA  . ASP B  1 328 ? 96.372  3.054   6.625   1.00 11.33 ? 328  ASP B CA  1 
ATOM   5134  C  C   . ASP B  1 328 ? 94.958  2.989   6.109   1.00 10.88 ? 328  ASP B C   1 
ATOM   5135  O  O   . ASP B  1 328 ? 94.455  1.932   5.727   1.00 10.06 ? 328  ASP B O   1 
ATOM   5136  C  CB  . ASP B  1 328 ? 96.890  1.662   6.947   1.00 13.23 ? 328  ASP B CB  1 
ATOM   5137  C  CG  . ASP B  1 328 ? 98.387  1.676   7.154   1.00 19.47 ? 328  ASP B CG  1 
ATOM   5138  O  OD1 . ASP B  1 328 ? 99.129  1.575   6.123   1.00 25.65 ? 328  ASP B OD1 1 
ATOM   5139  O  OD2 . ASP B  1 328 ? 98.894  1.882   8.281   1.00 23.38 ? 328  ASP B OD2 1 
ATOM   5140  N  N   . GLY B  1 329 ? 94.298  4.128   6.066   1.00 8.64  ? 329  GLY B N   1 
ATOM   5141  C  CA  . GLY B  1 329 ? 92.954  4.134   5.524   1.00 8.83  ? 329  GLY B CA  1 
ATOM   5142  C  C   . GLY B  1 329 ? 92.934  4.167   3.985   1.00 9.83  ? 329  GLY B C   1 
ATOM   5143  O  O   . GLY B  1 329 ? 93.961  3.974   3.318   1.00 10.55 ? 329  GLY B O   1 
ATOM   5144  N  N   . LEU B  1 330 ? 91.759  4.373   3.409   1.00 9.64  ? 330  LEU B N   1 
ATOM   5145  C  CA  . LEU B  1 330 ? 91.592  4.257   1.958   1.00 8.61  ? 330  LEU B CA  1 
ATOM   5146  C  C   . LEU B  1 330 ? 92.681  4.984   1.103   1.00 9.33  ? 330  LEU B C   1 
ATOM   5147  O  O   . LEU B  1 330 ? 93.214  4.395   0.166   1.00 8.97  ? 330  LEU B O   1 
ATOM   5148  C  CB  . LEU B  1 330 ? 90.222  4.819   1.586   1.00 9.91  ? 330  LEU B CB  1 
ATOM   5149  C  CG  . LEU B  1 330 ? 89.896  4.761   0.077   1.00 7.29  ? 330  LEU B CG  1 
ATOM   5150  C  CD1 . LEU B  1 330 ? 89.701  3.256   -0.408  1.00 4.79  ? 330  LEU B CD1 1 
ATOM   5151  C  CD2 . LEU B  1 330 ? 88.662  5.619   -0.245  1.00 5.65  ? 330  LEU B CD2 1 
ATOM   5152  N  N   . ASP B  1 331 ? 93.001  6.247   1.415   1.00 8.48  ? 331  ASP B N   1 
ATOM   5153  C  CA  . ASP B  1 331 ? 93.962  6.974   0.574   1.00 9.93  ? 331  ASP B CA  1 
ATOM   5154  C  C   . ASP B  1 331 ? 95.342  6.316   0.536   1.00 9.65  ? 331  ASP B C   1 
ATOM   5155  O  O   . ASP B  1 331 ? 95.890  6.090   -0.559  1.00 9.44  ? 331  ASP B O   1 
ATOM   5156  C  CB  . ASP B  1 331 ? 94.007  8.515   0.838   1.00 9.67  ? 331  ASP B CB  1 
ATOM   5157  C  CG  . ASP B  1 331 ? 94.379  8.906   2.283   1.00 11.36 ? 331  ASP B CG  1 
ATOM   5158  O  OD1 . ASP B  1 331 ? 94.430  8.066   3.219   1.00 9.17  ? 331  ASP B OD1 1 
ATOM   5159  O  OD2 . ASP B  1 331 ? 94.653  10.095  2.570   1.00 12.58 ? 331  ASP B OD2 1 
ATOM   5160  N  N   . GLN B  1 332 ? 95.889  6.027   1.709   1.00 9.29  ? 332  GLN B N   1 
ATOM   5161  C  CA  . GLN B  1 332 ? 97.172  5.332   1.850   1.00 10.68 ? 332  GLN B CA  1 
ATOM   5162  C  C   . GLN B  1 332 ? 97.107  3.954   1.198   1.00 10.03 ? 332  GLN B C   1 
ATOM   5163  O  O   . GLN B  1 332 ? 98.073  3.489   0.583   1.00 9.87  ? 332  GLN B O   1 
ATOM   5164  C  CB  . GLN B  1 332 ? 97.555  5.199   3.344   1.00 11.01 ? 332  GLN B CB  1 
ATOM   5165  C  CG  . GLN B  1 332 ? 99.036  4.899   3.611   1.00 16.88 ? 332  GLN B CG  1 
ATOM   5166  C  CD  . GLN B  1 332 ? 99.956  5.961   3.012   1.00 21.45 ? 332  GLN B CD  1 
ATOM   5167  O  OE1 . GLN B  1 332 ? 100.859 5.648   2.231   1.00 26.07 ? 332  GLN B OE1 1 
ATOM   5168  N  NE2 . GLN B  1 332 ? 99.695  7.210   3.338   1.00 23.28 ? 332  GLN B NE2 1 
ATOM   5169  N  N   . ASN B  1 333 ? 95.946  3.318   1.290   1.00 9.52  ? 333  ASN B N   1 
ATOM   5170  C  CA  . ASN B  1 333 ? 95.797  2.008   0.651   1.00 9.50  ? 333  ASN B CA  1 
ATOM   5171  C  C   . ASN B  1 333 ? 95.958  2.101   -0.892  1.00 7.72  ? 333  ASN B C   1 
ATOM   5172  O  O   . ASN B  1 333 ? 96.703  1.344   -1.505  1.00 6.99  ? 333  ASN B O   1 
ATOM   5173  C  CB  . ASN B  1 333 ? 94.454  1.395   1.054   1.00 10.51 ? 333  ASN B CB  1 
ATOM   5174  C  CG  . ASN B  1 333 ? 94.291  -0.003  0.537   1.00 12.58 ? 333  ASN B CG  1 
ATOM   5175  O  OD1 . ASN B  1 333 ? 94.139  -0.204  -0.671  1.00 15.60 ? 333  ASN B OD1 1 
ATOM   5176  N  ND2 . ASN B  1 333 ? 94.324  -0.978  1.431   1.00 13.81 ? 333  ASN B ND2 1 
ATOM   5177  N  N   . LEU B  1 334 ? 95.267  3.050   -1.498  1.00 6.00  ? 334  LEU B N   1 
ATOM   5178  C  CA  . LEU B  1 334 ? 95.327  3.276   -2.938  1.00 7.10  ? 334  LEU B CA  1 
ATOM   5179  C  C   . LEU B  1 334 ? 96.732  3.713   -3.317  1.00 6.87  ? 334  LEU B C   1 
ATOM   5180  O  O   . LEU B  1 334 ? 97.263  3.233   -4.328  1.00 7.49  ? 334  LEU B O   1 
ATOM   5181  C  CB  . LEU B  1 334 ? 94.275  4.357   -3.383  1.00 4.94  ? 334  LEU B CB  1 
ATOM   5182  C  CG  . LEU B  1 334 ? 92.798  3.930   -3.148  1.00 7.13  ? 334  LEU B CG  1 
ATOM   5183  C  CD1 . LEU B  1 334 ? 91.854  5.090   -3.338  1.00 5.69  ? 334  LEU B CD1 1 
ATOM   5184  C  CD2 . LEU B  1 334 ? 92.300  2.732   -3.990  1.00 12.44 ? 334  LEU B CD2 1 
ATOM   5185  N  N   . VAL B  1 335 ? 97.344  4.588   -2.511  1.00 7.41  ? 335  VAL B N   1 
ATOM   5186  C  CA  . VAL B  1 335 ? 98.737  4.995   -2.787  1.00 7.46  ? 335  VAL B CA  1 
ATOM   5187  C  C   . VAL B  1 335 ? 99.679  3.767   -2.803  1.00 8.10  ? 335  VAL B C   1 
ATOM   5188  O  O   . VAL B  1 335 ? 100.475 3.556   -3.744  1.00 9.51  ? 335  VAL B O   1 
ATOM   5189  C  CB  . VAL B  1 335 ? 99.268  6.022   -1.741  1.00 6.24  ? 335  VAL B CB  1 
ATOM   5190  C  CG1 . VAL B  1 335 ? 100.845 6.131   -1.844  1.00 7.79  ? 335  VAL B CG1 1 
ATOM   5191  C  CG2 . VAL B  1 335 ? 98.612  7.338   -1.888  1.00 7.57  ? 335  VAL B CG2 1 
ATOM   5192  N  N   . ASN B  1 336 ? 99.593  2.948   -1.769  1.00 8.27  ? 336  ASN B N   1 
ATOM   5193  C  CA  . ASN B  1 336 ? 100.472 1.770   -1.655  1.00 9.22  ? 336  ASN B CA  1 
ATOM   5194  C  C   . ASN B  1 336 ? 100.230 0.778   -2.827  1.00 9.21  ? 336  ASN B C   1 
ATOM   5195  O  O   . ASN B  1 336 ? 101.138 0.051   -3.281  1.00 6.94  ? 336  ASN B O   1 
ATOM   5196  C  CB  . ASN B  1 336 ? 100.227 1.071   -0.319  1.00 10.13 ? 336  ASN B CB  1 
ATOM   5197  C  CG  . ASN B  1 336 ? 100.816 1.828   0.865   1.00 13.70 ? 336  ASN B CG  1 
ATOM   5198  O  OD1 . ASN B  1 336 ? 101.575 2.796   0.700   1.00 19.42 ? 336  ASN B OD1 1 
ATOM   5199  N  ND2 . ASN B  1 336 ? 100.489 1.377   2.068   1.00 13.03 ? 336  ASN B ND2 1 
ATOM   5200  N  N   . GLY B  1 337 ? 98.996  0.734   -3.312  1.00 7.93  ? 337  GLY B N   1 
ATOM   5201  C  CA  . GLY B  1 337 ? 98.684  -0.163  -4.431  1.00 7.37  ? 337  GLY B CA  1 
ATOM   5202  C  C   . GLY B  1 337 ? 98.867  0.532   -5.804  1.00 7.35  ? 337  GLY B C   1 
ATOM   5203  O  O   . GLY B  1 337 ? 98.573  -0.036  -6.839  1.00 8.20  ? 337  GLY B O   1 
ATOM   5204  N  N   . GLY B  1 338 ? 99.352  1.759   -5.827  1.00 7.13  ? 338  GLY B N   1 
ATOM   5205  C  CA  . GLY B  1 338 ? 99.549  2.446   -7.096  1.00 7.33  ? 338  GLY B CA  1 
ATOM   5206  C  C   . GLY B  1 338 ? 101.021 2.830   -7.259  1.00 7.04  ? 338  GLY B C   1 
ATOM   5207  O  O   . GLY B  1 338 ? 101.903 2.253   -6.593  1.00 4.03  ? 338  GLY B O   1 
ATOM   5208  N  N   . GLU B  1 339 ? 101.273 3.828   -8.108  1.00 6.63  ? 339  GLU B N   1 
ATOM   5209  C  CA  . GLU B  1 339 ? 102.652 4.280   -8.477  1.00 6.27  ? 339  GLU B CA  1 
ATOM   5210  C  C   . GLU B  1 339 ? 102.633 5.814   -8.580  1.00 6.74  ? 339  GLU B C   1 
ATOM   5211  O  O   . GLU B  1 339 ? 101.593 6.376   -8.859  1.00 6.28  ? 339  GLU B O   1 
ATOM   5212  C  CB  . GLU B  1 339 ? 103.052 3.744   -9.836  1.00 6.25  ? 339  GLU B CB  1 
ATOM   5213  C  CG  . GLU B  1 339 ? 102.988 2.225   -10.023 1.00 9.25  ? 339  GLU B CG  1 
ATOM   5214  C  CD  . GLU B  1 339 ? 103.905 1.471   -9.105  1.00 8.54  ? 339  GLU B CD  1 
ATOM   5215  O  OE1 . GLU B  1 339 ? 104.845 2.070   -8.573  1.00 10.59 ? 339  GLU B OE1 1 
ATOM   5216  O  OE2 . GLU B  1 339 ? 103.672 0.244   -8.926  1.00 10.86 ? 339  GLU B OE2 1 
ATOM   5217  N  N   . GLU B  1 340 ? 103.768 6.473   -8.340  1.00 5.69  ? 340  GLU B N   1 
ATOM   5218  C  CA  . GLU B  1 340 ? 103.881 7.926   -8.495  1.00 6.37  ? 340  GLU B CA  1 
ATOM   5219  C  C   . GLU B  1 340 ? 103.459 8.319   -9.897  1.00 5.56  ? 340  GLU B C   1 
ATOM   5220  O  O   . GLU B  1 340 ? 103.752 7.602   -10.868 1.00 5.77  ? 340  GLU B O   1 
ATOM   5221  C  CB  . GLU B  1 340 ? 105.333 8.375   -8.245  1.00 6.47  ? 340  GLU B CB  1 
ATOM   5222  C  CG  . GLU B  1 340 ? 105.578 8.782   -6.818  1.00 9.89  ? 340  GLU B CG  1 
ATOM   5223  C  CD  . GLU B  1 340 ? 107.001 9.240   -6.543  1.00 15.20 ? 340  GLU B CD  1 
ATOM   5224  O  OE1 . GLU B  1 340 ? 107.815 9.300   -7.499  1.00 13.58 ? 340  GLU B OE1 1 
ATOM   5225  O  OE2 . GLU B  1 340 ? 107.290 9.507   -5.330  1.00 17.15 ? 340  GLU B OE2 1 
ATOM   5226  N  N   . TRP B  1 341 ? 102.778 9.449   -9.987  1.00 5.17  ? 341  TRP B N   1 
ATOM   5227  C  CA  . TRP B  1 341 ? 102.070 9.865   -11.202 1.00 5.48  ? 341  TRP B CA  1 
ATOM   5228  C  C   . TRP B  1 341 ? 102.232 11.369  -11.331 1.00 7.14  ? 341  TRP B C   1 
ATOM   5229  O  O   . TRP B  1 341 ? 102.092 12.087  -10.365 1.00 7.06  ? 341  TRP B O   1 
ATOM   5230  C  CB  . TRP B  1 341 ? 100.580 9.575   -11.049 1.00 3.17  ? 341  TRP B CB  1 
ATOM   5231  C  CG  . TRP B  1 341 ? 99.753  9.858   -12.294 1.00 4.90  ? 341  TRP B CG  1 
ATOM   5232  C  CD1 . TRP B  1 341 ? 98.646  10.668  -12.354 1.00 8.28  ? 341  TRP B CD1 1 
ATOM   5233  C  CD2 . TRP B  1 341 ? 99.908  9.305   -13.592 1.00 7.45  ? 341  TRP B CD2 1 
ATOM   5234  N  NE1 . TRP B  1 341 ? 98.135  10.689  -13.621 1.00 4.74  ? 341  TRP B NE1 1 
ATOM   5235  C  CE2 . TRP B  1 341 ? 98.874  9.851   -14.405 1.00 8.02  ? 341  TRP B CE2 1 
ATOM   5236  C  CE3 . TRP B  1 341 ? 100.801 8.376   -14.168 1.00 8.79  ? 341  TRP B CE3 1 
ATOM   5237  C  CZ2 . TRP B  1 341 ? 98.714  9.521   -15.749 1.00 8.04  ? 341  TRP B CZ2 1 
ATOM   5238  C  CZ3 . TRP B  1 341 ? 100.659 8.065   -15.507 1.00 11.42 ? 341  TRP B CZ3 1 
ATOM   5239  C  CH2 . TRP B  1 341 ? 99.617  8.663   -16.297 1.00 7.77  ? 341  TRP B CH2 1 
ATOM   5240  N  N   . SER B  1 342 ? 102.452 11.842  -12.547 1.00 7.60  ? 342  SER B N   1 
ATOM   5241  C  CA  . SER B  1 342 ? 102.770 13.236  -12.731 1.00 9.80  ? 342  SER B CA  1 
ATOM   5242  C  C   . SER B  1 342 ? 101.618 14.149  -13.216 1.00 10.32 ? 342  SER B C   1 
ATOM   5243  O  O   . SER B  1 342 ? 101.885 15.276  -13.608 1.00 13.45 ? 342  SER B O   1 
ATOM   5244  C  CB  . SER B  1 342 ? 103.944 13.317  -13.710 1.00 10.52 ? 342  SER B CB  1 
ATOM   5245  O  OG  A SER B  1 342 ? 105.141 12.991  -13.003 0.50 10.93 ? 342  SER B OG  1 
ATOM   5246  O  OG  B SER B  1 342 ? 103.542 12.821  -14.997 0.50 9.02  ? 342  SER B OG  1 
ATOM   5247  N  N   . SER B  1 343 ? 100.375 13.682  -13.200 1.00 8.89  ? 343  SER B N   1 
ATOM   5248  C  CA  . SER B  1 343 ? 99.269  14.434  -13.795 1.00 8.00  ? 343  SER B CA  1 
ATOM   5249  C  C   . SER B  1 343 ? 98.073  14.441  -12.917 1.00 8.36  ? 343  SER B C   1 
ATOM   5250  O  O   . SER B  1 343 ? 97.806  13.456  -12.203 1.00 9.30  ? 343  SER B O   1 
ATOM   5251  C  CB  . SER B  1 343 ? 98.845  13.821  -15.159 1.00 8.31  ? 343  SER B CB  1 
ATOM   5252  O  OG  . SER B  1 343 ? 97.891  14.679  -15.805 1.00 11.15 ? 343  SER B OG  1 
ATOM   5253  N  N   . VAL B  1 344 ? 97.258  15.491  -13.033 1.00 8.54  ? 344  VAL B N   1 
ATOM   5254  C  CA  . VAL B  1 344 ? 95.947  15.465  -12.397 1.00 6.79  ? 344  VAL B CA  1 
ATOM   5255  C  C   . VAL B  1 344 ? 94.946  14.653  -13.185 1.00 7.72  ? 344  VAL B C   1 
ATOM   5256  O  O   . VAL B  1 344 ? 93.803  14.424  -12.673 1.00 9.24  ? 344  VAL B O   1 
ATOM   5257  C  CB  . VAL B  1 344 ? 95.393  16.941  -12.163 1.00 8.25  ? 344  VAL B CB  1 
ATOM   5258  C  CG1 . VAL B  1 344 ? 96.338  17.712  -11.144 1.00 7.39  ? 344  VAL B CG1 1 
ATOM   5259  C  CG2 . VAL B  1 344 ? 95.304  17.690  -13.505 1.00 6.49  ? 344  VAL B CG2 1 
ATOM   5260  N  N   . SER B  1 345 ? 95.307  14.295  -14.422 1.00 7.74  ? 345  SER B N   1 
ATOM   5261  C  CA  . SER B  1 345 ? 94.427  13.554  -15.323 1.00 7.78  ? 345  SER B CA  1 
ATOM   5262  C  C   . SER B  1 345 ? 94.918  12.131  -15.373 1.00 7.50  ? 345  SER B C   1 
ATOM   5263  O  O   . SER B  1 345 ? 96.127  11.903  -15.192 1.00 8.03  ? 345  SER B O   1 
ATOM   5264  C  CB  . SER B  1 345 ? 94.573  14.155  -16.727 1.00 10.20 ? 345  SER B CB  1 
ATOM   5265  O  OG  . SER B  1 345 ? 93.564  15.155  -16.859 1.00 10.06 ? 345  SER B OG  1 
ATOM   5266  N  N   . PHE B  1 346 ? 94.005  11.172  -15.585 1.00 7.98  ? 346  PHE B N   1 
ATOM   5267  C  CA  . PHE B  1 346 ? 94.370  9.747   -15.662 1.00 6.92  ? 346  PHE B CA  1 
ATOM   5268  C  C   . PHE B  1 346 ? 94.574  9.377   -17.096 1.00 6.29  ? 346  PHE B C   1 
ATOM   5269  O  O   . PHE B  1 346 ? 94.318  10.201  -17.968 1.00 7.60  ? 346  PHE B O   1 
ATOM   5270  C  CB  . PHE B  1 346 ? 93.378  8.824   -14.905 1.00 6.34  ? 346  PHE B CB  1 
ATOM   5271  C  CG  . PHE B  1 346 ? 91.938  9.191   -15.114 1.00 8.36  ? 346  PHE B CG  1 
ATOM   5272  C  CD1 . PHE B  1 346 ? 91.300  8.880   -16.318 1.00 8.68  ? 346  PHE B CD1 1 
ATOM   5273  C  CD2 . PHE B  1 346 ? 91.237  9.886   -14.117 1.00 6.91  ? 346  PHE B CD2 1 
ATOM   5274  C  CE1 . PHE B  1 346 ? 89.924  9.217   -16.526 1.00 8.55  ? 346  PHE B CE1 1 
ATOM   5275  C  CE2 . PHE B  1 346 ? 89.901  10.290  -14.344 1.00 6.29  ? 346  PHE B CE2 1 
ATOM   5276  C  CZ  . PHE B  1 346 ? 89.251  9.963   -15.537 1.00 6.87  ? 346  PHE B CZ  1 
ATOM   5277  N  N   . PRO B  1 347 ? 95.155  8.209   -17.379 1.00 7.33  ? 347  PRO B N   1 
ATOM   5278  C  CA  . PRO B  1 347 ? 95.405  7.832   -18.771 1.00 7.45  ? 347  PRO B CA  1 
ATOM   5279  C  C   . PRO B  1 347 ? 94.108  7.813   -19.605 1.00 7.49  ? 347  PRO B C   1 
ATOM   5280  O  O   . PRO B  1 347 ? 93.002  7.545   -19.084 1.00 6.55  ? 347  PRO B O   1 
ATOM   5281  C  CB  . PRO B  1 347 ? 96.002  6.417   -18.651 1.00 8.23  ? 347  PRO B CB  1 
ATOM   5282  C  CG  . PRO B  1 347 ? 96.707  6.451   -17.287 1.00 7.17  ? 347  PRO B CG  1 
ATOM   5283  C  CD  . PRO B  1 347 ? 95.661  7.183   -16.450 1.00 5.44  ? 347  PRO B CD  1 
ATOM   5284  N  N   . ALA B  1 348 ? 94.267  8.111   -20.899 1.00 7.08  ? 348  ALA B N   1 
ATOM   5285  C  CA  . ALA B  1 348 ? 93.127  8.138   -21.836 1.00 5.84  ? 348  ALA B CA  1 
ATOM   5286  C  C   . ALA B  1 348 ? 92.648  6.717   -22.215 1.00 6.41  ? 348  ALA B C   1 
ATOM   5287  O  O   . ALA B  1 348 ? 91.543  6.582   -22.753 1.00 7.69  ? 348  ALA B O   1 
ATOM   5288  C  CB  . ALA B  1 348 ? 93.494  8.891   -23.083 1.00 5.90  ? 348  ALA B CB  1 
ATOM   5289  N  N   . ASP B  1 349 ? 93.458  5.678   -21.934 1.00 6.70  ? 349  ASP B N   1 
ATOM   5290  C  CA  . ASP B  1 349 ? 93.082  4.300   -22.203 1.00 7.42  ? 349  ASP B CA  1 
ATOM   5291  C  C   . ASP B  1 349 ? 93.073  3.472   -20.943 1.00 8.44  ? 349  ASP B C   1 
ATOM   5292  O  O   . ASP B  1 349 ? 93.915  3.655   -20.076 1.00 7.80  ? 349  ASP B O   1 
ATOM   5293  C  CB  . ASP B  1 349 ? 94.046  3.607   -23.173 1.00 7.81  ? 349  ASP B CB  1 
ATOM   5294  C  CG  . ASP B  1 349 ? 94.292  4.419   -24.410 1.00 13.16 ? 349  ASP B CG  1 
ATOM   5295  O  OD1 . ASP B  1 349 ? 93.340  4.576   -25.203 1.00 14.52 ? 349  ASP B OD1 1 
ATOM   5296  O  OD2 . ASP B  1 349 ? 95.390  4.975   -24.643 1.00 19.83 ? 349  ASP B OD2 1 
ATOM   5297  N  N   . TRP B  1 350 ? 92.194  2.476   -20.905 1.00 9.71  ? 350  TRP B N   1 
ATOM   5298  C  CA  . TRP B  1 350 ? 92.149  1.577   -19.749 1.00 11.42 ? 350  TRP B CA  1 
ATOM   5299  C  C   . TRP B  1 350 ? 93.384  0.635   -19.758 1.00 12.70 ? 350  TRP B C   1 
ATOM   5300  O  O   . TRP B  1 350 ? 93.976  0.395   -20.816 1.00 13.05 ? 350  TRP B O   1 
ATOM   5301  C  CB  . TRP B  1 350 ? 90.855  0.723   -19.723 1.00 10.57 ? 350  TRP B CB  1 
ATOM   5302  C  CG  . TRP B  1 350 ? 89.576  1.516   -19.687 1.00 9.66  ? 350  TRP B CG  1 
ATOM   5303  C  CD1 . TRP B  1 350 ? 88.639  1.606   -20.673 1.00 12.48 ? 350  TRP B CD1 1 
ATOM   5304  C  CD2 . TRP B  1 350 ? 89.123  2.340   -18.626 1.00 9.46  ? 350  TRP B CD2 1 
ATOM   5305  N  NE1 . TRP B  1 350 ? 87.632  2.463   -20.288 1.00 9.95  ? 350  TRP B NE1 1 
ATOM   5306  C  CE2 . TRP B  1 350 ? 87.916  2.935   -19.037 1.00 11.57 ? 350  TRP B CE2 1 
ATOM   5307  C  CE3 . TRP B  1 350 ? 89.641  2.676   -17.362 1.00 11.49 ? 350  TRP B CE3 1 
ATOM   5308  C  CZ2 . TRP B  1 350 ? 87.192  3.808   -18.222 1.00 11.66 ? 350  TRP B CZ2 1 
ATOM   5309  C  CZ3 . TRP B  1 350 ? 88.941  3.558   -16.570 1.00 10.16 ? 350  TRP B CZ3 1 
ATOM   5310  C  CH2 . TRP B  1 350 ? 87.716  4.100   -16.994 1.00 11.95 ? 350  TRP B CH2 1 
ATOM   5311  O  OXT . TRP B  1 350 ? 93.724  0.116   -18.694 1.00 12.26 ? 350  TRP B OXT 1 
ATOM   5312  N  N   . SER C  1 3   ? 78.658  39.056  35.195  1.00 31.07 ? 3    SER C N   1 
ATOM   5313  C  CA  . SER C  1 3   ? 77.206  38.863  34.870  1.00 31.14 ? 3    SER C CA  1 
ATOM   5314  C  C   . SER C  1 3   ? 76.494  38.348  36.104  1.00 30.10 ? 3    SER C C   1 
ATOM   5315  O  O   . SER C  1 3   ? 76.043  39.130  36.946  1.00 30.85 ? 3    SER C O   1 
ATOM   5316  C  CB  . SER C  1 3   ? 77.009  37.926  33.666  1.00 31.54 ? 3    SER C CB  1 
ATOM   5317  O  OG  . SER C  1 3   ? 76.663  38.706  32.517  1.00 33.56 ? 3    SER C OG  1 
ATOM   5318  N  N   . SER C  1 4   ? 76.380  37.033  36.227  1.00 27.71 ? 4    SER C N   1 
ATOM   5319  C  CA  . SER C  1 4   ? 76.198  36.488  37.568  1.00 25.14 ? 4    SER C CA  1 
ATOM   5320  C  C   . SER C  1 4   ? 77.069  35.270  37.707  1.00 22.16 ? 4    SER C C   1 
ATOM   5321  O  O   . SER C  1 4   ? 77.109  34.413  36.766  1.00 20.76 ? 4    SER C O   1 
ATOM   5322  C  CB  . SER C  1 4   ? 74.743  36.126  37.902  1.00 25.69 ? 4    SER C CB  1 
ATOM   5323  O  OG  . SER C  1 4   ? 74.627  35.804  39.309  1.00 29.63 ? 4    SER C OG  1 
ATOM   5324  N  N   . LEU C  1 5   ? 77.719  35.181  38.868  1.00 17.91 ? 5    LEU C N   1 
ATOM   5325  C  CA  . LEU C  1 5   ? 78.289  33.897  39.299  1.00 15.64 ? 5    LEU C CA  1 
ATOM   5326  C  C   . LEU C  1 5   ? 77.301  32.710  39.146  1.00 12.51 ? 5    LEU C C   1 
ATOM   5327  O  O   . LEU C  1 5   ? 77.718  31.636  38.774  1.00 11.45 ? 5    LEU C O   1 
ATOM   5328  C  CB  . LEU C  1 5   ? 78.808  33.956  40.730  1.00 15.62 ? 5    LEU C CB  1 
ATOM   5329  C  CG  . LEU C  1 5   ? 79.750  32.843  41.298  1.00 15.63 ? 5    LEU C CG  1 
ATOM   5330  C  CD1 . LEU C  1 5   ? 81.073  32.582  40.474  1.00 16.30 ? 5    LEU C CD1 1 
ATOM   5331  C  CD2 . LEU C  1 5   ? 80.179  33.156  42.748  1.00 19.09 ? 5    LEU C CD2 1 
ATOM   5332  N  N   . ILE C  1 6   ? 76.025  32.909  39.480  1.00 9.97  ? 6    ILE C N   1 
ATOM   5333  C  CA  . ILE C  1 6   ? 75.055  31.810  39.432  1.00 9.84  ? 6    ILE C CA  1 
ATOM   5334  C  C   . ILE C  1 6   ? 74.568  31.599  38.007  1.00 9.23  ? 6    ILE C C   1 
ATOM   5335  O  O   . ILE C  1 6   ? 74.238  32.575  37.321  1.00 10.06 ? 6    ILE C O   1 
ATOM   5336  C  CB  . ILE C  1 6   ? 73.877  32.043  40.413  1.00 10.35 ? 6    ILE C CB  1 
ATOM   5337  C  CG1 . ILE C  1 6   ? 74.391  31.869  41.858  1.00 13.27 ? 6    ILE C CG1 1 
ATOM   5338  C  CG2 . ILE C  1 6   ? 72.718  30.955  40.164  1.00 10.59 ? 6    ILE C CG2 1 
ATOM   5339  C  CD1 . ILE C  1 6   ? 73.872  32.808  42.832  1.00 19.14 ? 6    ILE C CD1 1 
ATOM   5340  N  N   . VAL C  1 7   ? 74.566  30.337  37.566  1.00 7.38  ? 7    VAL C N   1 
ATOM   5341  C  CA  . VAL C  1 7   ? 74.149  29.972  36.222  1.00 7.16  ? 7    VAL C CA  1 
ATOM   5342  C  C   . VAL C  1 7   ? 73.112  28.824  36.334  1.00 8.25  ? 7    VAL C C   1 
ATOM   5343  O  O   . VAL C  1 7   ? 73.126  28.072  37.295  1.00 8.49  ? 7    VAL C O   1 
ATOM   5344  C  CB  . VAL C  1 7   ? 75.348  29.525  35.343  1.00 6.84  ? 7    VAL C CB  1 
ATOM   5345  C  CG1 . VAL C  1 7   ? 76.338  30.693  35.146  1.00 6.44  ? 7    VAL C CG1 1 
ATOM   5346  C  CG2 . VAL C  1 7   ? 76.049  28.358  35.953  1.00 6.30  ? 7    VAL C CG2 1 
ATOM   5347  N  N   . GLU C  1 8   ? 72.218  28.699  35.361  1.00 8.01  ? 8    GLU C N   1 
ATOM   5348  C  CA  . GLU C  1 8   ? 71.217  27.630  35.412  1.00 6.95  ? 8    GLU C CA  1 
ATOM   5349  C  C   . GLU C  1 8   ? 71.625  26.341  34.663  1.00 7.63  ? 8    GLU C C   1 
ATOM   5350  O  O   . GLU C  1 8   ? 71.022  25.267  34.883  1.00 6.85  ? 8    GLU C O   1 
ATOM   5351  C  CB  . GLU C  1 8   ? 69.900  28.172  34.832  1.00 8.50  ? 8    GLU C CB  1 
ATOM   5352  C  CG  A GLU C  1 8   ? 68.789  27.171  34.824  0.50 7.18  ? 8    GLU C CG  1 
ATOM   5353  C  CG  B GLU C  1 8   ? 69.317  29.397  35.527  0.50 8.12  ? 8    GLU C CG  1 
ATOM   5354  C  CD  A GLU C  1 8   ? 68.209  26.900  36.200  0.50 6.33  ? 8    GLU C CD  1 
ATOM   5355  C  CD  B GLU C  1 8   ? 68.983  29.184  36.998  0.50 11.68 ? 8    GLU C CD  1 
ATOM   5356  O  OE1 A GLU C  1 8   ? 68.469  27.673  37.158  0.50 4.40  ? 8    GLU C OE1 1 
ATOM   5357  O  OE1 B GLU C  1 8   ? 68.617  28.048  37.375  0.50 8.99  ? 8    GLU C OE1 1 
ATOM   5358  O  OE2 A GLU C  1 8   ? 67.478  25.936  36.271  0.50 2.00  ? 8    GLU C OE2 1 
ATOM   5359  O  OE2 B GLU C  1 8   ? 69.096  30.166  37.793  0.50 10.03 ? 8    GLU C OE2 1 
ATOM   5360  N  N   . ASP C  1 9   ? 72.575  26.474  33.736  1.00 7.14  ? 9    ASP C N   1 
ATOM   5361  C  CA  . ASP C  1 9   ? 73.234  25.321  33.075  1.00 8.34  ? 9    ASP C CA  1 
ATOM   5362  C  C   . ASP C  1 9   ? 74.727  25.528  33.157  1.00 7.73  ? 9    ASP C C   1 
ATOM   5363  O  O   . ASP C  1 9   ? 75.151  26.675  33.190  1.00 7.34  ? 9    ASP C O   1 
ATOM   5364  C  CB  . ASP C  1 9   ? 72.823  25.268  31.621  1.00 8.05  ? 9    ASP C CB  1 
ATOM   5365  C  CG  . ASP C  1 9   ? 71.341  25.071  31.469  1.00 11.34 ? 9    ASP C CG  1 
ATOM   5366  O  OD1 . ASP C  1 9   ? 70.593  26.077  31.461  1.00 9.86  ? 9    ASP C OD1 1 
ATOM   5367  O  OD2 . ASP C  1 9   ? 70.851  23.924  31.445  1.00 8.61  ? 9    ASP C OD2 1 
ATOM   5368  N  N   . ALA C  1 10  ? 75.525  24.454  33.149  1.00 8.72  ? 10   ALA C N   1 
ATOM   5369  C  CA  . ALA C  1 10  ? 76.990  24.638  33.147  1.00 8.31  ? 10   ALA C CA  1 
ATOM   5370  C  C   . ALA C  1 10  ? 77.348  25.515  31.929  1.00 8.18  ? 10   ALA C C   1 
ATOM   5371  O  O   . ALA C  1 10  ? 76.828  25.293  30.857  1.00 7.53  ? 10   ALA C O   1 
ATOM   5372  C  CB  . ALA C  1 10  ? 77.713  23.330  33.040  1.00 8.46  ? 10   ALA C CB  1 
ATOM   5373  N  N   . PRO C  1 11  ? 78.211  26.508  32.096  1.00 8.07  ? 11   PRO C N   1 
ATOM   5374  C  CA  . PRO C  1 11  ? 78.660  27.355  30.977  1.00 7.84  ? 11   PRO C CA  1 
ATOM   5375  C  C   . PRO C  1 11  ? 79.288  26.549  29.846  1.00 7.60  ? 11   PRO C C   1 
ATOM   5376  O  O   . PRO C  1 11  ? 79.739  25.434  30.078  1.00 8.40  ? 11   PRO C O   1 
ATOM   5377  C  CB  . PRO C  1 11  ? 79.756  28.235  31.600  1.00 7.56  ? 11   PRO C CB  1 
ATOM   5378  C  CG  . PRO C  1 11  ? 79.378  28.317  33.029  1.00 7.45  ? 11   PRO C CG  1 
ATOM   5379  C  CD  . PRO C  1 11  ? 78.802  26.941  33.369  1.00 9.09  ? 11   PRO C CD  1 
ATOM   5380  N  N   . ASP C  1 12  ? 79.331  27.131  28.658  1.00 7.13  ? 12   ASP C N   1 
ATOM   5381  C  CA  . ASP C  1 12  ? 79.938  26.460  27.484  1.00 8.40  ? 12   ASP C CA  1 
ATOM   5382  C  C   . ASP C  1 12  ? 81.435  26.821  27.313  1.00 7.89  ? 12   ASP C C   1 
ATOM   5383  O  O   . ASP C  1 12  ? 82.038  26.592  26.250  1.00 7.90  ? 12   ASP C O   1 
ATOM   5384  C  CB  . ASP C  1 12  ? 79.135  26.745  26.200  1.00 6.94  ? 12   ASP C CB  1 
ATOM   5385  C  CG  . ASP C  1 12  ? 79.165  28.224  25.808  1.00 10.65 ? 12   ASP C CG  1 
ATOM   5386  O  OD1 . ASP C  1 12  ? 79.867  29.022  26.460  1.00 15.23 ? 12   ASP C OD1 1 
ATOM   5387  O  OD2 . ASP C  1 12  ? 78.523  28.684  24.847  1.00 15.31 ? 12   ASP C OD2 1 
ATOM   5388  N  N   . HIS C  1 13  ? 82.034  27.373  28.367  1.00 7.22  ? 13   HIS C N   1 
ATOM   5389  C  CA  . HIS C  1 13  ? 83.461  27.669  28.382  1.00 7.09  ? 13   HIS C CA  1 
ATOM   5390  C  C   . HIS C  1 13  ? 83.852  27.720  29.848  1.00 7.77  ? 13   HIS C C   1 
ATOM   5391  O  O   . HIS C  1 13  ? 82.977  27.726  30.739  1.00 7.73  ? 13   HIS C O   1 
ATOM   5392  C  CB  . HIS C  1 13  ? 83.754  29.036  27.741  1.00 7.10  ? 13   HIS C CB  1 
ATOM   5393  C  CG  . HIS C  1 13  ? 83.076  30.186  28.409  1.00 10.33 ? 13   HIS C CG  1 
ATOM   5394  N  ND1 . HIS C  1 13  ? 81.699  30.327  28.434  1.00 11.21 ? 13   HIS C ND1 1 
ATOM   5395  C  CD2 . HIS C  1 13  ? 83.582  31.247  29.089  1.00 12.10 ? 13   HIS C CD2 1 
ATOM   5396  C  CE1 . HIS C  1 13  ? 81.390  31.425  29.113  1.00 12.28 ? 13   HIS C CE1 1 
ATOM   5397  N  NE2 . HIS C  1 13  ? 82.514  32.014  29.500  1.00 9.50  ? 13   HIS C NE2 1 
ATOM   5398  N  N   . VAL C  1 14  ? 85.135  27.846  30.103  1.00 6.55  ? 14   VAL C N   1 
ATOM   5399  C  CA  . VAL C  1 14  ? 85.661  27.891  31.468  1.00 6.97  ? 14   VAL C CA  1 
ATOM   5400  C  C   . VAL C  1 14  ? 85.523  29.283  32.086  1.00 6.55  ? 14   VAL C C   1 
ATOM   5401  O  O   . VAL C  1 14  ? 85.975  30.248  31.505  1.00 5.53  ? 14   VAL C O   1 
ATOM   5402  C  CB  . VAL C  1 14  ? 87.155  27.456  31.491  1.00 7.18  ? 14   VAL C CB  1 
ATOM   5403  C  CG1 . VAL C  1 14  ? 87.827  27.829  32.866  1.00 8.52  ? 14   VAL C CG1 1 
ATOM   5404  C  CG2 . VAL C  1 14  ? 87.257  25.966  31.200  1.00 6.00  ? 14   VAL C CG2 1 
ATOM   5405  N  N   . ARG C  1 15  ? 84.964  29.343  33.293  1.00 5.77  ? 15   ARG C N   1 
ATOM   5406  C  CA  . ARG C  1 15  ? 84.797  30.595  34.033  1.00 6.24  ? 15   ARG C CA  1 
ATOM   5407  C  C   . ARG C  1 15  ? 84.324  30.214  35.453  1.00 5.40  ? 15   ARG C C   1 
ATOM   5408  O  O   . ARG C  1 15  ? 83.723  29.150  35.650  1.00 6.01  ? 15   ARG C O   1 
ATOM   5409  C  CB  . ARG C  1 15  ? 83.759  31.507  33.314  1.00 5.56  ? 15   ARG C CB  1 
ATOM   5410  C  CG  . ARG C  1 15  ? 82.424  30.733  32.981  1.00 5.85  ? 15   ARG C CG  1 
ATOM   5411  C  CD  . ARG C  1 15  ? 81.118  31.605  32.996  1.00 4.00  ? 15   ARG C CD  1 
ATOM   5412  N  NE  . ARG C  1 15  ? 80.715  31.905  34.374  1.00 6.32  ? 15   ARG C NE  1 
ATOM   5413  C  CZ  . ARG C  1 15  ? 79.577  32.512  34.705  1.00 10.44 ? 15   ARG C CZ  1 
ATOM   5414  N  NH1 . ARG C  1 15  ? 78.711  32.886  33.771  1.00 7.64  ? 15   ARG C NH1 1 
ATOM   5415  N  NH2 . ARG C  1 15  ? 79.310  32.767  35.980  1.00 10.25 ? 15   ARG C NH2 1 
ATOM   5416  N  N   . PRO C  1 16  ? 84.583  31.045  36.447  1.00 5.28  ? 16   PRO C N   1 
ATOM   5417  C  CA  . PRO C  1 16  ? 83.979  30.821  37.777  1.00 5.87  ? 16   PRO C CA  1 
ATOM   5418  C  C   . PRO C  1 16  ? 82.441  30.729  37.679  1.00 5.24  ? 16   PRO C C   1 
ATOM   5419  O  O   . PRO C  1 16  ? 81.822  31.507  36.959  1.00 6.68  ? 16   PRO C O   1 
ATOM   5420  C  CB  . PRO C  1 16  ? 84.344  32.083  38.547  1.00 4.98  ? 16   PRO C CB  1 
ATOM   5421  C  CG  . PRO C  1 16  ? 85.683  32.516  37.892  1.00 7.29  ? 16   PRO C CG  1 
ATOM   5422  C  CD  . PRO C  1 16  ? 85.395  32.289  36.382  1.00 5.87  ? 16   PRO C CD  1 
ATOM   5423  N  N   . TYR C  1 17  ? 81.846  29.771  38.364  1.00 5.79  ? 17   TYR C N   1 
ATOM   5424  C  CA  . TYR C  1 17  ? 80.381  29.694  38.450  1.00 6.67  ? 17   TYR C CA  1 
ATOM   5425  C  C   . TYR C  1 17  ? 79.916  28.906  39.616  1.00 5.91  ? 17   TYR C C   1 
ATOM   5426  O  O   . TYR C  1 17  ? 80.650  28.077  40.170  1.00 7.74  ? 17   TYR C O   1 
ATOM   5427  C  CB  . TYR C  1 17  ? 79.715  29.183  37.162  1.00 6.20  ? 17   TYR C CB  1 
ATOM   5428  C  CG  . TYR C  1 17  ? 79.891  27.677  36.846  1.00 6.90  ? 17   TYR C CG  1 
ATOM   5429  C  CD1 . TYR C  1 17  ? 78.951  26.753  37.238  1.00 7.29  ? 17   TYR C CD1 1 
ATOM   5430  C  CD2 . TYR C  1 17  ? 80.969  27.242  36.112  1.00 8.04  ? 17   TYR C CD2 1 
ATOM   5431  C  CE1 . TYR C  1 17  ? 79.064  25.404  36.889  1.00 10.47 ? 17   TYR C CE1 1 
ATOM   5432  C  CE2 . TYR C  1 17  ? 81.141  25.914  35.803  1.00 5.53  ? 17   TYR C CE2 1 
ATOM   5433  C  CZ  . TYR C  1 17  ? 80.183  25.011  36.172  1.00 10.22 ? 17   TYR C CZ  1 
ATOM   5434  O  OH  . TYR C  1 17  ? 80.357  23.708  35.820  1.00 7.21  ? 17   TYR C OH  1 
ATOM   5435  N  N   . VAL C  1 18  ? 78.668  29.190  39.989  1.00 6.79  ? 18   VAL C N   1 
ATOM   5436  C  CA  . VAL C  1 18  ? 77.942  28.352  40.896  1.00 6.61  ? 18   VAL C CA  1 
ATOM   5437  C  C   . VAL C  1 18  ? 76.677  27.903  40.210  1.00 7.45  ? 18   VAL C C   1 
ATOM   5438  O  O   . VAL C  1 18  ? 76.011  28.703  39.532  1.00 7.02  ? 18   VAL C O   1 
ATOM   5439  C  CB  . VAL C  1 18  ? 77.636  29.129  42.214  1.00 7.59  ? 18   VAL C CB  1 
ATOM   5440  C  CG1 . VAL C  1 18  ? 76.651  28.368  43.114  1.00 2.04  ? 18   VAL C CG1 1 
ATOM   5441  C  CG2 . VAL C  1 18  ? 78.926  29.371  42.974  1.00 7.13  ? 18   VAL C CG2 1 
ATOM   5442  N  N   . ILE C  1 19  ? 76.304  26.649  40.442  1.00 5.92  ? 19   ILE C N   1 
ATOM   5443  C  CA  . ILE C  1 19  ? 75.061  26.164  39.933  1.00 6.56  ? 19   ILE C CA  1 
ATOM   5444  C  C   . ILE C  1 19  ? 74.321  25.570  41.122  1.00 7.77  ? 19   ILE C C   1 
ATOM   5445  O  O   . ILE C  1 19  ? 74.863  24.716  41.856  1.00 8.16  ? 19   ILE C O   1 
ATOM   5446  C  CB  . ILE C  1 19  ? 75.275  25.168  38.765  1.00 6.41  ? 19   ILE C CB  1 
ATOM   5447  C  CG1 . ILE C  1 19  ? 73.959  24.609  38.231  1.00 6.33  ? 19   ILE C CG1 1 
ATOM   5448  C  CG2 . ILE C  1 19  ? 76.250  24.038  39.104  1.00 4.50  ? 19   ILE C CG2 1 
ATOM   5449  C  CD1 . ILE C  1 19  ? 74.034  24.277  36.686  1.00 4.01  ? 19   ILE C CD1 1 
ATOM   5450  N  N   . ARG C  1 20  ? 73.092  26.050  41.332  1.00 7.18  ? 20   ARG C N   1 
ATOM   5451  C  CA  . ARG C  1 20  ? 72.285  25.547  42.434  1.00 6.59  ? 20   ARG C CA  1 
ATOM   5452  C  C   . ARG C  1 20  ? 71.841  24.106  42.242  1.00 6.99  ? 20   ARG C C   1 
ATOM   5453  O  O   . ARG C  1 20  ? 71.647  23.633  41.107  1.00 8.52  ? 20   ARG C O   1 
ATOM   5454  C  CB  . ARG C  1 20  ? 71.001  26.408  42.627  1.00 4.74  ? 20   ARG C CB  1 
ATOM   5455  C  CG  . ARG C  1 20  ? 71.299  27.897  42.931  1.00 7.39  ? 20   ARG C CG  1 
ATOM   5456  C  CD  . ARG C  1 20  ? 72.107  28.099  44.263  1.00 8.44  ? 20   ARG C CD  1 
ATOM   5457  N  NE  . ARG C  1 20  ? 72.089  29.504  44.704  1.00 9.37  ? 20   ARG C NE  1 
ATOM   5458  C  CZ  . ARG C  1 20  ? 72.627  29.910  45.857  1.00 11.16 ? 20   ARG C CZ  1 
ATOM   5459  N  NH1 . ARG C  1 20  ? 73.218  29.016  46.677  1.00 7.89  ? 20   ARG C NH1 1 
ATOM   5460  N  NH2 . ARG C  1 20  ? 72.641  31.194  46.161  1.00 9.12  ? 20   ARG C NH2 1 
ATOM   5461  N  N   . HIS C  1 21  ? 71.598  23.431  43.357  1.00 7.98  ? 21   HIS C N   1 
ATOM   5462  C  CA  . HIS C  1 21  ? 71.115  22.039  43.333  1.00 8.11  ? 21   HIS C CA  1 
ATOM   5463  C  C   . HIS C  1 21  ? 69.798  21.965  42.518  1.00 9.10  ? 21   HIS C C   1 
ATOM   5464  O  O   . HIS C  1 21  ? 68.955  22.831  42.696  1.00 10.37 ? 21   HIS C O   1 
ATOM   5465  C  CB  . HIS C  1 21  ? 70.809  21.584  44.769  1.00 7.52  ? 21   HIS C CB  1 
ATOM   5466  C  CG  . HIS C  1 21  ? 70.757  20.080  44.929  1.00 6.66  ? 21   HIS C CG  1 
ATOM   5467  N  ND1 . HIS C  1 21  ? 70.161  19.461  46.007  1.00 10.61 ? 21   HIS C ND1 1 
ATOM   5468  C  CD2 . HIS C  1 21  ? 71.281  19.080  44.171  1.00 7.57  ? 21   HIS C CD2 1 
ATOM   5469  C  CE1 . HIS C  1 21  ? 70.288  18.143  45.903  1.00 6.41  ? 21   HIS C CE1 1 
ATOM   5470  N  NE2 . HIS C  1 21  ? 70.951  17.884  44.790  1.00 9.40  ? 21   HIS C NE2 1 
ATOM   5471  N  N   . TYR C  1 22  ? 69.653  20.949  41.650  1.00 8.40  ? 22   TYR C N   1 
ATOM   5472  C  CA  . TYR C  1 22  ? 68.456  20.760  40.771  1.00 9.33  ? 22   TYR C CA  1 
ATOM   5473  C  C   . TYR C  1 22  ? 68.241  21.845  39.731  1.00 7.74  ? 22   TYR C C   1 
ATOM   5474  O  O   . TYR C  1 22  ? 67.157  21.967  39.144  1.00 7.95  ? 22   TYR C O   1 
ATOM   5475  C  CB  . TYR C  1 22  ? 67.173  20.591  41.607  1.00 7.77  ? 22   TYR C CB  1 
ATOM   5476  C  CG  . TYR C  1 22  ? 67.292  19.468  42.622  1.00 7.99  ? 22   TYR C CG  1 
ATOM   5477  C  CD1 . TYR C  1 22  ? 67.655  18.184  42.235  1.00 6.39  ? 22   TYR C CD1 1 
ATOM   5478  C  CD2 . TYR C  1 22  ? 67.030  19.724  43.978  1.00 9.98  ? 22   TYR C CD2 1 
ATOM   5479  C  CE1 . TYR C  1 22  ? 67.735  17.142  43.190  1.00 11.55 ? 22   TYR C CE1 1 
ATOM   5480  C  CE2 . TYR C  1 22  ? 67.118  18.745  44.924  1.00 10.10 ? 22   TYR C CE2 1 
ATOM   5481  C  CZ  . TYR C  1 22  ? 67.463  17.433  44.533  1.00 12.79 ? 22   TYR C CZ  1 
ATOM   5482  O  OH  . TYR C  1 22  ? 67.573  16.457  45.495  1.00 13.92 ? 22   TYR C OH  1 
ATOM   5483  N  N   . SER C  1 23  ? 69.255  22.657  39.496  1.00 7.08  ? 23   SER C N   1 
ATOM   5484  C  CA  . SER C  1 23  ? 69.213  23.580  38.359  1.00 7.05  ? 23   SER C CA  1 
ATOM   5485  C  C   . SER C  1 23  ? 68.971  22.760  37.074  1.00 7.78  ? 23   SER C C   1 
ATOM   5486  O  O   . SER C  1 23  ? 69.196  21.558  37.078  1.00 7.28  ? 23   SER C O   1 
ATOM   5487  C  CB  . SER C  1 23  ? 70.555  24.315  38.212  1.00 8.57  ? 23   SER C CB  1 
ATOM   5488  O  OG  . SER C  1 23  ? 70.692  25.320  39.236  1.00 6.65  ? 23   SER C OG  1 
ATOM   5489  N  N   . HIS C  1 24  ? 68.521  23.390  35.994  1.00 6.90  ? 24   HIS C N   1 
ATOM   5490  C  CA  . HIS C  1 24  ? 68.254  22.643  34.752  1.00 7.90  ? 24   HIS C CA  1 
ATOM   5491  C  C   . HIS C  1 24  ? 69.449  21.768  34.331  1.00 7.72  ? 24   HIS C C   1 
ATOM   5492  O  O   . HIS C  1 24  ? 69.307  20.526  34.028  1.00 9.12  ? 24   HIS C O   1 
ATOM   5493  C  CB  . HIS C  1 24  ? 67.810  23.581  33.585  1.00 6.79  ? 24   HIS C CB  1 
ATOM   5494  C  CG  . HIS C  1 24  ? 67.474  22.811  32.331  1.00 7.87  ? 24   HIS C CG  1 
ATOM   5495  N  ND1 . HIS C  1 24  ? 68.237  22.856  31.184  1.00 4.15  ? 24   HIS C ND1 1 
ATOM   5496  C  CD2 . HIS C  1 24  ? 66.496  21.900  32.095  1.00 7.63  ? 24   HIS C CD2 1 
ATOM   5497  C  CE1 . HIS C  1 24  ? 67.723  22.028  30.283  1.00 5.50  ? 24   HIS C CE1 1 
ATOM   5498  N  NE2 . HIS C  1 24  ? 66.689  21.415  30.820  1.00 6.69  ? 24   HIS C NE2 1 
ATOM   5499  N  N   . ALA C  1 25  ? 70.624  22.403  34.258  1.00 6.91  ? 25   ALA C N   1 
ATOM   5500  C  CA  . ALA C  1 25  ? 71.900  21.687  34.012  1.00 7.10  ? 25   ALA C CA  1 
ATOM   5501  C  C   . ALA C  1 25  ? 71.840  20.672  32.848  1.00 7.48  ? 25   ALA C C   1 
ATOM   5502  O  O   . ALA C  1 25  ? 72.269  19.506  32.961  1.00 7.48  ? 25   ALA C O   1 
ATOM   5503  C  CB  . ALA C  1 25  ? 72.419  21.012  35.360  1.00 6.75  ? 25   ALA C CB  1 
ATOM   5504  N  N   . ARG C  1 26  ? 71.389  21.170  31.707  1.00 7.96  ? 26   ARG C N   1 
ATOM   5505  C  CA  . ARG C  1 26  ? 71.232  20.411  30.474  1.00 8.61  ? 26   ARG C CA  1 
ATOM   5506  C  C   . ARG C  1 26  ? 70.522  19.068  30.669  1.00 7.75  ? 26   ARG C C   1 
ATOM   5507  O  O   . ARG C  1 26  ? 70.912  18.064  30.031  1.00 7.00  ? 26   ARG C O   1 
ATOM   5508  C  CB  . ARG C  1 26  ? 72.595  20.186  29.835  1.00 8.66  ? 26   ARG C CB  1 
ATOM   5509  C  CG  . ARG C  1 26  ? 72.975  21.240  28.870  1.00 15.12 ? 26   ARG C CG  1 
ATOM   5510  C  CD  . ARG C  1 26  ? 74.067  20.797  27.906  1.00 27.32 ? 26   ARG C CD  1 
ATOM   5511  N  NE  . ARG C  1 26  ? 74.716  21.836  27.039  1.00 34.77 ? 26   ARG C NE  1 
ATOM   5512  C  CZ  . ARG C  1 26  ? 74.642  23.191  27.125  1.00 36.74 ? 26   ARG C CZ  1 
ATOM   5513  N  NH1 . ARG C  1 26  ? 73.905  23.816  28.061  1.00 37.32 ? 26   ARG C NH1 1 
ATOM   5514  N  NH2 . ARG C  1 26  ? 75.320  23.930  26.226  1.00 33.47 ? 26   ARG C NH2 1 
ATOM   5515  N  N   . ALA C  1 27  ? 69.516  19.037  31.566  1.00 6.97  ? 27   ALA C N   1 
ATOM   5516  C  CA  . ALA C  1 27  ? 68.884  17.784  32.013  1.00 6.87  ? 27   ALA C CA  1 
ATOM   5517  C  C   . ALA C  1 27  ? 68.434  16.855  30.916  1.00 7.62  ? 27   ALA C C   1 
ATOM   5518  O  O   . ALA C  1 27  ? 67.802  17.289  29.922  1.00 8.09  ? 27   ALA C O   1 
ATOM   5519  C  CB  . ALA C  1 27  ? 67.696  18.039  32.946  1.00 6.34  ? 27   ALA C CB  1 
ATOM   5520  N  N   . VAL C  1 28  ? 68.743  15.561  31.091  1.00 7.57  ? 28   VAL C N   1 
ATOM   5521  C  CA  . VAL C  1 28  ? 68.100  14.536  30.256  1.00 7.84  ? 28   VAL C CA  1 
ATOM   5522  C  C   . VAL C  1 28  ? 67.537  13.435  31.160  1.00 7.72  ? 28   VAL C C   1 
ATOM   5523  O  O   . VAL C  1 28  ? 67.987  13.246  32.291  1.00 8.34  ? 28   VAL C O   1 
ATOM   5524  C  CB  . VAL C  1 28  ? 69.091  13.885  29.241  1.00 7.03  ? 28   VAL C CB  1 
ATOM   5525  C  CG1 . VAL C  1 28  ? 69.801  14.946  28.421  1.00 7.21  ? 28   VAL C CG1 1 
ATOM   5526  C  CG2 . VAL C  1 28  ? 70.122  12.987  30.002  1.00 5.75  ? 28   VAL C CG2 1 
ATOM   5527  N  N   . THR C  1 29  ? 66.544  12.717  30.654  1.00 7.64  ? 29   THR C N   1 
ATOM   5528  C  CA  . THR C  1 29  ? 66.118  11.490  31.318  1.00 6.57  ? 29   THR C CA  1 
ATOM   5529  C  C   . THR C  1 29  ? 66.568  10.272  30.531  1.00 7.04  ? 29   THR C C   1 
ATOM   5530  O  O   . THR C  1 29  ? 66.538  10.268  29.293  1.00 6.85  ? 29   THR C O   1 
ATOM   5531  C  CB  . THR C  1 29  ? 64.576  11.407  31.473  1.00 6.12  ? 29   THR C CB  1 
ATOM   5532  O  OG1 . THR C  1 29  ? 63.936  11.635  30.203  1.00 7.47  ? 29   THR C OG1 1 
ATOM   5533  C  CG2 . THR C  1 29  ? 64.077  12.531  32.345  1.00 8.68  ? 29   THR C CG2 1 
ATOM   5534  N  N   . VAL C  1 30  ? 66.965  9.238   31.273  1.00 7.41  ? 30   VAL C N   1 
ATOM   5535  C  CA  . VAL C  1 30  ? 67.093  7.873   30.710  1.00 7.77  ? 30   VAL C CA  1 
ATOM   5536  C  C   . VAL C  1 30  ? 66.058  7.011   31.442  1.00 8.41  ? 30   VAL C C   1 
ATOM   5537  O  O   . VAL C  1 30  ? 66.262  6.623   32.602  1.00 7.27  ? 30   VAL C O   1 
ATOM   5538  C  CB  . VAL C  1 30  ? 68.553  7.292   30.914  1.00 7.69  ? 30   VAL C CB  1 
ATOM   5539  C  CG1 . VAL C  1 30  ? 68.658  5.900   30.244  1.00 8.75  ? 30   VAL C CG1 1 
ATOM   5540  C  CG2 . VAL C  1 30  ? 69.601  8.257   30.305  1.00 8.08  ? 30   VAL C CG2 1 
ATOM   5541  N  N   . ASP C  1 31  ? 64.913  6.783   30.815  1.00 8.55  ? 31   ASP C N   1 
ATOM   5542  C  CA  . ASP C  1 31  ? 63.833  6.024   31.469  1.00 10.28 ? 31   ASP C CA  1 
ATOM   5543  C  C   . ASP C  1 31  ? 63.453  6.794   32.732  1.00 9.82  ? 31   ASP C C   1 
ATOM   5544  O  O   . ASP C  1 31  ? 63.176  7.983   32.608  1.00 8.84  ? 31   ASP C O   1 
ATOM   5545  C  CB  . ASP C  1 31  ? 64.248  4.592   31.748  1.00 9.92  ? 31   ASP C CB  1 
ATOM   5546  C  CG  . ASP C  1 31  ? 64.519  3.814   30.458  1.00 15.44 ? 31   ASP C CG  1 
ATOM   5547  O  OD1 . ASP C  1 31  ? 63.610  3.801   29.582  1.00 16.33 ? 31   ASP C OD1 1 
ATOM   5548  O  OD2 . ASP C  1 31  ? 65.619  3.222   30.234  1.00 17.03 ? 31   ASP C OD2 1 
ATOM   5549  N  N   . THR C  1 32  ? 63.507  6.187   33.938  1.00 8.91  ? 32   THR C N   1 
ATOM   5550  C  CA  . THR C  1 32  ? 63.072  6.933   35.140  1.00 9.70  ? 32   THR C CA  1 
ATOM   5551  C  C   . THR C  1 32  ? 64.152  7.848   35.741  1.00 9.80  ? 32   THR C C   1 
ATOM   5552  O  O   . THR C  1 32  ? 63.854  8.712   36.604  1.00 10.81 ? 32   THR C O   1 
ATOM   5553  C  CB  . THR C  1 32  ? 62.588  5.974   36.234  1.00 9.67  ? 32   THR C CB  1 
ATOM   5554  O  OG1 . THR C  1 32  ? 63.670  5.098   36.592  1.00 7.76  ? 32   THR C OG1 1 
ATOM   5555  C  CG2 . THR C  1 32  ? 61.471  5.052   35.675  1.00 7.26  ? 32   THR C CG2 1 
ATOM   5556  N  N   . GLN C  1 33  ? 65.391  7.720   35.276  1.00 10.19 ? 33   GLN C N   1 
ATOM   5557  C  CA  . GLN C  1 33  ? 66.510  8.470   35.875  1.00 8.22  ? 33   GLN C CA  1 
ATOM   5558  C  C   . GLN C  1 33  ? 66.635  9.838   35.225  1.00 10.46 ? 33   GLN C C   1 
ATOM   5559  O  O   . GLN C  1 33  ? 66.473  9.972   33.996  1.00 9.64  ? 33   GLN C O   1 
ATOM   5560  C  CB  . GLN C  1 33  ? 67.828  7.695   35.705  1.00 9.87  ? 33   GLN C CB  1 
ATOM   5561  C  CG  . GLN C  1 33  ? 67.819  6.244   36.220  1.00 9.06  ? 33   GLN C CG  1 
ATOM   5562  C  CD  . GLN C  1 33  ? 68.953  5.417   35.616  1.00 11.00 ? 33   GLN C CD  1 
ATOM   5563  O  OE1 . GLN C  1 33  ? 69.710  5.916   34.759  1.00 12.90 ? 33   GLN C OE1 1 
ATOM   5564  N  NE2 . GLN C  1 33  ? 69.072  4.172   36.053  1.00 8.21  ? 33   GLN C NE2 1 
ATOM   5565  N  N   . LEU C  1 34  ? 66.915  10.866  36.041  1.00 9.39  ? 34   LEU C N   1 
ATOM   5566  C  CA  . LEU C  1 34  ? 67.146  12.203  35.519  1.00 8.69  ? 34   LEU C CA  1 
ATOM   5567  C  C   . LEU C  1 34  ? 68.592  12.597  35.845  1.00 8.80  ? 34   LEU C C   1 
ATOM   5568  O  O   . LEU C  1 34  ? 69.022  12.510  37.013  1.00 8.24  ? 34   LEU C O   1 
ATOM   5569  C  CB  . LEU C  1 34  ? 66.177  13.227  36.169  1.00 7.62  ? 34   LEU C CB  1 
ATOM   5570  C  CG  . LEU C  1 34  ? 66.028  14.559  35.436  1.00 9.23  ? 34   LEU C CG  1 
ATOM   5571  C  CD1 . LEU C  1 34  ? 64.710  15.241  35.862  1.00 8.27  ? 34   LEU C CD1 1 
ATOM   5572  C  CD2 . LEU C  1 34  ? 67.128  15.563  35.784  1.00 7.38  ? 34   LEU C CD2 1 
ATOM   5573  N  N   . TYR C  1 35  ? 69.321  13.048  34.823  1.00 8.14  ? 35   TYR C N   1 
ATOM   5574  C  CA  . TYR C  1 35  ? 70.722  13.390  34.918  1.00 8.14  ? 35   TYR C CA  1 
ATOM   5575  C  C   . TYR C  1 35  ? 70.866  14.862  34.739  1.00 7.77  ? 35   TYR C C   1 
ATOM   5576  O  O   . TYR C  1 35  ? 70.245  15.455  33.837  1.00 8.89  ? 35   TYR C O   1 
ATOM   5577  C  CB  . TYR C  1 35  ? 71.510  12.684  33.772  1.00 8.52  ? 35   TYR C CB  1 
ATOM   5578  C  CG  . TYR C  1 35  ? 71.665  11.192  33.950  1.00 9.92  ? 35   TYR C CG  1 
ATOM   5579  C  CD1 . TYR C  1 35  ? 70.606  10.288  33.655  1.00 8.43  ? 35   TYR C CD1 1 
ATOM   5580  C  CD2 . TYR C  1 35  ? 72.886  10.658  34.357  1.00 7.86  ? 35   TYR C CD2 1 
ATOM   5581  C  CE1 . TYR C  1 35  ? 70.768  8.919   33.857  1.00 7.96  ? 35   TYR C CE1 1 
ATOM   5582  C  CE2 . TYR C  1 35  ? 73.043  9.319   34.536  1.00 9.02  ? 35   TYR C CE2 1 
ATOM   5583  C  CZ  . TYR C  1 35  ? 71.978  8.452   34.310  1.00 7.92  ? 35   TYR C CZ  1 
ATOM   5584  O  OH  . TYR C  1 35  ? 72.202  7.090   34.505  1.00 11.96 ? 35   TYR C OH  1 
ATOM   5585  N  N   . ARG C  1 36  ? 71.695  15.465  35.587  1.00 6.98  ? 36   ARG C N   1 
ATOM   5586  C  CA  . ARG C  1 36  ? 71.963  16.887  35.545  1.00 7.37  ? 36   ARG C CA  1 
ATOM   5587  C  C   . ARG C  1 36  ? 73.498  16.993  35.496  1.00 9.12  ? 36   ARG C C   1 
ATOM   5588  O  O   . ARG C  1 36  ? 74.234  16.240  36.228  1.00 9.00  ? 36   ARG C O   1 
ATOM   5589  C  CB  . ARG C  1 36  ? 71.428  17.560  36.830  1.00 6.13  ? 36   ARG C CB  1 
ATOM   5590  C  CG  . ARG C  1 36  ? 69.904  17.888  36.779  1.00 6.41  ? 36   ARG C CG  1 
ATOM   5591  C  CD  . ARG C  1 36  ? 69.383  18.563  38.075  1.00 4.18  ? 36   ARG C CD  1 
ATOM   5592  N  NE  . ARG C  1 36  ? 67.927  18.807  37.956  1.00 9.57  ? 36   ARG C NE  1 
ATOM   5593  C  CZ  . ARG C  1 36  ? 66.998  17.949  38.359  1.00 9.76  ? 36   ARG C CZ  1 
ATOM   5594  N  NH1 . ARG C  1 36  ? 67.356  16.756  38.864  1.00 6.62  ? 36   ARG C NH1 1 
ATOM   5595  N  NH2 . ARG C  1 36  ? 65.700  18.261  38.212  1.00 7.18  ? 36   ARG C NH2 1 
ATOM   5596  N  N   . PHE C  1 37  ? 73.979  17.839  34.597  1.00 8.30  ? 37   PHE C N   1 
ATOM   5597  C  CA  . PHE C  1 37  ? 75.422  18.008  34.348  1.00 8.84  ? 37   PHE C CA  1 
ATOM   5598  C  C   . PHE C  1 37  ? 75.942  19.340  34.903  1.00 8.96  ? 37   PHE C C   1 
ATOM   5599  O  O   . PHE C  1 37  ? 75.978  20.372  34.195  1.00 9.50  ? 37   PHE C O   1 
ATOM   5600  C  CB  . PHE C  1 37  ? 75.733  17.812  32.840  1.00 9.45  ? 37   PHE C CB  1 
ATOM   5601  C  CG  . PHE C  1 37  ? 75.042  16.617  32.274  1.00 6.12  ? 37   PHE C CG  1 
ATOM   5602  C  CD1 . PHE C  1 37  ? 75.533  15.348  32.496  1.00 9.42  ? 37   PHE C CD1 1 
ATOM   5603  C  CD2 . PHE C  1 37  ? 73.793  16.781  31.639  1.00 8.69  ? 37   PHE C CD2 1 
ATOM   5604  C  CE1 . PHE C  1 37  ? 74.839  14.227  32.038  1.00 7.76  ? 37   PHE C CE1 1 
ATOM   5605  C  CE2 . PHE C  1 37  ? 73.087  15.690  31.191  1.00 6.34  ? 37   PHE C CE2 1 
ATOM   5606  C  CZ  . PHE C  1 37  ? 73.596  14.418  31.396  1.00 5.60  ? 37   PHE C CZ  1 
ATOM   5607  N  N   . TYR C  1 38  ? 76.320  19.301  36.178  1.00 7.10  ? 38   TYR C N   1 
ATOM   5608  C  CA  . TYR C  1 38  ? 76.677  20.532  36.888  1.00 8.32  ? 38   TYR C CA  1 
ATOM   5609  C  C   . TYR C  1 38  ? 78.057  21.042  36.468  1.00 8.08  ? 38   TYR C C   1 
ATOM   5610  O  O   . TYR C  1 38  ? 78.312  22.268  36.453  1.00 9.57  ? 38   TYR C O   1 
ATOM   5611  C  CB  . TYR C  1 38  ? 76.659  20.290  38.395  1.00 8.16  ? 38   TYR C CB  1 
ATOM   5612  C  CG  . TYR C  1 38  ? 75.314  19.912  38.984  1.00 6.25  ? 38   TYR C CG  1 
ATOM   5613  C  CD1 . TYR C  1 38  ? 74.222  20.795  38.919  1.00 13.54 ? 38   TYR C CD1 1 
ATOM   5614  C  CD2 . TYR C  1 38  ? 75.140  18.685  39.618  1.00 8.55  ? 38   TYR C CD2 1 
ATOM   5615  C  CE1 . TYR C  1 38  ? 73.018  20.467  39.471  1.00 8.56  ? 38   TYR C CE1 1 
ATOM   5616  C  CE2 . TYR C  1 38  ? 73.901  18.333  40.205  1.00 8.82  ? 38   TYR C CE2 1 
ATOM   5617  C  CZ  . TYR C  1 38  ? 72.873  19.220  40.138  1.00 9.05  ? 38   TYR C CZ  1 
ATOM   5618  O  OH  . TYR C  1 38  ? 71.655  18.913  40.709  1.00 8.00  ? 38   TYR C OH  1 
ATOM   5619  N  N   . VAL C  1 39  ? 78.917  20.089  36.132  1.00 7.62  ? 39   VAL C N   1 
ATOM   5620  C  CA  . VAL C  1 39  ? 80.205  20.364  35.519  1.00 7.75  ? 39   VAL C CA  1 
ATOM   5621  C  C   . VAL C  1 39  ? 80.355  19.451  34.279  1.00 8.37  ? 39   VAL C C   1 
ATOM   5622  O  O   . VAL C  1 39  ? 80.119  18.225  34.325  1.00 8.89  ? 39   VAL C O   1 
ATOM   5623  C  CB  . VAL C  1 39  ? 81.405  20.164  36.525  1.00 8.35  ? 39   VAL C CB  1 
ATOM   5624  C  CG1 . VAL C  1 39  ? 82.765  20.556  35.839  1.00 3.70  ? 39   VAL C CG1 1 
ATOM   5625  C  CG2 . VAL C  1 39  ? 81.211  21.037  37.776  1.00 7.31  ? 39   VAL C CG2 1 
ATOM   5626  N  N   . THR C  1 40  ? 80.733  20.059  33.163  1.00 9.43  ? 40   THR C N   1 
ATOM   5627  C  CA  . THR C  1 40  ? 80.893  19.335  31.887  1.00 8.94  ? 40   THR C CA  1 
ATOM   5628  C  C   . THR C  1 40  ? 82.314  19.484  31.360  1.00 9.07  ? 40   THR C C   1 
ATOM   5629  O  O   . THR C  1 40  ? 83.139  20.206  31.938  1.00 7.78  ? 40   THR C O   1 
ATOM   5630  C  CB  . THR C  1 40  ? 79.974  19.956  30.810  1.00 10.45 ? 40   THR C CB  1 
ATOM   5631  O  OG1 . THR C  1 40  ? 80.365  21.328  30.606  1.00 9.35  ? 40   THR C OG1 1 
ATOM   5632  C  CG2 . THR C  1 40  ? 78.501  19.954  31.225  1.00 6.32  ? 40   THR C CG2 1 
ATOM   5633  N  N   . GLY C  1 41  ? 82.597  18.785  30.262  1.00 8.81  ? 41   GLY C N   1 
ATOM   5634  C  CA  . GLY C  1 41  ? 83.857  18.991  29.556  1.00 8.54  ? 41   GLY C CA  1 
ATOM   5635  C  C   . GLY C  1 41  ? 84.073  20.454  29.180  1.00 7.42  ? 41   GLY C C   1 
ATOM   5636  O  O   . GLY C  1 41  ? 85.107  21.040  29.521  1.00 6.73  ? 41   GLY C O   1 
ATOM   5637  N  N   . PRO C  1 42  ? 83.150  21.043  28.424  1.00 7.52  ? 42   PRO C N   1 
ATOM   5638  C  CA  . PRO C  1 42  ? 83.288  22.463  28.065  1.00 7.53  ? 42   PRO C CA  1 
ATOM   5639  C  C   . PRO C  1 42  ? 83.441  23.396  29.304  1.00 7.93  ? 42   PRO C C   1 
ATOM   5640  O  O   . PRO C  1 42  ? 84.282  24.292  29.234  1.00 9.03  ? 42   PRO C O   1 
ATOM   5641  C  CB  . PRO C  1 42  ? 82.016  22.753  27.256  1.00 8.07  ? 42   PRO C CB  1 
ATOM   5642  C  CG  . PRO C  1 42  ? 81.708  21.397  26.607  1.00 6.99  ? 42   PRO C CG  1 
ATOM   5643  C  CD  . PRO C  1 42  ? 81.992  20.407  27.737  1.00 7.87  ? 42   PRO C CD  1 
ATOM   5644  N  N   . SER C  1 43  ? 82.676  23.185  30.372  1.00 6.53  ? 43   SER C N   1 
ATOM   5645  C  CA  . SER C  1 43  ? 82.702  24.061  31.530  1.00 7.65  ? 43   SER C CA  1 
ATOM   5646  C  C   . SER C  1 43  ? 83.949  23.867  32.382  1.00 8.52  ? 43   SER C C   1 
ATOM   5647  O  O   . SER C  1 43  ? 84.340  24.779  33.138  1.00 8.36  ? 43   SER C O   1 
ATOM   5648  C  CB  . SER C  1 43  ? 81.439  23.873  32.398  1.00 6.66  ? 43   SER C CB  1 
ATOM   5649  O  OG  . SER C  1 43  ? 81.587  22.839  33.350  1.00 6.80  ? 43   SER C OG  1 
ATOM   5650  N  N   . SER C  1 44  ? 84.559  22.673  32.296  1.00 7.88  ? 44   SER C N   1 
ATOM   5651  C  CA  . SER C  1 44  ? 85.790  22.466  33.056  1.00 8.56  ? 44   SER C CA  1 
ATOM   5652  C  C   . SER C  1 44  ? 87.085  22.426  32.209  1.00 9.29  ? 44   SER C C   1 
ATOM   5653  O  O   . SER C  1 44  ? 88.152  22.140  32.748  1.00 7.86  ? 44   SER C O   1 
ATOM   5654  C  CB  . SER C  1 44  ? 85.674  21.191  33.899  1.00 9.62  ? 44   SER C CB  1 
ATOM   5655  O  OG  . SER C  1 44  ? 85.812  20.036  33.090  1.00 10.06 ? 44   SER C OG  1 
ATOM   5656  N  N   . GLY C  1 45  ? 86.997  22.731  30.908  1.00 7.83  ? 45   GLY C N   1 
ATOM   5657  C  CA  . GLY C  1 45  ? 88.159  22.561  30.034  1.00 8.00  ? 45   GLY C CA  1 
ATOM   5658  C  C   . GLY C  1 45  ? 88.634  21.111  30.061  1.00 8.17  ? 45   GLY C C   1 
ATOM   5659  O  O   . GLY C  1 45  ? 89.857  20.849  30.039  1.00 6.73  ? 45   GLY C O   1 
ATOM   5660  N  N   . TYR C  1 46  ? 87.637  20.208  30.167  1.00 7.20  ? 46   TYR C N   1 
ATOM   5661  C  CA  . TYR C  1 46  ? 87.766  18.765  29.940  1.00 7.75  ? 46   TYR C CA  1 
ATOM   5662  C  C   . TYR C  1 46  ? 88.443  18.077  31.110  1.00 7.13  ? 46   TYR C C   1 
ATOM   5663  O  O   . TYR C  1 46  ? 88.809  16.914  31.025  1.00 7.01  ? 46   TYR C O   1 
ATOM   5664  C  CB  . TYR C  1 46  ? 88.409  18.443  28.542  1.00 8.24  ? 46   TYR C CB  1 
ATOM   5665  C  CG  . TYR C  1 46  ? 87.710  19.271  27.492  1.00 7.67  ? 46   TYR C CG  1 
ATOM   5666  C  CD1 . TYR C  1 46  ? 86.469  18.880  26.986  1.00 5.43  ? 46   TYR C CD1 1 
ATOM   5667  C  CD2 . TYR C  1 46  ? 88.252  20.505  27.080  1.00 8.63  ? 46   TYR C CD2 1 
ATOM   5668  C  CE1 . TYR C  1 46  ? 85.769  19.707  26.088  1.00 6.28  ? 46   TYR C CE1 1 
ATOM   5669  C  CE2 . TYR C  1 46  ? 87.568  21.342  26.194  1.00 10.64 ? 46   TYR C CE2 1 
ATOM   5670  C  CZ  . TYR C  1 46  ? 86.325  20.939  25.710  1.00 9.69  ? 46   TYR C CZ  1 
ATOM   5671  O  OH  . TYR C  1 46  ? 85.661  21.757  24.824  1.00 11.80 ? 46   TYR C OH  1 
ATOM   5672  N  N   . ALA C  1 47  ? 88.570  18.802  32.222  1.00 7.27  ? 47   ALA C N   1 
ATOM   5673  C  CA  . ALA C  1 47  ? 89.186  18.260  33.453  1.00 6.90  ? 47   ALA C CA  1 
ATOM   5674  C  C   . ALA C  1 47  ? 88.379  17.131  34.093  1.00 6.17  ? 47   ALA C C   1 
ATOM   5675  O  O   . ALA C  1 47  ? 88.907  16.069  34.419  1.00 6.55  ? 47   ALA C O   1 
ATOM   5676  C  CB  . ALA C  1 47  ? 89.419  19.436  34.504  1.00 5.46  ? 47   ALA C CB  1 
ATOM   5677  N  N   . PHE C  1 48  ? 87.078  17.345  34.261  1.00 7.82  ? 48   PHE C N   1 
ATOM   5678  C  CA  . PHE C  1 48  ? 86.219  16.357  34.917  1.00 7.87  ? 48   PHE C CA  1 
ATOM   5679  C  C   . PHE C  1 48  ? 84.765  16.666  34.613  1.00 8.58  ? 48   PHE C C   1 
ATOM   5680  O  O   . PHE C  1 48  ? 84.429  17.776  34.183  1.00 8.98  ? 48   PHE C O   1 
ATOM   5681  C  CB  . PHE C  1 48  ? 86.475  16.273  36.458  1.00 7.34  ? 48   PHE C CB  1 
ATOM   5682  C  CG  . PHE C  1 48  ? 86.588  17.637  37.167  1.00 9.62  ? 48   PHE C CG  1 
ATOM   5683  C  CD1 . PHE C  1 48  ? 85.441  18.347  37.580  1.00 11.60 ? 48   PHE C CD1 1 
ATOM   5684  C  CD2 . PHE C  1 48  ? 87.838  18.178  37.453  1.00 9.29  ? 48   PHE C CD2 1 
ATOM   5685  C  CE1 . PHE C  1 48  ? 85.544  19.625  38.204  1.00 13.06 ? 48   PHE C CE1 1 
ATOM   5686  C  CE2 . PHE C  1 48  ? 87.950  19.461  38.081  1.00 12.12 ? 48   PHE C CE2 1 
ATOM   5687  C  CZ  . PHE C  1 48  ? 86.792  20.178  38.459  1.00 9.71  ? 48   PHE C CZ  1 
ATOM   5688  N  N   . THR C  1 49  ? 83.911  15.669  34.813  1.00 8.35  ? 49   THR C N   1 
ATOM   5689  C  CA  . THR C  1 49  ? 82.481  15.822  34.724  1.00 8.61  ? 49   THR C CA  1 
ATOM   5690  C  C   . THR C  1 49  ? 81.959  15.617  36.136  1.00 8.99  ? 49   THR C C   1 
ATOM   5691  O  O   . THR C  1 49  ? 82.462  14.742  36.849  1.00 9.83  ? 49   THR C O   1 
ATOM   5692  C  CB  . THR C  1 49  ? 81.900  14.781  33.763  1.00 8.08  ? 49   THR C CB  1 
ATOM   5693  O  OG1 . THR C  1 49  ? 82.311  15.085  32.424  1.00 7.98  ? 49   THR C OG1 1 
ATOM   5694  C  CG2 . THR C  1 49  ? 80.355  14.927  33.680  1.00 8.05  ? 49   THR C CG2 1 
ATOM   5695  N  N   . LEU C  1 50  ? 80.985  16.426  36.549  1.00 7.31  ? 50   LEU C N   1 
ATOM   5696  C  CA  . LEU C  1 50  ? 80.330  16.193  37.834  1.00 6.97  ? 50   LEU C CA  1 
ATOM   5697  C  C   . LEU C  1 50  ? 78.854  16.230  37.542  1.00 8.70  ? 50   LEU C C   1 
ATOM   5698  O  O   . LEU C  1 50  ? 78.339  17.263  37.102  1.00 8.99  ? 50   LEU C O   1 
ATOM   5699  C  CB  . LEU C  1 50  ? 80.682  17.294  38.842  1.00 6.47  ? 50   LEU C CB  1 
ATOM   5700  C  CG  . LEU C  1 50  ? 80.178  17.054  40.276  1.00 6.64  ? 50   LEU C CG  1 
ATOM   5701  C  CD1 . LEU C  1 50  ? 81.152  17.616  41.298  1.00 12.13 ? 50   LEU C CD1 1 
ATOM   5702  C  CD2 . LEU C  1 50  ? 78.715  17.532  40.523  1.00 10.32 ? 50   LEU C CD2 1 
ATOM   5703  N  N   . MET C  1 51  ? 78.183  15.083  37.747  1.00 9.28  ? 51   MET C N   1 
ATOM   5704  C  CA  . MET C  1 51  ? 76.791  14.952  37.380  1.00 9.36  ? 51   MET C CA  1 
ATOM   5705  C  C   . MET C  1 51  ? 75.957  14.447  38.562  1.00 9.98  ? 51   MET C C   1 
ATOM   5706  O  O   . MET C  1 51  ? 76.454  13.681  39.438  1.00 10.19 ? 51   MET C O   1 
ATOM   5707  C  CB  . MET C  1 51  ? 76.594  14.016  36.158  1.00 10.63 ? 51   MET C CB  1 
ATOM   5708  C  CG  . MET C  1 51  ? 77.176  12.657  36.282  1.00 13.10 ? 51   MET C CG  1 
ATOM   5709  S  SD  . MET C  1 51  ? 76.812  11.746  34.719  1.00 16.06 ? 51   MET C SD  1 
ATOM   5710  C  CE  . MET C  1 51  ? 77.006  10.252  35.339  1.00 14.60 ? 51   MET C CE  1 
ATOM   5711  N  N   . GLY C  1 52  ? 74.690  14.837  38.569  1.00 8.48  ? 52   GLY C N   1 
ATOM   5712  C  CA  . GLY C  1 52  ? 73.779  14.336  39.583  1.00 8.74  ? 52   GLY C CA  1 
ATOM   5713  C  C   . GLY C  1 52  ? 72.790  13.427  38.899  1.00 9.27  ? 52   GLY C C   1 
ATOM   5714  O  O   . GLY C  1 52  ? 72.343  13.732  37.800  1.00 8.79  ? 52   GLY C O   1 
ATOM   5715  N  N   . THR C  1 53  ? 72.440  12.304  39.523  1.00 7.94  ? 53   THR C N   1 
ATOM   5716  C  CA  . THR C  1 53  ? 71.426  11.446  38.918  1.00 8.15  ? 53   THR C CA  1 
ATOM   5717  C  C   . THR C  1 53  ? 70.377  11.214  40.005  1.00 8.75  ? 53   THR C C   1 
ATOM   5718  O  O   . THR C  1 53  ? 70.716  10.713  41.085  1.00 8.04  ? 53   THR C O   1 
ATOM   5719  C  CB  . THR C  1 53  ? 72.044  10.120  38.478  1.00 9.86  ? 53   THR C CB  1 
ATOM   5720  O  OG1 . THR C  1 53  ? 72.971  10.310  37.404  1.00 7.06  ? 53   THR C OG1 1 
ATOM   5721  C  CG2 . THR C  1 53  ? 70.936  9.187   37.887  1.00 9.81  ? 53   THR C CG2 1 
ATOM   5722  N  N   . ASN C  1 54  ? 69.119  11.582  39.733  1.00 8.96  ? 54   ASN C N   1 
ATOM   5723  C  CA  . ASN C  1 54  ? 68.009  11.399  40.680  1.00 8.38  ? 54   ASN C CA  1 
ATOM   5724  C  C   . ASN C  1 54  ? 67.060  10.371  40.079  1.00 8.59  ? 54   ASN C C   1 
ATOM   5725  O  O   . ASN C  1 54  ? 66.782  10.378  38.853  1.00 8.34  ? 54   ASN C O   1 
ATOM   5726  C  CB  . ASN C  1 54  ? 67.287  12.718  40.964  1.00 8.19  ? 54   ASN C CB  1 
ATOM   5727  C  CG  . ASN C  1 54  ? 68.094  13.648  41.889  1.00 8.14  ? 54   ASN C CG  1 
ATOM   5728  O  OD1 . ASN C  1 54  ? 69.030  14.363  41.454  1.00 10.52 ? 54   ASN C OD1 1 
ATOM   5729  N  ND2 . ASN C  1 54  ? 67.701  13.679  43.164  1.00 8.86  ? 54   ASN C ND2 1 
ATOM   5730  N  N   . ALA C  1 55  ? 66.621  9.446   40.921  1.00 7.34  ? 55   ALA C N   1 
ATOM   5731  C  CA  . ALA C  1 55  ? 65.887  8.273   40.432  1.00 6.74  ? 55   ALA C CA  1 
ATOM   5732  C  C   . ALA C  1 55  ? 65.096  7.563   41.526  1.00 6.73  ? 55   ALA C C   1 
ATOM   5733  O  O   . ALA C  1 55  ? 65.480  7.583   42.704  1.00 5.96  ? 55   ALA C O   1 
ATOM   5734  C  CB  . ALA C  1 55  ? 66.826  7.337   39.696  1.00 6.74  ? 55   ALA C CB  1 
ATOM   5735  N  N   . PRO C  1 56  ? 63.957  6.969   41.153  1.00 7.02  ? 56   PRO C N   1 
ATOM   5736  C  CA  . PRO C  1 56  ? 63.147  6.190   42.091  1.00 6.21  ? 56   PRO C CA  1 
ATOM   5737  C  C   . PRO C  1 56  ? 63.637  4.727   42.209  1.00 7.80  ? 56   PRO C C   1 
ATOM   5738  O  O   . PRO C  1 56  ? 64.454  4.210   41.411  1.00 9.75  ? 56   PRO C O   1 
ATOM   5739  C  CB  . PRO C  1 56  ? 61.737  6.239   41.450  1.00 5.16  ? 56   PRO C CB  1 
ATOM   5740  C  CG  . PRO C  1 56  ? 62.031  6.199   39.964  1.00 6.70  ? 56   PRO C CG  1 
ATOM   5741  C  CD  . PRO C  1 56  ? 63.306  7.093   39.837  1.00 6.81  ? 56   PRO C CD  1 
ATOM   5742  N  N   . HIS C  1 57  ? 63.148  4.061   43.236  1.00 6.79  ? 57   HIS C N   1 
ATOM   5743  C  CA  . HIS C  1 57  ? 63.388  2.643   43.386  1.00 8.12  ? 57   HIS C CA  1 
ATOM   5744  C  C   . HIS C  1 57  ? 63.206  1.908   42.050  1.00 8.53  ? 57   HIS C C   1 
ATOM   5745  O  O   . HIS C  1 57  ? 62.264  2.198   41.318  1.00 7.25  ? 57   HIS C O   1 
ATOM   5746  C  CB  . HIS C  1 57  ? 62.366  2.039   44.374  1.00 6.95  ? 57   HIS C CB  1 
ATOM   5747  C  CG  . HIS C  1 57  ? 62.465  0.546   44.432  1.00 7.11  ? 57   HIS C CG  1 
ATOM   5748  N  ND1 . HIS C  1 57  ? 63.491  -0.104  45.091  1.00 8.11  ? 57   HIS C ND1 1 
ATOM   5749  C  CD2 . HIS C  1 57  ? 61.728  -0.419  43.840  1.00 8.17  ? 57   HIS C CD2 1 
ATOM   5750  C  CE1 . HIS C  1 57  ? 63.382  -1.413  44.901  1.00 7.10  ? 57   HIS C CE1 1 
ATOM   5751  N  NE2 . HIS C  1 57  ? 62.332  -1.627  44.125  1.00 12.05 ? 57   HIS C NE2 1 
ATOM   5752  N  N   . SER C  1 58  ? 64.071  0.939   41.738  1.00 9.30  ? 58   SER C N   1 
ATOM   5753  C  CA  . SER C  1 58  ? 63.838  0.070   40.584  1.00 10.07 ? 58   SER C CA  1 
ATOM   5754  C  C   . SER C  1 58  ? 64.155  -1.350  40.983  1.00 10.37 ? 58   SER C C   1 
ATOM   5755  O  O   . SER C  1 58  ? 65.084  -1.561  41.733  1.00 9.30  ? 58   SER C O   1 
ATOM   5756  C  CB  . SER C  1 58  ? 64.737  0.489   39.422  1.00 11.15 ? 58   SER C CB  1 
ATOM   5757  O  OG  . SER C  1 58  ? 64.486  -0.335  38.300  1.00 11.19 ? 58   SER C OG  1 
ATOM   5758  N  N   . ASP C  1 59  ? 63.373  -2.311  40.489  1.00 10.49 ? 59   ASP C N   1 
ATOM   5759  C  CA  . ASP C  1 59  ? 63.656  -3.711  40.703  1.00 11.72 ? 59   ASP C CA  1 
ATOM   5760  C  C   . ASP C  1 59  ? 64.653  -4.235  39.641  1.00 11.38 ? 59   ASP C C   1 
ATOM   5761  O  O   . ASP C  1 59  ? 64.976  -5.439  39.620  1.00 11.44 ? 59   ASP C O   1 
ATOM   5762  C  CB  . ASP C  1 59  ? 62.371  -4.551  40.585  1.00 12.68 ? 59   ASP C CB  1 
ATOM   5763  C  CG  . ASP C  1 59  ? 61.378  -4.298  41.707  1.00 16.43 ? 59   ASP C CG  1 
ATOM   5764  O  OD1 . ASP C  1 59  ? 61.784  -3.942  42.844  1.00 16.74 ? 59   ASP C OD1 1 
ATOM   5765  O  OD2 . ASP C  1 59  ? 60.151  -4.495  41.531  1.00 22.08 ? 59   ASP C OD2 1 
ATOM   5766  N  N   . ALA C  1 60  ? 65.061  -3.374  38.718  1.00 9.65  ? 60   ALA C N   1 
ATOM   5767  C  CA  . ALA C  1 60  ? 65.962  -3.799  37.639  1.00 9.42  ? 60   ALA C CA  1 
ATOM   5768  C  C   . ALA C  1 60  ? 67.265  -3.010  37.743  1.00 9.14  ? 60   ALA C C   1 
ATOM   5769  O  O   . ALA C  1 60  ? 67.283  -1.967  38.351  1.00 8.58  ? 60   ALA C O   1 
ATOM   5770  C  CB  . ALA C  1 60  ? 65.326  -3.553  36.262  1.00 8.21  ? 60   ALA C CB  1 
ATOM   5771  N  N   . LEU C  1 61  ? 68.348  -3.510  37.136  1.00 8.83  ? 61   LEU C N   1 
ATOM   5772  C  CA  . LEU C  1 61  ? 69.627  -2.778  37.088  1.00 8.32  ? 61   LEU C CA  1 
ATOM   5773  C  C   . LEU C  1 61  ? 69.408  -1.411  36.495  1.00 8.56  ? 61   LEU C C   1 
ATOM   5774  O  O   . LEU C  1 61  ? 68.460  -1.198  35.701  1.00 8.67  ? 61   LEU C O   1 
ATOM   5775  C  CB  . LEU C  1 61  ? 70.670  -3.532  36.237  1.00 8.71  ? 61   LEU C CB  1 
ATOM   5776  C  CG  . LEU C  1 61  ? 71.186  -4.787  36.966  1.00 9.46  ? 61   LEU C CG  1 
ATOM   5777  C  CD1 . LEU C  1 61  ? 72.055  -5.580  36.029  1.00 11.01 ? 61   LEU C CD1 1 
ATOM   5778  C  CD2 . LEU C  1 61  ? 71.994  -4.439  38.215  1.00 6.18  ? 61   LEU C CD2 1 
ATOM   5779  N  N   . GLY C  1 62  ? 70.226  -0.456  36.916  1.00 8.33  ? 62   GLY C N   1 
ATOM   5780  C  CA  . GLY C  1 62  ? 70.125  0.905   36.426  1.00 8.08  ? 62   GLY C CA  1 
ATOM   5781  C  C   . GLY C  1 62  ? 70.869  1.101   35.097  1.00 8.29  ? 62   GLY C C   1 
ATOM   5782  O  O   . GLY C  1 62  ? 70.717  2.108   34.438  1.00 8.56  ? 62   GLY C O   1 
ATOM   5783  N  N   . VAL C  1 63  ? 71.679  0.120   34.736  1.00 9.10  ? 63   VAL C N   1 
ATOM   5784  C  CA  . VAL C  1 63  ? 72.442  0.134   33.507  1.00 9.15  ? 63   VAL C CA  1 
ATOM   5785  C  C   . VAL C  1 63  ? 72.989  -1.269  33.306  1.00 8.72  ? 63   VAL C C   1 
ATOM   5786  O  O   . VAL C  1 63  ? 73.216  -1.991  34.270  1.00 8.28  ? 63   VAL C O   1 
ATOM   5787  C  CB  . VAL C  1 63  ? 73.622  1.167   33.591  1.00 8.80  ? 63   VAL C CB  1 
ATOM   5788  C  CG1 . VAL C  1 63  ? 74.690  0.708   34.606  1.00 7.58  ? 63   VAL C CG1 1 
ATOM   5789  C  CG2 . VAL C  1 63  ? 74.246  1.357   32.244  1.00 8.47  ? 63   VAL C CG2 1 
ATOM   5790  N  N   . LEU C  1 64  ? 73.241  -1.667  32.069  1.00 8.73  ? 64   LEU C N   1 
ATOM   5791  C  CA  . LEU C  1 64  ? 73.827  -2.982  31.862  1.00 8.76  ? 64   LEU C CA  1 
ATOM   5792  C  C   . LEU C  1 64  ? 75.298  -2.909  32.232  1.00 8.09  ? 64   LEU C C   1 
ATOM   5793  O  O   . LEU C  1 64  ? 75.892  -1.850  32.113  1.00 8.67  ? 64   LEU C O   1 
ATOM   5794  C  CB  . LEU C  1 64  ? 73.646  -3.450  30.411  1.00 9.65  ? 64   LEU C CB  1 
ATOM   5795  C  CG  . LEU C  1 64  ? 72.247  -3.915  30.040  1.00 9.86  ? 64   LEU C CG  1 
ATOM   5796  C  CD1 . LEU C  1 64  ? 72.152  -4.051  28.515  1.00 11.56 ? 64   LEU C CD1 1 
ATOM   5797  C  CD2 . LEU C  1 64  ? 71.838  -5.260  30.781  1.00 10.96 ? 64   LEU C CD2 1 
ATOM   5798  N  N   . PRO C  1 65  ? 75.901  -4.007  32.678  1.00 8.17  ? 65   PRO C N   1 
ATOM   5799  C  CA  . PRO C  1 65  ? 77.317  -3.967  33.087  1.00 7.73  ? 65   PRO C CA  1 
ATOM   5800  C  C   . PRO C  1 65  ? 78.251  -3.584  31.947  1.00 7.59  ? 65   PRO C C   1 
ATOM   5801  O  O   . PRO C  1 65  ? 78.035  -3.987  30.804  1.00 8.69  ? 65   PRO C O   1 
ATOM   5802  C  CB  . PRO C  1 65  ? 77.608  -5.417  33.507  1.00 7.77  ? 65   PRO C CB  1 
ATOM   5803  C  CG  . PRO C  1 65  ? 76.244  -5.940  33.873  1.00 8.64  ? 65   PRO C CG  1 
ATOM   5804  C  CD  . PRO C  1 65  ? 75.323  -5.352  32.837  1.00 7.78  ? 65   PRO C CD  1 
ATOM   5805  N  N   . HIS C  1 66  ? 79.314  -2.865  32.287  1.00 6.60  ? 66   HIS C N   1 
ATOM   5806  C  CA  . HIS C  1 66  ? 80.174  -2.208  31.322  1.00 6.66  ? 66   HIS C CA  1 
ATOM   5807  C  C   . HIS C  1 66  ? 81.508  -1.847  31.981  1.00 6.86  ? 66   HIS C C   1 
ATOM   5808  O  O   . HIS C  1 66  ? 81.628  -1.862  33.209  1.00 7.64  ? 66   HIS C O   1 
ATOM   5809  C  CB  . HIS C  1 66  ? 79.452  -0.939  30.730  1.00 4.93  ? 66   HIS C CB  1 
ATOM   5810  C  CG  . HIS C  1 66  ? 79.269  0.198   31.700  1.00 5.13  ? 66   HIS C CG  1 
ATOM   5811  N  ND1 . HIS C  1 66  ? 78.173  0.309   32.531  1.00 5.34  ? 66   HIS C ND1 1 
ATOM   5812  C  CD2 . HIS C  1 66  ? 80.047  1.273   31.974  1.00 5.37  ? 66   HIS C CD2 1 
ATOM   5813  C  CE1 . HIS C  1 66  ? 78.275  1.398   33.271  1.00 6.08  ? 66   HIS C CE1 1 
ATOM   5814  N  NE2 . HIS C  1 66  ? 79.403  2.009   32.952  1.00 8.29  ? 66   HIS C NE2 1 
ATOM   5815  N  N   . ILE C  1 67  ? 82.482  -1.485  31.147  1.00 7.15  ? 67   ILE C N   1 
ATOM   5816  C  CA  . ILE C  1 67  ? 83.800  -1.007  31.528  1.00 8.15  ? 67   ILE C CA  1 
ATOM   5817  C  C   . ILE C  1 67  ? 84.067  0.334   30.784  1.00 8.30  ? 67   ILE C C   1 
ATOM   5818  O  O   . ILE C  1 67  ? 83.541  0.546   29.681  1.00 8.89  ? 67   ILE C O   1 
ATOM   5819  C  CB  . ILE C  1 67  ? 84.860  -2.085  31.099  1.00 9.12  ? 67   ILE C CB  1 
ATOM   5820  C  CG1 . ILE C  1 67  ? 85.202  -3.039  32.233  1.00 8.34  ? 67   ILE C CG1 1 
ATOM   5821  C  CG2 . ILE C  1 67  ? 86.174  -1.449  30.587  1.00 11.52 ? 67   ILE C CG2 1 
ATOM   5822  C  CD1 . ILE C  1 67  ? 85.954  -4.337  31.735  1.00 14.19 ? 67   ILE C CD1 1 
ATOM   5823  N  N   . HIS C  1 68  ? 84.856  1.217   31.390  1.00 7.57  ? 68   HIS C N   1 
ATOM   5824  C  CA  . HIS C  1 68  ? 85.494  2.364   30.697  1.00 8.42  ? 68   HIS C CA  1 
ATOM   5825  C  C   . HIS C  1 68  ? 86.993  2.136   30.665  1.00 9.09  ? 68   HIS C C   1 
ATOM   5826  O  O   . HIS C  1 68  ? 87.587  1.877   31.698  1.00 9.40  ? 68   HIS C O   1 
ATOM   5827  C  CB  . HIS C  1 68  ? 85.211  3.668   31.402  1.00 7.14  ? 68   HIS C CB  1 
ATOM   5828  C  CG  . HIS C  1 68  ? 83.783  3.799   31.809  1.00 7.44  ? 68   HIS C CG  1 
ATOM   5829  N  ND1 . HIS C  1 68  ? 82.775  3.951   30.887  1.00 8.23  ? 68   HIS C ND1 1 
ATOM   5830  C  CD2 . HIS C  1 68  ? 83.191  3.772   33.024  1.00 8.41  ? 68   HIS C CD2 1 
ATOM   5831  C  CE1 . HIS C  1 68  ? 81.614  4.009   31.523  1.00 12.03 ? 68   HIS C CE1 1 
ATOM   5832  N  NE2 . HIS C  1 68  ? 81.836  3.876   32.819  1.00 9.52  ? 68   HIS C NE2 1 
ATOM   5833  N  N   . GLN C  1 69  ? 87.595  2.292   29.489  1.00 8.87  ? 69   GLN C N   1 
ATOM   5834  C  CA  . GLN C  1 69  ? 89.031  2.038   29.335  1.00 8.93  ? 69   GLN C CA  1 
ATOM   5835  C  C   . GLN C  1 69  ? 89.843  3.273   29.667  1.00 8.81  ? 69   GLN C C   1 
ATOM   5836  O  O   . GLN C  1 69  ? 91.009  3.154   30.058  1.00 7.24  ? 69   GLN C O   1 
ATOM   5837  C  CB  . GLN C  1 69  ? 89.371  1.529   27.939  1.00 8.58  ? 69   GLN C CB  1 
ATOM   5838  C  CG  . GLN C  1 69  ? 88.881  0.085   27.657  1.00 9.62  ? 69   GLN C CG  1 
ATOM   5839  C  CD  . GLN C  1 69  ? 89.271  -0.438  26.274  1.00 13.57 ? 69   GLN C CD  1 
ATOM   5840  O  OE1 . GLN C  1 69  ? 90.034  0.206   25.552  1.00 12.94 ? 69   GLN C OE1 1 
ATOM   5841  N  NE2 . GLN C  1 69  ? 88.781  -1.632  25.924  1.00 14.69 ? 69   GLN C NE2 1 
ATOM   5842  N  N   . LYS C  1 70  ? 89.198  4.432   29.535  1.00 8.62  ? 70   LYS C N   1 
ATOM   5843  C  CA  . LYS C  1 70  ? 89.857  5.761   29.652  1.00 9.92  ? 70   LYS C CA  1 
ATOM   5844  C  C   . LYS C  1 70  ? 89.269  6.695   30.704  1.00 9.15  ? 70   LYS C C   1 
ATOM   5845  O  O   . LYS C  1 70  ? 89.827  7.734   30.947  1.00 11.25 ? 70   LYS C O   1 
ATOM   5846  C  CB  . LYS C  1 70  ? 89.907  6.517   28.304  1.00 8.14  ? 70   LYS C CB  1 
ATOM   5847  C  CG  . LYS C  1 70  ? 90.870  5.898   27.296  1.00 11.56 ? 70   LYS C CG  1 
ATOM   5848  C  CD  . LYS C  1 70  ? 90.929  6.750   26.049  1.00 15.75 ? 70   LYS C CD  1 
ATOM   5849  C  CE  . LYS C  1 70  ? 92.341  6.755   25.473  1.00 21.45 ? 70   LYS C CE  1 
ATOM   5850  N  NZ  . LYS C  1 70  ? 92.429  7.246   24.012  1.00 23.83 ? 70   LYS C NZ  1 
ATOM   5851  N  N   . HIS C  1 71  ? 88.161  6.341   31.329  1.00 8.76  ? 71   HIS C N   1 
ATOM   5852  C  CA  . HIS C  1 71  ? 87.599  7.186   32.344  1.00 7.86  ? 71   HIS C CA  1 
ATOM   5853  C  C   . HIS C  1 71  ? 87.588  6.494   33.673  1.00 8.63  ? 71   HIS C C   1 
ATOM   5854  O  O   . HIS C  1 71  ? 87.254  5.308   33.755  1.00 9.42  ? 71   HIS C O   1 
ATOM   5855  C  CB  . HIS C  1 71  ? 86.170  7.591   31.999  1.00 7.87  ? 71   HIS C CB  1 
ATOM   5856  C  CG  . HIS C  1 71  ? 86.076  8.473   30.799  1.00 9.06  ? 71   HIS C CG  1 
ATOM   5857  N  ND1 . HIS C  1 71  ? 86.073  7.976   29.513  1.00 7.86  ? 71   HIS C ND1 1 
ATOM   5858  C  CD2 . HIS C  1 71  ? 86.007  9.821   30.687  1.00 5.46  ? 71   HIS C CD2 1 
ATOM   5859  C  CE1 . HIS C  1 71  ? 86.006  8.985   28.655  1.00 10.00 ? 71   HIS C CE1 1 
ATOM   5860  N  NE2 . HIS C  1 71  ? 85.994  10.116  29.343  1.00 8.28  ? 71   HIS C NE2 1 
ATOM   5861  N  N   . TYR C  1 72  ? 87.913  7.256   34.717  1.00 8.04  ? 72   TYR C N   1 
ATOM   5862  C  CA  . TYR C  1 72  ? 87.804  6.787   36.095  1.00 9.67  ? 72   TYR C CA  1 
ATOM   5863  C  C   . TYR C  1 72  ? 86.479  7.330   36.621  1.00 10.00 ? 72   TYR C C   1 
ATOM   5864  O  O   . TYR C  1 72  ? 86.216  8.557   36.584  1.00 10.37 ? 72   TYR C O   1 
ATOM   5865  C  CB  . TYR C  1 72  ? 88.987  7.342   36.897  1.00 9.58  ? 72   TYR C CB  1 
ATOM   5866  C  CG  . TYR C  1 72  ? 89.275  6.701   38.256  1.00 9.94  ? 72   TYR C CG  1 
ATOM   5867  C  CD1 . TYR C  1 72  ? 88.280  6.567   39.213  1.00 9.67  ? 72   TYR C CD1 1 
ATOM   5868  C  CD2 . TYR C  1 72  ? 90.581  6.294   38.593  1.00 7.45  ? 72   TYR C CD2 1 
ATOM   5869  C  CE1 . TYR C  1 72  ? 88.555  6.054   40.480  1.00 8.26  ? 72   TYR C CE1 1 
ATOM   5870  C  CE2 . TYR C  1 72  ? 90.874  5.765   39.852  1.00 10.79 ? 72   TYR C CE2 1 
ATOM   5871  C  CZ  . TYR C  1 72  ? 89.857  5.664   40.799  1.00 10.36 ? 72   TYR C CZ  1 
ATOM   5872  O  OH  . TYR C  1 72  ? 90.077  5.125   42.053  1.00 10.27 ? 72   TYR C OH  1 
ATOM   5873  N  N   . GLU C  1 73  ? 85.636  6.424   37.088  1.00 9.43  ? 73   GLU C N   1 
ATOM   5874  C  CA  . GLU C  1 73  ? 84.311  6.762   37.558  1.00 11.42 ? 73   GLU C CA  1 
ATOM   5875  C  C   . GLU C  1 73  ? 84.241  6.720   39.096  1.00 10.68 ? 73   GLU C C   1 
ATOM   5876  O  O   . GLU C  1 73  ? 84.775  5.801   39.704  1.00 11.31 ? 73   GLU C O   1 
ATOM   5877  C  CB  . GLU C  1 73  ? 83.356  5.763   36.975  1.00 12.56 ? 73   GLU C CB  1 
ATOM   5878  C  CG  . GLU C  1 73  ? 82.065  6.386   36.534  1.00 21.52 ? 73   GLU C CG  1 
ATOM   5879  C  CD  . GLU C  1 73  ? 81.551  5.791   35.241  1.00 28.74 ? 73   GLU C CD  1 
ATOM   5880  O  OE1 . GLU C  1 73  ? 81.387  4.540   35.180  1.00 31.90 ? 73   GLU C OE1 1 
ATOM   5881  O  OE2 . GLU C  1 73  ? 81.251  6.578   34.296  1.00 33.66 ? 73   GLU C OE2 1 
ATOM   5882  N  N   . ASN C  1 74  ? 83.568  7.712   39.687  1.00 10.08 ? 74   ASN C N   1 
ATOM   5883  C  CA  . ASN C  1 74  ? 83.397  7.890   41.139  1.00 8.88  ? 74   ASN C CA  1 
ATOM   5884  C  C   . ASN C  1 74  ? 81.926  8.041   41.465  1.00 9.29  ? 74   ASN C C   1 
ATOM   5885  O  O   . ASN C  1 74  ? 81.221  8.897   40.898  1.00 9.47  ? 74   ASN C O   1 
ATOM   5886  C  CB  . ASN C  1 74  ? 84.180  9.104   41.637  1.00 8.20  ? 74   ASN C CB  1 
ATOM   5887  C  CG  . ASN C  1 74  ? 85.662  8.978   41.360  1.00 9.12  ? 74   ASN C CG  1 
ATOM   5888  O  OD1 . ASN C  1 74  ? 86.395  8.365   42.140  1.00 9.18  ? 74   ASN C OD1 1 
ATOM   5889  N  ND2 . ASN C  1 74  ? 86.097  9.481   40.224  1.00 5.58  ? 74   ASN C ND2 1 
ATOM   5890  N  N   . PHE C  1 75  ? 81.465  7.187   42.380  1.00 8.94  ? 75   PHE C N   1 
ATOM   5891  C  CA  . PHE C  1 75  ? 80.050  7.130   42.743  1.00 9.03  ? 75   PHE C CA  1 
ATOM   5892  C  C   . PHE C  1 75  ? 79.898  7.640   44.151  1.00 9.62  ? 75   PHE C C   1 
ATOM   5893  O  O   . PHE C  1 75  ? 80.466  7.056   45.100  1.00 9.94  ? 75   PHE C O   1 
ATOM   5894  C  CB  . PHE C  1 75  ? 79.524  5.663   42.674  1.00 10.63 ? 75   PHE C CB  1 
ATOM   5895  C  CG  . PHE C  1 75  ? 79.339  5.144   41.277  1.00 9.43  ? 75   PHE C CG  1 
ATOM   5896  C  CD1 . PHE C  1 75  ? 80.422  4.731   40.530  1.00 10.34 ? 75   PHE C CD1 1 
ATOM   5897  C  CD2 . PHE C  1 75  ? 78.059  5.083   40.717  1.00 15.14 ? 75   PHE C CD2 1 
ATOM   5898  C  CE1 . PHE C  1 75  ? 80.269  4.234   39.256  1.00 9.35  ? 75   PHE C CE1 1 
ATOM   5899  C  CE2 . PHE C  1 75  ? 77.864  4.602   39.435  1.00 15.93 ? 75   PHE C CE2 1 
ATOM   5900  C  CZ  . PHE C  1 75  ? 78.982  4.183   38.678  1.00 14.24 ? 75   PHE C CZ  1 
ATOM   5901  N  N   . TYR C  1 76  ? 79.081  8.683   44.325  1.00 8.56  ? 76   TYR C N   1 
ATOM   5902  C  CA  . TYR C  1 76  ? 78.861  9.231   45.656  1.00 9.22  ? 76   TYR C CA  1 
ATOM   5903  C  C   . TYR C  1 76  ? 77.355  9.297   45.903  1.00 11.45 ? 76   TYR C C   1 
ATOM   5904  O  O   . TYR C  1 76  ? 76.605  9.847   45.102  1.00 11.13 ? 76   TYR C O   1 
ATOM   5905  C  CB  . TYR C  1 76  ? 79.510  10.628  45.788  1.00 8.04  ? 76   TYR C CB  1 
ATOM   5906  C  CG  . TYR C  1 76  ? 79.431  11.213  47.170  1.00 9.04  ? 76   TYR C CG  1 
ATOM   5907  C  CD1 . TYR C  1 76  ? 80.344  10.810  48.175  1.00 6.96  ? 76   TYR C CD1 1 
ATOM   5908  C  CD2 . TYR C  1 76  ? 78.429  12.147  47.506  1.00 8.15  ? 76   TYR C CD2 1 
ATOM   5909  C  CE1 . TYR C  1 76  ? 80.262  11.333  49.460  1.00 9.31  ? 76   TYR C CE1 1 
ATOM   5910  C  CE2 . TYR C  1 76  ? 78.364  12.711  48.792  1.00 12.48 ? 76   TYR C CE2 1 
ATOM   5911  C  CZ  . TYR C  1 76  ? 79.282  12.273  49.774  1.00 10.34 ? 76   TYR C CZ  1 
ATOM   5912  O  OH  . TYR C  1 76  ? 79.241  12.754  51.081  1.00 12.33 ? 76   TYR C OH  1 
ATOM   5913  N  N   . CYS C  1 77  ? 76.923  8.798   47.048  1.00 10.28 ? 77   CYS C N   1 
ATOM   5914  C  CA  . CYS C  1 77  ? 75.496  8.812   47.340  1.00 10.93 ? 77   CYS C CA  1 
ATOM   5915  C  C   . CYS C  1 77  ? 75.127  10.040  48.173  1.00 10.85 ? 77   CYS C C   1 
ATOM   5916  O  O   . CYS C  1 77  ? 75.546  10.159  49.334  1.00 11.13 ? 77   CYS C O   1 
ATOM   5917  C  CB  . CYS C  1 77  ? 75.094  7.515   48.063  1.00 9.59  ? 77   CYS C CB  1 
ATOM   5918  S  SG  . CYS C  1 77  ? 73.324  7.568   48.506  1.00 9.72  ? 77   CYS C SG  1 
ATOM   5919  N  N   . ASN C  1 78  ? 74.407  10.975  47.559  1.00 10.88 ? 78   ASN C N   1 
ATOM   5920  C  CA  . ASN C  1 78  ? 73.992  12.224  48.229  1.00 11.32 ? 78   ASN C CA  1 
ATOM   5921  C  C   . ASN C  1 78  ? 72.877  11.943  49.185  1.00 10.58 ? 78   ASN C C   1 
ATOM   5922  O  O   . ASN C  1 78  ? 72.859  12.513  50.250  1.00 10.46 ? 78   ASN C O   1 
ATOM   5923  C  CB  . ASN C  1 78  ? 73.549  13.229  47.160  1.00 12.41 ? 78   ASN C CB  1 
ATOM   5924  C  CG  A ASN C  1 78  ? 74.579  13.431  46.175  0.50 12.47 ? 78   ASN C CG  1 
ATOM   5925  C  CG  B ASN C  1 78  ? 73.053  14.529  47.705  0.50 13.28 ? 78   ASN C CG  1 
ATOM   5926  O  OD1 A ASN C  1 78  ? 74.598  12.756  45.169  0.50 13.70 ? 78   ASN C OD1 1 
ATOM   5927  O  OD1 B ASN C  1 78  ? 73.849  15.398  48.109  0.50 17.90 ? 78   ASN C OD1 1 
ATOM   5928  N  ND2 A ASN C  1 78  ? 75.501  14.332  46.465  0.50 15.69 ? 78   ASN C ND2 1 
ATOM   5929  N  ND2 B ASN C  1 78  ? 71.734  14.735  47.629  0.50 13.61 ? 78   ASN C ND2 1 
ATOM   5930  N  N   . LYS C  1 79  ? 71.959  11.054  48.796  1.00 9.18  ? 79   LYS C N   1 
ATOM   5931  C  CA  . LYS C  1 79  ? 70.796  10.668  49.628  1.00 10.07 ? 79   LYS C CA  1 
ATOM   5932  C  C   . LYS C  1 79  ? 70.173  9.384   49.026  1.00 8.66  ? 79   LYS C C   1 
ATOM   5933  O  O   . LYS C  1 79  ? 70.452  9.036   47.892  1.00 9.34  ? 79   LYS C O   1 
ATOM   5934  C  CB  . LYS C  1 79  ? 69.709  11.754  49.738  1.00 7.33  ? 79   LYS C CB  1 
ATOM   5935  C  CG  . LYS C  1 79  ? 69.162  12.277  48.385  1.00 9.35  ? 79   LYS C CG  1 
ATOM   5936  C  CD  . LYS C  1 79  ? 68.020  13.317  48.645  1.00 8.02  ? 79   LYS C CD  1 
ATOM   5937  C  CE  . LYS C  1 79  ? 67.491  13.837  47.298  1.00 8.81  ? 79   LYS C CE  1 
ATOM   5938  N  NZ  . LYS C  1 79  ? 66.254  14.620  47.542  1.00 10.21 ? 79   LYS C NZ  1 
ATOM   5939  N  N   . GLY C  1 80  ? 69.327  8.744   49.793  1.00 8.34  ? 80   GLY C N   1 
ATOM   5940  C  CA  . GLY C  1 80  ? 68.654  7.520   49.376  1.00 6.68  ? 80   GLY C CA  1 
ATOM   5941  C  C   . GLY C  1 80  ? 69.719  6.424   49.376  1.00 7.38  ? 80   GLY C C   1 
ATOM   5942  O  O   . GLY C  1 80  ? 70.583  6.380   50.257  1.00 7.29  ? 80   GLY C O   1 
ATOM   5943  N  N   . SER C  1 81  ? 69.634  5.496   48.420  1.00 7.94  ? 81   SER C N   1 
ATOM   5944  C  CA  . SER C  1 81  ? 70.564  4.387   48.368  1.00 8.23  ? 81   SER C CA  1 
ATOM   5945  C  C   . SER C  1 81  ? 70.512  3.678   47.037  1.00 8.05  ? 81   SER C C   1 
ATOM   5946  O  O   . SER C  1 81  ? 69.432  3.576   46.398  1.00 7.81  ? 81   SER C O   1 
ATOM   5947  C  CB  . SER C  1 81  ? 70.376  3.383   49.535  1.00 8.40  ? 81   SER C CB  1 
ATOM   5948  O  OG  . SER C  1 81  ? 69.138  2.696   49.481  1.00 10.48 ? 81   SER C OG  1 
ATOM   5949  N  N   . PHE C  1 82  ? 71.688  3.155   46.678  1.00 8.05  ? 82   PHE C N   1 
ATOM   5950  C  CA  . PHE C  1 82  ? 71.882  2.357   45.472  1.00 7.08  ? 82   PHE C CA  1 
ATOM   5951  C  C   . PHE C  1 82  ? 72.964  1.326   45.704  1.00 8.24  ? 82   PHE C C   1 
ATOM   5952  O  O   . PHE C  1 82  ? 73.904  1.563   46.482  1.00 7.17  ? 82   PHE C O   1 
ATOM   5953  C  CB  . PHE C  1 82  ? 72.188  3.223   44.206  1.00 6.89  ? 82   PHE C CB  1 
ATOM   5954  C  CG  . PHE C  1 82  ? 73.414  4.071   44.304  1.00 5.87  ? 82   PHE C CG  1 
ATOM   5955  C  CD1 . PHE C  1 82  ? 74.639  3.567   43.873  1.00 8.83  ? 82   PHE C CD1 1 
ATOM   5956  C  CD2 . PHE C  1 82  ? 73.359  5.399   44.777  1.00 8.94  ? 82   PHE C CD2 1 
ATOM   5957  C  CE1 . PHE C  1 82  ? 75.807  4.345   43.932  1.00 7.49  ? 82   PHE C CE1 1 
ATOM   5958  C  CE2 . PHE C  1 82  ? 74.514  6.202   44.844  1.00 8.37  ? 82   PHE C CE2 1 
ATOM   5959  C  CZ  . PHE C  1 82  ? 75.757  5.663   44.413  1.00 10.70 ? 82   PHE C CZ  1 
ATOM   5960  N  N   . GLN C  1 83  ? 72.784  0.166   45.060  1.00 8.82  ? 83   GLN C N   1 
ATOM   5961  C  CA  . GLN C  1 83  ? 73.765  -0.894  45.095  1.00 7.76  ? 83   GLN C CA  1 
ATOM   5962  C  C   . GLN C  1 83  ? 74.730  -0.634  43.945  1.00 7.49  ? 83   GLN C C   1 
ATOM   5963  O  O   . GLN C  1 83  ? 74.324  -0.168  42.870  1.00 6.57  ? 83   GLN C O   1 
ATOM   5964  C  CB  . GLN C  1 83  ? 73.102  -2.249  44.930  1.00 8.45  ? 83   GLN C CB  1 
ATOM   5965  C  CG  . GLN C  1 83  ? 74.106  -3.383  45.287  1.00 8.97  ? 83   GLN C CG  1 
ATOM   5966  C  CD  . GLN C  1 83  ? 73.489  -4.648  45.843  1.00 6.23  ? 83   GLN C CD  1 
ATOM   5967  O  OE1 . GLN C  1 83  ? 74.211  -5.668  46.071  1.00 10.12 ? 83   GLN C OE1 1 
ATOM   5968  N  NE2 . GLN C  1 83  ? 72.207  -4.628  46.079  1.00 7.56  ? 83   GLN C NE2 1 
ATOM   5969  N  N   . LEU C  1 84  ? 76.016  -0.876  44.199  1.00 8.12  ? 84   LEU C N   1 
ATOM   5970  C  CA  . LEU C  1 84  ? 77.039  -0.770  43.190  1.00 7.04  ? 84   LEU C CA  1 
ATOM   5971  C  C   . LEU C  1 84  ? 77.769  -2.088  43.177  1.00 6.98  ? 84   LEU C C   1 
ATOM   5972  O  O   . LEU C  1 84  ? 78.131  -2.560  44.232  1.00 6.69  ? 84   LEU C O   1 
ATOM   5973  C  CB  . LEU C  1 84  ? 77.972  0.370   43.560  1.00 6.65  ? 84   LEU C CB  1 
ATOM   5974  C  CG  . LEU C  1 84  ? 79.169  0.620   42.655  1.00 7.14  ? 84   LEU C CG  1 
ATOM   5975  C  CD1 . LEU C  1 84  ? 78.646  1.112   41.241  1.00 7.35  ? 84   LEU C CD1 1 
ATOM   5976  C  CD2 . LEU C  1 84  ? 80.015  1.743   43.314  1.00 8.87  ? 84   LEU C CD2 1 
ATOM   5977  N  N   . TRP C  1 85  ? 77.959  -2.674  41.983  1.00 6.56  ? 85   TRP C N   1 
ATOM   5978  C  CA  . TRP C  1 85  ? 78.790  -3.854  41.796  1.00 6.23  ? 85   TRP C CA  1 
ATOM   5979  C  C   . TRP C  1 85  ? 80.040  -3.455  41.027  1.00 6.44  ? 85   TRP C C   1 
ATOM   5980  O  O   . TRP C  1 85  ? 79.960  -2.601  40.115  1.00 5.67  ? 85   TRP C O   1 
ATOM   5981  C  CB  . TRP C  1 85  ? 78.046  -4.924  40.965  1.00 5.96  ? 85   TRP C CB  1 
ATOM   5982  C  CG  . TRP C  1 85  ? 76.842  -5.561  41.649  1.00 5.53  ? 85   TRP C CG  1 
ATOM   5983  C  CD1 . TRP C  1 85  ? 76.804  -6.803  42.276  1.00 9.23  ? 85   TRP C CD1 1 
ATOM   5984  C  CD2 . TRP C  1 85  ? 75.508  -5.048  41.716  1.00 3.80  ? 85   TRP C CD2 1 
ATOM   5985  N  NE1 . TRP C  1 85  ? 75.536  -7.050  42.753  1.00 6.51  ? 85   TRP C NE1 1 
ATOM   5986  C  CE2 . TRP C  1 85  ? 74.727  -5.987  42.420  1.00 3.78  ? 85   TRP C CE2 1 
ATOM   5987  C  CE3 . TRP C  1 85  ? 74.884  -3.869  41.242  1.00 2.00  ? 85   TRP C CE3 1 
ATOM   5988  C  CZ2 . TRP C  1 85  ? 73.376  -5.815  42.647  1.00 3.19  ? 85   TRP C CZ2 1 
ATOM   5989  C  CZ3 . TRP C  1 85  ? 73.555  -3.694  41.475  1.00 2.00  ? 85   TRP C CZ3 1 
ATOM   5990  C  CH2 . TRP C  1 85  ? 72.800  -4.642  42.173  1.00 5.46  ? 85   TRP C CH2 1 
ATOM   5991  N  N   . ALA C  1 86  ? 81.166  -4.110  41.340  1.00 6.24  ? 86   ALA C N   1 
ATOM   5992  C  CA  . ALA C  1 86  ? 82.445  -3.823  40.683  1.00 6.68  ? 86   ALA C CA  1 
ATOM   5993  C  C   . ALA C  1 86  ? 83.388  -4.970  40.682  1.00 7.16  ? 86   ALA C C   1 
ATOM   5994  O  O   . ALA C  1 86  ? 83.501  -5.732  41.686  1.00 7.75  ? 86   ALA C O   1 
ATOM   5995  C  CB  . ALA C  1 86  ? 83.160  -2.589  41.325  1.00 7.59  ? 86   ALA C CB  1 
ATOM   5996  N  N   . GLN C  1 87  ? 84.116  -5.108  39.571  1.00 6.58  ? 87   GLN C N   1 
ATOM   5997  C  CA  . GLN C  1 87  ? 85.133  -6.158  39.513  1.00 7.27  ? 87   GLN C CA  1 
ATOM   5998  C  C   . GLN C  1 87  ? 86.281  -5.788  38.591  1.00 7.50  ? 87   GLN C C   1 
ATOM   5999  O  O   . GLN C  1 87  ? 86.063  -5.342  37.446  1.00 5.42  ? 87   GLN C O   1 
ATOM   6000  C  CB  . GLN C  1 87  ? 84.525  -7.506  39.109  1.00 6.81  ? 87   GLN C CB  1 
ATOM   6001  C  CG  . GLN C  1 87  ? 85.523  -8.654  39.104  1.00 7.24  ? 87   GLN C CG  1 
ATOM   6002  C  CD  . GLN C  1 87  ? 84.955  -9.990  38.604  1.00 9.67  ? 87   GLN C CD  1 
ATOM   6003  O  OE1 . GLN C  1 87  ? 83.991  -10.035 37.843  1.00 11.03 ? 87   GLN C OE1 1 
ATOM   6004  N  NE2 . GLN C  1 87  ? 85.590  -11.083 39.016  1.00 11.47 ? 87   GLN C NE2 1 
ATOM   6005  N  N   . SER C  1 88  ? 87.497  -5.961  39.104  1.00 8.74  ? 88   SER C N   1 
ATOM   6006  C  CA  . SER C  1 88  ? 88.696  -5.784  38.281  1.00 10.91 ? 88   SER C CA  1 
ATOM   6007  C  C   . SER C  1 88  ? 89.233  -7.167  37.912  1.00 12.10 ? 88   SER C C   1 
ATOM   6008  O  O   . SER C  1 88  ? 89.325  -8.034  38.790  1.00 12.91 ? 88   SER C O   1 
ATOM   6009  C  CB  . SER C  1 88  ? 89.789  -4.999  39.034  1.00 10.79 ? 88   SER C CB  1 
ATOM   6010  O  OG  . SER C  1 88  ? 91.047  -5.059  38.312  1.00 11.50 ? 88   SER C OG  1 
ATOM   6011  N  N   . GLY C  1 89  ? 89.599  -7.376  36.643  1.00 13.15 ? 89   GLY C N   1 
ATOM   6012  C  CA  . GLY C  1 89  ? 90.253  -8.606  36.222  1.00 14.35 ? 89   GLY C CA  1 
ATOM   6013  C  C   . GLY C  1 89  ? 89.520  -9.826  36.742  1.00 15.71 ? 89   GLY C C   1 
ATOM   6014  O  O   . GLY C  1 89  ? 88.272  -9.860  36.714  1.00 15.67 ? 89   GLY C O   1 
ATOM   6015  N  N   . ASN C  1 90  ? 90.280  -10.803 37.234  1.00 15.83 ? 90   ASN C N   1 
ATOM   6016  C  CA  . ASN C  1 90  ? 89.708  -11.988 37.884  1.00 16.73 ? 90   ASN C CA  1 
ATOM   6017  C  C   . ASN C  1 90  ? 89.724  -11.905 39.425  1.00 15.72 ? 90   ASN C C   1 
ATOM   6018  O  O   . ASN C  1 90  ? 89.760  -12.929 40.119  1.00 14.88 ? 90   ASN C O   1 
ATOM   6019  C  CB  . ASN C  1 90  ? 90.444  -13.247 37.449  1.00 17.74 ? 90   ASN C CB  1 
ATOM   6020  C  CG  . ASN C  1 90  ? 91.944  -13.142 37.661  1.00 22.02 ? 90   ASN C CG  1 
ATOM   6021  O  OD1 . ASN C  1 90  ? 92.436  -12.164 38.258  1.00 26.11 ? 90   ASN C OD1 1 
ATOM   6022  N  ND2 . ASN C  1 90  ? 92.684  -14.138 37.165  1.00 22.90 ? 90   ASN C ND2 1 
ATOM   6023  N  N   . GLU C  1 91  ? 89.757  -10.682 39.940  1.00 13.81 ? 91   GLU C N   1 
ATOM   6024  C  CA  . GLU C  1 91  ? 89.610  -10.445 41.364  1.00 13.59 ? 91   GLU C CA  1 
ATOM   6025  C  C   . GLU C  1 91  ? 88.169  -10.753 41.714  1.00 12.62 ? 91   GLU C C   1 
ATOM   6026  O  O   . GLU C  1 91  ? 87.288  -10.708 40.848  1.00 12.46 ? 91   GLU C O   1 
ATOM   6027  C  CB  . GLU C  1 91  ? 89.899  -8.965  41.698  1.00 13.49 ? 91   GLU C CB  1 
ATOM   6028  C  CG  . GLU C  1 91  ? 91.371  -8.702  41.939  1.00 16.69 ? 91   GLU C CG  1 
ATOM   6029  C  CD  . GLU C  1 91  ? 91.710  -7.225  41.915  1.00 18.84 ? 91   GLU C CD  1 
ATOM   6030  O  OE1 . GLU C  1 91  ? 90.907  -6.395  42.445  1.00 20.99 ? 91   GLU C OE1 1 
ATOM   6031  O  OE2 . GLU C  1 91  ? 92.784  -6.895  41.357  1.00 18.12 ? 91   GLU C OE2 1 
ATOM   6032  N  N   . THR C  1 92  ? 87.942  -11.053 42.995  1.00 11.46 ? 92   THR C N   1 
ATOM   6033  C  CA  . THR C  1 92  ? 86.629  -11.235 43.572  1.00 8.76  ? 92   THR C CA  1 
ATOM   6034  C  C   . THR C  1 92  ? 85.716  -10.074 43.172  1.00 7.53  ? 92   THR C C   1 
ATOM   6035  O  O   . THR C  1 92  ? 86.099  -8.917  43.293  1.00 7.74  ? 92   THR C O   1 
ATOM   6036  C  CB  . THR C  1 92  ? 86.780  -11.273 45.108  1.00 8.58  ? 92   THR C CB  1 
ATOM   6037  O  OG1 . THR C  1 92  ? 87.543  -12.412 45.504  1.00 10.52 ? 92   THR C OG1 1 
ATOM   6038  C  CG2 . THR C  1 92  ? 85.474  -11.534 45.760  1.00 9.86  ? 92   THR C CG2 1 
ATOM   6039  N  N   . GLN C  1 93  ? 84.513  -10.380 42.708  1.00 6.70  ? 93   GLN C N   1 
ATOM   6040  C  CA  . GLN C  1 93  ? 83.516  -9.346  42.442  1.00 6.96  ? 93   GLN C CA  1 
ATOM   6041  C  C   . GLN C  1 93  ? 83.013  -8.747  43.775  1.00 6.71  ? 93   GLN C C   1 
ATOM   6042  O  O   . GLN C  1 93  ? 82.577  -9.497  44.664  1.00 6.91  ? 93   GLN C O   1 
ATOM   6043  C  CB  . GLN C  1 93  ? 82.336  -9.941  41.671  1.00 6.79  ? 93   GLN C CB  1 
ATOM   6044  C  CG  . GLN C  1 93  ? 81.364  -8.850  41.207  1.00 5.61  ? 93   GLN C CG  1 
ATOM   6045  C  CD  . GLN C  1 93  ? 80.003  -9.379  40.832  1.00 6.15  ? 93   GLN C CD  1 
ATOM   6046  O  OE1 . GLN C  1 93  ? 79.003  -8.846  41.279  1.00 7.12  ? 93   GLN C OE1 1 
ATOM   6047  N  NE2 . GLN C  1 93  ? 79.956  -10.396 39.995  1.00 4.80  ? 93   GLN C NE2 1 
ATOM   6048  N  N   . GLN C  1 94  ? 83.048  -7.418  43.893  1.00 6.16  ? 94   GLN C N   1 
ATOM   6049  C  CA  . GLN C  1 94  ? 82.644  -6.716  45.099  1.00 6.68  ? 94   GLN C CA  1 
ATOM   6050  C  C   . GLN C  1 94  ? 81.302  -5.957  44.830  1.00 6.94  ? 94   GLN C C   1 
ATOM   6051  O  O   . GLN C  1 94  ? 81.053  -5.483  43.708  1.00 6.81  ? 94   GLN C O   1 
ATOM   6052  C  CB  . GLN C  1 94  ? 83.692  -5.648  45.493  1.00 5.89  ? 94   GLN C CB  1 
ATOM   6053  C  CG  . GLN C  1 94  ? 85.073  -6.144  45.870  1.00 5.88  ? 94   GLN C CG  1 
ATOM   6054  C  CD  . GLN C  1 94  ? 85.046  -6.878  47.192  1.00 5.09  ? 94   GLN C CD  1 
ATOM   6055  O  OE1 . GLN C  1 94  ? 84.219  -6.571  48.041  1.00 7.29  ? 94   GLN C OE1 1 
ATOM   6056  N  NE2 . GLN C  1 94  ? 85.933  -7.834  47.371  1.00 3.93  ? 94   GLN C NE2 1 
ATOM   6057  N  N   . THR C  1 95  ? 80.471  -5.858  45.859  1.00 6.49  ? 95   THR C N   1 
ATOM   6058  C  CA  . THR C  1 95  ? 79.264  -5.023  45.827  1.00 5.69  ? 95   THR C CA  1 
ATOM   6059  C  C   . THR C  1 95  ? 78.953  -4.415  47.203  1.00 6.59  ? 95   THR C C   1 
ATOM   6060  O  O   . THR C  1 95  ? 79.266  -5.025  48.248  1.00 6.58  ? 95   THR C O   1 
ATOM   6061  C  CB  . THR C  1 95  ? 78.018  -5.804  45.283  1.00 5.44  ? 95   THR C CB  1 
ATOM   6062  O  OG1 . THR C  1 95  ? 76.906  -4.902  45.296  1.00 7.12  ? 95   THR C OG1 1 
ATOM   6063  C  CG2 . THR C  1 95  ? 77.562  -6.966  46.210  1.00 4.51  ? 95   THR C CG2 1 
ATOM   6064  N  N   . ARG C  1 96  ? 78.314  -3.235  47.194  1.00 5.87  ? 96   ARG C N   1 
ATOM   6065  C  CA  . ARG C  1 96  ? 77.957  -2.536  48.417  1.00 6.32  ? 96   ARG C CA  1 
ATOM   6066  C  C   . ARG C  1 96  ? 76.687  -1.774  48.132  1.00 5.73  ? 96   ARG C C   1 
ATOM   6067  O  O   . ARG C  1 96  ? 76.456  -1.329  47.005  1.00 5.62  ? 96   ARG C O   1 
ATOM   6068  C  CB  . ARG C  1 96  ? 78.988  -1.465  48.799  1.00 6.35  ? 96   ARG C CB  1 
ATOM   6069  C  CG  . ARG C  1 96  ? 80.434  -1.915  49.059  1.00 6.99  ? 96   ARG C CG  1 
ATOM   6070  C  CD  . ARG C  1 96  ? 80.616  -2.864  50.227  1.00 6.43  ? 96   ARG C CD  1 
ATOM   6071  N  NE  . ARG C  1 96  ? 82.027  -3.209  50.376  1.00 3.95  ? 96   ARG C NE  1 
ATOM   6072  C  CZ  . ARG C  1 96  ? 82.607  -4.276  49.818  1.00 5.19  ? 96   ARG C CZ  1 
ATOM   6073  N  NH1 . ARG C  1 96  ? 81.917  -5.176  49.097  1.00 4.88  ? 96   ARG C NH1 1 
ATOM   6074  N  NH2 . ARG C  1 96  ? 83.896  -4.458  49.992  1.00 3.43  ? 96   ARG C NH2 1 
ATOM   6075  N  N   . VAL C  1 97  ? 75.847  -1.631  49.152  1.00 6.07  ? 97   VAL C N   1 
ATOM   6076  C  CA  . VAL C  1 97  ? 74.727  -0.710  49.023  1.00 6.73  ? 97   VAL C CA  1 
ATOM   6077  C  C   . VAL C  1 97  ? 75.180  0.593   49.653  1.00 7.87  ? 97   VAL C C   1 
ATOM   6078  O  O   . VAL C  1 97  ? 75.466  0.616   50.874  1.00 7.98  ? 97   VAL C O   1 
ATOM   6079  C  CB  . VAL C  1 97  ? 73.506  -1.282  49.705  1.00 5.72  ? 97   VAL C CB  1 
ATOM   6080  C  CG1 . VAL C  1 97  ? 72.309  -0.281  49.668  1.00 5.00  ? 97   VAL C CG1 1 
ATOM   6081  C  CG2 . VAL C  1 97  ? 73.135  -2.607  49.020  1.00 5.11  ? 97   VAL C CG2 1 
ATOM   6082  N  N   . LEU C  1 98  ? 75.272  1.641   48.828  1.00 7.36  ? 98   LEU C N   1 
ATOM   6083  C  CA  . LEU C  1 98  ? 75.687  2.947   49.297  1.00 9.14  ? 98   LEU C CA  1 
ATOM   6084  C  C   . LEU C  1 98  ? 74.450  3.646   49.809  1.00 10.37 ? 98   LEU C C   1 
ATOM   6085  O  O   . LEU C  1 98  ? 73.438  3.712   49.095  1.00 10.43 ? 98   LEU C O   1 
ATOM   6086  C  CB  . LEU C  1 98  ? 76.301  3.788   48.144  1.00 9.02  ? 98   LEU C CB  1 
ATOM   6087  C  CG  . LEU C  1 98  ? 77.775  3.482   47.798  1.00 10.05 ? 98   LEU C CG  1 
ATOM   6088  C  CD1 . LEU C  1 98  ? 77.935  2.071   47.226  1.00 11.13 ? 98   LEU C CD1 1 
ATOM   6089  C  CD2 . LEU C  1 98  ? 78.359  4.521   46.856  1.00 7.48  ? 98   LEU C CD2 1 
ATOM   6090  N  N   . SER C  1 99  ? 74.524  4.182   51.035  1.00 9.51  ? 99   SER C N   1 
ATOM   6091  C  CA  . SER C  1 99  ? 73.534  5.120   51.476  1.00 7.97  ? 99   SER C CA  1 
ATOM   6092  C  C   . SER C  1 99  ? 74.235  6.465   51.647  1.00 8.74  ? 99   SER C C   1 
ATOM   6093  O  O   . SER C  1 99  ? 75.384  6.655   51.229  1.00 7.28  ? 99   SER C O   1 
ATOM   6094  C  CB  . SER C  1 99  ? 72.903  4.633   52.805  1.00 9.11  ? 99   SER C CB  1 
ATOM   6095  O  OG  . SER C  1 99  ? 73.944  4.331   53.744  1.00 7.41  ? 99   SER C OG  1 
ATOM   6096  N  N   . SER C  1 100 ? 73.549  7.402   52.286  1.00 8.55  ? 100  SER C N   1 
ATOM   6097  C  CA  . SER C  1 100 ? 73.989  8.811   52.282  1.00 8.83  ? 100  SER C CA  1 
ATOM   6098  C  C   . SER C  1 100 ? 75.416  8.992   52.771  1.00 9.07  ? 100  SER C C   1 
ATOM   6099  O  O   . SER C  1 100 ? 75.739  8.573   53.869  1.00 9.91  ? 100  SER C O   1 
ATOM   6100  C  CB  . SER C  1 100 ? 73.072  9.616   53.202  1.00 8.86  ? 100  SER C CB  1 
ATOM   6101  O  OG  A SER C  1 100 ? 73.420  10.976  53.165  0.50 11.13 ? 100  SER C OG  1 
ATOM   6102  O  OG  B SER C  1 100 ? 71.799  9.750   52.598  0.50 4.50  ? 100  SER C OG  1 
ATOM   6103  N  N   . GLY C  1 101 ? 76.221  9.644   51.945  1.00 8.76  ? 101  GLY C N   1 
ATOM   6104  C  CA  . GLY C  1 101 ? 77.607  10.007  52.234  1.00 8.94  ? 101  GLY C CA  1 
ATOM   6105  C  C   . GLY C  1 101 ? 78.601  8.900   51.926  1.00 8.05  ? 101  GLY C C   1 
ATOM   6106  O  O   . GLY C  1 101 ? 79.812  9.109   52.105  1.00 9.43  ? 101  GLY C O   1 
ATOM   6107  N  N   . ASP C  1 102 ? 78.120  7.786   51.374  1.00 6.75  ? 102  ASP C N   1 
ATOM   6108  C  CA  . ASP C  1 102 ? 79.006  6.679   51.018  1.00 7.27  ? 102  ASP C CA  1 
ATOM   6109  C  C   . ASP C  1 102 ? 79.588  6.846   49.608  1.00 7.60  ? 102  ASP C C   1 
ATOM   6110  O  O   . ASP C  1 102 ? 78.981  7.486   48.735  1.00 9.25  ? 102  ASP C O   1 
ATOM   6111  C  CB  . ASP C  1 102 ? 78.271  5.332   50.982  1.00 8.63  ? 102  ASP C CB  1 
ATOM   6112  C  CG  . ASP C  1 102 ? 77.795  4.819   52.384  1.00 9.54  ? 102  ASP C CG  1 
ATOM   6113  O  OD1 . ASP C  1 102 ? 78.300  5.242   53.441  1.00 8.55  ? 102  ASP C OD1 1 
ATOM   6114  O  OD2 . ASP C  1 102 ? 76.912  3.940   52.486  1.00 6.80  ? 102  ASP C OD2 1 
ATOM   6115  N  N   . TYR C  1 103 ? 80.680  6.126   49.370  1.00 7.48  ? 103  TYR C N   1 
ATOM   6116  C  CA  . TYR C  1 103 ? 81.536  6.322   48.229  1.00 7.18  ? 103  TYR C CA  1 
ATOM   6117  C  C   . TYR C  1 103 ? 81.988  4.997   47.619  1.00 8.06  ? 103  TYR C C   1 
ATOM   6118  O  O   . TYR C  1 103 ? 82.285  4.002   48.335  1.00 8.65  ? 103  TYR C O   1 
ATOM   6119  C  CB  . TYR C  1 103 ? 82.734  7.237   48.620  1.00 6.76  ? 103  TYR C CB  1 
ATOM   6120  C  CG  . TYR C  1 103 ? 83.772  7.286   47.565  1.00 6.21  ? 103  TYR C CG  1 
ATOM   6121  C  CD1 . TYR C  1 103 ? 83.529  7.954   46.367  1.00 8.63  ? 103  TYR C CD1 1 
ATOM   6122  C  CD2 . TYR C  1 103 ? 84.973  6.568   47.704  1.00 10.37 ? 103  TYR C CD2 1 
ATOM   6123  C  CE1 . TYR C  1 103 ? 84.475  7.956   45.360  1.00 8.81  ? 103  TYR C CE1 1 
ATOM   6124  C  CE2 . TYR C  1 103 ? 85.936  6.566   46.691  1.00 8.90  ? 103  TYR C CE2 1 
ATOM   6125  C  CZ  . TYR C  1 103 ? 85.671  7.259   45.521  1.00 11.41 ? 103  TYR C CZ  1 
ATOM   6126  O  OH  . TYR C  1 103 ? 86.630  7.270   44.505  1.00 11.81 ? 103  TYR C OH  1 
ATOM   6127  N  N   . GLY C  1 104 ? 82.003  4.974   46.284  1.00 9.04  ? 104  GLY C N   1 
ATOM   6128  C  CA  . GLY C  1 104 ? 82.521  3.824   45.559  1.00 6.36  ? 104  GLY C CA  1 
ATOM   6129  C  C   . GLY C  1 104 ? 83.469  4.276   44.464  1.00 7.67  ? 104  GLY C C   1 
ATOM   6130  O  O   . GLY C  1 104 ? 83.121  5.185   43.648  1.00 6.66  ? 104  GLY C O   1 
ATOM   6131  N  N   . SER C  1 105 ? 84.637  3.627   44.409  1.00 6.09  ? 105  SER C N   1 
ATOM   6132  C  CA  . SER C  1 105 ? 85.664  3.981   43.439  1.00 8.04  ? 105  SER C CA  1 
ATOM   6133  C  C   . SER C  1 105 ? 85.736  2.974   42.289  1.00 8.04  ? 105  SER C C   1 
ATOM   6134  O  O   . SER C  1 105 ? 85.949  1.784   42.531  1.00 9.82  ? 105  SER C O   1 
ATOM   6135  C  CB  . SER C  1 105 ? 87.040  4.119   44.116  1.00 7.29  ? 105  SER C CB  1 
ATOM   6136  O  OG  . SER C  1 105 ? 87.886  4.994   43.360  1.00 10.46 ? 105  SER C OG  1 
ATOM   6137  N  N   . VAL C  1 106 ? 85.536  3.458   41.055  1.00 8.08  ? 106  VAL C N   1 
ATOM   6138  C  CA  . VAL C  1 106 ? 85.587  2.606   39.872  1.00 8.05  ? 106  VAL C CA  1 
ATOM   6139  C  C   . VAL C  1 106 ? 86.685  3.018   38.847  1.00 7.80  ? 106  VAL C C   1 
ATOM   6140  O  O   . VAL C  1 106 ? 86.441  3.806   37.906  1.00 9.06  ? 106  VAL C O   1 
ATOM   6141  C  CB  . VAL C  1 106 ? 84.138  2.435   39.259  1.00 9.36  ? 106  VAL C CB  1 
ATOM   6142  C  CG1 . VAL C  1 106 ? 84.136  1.440   38.122  1.00 5.83  ? 106  VAL C CG1 1 
ATOM   6143  C  CG2 . VAL C  1 106 ? 83.156  2.007   40.325  1.00 7.03  ? 106  VAL C CG2 1 
ATOM   6144  N  N   . PRO C  1 107 ? 87.910  2.520   39.059  1.00 7.41  ? 107  PRO C N   1 
ATOM   6145  C  CA  . PRO C  1 107 ? 89.031  2.753   38.139  1.00 6.76  ? 107  PRO C CA  1 
ATOM   6146  C  C   . PRO C  1 107 ? 88.756  2.229   36.729  1.00 7.32  ? 107  PRO C C   1 
ATOM   6147  O  O   . PRO C  1 107 ? 87.833  1.444   36.518  1.00 7.24  ? 107  PRO C O   1 
ATOM   6148  C  CB  . PRO C  1 107 ? 90.186  1.914   38.769  1.00 6.03  ? 107  PRO C CB  1 
ATOM   6149  C  CG  . PRO C  1 107 ? 89.856  1.915   40.220  1.00 5.99  ? 107  PRO C CG  1 
ATOM   6150  C  CD  . PRO C  1 107 ? 88.339  1.769   40.263  1.00 6.04  ? 107  PRO C CD  1 
ATOM   6151  N  N   . ARG C  1 108 ? 89.592  2.657   35.790  1.00 7.50  ? 108  ARG C N   1 
ATOM   6152  C  CA  . ARG C  1 108 ? 89.534  2.198   34.400  1.00 6.84  ? 108  ARG C CA  1 
ATOM   6153  C  C   . ARG C  1 108 ? 89.607  0.693   34.375  1.00 7.70  ? 108  ARG C C   1 
ATOM   6154  O  O   . ARG C  1 108 ? 90.305  0.079   35.213  1.00 6.62  ? 108  ARG C O   1 
ATOM   6155  C  CB  . ARG C  1 108 ? 90.703  2.811   33.588  1.00 6.54  ? 108  ARG C CB  1 
ATOM   6156  C  CG  . ARG C  1 108 ? 90.545  4.291   33.337  1.00 5.12  ? 108  ARG C CG  1 
ATOM   6157  C  CD  . ARG C  1 108 ? 91.825  5.016   32.886  1.00 9.92  ? 108  ARG C CD  1 
ATOM   6158  N  NE  . ARG C  1 108 ? 92.834  5.030   33.947  1.00 10.76 ? 108  ARG C NE  1 
ATOM   6159  C  CZ  . ARG C  1 108 ? 94.078  5.431   33.778  1.00 8.85  ? 108  ARG C CZ  1 
ATOM   6160  N  NH1 . ARG C  1 108 ? 94.471  5.918   32.588  1.00 8.60  ? 108  ARG C NH1 1 
ATOM   6161  N  NH2 . ARG C  1 108 ? 94.927  5.384   34.796  1.00 9.37  ? 108  ARG C NH2 1 
ATOM   6162  N  N   . ASN C  1 109 ? 88.883  0.093   33.425  1.00 8.10  ? 109  ASN C N   1 
ATOM   6163  C  CA  . ASN C  1 109 ? 88.941  -1.370  33.209  1.00 8.81  ? 109  ASN C CA  1 
ATOM   6164  C  C   . ASN C  1 109 ? 88.284  -2.159  34.358  1.00 8.43  ? 109  ASN C C   1 
ATOM   6165  O  O   . ASN C  1 109 ? 88.446  -3.370  34.505  1.00 8.73  ? 109  ASN C O   1 
ATOM   6166  C  CB  . ASN C  1 109 ? 90.364  -1.815  32.907  1.00 8.93  ? 109  ASN C CB  1 
ATOM   6167  C  CG  . ASN C  1 109 ? 90.833  -1.321  31.541  1.00 13.77 ? 109  ASN C CG  1 
ATOM   6168  O  OD1 . ASN C  1 109 ? 90.013  -0.942  30.689  1.00 11.12 ? 109  ASN C OD1 1 
ATOM   6169  N  ND2 . ASN C  1 109 ? 92.147  -1.301  31.337  1.00 18.44 ? 109  ASN C ND2 1 
ATOM   6170  N  N   . VAL C  1 110 ? 87.476  -1.475  35.139  1.00 6.51  ? 110  VAL C N   1 
ATOM   6171  C  CA  . VAL C  1 110 ? 86.688  -2.188  36.177  1.00 6.34  ? 110  VAL C CA  1 
ATOM   6172  C  C   . VAL C  1 110 ? 85.246  -2.373  35.698  1.00 6.25  ? 110  VAL C C   1 
ATOM   6173  O  O   . VAL C  1 110 ? 84.544  -1.381  35.394  1.00 5.34  ? 110  VAL C O   1 
ATOM   6174  C  CB  . VAL C  1 110 ? 86.716  -1.426  37.544  1.00 5.47  ? 110  VAL C CB  1 
ATOM   6175  C  CG1 . VAL C  1 110 ? 85.770  -2.079  38.571  1.00 7.98  ? 110  VAL C CG1 1 
ATOM   6176  C  CG2 . VAL C  1 110 ? 88.123  -1.417  38.080  1.00 8.02  ? 110  VAL C CG2 1 
ATOM   6177  N  N   . THR C  1 111 ? 84.784  -3.622  35.630  1.00 5.12  ? 111  THR C N   1 
ATOM   6178  C  CA  . THR C  1 111 ? 83.393  -3.839  35.241  1.00 5.25  ? 111  THR C CA  1 
ATOM   6179  C  C   . THR C  1 111 ? 82.441  -3.361  36.347  1.00 5.73  ? 111  THR C C   1 
ATOM   6180  O  O   . THR C  1 111 ? 82.662  -3.642  37.529  1.00 4.92  ? 111  THR C O   1 
ATOM   6181  C  CB  . THR C  1 111 ? 83.170  -5.312  34.987  1.00 5.57  ? 111  THR C CB  1 
ATOM   6182  O  OG1 . THR C  1 111 ? 83.915  -5.719  33.839  1.00 4.32  ? 111  THR C OG1 1 
ATOM   6183  C  CG2 . THR C  1 111 ? 81.720  -5.565  34.606  1.00 4.57  ? 111  THR C CG2 1 
ATOM   6184  N  N   . HIS C  1 112 ? 81.357  -2.689  35.986  1.00 5.28  ? 112  HIS C N   1 
ATOM   6185  C  CA  . HIS C  1 112 ? 80.437  -2.228  37.021  1.00 6.67  ? 112  HIS C CA  1 
ATOM   6186  C  C   . HIS C  1 112 ? 78.999  -2.050  36.544  1.00 6.18  ? 112  HIS C C   1 
ATOM   6187  O  O   . HIS C  1 112 ? 78.745  -2.030  35.346  1.00 5.99  ? 112  HIS C O   1 
ATOM   6188  C  CB  . HIS C  1 112 ? 80.949  -0.930  37.621  1.00 5.55  ? 112  HIS C CB  1 
ATOM   6189  C  CG  . HIS C  1 112 ? 81.143  0.160   36.618  1.00 6.79  ? 112  HIS C CG  1 
ATOM   6190  N  ND1 . HIS C  1 112 ? 82.139  0.136   35.656  1.00 5.80  ? 112  HIS C ND1 1 
ATOM   6191  C  CD2 . HIS C  1 112 ? 80.435  1.295   36.400  1.00 5.35  ? 112  HIS C CD2 1 
ATOM   6192  C  CE1 . HIS C  1 112 ? 82.042  1.218   34.903  1.00 5.47  ? 112  HIS C CE1 1 
ATOM   6193  N  NE2 . HIS C  1 112 ? 81.011  1.927   35.326  1.00 5.20  ? 112  HIS C NE2 1 
ATOM   6194  N  N   . THR C  1 113 ? 78.078  -1.980  37.507  1.00 6.83  ? 113  THR C N   1 
ATOM   6195  C  CA  . THR C  1 113 ? 76.676  -1.588  37.275  1.00 6.31  ? 113  THR C CA  1 
ATOM   6196  C  C   . THR C  1 113 ? 76.116  -1.124  38.617  1.00 6.99  ? 113  THR C C   1 
ATOM   6197  O  O   . THR C  1 113 ? 76.781  -1.290  39.655  1.00 7.11  ? 113  THR C O   1 
ATOM   6198  C  CB  . THR C  1 113 ? 75.896  -2.762  36.664  1.00 6.92  ? 113  THR C CB  1 
ATOM   6199  O  OG1 . THR C  1 113 ? 74.500  -2.437  36.588  1.00 9.58  ? 113  THR C OG1 1 
ATOM   6200  C  CG2 . THR C  1 113 ? 75.967  -4.012  37.540  1.00 6.85  ? 113  THR C CG2 1 
ATOM   6201  N  N   . PHE C  1 114 ? 74.930  -0.520  38.603  1.00 5.60  ? 114  PHE C N   1 
ATOM   6202  C  CA  . PHE C  1 114 ? 74.259  -0.073  39.825  1.00 5.79  ? 114  PHE C CA  1 
ATOM   6203  C  C   . PHE C  1 114 ? 72.743  -0.332  39.773  1.00 6.06  ? 114  PHE C C   1 
ATOM   6204  O  O   . PHE C  1 114 ? 72.219  -0.645  38.713  1.00 7.93  ? 114  PHE C O   1 
ATOM   6205  C  CB  . PHE C  1 114 ? 74.557  1.405   40.083  1.00 6.07  ? 114  PHE C CB  1 
ATOM   6206  C  CG  . PHE C  1 114 ? 74.046  2.310   39.009  1.00 5.02  ? 114  PHE C CG  1 
ATOM   6207  C  CD1 . PHE C  1 114 ? 74.858  2.621   37.898  1.00 8.60  ? 114  PHE C CD1 1 
ATOM   6208  C  CD2 . PHE C  1 114 ? 72.744  2.854   39.095  1.00 7.26  ? 114  PHE C CD2 1 
ATOM   6209  C  CE1 . PHE C  1 114 ? 74.397  3.451   36.873  1.00 3.83  ? 114  PHE C CE1 1 
ATOM   6210  C  CE2 . PHE C  1 114 ? 72.239  3.691   38.073  1.00 5.34  ? 114  PHE C CE2 1 
ATOM   6211  C  CZ  . PHE C  1 114 ? 73.064  4.014   36.965  1.00 7.61  ? 114  PHE C CZ  1 
ATOM   6212  N  N   . GLN C  1 115 ? 72.070  -0.268  40.916  1.00 5.13  ? 115  GLN C N   1 
ATOM   6213  C  CA  . GLN C  1 115 ? 70.639  -0.469  40.972  1.00 6.19  ? 115  GLN C CA  1 
ATOM   6214  C  C   . GLN C  1 115 ? 70.136  0.485   42.021  1.00 7.69  ? 115  GLN C C   1 
ATOM   6215  O  O   . GLN C  1 115 ? 70.623  0.508   43.183  1.00 6.29  ? 115  GLN C O   1 
ATOM   6216  C  CB  . GLN C  1 115 ? 70.273  -1.896  41.358  1.00 4.64  ? 115  GLN C CB  1 
ATOM   6217  C  CG  . GLN C  1 115 ? 68.766  -2.085  41.489  1.00 9.29  ? 115  GLN C CG  1 
ATOM   6218  C  CD  . GLN C  1 115 ? 68.383  -3.541  41.503  1.00 14.62 ? 115  GLN C CD  1 
ATOM   6219  O  OE1 . GLN C  1 115 ? 69.102  -4.354  40.933  1.00 18.02 ? 115  GLN C OE1 1 
ATOM   6220  N  NE2 . GLN C  1 115 ? 67.213  -3.872  42.071  1.00 14.38 ? 115  GLN C NE2 1 
ATOM   6221  N  N   . ILE C  1 116 ? 69.161  1.300   41.619  1.00 7.76  ? 116  ILE C N   1 
ATOM   6222  C  CA  . ILE C  1 116 ? 68.521  2.187   42.562  1.00 7.61  ? 116  ILE C CA  1 
ATOM   6223  C  C   . ILE C  1 116 ? 67.568  1.510   43.590  1.00 6.95  ? 116  ILE C C   1 
ATOM   6224  O  O   . ILE C  1 116 ? 66.635  0.812   43.217  1.00 8.33  ? 116  ILE C O   1 
ATOM   6225  C  CB  . ILE C  1 116 ? 67.783  3.256   41.782  1.00 7.79  ? 116  ILE C CB  1 
ATOM   6226  C  CG1 . ILE C  1 116 ? 68.706  3.850   40.705  1.00 8.38  ? 116  ILE C CG1 1 
ATOM   6227  C  CG2 . ILE C  1 116 ? 67.298  4.404   42.754  1.00 8.99  ? 116  ILE C CG2 1 
ATOM   6228  C  CD1 . ILE C  1 116 ? 69.875  4.701   41.240  1.00 9.36  ? 116  ILE C CD1 1 
ATOM   6229  N  N   . GLN C  1 117 ? 67.761  1.776   44.874  1.00 6.28  ? 117  GLN C N   1 
ATOM   6230  C  CA  . GLN C  1 117 ? 66.937  1.153   45.912  1.00 8.13  ? 117  GLN C CA  1 
ATOM   6231  C  C   . GLN C  1 117 ? 65.887  2.073   46.522  1.00 7.91  ? 117  GLN C C   1 
ATOM   6232  O  O   . GLN C  1 117 ? 64.683  1.759   46.487  1.00 9.85  ? 117  GLN C O   1 
ATOM   6233  C  CB  . GLN C  1 117 ? 67.829  0.528   47.013  1.00 10.22 ? 117  GLN C CB  1 
ATOM   6234  C  CG  . GLN C  1 117 ? 67.057  -0.192  48.168  1.00 15.27 ? 117  GLN C CG  1 
ATOM   6235  C  CD  . GLN C  1 117 ? 67.610  0.159   49.608  1.00 27.10 ? 117  GLN C CD  1 
ATOM   6236  O  OE1 . GLN C  1 117 ? 68.768  -0.149  49.975  1.00 27.53 ? 117  GLN C OE1 1 
ATOM   6237  N  NE2 . GLN C  1 117 ? 66.761  0.804   50.410  1.00 30.21 ? 117  GLN C NE2 1 
ATOM   6238  N  N   . ASP C  1 118 ? 66.299  3.207   47.074  1.00 8.42  ? 118  ASP C N   1 
ATOM   6239  C  CA  . ASP C  1 118 ? 65.348  4.025   47.802  1.00 8.70  ? 118  ASP C CA  1 
ATOM   6240  C  C   . ASP C  1 118 ? 64.581  5.006   46.901  1.00 8.38  ? 118  ASP C C   1 
ATOM   6241  O  O   . ASP C  1 118 ? 65.065  5.353   45.826  1.00 8.44  ? 118  ASP C O   1 
ATOM   6242  C  CB  . ASP C  1 118 ? 66.007  4.773   48.947  1.00 8.89  ? 118  ASP C CB  1 
ATOM   6243  C  CG  . ASP C  1 118 ? 66.135  3.913   50.210  1.00 11.01 ? 118  ASP C CG  1 
ATOM   6244  O  OD1 . ASP C  1 118 ? 65.333  2.976   50.422  1.00 9.94  ? 118  ASP C OD1 1 
ATOM   6245  O  OD2 . ASP C  1 118 ? 67.048  4.108   51.028  1.00 15.47 ? 118  ASP C OD2 1 
ATOM   6246  N  N   . PRO C  1 119 ? 63.373  5.386   47.309  1.00 7.44  ? 119  PRO C N   1 
ATOM   6247  C  CA  . PRO C  1 119 ? 62.551  6.290   46.477  1.00 7.90  ? 119  PRO C CA  1 
ATOM   6248  C  C   . PRO C  1 119 ? 63.226  7.615   46.179  1.00 8.08  ? 119  PRO C C   1 
ATOM   6249  O  O   . PRO C  1 119 ? 63.059  8.163   45.070  1.00 9.55  ? 119  PRO C O   1 
ATOM   6250  C  CB  . PRO C  1 119 ? 61.269  6.460   47.318  1.00 8.15  ? 119  PRO C CB  1 
ATOM   6251  C  CG  . PRO C  1 119 ? 61.166  5.036   48.040  1.00 8.50  ? 119  PRO C CG  1 
ATOM   6252  C  CD  . PRO C  1 119 ? 62.634  4.899   48.484  1.00 7.20  ? 119  PRO C CD  1 
ATOM   6253  N  N   . ASP C  1 120 ? 63.940  8.167   47.146  1.00 8.14  ? 120  ASP C N   1 
ATOM   6254  C  CA  . ASP C  1 120 ? 64.536  9.502   46.953  1.00 8.69  ? 120  ASP C CA  1 
ATOM   6255  C  C   . ASP C  1 120 ? 66.036  9.406   46.829  1.00 9.78  ? 120  ASP C C   1 
ATOM   6256  O  O   . ASP C  1 120 ? 66.752  9.897   47.702  1.00 8.50  ? 120  ASP C O   1 
ATOM   6257  C  CB  . ASP C  1 120 ? 64.198  10.450  48.125  1.00 8.92  ? 120  ASP C CB  1 
ATOM   6258  C  CG  . ASP C  1 120 ? 64.419  11.936  47.736  1.00 11.33 ? 120  ASP C CG  1 
ATOM   6259  O  OD1 . ASP C  1 120 ? 64.676  12.160  46.518  1.00 11.53 ? 120  ASP C OD1 1 
ATOM   6260  O  OD2 . ASP C  1 120 ? 64.341  12.924  48.554  1.00 12.50 ? 120  ASP C OD2 1 
ATOM   6261  N  N   . THR C  1 121 ? 66.518  8.738   45.762  1.00 9.55  ? 121  THR C N   1 
ATOM   6262  C  CA  . THR C  1 121 ? 67.934  8.420   45.660  1.00 8.44  ? 121  THR C CA  1 
ATOM   6263  C  C   . THR C  1 121 ? 68.583  9.454   44.744  1.00 9.02  ? 121  THR C C   1 
ATOM   6264  O  O   . THR C  1 121 ? 68.012  9.830   43.700  1.00 8.54  ? 121  THR C O   1 
ATOM   6265  C  CB  . THR C  1 121 ? 68.118  7.047   45.168  1.00 9.11  ? 121  THR C CB  1 
ATOM   6266  O  OG1 . THR C  1 121 ? 67.678  6.118   46.195  1.00 8.37  ? 121  THR C OG1 1 
ATOM   6267  C  CG2 . THR C  1 121 ? 69.616  6.706   44.957  1.00 5.84  ? 121  THR C CG2 1 
ATOM   6268  N  N   . GLU C  1 122 ? 69.717  9.966   45.183  1.00 7.48  ? 122  GLU C N   1 
ATOM   6269  C  CA  . GLU C  1 122 ? 70.521  10.828  44.340  1.00 8.84  ? 122  GLU C CA  1 
ATOM   6270  C  C   . GLU C  1 122 ? 71.967  10.343  44.348  1.00 9.75  ? 122  GLU C C   1 
ATOM   6271  O  O   . GLU C  1 122 ? 72.559  10.090  45.447  1.00 9.78  ? 122  GLU C O   1 
ATOM   6272  C  CB  . GLU C  1 122 ? 70.468  12.272  44.846  1.00 8.38  ? 122  GLU C CB  1 
ATOM   6273  C  CG  . GLU C  1 122 ? 71.247  13.232  43.940  1.00 10.91 ? 122  GLU C CG  1 
ATOM   6274  C  CD  . GLU C  1 122 ? 70.916  14.694  44.267  1.00 15.49 ? 122  GLU C CD  1 
ATOM   6275  O  OE1 . GLU C  1 122 ? 69.874  14.942  44.931  1.00 17.18 ? 122  GLU C OE1 1 
ATOM   6276  O  OE2 . GLU C  1 122 ? 71.655  15.580  43.804  1.00 15.02 ? 122  GLU C OE2 1 
ATOM   6277  N  N   . MET C  1 123 ? 72.553  10.233  43.148  1.00 9.26  ? 123  MET C N   1 
ATOM   6278  C  CA  . MET C  1 123 ? 73.946  9.784   43.006  1.00 11.83 ? 123  MET C CA  1 
ATOM   6279  C  C   . MET C  1 123 ? 74.695  10.937  42.408  1.00 11.88 ? 123  MET C C   1 
ATOM   6280  O  O   . MET C  1 123 ? 74.199  11.561  41.455  1.00 12.95 ? 123  MET C O   1 
ATOM   6281  C  CB  . MET C  1 123 ? 74.078  8.638   41.987  1.00 12.54 ? 123  MET C CB  1 
ATOM   6282  C  CG  . MET C  1 123 ? 72.903  7.675   41.891  1.00 16.61 ? 123  MET C CG  1 
ATOM   6283  S  SD  . MET C  1 123 ? 72.936  6.636   40.273  1.00 22.84 ? 123  MET C SD  1 
ATOM   6284  C  CE  . MET C  1 123 ? 74.699  6.092   40.334  1.00 11.84 ? 123  MET C CE  1 
ATOM   6285  N  N   . THR C  1 124 ? 75.863  11.234  42.936  1.00 10.79 ? 124  THR C N   1 
ATOM   6286  C  CA  . THR C  1 124 ? 76.708  12.224  42.299  1.00 10.38 ? 124  THR C CA  1 
ATOM   6287  C  C   . THR C  1 124 ? 77.857  11.481  41.657  1.00 10.43 ? 124  THR C C   1 
ATOM   6288  O  O   . THR C  1 124 ? 78.578  10.820  42.344  1.00 11.49 ? 124  THR C O   1 
ATOM   6289  C  CB  . THR C  1 124 ? 77.221  13.201  43.316  1.00 9.64  ? 124  THR C CB  1 
ATOM   6290  O  OG1 . THR C  1 124 ? 76.121  14.020  43.757  1.00 12.38 ? 124  THR C OG1 1 
ATOM   6291  C  CG2 . THR C  1 124 ? 78.213  14.173  42.676  1.00 11.89 ? 124  THR C CG2 1 
ATOM   6292  N  N   . GLY C  1 125 ? 77.998  11.612  40.339  1.00 10.94 ? 125  GLY C N   1 
ATOM   6293  C  CA  . GLY C  1 125 ? 79.035  10.963  39.576  1.00 10.12 ? 125  GLY C CA  1 
ATOM   6294  C  C   . GLY C  1 125 ? 80.146  11.970  39.351  1.00 9.73  ? 125  GLY C C   1 
ATOM   6295  O  O   . GLY C  1 125 ? 79.913  13.093  38.901  1.00 10.81 ? 125  GLY C O   1 
ATOM   6296  N  N   . VAL C  1 126 ? 81.379  11.575  39.620  1.00 8.54  ? 126  VAL C N   1 
ATOM   6297  C  CA  . VAL C  1 126 ? 82.505  12.428  39.246  1.00 7.78  ? 126  VAL C CA  1 
ATOM   6298  C  C   . VAL C  1 126 ? 83.357  11.598  38.331  1.00 8.52  ? 126  VAL C C   1 
ATOM   6299  O  O   . VAL C  1 126 ? 83.851  10.553  38.739  1.00 6.43  ? 126  VAL C O   1 
ATOM   6300  C  CB  . VAL C  1 126 ? 83.333  12.906  40.465  1.00 7.37  ? 126  VAL C CB  1 
ATOM   6301  C  CG1 . VAL C  1 126 ? 84.606  13.653  40.023  1.00 7.95  ? 126  VAL C CG1 1 
ATOM   6302  C  CG2 . VAL C  1 126 ? 82.443  13.753  41.406  1.00 6.67  ? 126  VAL C CG2 1 
ATOM   6303  N  N   . ILE C  1 127 ? 83.513  12.055  37.086  1.00 8.80  ? 127  ILE C N   1 
ATOM   6304  C  CA  . ILE C  1 127 ? 84.192  11.245  36.067  1.00 8.34  ? 127  ILE C CA  1 
ATOM   6305  C  C   . ILE C  1 127 ? 85.377  12.024  35.540  1.00 9.06  ? 127  ILE C C   1 
ATOM   6306  O  O   . ILE C  1 127 ? 85.232  13.208  35.233  1.00 8.66  ? 127  ILE C O   1 
ATOM   6307  C  CB  . ILE C  1 127 ? 83.236  10.883  34.915  1.00 9.42  ? 127  ILE C CB  1 
ATOM   6308  C  CG1 . ILE C  1 127 ? 81.968  10.173  35.449  1.00 12.11 ? 127  ILE C CG1 1 
ATOM   6309  C  CG2 . ILE C  1 127 ? 83.908  9.903   33.934  1.00 7.46  ? 127  ILE C CG2 1 
ATOM   6310  C  CD1 . ILE C  1 127 ? 80.915  11.144  35.871  1.00 16.80 ? 127  ILE C CD1 1 
ATOM   6311  N  N   . VAL C  1 128 ? 86.535  11.370  35.429  1.00 8.64  ? 128  VAL C N   1 
ATOM   6312  C  CA  . VAL C  1 128 ? 87.781  12.028  35.005  1.00 8.50  ? 128  VAL C CA  1 
ATOM   6313  C  C   . VAL C  1 128 ? 88.331  11.217  33.837  1.00 9.01  ? 128  VAL C C   1 
ATOM   6314  O  O   . VAL C  1 128 ? 88.398  9.993   33.974  1.00 10.89 ? 128  VAL C O   1 
ATOM   6315  C  CB  . VAL C  1 128 ? 88.818  12.036  36.157  1.00 8.09  ? 128  VAL C CB  1 
ATOM   6316  C  CG1 . VAL C  1 128 ? 90.089  12.779  35.745  1.00 9.15  ? 128  VAL C CG1 1 
ATOM   6317  C  CG2 . VAL C  1 128 ? 88.207  12.705  37.474  1.00 6.19  ? 128  VAL C CG2 1 
ATOM   6318  N  N   . PRO C  1 129 ? 88.695  11.820  32.687  1.00 8.69  ? 129  PRO C N   1 
ATOM   6319  C  CA  . PRO C  1 129 ? 88.524  13.251  32.389  1.00 7.25  ? 129  PRO C CA  1 
ATOM   6320  C  C   . PRO C  1 129 ? 87.113  13.621  32.029  1.00 7.78  ? 129  PRO C C   1 
ATOM   6321  O  O   . PRO C  1 129 ? 86.215  12.754  31.971  1.00 8.60  ? 129  PRO C O   1 
ATOM   6322  C  CB  . PRO C  1 129 ? 89.392  13.460  31.142  1.00 7.01  ? 129  PRO C CB  1 
ATOM   6323  C  CG  . PRO C  1 129 ? 89.375  12.090  30.417  1.00 9.24  ? 129  PRO C CG  1 
ATOM   6324  C  CD  . PRO C  1 129 ? 89.298  11.086  31.561  1.00 7.97  ? 129  PRO C CD  1 
ATOM   6325  N  N   . GLY C  1 130 ? 86.930  14.911  31.776  1.00 8.26  ? 130  GLY C N   1 
ATOM   6326  C  CA  . GLY C  1 130 ? 85.631  15.482  31.491  1.00 8.35  ? 130  GLY C CA  1 
ATOM   6327  C  C   . GLY C  1 130 ? 85.204  15.265  30.055  1.00 9.15  ? 130  GLY C C   1 
ATOM   6328  O  O   . GLY C  1 130 ? 86.023  14.910  29.185  1.00 9.71  ? 130  GLY C O   1 
ATOM   6329  N  N   . GLY C  1 131 ? 83.917  15.440  29.811  1.00 9.11  ? 131  GLY C N   1 
ATOM   6330  C  CA  . GLY C  1 131 ? 83.346  15.284  28.480  1.00 10.77 ? 131  GLY C CA  1 
ATOM   6331  C  C   . GLY C  1 131 ? 82.573  13.984  28.320  1.00 11.96 ? 131  GLY C C   1 
ATOM   6332  O  O   . GLY C  1 131 ? 81.904  13.768  27.290  1.00 13.94 ? 131  GLY C O   1 
ATOM   6333  N  N   . PHE C  1 132 ? 82.611  13.146  29.345  1.00 11.28 ? 132  PHE C N   1 
ATOM   6334  C  CA  . PHE C  1 132 ? 81.927  11.856  29.339  1.00 11.29 ? 132  PHE C CA  1 
ATOM   6335  C  C   . PHE C  1 132 ? 80.437  12.056  29.129  1.00 10.81 ? 132  PHE C C   1 
ATOM   6336  O  O   . PHE C  1 132 ? 79.805  11.192  28.553  1.00 9.92  ? 132  PHE C O   1 
ATOM   6337  C  CB  . PHE C  1 132 ? 82.194  11.036  30.635  1.00 12.80 ? 132  PHE C CB  1 
ATOM   6338  C  CG  . PHE C  1 132 ? 81.572  9.646   30.619  1.00 13.72 ? 132  PHE C CG  1 
ATOM   6339  C  CD1 . PHE C  1 132 ? 82.163  8.619   29.911  1.00 16.40 ? 132  PHE C CD1 1 
ATOM   6340  C  CD2 . PHE C  1 132 ? 80.386  9.392   31.314  1.00 17.11 ? 132  PHE C CD2 1 
ATOM   6341  C  CE1 . PHE C  1 132 ? 81.589  7.327   29.895  1.00 20.58 ? 132  PHE C CE1 1 
ATOM   6342  C  CE2 . PHE C  1 132 ? 79.799  8.132   31.262  1.00 19.62 ? 132  PHE C CE2 1 
ATOM   6343  C  CZ  . PHE C  1 132 ? 80.412  7.098   30.566  1.00 17.92 ? 132  PHE C CZ  1 
ATOM   6344  N  N   . GLU C  1 133 ? 79.902  13.216  29.543  1.00 10.21 ? 133  GLU C N   1 
ATOM   6345  C  CA  . GLU C  1 133 ? 78.487  13.501  29.372  1.00 8.83  ? 133  GLU C CA  1 
ATOM   6346  C  C   . GLU C  1 133 ? 77.912  13.371  27.954  1.00 8.77  ? 133  GLU C C   1 
ATOM   6347  O  O   . GLU C  1 133 ? 76.693  13.245  27.809  1.00 8.63  ? 133  GLU C O   1 
ATOM   6348  C  CB  . GLU C  1 133 ? 78.080  14.855  29.976  1.00 8.83  ? 133  GLU C CB  1 
ATOM   6349  C  CG  . GLU C  1 133 ? 78.648  16.091  29.217  1.00 11.35 ? 133  GLU C CG  1 
ATOM   6350  C  CD  . GLU C  1 133 ? 80.116  16.420  29.585  1.00 6.50  ? 133  GLU C CD  1 
ATOM   6351  O  OE1 . GLU C  1 133 ? 80.693  15.788  30.484  1.00 10.25 ? 133  GLU C OE1 1 
ATOM   6352  O  OE2 . GLU C  1 133 ? 80.737  17.290  28.961  1.00 9.57  ? 133  GLU C OE2 1 
ATOM   6353  N  N   . ASP C  1 134 ? 78.746  13.452  26.905  1.00 7.15  ? 134  ASP C N   1 
ATOM   6354  C  CA  . ASP C  1 134 ? 78.222  13.317  25.557  1.00 6.83  ? 134  ASP C CA  1 
ATOM   6355  C  C   . ASP C  1 134 ? 77.447  12.008  25.475  1.00 5.93  ? 134  ASP C C   1 
ATOM   6356  O  O   . ASP C  1 134 ? 76.509  11.928  24.702  1.00 6.08  ? 134  ASP C O   1 
ATOM   6357  C  CB  . ASP C  1 134 ? 79.303  13.236  24.494  1.00 5.84  ? 134  ASP C CB  1 
ATOM   6358  C  CG  . ASP C  1 134 ? 79.976  14.560  24.191  1.00 8.83  ? 134  ASP C CG  1 
ATOM   6359  O  OD1 . ASP C  1 134 ? 79.559  15.635  24.676  1.00 8.62  ? 134  ASP C OD1 1 
ATOM   6360  O  OD2 . ASP C  1 134 ? 80.963  14.595  23.430  1.00 10.89 ? 134  ASP C OD2 1 
ATOM   6361  N  N   . LEU C  1 135 ? 77.839  11.007  26.251  1.00 5.38  ? 135  LEU C N   1 
ATOM   6362  C  CA  . LEU C  1 135 ? 77.134  9.701   26.234  1.00 7.28  ? 135  LEU C CA  1 
ATOM   6363  C  C   . LEU C  1 135 ? 75.657  9.858   26.573  1.00 8.15  ? 135  LEU C C   1 
ATOM   6364  O  O   . LEU C  1 135 ? 74.788  9.312   25.889  1.00 8.73  ? 135  LEU C O   1 
ATOM   6365  C  CB  . LEU C  1 135 ? 77.789  8.704   27.209  1.00 8.07  ? 135  LEU C CB  1 
ATOM   6366  C  CG  . LEU C  1 135 ? 77.014  7.400   27.441  1.00 8.68  ? 135  LEU C CG  1 
ATOM   6367  C  CD1 . LEU C  1 135 ? 77.172  6.343   26.356  1.00 6.09  ? 135  LEU C CD1 1 
ATOM   6368  C  CD2 . LEU C  1 135 ? 77.394  6.854   28.791  1.00 11.58 ? 135  LEU C CD2 1 
ATOM   6369  N  N   . PHE C  1 136 ? 75.387  10.654  27.617  1.00 8.73  ? 136  PHE C N   1 
ATOM   6370  C  CA  . PHE C  1 136 ? 74.001  10.902  28.081  1.00 8.34  ? 136  PHE C CA  1 
ATOM   6371  C  C   . PHE C  1 136 ? 73.200  11.792  27.188  1.00 8.95  ? 136  PHE C C   1 
ATOM   6372  O  O   . PHE C  1 136 ? 71.989  11.656  27.142  1.00 9.52  ? 136  PHE C O   1 
ATOM   6373  C  CB  . PHE C  1 136 ? 73.971  11.382  29.537  1.00 5.89  ? 136  PHE C CB  1 
ATOM   6374  C  CG  . PHE C  1 136 ? 74.650  10.392  30.492  1.00 7.89  ? 136  PHE C CG  1 
ATOM   6375  C  CD1 . PHE C  1 136 ? 74.030  9.143   30.771  1.00 11.78 ? 136  PHE C CD1 1 
ATOM   6376  C  CD2 . PHE C  1 136 ? 75.910  10.642  30.983  1.00 7.29  ? 136  PHE C CD2 1 
ATOM   6377  C  CE1 . PHE C  1 136 ? 74.644  8.181   31.629  1.00 11.17 ? 136  PHE C CE1 1 
ATOM   6378  C  CE2 . PHE C  1 136 ? 76.554  9.690   31.839  1.00 11.07 ? 136  PHE C CE2 1 
ATOM   6379  C  CZ  . PHE C  1 136 ? 75.898  8.436   32.125  1.00 14.38 ? 136  PHE C CZ  1 
ATOM   6380  N  N   . TYR C  1 137 ? 73.855  12.689  26.458  1.00 9.35  ? 137  TYR C N   1 
ATOM   6381  C  CA  . TYR C  1 137 ? 73.168  13.432  25.407  1.00 9.16  ? 137  TYR C CA  1 
ATOM   6382  C  C   . TYR C  1 137 ? 72.589  12.509  24.333  1.00 9.37  ? 137  TYR C C   1 
ATOM   6383  O  O   . TYR C  1 137 ? 71.516  12.750  23.800  1.00 10.25 ? 137  TYR C O   1 
ATOM   6384  C  CB  . TYR C  1 137 ? 74.134  14.429  24.762  1.00 10.68 ? 137  TYR C CB  1 
ATOM   6385  C  CG  . TYR C  1 137 ? 74.716  15.463  25.725  1.00 9.82  ? 137  TYR C CG  1 
ATOM   6386  C  CD1 . TYR C  1 137 ? 74.155  15.679  26.995  1.00 13.38 ? 137  TYR C CD1 1 
ATOM   6387  C  CD2 . TYR C  1 137 ? 75.858  16.207  25.372  1.00 11.41 ? 137  TYR C CD2 1 
ATOM   6388  C  CE1 . TYR C  1 137 ? 74.689  16.662  27.884  1.00 14.16 ? 137  TYR C CE1 1 
ATOM   6389  C  CE2 . TYR C  1 137 ? 76.404  17.175  26.255  1.00 10.21 ? 137  TYR C CE2 1 
ATOM   6390  C  CZ  . TYR C  1 137 ? 75.821  17.404  27.490  1.00 13.05 ? 137  TYR C CZ  1 
ATOM   6391  O  OH  . TYR C  1 137 ? 76.375  18.364  28.329  1.00 12.09 ? 137  TYR C OH  1 
ATOM   6392  N  N   . TYR C  1 138 ? 73.300  11.431  24.036  1.00 8.17  ? 138  TYR C N   1 
ATOM   6393  C  CA  . TYR C  1 138 ? 72.836  10.490  23.020  1.00 7.78  ? 138  TYR C CA  1 
ATOM   6394  C  C   . TYR C  1 138 ? 71.792  9.577   23.616  1.00 7.99  ? 138  TYR C C   1 
ATOM   6395  O  O   . TYR C  1 138 ? 70.718  9.395   23.046  1.00 7.30  ? 138  TYR C O   1 
ATOM   6396  C  CB  . TYR C  1 138 ? 74.021  9.679   22.499  1.00 7.53  ? 138  TYR C CB  1 
ATOM   6397  C  CG  . TYR C  1 138 ? 73.625  8.422   21.726  1.00 8.04  ? 138  TYR C CG  1 
ATOM   6398  C  CD1 . TYR C  1 138 ? 72.724  8.499   20.671  1.00 6.96  ? 138  TYR C CD1 1 
ATOM   6399  C  CD2 . TYR C  1 138 ? 74.116  7.173   22.087  1.00 7.38  ? 138  TYR C CD2 1 
ATOM   6400  C  CE1 . TYR C  1 138 ? 72.312  7.369   19.974  1.00 10.02 ? 138  TYR C CE1 1 
ATOM   6401  C  CE2 . TYR C  1 138 ? 73.748  6.041   21.363  1.00 11.82 ? 138  TYR C CE2 1 
ATOM   6402  C  CZ  . TYR C  1 138 ? 72.846  6.142   20.308  1.00 13.41 ? 138  TYR C CZ  1 
ATOM   6403  O  OH  . TYR C  1 138 ? 72.456  5.019   19.569  1.00 16.18 ? 138  TYR C OH  1 
ATOM   6404  N  N   . LEU C  1 139 ? 72.114  8.993   24.768  1.00 8.88  ? 139  LEU C N   1 
ATOM   6405  C  CA  . LEU C  1 139 ? 71.212  8.022   25.367  1.00 10.15 ? 139  LEU C CA  1 
ATOM   6406  C  C   . LEU C  1 139 ? 69.968  8.669   25.974  1.00 9.50  ? 139  LEU C C   1 
ATOM   6407  O  O   . LEU C  1 139 ? 68.922  8.029   26.017  1.00 8.34  ? 139  LEU C O   1 
ATOM   6408  C  CB  . LEU C  1 139 ? 71.906  7.190   26.436  1.00 11.02 ? 139  LEU C CB  1 
ATOM   6409  C  CG  . LEU C  1 139 ? 72.914  6.161   25.939  1.00 12.11 ? 139  LEU C CG  1 
ATOM   6410  C  CD1 . LEU C  1 139 ? 73.610  5.630   27.142  1.00 10.94 ? 139  LEU C CD1 1 
ATOM   6411  C  CD2 . LEU C  1 139 ? 72.177  5.072   25.170  1.00 17.03 ? 139  LEU C CD2 1 
ATOM   6412  N  N   . GLY C  1 140 ? 70.106  9.886   26.470  1.00 7.38  ? 140  GLY C N   1 
ATOM   6413  C  CA  . GLY C  1 140 ? 69.025  10.506  27.226  1.00 8.70  ? 140  GLY C CA  1 
ATOM   6414  C  C   . GLY C  1 140 ? 68.071  11.320  26.355  1.00 9.14  ? 140  GLY C C   1 
ATOM   6415  O  O   . GLY C  1 140 ? 68.387  11.636  25.181  1.00 9.64  ? 140  GLY C O   1 
ATOM   6416  N  N   . THR C  1 141 ? 66.884  11.637  26.883  1.00 9.27  ? 141  THR C N   1 
ATOM   6417  C  CA  . THR C  1 141 ? 65.987  12.537  26.168  1.00 8.99  ? 141  THR C CA  1 
ATOM   6418  C  C   . THR C  1 141 ? 65.993  13.870  26.891  1.00 9.08  ? 141  THR C C   1 
ATOM   6419  O  O   . THR C  1 141 ? 65.859  13.917  28.102  1.00 8.47  ? 141  THR C O   1 
ATOM   6420  C  CB  . THR C  1 141 ? 64.594  11.961  26.192  1.00 10.68 ? 141  THR C CB  1 
ATOM   6421  O  OG1 . THR C  1 141 ? 64.609  10.712  25.479  1.00 9.28  ? 141  THR C OG1 1 
ATOM   6422  C  CG2 . THR C  1 141 ? 63.612  12.868  25.449  1.00 11.18 ? 141  THR C CG2 1 
ATOM   6423  N  N   . ASN C  1 142 ? 66.091  14.961  26.161  1.00 8.99  ? 142  ASN C N   1 
ATOM   6424  C  CA  . ASN C  1 142 ? 66.130  16.259  26.845  1.00 9.75  ? 142  ASN C CA  1 
ATOM   6425  C  C   . ASN C  1 142 ? 64.918  16.414  27.721  1.00 8.74  ? 142  ASN C C   1 
ATOM   6426  O  O   . ASN C  1 142 ? 63.803  16.022  27.338  1.00 7.95  ? 142  ASN C O   1 
ATOM   6427  C  CB  . ASN C  1 142 ? 66.185  17.412  25.862  1.00 9.57  ? 142  ASN C CB  1 
ATOM   6428  C  CG  . ASN C  1 142 ? 67.488  17.485  25.123  1.00 14.55 ? 142  ASN C CG  1 
ATOM   6429  O  OD1 . ASN C  1 142 ? 68.464  16.797  25.462  1.00 15.15 ? 142  ASN C OD1 1 
ATOM   6430  N  ND2 . ASN C  1 142 ? 67.501  18.306  24.081  1.00 19.78 ? 142  ASN C ND2 1 
ATOM   6431  N  N   . ALA C  1 143 ? 65.108  17.007  28.882  1.00 8.90  ? 143  ALA C N   1 
ATOM   6432  C  CA  . ALA C  1 143 ? 63.953  17.301  29.731  1.00 9.33  ? 143  ALA C CA  1 
ATOM   6433  C  C   . ALA C  1 143 ? 63.871  18.808  30.075  1.00 10.22 ? 143  ALA C C   1 
ATOM   6434  O  O   . ALA C  1 143 ? 64.817  19.408  30.610  1.00 11.14 ? 143  ALA C O   1 
ATOM   6435  C  CB  . ALA C  1 143 ? 64.018  16.459  31.009  1.00 9.88  ? 143  ALA C CB  1 
ATOM   6436  N  N   . THR C  1 144 ? 62.710  19.402  29.833  1.00 8.36  ? 144  THR C N   1 
ATOM   6437  C  CA  . THR C  1 144 ? 62.496  20.767  30.242  1.00 8.58  ? 144  THR C CA  1 
ATOM   6438  C  C   . THR C  1 144 ? 62.428  20.915  31.774  1.00 8.22  ? 144  THR C C   1 
ATOM   6439  O  O   . THR C  1 144 ? 63.020  21.850  32.343  1.00 7.98  ? 144  THR C O   1 
ATOM   6440  C  CB  . THR C  1 144 ? 61.246  21.317  29.518  1.00 9.40  ? 144  THR C CB  1 
ATOM   6441  O  OG1 . THR C  1 144 ? 61.542  21.347  28.091  1.00 11.95 ? 144  THR C OG1 1 
ATOM   6442  C  CG2 . THR C  1 144 ? 60.993  22.775  29.861  0.50 8.24  ? 144  THR C CG2 1 
ATOM   6443  N  N   . ASP C  1 145 ? 61.762  19.969  32.431  1.00 7.69  ? 145  ASP C N   1 
ATOM   6444  C  CA  . ASP C  1 145 ? 61.561  19.970  33.891  1.00 7.76  ? 145  ASP C CA  1 
ATOM   6445  C  C   . ASP C  1 145 ? 61.288  21.403  34.410  1.00 8.07  ? 145  ASP C C   1 
ATOM   6446  O  O   . ASP C  1 145 ? 62.098  22.000  35.161  1.00 8.02  ? 145  ASP C O   1 
ATOM   6447  C  CB  . ASP C  1 145 ? 62.761  19.412  34.614  1.00 7.27  ? 145  ASP C CB  1 
ATOM   6448  C  CG  . ASP C  1 145 ? 62.425  18.977  35.996  1.00 7.41  ? 145  ASP C CG  1 
ATOM   6449  O  OD1 . ASP C  1 145 ? 61.299  19.300  36.455  1.00 6.68  ? 145  ASP C OD1 1 
ATOM   6450  O  OD2 . ASP C  1 145 ? 63.224  18.339  36.712  1.00 5.98  ? 145  ASP C OD2 1 
ATOM   6451  N  N   . THR C  1 146 ? 60.163  21.956  34.024  1.00 8.28  ? 146  THR C N   1 
ATOM   6452  C  CA  . THR C  1 146 ? 59.943  23.370  34.292  1.00 9.70  ? 146  THR C CA  1 
ATOM   6453  C  C   . THR C  1 146 ? 60.002  23.651  35.818  1.00 9.96  ? 146  THR C C   1 
ATOM   6454  O  O   . THR C  1 146 ? 60.589  24.653  36.239  1.00 10.49 ? 146  THR C O   1 
ATOM   6455  C  CB  . THR C  1 146 ? 58.593  23.781  33.725  1.00 10.81 ? 146  THR C CB  1 
ATOM   6456  O  OG1 . THR C  1 146 ? 58.660  23.742  32.286  1.00 12.32 ? 146  THR C OG1 1 
ATOM   6457  C  CG2 . THR C  1 146 ? 58.299  25.231  34.055  1.00 12.08 ? 146  THR C CG2 1 
ATOM   6458  N  N   . THR C  1 147 ? 59.423  22.761  36.629  1.00 8.51  ? 147  THR C N   1 
ATOM   6459  C  CA  . THR C  1 147 ? 59.398  22.974  38.095  1.00 8.20  ? 147  THR C CA  1 
ATOM   6460  C  C   . THR C  1 147 ? 60.688  22.595  38.852  1.00 8.36  ? 147  THR C C   1 
ATOM   6461  O  O   . THR C  1 147 ? 60.723  22.686  40.082  1.00 8.08  ? 147  THR C O   1 
ATOM   6462  C  CB  . THR C  1 147 ? 58.263  22.148  38.729  1.00 8.34  ? 147  THR C CB  1 
ATOM   6463  O  OG1 . THR C  1 147 ? 58.559  20.740  38.543  1.00 7.75  ? 147  THR C OG1 1 
ATOM   6464  C  CG2 . THR C  1 147 ? 56.931  22.393  38.017  1.00 6.81  ? 147  THR C CG2 1 
ATOM   6465  N  N   . HIS C  1 148 ? 61.691  22.103  38.137  1.00 7.53  ? 148  HIS C N   1 
ATOM   6466  C  CA  . HIS C  1 148 ? 62.966  21.654  38.699  1.00 8.68  ? 148  HIS C CA  1 
ATOM   6467  C  C   . HIS C  1 148 ? 62.773  20.480  39.698  1.00 9.04  ? 148  HIS C C   1 
ATOM   6468  O  O   . HIS C  1 148 ? 63.543  20.308  40.656  1.00 8.95  ? 148  HIS C O   1 
ATOM   6469  C  CB  . HIS C  1 148 ? 63.783  22.797  39.353  1.00 7.96  ? 148  HIS C CB  1 
ATOM   6470  C  CG  . HIS C  1 148 ? 63.986  23.990  38.463  1.00 10.49 ? 148  HIS C CG  1 
ATOM   6471  N  ND1 . HIS C  1 148 ? 65.213  24.332  37.935  1.00 12.47 ? 148  HIS C ND1 1 
ATOM   6472  C  CD2 . HIS C  1 148 ? 63.117  24.938  38.029  1.00 11.36 ? 148  HIS C CD2 1 
ATOM   6473  C  CE1 . HIS C  1 148 ? 65.091  25.408  37.180  1.00 8.26  ? 148  HIS C CE1 1 
ATOM   6474  N  NE2 . HIS C  1 148 ? 63.834  25.823  37.258  1.00 13.44 ? 148  HIS C NE2 1 
ATOM   6475  N  N   . THR C  1 149 ? 61.730  19.676  39.485  1.00 7.66  ? 149  THR C N   1 
ATOM   6476  C  CA  . THR C  1 149 ? 61.575  18.491  40.339  1.00 7.05  ? 149  THR C CA  1 
ATOM   6477  C  C   . THR C  1 149 ? 62.767  17.548  40.203  1.00 7.22  ? 149  THR C C   1 
ATOM   6478  O  O   . THR C  1 149 ? 63.295  17.386  39.080  1.00 9.28  ? 149  THR C O   1 
ATOM   6479  C  CB  . THR C  1 149 ? 60.211  17.843  39.998  1.00 5.88  ? 149  THR C CB  1 
ATOM   6480  O  OG1 . THR C  1 149 ? 59.876  16.838  40.964  1.00 7.71  ? 149  THR C OG1 1 
ATOM   6481  C  CG2 . THR C  1 149 ? 60.225  17.154  38.633  1.00 7.09  ? 149  THR C CG2 1 
ATOM   6482  N  N   . PRO C  1 150 ? 63.242  16.944  41.320  1.00 7.74  ? 150  PRO C N   1 
ATOM   6483  C  CA  . PRO C  1 150 ? 64.449  16.102  41.296  1.00 7.67  ? 150  PRO C CA  1 
ATOM   6484  C  C   . PRO C  1 150 ? 64.403  15.045  40.185  1.00 8.03  ? 150  PRO C C   1 
ATOM   6485  O  O   . PRO C  1 150 ? 65.421  14.845  39.445  1.00 8.32  ? 150  PRO C O   1 
ATOM   6486  C  CB  . PRO C  1 150 ? 64.504  15.478  42.730  1.00 6.81  ? 150  PRO C CB  1 
ATOM   6487  C  CG  . PRO C  1 150 ? 63.847  16.614  43.611  1.00 6.14  ? 150  PRO C CG  1 
ATOM   6488  C  CD  . PRO C  1 150 ? 62.706  17.106  42.702  1.00 7.79  ? 150  PRO C CD  1 
ATOM   6489  N  N   . TYR C  1 151 ? 63.259  14.403  40.034  1.00 6.75  ? 151  TYR C N   1 
ATOM   6490  C  CA  . TYR C  1 151 ? 63.093  13.467  38.923  1.00 7.45  ? 151  TYR C CA  1 
ATOM   6491  C  C   . TYR C  1 151 ? 61.592  13.428  38.561  1.00 8.59  ? 151  TYR C C   1 
ATOM   6492  O  O   . TYR C  1 151 ? 60.768  13.877  39.344  1.00 7.39  ? 151  TYR C O   1 
ATOM   6493  C  CB  . TYR C  1 151 ? 63.666  12.054  39.220  1.00 7.58  ? 151  TYR C CB  1 
ATOM   6494  C  CG  . TYR C  1 151 ? 62.984  11.228  40.304  1.00 7.35  ? 151  TYR C CG  1 
ATOM   6495  C  CD1 . TYR C  1 151 ? 61.723  10.589  40.091  1.00 5.19  ? 151  TYR C CD1 1 
ATOM   6496  C  CD2 . TYR C  1 151 ? 63.612  11.035  41.535  1.00 7.06  ? 151  TYR C CD2 1 
ATOM   6497  C  CE1 . TYR C  1 151 ? 61.119  9.830   41.115  1.00 8.47  ? 151  TYR C CE1 1 
ATOM   6498  C  CE2 . TYR C  1 151 ? 63.032  10.306  42.545  1.00 5.82  ? 151  TYR C CE2 1 
ATOM   6499  C  CZ  . TYR C  1 151 ? 61.823  9.689   42.342  1.00 8.88  ? 151  TYR C CZ  1 
ATOM   6500  O  OH  . TYR C  1 151 ? 61.346  8.929   43.394  1.00 6.94  ? 151  TYR C OH  1 
ATOM   6501  N  N   . ILE C  1 152 ? 61.253  12.961  37.364  1.00 7.60  ? 152  ILE C N   1 
ATOM   6502  C  CA  . ILE C  1 152 ? 59.850  13.006  36.912  1.00 10.07 ? 152  ILE C CA  1 
ATOM   6503  C  C   . ILE C  1 152 ? 59.095  11.887  37.567  1.00 10.66 ? 152  ILE C C   1 
ATOM   6504  O  O   . ILE C  1 152 ? 59.462  10.755  37.372  1.00 12.76 ? 152  ILE C O   1 
ATOM   6505  C  CB  . ILE C  1 152 ? 59.745  12.815  35.345  1.00 10.10 ? 152  ILE C CB  1 
ATOM   6506  C  CG1 . ILE C  1 152 ? 60.759  13.676  34.609  1.00 11.90 ? 152  ILE C CG1 1 
ATOM   6507  C  CG2 . ILE C  1 152 ? 58.304  13.102  34.846  1.00 11.08 ? 152  ILE C CG2 1 
ATOM   6508  C  CD1 . ILE C  1 152 ? 60.723  15.132  34.956  1.00 8.75  ? 152  ILE C CD1 1 
ATOM   6509  N  N   . PRO C  1 153 ? 58.034  12.186  38.314  1.00 12.41 ? 153  PRO C N   1 
ATOM   6510  C  CA  . PRO C  1 153 ? 57.254  11.186  39.073  1.00 12.71 ? 153  PRO C CA  1 
ATOM   6511  C  C   . PRO C  1 153 ? 56.676  9.969   38.296  1.00 13.73 ? 153  PRO C C   1 
ATOM   6512  O  O   . PRO C  1 153 ? 56.291  10.168  37.129  1.00 14.71 ? 153  PRO C O   1 
ATOM   6513  C  CB  . PRO C  1 153 ? 56.093  12.019  39.619  1.00 13.21 ? 153  PRO C CB  1 
ATOM   6514  C  CG  . PRO C  1 153 ? 56.629  13.316  39.729  1.00 13.56 ? 153  PRO C CG  1 
ATOM   6515  C  CD  . PRO C  1 153 ? 57.514  13.547  38.517  1.00 12.25 ? 153  PRO C CD  1 
ATOM   6516  N  N   . SER C  1 159 ? 60.226  -5.862  34.729  1.00 30.36 ? 159  SER C N   1 
ATOM   6517  C  CA  . SER C  1 159 ? 61.032  -4.639  34.742  1.00 30.19 ? 159  SER C CA  1 
ATOM   6518  C  C   . SER C  1 159 ? 62.324  -4.769  33.907  1.00 29.27 ? 159  SER C C   1 
ATOM   6519  O  O   . SER C  1 159 ? 63.243  -5.536  34.238  1.00 29.26 ? 159  SER C O   1 
ATOM   6520  C  CB  . SER C  1 159 ? 61.338  -4.205  36.189  1.00 30.60 ? 159  SER C CB  1 
ATOM   6521  O  OG  . SER C  1 159 ? 61.454  -2.784  36.282  1.00 31.99 ? 159  SER C OG  1 
ATOM   6522  N  N   . SER C  1 160 ? 62.373  -4.025  32.806  1.00 28.19 ? 160  SER C N   1 
ATOM   6523  C  CA  . SER C  1 160 ? 63.578  -3.949  31.981  1.00 26.49 ? 160  SER C CA  1 
ATOM   6524  C  C   . SER C  1 160 ? 64.738  -3.255  32.721  1.00 24.71 ? 160  SER C C   1 
ATOM   6525  O  O   . SER C  1 160 ? 64.510  -2.306  33.490  1.00 24.82 ? 160  SER C O   1 
ATOM   6526  C  CB  . SER C  1 160 ? 63.274  -3.190  30.684  1.00 26.61 ? 160  SER C CB  1 
ATOM   6527  O  OG  . SER C  1 160 ? 63.646  -3.975  29.570  1.00 28.43 ? 160  SER C OG  1 
ATOM   6528  N  N   . THR C  1 161 ? 65.969  -3.728  32.489  1.00 22.23 ? 161  THR C N   1 
ATOM   6529  C  CA  . THR C  1 161 ? 67.168  -2.952  32.838  1.00 19.98 ? 161  THR C CA  1 
ATOM   6530  C  C   . THR C  1 161 ? 67.059  -1.543  32.226  1.00 18.94 ? 161  THR C C   1 
ATOM   6531  O  O   . THR C  1 161 ? 66.755  -1.395  31.045  1.00 17.45 ? 161  THR C O   1 
ATOM   6532  C  CB  . THR C  1 161 ? 68.483  -3.642  32.332  1.00 20.50 ? 161  THR C CB  1 
ATOM   6533  O  OG1 . THR C  1 161 ? 68.740  -4.858  33.068  1.00 17.11 ? 161  THR C OG1 1 
ATOM   6534  C  CG2 . THR C  1 161 ? 69.709  -2.727  32.614  1.00 18.08 ? 161  THR C CG2 1 
ATOM   6535  N  N   . THR C  1 162 ? 67.298  -0.524  33.048  1.00 17.93 ? 162  THR C N   1 
ATOM   6536  C  CA  . THR C  1 162 ? 67.271  0.851   32.604  1.00 18.11 ? 162  THR C CA  1 
ATOM   6537  C  C   . THR C  1 162 ? 68.406  1.112   31.602  1.00 18.00 ? 162  THR C C   1 
ATOM   6538  O  O   . THR C  1 162 ? 69.504  0.577   31.739  1.00 17.58 ? 162  THR C O   1 
ATOM   6539  C  CB  . THR C  1 162 ? 67.392  1.814   33.823  1.00 19.22 ? 162  THR C CB  1 
ATOM   6540  O  OG1 . THR C  1 162 ? 66.238  1.644   34.675  1.00 19.37 ? 162  THR C OG1 1 
ATOM   6541  C  CG2 . THR C  1 162 ? 67.359  3.279   33.357  1.00 15.53 ? 162  THR C CG2 1 
ATOM   6542  N  N   . GLY C  1 163 ? 68.108  1.938   30.605  1.00 17.63 ? 163  GLY C N   1 
ATOM   6543  C  CA  . GLY C  1 163 ? 69.081  2.410   29.638  1.00 17.93 ? 163  GLY C CA  1 
ATOM   6544  C  C   . GLY C  1 163 ? 69.078  1.557   28.386  1.00 17.72 ? 163  GLY C C   1 
ATOM   6545  O  O   . GLY C  1 163 ? 68.127  0.804   28.138  1.00 17.63 ? 163  GLY C O   1 
ATOM   6546  N  N   . PRO C  1 164 ? 70.156  1.646   27.608  1.00 17.98 ? 164  PRO C N   1 
ATOM   6547  C  CA  . PRO C  1 164 ? 70.269  0.885   26.345  1.00 17.58 ? 164  PRO C CA  1 
ATOM   6548  C  C   . PRO C  1 164 ? 70.172  -0.663  26.540  1.00 17.81 ? 164  PRO C C   1 
ATOM   6549  O  O   . PRO C  1 164 ? 70.672  -1.219  27.548  1.00 17.00 ? 164  PRO C O   1 
ATOM   6550  C  CB  . PRO C  1 164 ? 71.667  1.276   25.841  1.00 17.77 ? 164  PRO C CB  1 
ATOM   6551  C  CG  . PRO C  1 164 ? 72.396  1.734   27.073  1.00 17.23 ? 164  PRO C CG  1 
ATOM   6552  C  CD  . PRO C  1 164 ? 71.361  2.447   27.891  1.00 17.12 ? 164  PRO C CD  1 
ATOM   6553  N  N   . ASP C  1 165 ? 69.535  -1.349  25.588  1.00 17.24 ? 165  ASP C N   1 
ATOM   6554  C  CA  . ASP C  1 165 ? 69.462  -2.813  25.650  1.00 17.83 ? 165  ASP C CA  1 
ATOM   6555  C  C   . ASP C  1 165 ? 70.807  -3.496  25.288  1.00 17.75 ? 165  ASP C C   1 
ATOM   6556  O  O   . ASP C  1 165 ? 71.814  -2.812  25.025  1.00 17.42 ? 165  ASP C O   1 
ATOM   6557  C  CB  . ASP C  1 165 ? 68.279  -3.350  24.837  1.00 17.53 ? 165  ASP C CB  1 
ATOM   6558  C  CG  . ASP C  1 165 ? 68.391  -3.064  23.335  1.00 18.61 ? 165  ASP C CG  1 
ATOM   6559  O  OD1 . ASP C  1 165 ? 69.434  -2.579  22.843  1.00 20.93 ? 165  ASP C OD1 1 
ATOM   6560  O  OD2 . ASP C  1 165 ? 67.451  -3.300  22.568  1.00 15.61 ? 165  ASP C OD2 1 
ATOM   6561  N  N   . SER C  1 166 ? 70.844  -4.829  25.311  1.00 18.43 ? 166  SER C N   1 
ATOM   6562  C  CA  . SER C  1 166 ? 72.111  -5.525  25.062  1.00 19.25 ? 166  SER C CA  1 
ATOM   6563  C  C   . SER C  1 166 ? 72.739  -5.133  23.687  1.00 19.46 ? 166  SER C C   1 
ATOM   6564  O  O   . SER C  1 166 ? 73.913  -4.767  23.645  1.00 19.65 ? 166  SER C O   1 
ATOM   6565  C  CB  . SER C  1 166 ? 72.020  -7.039  25.352  1.00 19.59 ? 166  SER C CB  1 
ATOM   6566  O  OG  . SER C  1 166 ? 70.913  -7.639  24.688  1.00 21.47 ? 166  SER C OG  1 
ATOM   6567  N  N   . SER C  1 167 ? 71.954  -5.110  22.602  1.00 19.66 ? 167  SER C N   1 
ATOM   6568  C  CA  . SER C  1 167 ? 72.447  -4.574  21.300  1.00 20.07 ? 167  SER C CA  1 
ATOM   6569  C  C   . SER C  1 167 ? 73.139  -3.208  21.417  1.00 19.37 ? 167  SER C C   1 
ATOM   6570  O  O   . SER C  1 167 ? 74.304  -3.056  21.042  1.00 19.21 ? 167  SER C O   1 
ATOM   6571  C  CB  . SER C  1 167 ? 71.319  -4.426  20.277  1.00 20.13 ? 167  SER C CB  1 
ATOM   6572  O  OG  . SER C  1 167 ? 70.370  -5.459  20.417  1.00 23.02 ? 167  SER C OG  1 
ATOM   6573  N  N   . THR C  1 168 ? 72.402  -2.232  21.954  1.00 18.40 ? 168  THR C N   1 
ATOM   6574  C  CA  . THR C  1 168 ? 72.769  -0.827  21.861  1.00 17.25 ? 168  THR C CA  1 
ATOM   6575  C  C   . THR C  1 168 ? 73.990  -0.545  22.717  1.00 17.09 ? 168  THR C C   1 
ATOM   6576  O  O   . THR C  1 168 ? 74.926  0.075   22.221  1.00 16.73 ? 168  THR C O   1 
ATOM   6577  C  CB  . THR C  1 168 ? 71.578  0.099   22.241  1.00 16.95 ? 168  THR C CB  1 
ATOM   6578  O  OG1 . THR C  1 168 ? 70.478  -0.137  21.352  1.00 16.69 ? 168  THR C OG1 1 
ATOM   6579  C  CG2 . THR C  1 168 ? 71.937  1.571   22.023  1.00 15.04 ? 168  THR C CG2 1 
ATOM   6580  N  N   . ILE C  1 169 ? 73.984  -1.002  23.986  1.00 16.91 ? 169  ILE C N   1 
ATOM   6581  C  CA  . ILE C  1 169 ? 75.144  -0.812  24.894  1.00 16.02 ? 169  ILE C CA  1 
ATOM   6582  C  C   . ILE C  1 169 ? 76.472  -1.397  24.306  1.00 16.47 ? 169  ILE C C   1 
ATOM   6583  O  O   . ILE C  1 169 ? 77.575  -1.048  24.790  1.00 16.43 ? 169  ILE C O   1 
ATOM   6584  C  CB  . ILE C  1 169 ? 74.890  -1.349  26.344  1.00 15.45 ? 169  ILE C CB  1 
ATOM   6585  C  CG1 . ILE C  1 169 ? 75.738  -0.534  27.335  1.00 14.97 ? 169  ILE C CG1 1 
ATOM   6586  C  CG2 . ILE C  1 169 ? 75.281  -2.824  26.467  1.00 14.04 ? 169  ILE C CG2 1 
ATOM   6587  C  CD1 . ILE C  1 169 ? 75.305  -0.563  28.779  1.00 15.54 ? 169  ILE C CD1 1 
ATOM   6588  N  N   . SER C  1 170 ? 76.337  -2.269  23.293  1.00 15.26 ? 170  SER C N   1 
ATOM   6589  C  CA  . SER C  1 170 ? 77.471  -2.841  22.564  1.00 15.68 ? 170  SER C CA  1 
ATOM   6590  C  C   . SER C  1 170 ? 77.895  -1.981  21.360  1.00 15.01 ? 170  SER C C   1 
ATOM   6591  O  O   . SER C  1 170 ? 78.552  -2.441  20.448  1.00 16.08 ? 170  SER C O   1 
ATOM   6592  C  CB  . SER C  1 170 ? 77.132  -4.264  22.116  1.00 16.28 ? 170  SER C CB  1 
ATOM   6593  O  OG  . SER C  1 170 ? 76.854  -5.072  23.250  1.00 16.77 ? 170  SER C OG  1 
ATOM   6594  N  N   . THR C  1 171 ? 77.568  -0.710  21.405  1.00 14.58 ? 171  THR C N   1 
ATOM   6595  C  CA  . THR C  1 171 ? 77.557  0.124   20.226  1.00 15.30 ? 171  THR C CA  1 
ATOM   6596  C  C   . THR C  1 171 ? 78.102  1.541   20.607  1.00 14.09 ? 171  THR C C   1 
ATOM   6597  O  O   . THR C  1 171 ? 78.129  2.483   19.788  1.00 14.22 ? 171  THR C O   1 
ATOM   6598  C  CB  . THR C  1 171 ? 76.073  0.078   19.689  1.00 15.48 ? 171  THR C CB  1 
ATOM   6599  O  OG1 . THR C  1 171 ? 76.038  -0.538  18.400  1.00 16.18 ? 171  THR C OG1 1 
ATOM   6600  C  CG2 . THR C  1 171 ? 75.437  1.440   19.524  1.00 16.18 ? 171  THR C CG2 1 
ATOM   6601  N  N   . LEU C  1 172 ? 78.622  1.621   21.835  1.00 12.17 ? 172  LEU C N   1 
ATOM   6602  C  CA  . LEU C  1 172 ? 78.948  2.865   22.494  1.00 9.27  ? 172  LEU C CA  1 
ATOM   6603  C  C   . LEU C  1 172 ? 80.447  2.955   22.773  1.00 7.88  ? 172  LEU C C   1 
ATOM   6604  O  O   . LEU C  1 172 ? 80.900  3.777   23.603  1.00 4.85  ? 172  LEU C O   1 
ATOM   6605  C  CB  . LEU C  1 172 ? 78.213  2.912   23.835  1.00 10.21 ? 172  LEU C CB  1 
ATOM   6606  C  CG  . LEU C  1 172 ? 76.689  2.747   23.875  1.00 12.17 ? 172  LEU C CG  1 
ATOM   6607  C  CD1 . LEU C  1 172 ? 76.250  2.617   25.313  1.00 11.16 ? 172  LEU C CD1 1 
ATOM   6608  C  CD2 . LEU C  1 172 ? 75.952  3.936   23.240  1.00 12.81 ? 172  LEU C CD2 1 
ATOM   6609  N  N   . GLN C  1 173 ? 81.231  2.114   22.098  1.00 6.30  ? 173  GLN C N   1 
ATOM   6610  C  CA  . GLN C  1 173 ? 82.670  2.122   22.335  1.00 6.85  ? 173  GLN C CA  1 
ATOM   6611  C  C   . GLN C  1 173 ? 83.299  3.540   22.054  1.00 6.16  ? 173  GLN C C   1 
ATOM   6612  O  O   . GLN C  1 173 ? 84.237  3.963   22.717  1.00 4.74  ? 173  GLN C O   1 
ATOM   6613  C  CB  . GLN C  1 173 ? 83.334  0.992   21.542  1.00 6.02  ? 173  GLN C CB  1 
ATOM   6614  C  CG  . GLN C  1 173 ? 82.326  0.055   20.825  1.00 10.82 ? 173  GLN C CG  1 
ATOM   6615  C  CD  . GLN C  1 173 ? 82.674  -1.408  20.996  1.00 17.31 ? 173  GLN C CD  1 
ATOM   6616  O  OE1 . GLN C  1 173 ? 83.683  -1.733  21.625  1.00 24.35 ? 173  GLN C OE1 1 
ATOM   6617  N  NE2 . GLN C  1 173 ? 81.853  -2.296  20.438  1.00 11.37 ? 173  GLN C NE2 1 
ATOM   6618  N  N   . SER C  1 174 ? 82.732  4.289   21.116  1.00 6.62  ? 174  SER C N   1 
ATOM   6619  C  CA  . SER C  1 174 ? 83.246  5.616   20.819  1.00 6.88  ? 174  SER C CA  1 
ATOM   6620  C  C   . SER C  1 174 ? 83.031  6.618   21.965  1.00 6.14  ? 174  SER C C   1 
ATOM   6621  O  O   . SER C  1 174 ? 83.757  7.584   22.040  1.00 7.84  ? 174  SER C O   1 
ATOM   6622  C  CB  . SER C  1 174 ? 82.716  6.110   19.489  1.00 6.65  ? 174  SER C CB  1 
ATOM   6623  O  OG  . SER C  1 174 ? 83.311  5.385   18.388  1.00 13.56 ? 174  SER C OG  1 
ATOM   6624  N  N   . PHE C  1 175 ? 82.072  6.364   22.879  1.00 4.49  ? 175  PHE C N   1 
ATOM   6625  C  CA  . PHE C  1 175 ? 81.964  7.101   24.132  1.00 3.50  ? 175  PHE C CA  1 
ATOM   6626  C  C   . PHE C  1 175 ? 82.764  6.524   25.280  1.00 2.64  ? 175  PHE C C   1 
ATOM   6627  O  O   . PHE C  1 175 ? 82.576  6.895   26.403  1.00 3.80  ? 175  PHE C O   1 
ATOM   6628  C  CB  . PHE C  1 175 ? 80.503  7.247   24.598  1.00 2.91  ? 175  PHE C CB  1 
ATOM   6629  C  CG  . PHE C  1 175 ? 79.619  7.969   23.620  1.00 2.00  ? 175  PHE C CG  1 
ATOM   6630  C  CD1 . PHE C  1 175 ? 79.676  9.338   23.495  1.00 2.73  ? 175  PHE C CD1 1 
ATOM   6631  C  CD2 . PHE C  1 175 ? 78.719  7.281   22.843  1.00 2.00  ? 175  PHE C CD2 1 
ATOM   6632  C  CE1 . PHE C  1 175 ? 78.833  9.999   22.604  1.00 2.00  ? 175  PHE C CE1 1 
ATOM   6633  C  CE2 . PHE C  1 175 ? 77.873  7.952   21.933  1.00 4.11  ? 175  PHE C CE2 1 
ATOM   6634  C  CZ  . PHE C  1 175 ? 77.938  9.315   21.843  1.00 2.00  ? 175  PHE C CZ  1 
ATOM   6635  N  N   . ASP C  1 176 ? 83.667  5.609   24.998  1.00 4.49  ? 176  ASP C N   1 
ATOM   6636  C  CA  . ASP C  1 176 ? 84.398  4.892   26.067  1.00 4.30  ? 176  ASP C CA  1 
ATOM   6637  C  C   . ASP C  1 176 ? 83.526  4.010   26.943  1.00 3.54  ? 176  ASP C C   1 
ATOM   6638  O  O   . ASP C  1 176 ? 83.774  3.902   28.128  1.00 3.05  ? 176  ASP C O   1 
ATOM   6639  C  CB  . ASP C  1 176 ? 85.234  5.845   26.923  1.00 4.61  ? 176  ASP C CB  1 
ATOM   6640  C  CG  . ASP C  1 176 ? 86.251  5.115   27.812  1.00 5.46  ? 176  ASP C CG  1 
ATOM   6641  O  OD1 . ASP C  1 176 ? 86.752  4.028   27.410  1.00 9.61  ? 176  ASP C OD1 1 
ATOM   6642  O  OD2 . ASP C  1 176 ? 86.631  5.578   28.914  1.00 7.03  ? 176  ASP C OD2 1 
ATOM   6643  N  N   . VAL C  1 177 ? 82.540  3.343   26.354  1.00 3.35  ? 177  VAL C N   1 
ATOM   6644  C  CA  . VAL C  1 177 ? 81.702  2.427   27.128  1.00 4.42  ? 177  VAL C CA  1 
ATOM   6645  C  C   . VAL C  1 177 ? 81.764  1.082   26.386  1.00 4.12  ? 177  VAL C C   1 
ATOM   6646  O  O   . VAL C  1 177 ? 81.451  0.990   25.189  1.00 5.43  ? 177  VAL C O   1 
ATOM   6647  C  CB  . VAL C  1 177 ? 80.208  2.883   27.185  1.00 4.79  ? 177  VAL C CB  1 
ATOM   6648  C  CG1 . VAL C  1 177 ? 79.295  1.773   27.806  1.00 5.28  ? 177  VAL C CG1 1 
ATOM   6649  C  CG2 . VAL C  1 177 ? 80.041  4.181   27.908  1.00 3.86  ? 177  VAL C CG2 1 
ATOM   6650  N  N   . TYR C  1 178 ? 82.171  0.046   27.106  1.00 4.04  ? 178  TYR C N   1 
ATOM   6651  C  CA  . TYR C  1 178 ? 82.360  -1.277  26.522  1.00 4.16  ? 178  TYR C CA  1 
ATOM   6652  C  C   . TYR C  1 178 ? 81.446  -2.229  27.278  1.00 3.99  ? 178  TYR C C   1 
ATOM   6653  O  O   . TYR C  1 178 ? 81.497  -2.303  28.502  1.00 2.00  ? 178  TYR C O   1 
ATOM   6654  C  CB  . TYR C  1 178 ? 83.852  -1.706  26.570  1.00 4.61  ? 178  TYR C CB  1 
ATOM   6655  C  CG  . TYR C  1 178 ? 84.761  -0.840  25.743  1.00 6.43  ? 178  TYR C CG  1 
ATOM   6656  C  CD1 . TYR C  1 178 ? 85.231  0.382   26.257  1.00 7.63  ? 178  TYR C CD1 1 
ATOM   6657  C  CD2 . TYR C  1 178 ? 85.144  -1.210  24.436  1.00 7.11  ? 178  TYR C CD2 1 
ATOM   6658  C  CE1 . TYR C  1 178 ? 86.068  1.222   25.495  1.00 8.52  ? 178  TYR C CE1 1 
ATOM   6659  C  CE2 . TYR C  1 178 ? 85.959  -0.354  23.641  1.00 8.36  ? 178  TYR C CE2 1 
ATOM   6660  C  CZ  . TYR C  1 178 ? 86.410  0.876   24.204  1.00 9.91  ? 178  TYR C CZ  1 
ATOM   6661  O  OH  . TYR C  1 178 ? 87.221  1.763   23.521  1.00 10.51 ? 178  TYR C OH  1 
ATOM   6662  N  N   . ALA C  1 179 ? 80.634  -2.982  26.534  1.00 5.13  ? 179  ALA C N   1 
ATOM   6663  C  CA  . ALA C  1 179 ? 79.656  -3.850  27.151  1.00 5.83  ? 179  ALA C CA  1 
ATOM   6664  C  C   . ALA C  1 179 ? 80.371  -5.000  27.854  1.00 6.75  ? 179  ALA C C   1 
ATOM   6665  O  O   . ALA C  1 179 ? 81.415  -5.470  27.383  1.00 5.66  ? 179  ALA C O   1 
ATOM   6666  C  CB  . ALA C  1 179 ? 78.726  -4.402  26.078  1.00 6.61  ? 179  ALA C CB  1 
ATOM   6667  N  N   . GLU C  1 180 ? 79.790  -5.470  28.957  1.00 7.82  ? 180  GLU C N   1 
ATOM   6668  C  CA  . GLU C  1 180 ? 80.229  -6.718  29.594  1.00 9.86  ? 180  GLU C CA  1 
ATOM   6669  C  C   . GLU C  1 180 ? 79.007  -7.591  29.903  1.00 9.79  ? 180  GLU C C   1 
ATOM   6670  O  O   . GLU C  1 180 ? 78.662  -7.766  31.049  1.00 9.41  ? 180  GLU C O   1 
ATOM   6671  C  CB  . GLU C  1 180 ? 81.011  -6.414  30.899  1.00 10.44 ? 180  GLU C CB  1 
ATOM   6672  C  CG  . GLU C  1 180 ? 82.284  -5.589  30.755  1.00 12.19 ? 180  GLU C CG  1 
ATOM   6673  C  CD  . GLU C  1 180 ? 83.363  -6.290  29.946  1.00 17.47 ? 180  GLU C CD  1 
ATOM   6674  O  OE1 . GLU C  1 180 ? 83.464  -7.550  29.973  1.00 16.20 ? 180  GLU C OE1 1 
ATOM   6675  O  OE2 . GLU C  1 180 ? 84.102  -5.559  29.252  1.00 22.53 ? 180  GLU C OE2 1 
ATOM   6676  N  N   . LEU C  1 181 ? 78.354  -8.132  28.883  1.00 11.42 ? 181  LEU C N   1 
ATOM   6677  C  CA  . LEU C  1 181 ? 77.052  -8.777  29.076  1.00 12.87 ? 181  LEU C CA  1 
ATOM   6678  C  C   . LEU C  1 181 ? 77.105  -10.163 29.744  1.00 13.83 ? 181  LEU C C   1 
ATOM   6679  O  O   . LEU C  1 181 ? 76.102  -10.629 30.316  1.00 14.83 ? 181  LEU C O   1 
ATOM   6680  C  CB  . LEU C  1 181 ? 76.288  -8.840  27.752  1.00 14.25 ? 181  LEU C CB  1 
ATOM   6681  C  CG  . LEU C  1 181 ? 76.254  -7.576  26.884  1.00 14.28 ? 181  LEU C CG  1 
ATOM   6682  C  CD1 . LEU C  1 181 ? 75.693  -7.946  25.521  1.00 17.69 ? 181  LEU C CD1 1 
ATOM   6683  C  CD2 . LEU C  1 181 ? 75.463  -6.427  27.538  1.00 15.38 ? 181  LEU C CD2 1 
ATOM   6684  N  N   . SER C  1 182 ? 78.264  -10.810 29.701  1.00 12.86 ? 182  SER C N   1 
ATOM   6685  C  CA  . SER C  1 182 ? 78.475  -12.012 30.513  1.00 13.05 ? 182  SER C CA  1 
ATOM   6686  C  C   . SER C  1 182 ? 78.602  -11.771 32.051  1.00 12.01 ? 182  SER C C   1 
ATOM   6687  O  O   . SER C  1 182 ? 78.515  -12.725 32.829  1.00 12.05 ? 182  SER C O   1 
ATOM   6688  C  CB  . SER C  1 182 ? 79.709  -12.750 30.013  1.00 13.66 ? 182  SER C CB  1 
ATOM   6689  O  OG  . SER C  1 182 ? 80.841  -11.945 30.293  1.00 15.90 ? 182  SER C OG  1 
ATOM   6690  N  N   . PHE C  1 183 ? 78.822  -10.529 32.486  1.00 10.23 ? 183  PHE C N   1 
ATOM   6691  C  CA  . PHE C  1 183 ? 78.968  -10.238 33.931  1.00 8.91  ? 183  PHE C CA  1 
ATOM   6692  C  C   . PHE C  1 183 ? 77.662  -10.468 34.674  1.00 8.64  ? 183  PHE C C   1 
ATOM   6693  O  O   . PHE C  1 183 ? 76.613  -9.894  34.319  1.00 7.86  ? 183  PHE C O   1 
ATOM   6694  C  CB  . PHE C  1 183 ? 79.404  -8.783  34.108  1.00 8.79  ? 183  PHE C CB  1 
ATOM   6695  C  CG  . PHE C  1 183 ? 79.645  -8.348  35.548  1.00 7.69  ? 183  PHE C CG  1 
ATOM   6696  C  CD1 . PHE C  1 183 ? 80.863  -8.618  36.187  1.00 8.41  ? 183  PHE C CD1 1 
ATOM   6697  C  CD2 . PHE C  1 183 ? 78.697  -7.601  36.218  1.00 7.88  ? 183  PHE C CD2 1 
ATOM   6698  C  CE1 . PHE C  1 183 ? 81.101  -8.162  37.501  1.00 5.81  ? 183  PHE C CE1 1 
ATOM   6699  C  CE2 . PHE C  1 183 ? 78.900  -7.134  37.532  1.00 8.33  ? 183  PHE C CE2 1 
ATOM   6700  C  CZ  . PHE C  1 183 ? 80.103  -7.393  38.181  1.00 7.02  ? 183  PHE C CZ  1 
ATOM   6701  N  N   . THR C  1 184 ? 77.708  -11.279 35.724  1.00 7.62  ? 184  THR C N   1 
ATOM   6702  C  CA  . THR C  1 184 ? 76.518  -11.489 36.522  1.00 7.45  ? 184  THR C CA  1 
ATOM   6703  C  C   . THR C  1 184 ? 76.685  -10.814 37.890  1.00 6.43  ? 184  THR C C   1 
ATOM   6704  O  O   . THR C  1 184 ? 77.537  -11.220 38.671  1.00 6.52  ? 184  THR C O   1 
ATOM   6705  C  CB  . THR C  1 184 ? 76.190  -12.990 36.654  1.00 8.39  ? 184  THR C CB  1 
ATOM   6706  O  OG1 . THR C  1 184 ? 75.977  -13.537 35.344  1.00 8.77  ? 184  THR C OG1 1 
ATOM   6707  C  CG2 . THR C  1 184 ? 74.832  -13.154 37.336  1.00 9.29  ? 184  THR C CG2 1 
ATOM   6708  N  N   . PRO C  1 185 ? 75.927  -9.759  38.172  1.00 5.18  ? 185  PRO C N   1 
ATOM   6709  C  CA  . PRO C  1 185 ? 76.034  -9.123  39.508  1.00 5.31  ? 185  PRO C CA  1 
ATOM   6710  C  C   . PRO C  1 185 ? 75.693  -10.129 40.581  1.00 4.89  ? 185  PRO C C   1 
ATOM   6711  O  O   . PRO C  1 185 ? 74.730  -10.911 40.450  1.00 4.74  ? 185  PRO C O   1 
ATOM   6712  C  CB  . PRO C  1 185 ? 75.042  -7.936  39.452  1.00 4.17  ? 185  PRO C CB  1 
ATOM   6713  C  CG  . PRO C  1 185 ? 74.871  -7.690  37.996  1.00 5.78  ? 185  PRO C CG  1 
ATOM   6714  C  CD  . PRO C  1 185 ? 74.982  -9.042  37.289  1.00 4.16  ? 185  PRO C CD  1 
ATOM   6715  N  N   . ARG C  1 186 ? 76.524  -10.186 41.618  1.00 4.62  ? 186  ARG C N   1 
ATOM   6716  C  CA  . ARG C  1 186 ? 76.342  -11.269 42.583  1.00 4.77  ? 186  ARG C CA  1 
ATOM   6717  C  C   . ARG C  1 186 ? 75.080  -11.010 43.406  1.00 4.78  ? 186  ARG C C   1 
ATOM   6718  O  O   . ARG C  1 186 ? 74.593  -9.876  43.498  1.00 4.64  ? 186  ARG C O   1 
ATOM   6719  C  CB  . ARG C  1 186 ? 77.591  -11.476 43.426  1.00 4.67  ? 186  ARG C CB  1 
ATOM   6720  C  CG  . ARG C  1 186 ? 77.983  -10.230 44.243  1.00 3.38  ? 186  ARG C CG  1 
ATOM   6721  C  CD  . ARG C  1 186 ? 79.330  -10.382 44.996  1.00 4.37  ? 186  ARG C CD  1 
ATOM   6722  N  NE  . ARG C  1 186 ? 79.339  -11.618 45.766  1.00 3.26  ? 186  ARG C NE  1 
ATOM   6723  C  CZ  . ARG C  1 186 ? 80.391  -12.422 45.906  1.00 6.50  ? 186  ARG C CZ  1 
ATOM   6724  N  NH1 . ARG C  1 186 ? 81.583  -12.093 45.378  1.00 2.98  ? 186  ARG C NH1 1 
ATOM   6725  N  NH2 . ARG C  1 186 ? 80.245  -13.574 46.572  1.00 2.30  ? 186  ARG C NH2 1 
ATOM   6726  N  N   . THR C  1 187 ? 74.510  -12.081 43.941  1.00 5.16  ? 187  THR C N   1 
ATOM   6727  C  CA  . THR C  1 187 ? 73.176  -11.979 44.516  1.00 6.37  ? 187  THR C CA  1 
ATOM   6728  C  C   . THR C  1 187 ? 73.101  -12.549 45.928  1.00 6.15  ? 187  THR C C   1 
ATOM   6729  O  O   . THR C  1 187 ? 72.055  -13.010 46.363  1.00 6.14  ? 187  THR C O   1 
ATOM   6730  C  CB  . THR C  1 187 ? 72.168  -12.677 43.606  1.00 6.26  ? 187  THR C CB  1 
ATOM   6731  O  OG1 . THR C  1 187 ? 72.717  -13.919 43.139  1.00 7.66  ? 187  THR C OG1 1 
ATOM   6732  C  CG2 . THR C  1 187 ? 72.017  -11.842 42.331  1.00 5.61  ? 187  THR C CG2 1 
ATOM   6733  N  N   . ASP C  1 188 ? 74.231  -12.488 46.623  1.00 5.99  ? 188  ASP C N   1 
ATOM   6734  C  CA  . ASP C  1 188 ? 74.369  -12.990 47.967  1.00 5.87  ? 188  ASP C CA  1 
ATOM   6735  C  C   . ASP C  1 188 ? 74.639  -11.800 48.913  1.00 5.90  ? 188  ASP C C   1 
ATOM   6736  O  O   . ASP C  1 188 ? 75.398  -11.920 49.875  1.00 5.59  ? 188  ASP C O   1 
ATOM   6737  C  CB  . ASP C  1 188 ? 75.499  -14.061 47.991  1.00 6.98  ? 188  ASP C CB  1 
ATOM   6738  C  CG  . ASP C  1 188 ? 76.857  -13.507 47.549  1.00 6.36  ? 188  ASP C CG  1 
ATOM   6739  O  OD1 . ASP C  1 188 ? 76.927  -12.375 46.974  1.00 10.70 ? 188  ASP C OD1 1 
ATOM   6740  O  OD2 . ASP C  1 188 ? 77.919  -14.127 47.755  1.00 2.60  ? 188  ASP C OD2 1 
ATOM   6741  N  N   . THR C  1 189 ? 74.021  -10.646 48.630  1.00 4.72  ? 189  THR C N   1 
ATOM   6742  C  CA  . THR C  1 189 ? 74.203  -9.473  49.480  1.00 5.80  ? 189  THR C CA  1 
ATOM   6743  C  C   . THR C  1 189 ? 73.579  -9.696  50.864  1.00 5.90  ? 189  THR C C   1 
ATOM   6744  O  O   . THR C  1 189 ? 72.494  -10.265 50.973  1.00 6.40  ? 189  THR C O   1 
ATOM   6745  C  CB  . THR C  1 189 ? 73.574  -8.222  48.808  1.00 5.63  ? 189  THR C CB  1 
ATOM   6746  O  OG1 . THR C  1 189 ? 74.006  -8.139  47.430  1.00 6.31  ? 189  THR C OG1 1 
ATOM   6747  C  CG2 . THR C  1 189 ? 74.072  -6.919  49.459  1.00 6.85  ? 189  THR C CG2 1 
ATOM   6748  N  N   . VAL C  1 190 ? 74.296  -9.288  51.914  1.00 5.41  ? 190  VAL C N   1 
ATOM   6749  C  CA  . VAL C  1 190 ? 73.822  -9.362  53.292  1.00 4.09  ? 190  VAL C CA  1 
ATOM   6750  C  C   . VAL C  1 190 ? 74.282  -8.107  53.981  1.00 5.09  ? 190  VAL C C   1 
ATOM   6751  O  O   . VAL C  1 190 ? 75.430  -7.740  53.875  1.00 3.36  ? 190  VAL C O   1 
ATOM   6752  C  CB  . VAL C  1 190 ? 74.427  -10.577 54.055  1.00 5.90  ? 190  VAL C CB  1 
ATOM   6753  C  CG1 . VAL C  1 190 ? 73.778  -10.683 55.453  1.00 6.37  ? 190  VAL C CG1 1 
ATOM   6754  C  CG2 . VAL C  1 190 ? 74.182  -11.826 53.286  1.00 5.09  ? 190  VAL C CG2 1 
ATOM   6755  N  N   . ASN C  1 191 ? 73.380  -7.423  54.682  1.00 5.31  ? 191  ASN C N   1 
ATOM   6756  C  CA  . ASN C  1 191 ? 73.760  -6.171  55.336  1.00 6.10  ? 191  ASN C CA  1 
ATOM   6757  C  C   . ASN C  1 191 ? 74.506  -5.262  54.388  1.00 6.24  ? 191  ASN C C   1 
ATOM   6758  O  O   . ASN C  1 191 ? 75.444  -4.535  54.794  1.00 6.77  ? 191  ASN C O   1 
ATOM   6759  C  CB  . ASN C  1 191 ? 74.605  -6.434  56.603  1.00 6.75  ? 191  ASN C CB  1 
ATOM   6760  C  CG  . ASN C  1 191 ? 73.845  -7.191  57.621  1.00 7.40  ? 191  ASN C CG  1 
ATOM   6761  O  OD1 . ASN C  1 191 ? 72.592  -7.057  57.699  1.00 3.63  ? 191  ASN C OD1 1 
ATOM   6762  N  ND2 . ASN C  1 191 ? 74.569  -8.029  58.409  1.00 8.70  ? 191  ASN C ND2 1 
ATOM   6763  N  N   . GLY C  1 192 ? 74.046  -5.242  53.131  1.00 5.24  ? 192  GLY C N   1 
ATOM   6764  C  CA  . GLY C  1 192 ? 74.496  -4.243  52.187  1.00 5.70  ? 192  GLY C CA  1 
ATOM   6765  C  C   . GLY C  1 192 ? 75.874  -4.520  51.611  1.00 5.87  ? 192  GLY C C   1 
ATOM   6766  O  O   . GLY C  1 192 ? 76.461  -3.653  50.972  1.00 8.14  ? 192  GLY C O   1 
ATOM   6767  N  N   . THR C  1 193 ? 76.404  -5.719  51.793  1.00 6.46  ? 193  THR C N   1 
ATOM   6768  C  CA  . THR C  1 193 ? 77.690  -6.045  51.161  1.00 4.82  ? 193  THR C CA  1 
ATOM   6769  C  C   . THR C  1 193 ? 77.818  -7.504  50.788  1.00 4.04  ? 193  THR C C   1 
ATOM   6770  O  O   . THR C  1 193 ? 77.090  -8.368  51.348  1.00 2.86  ? 193  THR C O   1 
ATOM   6771  C  CB  . THR C  1 193 ? 78.876  -5.591  52.104  1.00 6.06  ? 193  THR C CB  1 
ATOM   6772  O  OG1 . THR C  1 193 ? 80.153  -5.756  51.439  1.00 7.61  ? 193  THR C OG1 1 
ATOM   6773  C  CG2 . THR C  1 193 ? 78.962  -6.507  53.360  1.00 5.75  ? 193  THR C CG2 1 
ATOM   6774  N  N   . ALA C  1 194 ? 78.729  -7.760  49.835  1.00 3.10  ? 194  ALA C N   1 
ATOM   6775  C  CA  . ALA C  1 194 ? 79.237  -9.117  49.525  1.00 3.72  ? 194  ALA C CA  1 
ATOM   6776  C  C   . ALA C  1 194 ? 80.560  -8.949  48.782  1.00 3.10  ? 194  ALA C C   1 
ATOM   6777  O  O   . ALA C  1 194 ? 80.756  -7.916  48.122  1.00 3.82  ? 194  ALA C O   1 
ATOM   6778  C  CB  . ALA C  1 194 ? 78.222  -9.957  48.683  1.00 3.20  ? 194  ALA C CB  1 
ATOM   6779  N  N   . PRO C  1 195 ? 81.484  -9.909  48.901  1.00 4.54  ? 195  PRO C N   1 
ATOM   6780  C  CA  . PRO C  1 195 ? 81.291  -11.167 49.642  1.00 3.68  ? 195  PRO C CA  1 
ATOM   6781  C  C   . PRO C  1 195 ? 81.312  -10.955 51.160  1.00 5.21  ? 195  PRO C C   1 
ATOM   6782  O  O   . PRO C  1 195 ? 81.406  -9.816  51.637  1.00 4.78  ? 195  PRO C O   1 
ATOM   6783  C  CB  . PRO C  1 195 ? 82.507  -12.021 49.203  1.00 4.62  ? 195  PRO C CB  1 
ATOM   6784  C  CG  . PRO C  1 195 ? 83.589  -10.968 48.971  1.00 3.45  ? 195  PRO C CG  1 
ATOM   6785  C  CD  . PRO C  1 195 ? 82.851  -9.781  48.355  1.00 4.73  ? 195  PRO C CD  1 
ATOM   6786  N  N   . ALA C  1 196 ? 81.188  -12.032 51.938  1.00 7.98  ? 196  ALA C N   1 
ATOM   6787  C  CA  . ALA C  1 196 ? 81.203  -11.904 53.411  1.00 10.26 ? 196  ALA C CA  1 
ATOM   6788  C  C   . ALA C  1 196 ? 82.591  -11.413 53.923  1.00 11.76 ? 196  ALA C C   1 
ATOM   6789  O  O   . ALA C  1 196 ? 83.617  -11.593 53.279  1.00 12.24 ? 196  ALA C O   1 
ATOM   6790  C  CB  . ALA C  1 196 ? 80.809  -13.230 54.057  1.00 9.78  ? 196  ALA C CB  1 
ATOM   6791  N  N   . ASN C  1 197 ? 82.662  -10.790 55.077  1.00 14.72 ? 197  ASN C N   1 
ATOM   6792  C  CA  . ASN C  1 197 ? 84.028  -10.513 55.565  1.00 17.80 ? 197  ASN C CA  1 
ATOM   6793  C  C   . ASN C  1 197 ? 84.703  -9.321  54.876  1.00 17.15 ? 197  ASN C C   1 
ATOM   6794  O  O   . ASN C  1 197 ? 85.895  -9.050  55.097  1.00 19.58 ? 197  ASN C O   1 
ATOM   6795  C  CB  . ASN C  1 197 ? 84.946  -11.756 55.426  1.00 18.81 ? 197  ASN C CB  1 
ATOM   6796  C  CG  . ASN C  1 197 ? 85.493  -12.244 56.786  1.00 24.09 ? 197  ASN C CG  1 
ATOM   6797  O  OD1 . ASN C  1 197 ? 85.540  -13.460 57.064  1.00 30.46 ? 197  ASN C OD1 1 
ATOM   6798  N  ND2 . ASN C  1 197 ? 85.935  -11.286 57.629  1.00 29.33 ? 197  ASN C ND2 1 
ATOM   6799  N  N   . THR C  1 198 ? 83.949  -8.658  54.020  1.00 13.88 ? 198  THR C N   1 
ATOM   6800  C  CA  . THR C  1 198 ? 84.204  -7.288  53.656  1.00 11.56 ? 198  THR C CA  1 
ATOM   6801  C  C   . THR C  1 198 ? 83.712  -6.426  54.812  1.00 10.51 ? 198  THR C C   1 
ATOM   6802  O  O   . THR C  1 198 ? 82.925  -6.862  55.643  1.00 8.70  ? 198  THR C O   1 
ATOM   6803  C  CB  . THR C  1 198 ? 83.429  -6.959  52.379  1.00 11.31 ? 198  THR C CB  1 
ATOM   6804  O  OG1 . THR C  1 198 ? 82.054  -7.356  52.556  1.00 9.22  ? 198  THR C OG1 1 
ATOM   6805  C  CG2 . THR C  1 198 ? 83.921  -7.860  51.259  1.00 11.91 ? 198  THR C CG2 1 
ATOM   6806  N  N   . VAL C  1 199 ? 84.149  -5.182  54.833  1.00 9.13  ? 199  VAL C N   1 
ATOM   6807  C  CA  . VAL C  1 199 ? 83.817  -4.273  55.913  1.00 9.33  ? 199  VAL C CA  1 
ATOM   6808  C  C   . VAL C  1 199 ? 82.967  -3.154  55.344  1.00 9.00  ? 199  VAL C C   1 
ATOM   6809  O  O   . VAL C  1 199 ? 83.417  -2.418  54.471  1.00 8.46  ? 199  VAL C O   1 
ATOM   6810  C  CB  . VAL C  1 199 ? 85.119  -3.673  56.544  1.00 8.95  ? 199  VAL C CB  1 
ATOM   6811  C  CG1 . VAL C  1 199 ? 84.752  -2.688  57.590  1.00 10.74 ? 199  VAL C CG1 1 
ATOM   6812  C  CG2 . VAL C  1 199 ? 85.996  -4.797  57.171  1.00 11.50 ? 199  VAL C CG2 1 
ATOM   6813  N  N   . TRP C  1 200 ? 81.754  -2.988  55.880  1.00 8.22  ? 200  TRP C N   1 
ATOM   6814  C  CA  . TRP C  1 200 ? 80.818  -2.039  55.285  1.00 7.60  ? 200  TRP C CA  1 
ATOM   6815  C  C   . TRP C  1 200 ? 79.915  -1.454  56.376  1.00 7.51  ? 200  TRP C C   1 
ATOM   6816  O  O   . TRP C  1 200 ? 78.964  -2.113  56.814  1.00 7.97  ? 200  TRP C O   1 
ATOM   6817  C  CB  . TRP C  1 200 ? 80.003  -2.667  54.118  1.00 5.76  ? 200  TRP C CB  1 
ATOM   6818  C  CG  . TRP C  1 200 ? 79.319  -1.562  53.297  1.00 8.90  ? 200  TRP C CG  1 
ATOM   6819  C  CD1 . TRP C  1 200 ? 77.976  -1.426  53.043  1.00 9.69  ? 200  TRP C CD1 1 
ATOM   6820  C  CD2 . TRP C  1 200 ? 79.960  -0.424  52.679  1.00 7.91  ? 200  TRP C CD2 1 
ATOM   6821  N  NE1 . TRP C  1 200 ? 77.746  -0.287  52.308  1.00 8.52  ? 200  TRP C NE1 1 
ATOM   6822  C  CE2 . TRP C  1 200 ? 78.945  0.343   52.059  1.00 8.09  ? 200  TRP C CE2 1 
ATOM   6823  C  CE3 . TRP C  1 200 ? 81.303  0.009   52.563  1.00 8.54  ? 200  TRP C CE3 1 
ATOM   6824  C  CZ2 . TRP C  1 200 ? 79.211  1.530   51.357  1.00 9.07  ? 200  TRP C CZ2 1 
ATOM   6825  C  CZ3 . TRP C  1 200 ? 81.578  1.179   51.832  1.00 8.77  ? 200  TRP C CZ3 1 
ATOM   6826  C  CH2 . TRP C  1 200 ? 80.532  1.937   51.253  1.00 8.27  ? 200  TRP C CH2 1 
ATOM   6827  N  N   . HIS C  1 201 ? 80.266  -0.236  56.831  1.00 8.79  ? 201  HIS C N   1 
ATOM   6828  C  CA  . HIS C  1 201 ? 79.612  0.486   57.951  1.00 8.71  ? 201  HIS C CA  1 
ATOM   6829  C  C   . HIS C  1 201 ? 79.845  -0.199  59.293  1.00 8.39  ? 201  HIS C C   1 
ATOM   6830  O  O   . HIS C  1 201 ? 79.082  0.045   60.234  1.00 8.68  ? 201  HIS C O   1 
ATOM   6831  C  CB  . HIS C  1 201 ? 78.100  0.657   57.714  1.00 8.87  ? 201  HIS C CB  1 
ATOM   6832  C  CG  . HIS C  1 201 ? 77.762  1.702   56.681  1.00 8.64  ? 201  HIS C CG  1 
ATOM   6833  N  ND1 . HIS C  1 201 ? 77.553  3.025   57.007  1.00 10.46 ? 201  HIS C ND1 1 
ATOM   6834  C  CD2 . HIS C  1 201 ? 77.616  1.621   55.333  1.00 9.06  ? 201  HIS C CD2 1 
ATOM   6835  C  CE1 . HIS C  1 201 ? 77.278  3.717   55.910  1.00 9.47  ? 201  HIS C CE1 1 
ATOM   6836  N  NE2 . HIS C  1 201 ? 77.335  2.894   54.877  1.00 7.46  ? 201  HIS C NE2 1 
ATOM   6837  N  N   . THR C  1 202 ? 80.852  -1.076  59.361  1.00 9.07  ? 202  THR C N   1 
ATOM   6838  C  CA  . THR C  1 202 ? 81.176  -1.833  60.580  1.00 8.60  ? 202  THR C CA  1 
ATOM   6839  C  C   . THR C  1 202 ? 82.658  -1.711  60.968  1.00 9.37  ? 202  THR C C   1 
ATOM   6840  O  O   . THR C  1 202 ? 83.115  -2.389  61.871  1.00 9.17  ? 202  THR C O   1 
ATOM   6841  C  CB  . THR C  1 202 ? 80.894  -3.329  60.404  1.00 9.45  ? 202  THR C CB  1 
ATOM   6842  O  OG1 . THR C  1 202 ? 81.557  -3.800  59.224  1.00 9.90  ? 202  THR C OG1 1 
ATOM   6843  C  CG2 . THR C  1 202 ? 79.378  -3.624  60.191  1.00 7.84  ? 202  THR C CG2 1 
ATOM   6844  N  N   . GLY C  1 203 ? 83.405  -0.852  60.280  1.00 9.26  ? 203  GLY C N   1 
ATOM   6845  C  CA  . GLY C  1 203 ? 84.816  -0.697  60.587  1.00 9.22  ? 203  GLY C CA  1 
ATOM   6846  C  C   . GLY C  1 203 ? 85.495  0.114   59.523  1.00 9.08  ? 203  GLY C C   1 
ATOM   6847  O  O   . GLY C  1 203 ? 84.867  0.508   58.555  1.00 6.56  ? 203  GLY C O   1 
ATOM   6848  N  N   . ALA C  1 204 ? 86.804  0.315   59.698  1.00 8.58  ? 204  ALA C N   1 
ATOM   6849  C  CA  . ALA C  1 204 ? 87.556  1.234   58.824  1.00 9.67  ? 204  ALA C CA  1 
ATOM   6850  C  C   . ALA C  1 204 ? 87.621  0.717   57.396  1.00 9.85  ? 204  ALA C C   1 
ATOM   6851  O  O   . ALA C  1 204 ? 87.649  -0.498  57.159  1.00 7.89  ? 204  ALA C O   1 
ATOM   6852  C  CB  . ALA C  1 204 ? 88.971  1.459   59.381  1.00 9.61  ? 204  ALA C CB  1 
ATOM   6853  N  N   . ASN C  1 205 ? 87.581  1.658   56.450  1.00 9.79  ? 205  ASN C N   1 
ATOM   6854  C  CA  . ASN C  1 205 ? 87.822  1.325   55.047  1.00 10.43 ? 205  ASN C CA  1 
ATOM   6855  C  C   . ASN C  1 205 ? 89.087  2.035   54.565  1.00 10.90 ? 205  ASN C C   1 
ATOM   6856  O  O   . ASN C  1 205 ? 89.188  3.254   54.660  1.00 13.20 ? 205  ASN C O   1 
ATOM   6857  C  CB  . ASN C  1 205 ? 86.656  1.793   54.196  1.00 8.95  ? 205  ASN C CB  1 
ATOM   6858  C  CG  . ASN C  1 205 ? 85.351  1.099   54.538  1.00 9.41  ? 205  ASN C CG  1 
ATOM   6859  O  OD1 . ASN C  1 205 ? 84.339  1.761   54.726  1.00 5.55  ? 205  ASN C OD1 1 
ATOM   6860  N  ND2 . ASN C  1 205 ? 85.363  -0.233  54.617  1.00 4.04  ? 205  ASN C ND2 1 
ATOM   6861  N  N   . ALA C  1 206 ? 90.029  1.294   54.005  1.00 10.29 ? 206  ALA C N   1 
ATOM   6862  C  CA  . ALA C  1 206 ? 91.242  1.923   53.453  1.00 10.59 ? 206  ALA C CA  1 
ATOM   6863  C  C   . ALA C  1 206 ? 91.017  2.179   51.951  1.00 10.48 ? 206  ALA C C   1 
ATOM   6864  O  O   . ALA C  1 206 ? 90.252  1.458   51.313  1.00 11.50 ? 206  ALA C O   1 
ATOM   6865  C  CB  . ALA C  1 206 ? 92.453  0.988   53.655  1.00 10.21 ? 206  ALA C CB  1 
ATOM   6866  N  N   . LEU C  1 207 ? 91.668  3.191   51.367  1.00 9.86  ? 207  LEU C N   1 
ATOM   6867  C  CA  . LEU C  1 207 ? 91.716  3.272   49.914  1.00 8.17  ? 207  LEU C CA  1 
ATOM   6868  C  C   . LEU C  1 207 ? 92.430  2.035   49.395  1.00 8.50  ? 207  LEU C C   1 
ATOM   6869  O  O   . LEU C  1 207 ? 93.317  1.537   50.070  1.00 9.13  ? 207  LEU C O   1 
ATOM   6870  C  CB  . LEU C  1 207 ? 92.437  4.539   49.460  1.00 7.81  ? 207  LEU C CB  1 
ATOM   6871  C  CG  . LEU C  1 207 ? 91.610  5.860   49.604  1.00 9.17  ? 207  LEU C CG  1 
ATOM   6872  C  CD1 . LEU C  1 207 ? 91.300  6.196   51.048  1.00 6.56  ? 207  LEU C CD1 1 
ATOM   6873  C  CD2 . LEU C  1 207 ? 92.354  7.043   48.993  1.00 9.35  ? 207  LEU C CD2 1 
ATOM   6874  N  N   . ALA C  1 208 ? 92.074  1.544   48.200  1.00 8.10  ? 208  ALA C N   1 
ATOM   6875  C  CA  . ALA C  1 208 ? 92.862  0.482   47.532  1.00 8.92  ? 208  ALA C CA  1 
ATOM   6876  C  C   . ALA C  1 208 ? 94.335  0.863   47.454  1.00 8.64  ? 208  ALA C C   1 
ATOM   6877  O  O   . ALA C  1 208 ? 94.659  1.952   47.035  1.00 9.17  ? 208  ALA C O   1 
ATOM   6878  C  CB  . ALA C  1 208 ? 92.314  0.212   46.136  1.00 7.10  ? 208  ALA C CB  1 
ATOM   6879  N  N   . SER C  1 209 ? 95.245  -0.025  47.856  1.00 10.48 ? 209  SER C N   1 
ATOM   6880  C  CA  . SER C  1 209 ? 96.664  0.291   47.721  1.00 10.98 ? 209  SER C CA  1 
ATOM   6881  C  C   . SER C  1 209 ? 97.214  -0.089  46.316  1.00 11.24 ? 209  SER C C   1 
ATOM   6882  O  O   . SER C  1 209 ? 98.296  0.320   45.954  1.00 11.61 ? 209  SER C O   1 
ATOM   6883  C  CB  . SER C  1 209 ? 97.496  -0.367  48.819  1.00 11.23 ? 209  SER C CB  1 
ATOM   6884  O  OG  . SER C  1 209 ? 97.286  -1.757  48.814  1.00 11.78 ? 209  SER C OG  1 
ATOM   6885  N  N   . THR C  1 210 ? 96.448  -0.861  45.550  1.00 10.71 ? 210  THR C N   1 
ATOM   6886  C  CA  . THR C  1 210 ? 96.803  -1.219  44.191  1.00 11.21 ? 210  THR C CA  1 
ATOM   6887  C  C   . THR C  1 210 ? 95.970  -0.402  43.180  1.00 11.10 ? 210  THR C C   1 
ATOM   6888  O  O   . THR C  1 210 ? 94.731  -0.316  43.293  1.00 9.67  ? 210  THR C O   1 
ATOM   6889  C  CB  . THR C  1 210 ? 96.567  -2.709  44.022  1.00 11.65 ? 210  THR C CB  1 
ATOM   6890  O  OG1 . THR C  1 210 ? 97.361  -3.424  44.995  1.00 13.52 ? 210  THR C OG1 1 
ATOM   6891  C  CG2 . THR C  1 210 ? 97.108  -3.198  42.675  1.00 12.96 ? 210  THR C CG2 1 
ATOM   6892  N  N   . ALA C  1 211 ? 96.639  0.227   42.211  1.00 11.18 ? 211  ALA C N   1 
ATOM   6893  C  CA  . ALA C  1 211 ? 95.919  0.981   41.190  1.00 11.85 ? 211  ALA C CA  1 
ATOM   6894  C  C   . ALA C  1 211 ? 95.120  0.010   40.312  1.00 11.29 ? 211  ALA C C   1 
ATOM   6895  O  O   . ALA C  1 211 ? 95.552  -1.106  40.043  1.00 10.39 ? 211  ALA C O   1 
ATOM   6896  C  CB  . ALA C  1 211 ? 96.876  1.810   40.370  1.00 12.61 ? 211  ALA C CB  1 
ATOM   6897  N  N   . GLY C  1 212 ? 93.928  0.428   39.907  1.00 11.54 ? 212  GLY C N   1 
ATOM   6898  C  CA  . GLY C  1 212 ? 93.067  -0.421  39.105  1.00 10.53 ? 212  GLY C CA  1 
ATOM   6899  C  C   . GLY C  1 212 ? 92.068  -1.260  39.888  1.00 10.35 ? 212  GLY C C   1 
ATOM   6900  O  O   . GLY C  1 212 ? 91.186  -1.860  39.276  1.00 10.55 ? 212  GLY C O   1 
ATOM   6901  N  N   . ASP C  1 213 ? 92.183  -1.336  41.216  1.00 10.29 ? 213  ASP C N   1 
ATOM   6902  C  CA  . ASP C  1 213 ? 91.191  -2.083  42.008  1.00 10.21 ? 213  ASP C CA  1 
ATOM   6903  C  C   . ASP C  1 213 ? 90.040  -1.185  42.437  1.00 9.25  ? 213  ASP C C   1 
ATOM   6904  O  O   . ASP C  1 213 ? 90.288  -0.071  42.893  1.00 9.77  ? 213  ASP C O   1 
ATOM   6905  C  CB  . ASP C  1 213 ? 91.837  -2.670  43.264  1.00 10.18 ? 213  ASP C CB  1 
ATOM   6906  C  CG  . ASP C  1 213 ? 92.766  -3.823  42.963  1.00 14.99 ? 213  ASP C CG  1 
ATOM   6907  O  OD1 . ASP C  1 213 ? 92.860  -4.227  41.776  1.00 17.23 ? 213  ASP C OD1 1 
ATOM   6908  O  OD2 . ASP C  1 213 ? 93.443  -4.389  43.865  1.00 16.89 ? 213  ASP C OD2 1 
ATOM   6909  N  N   . PRO C  1 214 ? 88.796  -1.656  42.361  1.00 8.76  ? 214  PRO C N   1 
ATOM   6910  C  CA  . PRO C  1 214 ? 87.691  -0.897  42.956  1.00 8.77  ? 214  PRO C CA  1 
ATOM   6911  C  C   . PRO C  1 214 ? 87.846  -0.827  44.475  1.00 8.76  ? 214  PRO C C   1 
ATOM   6912  O  O   . PRO C  1 214 ? 88.524  -1.670  45.096  1.00 10.15 ? 214  PRO C O   1 
ATOM   6913  C  CB  . PRO C  1 214 ? 86.460  -1.722  42.589  1.00 7.53  ? 214  PRO C CB  1 
ATOM   6914  C  CG  . PRO C  1 214 ? 86.960  -3.098  42.446  1.00 6.88  ? 214  PRO C CG  1 
ATOM   6915  C  CD  . PRO C  1 214 ? 88.304  -2.914  41.756  1.00 9.02  ? 214  PRO C CD  1 
ATOM   6916  N  N   . TYR C  1 215 ? 87.234  0.167   45.089  1.00 8.09  ? 215  TYR C N   1 
ATOM   6917  C  CA  . TYR C  1 215 ? 87.124  0.156   46.559  1.00 8.03  ? 215  TYR C CA  1 
ATOM   6918  C  C   . TYR C  1 215 ? 85.984  1.028   46.989  1.00 7.35  ? 215  TYR C C   1 
ATOM   6919  O  O   . TYR C  1 215 ? 85.435  1.748   46.166  1.00 7.25  ? 215  TYR C O   1 
ATOM   6920  C  CB  . TYR C  1 215 ? 88.416  0.628   47.209  1.00 8.12  ? 215  TYR C CB  1 
ATOM   6921  C  CG  . TYR C  1 215 ? 88.909  1.965   46.713  1.00 7.39  ? 215  TYR C CG  1 
ATOM   6922  C  CD1 . TYR C  1 215 ? 89.665  2.059   45.529  1.00 9.09  ? 215  TYR C CD1 1 
ATOM   6923  C  CD2 . TYR C  1 215 ? 88.636  3.140   47.439  1.00 5.68  ? 215  TYR C CD2 1 
ATOM   6924  C  CE1 . TYR C  1 215 ? 90.158  3.313   45.071  1.00 5.53  ? 215  TYR C CE1 1 
ATOM   6925  C  CE2 . TYR C  1 215 ? 89.138  4.380   47.018  1.00 5.33  ? 215  TYR C CE2 1 
ATOM   6926  C  CZ  . TYR C  1 215 ? 89.879  4.463   45.826  1.00 6.70  ? 215  TYR C CZ  1 
ATOM   6927  O  OH  . TYR C  1 215 ? 90.334  5.689   45.401  1.00 6.59  ? 215  TYR C OH  1 
ATOM   6928  N  N   . PHE C  1 216 ? 85.648  0.969   48.273  1.00 7.67  ? 216  PHE C N   1 
ATOM   6929  C  CA  . PHE C  1 216 ? 84.442  1.592   48.779  1.00 8.75  ? 216  PHE C CA  1 
ATOM   6930  C  C   . PHE C  1 216 ? 84.714  2.158   50.154  1.00 8.77  ? 216  PHE C C   1 
ATOM   6931  O  O   . PHE C  1 216 ? 85.390  1.528   50.955  1.00 9.95  ? 216  PHE C O   1 
ATOM   6932  C  CB  . PHE C  1 216 ? 83.302  0.569   48.894  1.00 8.80  ? 216  PHE C CB  1 
ATOM   6933  C  CG  . PHE C  1 216 ? 83.108  -0.269  47.667  1.00 9.99  ? 216  PHE C CG  1 
ATOM   6934  C  CD1 . PHE C  1 216 ? 83.855  -1.422  47.485  1.00 13.08 ? 216  PHE C CD1 1 
ATOM   6935  C  CD2 . PHE C  1 216 ? 82.116  0.065   46.724  1.00 13.90 ? 216  PHE C CD2 1 
ATOM   6936  C  CE1 . PHE C  1 216 ? 83.676  -2.214  46.356  1.00 13.25 ? 216  PHE C CE1 1 
ATOM   6937  C  CE2 . PHE C  1 216 ? 81.893  -0.768  45.609  1.00 11.72 ? 216  PHE C CE2 1 
ATOM   6938  C  CZ  . PHE C  1 216 ? 82.682  -1.881  45.424  1.00 14.06 ? 216  PHE C CZ  1 
ATOM   6939  N  N   . ILE C  1 217 ? 84.210  3.353   50.416  1.00 6.94  ? 217  ILE C N   1 
ATOM   6940  C  CA  . ILE C  1 217 ? 84.411  3.933   51.730  1.00 7.25  ? 217  ILE C CA  1 
ATOM   6941  C  C   . ILE C  1 217 ? 83.045  4.338   52.276  1.00 7.22  ? 217  ILE C C   1 
ATOM   6942  O  O   . ILE C  1 217 ? 82.328  5.174   51.668  1.00 9.18  ? 217  ILE C O   1 
ATOM   6943  C  CB  . ILE C  1 217 ? 85.356  5.138   51.683  1.00 7.19  ? 217  ILE C CB  1 
ATOM   6944  C  CG1 . ILE C  1 217 ? 86.754  4.770   51.193  1.00 8.87  ? 217  ILE C CG1 1 
ATOM   6945  C  CG2 . ILE C  1 217 ? 85.372  5.856   53.069  1.00 6.15  ? 217  ILE C CG2 1 
ATOM   6946  C  CD1 . ILE C  1 217 ? 87.432  5.974   50.581  1.00 11.05 ? 217  ILE C CD1 1 
ATOM   6947  N  N   . ALA C  1 218 ? 82.685  3.753   53.426  1.00 8.26  ? 218  ALA C N   1 
ATOM   6948  C  CA  . ALA C  1 218 ? 81.410  4.095   54.073  1.00 9.14  ? 218  ALA C CA  1 
ATOM   6949  C  C   . ALA C  1 218 ? 81.573  5.429   54.804  1.00 9.31  ? 218  ALA C C   1 
ATOM   6950  O  O   . ALA C  1 218 ? 82.668  5.743   55.262  1.00 9.67  ? 218  ALA C O   1 
ATOM   6951  C  CB  . ALA C  1 218 ? 81.014  3.003   55.013  1.00 7.20  ? 218  ALA C CB  1 
ATOM   6952  N  N   . ASN C  1 219 ? 80.500  6.197   54.872  1.00 8.24  ? 219  ASN C N   1 
ATOM   6953  C  CA  . ASN C  1 219 ? 80.499  7.582   55.390  1.00 10.27 ? 219  ASN C CA  1 
ATOM   6954  C  C   . ASN C  1 219 ? 81.166  7.624   56.762  1.00 9.28  ? 219  ASN C C   1 
ATOM   6955  O  O   . ASN C  1 219 ? 80.638  7.071   57.678  1.00 9.99  ? 219  ASN C O   1 
ATOM   6956  C  CB  . ASN C  1 219 ? 79.050  8.076   55.547  1.00 9.18  ? 219  ASN C CB  1 
ATOM   6957  C  CG  . ASN C  1 219 ? 78.973  9.587   55.860  1.00 13.46 ? 219  ASN C CG  1 
ATOM   6958  O  OD1 . ASN C  1 219 ? 79.992  10.282  55.958  1.00 13.67 ? 219  ASN C OD1 1 
ATOM   6959  N  ND2 . ASN C  1 219 ? 77.770  10.100  55.953  1.00 20.19 ? 219  ASN C ND2 1 
ATOM   6960  N  N   . GLY C  1 220 ? 82.316  8.276   56.891  1.00 8.86  ? 220  GLY C N   1 
ATOM   6961  C  CA  . GLY C  1 220 ? 82.913  8.403   58.199  1.00 8.99  ? 220  GLY C CA  1 
ATOM   6962  C  C   . GLY C  1 220 ? 83.971  7.367   58.536  1.00 9.43  ? 220  GLY C C   1 
ATOM   6963  O  O   . GLY C  1 220 ? 84.717  7.549   59.525  1.00 10.21 ? 220  GLY C O   1 
ATOM   6964  N  N   . TRP C  1 221 ? 84.072  6.318   57.726  1.00 6.85  ? 221  TRP C N   1 
ATOM   6965  C  CA  . TRP C  1 221 ? 84.913  5.177   58.076  1.00 7.67  ? 221  TRP C CA  1 
ATOM   6966  C  C   . TRP C  1 221 ? 86.279  5.162   57.346  1.00 6.71  ? 221  TRP C C   1 
ATOM   6967  O  O   . TRP C  1 221 ? 87.069  4.252   57.544  1.00 5.80  ? 221  TRP C O   1 
ATOM   6968  C  CB  . TRP C  1 221 ? 84.134  3.906   57.730  1.00 8.23  ? 221  TRP C CB  1 
ATOM   6969  C  CG  . TRP C  1 221 ? 82.928  3.594   58.662  1.00 7.70  ? 221  TRP C CG  1 
ATOM   6970  C  CD1 . TRP C  1 221 ? 81.575  3.758   58.384  1.00 10.70 ? 221  TRP C CD1 1 
ATOM   6971  C  CD2 . TRP C  1 221 ? 83.002  3.081   59.963  1.00 6.51  ? 221  TRP C CD2 1 
ATOM   6972  N  NE1 . TRP C  1 221 ? 80.824  3.340   59.452  1.00 9.51  ? 221  TRP C NE1 1 
ATOM   6973  C  CE2 . TRP C  1 221 ? 81.673  2.931   60.444  1.00 6.54  ? 221  TRP C CE2 1 
ATOM   6974  C  CE3 . TRP C  1 221 ? 84.068  2.682   60.791  1.00 7.77  ? 221  TRP C CE3 1 
ATOM   6975  C  CZ2 . TRP C  1 221 ? 81.386  2.425   61.717  1.00 7.41  ? 221  TRP C CZ2 1 
ATOM   6976  C  CZ3 . TRP C  1 221 ? 83.774  2.189   62.063  1.00 6.88  ? 221  TRP C CZ3 1 
ATOM   6977  C  CH2 . TRP C  1 221 ? 82.453  2.026   62.493  1.00 4.43  ? 221  TRP C CH2 1 
ATOM   6978  N  N   . GLY C  1 222 ? 86.536  6.128   56.464  1.00 5.99  ? 222  GLY C N   1 
ATOM   6979  C  CA  . GLY C  1 222 ? 87.833  6.204   55.773  1.00 7.21  ? 222  GLY C CA  1 
ATOM   6980  C  C   . GLY C  1 222 ? 88.902  6.921   56.591  1.00 7.69  ? 222  GLY C C   1 
ATOM   6981  O  O   . GLY C  1 222 ? 88.576  7.356   57.695  1.00 7.41  ? 222  GLY C O   1 
ATOM   6982  N  N   . PRO C  1 223 ? 90.160  7.013   56.101  1.00 8.11  ? 223  PRO C N   1 
ATOM   6983  C  CA  . PRO C  1 223 ? 91.186  7.808   56.785  1.00 8.03  ? 223  PRO C CA  1 
ATOM   6984  C  C   . PRO C  1 223 ? 90.874  9.289   56.735  1.00 7.42  ? 223  PRO C C   1 
ATOM   6985  O  O   . PRO C  1 223 ? 90.341  9.775   55.737  1.00 8.84  ? 223  PRO C O   1 
ATOM   6986  C  CB  . PRO C  1 223 ? 92.477  7.553   55.979  1.00 7.45  ? 223  PRO C CB  1 
ATOM   6987  C  CG  . PRO C  1 223 ? 92.049  7.003   54.685  1.00 10.06 ? 223  PRO C CG  1 
ATOM   6988  C  CD  . PRO C  1 223 ? 90.675  6.388   54.869  1.00 8.17  ? 223  PRO C CD  1 
ATOM   6989  N  N   . LYS C  1 224 ? 91.198  10.000  57.799  1.00 6.69  ? 224  LYS C N   1 
ATOM   6990  C  CA  . LYS C  1 224 ? 90.847  11.419  57.830  1.00 8.18  ? 224  LYS C CA  1 
ATOM   6991  C  C   . LYS C  1 224 ? 92.111  12.167  58.277  1.00 7.76  ? 224  LYS C C   1 
ATOM   6992  O  O   . LYS C  1 224 ? 93.000  11.578  58.913  1.00 7.31  ? 224  LYS C O   1 
ATOM   6993  C  CB  . LYS C  1 224 ? 89.669  11.697  58.802  1.00 7.32  ? 224  LYS C CB  1 
ATOM   6994  C  CG  . LYS C  1 224 ? 88.254  11.127  58.362  1.00 7.85  ? 224  LYS C CG  1 
ATOM   6995  C  CD  . LYS C  1 224 ? 87.251  11.075  59.563  1.00 6.10  ? 224  LYS C CD  1 
ATOM   6996  C  CE  . LYS C  1 224 ? 87.470  9.825   60.492  1.00 10.79 ? 224  LYS C CE  1 
ATOM   6997  N  NZ  . LYS C  1 224 ? 87.182  8.508   59.856  1.00 11.40 ? 224  LYS C NZ  1 
ATOM   6998  N  N   . TYR C  1 225 ? 92.172  13.459  57.942  1.00 9.03  ? 225  TYR C N   1 
ATOM   6999  C  CA  . TYR C  1 225 ? 93.266  14.332  58.351  1.00 8.62  ? 225  TYR C CA  1 
ATOM   7000  C  C   . TYR C  1 225 ? 92.683  15.615  58.852  1.00 9.19  ? 225  TYR C C   1 
ATOM   7001  O  O   . TYR C  1 225 ? 91.772  16.147  58.224  1.00 8.60  ? 225  TYR C O   1 
ATOM   7002  C  CB  . TYR C  1 225 ? 94.183  14.611  57.166  1.00 10.14 ? 225  TYR C CB  1 
ATOM   7003  C  CG  . TYR C  1 225 ? 94.816  13.324  56.636  1.00 11.72 ? 225  TYR C CG  1 
ATOM   7004  C  CD1 . TYR C  1 225 ? 94.115  12.502  55.736  1.00 14.29 ? 225  TYR C CD1 1 
ATOM   7005  C  CD2 . TYR C  1 225 ? 96.073  12.907  57.075  1.00 13.87 ? 225  TYR C CD2 1 
ATOM   7006  C  CE1 . TYR C  1 225 ? 94.660  11.323  55.293  1.00 15.49 ? 225  TYR C CE1 1 
ATOM   7007  C  CE2 . TYR C  1 225 ? 96.631  11.721  56.616  1.00 17.63 ? 225  TYR C CE2 1 
ATOM   7008  C  CZ  . TYR C  1 225 ? 95.901  10.936  55.730  1.00 17.41 ? 225  TYR C CZ  1 
ATOM   7009  O  OH  . TYR C  1 225 ? 96.438  9.750   55.255  1.00 21.91 ? 225  TYR C OH  1 
ATOM   7010  N  N   . LEU C  1 226 ? 93.211  16.123  59.970  1.00 9.11  ? 226  LEU C N   1 
ATOM   7011  C  CA  . LEU C  1 226 ? 92.737  17.372  60.551  1.00 8.45  ? 226  LEU C CA  1 
ATOM   7012  C  C   . LEU C  1 226 ? 93.737  18.481  60.177  1.00 9.33  ? 226  LEU C C   1 
ATOM   7013  O  O   . LEU C  1 226 ? 94.918  18.394  60.523  1.00 8.56  ? 226  LEU C O   1 
ATOM   7014  C  CB  . LEU C  1 226 ? 92.703  17.278  62.090  1.00 8.53  ? 226  LEU C CB  1 
ATOM   7015  C  CG  . LEU C  1 226 ? 92.371  18.626  62.766  1.00 7.91  ? 226  LEU C CG  1 
ATOM   7016  C  CD1 . LEU C  1 226 ? 90.865  18.956  62.529  1.00 9.18  ? 226  LEU C CD1 1 
ATOM   7017  C  CD2 . LEU C  1 226 ? 92.740  18.588  64.272  1.00 4.75  ? 226  LEU C CD2 1 
ATOM   7018  N  N   . ASN C  1 227 ? 93.260  19.505  59.495  1.00 8.42  ? 227  ASN C N   1 
ATOM   7019  C  CA  . ASN C  1 227 ? 94.090  20.686  59.271  1.00 8.54  ? 227  ASN C CA  1 
ATOM   7020  C  C   . ASN C  1 227 ? 93.643  21.810  60.211  1.00 8.71  ? 227  ASN C C   1 
ATOM   7021  O  O   . ASN C  1 227 ? 92.444  22.187  60.214  1.00 8.61  ? 227  ASN C O   1 
ATOM   7022  C  CB  . ASN C  1 227 ? 94.026  21.117  57.812  1.00 8.07  ? 227  ASN C CB  1 
ATOM   7023  C  CG  . ASN C  1 227 ? 94.906  22.332  57.554  1.00 9.54  ? 227  ASN C CG  1 
ATOM   7024  O  OD1 . ASN C  1 227 ? 94.589  23.436  57.971  1.00 6.39  ? 227  ASN C OD1 1 
ATOM   7025  N  ND2 . ASN C  1 227 ? 96.021  22.115  56.914  1.00 5.78  ? 227  ASN C ND2 1 
ATOM   7026  N  N   . SER C  1 228 ? 94.592  22.360  60.973  1.00 7.62  ? 228  SER C N   1 
ATOM   7027  C  CA  . SER C  1 228 ? 94.288  23.410  61.942  1.00 7.82  ? 228  SER C CA  1 
ATOM   7028  C  C   . SER C  1 228 ? 94.808  24.812  61.546  1.00 7.61  ? 228  SER C C   1 
ATOM   7029  O  O   . SER C  1 228 ? 94.916  25.728  62.390  1.00 6.53  ? 228  SER C O   1 
ATOM   7030  C  CB  . SER C  1 228 ? 94.865  22.982  63.292  1.00 9.32  ? 228  SER C CB  1 
ATOM   7031  O  OG  . SER C  1 228 ? 94.425  21.639  63.550  1.00 10.06 ? 228  SER C OG  1 
ATOM   7032  N  N   . GLN C  1 229 ? 95.175  24.975  60.284  1.00 8.06  ? 229  GLN C N   1 
ATOM   7033  C  CA  . GLN C  1 229 ? 95.881  26.187  59.881  1.00 8.39  ? 229  GLN C CA  1 
ATOM   7034  C  C   . GLN C  1 229 ? 94.939  27.395  59.745  1.00 8.57  ? 229  GLN C C   1 
ATOM   7035  O  O   . GLN C  1 229 ? 95.359  28.545  59.955  1.00 8.63  ? 229  GLN C O   1 
ATOM   7036  C  CB  . GLN C  1 229 ? 96.638  25.980  58.564  1.00 8.53  ? 229  GLN C CB  1 
ATOM   7037  C  CG  . GLN C  1 229 ? 97.783  24.987  58.602  1.00 10.18 ? 229  GLN C CG  1 
ATOM   7038  C  CD  . GLN C  1 229 ? 98.450  24.843  57.255  1.00 10.70 ? 229  GLN C CD  1 
ATOM   7039  O  OE1 . GLN C  1 229 ? 98.011  24.060  56.386  1.00 11.21 ? 229  GLN C OE1 1 
ATOM   7040  N  NE2 . GLN C  1 229 ? 99.504  25.613  57.057  1.00 11.92 ? 229  GLN C NE2 1 
ATOM   7041  N  N   . TYR C  1 230 ? 93.696  27.155  59.355  1.00 8.29  ? 230  TYR C N   1 
ATOM   7042  C  CA  . TYR C  1 230 ? 92.718  28.238  59.050  1.00 9.60  ? 230  TYR C CA  1 
ATOM   7043  C  C   . TYR C  1 230 ? 91.343  27.890  59.618  1.00 9.70  ? 230  TYR C C   1 
ATOM   7044  O  O   . TYR C  1 230 ? 90.374  27.683  58.875  1.00 11.19 ? 230  TYR C O   1 
ATOM   7045  C  CB  . TYR C  1 230 ? 92.560  28.373  57.539  1.00 10.51 ? 230  TYR C CB  1 
ATOM   7046  C  CG  . TYR C  1 230 ? 93.853  28.227  56.783  1.00 12.24 ? 230  TYR C CG  1 
ATOM   7047  C  CD1 . TYR C  1 230 ? 94.767  29.271  56.736  1.00 12.97 ? 230  TYR C CD1 1 
ATOM   7048  C  CD2 . TYR C  1 230 ? 94.161  27.049  56.103  1.00 14.95 ? 230  TYR C CD2 1 
ATOM   7049  C  CE1 . TYR C  1 230 ? 95.950  29.159  56.013  1.00 16.71 ? 230  TYR C CE1 1 
ATOM   7050  C  CE2 . TYR C  1 230 ? 95.366  26.930  55.397  1.00 14.05 ? 230  TYR C CE2 1 
ATOM   7051  C  CZ  . TYR C  1 230 ? 96.228  27.975  55.346  1.00 15.82 ? 230  TYR C CZ  1 
ATOM   7052  O  OH  . TYR C  1 230 ? 97.431  27.830  54.658  1.00 21.84 ? 230  TYR C OH  1 
ATOM   7053  N  N   . GLY C  1 231 ? 91.255  27.783  60.933  1.00 9.56  ? 231  GLY C N   1 
ATOM   7054  C  CA  . GLY C  1 231 ? 90.112  27.095  61.517  1.00 8.87  ? 231  GLY C CA  1 
ATOM   7055  C  C   . GLY C  1 231 ? 90.374  25.602  61.381  1.00 9.16  ? 231  GLY C C   1 
ATOM   7056  O  O   . GLY C  1 231 ? 91.483  25.203  60.994  1.00 10.80 ? 231  GLY C O   1 
ATOM   7057  N  N   . TYR C  1 232 ? 89.384  24.777  61.681  1.00 8.93  ? 232  TYR C N   1 
ATOM   7058  C  CA  . TYR C  1 232 ? 89.563  23.332  61.554  1.00 8.29  ? 232  TYR C CA  1 
ATOM   7059  C  C   . TYR C  1 232 ? 88.930  22.827  60.275  1.00 8.94  ? 232  TYR C C   1 
ATOM   7060  O  O   . TYR C  1 232 ? 87.791  23.197  59.934  1.00 7.18  ? 232  TYR C O   1 
ATOM   7061  C  CB  . TYR C  1 232 ? 88.934  22.602  62.716  1.00 7.97  ? 232  TYR C CB  1 
ATOM   7062  C  CG  . TYR C  1 232 ? 89.644  22.769  64.034  1.00 5.61  ? 232  TYR C CG  1 
ATOM   7063  C  CD1 . TYR C  1 232 ? 91.001  22.382  64.203  1.00 6.44  ? 232  TYR C CD1 1 
ATOM   7064  C  CD2 . TYR C  1 232 ? 88.967  23.294  65.127  1.00 7.71  ? 232  TYR C CD2 1 
ATOM   7065  C  CE1 . TYR C  1 232 ? 91.649  22.519  65.442  1.00 3.22  ? 232  TYR C CE1 1 
ATOM   7066  C  CE2 . TYR C  1 232 ? 89.608  23.440  66.379  1.00 9.54  ? 232  TYR C CE2 1 
ATOM   7067  C  CZ  . TYR C  1 232 ? 90.953  23.054  66.521  1.00 8.91  ? 232  TYR C CZ  1 
ATOM   7068  O  OH  . TYR C  1 232 ? 91.572  23.197  67.744  1.00 2.10  ? 232  TYR C OH  1 
ATOM   7069  N  N   . GLN C  1 233 ? 89.683  22.002  59.557  1.00 8.46  ? 233  GLN C N   1 
ATOM   7070  C  CA  . GLN C  1 233 ? 89.123  21.348  58.389  1.00 8.67  ? 233  GLN C CA  1 
ATOM   7071  C  C   . GLN C  1 233 ? 89.527  19.900  58.447  1.00 9.43  ? 233  GLN C C   1 
ATOM   7072  O  O   . GLN C  1 233 ? 90.691  19.582  58.784  1.00 10.26 ? 233  GLN C O   1 
ATOM   7073  C  CB  . GLN C  1 233 ? 89.650  22.038  57.125  1.00 9.66  ? 233  GLN C CB  1 
ATOM   7074  C  CG  . GLN C  1 233 ? 89.168  23.489  57.000  1.00 9.96  ? 233  GLN C CG  1 
ATOM   7075  C  CD  . GLN C  1 233 ? 89.626  24.179  55.762  1.00 10.11 ? 233  GLN C CD  1 
ATOM   7076  O  OE1 . GLN C  1 233 ? 90.585  25.015  55.777  1.00 11.41 ? 233  GLN C OE1 1 
ATOM   7077  N  NE2 . GLN C  1 233 ? 88.931  23.901  54.679  1.00 7.47  ? 233  GLN C NE2 1 
ATOM   7078  N  N   . ILE C  1 234 ? 88.582  19.006  58.150  1.00 8.71  ? 234  ILE C N   1 
ATOM   7079  C  CA  . ILE C  1 234 ? 88.879  17.577  58.169  1.00 6.77  ? 234  ILE C CA  1 
ATOM   7080  C  C   . ILE C  1 234 ? 88.780  17.044  56.759  1.00 7.34  ? 234  ILE C C   1 
ATOM   7081  O  O   . ILE C  1 234 ? 87.737  17.168  56.118  1.00 6.22  ? 234  ILE C O   1 
ATOM   7082  C  CB  . ILE C  1 234 ? 87.943  16.820  59.122  1.00 7.85  ? 234  ILE C CB  1 
ATOM   7083  C  CG1 . ILE C  1 234 ? 88.115  17.311  60.559  1.00 7.20  ? 234  ILE C CG1 1 
ATOM   7084  C  CG2 . ILE C  1 234 ? 88.175  15.263  59.047  1.00 6.51  ? 234  ILE C CG2 1 
ATOM   7085  C  CD1 . ILE C  1 234 ? 87.127  16.669  61.529  1.00 5.72  ? 234  ILE C CD1 1 
ATOM   7086  N  N   . VAL C  1 235 ? 89.857  16.458  56.249  1.00 6.67  ? 235  VAL C N   1 
ATOM   7087  C  CA  . VAL C  1 235 ? 89.813  15.965  54.873  1.00 6.75  ? 235  VAL C CA  1 
ATOM   7088  C  C   . VAL C  1 235 ? 89.698  14.453  54.943  1.00 7.80  ? 235  VAL C C   1 
ATOM   7089  O  O   . VAL C  1 235 ? 90.487  13.822  55.631  1.00 8.25  ? 235  VAL C O   1 
ATOM   7090  C  CB  . VAL C  1 235 ? 91.087  16.320  54.038  1.00 8.27  ? 235  VAL C CB  1 
ATOM   7091  C  CG1 . VAL C  1 235 ? 90.965  15.698  52.614  1.00 5.13  ? 235  VAL C CG1 1 
ATOM   7092  C  CG2 . VAL C  1 235 ? 91.345  17.873  53.987  1.00 5.44  ? 235  VAL C CG2 1 
ATOM   7093  N  N   . ALA C  1 236 ? 88.707  13.895  54.241  1.00 8.34  ? 236  ALA C N   1 
ATOM   7094  C  CA  . ALA C  1 236 ? 88.597  12.440  54.070  1.00 8.03  ? 236  ALA C CA  1 
ATOM   7095  C  C   . ALA C  1 236 ? 88.900  12.079  52.606  1.00 7.49  ? 236  ALA C C   1 
ATOM   7096  O  O   . ALA C  1 236 ? 88.017  12.160  51.766  1.00 8.74  ? 236  ALA C O   1 
ATOM   7097  C  CB  . ALA C  1 236 ? 87.158  11.967  54.407  1.00 7.21  ? 236  ALA C CB  1 
ATOM   7098  N  N   . PRO C  1 237 ? 90.119  11.665  52.298  1.00 7.82  ? 237  PRO C N   1 
ATOM   7099  C  CA  . PRO C  1 237 ? 90.462  11.343  50.910  1.00 7.83  ? 237  PRO C CA  1 
ATOM   7100  C  C   . PRO C  1 237 ? 89.662  10.183  50.384  1.00 8.44  ? 237  PRO C C   1 
ATOM   7101  O  O   . PRO C  1 237 ? 89.428  9.249   51.124  1.00 7.66  ? 237  PRO C O   1 
ATOM   7102  C  CB  . PRO C  1 237 ? 91.938  10.970  50.980  1.00 8.14  ? 237  PRO C CB  1 
ATOM   7103  C  CG  . PRO C  1 237 ? 92.435  11.444  52.292  1.00 7.87  ? 237  PRO C CG  1 
ATOM   7104  C  CD  . PRO C  1 237 ? 91.259  11.509  53.222  1.00 5.85  ? 237  PRO C CD  1 
ATOM   7105  N  N   . PHE C  1 238 ? 89.280  10.252  49.109  1.00 9.60  ? 238  PHE C N   1 
ATOM   7106  C  CA  . PHE C  1 238 ? 88.590  9.173   48.392  1.00 9.31  ? 238  PHE C CA  1 
ATOM   7107  C  C   . PHE C  1 238 ? 89.499  8.735   47.251  1.00 8.78  ? 238  PHE C C   1 
ATOM   7108  O  O   . PHE C  1 238 ? 89.590  7.546   46.955  1.00 9.98  ? 238  PHE C O   1 
ATOM   7109  C  CB  . PHE C  1 238 ? 87.301  9.746   47.773  1.00 9.30  ? 238  PHE C CB  1 
ATOM   7110  C  CG  . PHE C  1 238 ? 86.147  9.977   48.774  1.00 10.85 ? 238  PHE C CG  1 
ATOM   7111  C  CD1 . PHE C  1 238 ? 86.148  9.404   50.070  1.00 9.10  ? 238  PHE C CD1 1 
ATOM   7112  C  CD2 . PHE C  1 238 ? 85.054  10.749  48.393  1.00 10.27 ? 238  PHE C CD2 1 
ATOM   7113  C  CE1 . PHE C  1 238 ? 85.085  9.617   50.965  1.00 8.59  ? 238  PHE C CE1 1 
ATOM   7114  C  CE2 . PHE C  1 238 ? 83.978  10.979  49.284  1.00 10.17 ? 238  PHE C CE2 1 
ATOM   7115  C  CZ  . PHE C  1 238 ? 83.985  10.421  50.554  1.00 7.11  ? 238  PHE C CZ  1 
ATOM   7116  N  N   . VAL C  1 239 ? 90.141  9.692   46.563  1.00 7.57  ? 239  VAL C N   1 
ATOM   7117  C  CA  . VAL C  1 239 ? 91.131  9.340   45.505  1.00 7.29  ? 239  VAL C CA  1 
ATOM   7118  C  C   . VAL C  1 239 ? 92.382  10.176  45.729  1.00 8.22  ? 239  VAL C C   1 
ATOM   7119  O  O   . VAL C  1 239 ? 92.289  11.389  45.884  1.00 6.03  ? 239  VAL C O   1 
ATOM   7120  C  CB  . VAL C  1 239 ? 90.550  9.599   44.082  1.00 7.33  ? 239  VAL C CB  1 
ATOM   7121  C  CG1 . VAL C  1 239 ? 91.646  9.475   42.964  1.00 8.07  ? 239  VAL C CG1 1 
ATOM   7122  C  CG2 . VAL C  1 239 ? 89.355  8.647   43.794  1.00 6.54  ? 239  VAL C CG2 1 
ATOM   7123  N  N   . THR C  1 240 ? 93.541  9.515   45.817  1.00 8.50  ? 240  THR C N   1 
ATOM   7124  C  CA  . THR C  1 240 ? 94.817  10.220  45.810  1.00 10.40 ? 240  THR C CA  1 
ATOM   7125  C  C   . THR C  1 240 ? 95.679  9.792   44.601  1.00 10.67 ? 240  THR C C   1 
ATOM   7126  O  O   . THR C  1 240 ? 95.241  8.962   43.784  1.00 9.68  ? 240  THR C O   1 
ATOM   7127  C  CB  . THR C  1 240 ? 95.611  9.865   47.091  1.00 10.94 ? 240  THR C CB  1 
ATOM   7128  O  OG1 . THR C  1 240 ? 96.022  8.494   47.019  1.00 10.88 ? 240  THR C OG1 1 
ATOM   7129  C  CG2 . THR C  1 240 ? 94.727  9.985   48.345  1.00 9.69  ? 240  THR C CG2 1 
ATOM   7130  N  N   . ALA C  1 241 ? 96.916  10.295  44.524  1.00 11.38 ? 241  ALA C N   1 
ATOM   7131  C  CA  . ALA C  1 241 ? 97.783  9.970   43.392  1.00 12.00 ? 241  ALA C CA  1 
ATOM   7132  C  C   . ALA C  1 241 ? 97.942  8.461   43.244  1.00 12.22 ? 241  ALA C C   1 
ATOM   7133  O  O   . ALA C  1 241 ? 98.066  7.947   42.120  1.00 12.99 ? 241  ALA C O   1 
ATOM   7134  C  CB  . ALA C  1 241 ? 99.153  10.627  43.535  1.00 12.70 ? 241  ALA C CB  1 
ATOM   7135  N  N   . THR C  1 242 ? 97.962  7.741   44.364  1.00 12.08 ? 242  THR C N   1 
ATOM   7136  C  CA  . THR C  1 242 ? 98.144  6.297   44.331  1.00 11.84 ? 242  THR C CA  1 
ATOM   7137  C  C   . THR C  1 242 ? 97.124  5.646   43.411  1.00 11.40 ? 242  THR C C   1 
ATOM   7138  O  O   . THR C  1 242 ? 97.439  4.690   42.691  1.00 10.27 ? 242  THR C O   1 
ATOM   7139  C  CB  . THR C  1 242 ? 97.939  5.738   45.739  1.00 13.00 ? 242  THR C CB  1 
ATOM   7140  O  OG1 . THR C  1 242 ? 98.992  6.225   46.580  1.00 12.42 ? 242  THR C OG1 1 
ATOM   7141  C  CG2 . THR C  1 242 ? 98.041  4.177   45.787  1.00 13.19 ? 242  THR C CG2 1 
ATOM   7142  N  N   . GLN C  1 243 ? 95.895  6.157   43.473  1.00 9.30  ? 243  GLN C N   1 
ATOM   7143  C  CA  . GLN C  1 243 ? 94.793  5.544   42.774  1.00 9.88  ? 243  GLN C CA  1 
ATOM   7144  C  C   . GLN C  1 243 ? 94.587  6.184   41.417  1.00 9.48  ? 243  GLN C C   1 
ATOM   7145  O  O   . GLN C  1 243 ? 94.341  5.475   40.445  1.00 9.60  ? 243  GLN C O   1 
ATOM   7146  C  CB  . GLN C  1 243 ? 93.514  5.596   43.613  1.00 10.61 ? 243  GLN C CB  1 
ATOM   7147  C  CG  . GLN C  1 243 ? 93.617  4.729   44.876  1.00 9.42  ? 243  GLN C CG  1 
ATOM   7148  C  CD  . GLN C  1 243 ? 94.269  5.466   46.041  1.00 11.13 ? 243  GLN C CD  1 
ATOM   7149  O  OE1 . GLN C  1 243 ? 94.232  6.692   46.099  1.00 7.74  ? 243  GLN C OE1 1 
ATOM   7150  N  NE2 . GLN C  1 243 ? 94.834  4.707   46.994  1.00 5.76  ? 243  GLN C NE2 1 
ATOM   7151  N  N   . ALA C  1 244 ? 94.705  7.511   41.353  1.00 9.02  ? 244  ALA C N   1 
ATOM   7152  C  CA  . ALA C  1 244 ? 94.479  8.269   40.102  1.00 9.58  ? 244  ALA C CA  1 
ATOM   7153  C  C   . ALA C  1 244 ? 95.511  7.970   39.021  1.00 9.68  ? 244  ALA C C   1 
ATOM   7154  O  O   . ALA C  1 244 ? 95.173  7.849   37.825  1.00 8.84  ? 244  ALA C O   1 
ATOM   7155  C  CB  . ALA C  1 244 ? 94.472  9.776   40.404  1.00 9.48  ? 244  ALA C CB  1 
ATOM   7156  N  N   . GLN C  1 245 ? 96.769  7.845   39.451  1.00 9.35  ? 245  GLN C N   1 
ATOM   7157  C  CA  . GLN C  1 245 ? 97.932  7.760   38.564  1.00 10.29 ? 245  GLN C CA  1 
ATOM   7158  C  C   . GLN C  1 245 ? 97.841  8.841   37.498  1.00 9.47  ? 245  GLN C C   1 
ATOM   7159  O  O   . GLN C  1 245 ? 97.561  9.981   37.832  1.00 10.33 ? 245  GLN C O   1 
ATOM   7160  C  CB  . GLN C  1 245 ? 98.043  6.381   37.934  1.00 10.04 ? 245  GLN C CB  1 
ATOM   7161  C  CG  . GLN C  1 245 ? 98.110  5.286   38.941  1.00 12.93 ? 245  GLN C CG  1 
ATOM   7162  C  CD  . GLN C  1 245 ? 98.148  3.954   38.273  1.00 17.63 ? 245  GLN C CD  1 
ATOM   7163  O  OE1 . GLN C  1 245 ? 97.155  3.549   37.635  1.00 18.74 ? 245  GLN C OE1 1 
ATOM   7164  N  NE2 . GLN C  1 245 ? 99.295  3.267   38.371  1.00 17.87 ? 245  GLN C NE2 1 
ATOM   7165  N  N   . ASP C  1 246 ? 98.032  8.474   36.233  1.00 9.43  ? 246  ASP C N   1 
ATOM   7166  C  CA  . ASP C  1 246 ? 98.028  9.429   35.124  1.00 9.65  ? 246  ASP C CA  1 
ATOM   7167  C  C   . ASP C  1 246 ? 96.700  10.158  34.913  1.00 9.41  ? 246  ASP C C   1 
ATOM   7168  O  O   . ASP C  1 246 ? 96.671  11.136  34.166  1.00 8.62  ? 246  ASP C O   1 
ATOM   7169  C  CB  . ASP C  1 246 ? 98.436  8.719   33.840  1.00 10.21 ? 246  ASP C CB  1 
ATOM   7170  C  CG  . ASP C  1 246 ? 97.548  7.514   33.543  1.00 14.55 ? 246  ASP C CG  1 
ATOM   7171  O  OD1 . ASP C  1 246 ? 97.627  6.454   34.280  1.00 16.55 ? 246  ASP C OD1 1 
ATOM   7172  O  OD2 . ASP C  1 246 ? 96.745  7.544   32.588  1.00 11.21 ? 246  ASP C OD2 1 
ATOM   7173  N  N   . THR C  1 247 ? 95.596  9.688   35.512  1.00 7.98  ? 247  THR C N   1 
ATOM   7174  C  CA  . THR C  1 247 ? 94.362  10.505  35.480  1.00 8.62  ? 247  THR C CA  1 
ATOM   7175  C  C   . THR C  1 247 ? 94.480  11.766  36.325  1.00 9.75  ? 247  THR C C   1 
ATOM   7176  O  O   . THR C  1 247 ? 93.651  12.673  36.171  1.00 8.18  ? 247  THR C O   1 
ATOM   7177  C  CB  . THR C  1 247 ? 93.042  9.788   35.820  1.00 7.80  ? 247  THR C CB  1 
ATOM   7178  O  OG1 . THR C  1 247 ? 93.084  9.276   37.165  1.00 7.34  ? 247  THR C OG1 1 
ATOM   7179  C  CG2 . THR C  1 247 ? 92.750  8.619   34.863  1.00 7.78  ? 247  THR C CG2 1 
ATOM   7180  N  N   . ASN C  1 248 ? 95.517  11.840  37.178  1.00 9.94  ? 248  ASN C N   1 
ATOM   7181  C  CA  . ASN C  1 248 ? 95.990  13.131  37.669  1.00 10.22 ? 248  ASN C CA  1 
ATOM   7182  C  C   . ASN C  1 248 ? 94.872  13.967  38.278  1.00 9.74  ? 248  ASN C C   1 
ATOM   7183  O  O   . ASN C  1 248 ? 94.548  15.050  37.772  1.00 9.57  ? 248  ASN C O   1 
ATOM   7184  C  CB  . ASN C  1 248 ? 96.687  13.873  36.509  1.00 10.87 ? 248  ASN C CB  1 
ATOM   7185  C  CG  . ASN C  1 248 ? 97.397  15.163  36.930  1.00 15.87 ? 248  ASN C CG  1 
ATOM   7186  O  OD1 . ASN C  1 248 ? 97.823  15.322  38.087  1.00 15.31 ? 248  ASN C OD1 1 
ATOM   7187  N  ND2 . ASN C  1 248 ? 97.526  16.099  35.955  1.00 19.84 ? 248  ASN C ND2 1 
ATOM   7188  N  N   . TYR C  1 249 ? 94.238  13.457  39.347  1.00 9.46  ? 249  TYR C N   1 
ATOM   7189  C  CA  . TYR C  1 249 ? 93.243  14.251  40.095  1.00 9.12  ? 249  TYR C CA  1 
ATOM   7190  C  C   . TYR C  1 249 ? 93.193  13.809  41.564  1.00 9.06  ? 249  TYR C C   1 
ATOM   7191  O  O   . TYR C  1 249 ? 93.743  12.766  41.876  1.00 7.20  ? 249  TYR C O   1 
ATOM   7192  C  CB  . TYR C  1 249 ? 91.841  14.121  39.485  1.00 9.05  ? 249  TYR C CB  1 
ATOM   7193  C  CG  . TYR C  1 249 ? 91.107  12.784  39.703  1.00 10.35 ? 249  TYR C CG  1 
ATOM   7194  C  CD1 . TYR C  1 249 ? 91.447  11.638  38.963  1.00 9.41  ? 249  TYR C CD1 1 
ATOM   7195  C  CD2 . TYR C  1 249 ? 90.032  12.682  40.600  1.00 9.32  ? 249  TYR C CD2 1 
ATOM   7196  C  CE1 . TYR C  1 249 ? 90.757  10.424  39.160  1.00 11.58 ? 249  TYR C CE1 1 
ATOM   7197  C  CE2 . TYR C  1 249 ? 89.351  11.488  40.800  1.00 7.84  ? 249  TYR C CE2 1 
ATOM   7198  C  CZ  . TYR C  1 249 ? 89.690  10.367  40.086  1.00 11.40 ? 249  TYR C CZ  1 
ATOM   7199  O  OH  . TYR C  1 249 ? 89.005  9.159   40.280  1.00 9.63  ? 249  TYR C OH  1 
ATOM   7200  N  N   . THR C  1 250 ? 92.471  14.565  42.413  1.00 8.26  ? 250  THR C N   1 
ATOM   7201  C  CA  . THR C  1 250 ? 92.147  14.113  43.771  1.00 9.28  ? 250  THR C CA  1 
ATOM   7202  C  C   . THR C  1 250 ? 90.660  14.285  44.035  1.00 10.20 ? 250  THR C C   1 
ATOM   7203  O  O   . THR C  1 250 ? 90.001  15.130  43.404  1.00 8.65  ? 250  THR C O   1 
ATOM   7204  C  CB  . THR C  1 250 ? 92.972  14.882  44.895  1.00 10.03 ? 250  THR C CB  1 
ATOM   7205  O  OG1 . THR C  1 250 ? 92.784  16.309  44.764  1.00 9.02  ? 250  THR C OG1 1 
ATOM   7206  C  CG2 . THR C  1 250 ? 94.507  14.660  44.754  1.00 10.26 ? 250  THR C CG2 1 
ATOM   7207  N  N   . LEU C  1 251 ? 90.141  13.487  44.981  1.00 9.67  ? 251  LEU C N   1 
ATOM   7208  C  CA  . LEU C  1 251 ? 88.739  13.548  45.356  1.00 9.53  ? 251  LEU C CA  1 
ATOM   7209  C  C   . LEU C  1 251 ? 88.676  13.232  46.841  1.00 8.75  ? 251  LEU C C   1 
ATOM   7210  O  O   . LEU C  1 251 ? 89.410  12.350  47.324  1.00 8.02  ? 251  LEU C O   1 
ATOM   7211  C  CB  . LEU C  1 251 ? 87.942  12.483  44.572  1.00 8.44  ? 251  LEU C CB  1 
ATOM   7212  C  CG  . LEU C  1 251 ? 86.426  12.513  44.792  1.00 10.25 ? 251  LEU C CG  1 
ATOM   7213  C  CD1 . LEU C  1 251 ? 85.786  13.640  44.031  1.00 8.41  ? 251  LEU C CD1 1 
ATOM   7214  C  CD2 . LEU C  1 251 ? 85.841  11.163  44.364  1.00 8.67  ? 251  LEU C CD2 1 
ATOM   7215  N  N   . SER C  1 252 ? 87.795  13.929  47.566  1.00 9.07  ? 252  SER C N   1 
ATOM   7216  C  CA  . SER C  1 252 ? 87.709  13.772  49.011  1.00 9.00  ? 252  SER C CA  1 
ATOM   7217  C  C   . SER C  1 252 ? 86.427  14.470  49.483  1.00 9.83  ? 252  SER C C   1 
ATOM   7218  O  O   . SER C  1 252 ? 85.778  15.203  48.699  1.00 9.57  ? 252  SER C O   1 
ATOM   7219  C  CB  . SER C  1 252 ? 88.908  14.476  49.662  1.00 9.13  ? 252  SER C CB  1 
ATOM   7220  O  OG  . SER C  1 252 ? 88.912  15.854  49.298  1.00 10.98 ? 252  SER C OG  1 
ATOM   7221  N  N   . THR C  1 253 ? 86.067  14.309  50.760  1.00 9.50  ? 253  THR C N   1 
ATOM   7222  C  CA  . THR C  1 253 ? 85.212  15.344  51.378  1.00 9.52  ? 253  THR C CA  1 
ATOM   7223  C  C   . THR C  1 253 ? 86.095  16.231  52.241  1.00 9.68  ? 253  THR C C   1 
ATOM   7224  O  O   . THR C  1 253 ? 87.123  15.793  52.722  1.00 10.73 ? 253  THR C O   1 
ATOM   7225  C  CB  . THR C  1 253 ? 84.080  14.804  52.228  1.00 9.40  ? 253  THR C CB  1 
ATOM   7226  O  OG1 . THR C  1 253 ? 84.630  14.006  53.286  1.00 12.25 ? 253  THR C OG1 1 
ATOM   7227  C  CG2 . THR C  1 253 ? 83.111  13.926  51.362  1.00 10.47 ? 253  THR C CG2 1 
ATOM   7228  N  N   . ILE C  1 254 ? 85.692  17.490  52.385  1.00 10.99 ? 254  ILE C N   1 
ATOM   7229  C  CA  . ILE C  1 254 ? 86.301  18.420  53.334  1.00 9.84  ? 254  ILE C CA  1 
ATOM   7230  C  C   . ILE C  1 254 ? 85.167  18.910  54.268  1.00 10.15 ? 254  ILE C C   1 
ATOM   7231  O  O   . ILE C  1 254 ? 84.175  19.485  53.785  1.00 11.85 ? 254  ILE C O   1 
ATOM   7232  C  CB  . ILE C  1 254 ? 86.928  19.631  52.611  1.00 10.72 ? 254  ILE C CB  1 
ATOM   7233  C  CG1 . ILE C  1 254 ? 87.925  19.201  51.535  1.00 9.43  ? 254  ILE C CG1 1 
ATOM   7234  C  CG2 . ILE C  1 254 ? 87.612  20.575  53.622  1.00 10.46 ? 254  ILE C CG2 1 
ATOM   7235  C  CD1 . ILE C  1 254 ? 88.351  20.373  50.620  1.00 13.64 ? 254  ILE C CD1 1 
ATOM   7236  N  N   . SER C  1 255 ? 85.330  18.642  55.568  1.00 9.02  ? 255  SER C N   1 
ATOM   7237  C  CA  . SER C  1 255 ? 84.445  19.115  56.636  1.00 8.94  ? 255  SER C CA  1 
ATOM   7238  C  C   . SER C  1 255 ? 85.085  20.339  57.266  1.00 8.95  ? 255  SER C C   1 
ATOM   7239  O  O   . SER C  1 255 ? 86.303  20.431  57.321  1.00 9.16  ? 255  SER C O   1 
ATOM   7240  C  CB  . SER C  1 255 ? 84.232  18.047  57.683  1.00 8.46  ? 255  SER C CB  1 
ATOM   7241  O  OG  . SER C  1 255 ? 83.663  16.909  57.083  1.00 11.66 ? 255  SER C OG  1 
ATOM   7242  N  N   . MET C  1 256 ? 84.273  21.290  57.705  1.00 9.36  ? 256  MET C N   1 
ATOM   7243  C  CA  . MET C  1 256 ? 84.796  22.632  58.100  1.00 9.51  ? 256  MET C CA  1 
ATOM   7244  C  C   . MET C  1 256 ? 84.075  23.109  59.342  1.00 8.48  ? 256  MET C C   1 
ATOM   7245  O  O   . MET C  1 256 ? 82.853  22.992  59.421  1.00 8.41  ? 256  MET C O   1 
ATOM   7246  C  CB  . MET C  1 256 ? 84.502  23.688  57.034  1.00 10.55 ? 256  MET C CB  1 
ATOM   7247  C  CG  . MET C  1 256 ? 84.836  23.278  55.637  1.00 14.40 ? 256  MET C CG  1 
ATOM   7248  S  SD  . MET C  1 256 ? 84.250  24.465  54.423  1.00 14.21 ? 256  MET C SD  1 
ATOM   7249  C  CE  . MET C  1 256 ? 84.565  23.430  53.107  1.00 14.03 ? 256  MET C CE  1 
ATOM   7250  N  N   . SER C  1 257 ? 84.854  23.657  60.270  1.00 8.79  ? 257  SER C N   1 
ATOM   7251  C  CA  . SER C  1 257 ? 84.414  24.513  61.346  1.00 8.79  ? 257  SER C CA  1 
ATOM   7252  C  C   . SER C  1 257 ? 84.185  25.905  60.723  1.00 8.12  ? 257  SER C C   1 
ATOM   7253  O  O   . SER C  1 257 ? 84.425  26.087  59.536  1.00 8.81  ? 257  SER C O   1 
ATOM   7254  C  CB  . SER C  1 257 ? 85.548  24.620  62.379  1.00 8.92  ? 257  SER C CB  1 
ATOM   7255  O  OG  . SER C  1 257 ? 86.612  25.479  61.917  1.00 8.36  ? 257  SER C OG  1 
ATOM   7256  N  N   . THR C  1 258 ? 83.746  26.869  61.527  1.00 8.24  ? 258  THR C N   1 
ATOM   7257  C  CA  . THR C  1 258 ? 83.836  28.287  61.122  1.00 7.95  ? 258  THR C CA  1 
ATOM   7258  C  C   . THR C  1 258 ? 85.273  28.762  61.167  1.00 8.08  ? 258  THR C C   1 
ATOM   7259  O  O   . THR C  1 258 ? 86.176  28.075  61.700  1.00 7.90  ? 258  THR C O   1 
ATOM   7260  C  CB  . THR C  1 258 ? 83.020  29.218  62.029  1.00 7.85  ? 258  THR C CB  1 
ATOM   7261  O  OG1 . THR C  1 258 ? 83.392  28.996  63.393  1.00 9.76  ? 258  THR C OG1 1 
ATOM   7262  C  CG2 . THR C  1 258 ? 81.503  28.922  61.931  1.00 6.07  ? 258  THR C CG2 1 
ATOM   7263  N  N   . THR C  1 259 ? 85.494  29.937  60.603  1.00 7.21  ? 259  THR C N   1 
ATOM   7264  C  CA  . THR C  1 259 ? 86.814  30.523  60.698  1.00 7.21  ? 259  THR C CA  1 
ATOM   7265  C  C   . THR C  1 259 ? 86.748  31.520  61.846  1.00 8.39  ? 259  THR C C   1 
ATOM   7266  O  O   . THR C  1 259 ? 85.943  32.454  61.793  1.00 9.43  ? 259  THR C O   1 
ATOM   7267  C  CB  . THR C  1 259 ? 87.189  31.204  59.383  1.00 6.90  ? 259  THR C CB  1 
ATOM   7268  O  OG1 . THR C  1 259 ? 87.267  30.209  58.333  1.00 4.67  ? 259  THR C OG1 1 
ATOM   7269  C  CG2 . THR C  1 259 ? 88.602  31.905  59.490  1.00 5.21  ? 259  THR C CG2 1 
ATOM   7270  N  N   . PRO C  1 260 ? 87.575  31.339  62.878  1.00 9.25  ? 260  PRO C N   1 
ATOM   7271  C  CA  . PRO C  1 260 ? 87.616  32.283  64.005  1.00 10.57 ? 260  PRO C CA  1 
ATOM   7272  C  C   . PRO C  1 260 ? 87.963  33.702  63.504  1.00 11.95 ? 260  PRO C C   1 
ATOM   7273  O  O   . PRO C  1 260 ? 88.697  33.799  62.531  1.00 10.03 ? 260  PRO C O   1 
ATOM   7274  C  CB  . PRO C  1 260 ? 88.792  31.768  64.854  1.00 11.26 ? 260  PRO C CB  1 
ATOM   7275  C  CG  . PRO C  1 260 ? 88.905  30.304  64.472  1.00 11.33 ? 260  PRO C CG  1 
ATOM   7276  C  CD  . PRO C  1 260 ? 88.535  30.223  63.016  1.00 9.10  ? 260  PRO C CD  1 
ATOM   7277  N  N   . SER C  1 261 ? 87.479  34.750  64.183  1.00 14.34 ? 261  SER C N   1 
ATOM   7278  C  CA  . SER C  1 261 ? 87.665  36.147  63.748  1.00 17.22 ? 261  SER C CA  1 
ATOM   7279  C  C   . SER C  1 261 ? 89.136  36.595  63.790  1.00 17.37 ? 261  SER C C   1 
ATOM   7280  O  O   . SER C  1 261 ? 89.515  37.600  63.158  1.00 17.42 ? 261  SER C O   1 
ATOM   7281  C  CB  . SER C  1 261 ? 86.767  37.118  64.559  1.00 17.91 ? 261  SER C CB  1 
ATOM   7282  O  OG  . SER C  1 261 ? 87.060  37.070  65.961  1.00 20.91 ? 261  SER C OG  1 
ATOM   7283  N  N   . THR C  1 262 ? 89.963  35.803  64.475  1.00 17.39 ? 262  THR C N   1 
ATOM   7284  C  CA  . THR C  1 262 ? 91.411  36.069  64.603  1.00 17.31 ? 262  THR C CA  1 
ATOM   7285  C  C   . THR C  1 262 ? 92.216  35.412  63.482  1.00 16.84 ? 262  THR C C   1 
ATOM   7286  O  O   . THR C  1 262 ? 93.429  35.544  63.411  1.00 17.56 ? 262  THR C O   1 
ATOM   7287  C  CB  . THR C  1 262 ? 91.937  35.487  65.945  1.00 18.04 ? 262  THR C CB  1 
ATOM   7288  O  OG1 . THR C  1 262 ? 91.499  34.113  66.090  1.00 18.41 ? 262  THR C OG1 1 
ATOM   7289  C  CG2 . THR C  1 262 ? 91.339  36.234  67.152  1.00 20.13 ? 262  THR C CG2 1 
ATOM   7290  N  N   . VAL C  1 263 ? 91.544  34.665  62.627  1.00 15.06 ? 263  VAL C N   1 
ATOM   7291  C  CA  . VAL C  1 263 ? 92.214  33.996  61.526  1.00 13.64 ? 263  VAL C CA  1 
ATOM   7292  C  C   . VAL C  1 263 ? 91.766  34.621  60.200  1.00 11.91 ? 263  VAL C C   1 
ATOM   7293  O  O   . VAL C  1 263 ? 90.575  34.731  59.943  1.00 11.80 ? 263  VAL C O   1 
ATOM   7294  C  CB  . VAL C  1 263 ? 91.901  32.455  61.553  1.00 13.68 ? 263  VAL C CB  1 
ATOM   7295  C  CG1 . VAL C  1 263 ? 92.294  31.788  60.247  1.00 12.62 ? 263  VAL C CG1 1 
ATOM   7296  C  CG2 . VAL C  1 263 ? 92.636  31.806  62.721  1.00 14.70 ? 263  VAL C CG2 1 
ATOM   7297  N  N   . THR C  1 264 ? 92.722  34.995  59.361  1.00 10.18 ? 264  THR C N   1 
ATOM   7298  C  CA  . THR C  1 264 ? 92.442  35.543  58.046  1.00 9.76  ? 264  THR C CA  1 
ATOM   7299  C  C   . THR C  1 264 ? 92.047  34.407  57.097  1.00 9.27  ? 264  THR C C   1 
ATOM   7300  O  O   . THR C  1 264 ? 92.774  33.404  56.961  1.00 8.69  ? 264  THR C O   1 
ATOM   7301  C  CB  . THR C  1 264 ? 93.675  36.295  57.559  1.00 9.91  ? 264  THR C CB  1 
ATOM   7302  O  OG1 . THR C  1 264 ? 93.869  37.458  58.387  1.00 9.81  ? 264  THR C OG1 1 
ATOM   7303  C  CG2 . THR C  1 264 ? 93.454  36.863  56.151  1.00 9.76  ? 264  THR C CG2 1 
ATOM   7304  N  N   . VAL C  1 265 ? 90.852  34.499  56.511  1.00 9.44  ? 265  VAL C N   1 
ATOM   7305  C  CA  . VAL C  1 265 ? 90.420  33.487  55.528  1.00 7.89  ? 265  VAL C CA  1 
ATOM   7306  C  C   . VAL C  1 265 ? 91.445  33.492  54.356  1.00 7.85  ? 265  VAL C C   1 
ATOM   7307  O  O   . VAL C  1 265 ? 91.634  34.510  53.718  1.00 7.15  ? 265  VAL C O   1 
ATOM   7308  C  CB  . VAL C  1 265 ? 89.016  33.736  54.989  1.00 8.05  ? 265  VAL C CB  1 
ATOM   7309  C  CG1 . VAL C  1 265 ? 88.639  32.672  53.853  1.00 8.07  ? 265  VAL C CG1 1 
ATOM   7310  C  CG2 . VAL C  1 265 ? 87.939  33.595  56.086  1.00 10.02 ? 265  VAL C CG2 1 
ATOM   7311  N  N   . PRO C  1 266 ? 92.125  32.366  54.107  1.00 8.45  ? 266  PRO C N   1 
ATOM   7312  C  CA  . PRO C  1 266 ? 93.209  32.316  53.111  1.00 8.17  ? 266  PRO C CA  1 
ATOM   7313  C  C   . PRO C  1 266 ? 92.746  32.513  51.659  1.00 8.05  ? 266  PRO C C   1 
ATOM   7314  O  O   . PRO C  1 266 ? 91.629  32.154  51.316  1.00 7.72  ? 266  PRO C O   1 
ATOM   7315  C  CB  . PRO C  1 266 ? 93.778  30.882  53.268  1.00 9.07  ? 266  PRO C CB  1 
ATOM   7316  C  CG  . PRO C  1 266 ? 92.679  30.088  53.891  1.00 8.75  ? 266  PRO C CG  1 
ATOM   7317  C  CD  . PRO C  1 266 ? 91.869  31.047  54.749  1.00 7.95  ? 266  PRO C CD  1 
ATOM   7318  N  N   . THR C  1 267 ? 93.600  33.077  50.807  1.00 8.14  ? 267  THR C N   1 
ATOM   7319  C  CA  . THR C  1 267 ? 93.322  33.083  49.371  1.00 8.05  ? 267  THR C CA  1 
ATOM   7320  C  C   . THR C  1 267 ? 94.084  31.976  48.699  1.00 8.64  ? 267  THR C C   1 
ATOM   7321  O  O   . THR C  1 267 ? 95.278  31.921  48.829  1.00 8.19  ? 267  THR C O   1 
ATOM   7322  C  CB  . THR C  1 267 ? 93.753  34.375  48.766  1.00 7.88  ? 267  THR C CB  1 
ATOM   7323  O  OG1 . THR C  1 267 ? 92.954  35.437  49.301  1.00 8.35  ? 267  THR C OG1 1 
ATOM   7324  C  CG2 . THR C  1 267 ? 93.463  34.392  47.252  1.00 8.53  ? 267  THR C CG2 1 
ATOM   7325  N  N   . TRP C  1 268 ? 93.390  31.128  47.947  1.00 8.77  ? 268  TRP C N   1 
ATOM   7326  C  CA  . TRP C  1 268 ? 94.023  30.031  47.220  1.00 8.49  ? 268  TRP C CA  1 
ATOM   7327  C  C   . TRP C  1 268 ? 94.083  30.243  45.694  1.00 9.20  ? 268  TRP C C   1 
ATOM   7328  O  O   . TRP C  1 268 ? 93.254  30.959  45.134  1.00 8.40  ? 268  TRP C O   1 
ATOM   7329  C  CB  . TRP C  1 268 ? 93.224  28.777  47.444  1.00 7.23  ? 268  TRP C CB  1 
ATOM   7330  C  CG  . TRP C  1 268 ? 93.087  28.371  48.871  1.00 9.89  ? 268  TRP C CG  1 
ATOM   7331  C  CD1 . TRP C  1 268 ? 92.002  28.575  49.688  1.00 8.22  ? 268  TRP C CD1 1 
ATOM   7332  C  CD2 . TRP C  1 268 ? 94.057  27.650  49.666  1.00 9.43  ? 268  TRP C CD2 1 
ATOM   7333  N  NE1 . TRP C  1 268 ? 92.237  28.031  50.934  1.00 9.98  ? 268  TRP C NE1 1 
ATOM   7334  C  CE2 . TRP C  1 268 ? 93.487  27.460  50.954  1.00 9.82  ? 268  TRP C CE2 1 
ATOM   7335  C  CE3 . TRP C  1 268 ? 95.331  27.127  49.415  1.00 13.81 ? 268  TRP C CE3 1 
ATOM   7336  C  CZ2 . TRP C  1 268 ? 94.152  26.785  51.991  1.00 13.14 ? 268  TRP C CZ2 1 
ATOM   7337  C  CZ3 . TRP C  1 268 ? 96.015  26.426  50.482  1.00 13.32 ? 268  TRP C CZ3 1 
ATOM   7338  C  CH2 . TRP C  1 268 ? 95.416  26.278  51.734  1.00 12.06 ? 268  TRP C CH2 1 
ATOM   7339  N  N   . SER C  1 269 ? 95.029  29.536  45.051  1.00 9.01  ? 269  SER C N   1 
ATOM   7340  C  CA  . SER C  1 269 ? 95.141  29.424  43.611  1.00 9.74  ? 269  SER C CA  1 
ATOM   7341  C  C   . SER C  1 269 ? 95.887  28.091  43.302  1.00 10.16 ? 269  SER C C   1 
ATOM   7342  O  O   . SER C  1 269 ? 96.930  27.802  43.908  1.00 10.70 ? 269  SER C O   1 
ATOM   7343  C  CB  . SER C  1 269 ? 95.991  30.589  43.098  1.00 10.25 ? 269  SER C CB  1 
ATOM   7344  O  OG  . SER C  1 269 ? 95.851  30.700  41.704  1.00 14.60 ? 269  SER C OG  1 
ATOM   7345  N  N   . PHE C  1 270 ? 95.379  27.301  42.361  1.00 9.35  ? 270  PHE C N   1 
ATOM   7346  C  CA  . PHE C  1 270 ? 96.006  26.028  41.974  1.00 9.14  ? 270  PHE C CA  1 
ATOM   7347  C  C   . PHE C  1 270 ? 96.001  25.936  40.462  1.00 8.07  ? 270  PHE C C   1 
ATOM   7348  O  O   . PHE C  1 270 ? 95.077  26.475  39.826  1.00 8.18  ? 270  PHE C O   1 
ATOM   7349  C  CB  . PHE C  1 270 ? 95.194  24.869  42.564  1.00 9.05  ? 270  PHE C CB  1 
ATOM   7350  C  CG  . PHE C  1 270 ? 95.233  24.827  44.072  1.00 12.36 ? 270  PHE C CG  1 
ATOM   7351  C  CD1 . PHE C  1 270 ? 96.307  24.251  44.723  1.00 12.76 ? 270  PHE C CD1 1 
ATOM   7352  C  CD2 . PHE C  1 270 ? 94.226  25.408  44.833  1.00 10.32 ? 270  PHE C CD2 1 
ATOM   7353  C  CE1 . PHE C  1 270 ? 96.378  24.216  46.130  1.00 13.85 ? 270  PHE C CE1 1 
ATOM   7354  C  CE2 . PHE C  1 270 ? 94.269  25.330  46.249  1.00 12.90 ? 270  PHE C CE2 1 
ATOM   7355  C  CZ  . PHE C  1 270 ? 95.374  24.753  46.876  1.00 15.12 ? 270  PHE C CZ  1 
ATOM   7356  N  N   . PRO C  1 271 ? 96.990  25.272  39.863  1.00 8.69  ? 271  PRO C N   1 
ATOM   7357  C  CA  . PRO C  1 271 ? 97.076  25.210  38.400  1.00 7.60  ? 271  PRO C CA  1 
ATOM   7358  C  C   . PRO C  1 271 ? 95.876  24.455  37.780  1.00 8.70  ? 271  PRO C C   1 
ATOM   7359  O  O   . PRO C  1 271 ? 95.482  24.825  36.682  1.00 8.17  ? 271  PRO C O   1 
ATOM   7360  C  CB  . PRO C  1 271 ? 98.401  24.483  38.153  1.00 8.71  ? 271  PRO C CB  1 
ATOM   7361  C  CG  . PRO C  1 271 ? 98.638  23.714  39.368  1.00 9.33  ? 271  PRO C CG  1 
ATOM   7362  C  CD  . PRO C  1 271 ? 98.105  24.551  40.504  1.00 7.82  ? 271  PRO C CD  1 
ATOM   7363  N  N   . GLY C  1 272 ? 95.291  23.460  38.463  1.00 7.39  ? 272  GLY C N   1 
ATOM   7364  C  CA  . GLY C  1 272 ? 94.156  22.758  37.883  1.00 8.06  ? 272  GLY C CA  1 
ATOM   7365  C  C   . GLY C  1 272 ? 92.805  23.267  38.368  1.00 8.53  ? 272  GLY C C   1 
ATOM   7366  O  O   . GLY C  1 272 ? 92.664  23.781  39.503  1.00 9.39  ? 272  GLY C O   1 
ATOM   7367  N  N   . ALA C  1 273 ? 91.788  23.104  37.522  1.00 8.54  ? 273  ALA C N   1 
ATOM   7368  C  CA  . ALA C  1 273 ? 90.400  23.374  37.914  1.00 7.76  ? 273  ALA C CA  1 
ATOM   7369  C  C   . ALA C  1 273 ? 90.014  22.592  39.144  1.00 8.07  ? 273  ALA C C   1 
ATOM   7370  O  O   . ALA C  1 273 ? 90.508  21.460  39.376  1.00 8.14  ? 273  ALA C O   1 
ATOM   7371  C  CB  . ALA C  1 273 ? 89.429  23.000  36.765  1.00 7.99  ? 273  ALA C CB  1 
ATOM   7372  N  N   . CYS C  1 274 ? 89.122  23.148  39.946  1.00 6.58  ? 274  CYS C N   1 
ATOM   7373  C  CA  . CYS C  1 274 ? 88.557  22.317  41.026  1.00 7.76  ? 274  CYS C CA  1 
ATOM   7374  C  C   . CYS C  1 274 ? 87.126  22.712  41.223  1.00 8.00  ? 274  CYS C C   1 
ATOM   7375  O  O   . CYS C  1 274 ? 86.696  23.780  40.748  1.00 7.69  ? 274  CYS C O   1 
ATOM   7376  C  CB  . CYS C  1 274 ? 89.342  22.417  42.375  1.00 8.37  ? 274  CYS C CB  1 
ATOM   7377  S  SG  . CYS C  1 274 ? 89.318  24.053  43.185  1.00 8.71  ? 274  CYS C SG  1 
ATOM   7378  N  N   . ALA C  1 275 ? 86.415  21.847  41.939  1.00 8.45  ? 275  ALA C N   1 
ATOM   7379  C  CA  . ALA C  1 275 ? 84.993  22.043  42.204  1.00 9.33  ? 275  ALA C CA  1 
ATOM   7380  C  C   . ALA C  1 275 ? 84.566  21.413  43.515  1.00 7.85  ? 275  ALA C C   1 
ATOM   7381  O  O   . ALA C  1 275 ? 85.213  20.530  44.053  1.00 9.18  ? 275  ALA C O   1 
ATOM   7382  C  CB  . ALA C  1 275 ? 84.127  21.471  41.022  1.00 8.28  ? 275  ALA C CB  1 
ATOM   7383  N  N   . PHE C  1 276 ? 83.466  21.897  44.063  1.00 9.29  ? 276  PHE C N   1 
ATOM   7384  C  CA  . PHE C  1 276 ? 82.896  21.169  45.191  1.00 7.86  ? 276  PHE C CA  1 
ATOM   7385  C  C   . PHE C  1 276 ? 81.382  21.235  45.182  1.00 7.85  ? 276  PHE C C   1 
ATOM   7386  O  O   . PHE C  1 276 ? 80.796  22.207  44.697  1.00 6.65  ? 276  PHE C O   1 
ATOM   7387  C  CB  . PHE C  1 276 ? 83.500  21.591  46.554  1.00 9.60  ? 276  PHE C CB  1 
ATOM   7388  C  CG  . PHE C  1 276 ? 83.245  23.018  46.947  1.00 7.12  ? 276  PHE C CG  1 
ATOM   7389  C  CD1 . PHE C  1 276 ? 82.059  23.386  47.635  1.00 10.37 ? 276  PHE C CD1 1 
ATOM   7390  C  CD2 . PHE C  1 276 ? 84.212  23.987  46.691  1.00 11.00 ? 276  PHE C CD2 1 
ATOM   7391  C  CE1 . PHE C  1 276 ? 81.823  24.737  47.999  1.00 11.53 ? 276  PHE C CE1 1 
ATOM   7392  C  CE2 . PHE C  1 276 ? 84.006  25.320  47.087  1.00 10.29 ? 276  PHE C CE2 1 
ATOM   7393  C  CZ  . PHE C  1 276 ? 82.829  25.693  47.738  1.00 10.54 ? 276  PHE C CZ  1 
ATOM   7394  N  N   . GLN C  1 277 ? 80.767  20.227  45.774  1.00 6.41  ? 277  GLN C N   1 
ATOM   7395  C  CA  . GLN C  1 277 ? 79.323  20.247  45.974  1.00 7.49  ? 277  GLN C CA  1 
ATOM   7396  C  C   . GLN C  1 277 ? 79.088  20.156  47.466  1.00 8.26  ? 277  GLN C C   1 
ATOM   7397  O  O   . GLN C  1 277 ? 79.593  19.227  48.133  1.00 7.23  ? 277  GLN C O   1 
ATOM   7398  C  CB  . GLN C  1 277 ? 78.628  19.069  45.266  1.00 6.41  ? 277  GLN C CB  1 
ATOM   7399  C  CG  . GLN C  1 277 ? 77.107  18.990  45.525  1.00 6.87  ? 277  GLN C CG  1 
ATOM   7400  C  CD  . GLN C  1 277 ? 76.459  17.790  44.887  1.00 11.01 ? 277  GLN C CD  1 
ATOM   7401  O  OE1 . GLN C  1 277 ? 76.880  16.646  45.131  1.00 10.23 ? 277  GLN C OE1 1 
ATOM   7402  N  NE2 . GLN C  1 277 ? 75.429  18.020  44.102  1.00 10.45 ? 277  GLN C NE2 1 
ATOM   7403  N  N   . VAL C  1 278 ? 78.314  21.112  47.988  1.00 8.15  ? 278  VAL C N   1 
ATOM   7404  C  CA  . VAL C  1 278 ? 77.976  21.113  49.428  1.00 8.61  ? 278  VAL C CA  1 
ATOM   7405  C  C   . VAL C  1 278 ? 77.123  19.879  49.731  1.00 9.57  ? 278  VAL C C   1 
ATOM   7406  O  O   . VAL C  1 278 ? 76.131  19.608  49.020  1.00 11.23 ? 278  VAL C O   1 
ATOM   7407  C  CB  . VAL C  1 278 ? 77.237  22.453  49.832  1.00 8.72  ? 278  VAL C CB  1 
ATOM   7408  C  CG1 . VAL C  1 278 ? 76.818  22.389  51.333  1.00 6.05  ? 278  VAL C CG1 1 
ATOM   7409  C  CG2 . VAL C  1 278 ? 78.187  23.633  49.620  1.00 7.77  ? 278  VAL C CG2 1 
ATOM   7410  N  N   . GLN C  1 279 ? 77.498  19.120  50.776  1.00 8.77  ? 279  GLN C N   1 
ATOM   7411  C  CA  . GLN C  1 279 ? 76.691  17.988  51.203  1.00 8.85  ? 279  GLN C CA  1 
ATOM   7412  C  C   . GLN C  1 279 ? 75.919  18.390  52.427  1.00 10.08 ? 279  GLN C C   1 
ATOM   7413  O  O   . GLN C  1 279 ? 74.727  18.098  52.522  1.00 10.71 ? 279  GLN C O   1 
ATOM   7414  C  CB  . GLN C  1 279 ? 77.582  16.783  51.505  1.00 8.57  ? 279  GLN C CB  1 
ATOM   7415  C  CG  . GLN C  1 279 ? 78.352  16.300  50.275  1.00 9.34  ? 279  GLN C CG  1 
ATOM   7416  C  CD  . GLN C  1 279 ? 77.459  16.140  49.072  1.00 10.75 ? 279  GLN C CD  1 
ATOM   7417  O  OE1 . GLN C  1 279 ? 76.353  15.590  49.177  1.00 11.69 ? 279  GLN C OE1 1 
ATOM   7418  N  NE2 . GLN C  1 279 ? 77.929  16.634  47.913  1.00 7.84  ? 279  GLN C NE2 1 
ATOM   7419  N  N   . GLU C  1 280 ? 76.576  19.123  53.335  1.00 8.33  ? 280  GLU C N   1 
ATOM   7420  C  CA  . GLU C  1 280 ? 75.864  19.579  54.526  1.00 10.45 ? 280  GLU C CA  1 
ATOM   7421  C  C   . GLU C  1 280 ? 76.406  20.961  54.889  1.00 10.48 ? 280  GLU C C   1 
ATOM   7422  O  O   . GLU C  1 280 ? 77.612  21.245  54.676  1.00 9.92  ? 280  GLU C O   1 
ATOM   7423  C  CB  . GLU C  1 280 ? 76.136  18.574  55.679  1.00 10.46 ? 280  GLU C CB  1 
ATOM   7424  C  CG  . GLU C  1 280 ? 75.448  18.960  56.970  1.00 16.38 ? 280  GLU C CG  1 
ATOM   7425  C  CD  . GLU C  1 280 ? 75.882  18.124  58.179  1.00 19.22 ? 280  GLU C CD  1 
ATOM   7426  O  OE1 . GLU C  1 280 ? 76.646  17.117  58.021  1.00 16.00 ? 280  GLU C OE1 1 
ATOM   7427  O  OE2 . GLU C  1 280 ? 75.365  18.464  59.273  1.00 18.35 ? 280  GLU C OE2 1 
ATOM   7428  N  N   . GLY C  1 281 ? 75.539  21.819  55.403  1.00 10.03 ? 281  GLY C N   1 
ATOM   7429  C  CA  . GLY C  1 281 ? 75.969  23.120  55.876  1.00 9.39  ? 281  GLY C CA  1 
ATOM   7430  C  C   . GLY C  1 281 ? 75.816  24.267  54.918  1.00 9.11  ? 281  GLY C C   1 
ATOM   7431  O  O   . GLY C  1 281 ? 75.006  24.235  53.977  1.00 8.75  ? 281  GLY C O   1 
ATOM   7432  N  N   . ARG C  1 282 ? 76.599  25.334  55.144  1.00 7.32  ? 282  ARG C N   1 
ATOM   7433  C  CA  . ARG C  1 282 ? 76.401  26.553  54.393  1.00 5.79  ? 282  ARG C CA  1 
ATOM   7434  C  C   . ARG C  1 282 ? 77.820  27.113  54.232  1.00 4.85  ? 282  ARG C C   1 
ATOM   7435  O  O   . ARG C  1 282 ? 78.495  27.438  55.237  1.00 5.81  ? 282  ARG C O   1 
ATOM   7436  C  CB  . ARG C  1 282 ? 75.557  27.549  55.191  1.00 5.33  ? 282  ARG C CB  1 
ATOM   7437  C  CG  . ARG C  1 282 ? 74.240  26.979  55.682  1.00 6.14  ? 282  ARG C CG  1 
ATOM   7438  C  CD  . ARG C  1 282 ? 73.288  28.043  56.288  1.00 11.10 ? 282  ARG C CD  1 
ATOM   7439  N  NE  . ARG C  1 282 ? 73.737  28.547  57.585  1.00 9.93  ? 282  ARG C NE  1 
ATOM   7440  C  CZ  . ARG C  1 282 ? 73.994  29.811  57.900  1.00 11.48 ? 282  ARG C CZ  1 
ATOM   7441  N  NH1 . ARG C  1 282 ? 73.921  30.799  57.002  1.00 10.06 ? 282  ARG C NH1 1 
ATOM   7442  N  NH2 . ARG C  1 282 ? 74.390  30.082  59.133  1.00 14.43 ? 282  ARG C NH2 1 
ATOM   7443  N  N   . VAL C  1 283 ? 78.280  27.147  52.997  1.00 4.37  ? 283  VAL C N   1 
ATOM   7444  C  CA  . VAL C  1 283 ? 79.674  27.488  52.616  1.00 6.39  ? 283  VAL C CA  1 
ATOM   7445  C  C   . VAL C  1 283 ? 79.680  28.736  51.690  1.00 7.38  ? 283  VAL C C   1 
ATOM   7446  O  O   . VAL C  1 283 ? 78.998  28.776  50.662  1.00 8.77  ? 283  VAL C O   1 
ATOM   7447  C  CB  . VAL C  1 283 ? 80.359  26.306  51.961  1.00 5.96  ? 283  VAL C CB  1 
ATOM   7448  C  CG1 . VAL C  1 283 ? 81.845  26.612  51.502  1.00 4.08  ? 283  VAL C CG1 1 
ATOM   7449  C  CG2 . VAL C  1 283 ? 80.386  25.070  52.977  1.00 7.82  ? 283  VAL C CG2 1 
ATOM   7450  N  N   . VAL C  1 284 ? 80.460  29.732  52.059  1.00 7.51  ? 284  VAL C N   1 
ATOM   7451  C  CA  . VAL C  1 284 ? 80.558  30.948  51.311  1.00 7.90  ? 284  VAL C CA  1 
ATOM   7452  C  C   . VAL C  1 284 ? 81.779  30.809  50.414  1.00 8.79  ? 284  VAL C C   1 
ATOM   7453  O  O   . VAL C  1 284 ? 82.869  30.409  50.869  1.00 8.57  ? 284  VAL C O   1 
ATOM   7454  C  CB  . VAL C  1 284 ? 80.660  32.190  52.225  1.00 9.14  ? 284  VAL C CB  1 
ATOM   7455  C  CG1 . VAL C  1 284 ? 80.936  33.491  51.416  1.00 7.49  ? 284  VAL C CG1 1 
ATOM   7456  C  CG2 . VAL C  1 284 ? 79.414  32.350  53.104  1.00 8.75  ? 284  VAL C CG2 1 
ATOM   7457  N  N   . VAL C  1 285 ? 81.584  31.072  49.126  1.00 8.28  ? 285  VAL C N   1 
ATOM   7458  C  CA  . VAL C  1 285 ? 82.686  31.013  48.180  1.00 8.76  ? 285  VAL C CA  1 
ATOM   7459  C  C   . VAL C  1 285 ? 82.833  32.346  47.463  1.00 9.16  ? 285  VAL C C   1 
ATOM   7460  O  O   . VAL C  1 285 ? 81.822  32.993  47.082  1.00 10.00 ? 285  VAL C O   1 
ATOM   7461  C  CB  . VAL C  1 285 ? 82.533  29.805  47.208  1.00 9.26  ? 285  VAL C CB  1 
ATOM   7462  C  CG1 . VAL C  1 285 ? 81.464  30.096  46.058  1.00 4.92  ? 285  VAL C CG1 1 
ATOM   7463  C  CG2 . VAL C  1 285 ? 83.862  29.454  46.612  1.00 9.65  ? 285  VAL C CG2 1 
ATOM   7464  N  N   . GLN C  1 286 ? 84.082  32.807  47.336  1.00 8.78  ? 286  GLN C N   1 
ATOM   7465  C  CA  . GLN C  1 286 ? 84.339  34.034  46.598  1.00 9.26  ? 286  GLN C CA  1 
ATOM   7466  C  C   . GLN C  1 286 ? 85.396  33.683  45.559  1.00 9.32  ? 286  GLN C C   1 
ATOM   7467  O  O   . GLN C  1 286 ? 86.537  33.371  45.927  1.00 8.25  ? 286  GLN C O   1 
ATOM   7468  C  CB  . GLN C  1 286 ? 84.883  35.109  47.546  1.00 10.71 ? 286  GLN C CB  1 
ATOM   7469  C  CG  . GLN C  1 286 ? 85.102  36.430  46.885  1.00 11.91 ? 286  GLN C CG  1 
ATOM   7470  C  CD  . GLN C  1 286 ? 85.710  37.444  47.833  1.00 20.92 ? 286  GLN C CD  1 
ATOM   7471  O  OE1 . GLN C  1 286 ? 85.599  37.324  49.073  1.00 20.20 ? 286  GLN C OE1 1 
ATOM   7472  N  NE2 . GLN C  1 286 ? 86.329  38.471  47.264  1.00 19.79 ? 286  GLN C NE2 1 
ATOM   7473  N  N   . ILE C  1 287 ? 85.043  33.765  44.277  1.00 8.37  ? 287  ILE C N   1 
ATOM   7474  C  CA  . ILE C  1 287 ? 85.966  33.282  43.227  1.00 7.43  ? 287  ILE C CA  1 
ATOM   7475  C  C   . ILE C  1 287 ? 86.339  34.441  42.327  1.00 8.55  ? 287  ILE C C   1 
ATOM   7476  O  O   . ILE C  1 287 ? 85.469  35.174  41.888  1.00 9.20  ? 287  ILE C O   1 
ATOM   7477  C  CB  . ILE C  1 287 ? 85.307  32.120  42.404  1.00 7.68  ? 287  ILE C CB  1 
ATOM   7478  C  CG1 . ILE C  1 287 ? 84.823  31.007  43.345  1.00 7.15  ? 287  ILE C CG1 1 
ATOM   7479  C  CG2 . ILE C  1 287 ? 86.307  31.572  41.407  1.00 5.24  ? 287  ILE C CG2 1 
ATOM   7480  C  CD1 . ILE C  1 287 ? 83.684  30.063  42.778  1.00 7.22  ? 287  ILE C CD1 1 
ATOM   7481  N  N   . GLY C  1 288 ? 87.631  34.594  42.062  1.00 8.70  ? 288  GLY C N   1 
ATOM   7482  C  CA  . GLY C  1 288 ? 88.111  35.657  41.210  1.00 10.27 ? 288  GLY C CA  1 
ATOM   7483  C  C   . GLY C  1 288 ? 87.469  36.992  41.577  1.00 10.82 ? 288  GLY C C   1 
ATOM   7484  O  O   . GLY C  1 288 ? 87.495  37.391  42.741  1.00 9.18  ? 288  GLY C O   1 
ATOM   7485  N  N   . ASP C  1 289 ? 86.858  37.598  40.553  1.00 11.49 ? 289  ASP C N   1 
ATOM   7486  C  CA  . ASP C  1 289 ? 86.248  38.932  40.508  1.00 13.61 ? 289  ASP C CA  1 
ATOM   7487  C  C   . ASP C  1 289 ? 84.756  39.008  40.963  1.00 12.32 ? 289  ASP C C   1 
ATOM   7488  O  O   . ASP C  1 289 ? 84.165  40.100  41.035  1.00 11.83 ? 289  ASP C O   1 
ATOM   7489  C  CB  . ASP C  1 289 ? 86.306  39.348  39.020  1.00 15.09 ? 289  ASP C CB  1 
ATOM   7490  C  CG  . ASP C  1 289 ? 85.965  40.808  38.789  1.00 22.59 ? 289  ASP C CG  1 
ATOM   7491  O  OD1 . ASP C  1 289 ? 86.023  41.606  39.781  1.00 28.85 ? 289  ASP C OD1 1 
ATOM   7492  O  OD2 . ASP C  1 289 ? 85.632  41.250  37.642  1.00 27.40 ? 289  ASP C OD2 1 
ATOM   7493  N  N   . TYR C  1 290 ? 84.143  37.864  41.224  1.00 10.76 ? 290  TYR C N   1 
ATOM   7494  C  CA  . TYR C  1 290 ? 82.693  37.801  41.545  1.00 10.70 ? 290  TYR C CA  1 
ATOM   7495  C  C   . TYR C  1 290 ? 82.345  38.060  43.011  1.00 10.22 ? 290  TYR C C   1 
ATOM   7496  O  O   . TYR C  1 290 ? 83.192  37.895  43.870  1.00 9.84  ? 290  TYR C O   1 
ATOM   7497  C  CB  . TYR C  1 290 ? 82.160  36.406  41.183  1.00 9.23  ? 290  TYR C CB  1 
ATOM   7498  C  CG  . TYR C  1 290 ? 82.257  36.132  39.696  1.00 12.07 ? 290  TYR C CG  1 
ATOM   7499  C  CD1 . TYR C  1 290 ? 83.492  35.796  39.087  1.00 12.45 ? 290  TYR C CD1 1 
ATOM   7500  C  CD2 . TYR C  1 290 ? 81.129  36.215  38.893  1.00 12.01 ? 290  TYR C CD2 1 
ATOM   7501  C  CE1 . TYR C  1 290 ? 83.561  35.540  37.733  1.00 11.24 ? 290  TYR C CE1 1 
ATOM   7502  C  CE2 . TYR C  1 290 ? 81.195  35.955  37.543  1.00 13.22 ? 290  TYR C CE2 1 
ATOM   7503  C  CZ  . TYR C  1 290 ? 82.389  35.620  36.975  1.00 13.70 ? 290  TYR C CZ  1 
ATOM   7504  O  OH  . TYR C  1 290 ? 82.406  35.428  35.625  1.00 17.16 ? 290  TYR C OH  1 
ATOM   7505  N  N   . ALA C  1 291 ? 81.088  38.427  43.305  1.00 10.15 ? 291  ALA C N   1 
ATOM   7506  C  CA  . ALA C  1 291 ? 80.610  38.544  44.702  1.00 9.38  ? 291  ALA C CA  1 
ATOM   7507  C  C   . ALA C  1 291 ? 80.619  37.220  45.397  1.00 10.11 ? 291  ALA C C   1 
ATOM   7508  O  O   . ALA C  1 291 ? 80.378  36.198  44.760  1.00 8.84  ? 291  ALA C O   1 
ATOM   7509  C  CB  . ALA C  1 291 ? 79.142  39.147  44.741  1.00 9.95  ? 291  ALA C CB  1 
ATOM   7510  N  N   . ALA C  1 292 ? 80.880  37.244  46.712  1.00 10.09 ? 292  ALA C N   1 
ATOM   7511  C  CA  . ALA C  1 292 ? 80.808  36.058  47.562  1.00 11.57 ? 292  ALA C CA  1 
ATOM   7512  C  C   . ALA C  1 292 ? 79.381  35.553  47.496  1.00 11.37 ? 292  ALA C C   1 
ATOM   7513  O  O   . ALA C  1 292 ? 78.421  36.336  47.525  1.00 10.35 ? 292  ALA C O   1 
ATOM   7514  C  CB  . ALA C  1 292 ? 81.213  36.404  49.081  1.00 11.13 ? 292  ALA C CB  1 
ATOM   7515  N  N   . THR C  1 293 ? 79.259  34.241  47.426  1.00 10.25 ? 293  THR C N   1 
ATOM   7516  C  CA  . THR C  1 293 ? 77.962  33.588  47.332  1.00 9.90  ? 293  THR C CA  1 
ATOM   7517  C  C   . THR C  1 293 ? 77.913  32.496  48.352  1.00 8.48  ? 293  THR C C   1 
ATOM   7518  O  O   . THR C  1 293 ? 78.898  31.785  48.565  1.00 7.49  ? 293  THR C O   1 
ATOM   7519  C  CB  . THR C  1 293 ? 77.807  32.981  45.924  1.00 9.42  ? 293  THR C CB  1 
ATOM   7520  O  OG1 . THR C  1 293 ? 77.601  34.077  45.037  1.00 16.81 ? 293  THR C OG1 1 
ATOM   7521  C  CG2 . THR C  1 293 ? 76.498  32.158  45.792  1.00 13.31 ? 293  THR C CG2 1 
ATOM   7522  N  N   . GLU C  1 294 ? 76.763  32.349  48.998  1.00 7.04  ? 294  GLU C N   1 
ATOM   7523  C  CA  . GLU C  1 294 ? 76.655  31.269  49.945  1.00 6.69  ? 294  GLU C CA  1 
ATOM   7524  C  C   . GLU C  1 294 ? 75.933  30.062  49.313  1.00 7.35  ? 294  GLU C C   1 
ATOM   7525  O  O   . GLU C  1 294 ? 74.858  30.202  48.742  1.00 6.70  ? 294  GLU C O   1 
ATOM   7526  C  CB  . GLU C  1 294 ? 75.914  31.766  51.190  1.00 7.21  ? 294  GLU C CB  1 
ATOM   7527  C  CG  . GLU C  1 294 ? 75.873  30.739  52.320  1.00 9.99  ? 294  GLU C CG  1 
ATOM   7528  C  CD  . GLU C  1 294 ? 75.098  31.269  53.508  1.00 13.25 ? 294  GLU C CD  1 
ATOM   7529  O  OE1 . GLU C  1 294 ? 75.335  32.453  53.890  1.00 15.14 ? 294  GLU C OE1 1 
ATOM   7530  O  OE2 . GLU C  1 294 ? 74.240  30.533  54.025  1.00 16.04 ? 294  GLU C OE2 1 
ATOM   7531  N  N   . LEU C  1 295 ? 76.539  28.898  49.465  1.00 6.79  ? 295  LEU C N   1 
ATOM   7532  C  CA  . LEU C  1 295 ? 76.001  27.677  48.950  1.00 7.28  ? 295  LEU C CA  1 
ATOM   7533  C  C   . LEU C  1 295 ? 75.329  26.831  50.025  1.00 8.31  ? 295  LEU C C   1 
ATOM   7534  O  O   . LEU C  1 295 ? 75.838  26.711  51.139  1.00 9.16  ? 295  LEU C O   1 
ATOM   7535  C  CB  . LEU C  1 295 ? 77.149  26.878  48.334  1.00 6.78  ? 295  LEU C CB  1 
ATOM   7536  C  CG  . LEU C  1 295 ? 77.554  27.266  46.907  1.00 9.88  ? 295  LEU C CG  1 
ATOM   7537  C  CD1 . LEU C  1 295 ? 78.149  28.651  46.839  1.00 10.05 ? 295  LEU C CD1 1 
ATOM   7538  C  CD2 . LEU C  1 295 ? 78.583  26.196  46.375  1.00 7.88  ? 295  LEU C CD2 1 
ATOM   7539  N  N   . GLY C  1 296 ? 74.238  26.152  49.649  1.00 8.65  ? 296  GLY C N   1 
ATOM   7540  C  CA  . GLY C  1 296 ? 73.548  25.214  50.524  1.00 8.55  ? 296  GLY C CA  1 
ATOM   7541  C  C   . GLY C  1 296 ? 73.560  23.809  49.922  1.00 9.58  ? 296  GLY C C   1 
ATOM   7542  O  O   . GLY C  1 296 ? 74.353  23.529  49.003  1.00 9.96  ? 296  GLY C O   1 
ATOM   7543  N  N   . SER C  1 297 ? 72.660  22.945  50.389  1.00 8.43  ? 297  SER C N   1 
ATOM   7544  C  CA  . SER C  1 297 ? 72.744  21.484  50.073  1.00 11.19 ? 297  SER C CA  1 
ATOM   7545  C  C   . SER C  1 297 ? 72.750  21.229  48.566  1.00 9.30  ? 297  SER C C   1 
ATOM   7546  O  O   . SER C  1 297 ? 71.867  21.711  47.862  1.00 8.87  ? 297  SER C O   1 
ATOM   7547  C  CB  . SER C  1 297 ? 71.547  20.673  50.656  1.00 10.79 ? 297  SER C CB  1 
ATOM   7548  O  OG  . SER C  1 297 ? 70.811  21.398  51.616  1.00 18.88 ? 297  SER C OG  1 
ATOM   7549  N  N   . GLY C  1 298 ? 73.699  20.423  48.087  1.00 9.60  ? 298  GLY C N   1 
ATOM   7550  C  CA  . GLY C  1 298 ? 73.743  20.097  46.659  1.00 9.02  ? 298  GLY C CA  1 
ATOM   7551  C  C   . GLY C  1 298 ? 74.247  21.165  45.694  1.00 8.73  ? 298  GLY C C   1 
ATOM   7552  O  O   . GLY C  1 298 ? 74.411  20.853  44.521  1.00 7.85  ? 298  GLY C O   1 
ATOM   7553  N  N   . ASP C  1 299 ? 74.425  22.428  46.143  1.00 7.27  ? 299  ASP C N   1 
ATOM   7554  C  CA  . ASP C  1 299 ? 74.989  23.471  45.306  1.00 6.40  ? 299  ASP C CA  1 
ATOM   7555  C  C   . ASP C  1 299 ? 76.447  23.166  44.988  1.00 6.03  ? 299  ASP C C   1 
ATOM   7556  O  O   . ASP C  1 299 ? 77.146  22.619  45.808  1.00 7.49  ? 299  ASP C O   1 
ATOM   7557  C  CB  . ASP C  1 299 ? 74.907  24.847  45.965  1.00 5.47  ? 299  ASP C CB  1 
ATOM   7558  C  CG  . ASP C  1 299 ? 73.489  25.279  46.240  1.00 5.96  ? 299  ASP C CG  1 
ATOM   7559  O  OD1 . ASP C  1 299 ? 72.494  24.709  45.688  1.00 5.10  ? 299  ASP C OD1 1 
ATOM   7560  O  OD2 . ASP C  1 299 ? 73.242  26.207  47.003  1.00 6.91  ? 299  ASP C OD2 1 
ATOM   7561  N  N   . VAL C  1 300 ? 76.857  23.540  43.790  1.00 5.71  ? 300  VAL C N   1 
ATOM   7562  C  CA  . VAL C  1 300 ? 78.148  23.265  43.215  1.00 6.00  ? 300  VAL C CA  1 
ATOM   7563  C  C   . VAL C  1 300 ? 78.841  24.568  42.865  1.00 5.49  ? 300  VAL C C   1 
ATOM   7564  O  O   . VAL C  1 300 ? 78.240  25.425  42.238  1.00 5.61  ? 300  VAL C O   1 
ATOM   7565  C  CB  . VAL C  1 300 ? 78.000  22.418  41.894  1.00 6.91  ? 300  VAL C CB  1 
ATOM   7566  C  CG1 . VAL C  1 300 ? 79.378  22.181  41.233  1.00 5.58  ? 300  VAL C CG1 1 
ATOM   7567  C  CG2 . VAL C  1 300 ? 77.329  21.046  42.191  1.00 5.89  ? 300  VAL C CG2 1 
ATOM   7568  N  N   . ALA C  1 301 ? 80.113  24.703  43.275  1.00 6.07  ? 301  ALA C N   1 
ATOM   7569  C  CA  . ALA C  1 301 ? 80.970  25.846  42.915  1.00 6.63  ? 301  ALA C CA  1 
ATOM   7570  C  C   . ALA C  1 301 ? 82.053  25.292  42.011  1.00 7.72  ? 301  ALA C C   1 
ATOM   7571  O  O   . ALA C  1 301 ? 82.611  24.227  42.272  1.00 8.27  ? 301  ALA C O   1 
ATOM   7572  C  CB  . ALA C  1 301 ? 81.653  26.418  44.131  1.00 6.86  ? 301  ALA C CB  1 
ATOM   7573  N  N   . PHE C  1 302 ? 82.352  26.016  40.941  1.00 7.13  ? 302  PHE C N   1 
ATOM   7574  C  CA  . PHE C  1 302 ? 83.415  25.600  40.038  1.00 6.76  ? 302  PHE C CA  1 
ATOM   7575  C  C   . PHE C  1 302 ? 84.454  26.716  39.972  1.00 6.87  ? 302  PHE C C   1 
ATOM   7576  O  O   . PHE C  1 302 ? 84.083  27.886  39.769  1.00 6.03  ? 302  PHE C O   1 
ATOM   7577  C  CB  . PHE C  1 302 ? 82.914  25.226  38.646  1.00 6.62  ? 302  PHE C CB  1 
ATOM   7578  C  CG  . PHE C  1 302 ? 84.051  25.039  37.643  1.00 7.57  ? 302  PHE C CG  1 
ATOM   7579  C  CD1 . PHE C  1 302 ? 84.732  23.829  37.586  1.00 10.11 ? 302  PHE C CD1 1 
ATOM   7580  C  CD2 . PHE C  1 302 ? 84.504  26.109  36.882  1.00 8.69  ? 302  PHE C CD2 1 
ATOM   7581  C  CE1 . PHE C  1 302 ? 85.781  23.647  36.740  1.00 9.21  ? 302  PHE C CE1 1 
ATOM   7582  C  CE2 . PHE C  1 302 ? 85.581  25.959  36.010  1.00 10.61 ? 302  PHE C CE2 1 
ATOM   7583  C  CZ  . PHE C  1 302 ? 86.237  24.715  35.954  1.00 9.05  ? 302  PHE C CZ  1 
ATOM   7584  N  N   . ILE C  1 303 ? 85.736  26.353  40.178  1.00 5.91  ? 303  ILE C N   1 
ATOM   7585  C  CA  . ILE C  1 303 ? 86.859  27.314  40.121  1.00 6.48  ? 303  ILE C CA  1 
ATOM   7586  C  C   . ILE C  1 303 ? 87.890  26.932  39.042  1.00 6.71  ? 303  ILE C C   1 
ATOM   7587  O  O   . ILE C  1 303 ? 88.534  25.851  39.143  1.00 7.39  ? 303  ILE C O   1 
ATOM   7588  C  CB  . ILE C  1 303 ? 87.594  27.378  41.464  1.00 7.80  ? 303  ILE C CB  1 
ATOM   7589  C  CG1 . ILE C  1 303 ? 86.610  27.710  42.595  1.00 7.53  ? 303  ILE C CG1 1 
ATOM   7590  C  CG2 . ILE C  1 303 ? 88.715  28.464  41.397  1.00 6.55  ? 303  ILE C CG2 1 
ATOM   7591  C  CD1 . ILE C  1 303 ? 86.402  26.570  43.584  1.00 11.85 ? 303  ILE C CD1 1 
ATOM   7592  N  N   . PRO C  1 304 ? 88.023  27.753  38.005  1.00 6.25  ? 304  PRO C N   1 
ATOM   7593  C  CA  . PRO C  1 304 ? 88.995  27.467  36.946  1.00 6.05  ? 304  PRO C CA  1 
ATOM   7594  C  C   . PRO C  1 304 ? 90.422  27.415  37.505  1.00 7.01  ? 304  PRO C C   1 
ATOM   7595  O  O   . PRO C  1 304 ? 90.731  28.117  38.499  1.00 6.30  ? 304  PRO C O   1 
ATOM   7596  C  CB  . PRO C  1 304 ? 88.868  28.663  35.996  1.00 6.60  ? 304  PRO C CB  1 
ATOM   7597  C  CG  . PRO C  1 304 ? 87.519  29.277  36.305  1.00 5.43  ? 304  PRO C CG  1 
ATOM   7598  C  CD  . PRO C  1 304 ? 87.229  28.980  37.748  1.00 6.24  ? 304  PRO C CD  1 
ATOM   7599  N  N   . GLY C  1 305 ? 91.290  26.607  36.889  1.00 6.96  ? 305  GLY C N   1 
ATOM   7600  C  CA  . GLY C  1 305 ? 92.684  26.595  37.301  1.00 6.17  ? 305  GLY C CA  1 
ATOM   7601  C  C   . GLY C  1 305 ? 93.290  27.975  37.179  1.00 6.88  ? 305  GLY C C   1 
ATOM   7602  O  O   . GLY C  1 305 ? 93.035  28.700  36.213  1.00 7.03  ? 305  GLY C O   1 
ATOM   7603  N  N   . GLY C  1 306 ? 94.118  28.342  38.157  1.00 6.15  ? 306  GLY C N   1 
ATOM   7604  C  CA  . GLY C  1 306 ? 94.798  29.614  38.124  1.00 6.32  ? 306  GLY C CA  1 
ATOM   7605  C  C   . GLY C  1 306 ? 93.965  30.756  38.674  1.00 6.26  ? 306  GLY C C   1 
ATOM   7606  O  O   . GLY C  1 306 ? 94.444  31.865  38.667  1.00 5.87  ? 306  GLY C O   1 
ATOM   7607  N  N   . VAL C  1 307 ? 92.721  30.515  39.082  1.00 5.45  ? 307  VAL C N   1 
ATOM   7608  C  CA  . VAL C  1 307 ? 91.868  31.641  39.520  1.00 5.74  ? 307  VAL C CA  1 
ATOM   7609  C  C   . VAL C  1 307 ? 91.902  31.667  41.036  1.00 5.80  ? 307  VAL C C   1 
ATOM   7610  O  O   . VAL C  1 307 ? 91.808  30.622  41.649  1.00 5.65  ? 307  VAL C O   1 
ATOM   7611  C  CB  . VAL C  1 307 ? 90.386  31.504  38.988  1.00 5.41  ? 307  VAL C CB  1 
ATOM   7612  C  CG1 . VAL C  1 307 ? 89.408  32.475  39.704  1.00 6.42  ? 307  VAL C CG1 1 
ATOM   7613  C  CG2 . VAL C  1 307 ? 90.321  31.720  37.445  1.00 2.68  ? 307  VAL C CG2 1 
ATOM   7614  N  N   . GLU C  1 308 ? 92.069  32.843  41.642  1.00 5.64  ? 308  GLU C N   1 
ATOM   7615  C  CA  . GLU C  1 308 ? 92.136  32.939  43.101  1.00 6.67  ? 308  GLU C CA  1 
ATOM   7616  C  C   . GLU C  1 308 ? 90.746  32.744  43.657  1.00 7.38  ? 308  GLU C C   1 
ATOM   7617  O  O   . GLU C  1 308 ? 89.770  33.211  43.051  1.00 9.28  ? 308  GLU C O   1 
ATOM   7618  C  CB  . GLU C  1 308 ? 92.612  34.329  43.544  1.00 7.66  ? 308  GLU C CB  1 
ATOM   7619  C  CG  . GLU C  1 308 ? 94.115  34.473  43.517  1.00 10.30 ? 308  GLU C CG  1 
ATOM   7620  C  CD  . GLU C  1 308 ? 94.566  35.888  43.843  1.00 16.39 ? 308  GLU C CD  1 
ATOM   7621  O  OE1 . GLU C  1 308 ? 93.726  36.831  43.843  1.00 18.47 ? 308  GLU C OE1 1 
ATOM   7622  O  OE2 . GLU C  1 308 ? 95.776  36.049  44.050  1.00 19.34 ? 308  GLU C OE2 1 
ATOM   7623  N  N   . PHE C  1 309 ? 90.666  32.080  44.812  1.00 7.59  ? 309  PHE C N   1 
ATOM   7624  C  CA  . PHE C  1 309 ? 89.425  31.982  45.524  1.00 8.58  ? 309  PHE C CA  1 
ATOM   7625  C  C   . PHE C  1 309 ? 89.613  31.870  47.038  1.00 8.40  ? 309  PHE C C   1 
ATOM   7626  O  O   . PHE C  1 309 ? 90.697  31.498  47.540  1.00 9.10  ? 309  PHE C O   1 
ATOM   7627  C  CB  . PHE C  1 309 ? 88.606  30.784  45.025  1.00 7.11  ? 309  PHE C CB  1 
ATOM   7628  C  CG  . PHE C  1 309 ? 89.233  29.443  45.332  1.00 8.74  ? 309  PHE C CG  1 
ATOM   7629  C  CD1 . PHE C  1 309 ? 90.262  28.945  44.548  1.00 7.31  ? 309  PHE C CD1 1 
ATOM   7630  C  CD2 . PHE C  1 309 ? 88.763  28.656  46.396  1.00 9.04  ? 309  PHE C CD2 1 
ATOM   7631  C  CE1 . PHE C  1 309 ? 90.833  27.671  44.827  1.00 10.69 ? 309  PHE C CE1 1 
ATOM   7632  C  CE2 . PHE C  1 309 ? 89.350  27.416  46.703  1.00 12.28 ? 309  PHE C CE2 1 
ATOM   7633  C  CZ  . PHE C  1 309 ? 90.378  26.926  45.898  1.00 13.38 ? 309  PHE C CZ  1 
ATOM   7634  N  N   . LYS C  1 310 ? 88.492  32.118  47.728  1.00 8.00  ? 310  LYS C N   1 
ATOM   7635  C  CA  . LYS C  1 310 ? 88.400  32.056  49.161  1.00 7.53  ? 310  LYS C CA  1 
ATOM   7636  C  C   . LYS C  1 310 ? 87.104  31.306  49.438  1.00 7.33  ? 310  LYS C C   1 
ATOM   7637  O  O   . LYS C  1 310 ? 86.103  31.462  48.702  1.00 8.37  ? 310  LYS C O   1 
ATOM   7638  C  CB  . LYS C  1 310 ? 88.263  33.462  49.759  1.00 7.99  ? 310  LYS C CB  1 
ATOM   7639  C  CG  . LYS C  1 310 ? 89.507  34.310  49.754  1.00 11.35 ? 310  LYS C CG  1 
ATOM   7640  C  CD  . LYS C  1 310 ? 89.112  35.746  49.877  1.00 15.14 ? 310  LYS C CD  1 
ATOM   7641  C  CE  . LYS C  1 310 ? 89.067  36.229  51.286  1.00 18.39 ? 310  LYS C CE  1 
ATOM   7642  N  NZ  . LYS C  1 310 ? 89.754  37.605  51.324  1.00 21.58 ? 310  LYS C NZ  1 
ATOM   7643  N  N   . TYR C  1 311 ? 87.112  30.503  50.499  1.00 6.30  ? 311  TYR C N   1 
ATOM   7644  C  CA  . TYR C  1 311 ? 85.875  29.923  51.003  1.00 6.87  ? 311  TYR C CA  1 
ATOM   7645  C  C   . TYR C  1 311 ? 85.953  29.876  52.549  1.00 7.29  ? 311  TYR C C   1 
ATOM   7646  O  O   . TYR C  1 311 ? 87.060  29.898  53.146  1.00 6.05  ? 311  TYR C O   1 
ATOM   7647  C  CB  . TYR C  1 311 ? 85.625  28.538  50.385  1.00 5.37  ? 311  TYR C CB  1 
ATOM   7648  C  CG  . TYR C  1 311 ? 86.650  27.535  50.885  1.00 8.64  ? 311  TYR C CG  1 
ATOM   7649  C  CD1 . TYR C  1 311 ? 87.917  27.462  50.309  1.00 8.57  ? 311  TYR C CD1 1 
ATOM   7650  C  CD2 . TYR C  1 311 ? 86.365  26.706  51.986  1.00 7.75  ? 311  TYR C CD2 1 
ATOM   7651  C  CE1 . TYR C  1 311 ? 88.898  26.548  50.799  1.00 10.77 ? 311  TYR C CE1 1 
ATOM   7652  C  CE2 . TYR C  1 311 ? 87.330  25.825  52.495  1.00 8.59  ? 311  TYR C CE2 1 
ATOM   7653  C  CZ  . TYR C  1 311 ? 88.595  25.746  51.888  1.00 9.78  ? 311  TYR C CZ  1 
ATOM   7654  O  OH  . TYR C  1 311 ? 89.529  24.846  52.379  1.00 9.80  ? 311  TYR C OH  1 
ATOM   7655  N  N   . TYR C  1 312 ? 84.792  29.838  53.178  1.00 6.97  ? 312  TYR C N   1 
ATOM   7656  C  CA  . TYR C  1 312 ? 84.670  29.629  54.615  1.00 6.95  ? 312  TYR C CA  1 
ATOM   7657  C  C   . TYR C  1 312 ? 83.279  29.105  54.908  1.00 7.49  ? 312  TYR C C   1 
ATOM   7658  O  O   . TYR C  1 312 ? 82.356  29.262  54.069  1.00 8.12  ? 312  TYR C O   1 
ATOM   7659  C  CB  . TYR C  1 312 ? 84.989  30.915  55.428  1.00 5.86  ? 312  TYR C CB  1 
ATOM   7660  C  CG  . TYR C  1 312 ? 84.043  32.062  55.152  1.00 7.60  ? 312  TYR C CG  1 
ATOM   7661  C  CD1 . TYR C  1 312 ? 82.832  32.169  55.867  1.00 5.41  ? 312  TYR C CD1 1 
ATOM   7662  C  CD2 . TYR C  1 312 ? 84.344  33.053  54.171  1.00 8.42  ? 312  TYR C CD2 1 
ATOM   7663  C  CE1 . TYR C  1 312 ? 81.937  33.241  55.627  1.00 7.96  ? 312  TYR C CE1 1 
ATOM   7664  C  CE2 . TYR C  1 312 ? 83.435  34.131  53.924  1.00 7.54  ? 312  TYR C CE2 1 
ATOM   7665  C  CZ  . TYR C  1 312 ? 82.251  34.190  54.667  1.00 9.39  ? 312  TYR C CZ  1 
ATOM   7666  O  OH  . TYR C  1 312 ? 81.333  35.192  54.450  1.00 13.38 ? 312  TYR C OH  1 
ATOM   7667  N  N   . SER C  1 313 ? 83.127  28.446  56.067  1.00 7.64  ? 313  SER C N   1 
ATOM   7668  C  CA  . SER C  1 313 ? 81.823  27.944  56.528  1.00 8.36  ? 313  SER C CA  1 
ATOM   7669  C  C   . SER C  1 313 ? 81.087  29.015  57.369  1.00 9.33  ? 313  SER C C   1 
ATOM   7670  O  O   . SER C  1 313 ? 81.591  29.504  58.417  1.00 7.91  ? 313  SER C O   1 
ATOM   7671  C  CB  . SER C  1 313 ? 81.994  26.647  57.336  1.00 8.86  ? 313  SER C CB  1 
ATOM   7672  O  OG  . SER C  1 313 ? 80.707  26.006  57.569  1.00 7.33  ? 313  SER C OG  1 
ATOM   7673  N  N   . GLU C  1 314 ? 79.911  29.408  56.886  1.00 8.36  ? 314  GLU C N   1 
ATOM   7674  C  CA  . GLU C  1 314 ? 78.999  30.216  57.693  1.00 9.13  ? 314  GLU C CA  1 
ATOM   7675  C  C   . GLU C  1 314 ? 78.317  29.347  58.765  1.00 7.36  ? 314  GLU C C   1 
ATOM   7676  O  O   . GLU C  1 314 ? 78.009  29.794  59.876  1.00 8.51  ? 314  GLU C O   1 
ATOM   7677  C  CB  . GLU C  1 314 ? 77.971  30.857  56.756  1.00 8.87  ? 314  GLU C CB  1 
ATOM   7678  C  CG  . GLU C  1 314 ? 77.076  31.901  57.338  1.00 13.66 ? 314  GLU C CG  1 
ATOM   7679  C  CD  . GLU C  1 314 ? 77.803  33.073  58.025  1.00 20.49 ? 314  GLU C CD  1 
ATOM   7680  O  OE1 . GLU C  1 314 ? 78.917  33.423  57.626  1.00 23.67 ? 314  GLU C OE1 1 
ATOM   7681  O  OE2 . GLU C  1 314 ? 77.231  33.664  58.971  1.00 23.88 ? 314  GLU C OE2 1 
ATOM   7682  N  N   . ALA C  1 315 ? 78.036  28.108  58.409  1.00 6.86  ? 315  ALA C N   1 
ATOM   7683  C  CA  . ALA C  1 315 ? 77.515  27.135  59.358  1.00 6.32  ? 315  ALA C CA  1 
ATOM   7684  C  C   . ALA C  1 315 ? 78.604  26.653  60.326  1.00 5.41  ? 315  ALA C C   1 
ATOM   7685  O  O   . ALA C  1 315 ? 79.796  26.597  59.982  1.00 7.38  ? 315  ALA C O   1 
ATOM   7686  C  CB  . ALA C  1 315 ? 76.945  25.917  58.610  1.00 4.59  ? 315  ALA C CB  1 
ATOM   7687  N  N   . TYR C  1 316 ? 78.190  26.214  61.501  1.00 4.56  ? 316  TYR C N   1 
ATOM   7688  C  CA  . TYR C  1 316 ? 79.155  25.765  62.512  1.00 5.05  ? 316  TYR C CA  1 
ATOM   7689  C  C   . TYR C  1 316 ? 79.908  24.498  62.088  1.00 6.55  ? 316  TYR C C   1 
ATOM   7690  O  O   . TYR C  1 316 ? 81.028  24.251  62.558  1.00 6.07  ? 316  TYR C O   1 
ATOM   7691  C  CB  . TYR C  1 316 ? 78.422  25.534  63.843  1.00 3.73  ? 316  TYR C CB  1 
ATOM   7692  C  CG  . TYR C  1 316 ? 78.035  26.843  64.540  1.00 3.53  ? 316  TYR C CG  1 
ATOM   7693  C  CD1 . TYR C  1 316 ? 79.001  27.896  64.707  1.00 2.00  ? 316  TYR C CD1 1 
ATOM   7694  C  CD2 . TYR C  1 316 ? 76.753  27.033  65.040  1.00 2.00  ? 316  TYR C CD2 1 
ATOM   7695  C  CE1 . TYR C  1 316 ? 78.687  29.083  65.361  1.00 6.82  ? 316  TYR C CE1 1 
ATOM   7696  C  CE2 . TYR C  1 316 ? 76.421  28.257  65.701  1.00 7.16  ? 316  TYR C CE2 1 
ATOM   7697  C  CZ  . TYR C  1 316 ? 77.394  29.263  65.846  1.00 5.63  ? 316  TYR C CZ  1 
ATOM   7698  O  OH  . TYR C  1 316 ? 77.102  30.429  66.500  1.00 7.24  ? 316  TYR C OH  1 
ATOM   7699  N  N   . PHE C  1 317 ? 79.264  23.686  61.235  1.00 6.61  ? 317  PHE C N   1 
ATOM   7700  C  CA  . PHE C  1 317 ? 79.919  22.514  60.624  1.00 6.55  ? 317  PHE C CA  1 
ATOM   7701  C  C   . PHE C  1 317 ? 79.385  22.413  59.195  1.00 9.00  ? 317  PHE C C   1 
ATOM   7702  O  O   . PHE C  1 317 ? 78.128  22.423  58.980  1.00 7.38  ? 317  PHE C O   1 
ATOM   7703  C  CB  . PHE C  1 317 ? 79.503  21.249  61.359  1.00 7.74  ? 317  PHE C CB  1 
ATOM   7704  C  CG  . PHE C  1 317 ? 80.038  19.964  60.747  1.00 8.22  ? 317  PHE C CG  1 
ATOM   7705  C  CD1 . PHE C  1 317 ? 79.320  19.294  59.770  1.00 10.23 ? 317  PHE C CD1 1 
ATOM   7706  C  CD2 . PHE C  1 317 ? 81.256  19.437  61.167  1.00 10.05 ? 317  PHE C CD2 1 
ATOM   7707  C  CE1 . PHE C  1 317 ? 79.790  18.079  59.204  1.00 9.61  ? 317  PHE C CE1 1 
ATOM   7708  C  CE2 . PHE C  1 317 ? 81.766  18.246  60.593  1.00 11.87 ? 317  PHE C CE2 1 
ATOM   7709  C  CZ  . PHE C  1 317 ? 80.998  17.547  59.628  1.00 10.62 ? 317  PHE C CZ  1 
ATOM   7710  N  N   . SER C  1 318 ? 80.289  22.327  58.225  1.00 7.39  ? 318  SER C N   1 
ATOM   7711  C  CA  . SER C  1 318 ? 79.871  22.038  56.839  1.00 7.54  ? 318  SER C CA  1 
ATOM   7712  C  C   . SER C  1 318 ? 80.684  20.908  56.281  1.00 8.33  ? 318  SER C C   1 
ATOM   7713  O  O   . SER C  1 318 ? 81.841  20.645  56.756  1.00 9.66  ? 318  SER C O   1 
ATOM   7714  C  CB  . SER C  1 318 ? 80.055  23.270  55.955  1.00 7.00  ? 318  SER C CB  1 
ATOM   7715  O  OG  . SER C  1 318 ? 79.219  24.352  56.413  1.00 5.39  ? 318  SER C OG  1 
ATOM   7716  N  N   . LYS C  1 319 ? 80.113  20.216  55.284  1.00 8.00  ? 319  LYS C N   1 
ATOM   7717  C  CA  . LYS C  1 319 ? 80.836  19.141  54.612  1.00 8.99  ? 319  LYS C CA  1 
ATOM   7718  C  C   . LYS C  1 319 ? 80.635  19.254  53.115  1.00 8.06  ? 319  LYS C C   1 
ATOM   7719  O  O   . LYS C  1 319 ? 79.480  19.328  52.668  1.00 8.18  ? 319  LYS C O   1 
ATOM   7720  C  CB  . LYS C  1 319 ? 80.298  17.738  55.020  1.00 7.32  ? 319  LYS C CB  1 
ATOM   7721  C  CG  . LYS C  1 319 ? 81.236  16.606  54.515  1.00 7.70  ? 319  LYS C CG  1 
ATOM   7722  C  CD  . LYS C  1 319 ? 80.897  15.144  54.930  1.00 10.49 ? 319  LYS C CD  1 
ATOM   7723  C  CE  . LYS C  1 319 ? 79.512  14.720  54.448  1.00 12.55 ? 319  LYS C CE  1 
ATOM   7724  N  NZ  . LYS C  1 319 ? 79.266  13.205  54.611  1.00 16.90 ? 319  LYS C NZ  1 
ATOM   7725  N  N   . VAL C  1 320 ? 81.733  19.223  52.352  1.00 8.82  ? 320  VAL C N   1 
ATOM   7726  C  CA  . VAL C  1 320 ? 81.633  19.327  50.892  1.00 8.34  ? 320  VAL C CA  1 
ATOM   7727  C  C   . VAL C  1 320 ? 82.273  18.120  50.223  1.00 9.73  ? 320  VAL C C   1 
ATOM   7728  O  O   . VAL C  1 320 ? 83.202  17.467  50.806  1.00 8.54  ? 320  VAL C O   1 
ATOM   7729  C  CB  . VAL C  1 320 ? 82.173  20.667  50.319  1.00 8.93  ? 320  VAL C CB  1 
ATOM   7730  C  CG1 . VAL C  1 320 ? 81.537  21.859  51.046  1.00 7.03  ? 320  VAL C CG1 1 
ATOM   7731  C  CG2 . VAL C  1 320 ? 83.729  20.706  50.348  1.00 9.03  ? 320  VAL C CG2 1 
ATOM   7732  N  N   . LEU C  1 321 ? 81.754  17.759  49.049  1.00 8.77  ? 321  LEU C N   1 
ATOM   7733  C  CA  . LEU C  1 321 ? 82.509  16.793  48.221  1.00 9.03  ? 321  LEU C CA  1 
ATOM   7734  C  C   . LEU C  1 321 ? 83.383  17.599  47.288  1.00 9.02  ? 321  LEU C C   1 
ATOM   7735  O  O   . LEU C  1 321 ? 82.877  18.483  46.599  1.00 9.13  ? 321  LEU C O   1 
ATOM   7736  C  CB  . LEU C  1 321 ? 81.587  15.880  47.370  1.00 8.30  ? 321  LEU C CB  1 
ATOM   7737  C  CG  . LEU C  1 321 ? 82.228  14.872  46.376  1.00 11.03 ? 321  LEU C CG  1 
ATOM   7738  C  CD1 . LEU C  1 321 ? 82.873  13.688  47.087  1.00 8.15  ? 321  LEU C CD1 1 
ATOM   7739  C  CD2 . LEU C  1 321 ? 81.189  14.340  45.471  1.00 11.06 ? 321  LEU C CD2 1 
ATOM   7740  N  N   . PHE C  1 322 ? 84.673  17.261  47.231  1.00 9.82  ? 322  PHE C N   1 
ATOM   7741  C  CA  . PHE C  1 322 ? 85.649  18.122  46.561  1.00 8.99  ? 322  PHE C CA  1 
ATOM   7742  C  C   . PHE C  1 322 ? 86.451  17.344  45.508  1.00 9.43  ? 322  PHE C C   1 
ATOM   7743  O  O   . PHE C  1 322 ? 86.992  16.249  45.784  1.00 9.32  ? 322  PHE C O   1 
ATOM   7744  C  CB  . PHE C  1 322 ? 86.621  18.736  47.610  1.00 10.04 ? 322  PHE C CB  1 
ATOM   7745  C  CG  . PHE C  1 322 ? 87.778  19.438  46.998  1.00 9.20  ? 322  PHE C CG  1 
ATOM   7746  C  CD1 . PHE C  1 322 ? 88.951  18.731  46.665  1.00 8.06  ? 322  PHE C CD1 1 
ATOM   7747  C  CD2 . PHE C  1 322 ? 87.690  20.781  46.689  1.00 9.07  ? 322  PHE C CD2 1 
ATOM   7748  C  CE1 . PHE C  1 322 ? 90.032  19.359  46.013  1.00 7.99  ? 322  PHE C CE1 1 
ATOM   7749  C  CE2 . PHE C  1 322 ? 88.747  21.412  46.028  1.00 10.21 ? 322  PHE C CE2 1 
ATOM   7750  C  CZ  . PHE C  1 322 ? 89.941  20.690  45.721  1.00 8.26  ? 322  PHE C CZ  1 
ATOM   7751  N  N   . VAL C  1 323 ? 86.575  17.905  44.313  1.00 9.06  ? 323  VAL C N   1 
ATOM   7752  C  CA  . VAL C  1 323 ? 87.413  17.269  43.272  1.00 7.59  ? 323  VAL C CA  1 
ATOM   7753  C  C   . VAL C  1 323 ? 88.406  18.274  42.719  1.00 7.66  ? 323  VAL C C   1 
ATOM   7754  O  O   . VAL C  1 323 ? 88.025  19.419  42.504  1.00 8.59  ? 323  VAL C O   1 
ATOM   7755  C  CB  . VAL C  1 323 ? 86.524  16.676  42.133  1.00 7.91  ? 323  VAL C CB  1 
ATOM   7756  C  CG1 . VAL C  1 323 ? 85.621  17.756  41.539  1.00 7.96  ? 323  VAL C CG1 1 
ATOM   7757  C  CG2 . VAL C  1 323 ? 87.412  15.973  40.998  1.00 7.58  ? 323  VAL C CG2 1 
ATOM   7758  N  N   . SER C  1 324 ? 89.654  17.854  42.453  1.00 7.46  ? 324  SER C N   1 
ATOM   7759  C  CA  . SER C  1 324 ? 90.622  18.773  41.893  1.00 6.56  ? 324  SER C CA  1 
ATOM   7760  C  C   . SER C  1 324 ? 91.386  18.105  40.764  1.00 7.40  ? 324  SER C C   1 
ATOM   7761  O  O   . SER C  1 324 ? 91.803  16.941  40.890  1.00 7.34  ? 324  SER C O   1 
ATOM   7762  C  CB  . SER C  1 324 ? 91.578  19.326  42.983  1.00 5.88  ? 324  SER C CB  1 
ATOM   7763  O  OG  . SER C  1 324 ? 92.879  19.599  42.457  1.00 6.96  ? 324  SER C OG  1 
ATOM   7764  N  N   . SER C  1 325 ? 91.587  18.851  39.673  1.00 7.34  ? 325  SER C N   1 
ATOM   7765  C  CA  . SER C  1 325 ? 92.520  18.428  38.632  1.00 8.05  ? 325  SER C CA  1 
ATOM   7766  C  C   . SER C  1 325 ? 93.933  18.747  39.080  1.00 8.49  ? 325  SER C C   1 
ATOM   7767  O  O   . SER C  1 325 ? 94.200  19.857  39.574  1.00 8.84  ? 325  SER C O   1 
ATOM   7768  C  CB  . SER C  1 325 ? 92.245  19.120  37.288  1.00 7.58  ? 325  SER C CB  1 
ATOM   7769  O  OG  . SER C  1 325 ? 93.235  18.695  36.328  1.00 9.59  ? 325  SER C OG  1 
ATOM   7770  N  N   . GLY C  1 326 ? 94.843  17.787  38.895  1.00 9.47  ? 326  GLY C N   1 
ATOM   7771  C  CA  . GLY C  1 326 ? 96.227  17.931  39.351  1.00 9.85  ? 326  GLY C CA  1 
ATOM   7772  C  C   . GLY C  1 326 ? 96.479  17.087  40.593  1.00 11.31 ? 326  GLY C C   1 
ATOM   7773  O  O   . GLY C  1 326 ? 95.548  16.502  41.135  1.00 12.66 ? 326  GLY C O   1 
ATOM   7774  N  N   . SER C  1 327 ? 97.718  17.013  41.050  1.00 10.87 ? 327  SER C N   1 
ATOM   7775  C  CA  . SER C  1 327 ? 98.031  16.128  42.195  1.00 12.63 ? 327  SER C CA  1 
ATOM   7776  C  C   . SER C  1 327 ? 98.165  16.856  43.529  1.00 12.08 ? 327  SER C C   1 
ATOM   7777  O  O   . SER C  1 327 ? 98.271  16.211  44.575  1.00 13.08 ? 327  SER C O   1 
ATOM   7778  C  CB  . SER C  1 327 ? 99.307  15.296  41.926  1.00 12.31 ? 327  SER C CB  1 
ATOM   7779  O  OG  . SER C  1 327 ? 100.479 16.134  41.917  1.00 17.43 ? 327  SER C OG  1 
ATOM   7780  N  N   . ASP C  1 328 ? 98.151  18.193  43.511  1.00 12.15 ? 328  ASP C N   1 
ATOM   7781  C  CA  . ASP C  1 328 ? 98.281  18.969  44.756  1.00 11.28 ? 328  ASP C CA  1 
ATOM   7782  C  C   . ASP C  1 328 ? 97.328  20.113  44.867  1.00 10.26 ? 328  ASP C C   1 
ATOM   7783  O  O   . ASP C  1 328 ? 97.727  21.262  45.123  1.00 8.58  ? 328  ASP C O   1 
ATOM   7784  C  CB  . ASP C  1 328 ? 99.665  19.524  44.835  1.00 12.67 ? 328  ASP C CB  1 
ATOM   7785  C  CG  . ASP C  1 328 ? 100.653 18.451  45.031  1.00 17.80 ? 328  ASP C CG  1 
ATOM   7786  O  OD1 . ASP C  1 328 ? 100.863 18.086  46.213  1.00 22.73 ? 328  ASP C OD1 1 
ATOM   7787  O  OD2 . ASP C  1 328 ? 101.205 17.876  44.062  1.00 21.57 ? 328  ASP C OD2 1 
ATOM   7788  N  N   . GLY C  1 329 ? 96.075  19.821  44.586  1.00 8.96  ? 329  GLY C N   1 
ATOM   7789  C  CA  . GLY C  1 329 ? 95.038  20.798  44.811  1.00 8.92  ? 329  GLY C CA  1 
ATOM   7790  C  C   . GLY C  1 329 ? 94.731  20.935  46.291  1.00 9.15  ? 329  GLY C C   1 
ATOM   7791  O  O   . GLY C  1 329 ? 95.465  20.429  47.138  1.00 8.65  ? 329  GLY C O   1 
ATOM   7792  N  N   . LEU C  1 330 ? 93.607  21.582  46.580  1.00 8.00  ? 330  LEU C N   1 
ATOM   7793  C  CA  . LEU C  1 330 ? 93.298  22.072  47.912  1.00 8.06  ? 330  LEU C CA  1 
ATOM   7794  C  C   . LEU C  1 330 ? 93.320  20.971  48.957  1.00 9.06  ? 330  LEU C C   1 
ATOM   7795  O  O   . LEU C  1 330 ? 93.991  21.121  49.997  1.00 7.43  ? 330  LEU C O   1 
ATOM   7796  C  CB  . LEU C  1 330 ? 91.952  22.811  47.906  1.00 6.55  ? 330  LEU C CB  1 
ATOM   7797  C  CG  . LEU C  1 330 ? 91.373  23.279  49.262  1.00 7.35  ? 330  LEU C CG  1 
ATOM   7798  C  CD1 . LEU C  1 330 ? 92.192  24.528  49.783  1.00 6.87  ? 330  LEU C CD1 1 
ATOM   7799  C  CD2 . LEU C  1 330 ? 89.862  23.599  49.130  1.00 10.00 ? 330  LEU C CD2 1 
ATOM   7800  N  N   . ASP C  1 331 ? 92.636  19.861  48.656  1.00 8.15  ? 331  ASP C N   1 
ATOM   7801  C  CA  . ASP C  1 331 ? 92.506  18.808  49.612  1.00 10.07 ? 331  ASP C CA  1 
ATOM   7802  C  C   . ASP C  1 331 ? 93.871  18.186  49.960  1.00 9.91  ? 331  ASP C C   1 
ATOM   7803  O  O   . ASP C  1 331 ? 94.130  18.006  51.143  1.00 10.69 ? 331  ASP C O   1 
ATOM   7804  C  CB  . ASP C  1 331 ? 91.422  17.772  49.233  1.00 8.22  ? 331  ASP C CB  1 
ATOM   7805  C  CG  . ASP C  1 331 ? 91.748  16.994  47.944  1.00 12.99 ? 331  ASP C CG  1 
ATOM   7806  O  OD1 . ASP C  1 331 ? 92.578  17.482  47.113  1.00 11.23 ? 331  ASP C OD1 1 
ATOM   7807  O  OD2 . ASP C  1 331 ? 91.171  15.891  47.679  1.00 9.00  ? 331  ASP C OD2 1 
ATOM   7808  N  N   . GLN C  1 332 ? 94.742  17.934  48.959  1.00 9.69  ? 332  GLN C N   1 
ATOM   7809  C  CA  . GLN C  1 332 ? 96.078  17.422  49.235  1.00 10.69 ? 332  GLN C CA  1 
ATOM   7810  C  C   . GLN C  1 332 ? 96.880  18.447  50.036  1.00 10.50 ? 332  GLN C C   1 
ATOM   7811  O  O   . GLN C  1 332 ? 97.674  18.103  50.901  1.00 7.63  ? 332  GLN C O   1 
ATOM   7812  C  CB  . GLN C  1 332 ? 96.836  17.107  47.929  1.00 11.33 ? 332  GLN C CB  1 
ATOM   7813  C  CG  . GLN C  1 332 ? 98.101  16.221  48.167  1.00 13.96 ? 332  GLN C CG  1 
ATOM   7814  C  CD  . GLN C  1 332 ? 97.728  14.855  48.798  1.00 14.99 ? 332  GLN C CD  1 
ATOM   7815  O  OE1 . GLN C  1 332 ? 96.830  14.160  48.302  1.00 15.24 ? 332  GLN C OE1 1 
ATOM   7816  N  NE2 . GLN C  1 332 ? 98.367  14.516  49.915  1.00 12.92 ? 332  GLN C NE2 1 
ATOM   7817  N  N   . ASN C  1 333 ? 96.660  19.716  49.736  1.00 10.51 ? 333  ASN C N   1 
ATOM   7818  C  CA  . ASN C  1 333 ? 97.413  20.779  50.421  1.00 10.65 ? 333  ASN C CA  1 
ATOM   7819  C  C   . ASN C  1 333 ? 97.003  20.807  51.903  1.00 10.29 ? 333  ASN C C   1 
ATOM   7820  O  O   . ASN C  1 333 ? 97.881  20.920  52.793  1.00 9.31  ? 333  ASN C O   1 
ATOM   7821  C  CB  . ASN C  1 333 ? 97.135  22.120  49.751  1.00 10.26 ? 333  ASN C CB  1 
ATOM   7822  C  CG  . ASN C  1 333 ? 97.976  23.267  50.336  1.00 16.34 ? 333  ASN C CG  1 
ATOM   7823  O  OD1 . ASN C  1 333 ? 97.741  23.724  51.471  1.00 21.97 ? 333  ASN C OD1 1 
ATOM   7824  N  ND2 . ASN C  1 333 ? 98.934  23.755  49.550  1.00 12.83 ? 333  ASN C ND2 1 
ATOM   7825  N  N   . LEU C  1 334 ? 95.687  20.683  52.167  1.00 7.53  ? 334  LEU C N   1 
ATOM   7826  C  CA  . LEU C  1 334 ? 95.206  20.634  53.543  1.00 8.12  ? 334  LEU C CA  1 
ATOM   7827  C  C   . LEU C  1 334 ? 95.738  19.399  54.287  1.00 8.64  ? 334  LEU C C   1 
ATOM   7828  O  O   . LEU C  1 334 ? 96.159  19.518  55.434  1.00 8.48  ? 334  LEU C O   1 
ATOM   7829  C  CB  . LEU C  1 334 ? 93.688  20.692  53.622  1.00 7.97  ? 334  LEU C CB  1 
ATOM   7830  C  CG  . LEU C  1 334 ? 93.112  22.023  53.120  1.00 7.11  ? 334  LEU C CG  1 
ATOM   7831  C  CD1 . LEU C  1 334 ? 91.576  22.014  53.081  1.00 6.46  ? 334  LEU C CD1 1 
ATOM   7832  C  CD2 . LEU C  1 334 ? 93.645  23.167  53.966  1.00 8.37  ? 334  LEU C CD2 1 
ATOM   7833  N  N   . VAL C  1 335 ? 95.705  18.232  53.641  1.00 8.58  ? 335  VAL C N   1 
ATOM   7834  C  CA  . VAL C  1 335 ? 96.298  17.004  54.229  1.00 8.88  ? 335  VAL C CA  1 
ATOM   7835  C  C   . VAL C  1 335 ? 97.755  17.190  54.606  1.00 9.26  ? 335  VAL C C   1 
ATOM   7836  O  O   . VAL C  1 335 ? 98.150  16.849  55.727  1.00 8.74  ? 335  VAL C O   1 
ATOM   7837  C  CB  . VAL C  1 335 ? 96.165  15.767  53.249  1.00 9.68  ? 335  VAL C CB  1 
ATOM   7838  C  CG1 . VAL C  1 335 ? 97.110  14.588  53.658  1.00 9.25  ? 335  VAL C CG1 1 
ATOM   7839  C  CG2 . VAL C  1 335 ? 94.729  15.301  53.200  1.00 9.12  ? 335  VAL C CG2 1 
ATOM   7840  N  N   . ASN C  1 336 ? 98.544  17.681  53.643  1.00 8.46  ? 336  ASN C N   1 
ATOM   7841  C  CA  . ASN C  1 336 ? 99.983  17.847  53.786  1.00 9.09  ? 336  ASN C CA  1 
ATOM   7842  C  C   . ASN C  1 336 ? 100.295 18.790  54.904  1.00 8.16  ? 336  ASN C C   1 
ATOM   7843  O  O   . ASN C  1 336 ? 101.264 18.605  55.601  1.00 7.91  ? 336  ASN C O   1 
ATOM   7844  C  CB  . ASN C  1 336 ? 100.635 18.359  52.487  1.00 9.65  ? 336  ASN C CB  1 
ATOM   7845  C  CG  . ASN C  1 336 ? 100.714 17.284  51.369  1.00 14.21 ? 336  ASN C CG  1 
ATOM   7846  O  OD1 . ASN C  1 336 ? 101.001 17.614  50.186  1.00 16.78 ? 336  ASN C OD1 1 
ATOM   7847  N  ND2 . ASN C  1 336 ? 100.460 16.008  51.729  1.00 11.42 ? 336  ASN C ND2 1 
ATOM   7848  N  N   . GLY C  1 337 ? 99.449  19.801  55.103  1.00 7.47  ? 337  GLY C N   1 
ATOM   7849  C  CA  . GLY C  1 337 ? 99.682  20.719  56.196  1.00 8.21  ? 337  GLY C CA  1 
ATOM   7850  C  C   . GLY C  1 337 ? 98.984  20.312  57.495  1.00 8.35  ? 337  GLY C C   1 
ATOM   7851  O  O   . GLY C  1 337 ? 98.976  21.104  58.451  1.00 7.82  ? 337  GLY C O   1 
ATOM   7852  N  N   . GLY C  1 338 ? 98.400  19.104  57.517  1.00 8.26  ? 338  GLY C N   1 
ATOM   7853  C  CA  . GLY C  1 338 ? 97.550  18.649  58.612  1.00 8.59  ? 338  GLY C CA  1 
ATOM   7854  C  C   . GLY C  1 338 ? 98.128  17.417  59.287  1.00 9.40  ? 338  GLY C C   1 
ATOM   7855  O  O   . GLY C  1 338 ? 99.351  17.121  59.150  1.00 8.76  ? 338  GLY C O   1 
ATOM   7856  N  N   . GLU C  1 339 ? 97.301  16.717  60.060  1.00 8.49  ? 339  GLU C N   1 
ATOM   7857  C  CA  . GLU C  1 339 ? 97.782  15.505  60.788  1.00 9.91  ? 339  GLU C CA  1 
ATOM   7858  C  C   . GLU C  1 339 ? 96.760  14.359  60.697  1.00 9.55  ? 339  GLU C C   1 
ATOM   7859  O  O   . GLU C  1 339 ? 95.573  14.597  60.478  1.00 7.36  ? 339  GLU C O   1 
ATOM   7860  C  CB  . GLU C  1 339 ? 98.070  15.823  62.262  1.00 10.08 ? 339  GLU C CB  1 
ATOM   7861  C  CG  . GLU C  1 339 ? 96.806  16.094  63.089  1.00 14.95 ? 339  GLU C CG  1 
ATOM   7862  C  CD  . GLU C  1 339 ? 97.106  16.772  64.444  1.00 20.61 ? 339  GLU C CD  1 
ATOM   7863  O  OE1 . GLU C  1 339 ? 97.757  16.132  65.301  1.00 23.07 ? 339  GLU C OE1 1 
ATOM   7864  O  OE2 . GLU C  1 339 ? 96.697  17.940  64.662  1.00 22.95 ? 339  GLU C OE2 1 
ATOM   7865  N  N   . GLU C  1 340 ? 97.221  13.119  60.871  1.00 8.71  ? 340  GLU C N   1 
ATOM   7866  C  CA  . GLU C  1 340 ? 96.283  11.995  60.885  1.00 9.67  ? 340  GLU C CA  1 
ATOM   7867  C  C   . GLU C  1 340 ? 95.237  12.245  61.975  1.00 8.66  ? 340  GLU C C   1 
ATOM   7868  O  O   . GLU C  1 340 ? 95.560  12.738  63.047  1.00 6.39  ? 340  GLU C O   1 
ATOM   7869  C  CB  . GLU C  1 340 ? 97.052  10.726  61.176  1.00 9.99  ? 340  GLU C CB  1 
ATOM   7870  C  CG  . GLU C  1 340 ? 97.658  10.157  59.926  1.00 14.65 ? 340  GLU C CG  1 
ATOM   7871  C  CD  . GLU C  1 340 ? 98.348  8.819   60.158  1.00 23.49 ? 340  GLU C CD  1 
ATOM   7872  O  OE1 . GLU C  1 340 ? 98.907  8.614   61.263  1.00 22.46 ? 340  GLU C OE1 1 
ATOM   7873  O  OE2 . GLU C  1 340 ? 98.321  7.988   59.212  1.00 26.94 ? 340  GLU C OE2 1 
ATOM   7874  N  N   . TRP C  1 341 ? 93.979  11.913  61.707  1.00 8.86  ? 341  TRP C N   1 
ATOM   7875  C  CA  . TRP C  1 341 ? 92.928  12.270  62.643  1.00 9.59  ? 341  TRP C CA  1 
ATOM   7876  C  C   . TRP C  1 341 ? 91.849  11.196  62.696  1.00 10.04 ? 341  TRP C C   1 
ATOM   7877  O  O   . TRP C  1 341 ? 91.437  10.679  61.670  1.00 10.28 ? 341  TRP C O   1 
ATOM   7878  C  CB  . TRP C  1 341 ? 92.300  13.583  62.162  1.00 8.20  ? 341  TRP C CB  1 
ATOM   7879  C  CG  . TRP C  1 341 ? 91.271  14.201  63.120  1.00 9.11  ? 341  TRP C CG  1 
ATOM   7880  C  CD1 . TRP C  1 341 ? 89.921  14.445  62.864  1.00 10.76 ? 341  TRP C CD1 1 
ATOM   7881  C  CD2 . TRP C  1 341 ? 91.508  14.683  64.442  1.00 10.69 ? 341  TRP C CD2 1 
ATOM   7882  N  NE1 . TRP C  1 341 ? 89.340  15.037  63.959  1.00 8.66  ? 341  TRP C NE1 1 
ATOM   7883  C  CE2 . TRP C  1 341 ? 90.271  15.183  64.941  1.00 9.87  ? 341  TRP C CE2 1 
ATOM   7884  C  CE3 . TRP C  1 341 ? 92.639  14.754  65.265  1.00 10.96 ? 341  TRP C CE3 1 
ATOM   7885  C  CZ2 . TRP C  1 341 ? 90.148  15.727  66.216  1.00 13.15 ? 341  TRP C CZ2 1 
ATOM   7886  C  CZ3 . TRP C  1 341 ? 92.514  15.309  66.530  1.00 15.41 ? 341  TRP C CZ3 1 
ATOM   7887  C  CH2 . TRP C  1 341 ? 91.283  15.790  66.991  1.00 14.29 ? 341  TRP C CH2 1 
ATOM   7888  N  N   . SER C  1 342 ? 91.345  10.887  63.881  1.00 11.10 ? 342  SER C N   1 
ATOM   7889  C  CA  . SER C  1 342 ? 90.489  9.700   64.024  1.00 10.60 ? 342  SER C CA  1 
ATOM   7890  C  C   . SER C  1 342 ? 88.990  9.943   64.170  1.00 12.22 ? 342  SER C C   1 
ATOM   7891  O  O   . SER C  1 342 ? 88.239  9.008   64.486  1.00 12.89 ? 342  SER C O   1 
ATOM   7892  C  CB  . SER C  1 342 ? 90.976  8.871   65.216  1.00 11.65 ? 342  SER C CB  1 
ATOM   7893  O  OG  A SER C  1 342 ? 92.373  8.626   65.112  0.50 13.64 ? 342  SER C OG  1 
ATOM   7894  O  OG  B SER C  1 342 ? 90.749  9.576   66.427  0.50 8.01  ? 342  SER C OG  1 
ATOM   7895  N  N   . SER C  1 343 ? 88.533  11.161  63.898  1.00 10.82 ? 343  SER C N   1 
ATOM   7896  C  CA  . SER C  1 343 ? 87.167  11.557  64.236  1.00 10.77 ? 343  SER C CA  1 
ATOM   7897  C  C   . SER C  1 343 ? 86.576  12.336  63.076  1.00 10.06 ? 343  SER C C   1 
ATOM   7898  O  O   . SER C  1 343 ? 87.306  13.049  62.375  1.00 10.34 ? 343  SER C O   1 
ATOM   7899  C  CB  . SER C  1 343 ? 87.111  12.417  65.514  1.00 11.43 ? 343  SER C CB  1 
ATOM   7900  O  OG  . SER C  1 343 ? 85.740  12.652  65.878  1.00 13.23 ? 343  SER C OG  1 
ATOM   7901  N  N   . VAL C  1 344 ? 85.273  12.203  62.870  1.00 9.40  ? 344  VAL C N   1 
ATOM   7902  C  CA  . VAL C  1 344 ? 84.547  13.124  61.986  1.00 7.40  ? 344  VAL C CA  1 
ATOM   7903  C  C   . VAL C  1 344 ? 84.304  14.546  62.534  1.00 8.19  ? 344  VAL C C   1 
ATOM   7904  O  O   . VAL C  1 344 ? 83.852  15.434  61.797  1.00 7.66  ? 344  VAL C O   1 
ATOM   7905  C  CB  . VAL C  1 344 ? 83.183  12.506  61.549  1.00 8.46  ? 344  VAL C CB  1 
ATOM   7906  C  CG1 . VAL C  1 344 ? 83.427  11.359  60.618  1.00 6.79  ? 344  VAL C CG1 1 
ATOM   7907  C  CG2 . VAL C  1 344 ? 82.342  12.122  62.772  1.00 7.50  ? 344  VAL C CG2 1 
ATOM   7908  N  N   . SER C  1 345 ? 84.585  14.747  63.813  1.00 7.34  ? 345  SER C N   1 
ATOM   7909  C  CA  . SER C  1 345 ? 84.351  16.025  64.477  1.00 7.74  ? 345  SER C CA  1 
ATOM   7910  C  C   . SER C  1 345 ? 85.716  16.628  64.743  1.00 6.42  ? 345  SER C C   1 
ATOM   7911  O  O   . SER C  1 345 ? 86.667  15.874  64.920  1.00 7.19  ? 345  SER C O   1 
ATOM   7912  C  CB  . SER C  1 345 ? 83.711  15.775  65.841  1.00 8.38  ? 345  SER C CB  1 
ATOM   7913  O  OG  . SER C  1 345 ? 82.307  15.679  65.656  1.00 11.91 ? 345  SER C OG  1 
ATOM   7914  N  N   . PHE C  1 346 ? 85.794  17.955  64.789  1.00 5.85  ? 346  PHE C N   1 
ATOM   7915  C  CA  . PHE C  1 346 ? 87.048  18.662  65.110  1.00 6.92  ? 346  PHE C CA  1 
ATOM   7916  C  C   . PHE C  1 346 ? 87.053  18.955  66.603  1.00 6.20  ? 346  PHE C C   1 
ATOM   7917  O  O   . PHE C  1 346 ? 86.068  18.671  67.310  1.00 6.80  ? 346  PHE C O   1 
ATOM   7918  C  CB  . PHE C  1 346 ? 87.207  19.938  64.243  1.00 6.75  ? 346  PHE C CB  1 
ATOM   7919  C  CG  . PHE C  1 346 ? 85.925  20.778  64.145  1.00 7.95  ? 346  PHE C CG  1 
ATOM   7920  C  CD1 . PHE C  1 346 ? 85.596  21.688  65.152  1.00 6.96  ? 346  PHE C CD1 1 
ATOM   7921  C  CD2 . PHE C  1 346 ? 85.116  20.708  63.023  1.00 9.82  ? 346  PHE C CD2 1 
ATOM   7922  C  CE1 . PHE C  1 346 ? 84.438  22.482  65.069  1.00 8.76  ? 346  PHE C CE1 1 
ATOM   7923  C  CE2 . PHE C  1 346 ? 83.933  21.479  62.924  1.00 8.13  ? 346  PHE C CE2 1 
ATOM   7924  C  CZ  . PHE C  1 346 ? 83.593  22.364  63.977  1.00 5.92  ? 346  PHE C CZ  1 
ATOM   7925  N  N   . PRO C  1 347 ? 88.192  19.413  67.127  1.00 6.63  ? 347  PRO C N   1 
ATOM   7926  C  CA  . PRO C  1 347 ? 88.300  19.682  68.560  1.00 6.35  ? 347  PRO C CA  1 
ATOM   7927  C  C   . PRO C  1 347 ? 87.279  20.744  69.049  1.00 5.99  ? 347  PRO C C   1 
ATOM   7928  O  O   . PRO C  1 347 ? 86.920  21.642  68.267  1.00 5.68  ? 347  PRO C O   1 
ATOM   7929  C  CB  . PRO C  1 347 ? 89.743  20.191  68.717  1.00 5.55  ? 347  PRO C CB  1 
ATOM   7930  C  CG  . PRO C  1 347 ? 90.525  19.509  67.504  1.00 6.50  ? 347  PRO C CG  1 
ATOM   7931  C  CD  . PRO C  1 347 ? 89.464  19.600  66.395  1.00 5.15  ? 347  PRO C CD  1 
ATOM   7932  N  N   . ALA C  1 348 ? 86.939  20.663  70.332  1.00 3.99  ? 348  ALA C N   1 
ATOM   7933  C  CA  . ALA C  1 348 ? 85.960  21.524  70.973  1.00 5.19  ? 348  ALA C CA  1 
ATOM   7934  C  C   . ALA C  1 348 ? 86.571  22.886  71.349  1.00 5.47  ? 348  ALA C C   1 
ATOM   7935  O  O   . ALA C  1 348 ? 85.854  23.861  71.650  1.00 6.41  ? 348  ALA C O   1 
ATOM   7936  C  CB  . ALA C  1 348 ? 85.390  20.820  72.168  1.00 3.86  ? 348  ALA C CB  1 
ATOM   7937  N  N   . ASP C  1 349 ? 87.901  22.960  71.269  1.00 5.86  ? 349  ASP C N   1 
ATOM   7938  C  CA  . ASP C  1 349 ? 88.653  24.170  71.590  1.00 6.75  ? 349  ASP C CA  1 
ATOM   7939  C  C   . ASP C  1 349 ? 89.489  24.584  70.393  1.00 6.80  ? 349  ASP C C   1 
ATOM   7940  O  O   . ASP C  1 349 ? 89.982  23.736  69.645  1.00 7.55  ? 349  ASP C O   1 
ATOM   7941  C  CB  . ASP C  1 349 ? 89.588  23.926  72.793  1.00 7.71  ? 349  ASP C CB  1 
ATOM   7942  C  CG  . ASP C  1 349 ? 88.862  23.355  74.016  1.00 9.22  ? 349  ASP C CG  1 
ATOM   7943  O  OD1 . ASP C  1 349 ? 87.942  24.021  74.527  1.00 4.20  ? 349  ASP C OD1 1 
ATOM   7944  O  OD2 . ASP C  1 349 ? 89.187  22.267  74.538  1.00 11.95 ? 349  ASP C OD2 1 
ATOM   7945  N  N   . TRP C  1 350 ? 89.664  25.882  70.219  1.00 7.67  ? 350  TRP C N   1 
ATOM   7946  C  CA  . TRP C  1 350 ? 90.518  26.382  69.165  1.00 8.26  ? 350  TRP C CA  1 
ATOM   7947  C  C   . TRP C  1 350 ? 91.983  26.134  69.538  1.00 9.23  ? 350  TRP C C   1 
ATOM   7948  O  O   . TRP C  1 350 ? 92.300  25.737  70.669  1.00 9.09  ? 350  TRP C O   1 
ATOM   7949  C  CB  . TRP C  1 350 ? 90.302  27.878  68.943  1.00 7.69  ? 350  TRP C CB  1 
ATOM   7950  C  CG  . TRP C  1 350 ? 88.925  28.222  68.450  1.00 8.33  ? 350  TRP C CG  1 
ATOM   7951  C  CD1 . TRP C  1 350 ? 88.018  28.989  69.088  1.00 9.10  ? 350  TRP C CD1 1 
ATOM   7952  C  CD2 . TRP C  1 350 ? 88.332  27.855  67.190  1.00 7.19  ? 350  TRP C CD2 1 
ATOM   7953  N  NE1 . TRP C  1 350 ? 86.879  29.123  68.333  1.00 9.48  ? 350  TRP C NE1 1 
ATOM   7954  C  CE2 . TRP C  1 350 ? 87.037  28.426  67.161  1.00 8.60  ? 350  TRP C CE2 1 
ATOM   7955  C  CE3 . TRP C  1 350 ? 88.768  27.102  66.078  1.00 7.42  ? 350  TRP C CE3 1 
ATOM   7956  C  CZ2 . TRP C  1 350 ? 86.156  28.266  66.085  1.00 8.70  ? 350  TRP C CZ2 1 
ATOM   7957  C  CZ3 . TRP C  1 350 ? 87.885  26.938  64.989  1.00 8.97  ? 350  TRP C CZ3 1 
ATOM   7958  C  CH2 . TRP C  1 350 ? 86.581  27.516  65.011  1.00 9.29  ? 350  TRP C CH2 1 
ATOM   7959  O  OXT . TRP C  1 350 ? 92.794  26.360  68.652  1.00 10.74 ? 350  TRP C OXT 1 
ATOM   7960  N  N   . SER D  1 4   ? 65.162  10.337  -22.977 1.00 25.05 ? 4    SER D N   1 
ATOM   7961  C  CA  . SER D  1 4   ? 66.554  10.163  -23.564 1.00 23.92 ? 4    SER D CA  1 
ATOM   7962  C  C   . SER D  1 4   ? 67.198  11.531  -23.837 1.00 20.19 ? 4    SER D C   1 
ATOM   7963  O  O   . SER D  1 4   ? 67.889  11.759  -24.877 1.00 22.25 ? 4    SER D O   1 
ATOM   7964  C  CB  . SER D  1 4   ? 66.467  9.292   -24.843 1.00 25.60 ? 4    SER D CB  1 
ATOM   7965  O  OG  . SER D  1 4   ? 67.759  8.879   -25.299 1.00 29.97 ? 4    SER D OG  1 
ATOM   7966  N  N   . LEU D  1 5   ? 66.988  12.427  -22.889 1.00 16.41 ? 5    LEU D N   1 
ATOM   7967  C  CA  . LEU D  1 5   ? 67.614  13.776  -22.881 1.00 13.28 ? 5    LEU D CA  1 
ATOM   7968  C  C   . LEU D  1 5   ? 69.147  13.792  -22.950 1.00 12.00 ? 5    LEU D C   1 
ATOM   7969  O  O   . LEU D  1 5   ? 69.748  14.744  -23.460 1.00 8.62  ? 5    LEU D O   1 
ATOM   7970  C  CB  . LEU D  1 5   ? 67.282  14.430  -21.602 1.00 14.09 ? 5    LEU D CB  1 
ATOM   7971  C  CG  . LEU D  1 5   ? 67.257  15.935  -21.418 1.00 13.48 ? 5    LEU D CG  1 
ATOM   7972  C  CD1 . LEU D  1 5   ? 66.408  16.629  -22.487 1.00 9.49  ? 5    LEU D CD1 1 
ATOM   7973  C  CD2 . LEU D  1 5   ? 66.677  16.208  -20.036 1.00 14.37 ? 5    LEU D CD2 1 
ATOM   7974  N  N   . ILE D  1 6   ? 69.757  12.781  -22.351 1.00 8.81  ? 6    ILE D N   1 
ATOM   7975  C  CA  . ILE D  1 6   ? 71.194  12.764  -22.220 1.00 10.11 ? 6    ILE D CA  1 
ATOM   7976  C  C   . ILE D  1 6   ? 71.842  12.268  -23.514 1.00 10.00 ? 6    ILE D C   1 
ATOM   7977  O  O   . ILE D  1 6   ? 71.385  11.236  -24.082 1.00 9.73  ? 6    ILE D O   1 
ATOM   7978  C  CB  . ILE D  1 6   ? 71.608  11.912  -20.980 1.00 10.60 ? 6    ILE D CB  1 
ATOM   7979  C  CG1 . ILE D  1 6   ? 71.119  12.658  -19.713 1.00 13.38 ? 6    ILE D CG1 1 
ATOM   7980  C  CG2 . ILE D  1 6   ? 73.151  11.821  -20.921 1.00 11.95 ? 6    ILE D CG2 1 
ATOM   7981  C  CD1 . ILE D  1 6   ? 71.280  11.957  -18.377 1.00 18.36 ? 6    ILE D CD1 1 
ATOM   7982  N  N   . VAL D  1 7   ? 72.907  12.972  -23.938 1.00 8.14  ? 7    VAL D N   1 
ATOM   7983  C  CA  . VAL D  1 7   ? 73.697  12.682  -25.135 1.00 7.70  ? 7    VAL D CA  1 
ATOM   7984  C  C   . VAL D  1 7   ? 75.193  12.707  -24.829 1.00 7.39  ? 7    VAL D C   1 
ATOM   7985  O  O   . VAL D  1 7   ? 75.599  13.368  -23.885 1.00 7.92  ? 7    VAL D O   1 
ATOM   7986  C  CB  . VAL D  1 7   ? 73.393  13.701  -26.301 1.00 7.29  ? 7    VAL D CB  1 
ATOM   7987  C  CG1 . VAL D  1 7   ? 71.934  13.563  -26.751 1.00 7.71  ? 7    VAL D CG1 1 
ATOM   7988  C  CG2 . VAL D  1 7   ? 73.738  15.212  -25.922 1.00 7.35  ? 7    VAL D CG2 1 
ATOM   7989  N  N   . GLU D  1 8   ? 75.988  12.017  -25.637 1.00 7.27  ? 8    GLU D N   1 
ATOM   7990  C  CA  . GLU D  1 8   ? 77.427  11.879  -25.381 1.00 7.91  ? 8    GLU D CA  1 
ATOM   7991  C  C   . GLU D  1 8   ? 78.176  12.907  -26.260 1.00 7.42  ? 8    GLU D C   1 
ATOM   7992  O  O   . GLU D  1 8   ? 79.321  13.236  -25.981 1.00 5.94  ? 8    GLU D O   1 
ATOM   7993  C  CB  . GLU D  1 8   ? 77.900  10.429  -25.658 1.00 7.22  ? 8    GLU D CB  1 
ATOM   7994  C  CG  A GLU D  1 8   ? 79.367  10.122  -25.429 0.50 8.57  ? 8    GLU D CG  1 
ATOM   7995  C  CG  B GLU D  1 8   ? 77.435  9.303   -24.706 0.50 5.73  ? 8    GLU D CG  1 
ATOM   7996  C  CD  A GLU D  1 8   ? 79.852  10.248  -23.988 0.50 5.33  ? 8    GLU D CD  1 
ATOM   7997  C  CD  B GLU D  1 8   ? 77.517  9.597   -23.201 0.50 8.41  ? 8    GLU D CD  1 
ATOM   7998  O  OE1 A GLU D  1 8   ? 79.036  10.174  -23.016 0.50 9.94  ? 8    GLU D OE1 1 
ATOM   7999  O  OE1 B GLU D  1 8   ? 78.459  10.285  -22.742 0.50 9.50  ? 8    GLU D OE1 1 
ATOM   8000  O  OE2 A GLU D  1 8   ? 81.057  10.403  -23.831 0.50 2.00  ? 8    GLU D OE2 1 
ATOM   8001  O  OE2 B GLU D  1 8   ? 76.643  9.102   -22.433 0.50 5.36  ? 8    GLU D OE2 1 
ATOM   8002  N  N   . ASP D  1 9   ? 77.534  13.344  -27.340 1.00 6.53  ? 9    ASP D N   1 
ATOM   8003  C  CA  . ASP D  1 9   ? 78.072  14.375  -28.219 1.00 8.01  ? 9    ASP D CA  1 
ATOM   8004  C  C   . ASP D  1 9   ? 76.882  15.280  -28.509 1.00 9.07  ? 9    ASP D C   1 
ATOM   8005  O  O   . ASP D  1 9   ? 75.725  14.799  -28.537 1.00 8.53  ? 9    ASP D O   1 
ATOM   8006  C  CB  . ASP D  1 9   ? 78.564  13.805  -29.585 1.00 7.28  ? 9    ASP D CB  1 
ATOM   8007  C  CG  . ASP D  1 9   ? 79.722  12.834  -29.452 1.00 9.72  ? 9    ASP D CG  1 
ATOM   8008  O  OD1 . ASP D  1 9   ? 80.909  13.269  -29.337 1.00 8.75  ? 9    ASP D OD1 1 
ATOM   8009  O  OD2 . ASP D  1 9   ? 79.540  11.594  -29.479 1.00 9.16  ? 9    ASP D OD2 1 
ATOM   8010  N  N   . ALA D  1 10  ? 77.133  16.576  -28.718 1.00 8.62  ? 10   ALA D N   1 
ATOM   8011  C  CA  . ALA D  1 10  ? 76.028  17.486  -29.019 1.00 9.17  ? 10   ALA D CA  1 
ATOM   8012  C  C   . ALA D  1 10  ? 75.351  17.000  -30.310 1.00 9.49  ? 10   ALA D C   1 
ATOM   8013  O  O   . ALA D  1 10  ? 76.029  16.562  -31.238 1.00 9.85  ? 10   ALA D O   1 
ATOM   8014  C  CB  . ALA D  1 10  ? 76.540  18.951  -29.189 1.00 9.60  ? 10   ALA D CB  1 
ATOM   8015  N  N   . PRO D  1 11  ? 74.029  17.046  -30.373 1.00 9.55  ? 11   PRO D N   1 
ATOM   8016  C  CA  . PRO D  1 11  ? 73.296  16.621  -31.581 1.00 9.60  ? 11   PRO D CA  1 
ATOM   8017  C  C   . PRO D  1 11  ? 73.569  17.479  -32.839 1.00 10.46 ? 11   PRO D C   1 
ATOM   8018  O  O   . PRO D  1 11  ? 74.040  18.621  -32.758 1.00 11.23 ? 11   PRO D O   1 
ATOM   8019  C  CB  . PRO D  1 11  ? 71.830  16.750  -31.163 1.00 8.79  ? 11   PRO D CB  1 
ATOM   8020  C  CG  . PRO D  1 11  ? 71.887  16.694  -29.654 1.00 9.73  ? 11   PRO D CG  1 
ATOM   8021  C  CD  . PRO D  1 11  ? 73.126  17.454  -29.272 1.00 9.83  ? 11   PRO D CD  1 
ATOM   8022  N  N   . ASP D  1 12  ? 73.238  16.930  -34.004 1.00 10.26 ? 12   ASP D N   1 
ATOM   8023  C  CA  . ASP D  1 12  ? 73.434  17.621  -35.267 1.00 10.94 ? 12   ASP D CA  1 
ATOM   8024  C  C   . ASP D  1 12  ? 72.225  18.490  -35.643 1.00 10.16 ? 12   ASP D C   1 
ATOM   8025  O  O   . ASP D  1 12  ? 72.148  19.011  -36.772 1.00 9.56  ? 12   ASP D O   1 
ATOM   8026  C  CB  . ASP D  1 12  ? 73.709  16.588  -36.385 1.00 11.75 ? 12   ASP D CB  1 
ATOM   8027  C  CG  . ASP D  1 12  ? 72.540  15.598  -36.597 1.00 16.83 ? 12   ASP D CG  1 
ATOM   8028  O  OD1 . ASP D  1 12  ? 71.399  15.914  -36.175 1.00 15.60 ? 12   ASP D OD1 1 
ATOM   8029  O  OD2 . ASP D  1 12  ? 72.683  14.463  -37.132 1.00 18.20 ? 12   ASP D OD2 1 
ATOM   8030  N  N   . HIS D  1 13  ? 71.244  18.593  -34.739 1.00 8.85  ? 13   HIS D N   1 
ATOM   8031  C  CA  . HIS D  1 13  ? 70.059  19.442  -35.003 1.00 8.62  ? 13   HIS D CA  1 
ATOM   8032  C  C   . HIS D  1 13  ? 69.588  20.017  -33.692 1.00 8.28  ? 13   HIS D C   1 
ATOM   8033  O  O   . HIS D  1 13  ? 70.020  19.565  -32.647 1.00 5.67  ? 13   HIS D O   1 
ATOM   8034  C  CB  . HIS D  1 13  ? 68.901  18.668  -35.662 1.00 9.98  ? 13   HIS D CB  1 
ATOM   8035  C  CG  . HIS D  1 13  ? 68.428  17.517  -34.835 1.00 9.47  ? 13   HIS D CG  1 
ATOM   8036  N  ND1 . HIS D  1 13  ? 69.185  16.375  -34.664 1.00 12.14 ? 13   HIS D ND1 1 
ATOM   8037  C  CD2 . HIS D  1 13  ? 67.295  17.334  -34.105 1.00 14.08 ? 13   HIS D CD2 1 
ATOM   8038  C  CE1 . HIS D  1 13  ? 68.528  15.523  -33.887 1.00 13.12 ? 13   HIS D CE1 1 
ATOM   8039  N  NE2 . HIS D  1 13  ? 67.397  16.097  -33.494 1.00 10.43 ? 13   HIS D NE2 1 
ATOM   8040  N  N   . VAL D  1 14  ? 68.723  21.030  -33.742 1.00 8.15  ? 14   VAL D N   1 
ATOM   8041  C  CA  . VAL D  1 14  ? 68.261  21.663  -32.502 1.00 9.54  ? 14   VAL D CA  1 
ATOM   8042  C  C   . VAL D  1 14  ? 67.293  20.709  -31.794 1.00 9.15  ? 14   VAL D C   1 
ATOM   8043  O  O   . VAL D  1 14  ? 66.310  20.292  -32.377 1.00 9.49  ? 14   VAL D O   1 
ATOM   8044  C  CB  . VAL D  1 14  ? 67.529  23.008  -32.804 1.00 10.72 ? 14   VAL D CB  1 
ATOM   8045  C  CG1 . VAL D  1 14  ? 66.848  23.542  -31.551 1.00 11.10 ? 14   VAL D CG1 1 
ATOM   8046  C  CG2 . VAL D  1 14  ? 68.508  24.028  -33.279 1.00 11.79 ? 14   VAL D CG2 1 
ATOM   8047  N  N   . ARG D  1 15  ? 67.567  20.361  -30.543 1.00 8.61  ? 15   ARG D N   1 
ATOM   8048  C  CA  . ARG D  1 15  ? 66.585  19.633  -29.733 1.00 9.18  ? 15   ARG D CA  1 
ATOM   8049  C  C   . ARG D  1 15  ? 66.915  19.875  -28.248 1.00 8.94  ? 15   ARG D C   1 
ATOM   8050  O  O   . ARG D  1 15  ? 68.036  20.253  -27.935 1.00 10.22 ? 15   ARG D O   1 
ATOM   8051  C  CB  . ARG D  1 15  ? 66.671  18.122  -30.038 1.00 8.70  ? 15   ARG D CB  1 
ATOM   8052  C  CG  . ARG D  1 15  ? 68.118  17.564  -29.986 1.00 7.58  ? 15   ARG D CG  1 
ATOM   8053  C  CD  . ARG D  1 15  ? 68.233  16.034  -29.733 1.00 7.65  ? 15   ARG D CD  1 
ATOM   8054  N  NE  . ARG D  1 15  ? 68.093  15.718  -28.297 1.00 8.87  ? 15   ARG D NE  1 
ATOM   8055  C  CZ  . ARG D  1 15  ? 68.249  14.506  -27.762 1.00 10.10 ? 15   ARG D CZ  1 
ATOM   8056  N  NH1 . ARG D  1 15  ? 68.551  13.470  -28.529 1.00 8.49  ? 15   ARG D NH1 1 
ATOM   8057  N  NH2 . ARG D  1 15  ? 68.119  14.344  -26.447 1.00 11.44 ? 15   ARG D NH2 1 
ATOM   8058  N  N   . PRO D  1 16  ? 65.986  19.574  -27.336 1.00 8.72  ? 16   PRO D N   1 
ATOM   8059  C  CA  . PRO D  1 16  ? 66.315  19.606  -25.902 1.00 7.28  ? 16   PRO D CA  1 
ATOM   8060  C  C   . PRO D  1 16  ? 67.435  18.556  -25.587 1.00 7.45  ? 16   PRO D C   1 
ATOM   8061  O  O   . PRO D  1 16  ? 67.369  17.435  -26.108 1.00 5.95  ? 16   PRO D O   1 
ATOM   8062  C  CB  . PRO D  1 16  ? 65.006  19.184  -25.254 1.00 6.45  ? 16   PRO D CB  1 
ATOM   8063  C  CG  . PRO D  1 16  ? 63.943  19.599  -26.272 1.00 7.86  ? 16   PRO D CG  1 
ATOM   8064  C  CD  . PRO D  1 16  ? 64.559  19.211  -27.613 1.00 7.78  ? 16   PRO D CD  1 
ATOM   8065  N  N   . TYR D  1 17  ? 68.455  18.907  -24.802 1.00 6.31  ? 17   TYR D N   1 
ATOM   8066  C  CA  . TYR D  1 17  ? 69.395  17.882  -24.390 1.00 6.58  ? 17   TYR D CA  1 
ATOM   8067  C  C   . TYR D  1 17  ? 70.225  18.240  -23.153 1.00 7.11  ? 17   TYR D C   1 
ATOM   8068  O  O   . TYR D  1 17  ? 70.330  19.423  -22.781 1.00 5.24  ? 17   TYR D O   1 
ATOM   8069  C  CB  . TYR D  1 17  ? 70.352  17.439  -25.552 1.00 7.63  ? 17   TYR D CB  1 
ATOM   8070  C  CG  . TYR D  1 17  ? 71.417  18.414  -25.968 1.00 8.18  ? 17   TYR D CG  1 
ATOM   8071  C  CD1 . TYR D  1 17  ? 72.683  18.416  -25.364 1.00 8.80  ? 17   TYR D CD1 1 
ATOM   8072  C  CD2 . TYR D  1 17  ? 71.171  19.336  -26.994 1.00 7.35  ? 17   TYR D CD2 1 
ATOM   8073  C  CE1 . TYR D  1 17  ? 73.684  19.306  -25.789 1.00 10.15 ? 17   TYR D CE1 1 
ATOM   8074  C  CE2 . TYR D  1 17  ? 72.150  20.258  -27.389 1.00 6.07  ? 17   TYR D CE2 1 
ATOM   8075  C  CZ  . TYR D  1 17  ? 73.389  20.238  -26.791 1.00 9.01  ? 17   TYR D CZ  1 
ATOM   8076  O  OH  . TYR D  1 17  ? 74.356  21.115  -27.223 1.00 10.62 ? 17   TYR D OH  1 
ATOM   8077  N  N   . VAL D  1 18  ? 70.823  17.208  -22.556 1.00 5.53  ? 18   VAL D N   1 
ATOM   8078  C  CA  . VAL D  1 18  ? 71.773  17.396  -21.481 1.00 7.24  ? 18   VAL D CA  1 
ATOM   8079  C  C   . VAL D  1 18  ? 73.016  16.597  -21.830 1.00 7.35  ? 18   VAL D C   1 
ATOM   8080  O  O   . VAL D  1 18  ? 72.915  15.467  -22.274 1.00 8.43  ? 18   VAL D O   1 
ATOM   8081  C  CB  . VAL D  1 18  ? 71.243  16.892  -20.105 1.00 7.30  ? 18   VAL D CB  1 
ATOM   8082  C  CG1 . VAL D  1 18  ? 72.383  16.766  -19.064 1.00 3.98  ? 18   VAL D CG1 1 
ATOM   8083  C  CG2 . VAL D  1 18  ? 70.149  17.828  -19.533 1.00 7.28  ? 18   VAL D CG2 1 
ATOM   8084  N  N   . ILE D  1 19  ? 74.178  17.190  -21.587 1.00 7.60  ? 19   ILE D N   1 
ATOM   8085  C  CA  . ILE D  1 19  ? 75.406  16.484  -21.815 1.00 8.15  ? 19   ILE D CA  1 
ATOM   8086  C  C   . ILE D  1 19  ? 76.289  16.640  -20.580 1.00 8.45  ? 19   ILE D C   1 
ATOM   8087  O  O   . ILE D  1 19  ? 76.486  17.736  -20.078 1.00 7.65  ? 19   ILE D O   1 
ATOM   8088  C  CB  . ILE D  1 19  ? 76.040  16.949  -23.153 1.00 8.33  ? 19   ILE D CB  1 
ATOM   8089  C  CG1 . ILE D  1 19  ? 77.328  16.196  -23.428 1.00 6.79  ? 19   ILE D CG1 1 
ATOM   8090  C  CG2 . ILE D  1 19  ? 76.334  18.461  -23.139 1.00 8.01  ? 19   ILE D CG2 1 
ATOM   8091  C  CD1 . ILE D  1 19  ? 77.808  16.416  -24.861 1.00 7.47  ? 19   ILE D CD1 1 
ATOM   8092  N  N   . ARG D  1 20  ? 76.726  15.496  -20.050 1.00 8.46  ? 20   ARG D N   1 
ATOM   8093  C  CA  . ARG D  1 20  ? 77.493  15.456  -18.838 1.00 8.83  ? 20   ARG D CA  1 
ATOM   8094  C  C   . ARG D  1 20  ? 78.913  15.982  -19.025 1.00 8.51  ? 20   ARG D C   1 
ATOM   8095  O  O   . ARG D  1 20  ? 79.463  15.905  -20.093 1.00 7.60  ? 20   ARG D O   1 
ATOM   8096  C  CB  . ARG D  1 20  ? 77.579  14.010  -18.353 1.00 8.58  ? 20   ARG D CB  1 
ATOM   8097  C  CG  . ARG D  1 20  ? 76.231  13.380  -17.996 1.00 8.10  ? 20   ARG D CG  1 
ATOM   8098  C  CD  . ARG D  1 20  ? 75.513  14.026  -16.833 1.00 9.15  ? 20   ARG D CD  1 
ATOM   8099  N  NE  . ARG D  1 20  ? 74.356  13.219  -16.428 1.00 7.21  ? 20   ARG D NE  1 
ATOM   8100  C  CZ  . ARG D  1 20  ? 73.539  13.531  -15.405 1.00 9.05  ? 20   ARG D CZ  1 
ATOM   8101  N  NH1 . ARG D  1 20  ? 73.763  14.635  -14.709 1.00 9.91  ? 20   ARG D NH1 1 
ATOM   8102  N  NH2 . ARG D  1 20  ? 72.529  12.713  -15.058 1.00 8.62  ? 20   ARG D NH2 1 
ATOM   8103  N  N   . HIS D  1 21  ? 79.485  16.510  -17.954 1.00 8.73  ? 21   HIS D N   1 
ATOM   8104  C  CA  . HIS D  1 21  ? 80.833  17.069  -17.943 1.00 7.36  ? 21   HIS D CA  1 
ATOM   8105  C  C   . HIS D  1 21  ? 81.790  15.994  -18.416 1.00 7.77  ? 21   HIS D C   1 
ATOM   8106  O  O   . HIS D  1 21  ? 81.662  14.823  -18.002 1.00 8.23  ? 21   HIS D O   1 
ATOM   8107  C  CB  . HIS D  1 21  ? 81.179  17.444  -16.497 1.00 7.15  ? 21   HIS D CB  1 
ATOM   8108  C  CG  . HIS D  1 21  ? 82.319  18.417  -16.379 1.00 10.51 ? 21   HIS D CG  1 
ATOM   8109  N  ND1 . HIS D  1 21  ? 83.056  18.562  -15.223 1.00 11.17 ? 21   HIS D ND1 1 
ATOM   8110  C  CD2 . HIS D  1 21  ? 82.813  19.328  -17.258 1.00 7.65  ? 21   HIS D CD2 1 
ATOM   8111  C  CE1 . HIS D  1 21  ? 83.952  19.525  -15.391 1.00 10.63 ? 21   HIS D CE1 1 
ATOM   8112  N  NE2 . HIS D  1 21  ? 83.864  19.961  -16.635 1.00 9.05  ? 21   HIS D NE2 1 
ATOM   8113  N  N   . TYR D  1 22  ? 82.706  16.368  -19.308 1.00 7.17  ? 22   TYR D N   1 
ATOM   8114  C  CA  . TYR D  1 22  ? 83.696  15.409  -19.845 1.00 7.35  ? 22   TYR D CA  1 
ATOM   8115  C  C   . TYR D  1 22  ? 83.125  14.298  -20.722 1.00 7.04  ? 22   TYR D C   1 
ATOM   8116  O  O   . TYR D  1 22  ? 83.858  13.273  -20.986 1.00 7.38  ? 22   TYR D O   1 
ATOM   8117  C  CB  . TYR D  1 22  ? 84.480  14.719  -18.729 1.00 8.15  ? 22   TYR D CB  1 
ATOM   8118  C  CG  . TYR D  1 22  ? 85.159  15.706  -17.809 1.00 7.63  ? 22   TYR D CG  1 
ATOM   8119  C  CD1 . TYR D  1 22  ? 86.015  16.674  -18.315 1.00 8.25  ? 22   TYR D CD1 1 
ATOM   8120  C  CD2 . TYR D  1 22  ? 84.922  15.652  -16.431 1.00 5.26  ? 22   TYR D CD2 1 
ATOM   8121  C  CE1 . TYR D  1 22  ? 86.573  17.591  -17.515 1.00 6.43  ? 22   TYR D CE1 1 
ATOM   8122  C  CE2 . TYR D  1 22  ? 85.533  16.569  -15.587 1.00 10.65 ? 22   TYR D CE2 1 
ATOM   8123  C  CZ  . TYR D  1 22  ? 86.355  17.523  -16.135 1.00 10.35 ? 22   TYR D CZ  1 
ATOM   8124  O  OH  . TYR D  1 22  ? 86.970  18.472  -15.309 1.00 15.36 ? 22   TYR D OH  1 
ATOM   8125  N  N   . SER D  1 23  ? 81.915  14.514  -21.236 1.00 4.94  ? 23   SER D N   1 
ATOM   8126  C  CA  . SER D  1 23  ? 81.437  13.605  -22.312 1.00 5.61  ? 23   SER D CA  1 
ATOM   8127  C  C   . SER D  1 23  ? 82.360  13.831  -23.505 1.00 5.59  ? 23   SER D C   1 
ATOM   8128  O  O   . SER D  1 23  ? 83.069  14.814  -23.553 1.00 6.52  ? 23   SER D O   1 
ATOM   8129  C  CB  . SER D  1 23  ? 79.965  13.882  -22.721 1.00 5.84  ? 23   SER D CB  1 
ATOM   8130  O  OG  . SER D  1 23  ? 79.080  13.699  -21.600 1.00 7.02  ? 23   SER D OG  1 
ATOM   8131  N  N   . HIS D  1 24  ? 82.326  12.908  -24.442 1.00 6.32  ? 24   HIS D N   1 
ATOM   8132  C  CA  . HIS D  1 24  ? 83.220  12.928  -25.578 1.00 8.25  ? 24   HIS D CA  1 
ATOM   8133  C  C   . HIS D  1 24  ? 83.124  14.269  -26.309 1.00 8.68  ? 24   HIS D C   1 
ATOM   8134  O  O   . HIS D  1 24  ? 84.142  14.849  -26.601 1.00 8.72  ? 24   HIS D O   1 
ATOM   8135  C  CB  . HIS D  1 24  ? 82.905  11.790  -26.530 1.00 8.41  ? 24   HIS D CB  1 
ATOM   8136  C  CG  . HIS D  1 24  ? 83.857  11.758  -27.686 1.00 10.86 ? 24   HIS D CG  1 
ATOM   8137  N  ND1 . HIS D  1 24  ? 83.506  12.202  -28.945 1.00 11.67 ? 24   HIS D ND1 1 
ATOM   8138  C  CD2 . HIS D  1 24  ? 85.186  11.486  -27.732 1.00 8.93  ? 24   HIS D CD2 1 
ATOM   8139  C  CE1 . HIS D  1 24  ? 84.561  12.119  -29.735 1.00 8.06  ? 24   HIS D CE1 1 
ATOM   8140  N  NE2 . HIS D  1 24  ? 85.595  11.691  -29.018 1.00 7.15  ? 24   HIS D NE2 1 
ATOM   8141  N  N   . ALA D  1 25  ? 81.879  14.724  -26.581 1.00 8.80  ? 25   ALA D N   1 
ATOM   8142  C  CA  . ALA D  1 25  ? 81.580  16.069  -27.144 1.00 8.74  ? 25   ALA D CA  1 
ATOM   8143  C  C   . ALA D  1 25  ? 82.503  16.417  -28.301 1.00 8.68  ? 25   ALA D C   1 
ATOM   8144  O  O   . ALA D  1 25  ? 83.168  17.456  -28.278 1.00 8.79  ? 25   ALA D O   1 
ATOM   8145  C  CB  . ALA D  1 25  ? 81.629  17.185  -26.001 1.00 9.38  ? 25   ALA D CB  1 
ATOM   8146  N  N   . ARG D  1 26  ? 82.623  15.483  -29.260 1.00 8.02  ? 26   ARG D N   1 
ATOM   8147  C  CA  . ARG D  1 26  ? 83.504  15.636  -30.411 1.00 7.37  ? 26   ARG D CA  1 
ATOM   8148  C  C   . ARG D  1 26  ? 84.935  16.088  -30.021 1.00 8.14  ? 26   ARG D C   1 
ATOM   8149  O  O   . ARG D  1 26  ? 85.504  16.965  -30.668 1.00 8.28  ? 26   ARG D O   1 
ATOM   8150  C  CB  . ARG D  1 26  ? 82.873  16.663  -31.398 1.00 7.18  ? 26   ARG D CB  1 
ATOM   8151  C  CG  . ARG D  1 26  ? 81.715  16.060  -32.228 1.00 8.50  ? 26   ARG D CG  1 
ATOM   8152  C  CD  . ARG D  1 26  ? 81.249  17.020  -33.326 1.00 7.54  ? 26   ARG D CD  1 
ATOM   8153  N  NE  . ARG D  1 26  ? 80.263  16.417  -34.231 1.00 7.29  ? 26   ARG D NE  1 
ATOM   8154  C  CZ  . ARG D  1 26  ? 79.907  16.946  -35.405 1.00 9.74  ? 26   ARG D CZ  1 
ATOM   8155  N  NH1 . ARG D  1 26  ? 80.465  18.065  -35.854 1.00 7.72  ? 26   ARG D NH1 1 
ATOM   8156  N  NH2 . ARG D  1 26  ? 79.028  16.322  -36.173 1.00 10.35 ? 26   ARG D NH2 1 
ATOM   8157  N  N   . ALA D  1 27  ? 85.540  15.455  -28.996 1.00 8.68  ? 27   ALA D N   1 
ATOM   8158  C  CA  . ALA D  1 27  ? 86.811  15.942  -28.472 1.00 8.34  ? 27   ALA D CA  1 
ATOM   8159  C  C   . ALA D  1 27  ? 87.934  15.999  -29.516 1.00 8.04  ? 27   ALA D C   1 
ATOM   8160  O  O   . ALA D  1 27  ? 88.089  15.075  -30.358 1.00 8.30  ? 27   ALA D O   1 
ATOM   8161  C  CB  . ALA D  1 27  ? 87.258  15.054  -27.331 1.00 8.19  ? 27   ALA D CB  1 
ATOM   8162  N  N   . VAL D  1 28  ? 88.720  17.066  -29.436 1.00 7.65  ? 28   VAL D N   1 
ATOM   8163  C  CA  . VAL D  1 28  ? 90.002  17.131  -30.140 1.00 8.81  ? 28   VAL D CA  1 
ATOM   8164  C  C   . VAL D  1 28  ? 91.076  17.617  -29.193 1.00 8.98  ? 28   VAL D C   1 
ATOM   8165  O  O   . VAL D  1 28  ? 90.776  18.293  -28.204 1.00 8.79  ? 28   VAL D O   1 
ATOM   8166  C  CB  . VAL D  1 28  ? 90.031  18.143  -31.326 1.00 8.92  ? 28   VAL D CB  1 
ATOM   8167  C  CG1 . VAL D  1 28  ? 89.125  17.666  -32.470 1.00 10.22 ? 28   VAL D CG1 1 
ATOM   8168  C  CG2 . VAL D  1 28  ? 89.674  19.611  -30.862 1.00 6.47  ? 28   VAL D CG2 1 
ATOM   8169  N  N   . THR D  1 29  ? 92.330  17.375  -29.568 1.00 7.87  ? 29   THR D N   1 
ATOM   8170  C  CA  . THR D  1 29  ? 93.421  18.001  -28.847 1.00 7.54  ? 29   THR D CA  1 
ATOM   8171  C  C   . THR D  1 29  ? 94.129  18.999  -29.736 1.00 7.83  ? 29   THR D C   1 
ATOM   8172  O  O   . THR D  1 29  ? 94.252  18.799  -30.959 1.00 6.61  ? 29   THR D O   1 
ATOM   8173  C  CB  . THR D  1 29  ? 94.423  16.975  -28.315 1.00 7.42  ? 29   THR D CB  1 
ATOM   8174  O  OG1 . THR D  1 29  ? 94.831  16.094  -29.378 1.00 8.50  ? 29   THR D OG1 1 
ATOM   8175  C  CG2 . THR D  1 29  ? 93.745  16.013  -27.204 1.00 5.17  ? 29   THR D CG2 1 
ATOM   8176  N  N   . VAL D  1 30  ? 94.598  20.076  -29.109 1.00 7.63  ? 30   VAL D N   1 
ATOM   8177  C  CA  . VAL D  1 30  ? 95.559  20.912  -29.791 1.00 8.50  ? 30   VAL D CA  1 
ATOM   8178  C  C   . VAL D  1 30  ? 96.804  20.889  -28.897 1.00 9.05  ? 30   VAL D C   1 
ATOM   8179  O  O   . VAL D  1 30  ? 96.798  21.481  -27.836 1.00 9.44  ? 30   VAL D O   1 
ATOM   8180  C  CB  . VAL D  1 30  ? 95.002  22.320  -29.975 1.00 8.17  ? 30   VAL D CB  1 
ATOM   8181  C  CG1 . VAL D  1 30  ? 96.065  23.168  -30.714 1.00 8.22  ? 30   VAL D CG1 1 
ATOM   8182  C  CG2 . VAL D  1 30  ? 93.708  22.265  -30.787 1.00 6.84  ? 30   VAL D CG2 1 
ATOM   8183  N  N   . ASP D  1 31  ? 97.850  20.195  -29.342 1.00 10.54 ? 31   ASP D N   1 
ATOM   8184  C  CA  . ASP D  1 31  ? 98.985  19.924  -28.479 1.00 11.23 ? 31   ASP D CA  1 
ATOM   8185  C  C   . ASP D  1 31  ? 98.464  19.393  -27.118 1.00 10.21 ? 31   ASP D C   1 
ATOM   8186  O  O   . ASP D  1 31  ? 97.740  18.389  -27.097 1.00 11.70 ? 31   ASP D O   1 
ATOM   8187  C  CB  . ASP D  1 31  ? 99.807  21.215  -28.380 1.00 12.59 ? 31   ASP D CB  1 
ATOM   8188  C  CG  . ASP D  1 31  ? 100.353 21.658  -29.743 1.00 17.80 ? 31   ASP D CG  1 
ATOM   8189  O  OD1 . ASP D  1 31  ? 100.814 20.775  -30.492 1.00 21.73 ? 31   ASP D OD1 1 
ATOM   8190  O  OD2 . ASP D  1 31  ? 100.351 22.861  -30.159 1.00 25.04 ? 31   ASP D OD2 1 
ATOM   8191  N  N   . THR D  1 32  ? 98.735  20.052  -25.999 1.00 9.71  ? 32   THR D N   1 
ATOM   8192  C  CA  . THR D  1 32  ? 98.332  19.472  -24.686 1.00 9.42  ? 32   THR D CA  1 
ATOM   8193  C  C   . THR D  1 32  ? 96.889  19.785  -24.274 1.00 9.91  ? 32   THR D C   1 
ATOM   8194  O  O   . THR D  1 32  ? 96.408  19.227  -23.240 1.00 10.80 ? 32   THR D O   1 
ATOM   8195  C  CB  . THR D  1 32  ? 99.239  19.983  -23.545 1.00 10.75 ? 32   THR D CB  1 
ATOM   8196  O  OG1 . THR D  1 32  ? 99.226  21.425  -23.544 1.00 8.00  ? 32   THR D OG1 1 
ATOM   8197  C  CG2 . THR D  1 32  ? 100.744 19.611  -23.749 1.00 10.30 ? 32   THR D CG2 1 
ATOM   8198  N  N   . GLN D  1 33  ? 96.210  20.658  -25.046 1.00 8.63  ? 33   GLN D N   1 
ATOM   8199  C  CA  . GLN D  1 33  ? 94.841  21.154  -24.695 1.00 8.20  ? 33   GLN D CA  1 
ATOM   8200  C  C   . GLN D  1 33  ? 93.809  20.191  -25.231 1.00 7.80  ? 33   GLN D C   1 
ATOM   8201  O  O   . GLN D  1 33  ? 93.884  19.819  -26.409 1.00 8.27  ? 33   GLN D O   1 
ATOM   8202  C  CB  . GLN D  1 33  ? 94.547  22.536  -25.295 1.00 7.08  ? 33   GLN D CB  1 
ATOM   8203  C  CG  . GLN D  1 33  ? 95.541  23.623  -24.841 1.00 7.65  ? 33   GLN D CG  1 
ATOM   8204  C  CD  . GLN D  1 33  ? 95.558  24.883  -25.767 1.00 8.62  ? 33   GLN D CD  1 
ATOM   8205  O  OE1 . GLN D  1 33  ? 94.805  24.965  -26.724 1.00 10.53 ? 33   GLN D OE1 1 
ATOM   8206  N  NE2 . GLN D  1 33  ? 96.460  25.830  -25.479 1.00 7.80  ? 33   GLN D NE2 1 
ATOM   8207  N  N   . LEU D  1 34  ? 92.822  19.834  -24.410 1.00 7.49  ? 34   LEU D N   1 
ATOM   8208  C  CA  . LEU D  1 34  ? 91.696  19.030  -24.913 1.00 8.24  ? 34   LEU D CA  1 
ATOM   8209  C  C   . LEU D  1 34  ? 90.387  19.849  -24.946 1.00 9.19  ? 34   LEU D C   1 
ATOM   8210  O  O   . LEU D  1 34  ? 89.949  20.425  -23.900 1.00 10.98 ? 34   LEU D O   1 
ATOM   8211  C  CB  . LEU D  1 34  ? 91.540  17.792  -24.053 1.00 8.68  ? 34   LEU D CB  1 
ATOM   8212  C  CG  . LEU D  1 34  ? 90.717  16.719  -24.761 1.00 6.01  ? 34   LEU D CG  1 
ATOM   8213  C  CD1 . LEU D  1 34  ? 91.045  15.431  -24.070 1.00 10.67 ? 34   LEU D CD1 1 
ATOM   8214  C  CD2 . LEU D  1 34  ? 89.223  17.072  -24.551 1.00 7.96  ? 34   LEU D CD2 1 
ATOM   8215  N  N   . TYR D  1 35  ? 89.790  19.974  -26.146 1.00 9.20  ? 35   TYR D N   1 
ATOM   8216  C  CA  . TYR D  1 35  ? 88.542  20.747  -26.343 1.00 6.29  ? 35   TYR D CA  1 
ATOM   8217  C  C   . TYR D  1 35  ? 87.334  19.831  -26.448 1.00 7.57  ? 35   TYR D C   1 
ATOM   8218  O  O   . TYR D  1 35  ? 87.381  18.812  -27.156 1.00 10.10 ? 35   TYR D O   1 
ATOM   8219  C  CB  . TYR D  1 35  ? 88.634  21.550  -27.688 1.00 6.50  ? 35   TYR D CB  1 
ATOM   8220  C  CG  . TYR D  1 35  ? 89.634  22.670  -27.636 1.00 6.67  ? 35   TYR D CG  1 
ATOM   8221  C  CD1 . TYR D  1 35  ? 90.991  22.411  -27.663 1.00 7.77  ? 35   TYR D CD1 1 
ATOM   8222  C  CD2 . TYR D  1 35  ? 89.219  24.000  -27.545 1.00 8.43  ? 35   TYR D CD2 1 
ATOM   8223  C  CE1 . TYR D  1 35  ? 91.945  23.493  -27.570 1.00 10.67 ? 35   TYR D CE1 1 
ATOM   8224  C  CE2 . TYR D  1 35  ? 90.134  25.043  -27.460 1.00 7.53  ? 35   TYR D CE2 1 
ATOM   8225  C  CZ  . TYR D  1 35  ? 91.485  24.799  -27.470 1.00 8.96  ? 35   TYR D CZ  1 
ATOM   8226  O  OH  . TYR D  1 35  ? 92.412  25.885  -27.411 1.00 13.47 ? 35   TYR D OH  1 
ATOM   8227  N  N   . ARG D  1 36  ? 86.232  20.216  -25.806 1.00 6.82  ? 36   ARG D N   1 
ATOM   8228  C  CA  . ARG D  1 36  ? 84.979  19.504  -25.866 1.00 7.73  ? 36   ARG D CA  1 
ATOM   8229  C  C   . ARG D  1 36  ? 83.915  20.549  -26.259 1.00 7.52  ? 36   ARG D C   1 
ATOM   8230  O  O   . ARG D  1 36  ? 83.936  21.675  -25.749 1.00 8.83  ? 36   ARG D O   1 
ATOM   8231  C  CB  . ARG D  1 36  ? 84.653  18.881  -24.498 1.00 6.07  ? 36   ARG D CB  1 
ATOM   8232  C  CG  . ARG D  1 36  ? 85.464  17.570  -24.181 1.00 6.42  ? 36   ARG D CG  1 
ATOM   8233  C  CD  . ARG D  1 36  ? 85.057  16.967  -22.807 1.00 9.43  ? 36   ARG D CD  1 
ATOM   8234  N  NE  . ARG D  1 36  ? 85.810  15.754  -22.540 1.00 7.27  ? 36   ARG D NE  1 
ATOM   8235  C  CZ  . ARG D  1 36  ? 86.996  15.740  -21.938 1.00 7.28  ? 36   ARG D CZ  1 
ATOM   8236  N  NH1 . ARG D  1 36  ? 87.604  16.882  -21.587 1.00 9.81  ? 36   ARG D NH1 1 
ATOM   8237  N  NH2 . ARG D  1 36  ? 87.601  14.587  -21.765 1.00 8.41  ? 36   ARG D NH2 1 
ATOM   8238  N  N   . PHE D  1 37  ? 82.994  20.163  -27.131 1.00 7.87  ? 37   PHE D N   1 
ATOM   8239  C  CA  . PHE D  1 37  ? 81.977  21.078  -27.697 1.00 6.60  ? 37   PHE D CA  1 
ATOM   8240  C  C   . PHE D  1 37  ? 80.612  20.639  -27.202 1.00 7.93  ? 37   PHE D C   1 
ATOM   8241  O  O   . PHE D  1 37  ? 79.909  19.812  -27.830 1.00 7.58  ? 37   PHE D O   1 
ATOM   8242  C  CB  . PHE D  1 37  ? 82.127  21.090  -29.215 1.00 6.91  ? 37   PHE D CB  1 
ATOM   8243  C  CG  . PHE D  1 37  ? 83.558  21.317  -29.639 1.00 8.25  ? 37   PHE D CG  1 
ATOM   8244  C  CD1 . PHE D  1 37  ? 84.105  22.590  -29.589 1.00 10.53 ? 37   PHE D CD1 1 
ATOM   8245  C  CD2 . PHE D  1 37  ? 84.392  20.236  -29.984 1.00 9.46  ? 37   PHE D CD2 1 
ATOM   8246  C  CE1 . PHE D  1 37  ? 85.455  22.801  -29.922 1.00 9.23  ? 37   PHE D CE1 1 
ATOM   8247  C  CE2 . PHE D  1 37  ? 85.749  20.455  -30.308 1.00 8.57  ? 37   PHE D CE2 1 
ATOM   8248  C  CZ  . PHE D  1 37  ? 86.267  21.743  -30.235 1.00 10.98 ? 37   PHE D CZ  1 
ATOM   8249  N  N   . TYR D  1 38  ? 80.272  21.139  -26.022 1.00 7.60  ? 38   TYR D N   1 
ATOM   8250  C  CA  . TYR D  1 38  ? 79.005  20.845  -25.386 1.00 7.45  ? 38   TYR D CA  1 
ATOM   8251  C  C   . TYR D  1 38  ? 77.822  21.410  -26.122 1.00 8.05  ? 38   TYR D C   1 
ATOM   8252  O  O   . TYR D  1 38  ? 76.773  20.743  -26.228 1.00 9.48  ? 38   TYR D O   1 
ATOM   8253  C  CB  . TYR D  1 38  ? 79.000  21.349  -23.927 1.00 6.76  ? 38   TYR D CB  1 
ATOM   8254  C  CG  . TYR D  1 38  ? 80.067  20.733  -23.088 1.00 8.06  ? 38   TYR D CG  1 
ATOM   8255  C  CD1 . TYR D  1 38  ? 80.140  19.354  -22.927 1.00 6.78  ? 38   TYR D CD1 1 
ATOM   8256  C  CD2 . TYR D  1 38  ? 81.065  21.541  -22.477 1.00 6.06  ? 38   TYR D CD2 1 
ATOM   8257  C  CE1 . TYR D  1 38  ? 81.142  18.767  -22.104 1.00 8.17  ? 38   TYR D CE1 1 
ATOM   8258  C  CE2 . TYR D  1 38  ? 82.055  20.948  -21.656 1.00 9.23  ? 38   TYR D CE2 1 
ATOM   8259  C  CZ  . TYR D  1 38  ? 82.088  19.563  -21.498 1.00 6.59  ? 38   TYR D CZ  1 
ATOM   8260  O  OH  . TYR D  1 38  ? 83.067  18.940  -20.725 1.00 6.44  ? 38   TYR D OH  1 
ATOM   8261  N  N   . VAL D  1 39  ? 77.942  22.653  -26.586 1.00 7.19  ? 39   VAL D N   1 
ATOM   8262  C  CA  . VAL D  1 39  ? 76.933  23.202  -27.469 1.00 7.34  ? 39   VAL D CA  1 
ATOM   8263  C  C   . VAL D  1 39  ? 77.652  23.616  -28.733 1.00 8.31  ? 39   VAL D C   1 
ATOM   8264  O  O   . VAL D  1 39  ? 78.658  24.294  -28.648 1.00 7.98  ? 39   VAL D O   1 
ATOM   8265  C  CB  . VAL D  1 39  ? 76.179  24.394  -26.829 1.00 7.52  ? 39   VAL D CB  1 
ATOM   8266  C  CG1 . VAL D  1 39  ? 75.080  24.951  -27.799 1.00 6.88  ? 39   VAL D CG1 1 
ATOM   8267  C  CG2 . VAL D  1 39  ? 75.533  23.983  -25.449 1.00 7.69  ? 39   VAL D CG2 1 
ATOM   8268  N  N   . THR D  1 40  ? 77.134  23.215  -29.901 1.00 8.77  ? 40   THR D N   1 
ATOM   8269  C  CA  . THR D  1 40  ? 77.767  23.597  -31.147 1.00 8.65  ? 40   THR D CA  1 
ATOM   8270  C  C   . THR D  1 40  ? 76.844  24.470  -32.008 1.00 8.98  ? 40   THR D C   1 
ATOM   8271  O  O   . THR D  1 40  ? 75.655  24.733  -31.674 1.00 10.12 ? 40   THR D O   1 
ATOM   8272  C  CB  . THR D  1 40  ? 78.132  22.351  -31.965 1.00 8.88  ? 40   THR D CB  1 
ATOM   8273  O  OG1 . THR D  1 40  ? 76.939  21.620  -32.241 1.00 9.07  ? 40   THR D OG1 1 
ATOM   8274  C  CG2 . THR D  1 40  ? 79.067  21.361  -31.178 1.00 8.08  ? 40   THR D CG2 1 
ATOM   8275  N  N   . GLY D  1 41  ? 77.367  24.908  -33.156 1.00 8.19  ? 41   GLY D N   1 
ATOM   8276  C  CA  . GLY D  1 41  ? 76.511  25.580  -34.113 1.00 7.50  ? 41   GLY D CA  1 
ATOM   8277  C  C   . GLY D  1 41  ? 75.335  24.698  -34.545 1.00 7.91  ? 41   GLY D C   1 
ATOM   8278  O  O   . GLY D  1 41  ? 74.193  25.148  -34.446 1.00 8.42  ? 41   GLY D O   1 
ATOM   8279  N  N   . PRO D  1 42  ? 75.582  23.479  -35.046 1.00 7.37  ? 42   PRO D N   1 
ATOM   8280  C  CA  . PRO D  1 42  ? 74.477  22.564  -35.386 1.00 7.40  ? 42   PRO D CA  1 
ATOM   8281  C  C   . PRO D  1 42  ? 73.482  22.351  -34.244 1.00 7.43  ? 42   PRO D C   1 
ATOM   8282  O  O   . PRO D  1 42  ? 72.283  22.298  -34.501 1.00 7.17  ? 42   PRO D O   1 
ATOM   8283  C  CB  . PRO D  1 42  ? 75.191  21.259  -35.773 1.00 8.15  ? 42   PRO D CB  1 
ATOM   8284  C  CG  . PRO D  1 42  ? 76.600  21.795  -36.404 1.00 6.82  ? 42   PRO D CG  1 
ATOM   8285  C  CD  . PRO D  1 42  ? 76.896  22.910  -35.422 1.00 7.68  ? 42   PRO D CD  1 
ATOM   8286  N  N   . SER D  1 43  ? 73.943  22.298  -33.002 1.00 6.94  ? 43   SER D N   1 
ATOM   8287  C  CA  . SER D  1 43  ? 73.071  21.847  -31.913 1.00 6.88  ? 43   SER D CA  1 
ATOM   8288  C  C   . SER D  1 43  ? 72.212  22.994  -31.412 1.00 7.20  ? 43   SER D C   1 
ATOM   8289  O  O   . SER D  1 43  ? 71.180  22.803  -30.759 1.00 7.76  ? 43   SER D O   1 
ATOM   8290  C  CB  . SER D  1 43  ? 73.885  21.195  -30.774 1.00 6.35  ? 43   SER D CB  1 
ATOM   8291  O  OG  A SER D  1 43  ? 72.952  20.550  -29.944 0.50 12.87 ? 43   SER D OG  1 
ATOM   8292  O  OG  B SER D  1 43  ? 74.476  22.105  -29.860 0.50 2.00  ? 43   SER D OG  1 
ATOM   8293  N  N   . SER D  1 44  ? 72.668  24.201  -31.709 1.00 8.17  ? 44   SER D N   1 
ATOM   8294  C  CA  . SER D  1 44  ? 72.013  25.403  -31.218 1.00 7.26  ? 44   SER D CA  1 
ATOM   8295  C  C   . SER D  1 44  ? 71.341  26.191  -32.335 1.00 7.11  ? 44   SER D C   1 
ATOM   8296  O  O   . SER D  1 44  ? 70.833  27.281  -32.094 1.00 6.26  ? 44   SER D O   1 
ATOM   8297  C  CB  . SER D  1 44  ? 73.028  26.247  -30.409 1.00 7.69  ? 44   SER D CB  1 
ATOM   8298  O  OG  . SER D  1 44  ? 73.839  27.026  -31.284 1.00 9.92  ? 44   SER D OG  1 
ATOM   8299  N  N   . GLY D  1 45  ? 71.335  25.650  -33.562 1.00 6.58  ? 45   GLY D N   1 
ATOM   8300  C  CA  . GLY D  1 45  ? 70.850  26.393  -34.716 1.00 7.17  ? 45   GLY D CA  1 
ATOM   8301  C  C   . GLY D  1 45  ? 71.683  27.667  -34.873 1.00 8.54  ? 45   GLY D C   1 
ATOM   8302  O  O   . GLY D  1 45  ? 71.150  28.712  -35.241 1.00 7.68  ? 45   GLY D O   1 
ATOM   8303  N  N   . TYR D  1 46  ? 72.978  27.562  -34.571 1.00 7.84  ? 46   TYR D N   1 
ATOM   8304  C  CA  . TYR D  1 46  ? 73.969  28.643  -34.788 1.00 8.53  ? 46   TYR D CA  1 
ATOM   8305  C  C   . TYR D  1 46  ? 73.810  29.827  -33.868 1.00 7.69  ? 46   TYR D C   1 
ATOM   8306  O  O   . TYR D  1 46  ? 74.448  30.842  -34.061 1.00 8.44  ? 46   TYR D O   1 
ATOM   8307  C  CB  . TYR D  1 46  ? 74.179  28.998  -36.320 1.00 9.70  ? 46   TYR D CB  1 
ATOM   8308  C  CG  . TYR D  1 46  ? 74.547  27.722  -37.064 1.00 7.70  ? 46   TYR D CG  1 
ATOM   8309  C  CD1 . TYR D  1 46  ? 75.868  27.259  -37.088 1.00 7.76  ? 46   TYR D CD1 1 
ATOM   8310  C  CD2 . TYR D  1 46  ? 73.565  26.925  -37.628 1.00 11.52 ? 46   TYR D CD2 1 
ATOM   8311  C  CE1 . TYR D  1 46  ? 76.192  26.036  -37.683 1.00 9.69  ? 46   TYR D CE1 1 
ATOM   8312  C  CE2 . TYR D  1 46  ? 73.869  25.698  -38.213 1.00 10.47 ? 46   TYR D CE2 1 
ATOM   8313  C  CZ  . TYR D  1 46  ? 75.173  25.257  -38.212 1.00 9.16  ? 46   TYR D CZ  1 
ATOM   8314  O  OH  . TYR D  1 46  ? 75.470  24.056  -38.786 1.00 9.83  ? 46   TYR D OH  1 
ATOM   8315  N  N   . ALA D  1 47  ? 73.066  29.662  -32.776 1.00 7.11  ? 47   ALA D N   1 
ATOM   8316  C  CA  . ALA D  1 47  ? 72.963  30.743  -31.779 1.00 6.28  ? 47   ALA D CA  1 
ATOM   8317  C  C   . ALA D  1 47  ? 74.292  30.963  -31.080 1.00 7.07  ? 47   ALA D C   1 
ATOM   8318  O  O   . ALA D  1 47  ? 74.724  32.104  -30.930 1.00 9.21  ? 47   ALA D O   1 
ATOM   8319  C  CB  . ALA D  1 47  ? 71.868  30.462  -30.727 1.00 5.04  ? 47   ALA D CB  1 
ATOM   8320  N  N   . PHE D  1 48  ? 74.915  29.899  -30.602 1.00 6.34  ? 48   PHE D N   1 
ATOM   8321  C  CA  . PHE D  1 48  ? 76.172  30.042  -29.832 1.00 6.92  ? 48   PHE D CA  1 
ATOM   8322  C  C   . PHE D  1 48  ? 76.886  28.713  -29.664 1.00 7.20  ? 48   PHE D C   1 
ATOM   8323  O  O   . PHE D  1 48  ? 76.290  27.622  -29.872 1.00 8.93  ? 48   PHE D O   1 
ATOM   8324  C  CB  . PHE D  1 48  ? 75.908  30.646  -28.432 1.00 6.94  ? 48   PHE D CB  1 
ATOM   8325  C  CG  . PHE D  1 48  ? 74.738  30.000  -27.685 1.00 9.46  ? 48   PHE D CG  1 
ATOM   8326  C  CD1 . PHE D  1 48  ? 74.871  28.727  -27.075 1.00 13.30 ? 48   PHE D CD1 1 
ATOM   8327  C  CD2 . PHE D  1 48  ? 73.503  30.642  -27.635 1.00 9.03  ? 48   PHE D CD2 1 
ATOM   8328  C  CE1 . PHE D  1 48  ? 73.769  28.141  -26.395 1.00 8.82  ? 48   PHE D CE1 1 
ATOM   8329  C  CE2 . PHE D  1 48  ? 72.414  30.056  -26.984 1.00 7.97  ? 48   PHE D CE2 1 
ATOM   8330  C  CZ  . PHE D  1 48  ? 72.548  28.825  -26.370 1.00 8.35  ? 48   PHE D CZ  1 
ATOM   8331  N  N   . THR D  1 49  ? 78.146  28.785  -29.228 1.00 6.77  ? 49   THR D N   1 
ATOM   8332  C  CA  . THR D  1 49  ? 78.931  27.573  -28.966 1.00 7.45  ? 49   THR D CA  1 
ATOM   8333  C  C   . THR D  1 49  ? 79.253  27.646  -27.484 1.00 7.60  ? 49   THR D C   1 
ATOM   8334  O  O   . THR D  1 49  ? 79.532  28.740  -26.971 1.00 8.34  ? 49   THR D O   1 
ATOM   8335  C  CB  . THR D  1 49  ? 80.225  27.608  -29.770 1.00 6.02  ? 49   THR D CB  1 
ATOM   8336  O  OG1 . THR D  1 49  ? 79.915  27.467  -31.170 1.00 9.07  ? 49   THR D OG1 1 
ATOM   8337  C  CG2 . THR D  1 49  ? 81.200  26.375  -29.380 1.00 7.02  ? 49   THR D CG2 1 
ATOM   8338  N  N   . LEU D  1 50  ? 79.267  26.493  -26.816 1.00 8.36  ? 50   LEU D N   1 
ATOM   8339  C  CA  . LEU D  1 50  ? 79.743  26.455  -25.421 1.00 8.00  ? 50   LEU D CA  1 
ATOM   8340  C  C   . LEU D  1 50  ? 80.698  25.311  -25.413 1.00 8.72  ? 50   LEU D C   1 
ATOM   8341  O  O   . LEU D  1 50  ? 80.322  24.150  -25.669 1.00 8.81  ? 50   LEU D O   1 
ATOM   8342  C  CB  . LEU D  1 50  ? 78.601  26.184  -24.433 1.00 6.78  ? 50   LEU D CB  1 
ATOM   8343  C  CG  . LEU D  1 50  ? 78.916  26.344  -22.954 1.00 7.60  ? 50   LEU D CG  1 
ATOM   8344  C  CD1 . LEU D  1 50  ? 77.602  26.703  -22.263 1.00 10.97 ? 50   LEU D CD1 1 
ATOM   8345  C  CD2 . LEU D  1 50  ? 79.608  25.062  -22.379 1.00 9.10  ? 50   LEU D CD2 1 
ATOM   8346  N  N   . MET D  1 51  ? 81.947  25.639  -25.169 1.00 8.99  ? 51   MET D N   1 
ATOM   8347  C  CA  . MET D  1 51  ? 82.985  24.605  -25.210 1.00 9.52  ? 51   MET D CA  1 
ATOM   8348  C  C   . MET D  1 51  ? 83.792  24.595  -23.938 1.00 10.43 ? 51   MET D C   1 
ATOM   8349  O  O   . MET D  1 51  ? 83.813  25.628  -23.220 1.00 10.40 ? 51   MET D O   1 
ATOM   8350  C  CB  . MET D  1 51  ? 83.846  24.804  -26.446 1.00 9.42  ? 51   MET D CB  1 
ATOM   8351  C  CG  . MET D  1 51  ? 84.726  26.045  -26.401 1.00 11.12 ? 51   MET D CG  1 
ATOM   8352  S  SD  . MET D  1 51  ? 85.633  26.181  -27.929 1.00 13.66 ? 51   MET D SD  1 
ATOM   8353  C  CE  . MET D  1 51  ? 86.737  27.438  -27.454 1.00 15.69 ? 51   MET D CE  1 
ATOM   8354  N  N   . GLY D  1 52  ? 84.383  23.432  -23.627 1.00 10.05 ? 52   GLY D N   1 
ATOM   8355  C  CA  . GLY D  1 52  ? 85.260  23.275  -22.478 1.00 10.69 ? 52   GLY D CA  1 
ATOM   8356  C  C   . GLY D  1 52  ? 86.684  22.973  -22.937 1.00 11.15 ? 52   GLY D C   1 
ATOM   8357  O  O   . GLY D  1 52  ? 86.902  22.161  -23.862 1.00 12.48 ? 52   GLY D O   1 
ATOM   8358  N  N   . THR D  1 53  ? 87.680  23.642  -22.354 1.00 10.27 ? 53   THR D N   1 
ATOM   8359  C  CA  . THR D  1 53  ? 89.069  23.340  -22.698 1.00 8.31  ? 53   THR D CA  1 
ATOM   8360  C  C   . THR D  1 53  ? 89.755  22.925  -21.422 1.00 9.22  ? 53   THR D C   1 
ATOM   8361  O  O   . THR D  1 53  ? 89.837  23.741  -20.490 1.00 10.14 ? 53   THR D O   1 
ATOM   8362  C  CB  . THR D  1 53  ? 89.774  24.573  -23.283 1.00 7.99  ? 53   THR D CB  1 
ATOM   8363  O  OG1 . THR D  1 53  ? 89.095  25.000  -24.467 1.00 6.75  ? 53   THR D OG1 1 
ATOM   8364  C  CG2 . THR D  1 53  ? 91.245  24.215  -23.790 1.00 5.83  ? 53   THR D CG2 1 
ATOM   8365  N  N   . ASN D  1 54  ? 90.244  21.694  -21.362 1.00 7.59  ? 54   ASN D N   1 
ATOM   8366  C  CA  . ASN D  1 54  ? 91.044  21.264  -20.203 1.00 8.48  ? 54   ASN D CA  1 
ATOM   8367  C  C   . ASN D  1 54  ? 92.484  21.182  -20.582 1.00 8.99  ? 54   ASN D C   1 
ATOM   8368  O  O   . ASN D  1 54  ? 92.770  20.781  -21.693 1.00 10.25 ? 54   ASN D O   1 
ATOM   8369  C  CB  . ASN D  1 54  ? 90.528  19.931  -19.656 1.00 8.04  ? 54   ASN D CB  1 
ATOM   8370  C  CG  . ASN D  1 54  ? 89.214  20.083  -18.948 1.00 9.22  ? 54   ASN D CG  1 
ATOM   8371  O  OD1 . ASN D  1 54  ? 88.133  20.188  -19.575 1.00 9.62  ? 54   ASN D OD1 1 
ATOM   8372  N  ND2 . ASN D  1 54  ? 89.280  20.168  -17.619 1.00 7.20  ? 54   ASN D ND2 1 
ATOM   8373  N  N   . ALA D  1 55  ? 93.402  21.576  -19.692 1.00 8.57  ? 55   ALA D N   1 
ATOM   8374  C  CA  . ALA D  1 55  ? 94.811  21.730  -20.090 1.00 8.47  ? 55   ALA D CA  1 
ATOM   8375  C  C   . ALA D  1 55  ? 95.736  21.866  -18.881 1.00 7.90  ? 55   ALA D C   1 
ATOM   8376  O  O   . ALA D  1 55  ? 95.320  22.476  -17.871 1.00 7.28  ? 55   ALA D O   1 
ATOM   8377  C  CB  . ALA D  1 55  ? 94.985  22.994  -21.056 1.00 8.12  ? 55   ALA D CB  1 
ATOM   8378  N  N   . PRO D  1 56  ? 96.985  21.361  -18.995 1.00 7.68  ? 56   PRO D N   1 
ATOM   8379  C  CA  . PRO D  1 56  ? 97.996  21.479  -17.933 1.00 5.91  ? 56   PRO D CA  1 
ATOM   8380  C  C   . PRO D  1 56  ? 98.744  22.814  -18.054 1.00 7.71  ? 56   PRO D C   1 
ATOM   8381  O  O   . PRO D  1 56  ? 98.557  23.587  -19.014 1.00 6.31  ? 56   PRO D O   1 
ATOM   8382  C  CB  . PRO D  1 56  ? 98.972  20.335  -18.275 1.00 6.08  ? 56   PRO D CB  1 
ATOM   8383  C  CG  . PRO D  1 56  ? 98.966  20.399  -19.900 1.00 4.72  ? 56   PRO D CG  1 
ATOM   8384  C  CD  . PRO D  1 56  ? 97.509  20.601  -20.164 1.00 6.21  ? 56   PRO D CD  1 
ATOM   8385  N  N   . HIS D  1 57  ? 99.564  23.102  -17.059 1.00 6.09  ? 57   HIS D N   1 
ATOM   8386  C  CA  . HIS D  1 57  ? 100.414 24.250  -17.107 1.00 6.99  ? 57   HIS D CA  1 
ATOM   8387  C  C   . HIS D  1 57  ? 101.241 24.247  -18.375 1.00 9.05  ? 57   HIS D C   1 
ATOM   8388  O  O   . HIS D  1 57  ? 101.781 23.191  -18.768 1.00 8.93  ? 57   HIS D O   1 
ATOM   8389  C  CB  . HIS D  1 57  ? 101.398 24.181  -15.925 1.00 6.08  ? 57   HIS D CB  1 
ATOM   8390  C  CG  . HIS D  1 57  ? 102.464 25.212  -16.004 1.00 5.12  ? 57   HIS D CG  1 
ATOM   8391  N  ND1 . HIS D  1 57  ? 102.263 26.524  -15.633 1.00 9.48  ? 57   HIS D ND1 1 
ATOM   8392  C  CD2 . HIS D  1 57  ? 103.714 25.155  -16.517 1.00 9.93  ? 57   HIS D CD2 1 
ATOM   8393  C  CE1 . HIS D  1 57  ? 103.366 27.223  -15.861 1.00 10.91 ? 57   HIS D CE1 1 
ATOM   8394  N  NE2 . HIS D  1 57  ? 104.261 26.413  -16.400 1.00 11.61 ? 57   HIS D NE2 1 
ATOM   8395  N  N   . SER D  1 58  ? 101.426 25.431  -18.947 1.00 9.59  ? 58   SER D N   1 
ATOM   8396  C  CA  . SER D  1 58  ? 102.369 25.635  -20.054 1.00 9.65  ? 58   SER D CA  1 
ATOM   8397  C  C   . SER D  1 58  ? 103.161 26.893  -19.826 1.00 9.58  ? 58   SER D C   1 
ATOM   8398  O  O   . SER D  1 58  ? 102.635 27.931  -19.378 1.00 8.04  ? 58   SER D O   1 
ATOM   8399  C  CB  . SER D  1 58  ? 101.628 25.730  -21.384 1.00 10.74 ? 58   SER D CB  1 
ATOM   8400  O  OG  . SER D  1 58  ? 102.508 26.074  -22.420 1.00 13.03 ? 58   SER D OG  1 
ATOM   8401  N  N   . ASP D  1 59  ? 104.448 26.802  -20.131 1.00 9.41  ? 59   ASP D N   1 
ATOM   8402  C  CA  . ASP D  1 59  ? 105.312 27.979  -20.069 1.00 11.29 ? 59   ASP D CA  1 
ATOM   8403  C  C   . ASP D  1 59  ? 105.099 28.907  -21.263 1.00 11.29 ? 59   ASP D C   1 
ATOM   8404  O  O   . ASP D  1 59  ? 105.658 30.022  -21.272 1.00 11.64 ? 59   ASP D O   1 
ATOM   8405  C  CB  . ASP D  1 59  ? 106.760 27.562  -20.082 1.00 11.32 ? 59   ASP D CB  1 
ATOM   8406  C  CG  . ASP D  1 59  ? 107.188 26.931  -18.761 1.00 17.21 ? 59   ASP D CG  1 
ATOM   8407  O  OD1 . ASP D  1 59  ? 106.524 27.181  -17.712 1.00 16.73 ? 59   ASP D OD1 1 
ATOM   8408  O  OD2 . ASP D  1 59  ? 108.177 26.167  -18.696 1.00 24.18 ? 59   ASP D OD2 1 
ATOM   8409  N  N   . ALA D  1 60  ? 104.342 28.443  -22.262 1.00 9.60  ? 60   ALA D N   1 
ATOM   8410  C  CA  . ALA D  1 60  ? 104.157 29.215  -23.497 1.00 9.93  ? 60   ALA D CA  1 
ATOM   8411  C  C   . ALA D  1 60  ? 102.707 29.644  -23.696 1.00 9.17  ? 60   ALA D C   1 
ATOM   8412  O  O   . ALA D  1 60  ? 101.785 29.036  -23.117 1.00 9.66  ? 60   ALA D O   1 
ATOM   8413  C  CB  . ALA D  1 60  ? 104.699 28.453  -24.736 1.00 9.96  ? 60   ALA D CB  1 
ATOM   8414  N  N   . LEU D  1 61  ? 102.496 30.708  -24.464 1.00 9.16  ? 61   LEU D N   1 
ATOM   8415  C  CA  . LEU D  1 61  ? 101.134 31.085  -24.843 1.00 9.73  ? 61   LEU D CA  1 
ATOM   8416  C  C   . LEU D  1 61  ? 100.363 29.875  -25.367 1.00 9.63  ? 61   LEU D C   1 
ATOM   8417  O  O   . LEU D  1 61  ? 100.940 28.976  -25.996 1.00 9.45  ? 61   LEU D O   1 
ATOM   8418  C  CB  . LEU D  1 61  ? 101.133 32.201  -25.882 1.00 9.77  ? 61   LEU D CB  1 
ATOM   8419  C  CG  . LEU D  1 61  ? 101.668 33.603  -25.503 1.00 12.60 ? 61   LEU D CG  1 
ATOM   8420  C  CD1 . LEU D  1 61  ? 101.702 34.501  -26.744 1.00 9.21  ? 61   LEU D CD1 1 
ATOM   8421  C  CD2 . LEU D  1 61  ? 100.823 34.266  -24.400 1.00 8.59  ? 61   LEU D CD2 1 
ATOM   8422  N  N   . GLY D  1 62  ? 99.063  29.847  -25.088 1.00 9.61  ? 62   GLY D N   1 
ATOM   8423  C  CA  . GLY D  1 62  ? 98.202  28.743  -25.498 1.00 9.90  ? 62   GLY D CA  1 
ATOM   8424  C  C   . GLY D  1 62  ? 97.708  28.927  -26.929 1.00 10.27 ? 62   GLY D C   1 
ATOM   8425  O  O   . GLY D  1 62  ? 97.084  28.026  -27.509 1.00 11.48 ? 62   GLY D O   1 
ATOM   8426  N  N   . VAL D  1 63  ? 97.945  30.108  -27.481 1.00 8.80  ? 63   VAL D N   1 
ATOM   8427  C  CA  . VAL D  1 63  ? 97.605  30.410  -28.883 1.00 8.73  ? 63   VAL D CA  1 
ATOM   8428  C  C   . VAL D  1 63  ? 98.310  31.697  -29.276 1.00 8.15  ? 63   VAL D C   1 
ATOM   8429  O  O   . VAL D  1 63  ? 98.550  32.516  -28.423 1.00 7.95  ? 63   VAL D O   1 
ATOM   8430  C  CB  . VAL D  1 63  ? 96.091  30.558  -29.152 1.00 8.54  ? 63   VAL D CB  1 
ATOM   8431  C  CG1 . VAL D  1 63  ? 95.428  31.708  -28.344 1.00 8.01  ? 63   VAL D CG1 1 
ATOM   8432  C  CG2 . VAL D  1 63  ? 95.827  30.747  -30.671 1.00 10.26 ? 63   VAL D CG2 1 
ATOM   8433  N  N   . LEU D  1 64  ? 98.672  31.861  -30.549 1.00 8.07  ? 64   LEU D N   1 
ATOM   8434  C  CA  . LEU D  1 64  ? 99.273  33.141  -30.950 1.00 7.93  ? 64   LEU D CA  1 
ATOM   8435  C  C   . LEU D  1 64  ? 98.212  34.251  -30.912 1.00 7.91  ? 64   LEU D C   1 
ATOM   8436  O  O   . LEU D  1 64  ? 97.037  34.008  -31.071 1.00 7.92  ? 64   LEU D O   1 
ATOM   8437  C  CB  . LEU D  1 64  ? 99.955  33.062  -32.317 1.00 9.70  ? 64   LEU D CB  1 
ATOM   8438  C  CG  . LEU D  1 64  ? 101.304 32.333  -32.394 1.00 11.15 ? 64   LEU D CG  1 
ATOM   8439  C  CD1 . LEU D  1 64  ? 101.653 32.007  -33.880 1.00 14.79 ? 64   LEU D CD1 1 
ATOM   8440  C  CD2 . LEU D  1 64  ? 102.391 33.193  -31.790 1.00 10.11 ? 64   LEU D CD2 1 
ATOM   8441  N  N   . PRO D  1 65  ? 98.618  35.479  -30.667 1.00 7.46  ? 65   PRO D N   1 
ATOM   8442  C  CA  . PRO D  1 65  ? 97.631  36.570  -30.606 1.00 7.59  ? 65   PRO D CA  1 
ATOM   8443  C  C   . PRO D  1 65  ? 96.800  36.633  -31.922 1.00 7.93  ? 65   PRO D C   1 
ATOM   8444  O  O   . PRO D  1 65  ? 97.336  36.480  -33.021 1.00 7.92  ? 65   PRO D O   1 
ATOM   8445  C  CB  . PRO D  1 65  ? 98.492  37.833  -30.408 1.00 7.06  ? 65   PRO D CB  1 
ATOM   8446  C  CG  . PRO D  1 65  ? 99.859  37.289  -29.830 1.00 7.87  ? 65   PRO D CG  1 
ATOM   8447  C  CD  . PRO D  1 65  ? 100.008 35.923  -30.455 1.00 7.91  ? 65   PRO D CD  1 
ATOM   8448  N  N   . HIS D  1 66  ? 95.492  36.849  -31.799 1.00 8.24  ? 66   HIS D N   1 
ATOM   8449  C  CA  . HIS D  1 66  ? 94.644  36.965  -32.959 1.00 8.27  ? 66   HIS D CA  1 
ATOM   8450  C  C   . HIS D  1 66  ? 93.403  37.785  -32.660 1.00 9.00  ? 66   HIS D C   1 
ATOM   8451  O  O   . HIS D  1 66  ? 93.194  38.252  -31.535 1.00 8.66  ? 66   HIS D O   1 
ATOM   8452  C  CB  . HIS D  1 66  ? 94.212  35.549  -33.389 1.00 8.65  ? 66   HIS D CB  1 
ATOM   8453  C  CG  . HIS D  1 66  ? 93.393  34.841  -32.346 1.00 6.61  ? 66   HIS D CG  1 
ATOM   8454  N  ND1 . HIS D  1 66  ? 93.949  34.207  -31.255 1.00 10.08 ? 66   HIS D ND1 1 
ATOM   8455  C  CD2 . HIS D  1 66  ? 92.053  34.683  -32.223 1.00 7.88  ? 66   HIS D CD2 1 
ATOM   8456  C  CE1 . HIS D  1 66  ? 92.990  33.681  -30.506 1.00 8.82  ? 66   HIS D CE1 1 
ATOM   8457  N  NE2 . HIS D  1 66  ? 91.827  33.958  -31.073 1.00 10.00 ? 66   HIS D NE2 1 
ATOM   8458  N  N   . ILE D  1 67  ? 92.545  37.910  -33.665 1.00 9.37  ? 67   ILE D N   1 
ATOM   8459  C  CA  . ILE D  1 67  ? 91.335  38.704  -33.535 1.00 9.21  ? 67   ILE D CA  1 
ATOM   8460  C  C   . ILE D  1 67  ? 90.240  37.945  -34.279 1.00 8.67  ? 67   ILE D C   1 
ATOM   8461  O  O   . ILE D  1 67  ? 90.545  37.187  -35.209 1.00 8.72  ? 67   ILE D O   1 
ATOM   8462  C  CB  . ILE D  1 67  ? 91.595  40.069  -34.225 1.00 9.52  ? 67   ILE D CB  1 
ATOM   8463  C  CG1 . ILE D  1 67  ? 91.745  41.155  -33.212 1.00 9.36  ? 67   ILE D CG1 1 
ATOM   8464  C  CG2 . ILE D  1 67  ? 90.442  40.444  -35.131 1.00 13.13 ? 67   ILE D CG2 1 
ATOM   8465  C  CD1 . ILE D  1 67  ? 91.681  42.548  -33.780 1.00 11.82 ? 67   ILE D CD1 1 
ATOM   8466  N  N   . HIS D  1 68  ? 88.975  38.135  -33.884 1.00 8.13  ? 68   HIS D N   1 
ATOM   8467  C  CA  . HIS D  1 68  ? 87.855  37.695  -34.693 1.00 7.80  ? 68   HIS D CA  1 
ATOM   8468  C  C   . HIS D  1 68  ? 87.071  38.904  -35.120 1.00 8.81  ? 68   HIS D C   1 
ATOM   8469  O  O   . HIS D  1 68  ? 86.910  39.881  -34.356 1.00 8.56  ? 68   HIS D O   1 
ATOM   8470  C  CB  . HIS D  1 68  ? 86.959  36.785  -33.914 1.00 8.42  ? 68   HIS D CB  1 
ATOM   8471  C  CG  . HIS D  1 68  ? 87.714  35.709  -33.212 1.00 10.71 ? 68   HIS D CG  1 
ATOM   8472  N  ND1 . HIS D  1 68  ? 88.407  34.731  -33.892 1.00 9.17  ? 68   HIS D ND1 1 
ATOM   8473  C  CD2 . HIS D  1 68  ? 87.944  35.493  -31.892 1.00 13.24 ? 68   HIS D CD2 1 
ATOM   8474  C  CE1 . HIS D  1 68  ? 88.999  33.932  -33.018 1.00 10.42 ? 68   HIS D CE1 1 
ATOM   8475  N  NE2 . HIS D  1 68  ? 88.734  34.372  -31.804 1.00 14.15 ? 68   HIS D NE2 1 
ATOM   8476  N  N   . GLN D  1 69  ? 86.569  38.847  -36.334 1.00 6.91  ? 69   GLN D N   1 
ATOM   8477  C  CA  . GLN D  1 69  ? 85.804  39.972  -36.848 1.00 7.97  ? 69   GLN D CA  1 
ATOM   8478  C  C   . GLN D  1 69  ? 84.293  39.711  -36.676 1.00 8.25  ? 69   GLN D C   1 
ATOM   8479  O  O   . GLN D  1 69  ? 83.485  40.659  -36.621 1.00 7.51  ? 69   GLN D O   1 
ATOM   8480  C  CB  . GLN D  1 69  ? 86.163  40.194  -38.310 1.00 8.72  ? 69   GLN D CB  1 
ATOM   8481  C  CG  . GLN D  1 69  ? 87.328  41.162  -38.491 1.00 13.03 ? 69   GLN D CG  1 
ATOM   8482  C  CD  . GLN D  1 69  ? 87.736  41.343  -39.953 1.00 19.46 ? 69   GLN D CD  1 
ATOM   8483  O  OE1 . GLN D  1 69  ? 87.053  40.881  -40.871 1.00 19.81 ? 69   GLN D OE1 1 
ATOM   8484  N  NE2 . GLN D  1 69  ? 88.871  41.997  -40.166 1.00 21.93 ? 69   GLN D NE2 1 
ATOM   8485  N  N   . LYS D  1 70  ? 83.918  38.437  -36.562 1.00 7.92  ? 70   LYS D N   1 
ATOM   8486  C  CA  . LYS D  1 70  ? 82.512  38.106  -36.535 1.00 9.92  ? 70   LYS D CA  1 
ATOM   8487  C  C   . LYS D  1 70  ? 82.046  37.417  -35.277 1.00 10.06 ? 70   LYS D C   1 
ATOM   8488  O  O   . LYS D  1 70  ? 80.842  37.263  -35.111 1.00 11.55 ? 70   LYS D O   1 
ATOM   8489  C  CB  . LYS D  1 70  ? 82.133  37.247  -37.738 1.00 9.86  ? 70   LYS D CB  1 
ATOM   8490  C  CG  . LYS D  1 70  ? 82.281  38.010  -39.036 1.00 14.33 ? 70   LYS D CG  1 
ATOM   8491  C  CD  . LYS D  1 70  ? 82.302  37.097  -40.252 1.00 21.79 ? 70   LYS D CD  1 
ATOM   8492  C  CE  . LYS D  1 70  ? 81.548  35.812  -40.019 1.00 26.50 ? 70   LYS D CE  1 
ATOM   8493  N  NZ  . LYS D  1 70  ? 80.084  36.043  -40.248 1.00 29.27 ? 70   LYS D NZ  1 
ATOM   8494  N  N   . HIS D  1 71  ? 82.964  37.058  -34.387 1.00 8.83  ? 71   HIS D N   1 
ATOM   8495  C  CA  . HIS D  1 71  ? 82.621  36.302  -33.202 1.00 8.22  ? 71   HIS D CA  1 
ATOM   8496  C  C   . HIS D  1 71  ? 82.991  37.053  -31.928 1.00 8.40  ? 71   HIS D C   1 
ATOM   8497  O  O   . HIS D  1 71  ? 84.050  37.632  -31.854 1.00 7.42  ? 71   HIS D O   1 
ATOM   8498  C  CB  . HIS D  1 71  ? 83.317  34.955  -33.206 1.00 6.97  ? 71   HIS D CB  1 
ATOM   8499  C  CG  . HIS D  1 71  ? 82.848  34.090  -34.323 1.00 8.36  ? 71   HIS D CG  1 
ATOM   8500  N  ND1 . HIS D  1 71  ? 83.388  34.166  -35.589 1.00 3.82  ? 71   HIS D ND1 1 
ATOM   8501  C  CD2 . HIS D  1 71  ? 81.857  33.160  -34.378 1.00 6.55  ? 71   HIS D CD2 1 
ATOM   8502  C  CE1 . HIS D  1 71  ? 82.754  33.311  -36.376 1.00 6.60  ? 71   HIS D CE1 1 
ATOM   8503  N  NE2 . HIS D  1 71  ? 81.812  32.700  -35.673 1.00 7.23  ? 71   HIS D NE2 1 
ATOM   8504  N  N   . TYR D  1 72  ? 82.073  37.025  -30.960 1.00 7.91  ? 72   TYR D N   1 
ATOM   8505  C  CA  . TYR D  1 72  ? 82.287  37.586  -29.631 1.00 7.51  ? 72   TYR D CA  1 
ATOM   8506  C  C   . TYR D  1 72  ? 82.707  36.404  -28.783 1.00 8.53  ? 72   TYR D C   1 
ATOM   8507  O  O   . TYR D  1 72  ? 81.977  35.383  -28.689 1.00 8.49  ? 72   TYR D O   1 
ATOM   8508  C  CB  . TYR D  1 72  ? 80.965  38.245  -29.159 1.00 7.18  ? 72   TYR D CB  1 
ATOM   8509  C  CG  . TYR D  1 72  ? 81.059  39.125  -27.935 1.00 5.80  ? 72   TYR D CG  1 
ATOM   8510  C  CD1 . TYR D  1 72  ? 81.761  38.731  -26.794 1.00 4.61  ? 72   TYR D CD1 1 
ATOM   8511  C  CD2 . TYR D  1 72  ? 80.495  40.431  -27.957 1.00 7.89  ? 72   TYR D CD2 1 
ATOM   8512  C  CE1 . TYR D  1 72  ? 81.838  39.590  -25.668 1.00 6.69  ? 72   TYR D CE1 1 
ATOM   8513  C  CE2 . TYR D  1 72  ? 80.574  41.280  -26.857 1.00 3.19  ? 72   TYR D CE2 1 
ATOM   8514  C  CZ  . TYR D  1 72  ? 81.232  40.848  -25.712 1.00 5.53  ? 72   TYR D CZ  1 
ATOM   8515  O  OH  . TYR D  1 72  ? 81.289  41.699  -24.619 1.00 10.31 ? 72   TYR D OH  1 
ATOM   8516  N  N   . GLU D  1 73  ? 83.916  36.484  -28.227 1.00 8.31  ? 73   GLU D N   1 
ATOM   8517  C  CA  . GLU D  1 73  ? 84.427  35.425  -27.369 1.00 9.41  ? 73   GLU D CA  1 
ATOM   8518  C  C   . GLU D  1 73  ? 84.316  35.755  -25.877 1.00 8.99  ? 73   GLU D C   1 
ATOM   8519  O  O   . GLU D  1 73  ? 84.482  36.911  -25.458 1.00 10.76 ? 73   GLU D O   1 
ATOM   8520  C  CB  . GLU D  1 73  ? 85.856  35.027  -27.780 1.00 10.22 ? 73   GLU D CB  1 
ATOM   8521  C  CG  . GLU D  1 73  ? 85.839  34.303  -29.127 1.00 13.54 ? 73   GLU D CG  1 
ATOM   8522  C  CD  . GLU D  1 73  ? 87.118  33.535  -29.428 1.00 21.65 ? 73   GLU D CD  1 
ATOM   8523  O  OE1 . GLU D  1 73  ? 88.207  33.959  -28.916 1.00 23.01 ? 73   GLU D OE1 1 
ATOM   8524  O  OE2 . GLU D  1 73  ? 87.037  32.506  -30.212 1.00 22.89 ? 73   GLU D OE2 1 
ATOM   8525  N  N   . ASN D  1 74  ? 84.020  34.728  -25.093 1.00 9.05  ? 74   ASN D N   1 
ATOM   8526  C  CA  . ASN D  1 74  ? 83.818  34.842  -23.628 1.00 9.44  ? 74   ASN D CA  1 
ATOM   8527  C  C   . ASN D  1 74  ? 84.624  33.745  -22.940 1.00 9.81  ? 74   ASN D C   1 
ATOM   8528  O  O   . ASN D  1 74  ? 84.498  32.580  -23.284 1.00 10.65 ? 74   ASN D O   1 
ATOM   8529  C  CB  . ASN D  1 74  ? 82.326  34.680  -23.280 1.00 6.88  ? 74   ASN D CB  1 
ATOM   8530  C  CG  . ASN D  1 74  ? 81.484  35.783  -23.851 1.00 9.60  ? 74   ASN D CG  1 
ATOM   8531  O  OD1 . ASN D  1 74  ? 81.479  36.875  -23.330 1.00 8.76  ? 74   ASN D OD1 1 
ATOM   8532  N  ND2 . ASN D  1 74  ? 80.747  35.493  -24.924 1.00 7.81  ? 74   ASN D ND2 1 
ATOM   8533  N  N   . PHE D  1 75  ? 85.463  34.140  -21.979 1.00 10.03 ? 75   PHE D N   1 
ATOM   8534  C  CA  . PHE D  1 75  ? 86.314  33.197  -21.286 1.00 9.52  ? 75   PHE D CA  1 
ATOM   8535  C  C   . PHE D  1 75  ? 85.855  33.108  -19.869 1.00 9.89  ? 75   PHE D C   1 
ATOM   8536  O  O   . PHE D  1 75  ? 85.734  34.159  -19.198 1.00 9.27  ? 75   PHE D O   1 
ATOM   8537  C  CB  . PHE D  1 75  ? 87.740  33.721  -21.300 1.00 9.73  ? 75   PHE D CB  1 
ATOM   8538  C  CG  . PHE D  1 75  ? 88.382  33.677  -22.659 1.00 9.56  ? 75   PHE D CG  1 
ATOM   8539  C  CD1 . PHE D  1 75  ? 88.073  34.642  -23.623 1.00 10.03 ? 75   PHE D CD1 1 
ATOM   8540  C  CD2 . PHE D  1 75  ? 89.313  32.695  -22.953 1.00 7.35  ? 75   PHE D CD2 1 
ATOM   8541  C  CE1 . PHE D  1 75  ? 88.689  34.630  -24.855 1.00 9.60  ? 75   PHE D CE1 1 
ATOM   8542  C  CE2 . PHE D  1 75  ? 89.928  32.650  -24.198 1.00 11.46 ? 75   PHE D CE2 1 
ATOM   8543  C  CZ  . PHE D  1 75  ? 89.611  33.585  -25.170 1.00 9.29  ? 75   PHE D CZ  1 
ATOM   8544  N  N   . TYR D  1 76  ? 85.605  31.868  -19.420 1.00 8.51  ? 76   TYR D N   1 
ATOM   8545  C  CA  . TYR D  1 76  ? 85.158  31.632  -18.053 1.00 8.85  ? 76   TYR D CA  1 
ATOM   8546  C  C   . TYR D  1 76  ? 86.011  30.549  -17.451 1.00 8.74  ? 76   TYR D C   1 
ATOM   8547  O  O   . TYR D  1 76  ? 86.186  29.498  -18.062 1.00 10.51 ? 76   TYR D O   1 
ATOM   8548  C  CB  . TYR D  1 76  ? 83.686  31.267  -18.008 1.00 7.29  ? 76   TYR D CB  1 
ATOM   8549  C  CG  . TYR D  1 76  ? 83.137  31.130  -16.609 1.00 7.90  ? 76   TYR D CG  1 
ATOM   8550  C  CD1 . TYR D  1 76  ? 82.687  32.267  -15.892 1.00 4.86  ? 76   TYR D CD1 1 
ATOM   8551  C  CD2 . TYR D  1 76  ? 83.012  29.872  -16.021 1.00 6.82  ? 76   TYR D CD2 1 
ATOM   8552  C  CE1 . TYR D  1 76  ? 82.139  32.110  -14.572 1.00 8.02  ? 76   TYR D CE1 1 
ATOM   8553  C  CE2 . TYR D  1 76  ? 82.459  29.708  -14.744 1.00 9.79  ? 76   TYR D CE2 1 
ATOM   8554  C  CZ  . TYR D  1 76  ? 82.010  30.830  -14.034 1.00 11.93 ? 76   TYR D CZ  1 
ATOM   8555  O  OH  . TYR D  1 76  ? 81.490  30.647  -12.731 1.00 12.14 ? 76   TYR D OH  1 
ATOM   8556  N  N   . CYS D  1 77  ? 86.588  30.823  -16.298 1.00 8.77  ? 77   CYS D N   1 
ATOM   8557  C  CA  . CYS D  1 77  ? 87.436  29.813  -15.645 1.00 7.98  ? 77   CYS D CA  1 
ATOM   8558  C  C   . CYS D  1 77  ? 86.622  28.877  -14.774 1.00 8.91  ? 77   CYS D C   1 
ATOM   8559  O  O   . CYS D  1 77  ? 86.095  29.271  -13.728 1.00 7.82  ? 77   CYS D O   1 
ATOM   8560  C  CB  . CYS D  1 77  ? 88.528  30.495  -14.799 1.00 8.28  ? 77   CYS D CB  1 
ATOM   8561  S  SG  . CYS D  1 77  ? 89.635  29.287  -14.069 1.00 10.22 ? 77   CYS D SG  1 
ATOM   8562  N  N   . ASN D  1 78  ? 86.533  27.619  -15.167 1.00 8.50  ? 78   ASN D N   1 
ATOM   8563  C  CA  . ASN D  1 78  ? 85.816  26.672  -14.325 1.00 9.10  ? 78   ASN D CA  1 
ATOM   8564  C  C   . ASN D  1 78  ? 86.608  26.230  -13.111 1.00 9.25  ? 78   ASN D C   1 
ATOM   8565  O  O   . ASN D  1 78  ? 86.032  26.000  -12.022 1.00 10.53 ? 78   ASN D O   1 
ATOM   8566  C  CB  D ASN D  1 78  ? 85.391  25.429  -15.116 0.50 6.92  ? 78   ASN D CB  1 
ATOM   8567  C  CG  D ASN D  1 78  ? 84.637  25.792  -16.317 0.50 7.70  ? 78   ASN D CG  1 
ATOM   8568  O  OD1 D ASN D  1 78  ? 85.221  25.960  -17.378 0.50 10.20 ? 78   ASN D OD1 1 
ATOM   8569  N  ND2 D ASN D  1 78  ? 83.315  25.929  -16.190 0.50 6.97  ? 78   ASN D ND2 1 
ATOM   8570  N  N   . LYS D  1 79  ? 87.907  26.067  -13.314 1.00 7.70  ? 79   LYS D N   1 
ATOM   8571  C  CA  . LYS D  1 79  ? 88.847  25.613  -12.295 1.00 8.08  ? 79   LYS D CA  1 
ATOM   8572  C  C   . LYS D  1 79  ? 90.282  25.861  -12.810 1.00 8.09  ? 79   LYS D C   1 
ATOM   8573  O  O   . LYS D  1 79  ? 90.486  26.146  -13.990 1.00 7.53  ? 79   LYS D O   1 
ATOM   8574  C  CB  . LYS D  1 79  ? 88.646  24.130  -11.906 1.00 9.39  ? 79   LYS D CB  1 
ATOM   8575  C  CG  . LYS D  1 79  ? 88.823  23.104  -13.084 1.00 9.95  ? 79   LYS D CG  1 
ATOM   8576  C  CD  . LYS D  1 79  ? 88.805  21.664  -12.534 1.00 10.18 ? 79   LYS D CD  1 
ATOM   8577  C  CE  . LYS D  1 79  ? 88.609  20.601  -13.626 1.00 8.69  ? 79   LYS D CE  1 
ATOM   8578  N  NZ  . LYS D  1 79  ? 88.941  19.271  -13.030 1.00 9.89  ? 79   LYS D NZ  1 
ATOM   8579  N  N   . GLY D  1 80  ? 91.231  25.824  -11.894 1.00 5.82  ? 80   GLY D N   1 
ATOM   8580  C  CA  . GLY D  1 80  ? 92.609  26.029  -12.229 1.00 8.12  ? 80   GLY D CA  1 
ATOM   8581  C  C   . GLY D  1 80  ? 92.768  27.512  -12.522 1.00 8.15  ? 80   GLY D C   1 
ATOM   8582  O  O   . GLY D  1 80  ? 92.049  28.326  -11.925 1.00 7.26  ? 80   GLY D O   1 
ATOM   8583  N  N   . SER D  1 81  ? 93.668  27.865  -13.435 1.00 8.76  ? 81   SER D N   1 
ATOM   8584  C  CA  . SER D  1 81  ? 93.823  29.275  -13.771 1.00 8.29  ? 81   SER D CA  1 
ATOM   8585  C  C   . SER D  1 81  ? 94.539  29.480  -15.108 1.00 8.88  ? 81   SER D C   1 
ATOM   8586  O  O   . SER D  1 81  ? 95.313  28.639  -15.519 1.00 8.07  ? 81   SER D O   1 
ATOM   8587  C  CB  . SER D  1 81  ? 94.586  30.073  -12.683 1.00 8.35  ? 81   SER D CB  1 
ATOM   8588  O  OG  . SER D  1 81  ? 95.915  29.639  -12.554 1.00 10.19 ? 81   SER D OG  1 
ATOM   8589  N  N   . PHE D  1 82  ? 94.260  30.623  -15.745 1.00 8.47  ? 82   PHE D N   1 
ATOM   8590  C  CA  . PHE D  1 82  ? 94.869  30.969  -17.045 1.00 8.45  ? 82   PHE D CA  1 
ATOM   8591  C  C   . PHE D  1 82  ? 94.880  32.480  -17.169 1.00 9.57  ? 82   PHE D C   1 
ATOM   8592  O  O   . PHE D  1 82  ? 93.930  33.167  -16.690 1.00 9.21  ? 82   PHE D O   1 
ATOM   8593  C  CB  . PHE D  1 82  ? 94.103  30.269  -18.214 1.00 8.28  ? 82   PHE D CB  1 
ATOM   8594  C  CG  . PHE D  1 82  ? 92.666  30.716  -18.407 1.00 9.78  ? 82   PHE D CG  1 
ATOM   8595  C  CD1 . PHE D  1 82  ? 92.351  31.837  -19.180 1.00 10.43 ? 82   PHE D CD1 1 
ATOM   8596  C  CD2 . PHE D  1 82  ? 91.616  30.011  -17.832 1.00 10.31 ? 82   PHE D CD2 1 
ATOM   8597  C  CE1 . PHE D  1 82  ? 90.954  32.233  -19.379 1.00 10.17 ? 82   PHE D CE1 1 
ATOM   8598  C  CE2 . PHE D  1 82  ? 90.246  30.389  -18.022 1.00 9.67  ? 82   PHE D CE2 1 
ATOM   8599  C  CZ  . PHE D  1 82  ? 89.926  31.532  -18.777 1.00 10.56 ? 82   PHE D CZ  1 
ATOM   8600  N  N   . GLN D  1 83  ? 95.930  33.007  -17.797 1.00 8.64  ? 83   GLN D N   1 
ATOM   8601  C  CA  . GLN D  1 83  ? 96.018  34.433  -18.081 1.00 9.92  ? 83   GLN D CA  1 
ATOM   8602  C  C   . GLN D  1 83  ? 95.377  34.721  -19.425 1.00 10.28 ? 83   GLN D C   1 
ATOM   8603  O  O   . GLN D  1 83  ? 95.424  33.875  -20.340 1.00 9.33  ? 83   GLN D O   1 
ATOM   8604  C  CB  . GLN D  1 83  ? 97.438  34.883  -18.107 1.00 8.97  ? 83   GLN D CB  1 
ATOM   8605  C  CG  . GLN D  1 83  ? 97.599  36.414  -18.220 1.00 7.87  ? 83   GLN D CG  1 
ATOM   8606  C  CD  . GLN D  1 83  ? 98.810  36.919  -17.509 1.00 7.63  ? 83   GLN D CD  1 
ATOM   8607  O  OE1 . GLN D  1 83  ? 99.103  38.153  -17.515 1.00 9.22  ? 83   GLN D OE1 1 
ATOM   8608  N  NE2 . GLN D  1 83  ? 99.565  36.005  -16.928 1.00 4.82  ? 83   GLN D NE2 1 
ATOM   8609  N  N   . LEU D  1 84  ? 94.742  35.890  -19.500 1.00 8.85  ? 84   LEU D N   1 
ATOM   8610  C  CA  . LEU D  1 84  ? 94.062  36.336  -20.700 1.00 8.57  ? 84   LEU D CA  1 
ATOM   8611  C  C   . LEU D  1 84  ? 94.567  37.737  -20.940 1.00 8.28  ? 84   LEU D C   1 
ATOM   8612  O  O   . LEU D  1 84  ? 94.782  38.494  -19.988 1.00 8.23  ? 84   LEU D O   1 
ATOM   8613  C  CB  . LEU D  1 84  ? 92.521  36.302  -20.541 1.00 9.20  ? 84   LEU D CB  1 
ATOM   8614  C  CG  . LEU D  1 84  ? 91.595  36.847  -21.652 1.00 9.57  ? 84   LEU D CG  1 
ATOM   8615  C  CD1 . LEU D  1 84  ? 91.816  36.134  -23.020 1.00 10.74 ? 84   LEU D CD1 1 
ATOM   8616  C  CD2 . LEU D  1 84  ? 90.109  36.773  -21.244 1.00 10.76 ? 84   LEU D CD2 1 
ATOM   8617  N  N   . TRP D  1 85  ? 94.832  38.062  -22.206 1.00 7.57  ? 85   TRP D N   1 
ATOM   8618  C  CA  . TRP D  1 85  ? 95.311  39.374  -22.558 1.00 6.69  ? 85   TRP D CA  1 
ATOM   8619  C  C   . TRP D  1 85  ? 94.386  39.886  -23.642 1.00 8.41  ? 85   TRP D C   1 
ATOM   8620  O  O   . TRP D  1 85  ? 94.034  39.120  -24.552 1.00 7.74  ? 85   TRP D O   1 
ATOM   8621  C  CB  . TRP D  1 85  ? 96.709  39.278  -23.203 1.00 6.27  ? 85   TRP D CB  1 
ATOM   8622  C  CG  . TRP D  1 85  ? 97.896  39.037  -22.322 1.00 4.78  ? 85   TRP D CG  1 
ATOM   8623  C  CD1 . TRP D  1 85  ? 98.802  39.983  -21.837 1.00 4.96  ? 85   TRP D CD1 1 
ATOM   8624  C  CD2 . TRP D  1 85  ? 98.409  37.771  -21.939 1.00 4.00  ? 85   TRP D CD2 1 
ATOM   8625  N  NE1 . TRP D  1 85  ? 99.811  39.349  -21.148 1.00 5.92  ? 85   TRP D NE1 1 
ATOM   8626  C  CE2 . TRP D  1 85  ? 99.599  37.994  -21.203 1.00 4.44  ? 85   TRP D CE2 1 
ATOM   8627  C  CE3 . TRP D  1 85  ? 97.958  36.453  -22.104 1.00 5.96  ? 85   TRP D CE3 1 
ATOM   8628  C  CZ2 . TRP D  1 85  ? 100.347 36.952  -20.663 1.00 3.64  ? 85   TRP D CZ2 1 
ATOM   8629  C  CZ3 . TRP D  1 85  ? 98.706  35.433  -21.602 1.00 7.62  ? 85   TRP D CZ3 1 
ATOM   8630  C  CH2 . TRP D  1 85  ? 99.890  35.680  -20.869 1.00 3.74  ? 85   TRP D CH2 1 
ATOM   8631  N  N   . ALA D  1 86  ? 94.019  41.175  -23.589 1.00 8.03  ? 86   ALA D N   1 
ATOM   8632  C  CA  . ALA D  1 86  ? 93.097  41.742  -24.585 1.00 7.76  ? 86   ALA D CA  1 
ATOM   8633  C  C   . ALA D  1 86  ? 93.400  43.180  -24.862 1.00 8.66  ? 86   ALA D C   1 
ATOM   8634  O  O   . ALA D  1 86  ? 93.781  43.910  -23.932 1.00 8.94  ? 86   ALA D O   1 
ATOM   8635  C  CB  . ALA D  1 86  ? 91.657  41.621  -24.080 1.00 8.71  ? 86   ALA D CB  1 
ATOM   8636  N  N   . GLN D  1 87  ? 93.214  43.599  -26.127 1.00 7.32  ? 87   GLN D N   1 
ATOM   8637  C  CA  . GLN D  1 87  ? 93.345  44.992  -26.497 1.00 8.03  ? 87   GLN D CA  1 
ATOM   8638  C  C   . GLN D  1 87  ? 92.377  45.375  -27.608 1.00 8.11  ? 87   GLN D C   1 
ATOM   8639  O  O   . GLN D  1 87  ? 92.299  44.691  -28.625 1.00 9.11  ? 87   GLN D O   1 
ATOM   8640  C  CB  . GLN D  1 87  ? 94.783  45.290  -26.940 1.00 7.95  ? 87   GLN D CB  1 
ATOM   8641  C  CG  . GLN D  1 87  ? 95.001  46.779  -27.244 1.00 8.68  ? 87   GLN D CG  1 
ATOM   8642  C  CD  . GLN D  1 87  ? 96.442  47.084  -27.438 1.00 12.26 ? 87   GLN D CD  1 
ATOM   8643  O  OE1 . GLN D  1 87  ? 97.185  46.243  -27.935 1.00 12.32 ? 87   GLN D OE1 1 
ATOM   8644  N  NE2 . GLN D  1 87  ? 96.860  48.279  -27.046 1.00 13.64 ? 87   GLN D NE2 1 
ATOM   8645  N  N   . SER D  1 88  ? 91.655  46.479  -27.417 1.00 8.28  ? 88   SER D N   1 
ATOM   8646  C  CA  . SER D  1 88  ? 90.841  47.050  -28.468 1.00 8.97  ? 88   SER D CA  1 
ATOM   8647  C  C   . SER D  1 88  ? 91.533  48.358  -28.931 1.00 10.25 ? 88   SER D C   1 
ATOM   8648  O  O   . SER D  1 88  ? 91.906  49.205  -28.099 1.00 10.40 ? 88   SER D O   1 
ATOM   8649  C  CB  . SER D  1 88  ? 89.417  47.310  -27.970 1.00 8.03  ? 88   SER D CB  1 
ATOM   8650  O  OG  . SER D  1 88  ? 88.800  48.353  -28.724 1.00 10.51 ? 88   SER D OG  1 
ATOM   8651  N  N   . GLY D  1 89  ? 91.700  48.502  -30.245 1.00 11.64 ? 89   GLY D N   1 
ATOM   8652  C  CA  . GLY D  1 89  ? 92.388  49.632  -30.847 1.00 11.72 ? 89   GLY D CA  1 
ATOM   8653  C  C   . GLY D  1 89  ? 93.740  49.970  -30.231 1.00 13.11 ? 89   GLY D C   1 
ATOM   8654  O  O   . GLY D  1 89  ? 94.626  49.107  -30.104 1.00 13.69 ? 89   GLY D O   1 
ATOM   8655  N  N   . ASN D  1 90  ? 93.903  51.247  -29.882 1.00 13.84 ? 90   ASN D N   1 
ATOM   8656  C  CA  . ASN D  1 90  ? 95.050  51.716  -29.099 1.00 15.11 ? 90   ASN D CA  1 
ATOM   8657  C  C   . ASN D  1 90  ? 94.692  51.992  -27.622 1.00 14.15 ? 90   ASN D C   1 
ATOM   8658  O  O   . ASN D  1 90  ? 95.350  52.775  -26.933 1.00 14.98 ? 90   ASN D O   1 
ATOM   8659  C  CB  . ASN D  1 90  ? 95.777  52.903  -29.804 1.00 16.12 ? 90   ASN D CB  1 
ATOM   8660  C  CG  . ASN D  1 90  ? 95.242  54.290  -29.396 1.00 20.77 ? 90   ASN D CG  1 
ATOM   8661  O  OD1 . ASN D  1 90  ? 96.036  55.241  -29.145 1.00 23.86 ? 90   ASN D OD1 1 
ATOM   8662  N  ND2 . ASN D  1 90  ? 93.902  54.432  -29.344 1.00 24.95 ? 90   ASN D ND2 1 
ATOM   8663  N  N   . GLU D  1 91  ? 93.638  51.357  -27.126 1.00 12.98 ? 91   GLU D N   1 
ATOM   8664  C  CA  . GLU D  1 91  ? 93.367  51.469  -25.687 1.00 11.31 ? 91   GLU D CA  1 
ATOM   8665  C  C   . GLU D  1 91  ? 94.465  50.681  -24.981 1.00 9.68  ? 91   GLU D C   1 
ATOM   8666  O  O   . GLU D  1 91  ? 95.109  49.843  -25.601 1.00 8.86  ? 91   GLU D O   1 
ATOM   8667  C  CB  . GLU D  1 91  ? 91.997  50.917  -25.345 1.00 11.31 ? 91   GLU D CB  1 
ATOM   8668  C  CG  . GLU D  1 91  ? 90.840  51.632  -26.033 1.00 13.99 ? 91   GLU D CG  1 
ATOM   8669  C  CD  . GLU D  1 91  ? 89.518  50.910  -25.804 1.00 18.27 ? 91   GLU D CD  1 
ATOM   8670  O  OE1 . GLU D  1 91  ? 89.428  50.059  -24.873 1.00 22.20 ? 91   GLU D OE1 1 
ATOM   8671  O  OE2 . GLU D  1 91  ? 88.559  51.188  -26.548 1.00 20.43 ? 91   GLU D OE2 1 
ATOM   8672  N  N   . THR D  1 92  ? 94.708  50.979  -23.715 1.00 8.18  ? 92   THR D N   1 
ATOM   8673  C  CA  . THR D  1 92  ? 95.752  50.295  -22.979 1.00 7.14  ? 92   THR D CA  1 
ATOM   8674  C  C   . THR D  1 92  ? 95.454  48.783  -23.043 1.00 6.93  ? 92   THR D C   1 
ATOM   8675  O  O   . THR D  1 92  ? 94.311  48.383  -22.867 1.00 7.66  ? 92   THR D O   1 
ATOM   8676  C  CB  . THR D  1 92  ? 95.741  50.792  -21.565 1.00 7.35  ? 92   THR D CB  1 
ATOM   8677  O  OG1 . THR D  1 92  ? 96.068  52.187  -21.554 1.00 8.61  ? 92   THR D OG1 1 
ATOM   8678  C  CG2 . THR D  1 92  ? 96.867  50.131  -20.720 1.00 6.80  ? 92   THR D CG2 1 
ATOM   8679  N  N   . GLN D  1 93  ? 96.462  47.970  -23.346 1.00 6.49  ? 93   GLN D N   1 
ATOM   8680  C  CA  . GLN D  1 93  ? 96.338  46.522  -23.281 1.00 6.88  ? 93   GLN D CA  1 
ATOM   8681  C  C   . GLN D  1 93  ? 96.039  46.047  -21.830 1.00 6.32  ? 93   GLN D C   1 
ATOM   8682  O  O   . GLN D  1 93  ? 96.697  46.465  -20.875 1.00 6.34  ? 93   GLN D O   1 
ATOM   8683  C  CB  . GLN D  1 93  ? 97.635  45.852  -23.765 1.00 7.29  ? 93   GLN D CB  1 
ATOM   8684  C  CG  . GLN D  1 93  ? 97.515  44.306  -23.829 1.00 6.22  ? 93   GLN D CG  1 
ATOM   8685  C  CD  . GLN D  1 93  ? 98.833  43.622  -24.047 1.00 7.19  ? 93   GLN D CD  1 
ATOM   8686  O  OE1 . GLN D  1 93  ? 99.129  42.634  -23.392 1.00 9.31  ? 93   GLN D OE1 1 
ATOM   8687  N  NE2 . GLN D  1 93  ? 99.637  44.145  -24.953 1.00 5.31  ? 93   GLN D NE2 1 
ATOM   8688  N  N   . GLN D  1 94  ? 95.049  45.177  -21.693 1.00 7.03  ? 94   GLN D N   1 
ATOM   8689  C  CA  . GLN D  1 94  ? 94.594  44.702  -20.385 1.00 7.21  ? 94   GLN D CA  1 
ATOM   8690  C  C   . GLN D  1 94  ? 94.946  43.231  -20.229 1.00 7.42  ? 94   GLN D C   1 
ATOM   8691  O  O   . GLN D  1 94  ? 94.809  42.441  -21.173 1.00 9.45  ? 94   GLN D O   1 
ATOM   8692  C  CB  . GLN D  1 94  ? 93.072  44.844  -20.273 1.00 6.66  ? 94   GLN D CB  1 
ATOM   8693  C  CG  . GLN D  1 94  ? 92.569  46.299  -20.221 1.00 3.80  ? 94   GLN D CG  1 
ATOM   8694  C  CD  . GLN D  1 94  ? 92.948  47.028  -18.924 1.00 6.52  ? 94   GLN D CD  1 
ATOM   8695  O  OE1 . GLN D  1 94  ? 93.143  46.396  -17.889 1.00 7.39  ? 94   GLN D OE1 1 
ATOM   8696  N  NE2 . GLN D  1 94  ? 93.096  48.339  -18.998 1.00 11.82 ? 94   GLN D NE2 1 
ATOM   8697  N  N   . THR D  1 95  ? 95.327  42.827  -19.035 1.00 6.59  ? 95   THR D N   1 
ATOM   8698  C  CA  . THR D  1 95  ? 95.426  41.377  -18.809 1.00 6.55  ? 95   THR D CA  1 
ATOM   8699  C  C   . THR D  1 95  ? 95.069  40.970  -17.362 1.00 6.15  ? 95   THR D C   1 
ATOM   8700  O  O   . THR D  1 95  ? 95.389  41.702  -16.428 1.00 6.19  ? 95   THR D O   1 
ATOM   8701  C  CB  . THR D  1 95  ? 96.863  40.944  -19.175 1.00 6.20  ? 95   THR D CB  1 
ATOM   8702  O  OG1 . THR D  1 95  ? 96.979  39.541  -18.979 1.00 6.30  ? 95   THR D OG1 1 
ATOM   8703  C  CG2 . THR D  1 95  ? 97.887  41.546  -18.202 1.00 4.38  ? 95   THR D CG2 1 
ATOM   8704  N  N   . ARG D  1 96  ? 94.447  39.807  -17.199 1.00 7.05  ? 96   ARG D N   1 
ATOM   8705  C  CA  . ARG D  1 96  ? 94.094  39.288  -15.892 1.00 7.53  ? 96   ARG D CA  1 
ATOM   8706  C  C   . ARG D  1 96  ? 94.521  37.849  -15.871 1.00 8.45  ? 96   ARG D C   1 
ATOM   8707  O  O   . ARG D  1 96  ? 94.471  37.162  -16.897 1.00 8.38  ? 96   ARG D O   1 
ATOM   8708  C  CB  . ARG D  1 96  ? 92.585  39.294  -15.650 1.00 7.28  ? 96   ARG D CB  1 
ATOM   8709  C  CG  . ARG D  1 96  ? 91.904  40.649  -15.625 1.00 5.27  ? 96   ARG D CG  1 
ATOM   8710  C  CD  . ARG D  1 96  ? 92.546  41.723  -14.706 1.00 7.67  ? 96   ARG D CD  1 
ATOM   8711  N  NE  . ARG D  1 96  ? 91.771  42.947  -14.905 1.00 6.32  ? 96   ARG D NE  1 
ATOM   8712  C  CZ  . ARG D  1 96  ? 92.147  43.936  -15.685 1.00 9.65  ? 96   ARG D CZ  1 
ATOM   8713  N  NH1 . ARG D  1 96  ? 93.356  43.926  -16.283 1.00 5.17  ? 96   ARG D NH1 1 
ATOM   8714  N  NH2 . ARG D  1 96  ? 91.323  44.959  -15.862 1.00 3.60  ? 96   ARG D NH2 1 
ATOM   8715  N  N   . VAL D  1 97  ? 94.892  37.383  -14.683 1.00 9.40  ? 97   VAL D N   1 
ATOM   8716  C  CA  . VAL D  1 97  ? 94.927  35.938  -14.448 1.00 9.89  ? 97   VAL D CA  1 
ATOM   8717  C  C   . VAL D  1 97  ? 93.589  35.465  -13.849 1.00 9.65  ? 97   VAL D C   1 
ATOM   8718  O  O   . VAL D  1 97  ? 93.274  35.817  -12.715 1.00 11.63 ? 97   VAL D O   1 
ATOM   8719  C  CB  . VAL D  1 97  ? 96.077  35.551  -13.517 1.00 10.33 ? 97   VAL D CB  1 
ATOM   8720  C  CG1 . VAL D  1 97  ? 96.161  34.050  -13.476 1.00 9.85  ? 97   VAL D CG1 1 
ATOM   8721  C  CG2 . VAL D  1 97  ? 97.385  36.148  -14.054 1.00 9.16  ? 97   VAL D CG2 1 
ATOM   8722  N  N   . LEU D  1 98  ? 92.798  34.707  -14.605 1.00 10.06 ? 98   LEU D N   1 
ATOM   8723  C  CA  . LEU D  1 98  ? 91.492  34.216  -14.144 1.00 8.77  ? 98   LEU D CA  1 
ATOM   8724  C  C   . LEU D  1 98  ? 91.695  32.947  -13.357 1.00 9.68  ? 98   LEU D C   1 
ATOM   8725  O  O   . LEU D  1 98  ? 92.397  32.065  -13.840 1.00 9.67  ? 98   LEU D O   1 
ATOM   8726  C  CB  . LEU D  1 98  ? 90.568  33.908  -15.329 1.00 9.22  ? 98   LEU D CB  1 
ATOM   8727  C  CG  . LEU D  1 98  ? 89.937  35.113  -16.050 1.00 6.89  ? 98   LEU D CG  1 
ATOM   8728  C  CD1 . LEU D  1 98  ? 90.996  35.953  -16.847 1.00 11.77 ? 98   LEU D CD1 1 
ATOM   8729  C  CD2 . LEU D  1 98  ? 88.803  34.634  -16.951 1.00 7.79  ? 98   LEU D CD2 1 
ATOM   8730  N  N   . SER D  1 99  ? 91.052  32.857  -12.177 1.00 8.58  ? 99   SER D N   1 
ATOM   8731  C  CA  . SER D  1 99  ? 90.995  31.641  -11.364 1.00 9.58  ? 99   SER D CA  1 
ATOM   8732  C  C   . SER D  1 99  ? 89.491  31.274  -11.232 1.00 9.37  ? 99   SER D C   1 
ATOM   8733  O  O   . SER D  1 99  ? 88.678  31.854  -11.929 1.00 7.81  ? 99   SER D O   1 
ATOM   8734  C  CB  . SER D  1 99  ? 91.639  31.873  -10.001 1.00 9.93  ? 99   SER D CB  1 
ATOM   8735  O  OG  . SER D  1 99  ? 91.073  33.022  -9.377  1.00 9.87  ? 99   SER D OG  1 
ATOM   8736  N  N   . SER D  1 100 ? 89.136  30.281  -10.433 1.00 10.19 ? 100  SER D N   1 
ATOM   8737  C  CA  . SER D  1 100 ? 87.783  29.698  -10.553 1.00 10.70 ? 100  SER D CA  1 
ATOM   8738  C  C   . SER D  1 100 ? 86.695  30.750  -10.408 1.00 9.88  ? 100  SER D C   1 
ATOM   8739  O  O   . SER D  1 100 ? 86.733  31.523  -9.453  1.00 9.66  ? 100  SER D O   1 
ATOM   8740  C  CB  . SER D  1 100 ? 87.531  28.619  -9.486  1.00 10.68 ? 100  SER D CB  1 
ATOM   8741  O  OG  . SER D  1 100 ? 88.503  27.630  -9.623  1.00 14.89 ? 100  SER D OG  1 
ATOM   8742  N  N   . GLY D  1 101 ? 85.752  30.761  -11.352 1.00 9.48  ? 101  GLY D N   1 
ATOM   8743  C  CA  . GLY D  1 101 ? 84.602  31.674  -11.337 1.00 8.78  ? 101  GLY D CA  1 
ATOM   8744  C  C   . GLY D  1 101 ? 84.877  33.042  -11.947 1.00 9.32  ? 101  GLY D C   1 
ATOM   8745  O  O   . GLY D  1 101 ? 83.948  33.876  -12.040 1.00 9.81  ? 101  GLY D O   1 
ATOM   8746  N  N   . ASP D  1 102 ? 86.134  33.294  -12.358 1.00 8.39  ? 102  ASP D N   1 
ATOM   8747  C  CA  . ASP D  1 102 ? 86.434  34.534  -13.074 1.00 9.54  ? 102  ASP D CA  1 
ATOM   8748  C  C   . ASP D  1 102 ? 86.031  34.489  -14.544 1.00 8.25  ? 102  ASP D C   1 
ATOM   8749  O  O   . ASP D  1 102 ? 85.900  33.409  -15.134 1.00 9.87  ? 102  ASP D O   1 
ATOM   8750  C  CB  . ASP D  1 102 ? 87.918  34.963  -12.987 1.00 8.91  ? 102  ASP D CB  1 
ATOM   8751  C  CG  . ASP D  1 102 ? 88.413  35.174  -11.559 1.00 10.87 ? 102  ASP D CG  1 
ATOM   8752  O  OD1 . ASP D  1 102 ? 87.569  35.353  -10.613 1.00 9.91  ? 102  ASP D OD1 1 
ATOM   8753  O  OD2 . ASP D  1 102 ? 89.669  35.167  -11.321 1.00 6.16  ? 102  ASP D OD2 1 
ATOM   8754  N  N   . TYR D  1 103 ? 85.868  35.691  -15.091 1.00 7.27  ? 103  TYR D N   1 
ATOM   8755  C  CA  . TYR D  1 103 ? 85.298  35.951  -16.388 1.00 7.24  ? 103  TYR D CA  1 
ATOM   8756  C  C   . TYR D  1 103 ? 86.030  37.044  -17.163 1.00 8.40  ? 103  TYR D C   1 
ATOM   8757  O  O   . TYR D  1 103 ? 86.420  38.090  -16.597 1.00 9.01  ? 103  TYR D O   1 
ATOM   8758  C  CB  . TYR D  1 103 ? 83.811  36.292  -16.242 1.00 5.58  ? 103  TYR D CB  1 
ATOM   8759  C  CG  . TYR D  1 103 ? 83.226  36.829  -17.552 1.00 7.94  ? 103  TYR D CG  1 
ATOM   8760  C  CD1 . TYR D  1 103 ? 82.947  35.964  -18.620 1.00 6.79  ? 103  TYR D CD1 1 
ATOM   8761  C  CD2 . TYR D  1 103 ? 83.030  38.194  -17.737 1.00 6.49  ? 103  TYR D CD2 1 
ATOM   8762  C  CE1 . TYR D  1 103 ? 82.469  36.438  -19.837 1.00 7.12  ? 103  TYR D CE1 1 
ATOM   8763  C  CE2 . TYR D  1 103 ? 82.576  38.687  -18.933 1.00 8.84  ? 103  TYR D CE2 1 
ATOM   8764  C  CZ  . TYR D  1 103 ? 82.261  37.794  -19.984 1.00 9.09  ? 103  TYR D CZ  1 
ATOM   8765  O  OH  . TYR D  1 103 ? 81.786  38.312  -21.186 1.00 8.85  ? 103  TYR D OH  1 
ATOM   8766  N  N   . GLY D  1 104 ? 86.205  36.799  -18.476 1.00 8.98  ? 104  GLY D N   1 
ATOM   8767  C  CA  . GLY D  1 104 ? 86.926  37.708  -19.370 1.00 8.61  ? 104  GLY D CA  1 
ATOM   8768  C  C   . GLY D  1 104 ? 86.091  37.863  -20.638 1.00 8.66  ? 104  GLY D C   1 
ATOM   8769  O  O   . GLY D  1 104 ? 85.733  36.861  -21.268 1.00 7.31  ? 104  GLY D O   1 
ATOM   8770  N  N   . SER D  1 105 ? 85.679  39.095  -20.942 1.00 7.34  ? 105  SER D N   1 
ATOM   8771  C  CA  . SER D  1 105 ? 84.873  39.355  -22.139 1.00 6.69  ? 105  SER D CA  1 
ATOM   8772  C  C   . SER D  1 105 ? 85.765  39.845  -23.266 1.00 6.91  ? 105  SER D C   1 
ATOM   8773  O  O   . SER D  1 105 ? 86.528  40.807  -23.062 1.00 7.18  ? 105  SER D O   1 
ATOM   8774  C  CB  . SER D  1 105 ? 83.857  40.441  -21.805 1.00 5.86  ? 105  SER D CB  1 
ATOM   8775  O  OG  . SER D  1 105 ? 82.762  40.465  -22.710 1.00 6.87  ? 105  SER D OG  1 
ATOM   8776  N  N   . VAL D  1 106 ? 85.649  39.223  -24.435 1.00 6.96  ? 106  VAL D N   1 
ATOM   8777  C  CA  . VAL D  1 106 ? 86.412  39.620  -25.640 1.00 7.07  ? 106  VAL D CA  1 
ATOM   8778  C  C   . VAL D  1 106 ? 85.518  39.875  -26.897 1.00 7.08  ? 106  VAL D C   1 
ATOM   8779  O  O   . VAL D  1 106 ? 85.270  38.955  -27.710 1.00 5.61  ? 106  VAL D O   1 
ATOM   8780  C  CB  . VAL D  1 106 ? 87.511  38.580  -25.979 1.00 6.83  ? 106  VAL D CB  1 
ATOM   8781  C  CG1 . VAL D  1 106 ? 88.353  39.069  -27.175 1.00 7.93  ? 106  VAL D CG1 1 
ATOM   8782  C  CG2 . VAL D  1 106 ? 88.389  38.270  -24.707 1.00 3.25  ? 106  VAL D CG2 1 
ATOM   8783  N  N   . PRO D  1 107 ? 84.982  41.090  -26.999 1.00 6.03  ? 107  PRO D N   1 
ATOM   8784  C  CA  . PRO D  1 107 ? 84.169  41.489  -28.157 1.00 6.44  ? 107  PRO D CA  1 
ATOM   8785  C  C   . PRO D  1 107 ? 84.919  41.283  -29.483 1.00 6.47  ? 107  PRO D C   1 
ATOM   8786  O  O   . PRO D  1 107 ? 86.157  41.060  -29.510 1.00 6.61  ? 107  PRO D O   1 
ATOM   8787  C  CB  . PRO D  1 107 ? 83.964  42.994  -27.932 1.00 5.08  ? 107  PRO D CB  1 
ATOM   8788  C  CG  . PRO D  1 107 ? 83.978  43.167  -26.408 1.00 6.28  ? 107  PRO D CG  1 
ATOM   8789  C  CD  . PRO D  1 107 ? 85.065  42.160  -25.984 1.00 6.68  ? 107  PRO D CD  1 
ATOM   8790  N  N   . ARG D  1 108 ? 84.157  41.368  -30.569 1.00 6.82  ? 108  ARG D N   1 
ATOM   8791  C  CA  . ARG D  1 108 ? 84.709  41.271  -31.906 1.00 6.81  ? 108  ARG D CA  1 
ATOM   8792  C  C   . ARG D  1 108 ? 85.822  42.316  -32.043 1.00 7.92  ? 108  ARG D C   1 
ATOM   8793  O  O   . ARG D  1 108 ? 85.717  43.431  -31.459 1.00 6.87  ? 108  ARG D O   1 
ATOM   8794  C  CB  . ARG D  1 108 ? 83.601  41.556  -32.921 1.00 6.47  ? 108  ARG D CB  1 
ATOM   8795  C  CG  . ARG D  1 108 ? 82.532  40.444  -32.987 1.00 7.97  ? 108  ARG D CG  1 
ATOM   8796  C  CD  . ARG D  1 108 ? 81.245  40.839  -33.751 1.00 9.54  ? 108  ARG D CD  1 
ATOM   8797  N  NE  . ARG D  1 108 ? 80.516  41.882  -33.026 1.00 8.70  ? 108  ARG D NE  1 
ATOM   8798  C  CZ  . ARG D  1 108 ? 79.404  42.438  -33.468 1.00 11.28 ? 108  ARG D CZ  1 
ATOM   8799  N  NH1 . ARG D  1 108 ? 78.871  42.019  -34.639 1.00 8.66  ? 108  ARG D NH1 1 
ATOM   8800  N  NH2 . ARG D  1 108 ? 78.819  43.399  -32.753 1.00 6.28  ? 108  ARG D NH2 1 
ATOM   8801  N  N   . ASN D  1 109 ? 86.874  41.966  -32.800 1.00 8.35  ? 109  ASN D N   1 
ATOM   8802  C  CA  . ASN D  1 109 ? 87.869  42.964  -33.206 1.00 9.68  ? 109  ASN D CA  1 
ATOM   8803  C  C   . ASN D  1 109 ? 88.741  43.393  -32.019 1.00 8.32  ? 109  ASN D C   1 
ATOM   8804  O  O   . ASN D  1 109 ? 89.244  44.496  -31.966 1.00 7.64  ? 109  ASN D O   1 
ATOM   8805  C  CB  . ASN D  1 109 ? 87.094  44.160  -33.734 1.00 9.91  ? 109  ASN D CB  1 
ATOM   8806  C  CG  A ASN D  1 109 ? 86.852  44.040  -35.215 0.50 12.52 ? 109  ASN D CG  1 
ATOM   8807  C  CG  B ASN D  1 109 ? 87.572  44.688  -35.075 0.50 15.74 ? 109  ASN D CG  1 
ATOM   8808  O  OD1 A ASN D  1 109 ? 87.175  43.013  -35.861 0.50 2.00  ? 109  ASN D OD1 1 
ATOM   8809  O  OD1 B ASN D  1 109 ? 88.785  44.715  -35.358 0.50 14.52 ? 109  ASN D OD1 1 
ATOM   8810  N  ND2 A ASN D  1 109 ? 86.320  45.108  -35.792 0.50 19.43 ? 109  ASN D ND2 1 
ATOM   8811  N  ND2 B ASN D  1 109 ? 86.593  45.266  -35.871 0.50 22.56 ? 109  ASN D ND2 1 
ATOM   8812  N  N   . VAL D  1 110 ? 88.912  42.488  -31.077 1.00 6.58  ? 110  VAL D N   1 
ATOM   8813  C  CA  . VAL D  1 110 ? 89.739  42.709  -29.888 1.00 6.06  ? 110  VAL D CA  1 
ATOM   8814  C  C   . VAL D  1 110 ? 90.852  41.657  -29.955 1.00 5.11  ? 110  VAL D C   1 
ATOM   8815  O  O   . VAL D  1 110 ? 90.556  40.472  -30.035 1.00 6.01  ? 110  VAL D O   1 
ATOM   8816  C  CB  . VAL D  1 110 ? 88.893  42.562  -28.571 1.00 5.35  ? 110  VAL D CB  1 
ATOM   8817  C  CG1 . VAL D  1 110 ? 89.827  42.445  -27.312 1.00 4.21  ? 110  VAL D CG1 1 
ATOM   8818  C  CG2 . VAL D  1 110 ? 87.961  43.786  -28.415 1.00 6.74  ? 110  VAL D CG2 1 
ATOM   8819  N  N   . THR D  1 111 ? 92.109  42.104  -29.997 1.00 6.23  ? 111  THR D N   1 
ATOM   8820  C  CA  . THR D  1 111 ? 93.259  41.201  -30.045 1.00 6.91  ? 111  THR D CA  1 
ATOM   8821  C  C   . THR D  1 111 ? 93.328  40.499  -28.712 1.00 6.02  ? 111  THR D C   1 
ATOM   8822  O  O   . THR D  1 111 ? 93.114  41.121  -27.686 1.00 5.82  ? 111  THR D O   1 
ATOM   8823  C  CB  . THR D  1 111 ? 94.564  41.994  -30.303 1.00 7.26  ? 111  THR D CB  1 
ATOM   8824  O  OG1 . THR D  1 111 ? 94.519  42.571  -31.607 1.00 9.34  ? 111  THR D OG1 1 
ATOM   8825  C  CG2 . THR D  1 111 ? 95.795  41.050  -30.369 1.00 8.72  ? 111  THR D CG2 1 
ATOM   8826  N  N   . HIS D  1 112 ? 93.671  39.208  -28.701 1.00 5.54  ? 112  HIS D N   1 
ATOM   8827  C  CA  . HIS D  1 112 ? 93.721  38.466  -27.451 1.00 4.98  ? 112  HIS D CA  1 
ATOM   8828  C  C   . HIS D  1 112 ? 94.586  37.202  -27.614 1.00 5.58  ? 112  HIS D C   1 
ATOM   8829  O  O   . HIS D  1 112 ? 94.842  36.760  -28.741 1.00 5.32  ? 112  HIS D O   1 
ATOM   8830  C  CB  . HIS D  1 112 ? 92.328  38.105  -26.975 1.00 3.74  ? 112  HIS D CB  1 
ATOM   8831  C  CG  . HIS D  1 112 ? 91.524  37.321  -27.977 1.00 7.89  ? 112  HIS D CG  1 
ATOM   8832  N  ND1 . HIS D  1 112 ? 90.994  37.898  -29.109 1.00 7.35  ? 112  HIS D ND1 1 
ATOM   8833  C  CD2 . HIS D  1 112 ? 91.196  36.001  -28.037 1.00 7.94  ? 112  HIS D CD2 1 
ATOM   8834  C  CE1 . HIS D  1 112 ? 90.341  36.980  -29.806 1.00 7.33  ? 112  HIS D CE1 1 
ATOM   8835  N  NE2 . HIS D  1 112 ? 90.435  35.826  -29.168 1.00 10.29 ? 112  HIS D NE2 1 
ATOM   8836  N  N   . THR D  1 113 ? 95.001  36.675  -26.472 1.00 5.57  ? 113  THR D N   1 
ATOM   8837  C  CA  . THR D  1 113 ? 95.656  35.378  -26.335 1.00 7.32  ? 113  THR D CA  1 
ATOM   8838  C  C   . THR D  1 113 ? 95.483  34.927  -24.850 1.00 7.57  ? 113  THR D C   1 
ATOM   8839  O  O   . THR D  1 113 ? 94.945  35.662  -24.039 1.00 9.61  ? 113  THR D O   1 
ATOM   8840  C  CB  . THR D  1 113 ? 97.137  35.449  -26.793 1.00 5.84  ? 113  THR D CB  1 
ATOM   8841  O  OG1 . THR D  1 113 ? 97.737  34.167  -26.564 1.00 7.74  ? 113  THR D OG1 1 
ATOM   8842  C  CG2 . THR D  1 113 ? 97.969  36.484  -25.916 1.00 5.52  ? 113  THR D CG2 1 
ATOM   8843  N  N   . PHE D  1 114 ? 95.856  33.715  -24.522 1.00 7.59  ? 114  PHE D N   1 
ATOM   8844  C  CA  . PHE D  1 114 ? 95.681  33.209  -23.177 1.00 6.67  ? 114  PHE D CA  1 
ATOM   8845  C  C   . PHE D  1 114 ? 96.878  32.308  -22.893 1.00 7.46  ? 114  PHE D C   1 
ATOM   8846  O  O   . PHE D  1 114 ? 97.605  31.897  -23.823 1.00 8.21  ? 114  PHE D O   1 
ATOM   8847  C  CB  . PHE D  1 114 ? 94.345  32.438  -22.999 1.00 6.27  ? 114  PHE D CB  1 
ATOM   8848  C  CG  . PHE D  1 114 ? 94.181  31.226  -23.896 1.00 8.60  ? 114  PHE D CG  1 
ATOM   8849  C  CD1 . PHE D  1 114 ? 94.768  29.994  -23.560 1.00 10.69 ? 114  PHE D CD1 1 
ATOM   8850  C  CD2 . PHE D  1 114 ? 93.452  31.302  -25.073 1.00 11.27 ? 114  PHE D CD2 1 
ATOM   8851  C  CE1 . PHE D  1 114 ? 94.587  28.842  -24.384 1.00 10.44 ? 114  PHE D CE1 1 
ATOM   8852  C  CE2 . PHE D  1 114 ? 93.300  30.172  -25.907 1.00 12.68 ? 114  PHE D CE2 1 
ATOM   8853  C  CZ  . PHE D  1 114 ? 93.887  28.955  -25.568 1.00 11.18 ? 114  PHE D CZ  1 
ATOM   8854  N  N   . GLN D  1 115 ? 97.100  32.021  -21.616 1.00 7.71  ? 115  GLN D N   1 
ATOM   8855  C  CA  . GLN D  1 115 ? 98.177  31.113  -21.236 1.00 8.11  ? 115  GLN D CA  1 
ATOM   8856  C  C   . GLN D  1 115 ? 97.651  30.330  -20.052 1.00 8.51  ? 115  GLN D C   1 
ATOM   8857  O  O   . GLN D  1 115 ? 97.140  30.918  -19.104 1.00 6.20  ? 115  GLN D O   1 
ATOM   8858  C  CB  . GLN D  1 115 ? 99.447  31.840  -20.851 1.00 8.27  ? 115  GLN D CB  1 
ATOM   8859  C  CG  . GLN D  1 115 ? 100.579 30.877  -20.436 1.00 10.19 ? 115  GLN D CG  1 
ATOM   8860  C  CD  . GLN D  1 115 ? 101.943 31.494  -20.459 1.00 19.26 ? 115  GLN D CD  1 
ATOM   8861  O  OE1 . GLN D  1 115 ? 102.164 32.478  -21.155 1.00 22.40 ? 115  GLN D OE1 1 
ATOM   8862  N  NE2 . GLN D  1 115 ? 102.894 30.893  -19.718 1.00 19.22 ? 115  GLN D NE2 1 
ATOM   8863  N  N   . ILE D  1 116 ? 97.806  29.017  -20.120 1.00 6.93  ? 116  ILE D N   1 
ATOM   8864  C  CA  . ILE D  1 116 ? 97.343  28.136  -19.078 1.00 8.76  ? 116  ILE D CA  1 
ATOM   8865  C  C   . ILE D  1 116 ? 98.383  28.049  -17.958 1.00 8.77  ? 116  ILE D C   1 
ATOM   8866  O  O   . ILE D  1 116 ? 99.583  27.766  -18.211 1.00 8.35  ? 116  ILE D O   1 
ATOM   8867  C  CB  . ILE D  1 116 ? 97.060  26.685  -19.627 1.00 7.44  ? 116  ILE D CB  1 
ATOM   8868  C  CG1 . ILE D  1 116 ? 96.163  26.675  -20.849 1.00 9.78  ? 116  ILE D CG1 1 
ATOM   8869  C  CG2 . ILE D  1 116 ? 96.458  25.800  -18.523 1.00 7.88  ? 116  ILE D CG2 1 
ATOM   8870  C  CD1 . ILE D  1 116 ? 94.701  27.236  -20.658 1.00 8.11  ? 116  ILE D CD1 1 
ATOM   8871  N  N   . GLN D  1 117 ? 97.931  28.340  -16.726 1.00 9.67  ? 117  GLN D N   1 
ATOM   8872  C  CA  . GLN D  1 117 ? 98.821  28.413  -15.575 1.00 10.43 ? 117  GLN D CA  1 
ATOM   8873  C  C   . GLN D  1 117 ? 98.793  27.151  -14.686 1.00 10.60 ? 117  GLN D C   1 
ATOM   8874  O  O   . GLN D  1 117 ? 99.863  26.608  -14.349 1.00 10.93 ? 117  GLN D O   1 
ATOM   8875  C  CB  . GLN D  1 117 ? 98.479  29.664  -14.722 1.00 11.32 ? 117  GLN D CB  1 
ATOM   8876  C  CG  . GLN D  1 117 ? 99.369  29.929  -13.461 1.00 19.26 ? 117  GLN D CG  1 
ATOM   8877  C  CD  . GLN D  1 117 ? 98.936  31.208  -12.601 1.00 26.19 ? 117  GLN D CD  1 
ATOM   8878  O  OE1 . GLN D  1 117 ? 98.016  31.139  -11.758 1.00 25.91 ? 117  GLN D OE1 1 
ATOM   8879  N  NE2 . GLN D  1 117 ? 99.650  32.333  -12.791 1.00 30.93 ? 117  GLN D NE2 1 
ATOM   8880  N  N   . ASP D  1 118 ? 97.607  26.709  -14.262 1.00 9.97  ? 118  ASP D N   1 
ATOM   8881  C  CA  . ASP D  1 118 ? 97.538  25.622  -13.256 1.00 9.43  ? 118  ASP D CA  1 
ATOM   8882  C  C   . ASP D  1 118 ? 97.354  24.238  -13.883 1.00 9.10  ? 118  ASP D C   1 
ATOM   8883  O  O   . ASP D  1 118 ? 96.840  24.128  -15.007 1.00 7.94  ? 118  ASP D O   1 
ATOM   8884  C  CB  . ASP D  1 118 ? 96.441  25.900  -12.210 1.00 9.09  ? 118  ASP D CB  1 
ATOM   8885  C  CG  . ASP D  1 118 ? 96.922  26.758  -11.061 1.00 11.58 ? 118  ASP D CG  1 
ATOM   8886  O  OD1 . ASP D  1 118 ? 98.133  26.700  -10.703 1.00 9.77  ? 118  ASP D OD1 1 
ATOM   8887  O  OD2 . ASP D  1 118 ? 96.111  27.546  -10.480 1.00 15.09 ? 118  ASP D OD2 1 
ATOM   8888  N  N   . PRO D  1 119 ? 97.810  23.184  -13.197 1.00 8.13  ? 119  PRO D N   1 
ATOM   8889  C  CA  . PRO D  1 119 ? 97.761  21.834  -13.761 1.00 8.05  ? 119  PRO D CA  1 
ATOM   8890  C  C   . PRO D  1 119 ? 96.348  21.323  -14.049 1.00 8.42  ? 119  PRO D C   1 
ATOM   8891  O  O   . PRO D  1 119 ? 96.152  20.592  -15.051 1.00 8.47  ? 119  PRO D O   1 
ATOM   8892  C  CB  . PRO D  1 119 ? 98.456  20.981  -12.684 1.00 7.41  ? 119  PRO D CB  1 
ATOM   8893  C  CG  . PRO D  1 119 ? 99.331  21.923  -11.949 1.00 7.05  ? 119  PRO D CG  1 
ATOM   8894  C  CD  . PRO D  1 119 ? 98.506  23.205  -11.891 1.00 9.46  ? 119  PRO D CD  1 
ATOM   8895  N  N   . ASP D  1 120 ? 95.378  21.705  -13.222 1.00 8.01  ? 120  ASP D N   1 
ATOM   8896  C  CA  . ASP D  1 120 ? 94.029  21.222  -13.441 1.00 8.50  ? 120  ASP D CA  1 
ATOM   8897  C  C   . ASP D  1 120 ? 93.151  22.372  -13.955 1.00 9.26  ? 120  ASP D C   1 
ATOM   8898  O  O   . ASP D  1 120 ? 92.182  22.802  -13.291 1.00 9.70  ? 120  ASP D O   1 
ATOM   8899  C  CB  . ASP D  1 120 ? 93.437  20.576  -12.181 1.00 6.65  ? 120  ASP D CB  1 
ATOM   8900  C  CG  . ASP D  1 120 ? 92.171  19.783  -12.495 1.00 9.60  ? 120  ASP D CG  1 
ATOM   8901  O  OD1 . ASP D  1 120 ? 91.945  19.501  -13.703 1.00 11.24 ? 120  ASP D OD1 1 
ATOM   8902  O  OD2 . ASP D  1 120 ? 91.378  19.330  -11.611 1.00 9.97  ? 120  ASP D OD2 1 
ATOM   8903  N  N   . THR D  1 121 ? 93.509  22.920  -15.118 1.00 8.12  ? 121  THR D N   1 
ATOM   8904  C  CA  . THR D  1 121 ? 92.789  24.128  -15.586 1.00 7.82  ? 121  THR D CA  1 
ATOM   8905  C  C   . THR D  1 121 ? 91.684  23.776  -16.544 1.00 7.67  ? 121  THR D C   1 
ATOM   8906  O  O   . THR D  1 121 ? 91.871  22.947  -17.451 1.00 8.72  ? 121  THR D O   1 
ATOM   8907  C  CB  . THR D  1 121 ? 93.770  25.126  -16.217 1.00 7.81  ? 121  THR D CB  1 
ATOM   8908  O  OG1 . THR D  1 121 ? 94.664  25.619  -15.208 1.00 5.79  ? 121  THR D OG1 1 
ATOM   8909  C  CG2 . THR D  1 121 ? 93.041  26.368  -16.813 1.00 8.87  ? 121  THR D CG2 1 
ATOM   8910  N  N   . GLU D  1 122 ? 90.521  24.410  -16.345 1.00 7.28  ? 122  GLU D N   1 
ATOM   8911  C  CA  . GLU D  1 122 ? 89.385  24.271  -17.233 1.00 8.11  ? 122  GLU D CA  1 
ATOM   8912  C  C   . GLU D  1 122 ? 88.816  25.627  -17.596 1.00 9.13  ? 122  GLU D C   1 
ATOM   8913  O  O   . GLU D  1 122 ? 88.478  26.438  -16.671 1.00 8.39  ? 122  GLU D O   1 
ATOM   8914  C  CB  . GLU D  1 122 ? 88.278  23.389  -16.618 1.00 7.30  ? 122  GLU D CB  1 
ATOM   8915  C  CG  . GLU D  1 122 ? 87.197  22.990  -17.662 1.00 10.01 ? 122  GLU D CG  1 
ATOM   8916  C  CD  . GLU D  1 122 ? 86.243  21.880  -17.227 1.00 12.66 ? 122  GLU D CD  1 
ATOM   8917  O  OE1 . GLU D  1 122 ? 86.597  21.092  -16.312 1.00 17.84 ? 122  GLU D OE1 1 
ATOM   8918  O  OE2 . GLU D  1 122 ? 85.157  21.760  -17.840 1.00 12.82 ? 122  GLU D OE2 1 
ATOM   8919  N  N   . MET D  1 123 ? 88.785  25.901  -18.921 1.00 9.52  ? 123  MET D N   1 
ATOM   8920  C  CA  . MET D  1 123 ? 88.229  27.120  -19.472 1.00 11.60 ? 123  MET D CA  1 
ATOM   8921  C  C   . MET D  1 123 ? 86.930  26.765  -20.186 1.00 12.03 ? 123  MET D C   1 
ATOM   8922  O  O   . MET D  1 123 ? 86.903  25.882  -21.044 1.00 12.30 ? 123  MET D O   1 
ATOM   8923  C  CB  . MET D  1 123 ? 89.148  27.807  -20.519 1.00 13.19 ? 123  MET D CB  1 
ATOM   8924  C  CG  . MET D  1 123 ? 90.675  27.643  -20.421 1.00 18.40 ? 123  MET D CG  1 
ATOM   8925  S  SD  . MET D  1 123 ? 91.471  28.104  -22.110 1.00 26.35 ? 123  MET D SD  1 
ATOM   8926  C  CE  . MET D  1 123 ? 90.867  29.724  -22.159 1.00 14.03 ? 123  MET D CE  1 
ATOM   8927  N  N   . THR D  1 124 ? 85.865  27.491  -19.861 1.00 12.57 ? 124  THR D N   1 
ATOM   8928  C  CA  . THR D  1 124 ? 84.636  27.361  -20.611 1.00 11.97 ? 124  THR D CA  1 
ATOM   8929  C  C   . THR D  1 124 ? 84.576  28.538  -21.544 1.00 11.55 ? 124  THR D C   1 
ATOM   8930  O  O   . THR D  1 124 ? 84.645  29.715  -21.100 1.00 9.28  ? 124  THR D O   1 
ATOM   8931  C  CB  . THR D  1 124 ? 83.400  27.309  -19.683 1.00 12.78 ? 124  THR D CB  1 
ATOM   8932  O  OG1 . THR D  1 124 ? 83.439  26.077  -18.934 1.00 12.43 ? 124  THR D OG1 1 
ATOM   8933  C  CG2 . THR D  1 124 ? 82.107  27.198  -20.541 1.00 12.19 ? 124  THR D CG2 1 
ATOM   8934  N  N   . GLY D  1 125 ? 84.488  28.243  -22.846 1.00 10.65 ? 125  GLY D N   1 
ATOM   8935  C  CA  . GLY D  1 125 ? 84.312  29.299  -23.831 1.00 9.74  ? 125  GLY D CA  1 
ATOM   8936  C  C   . GLY D  1 125 ? 82.872  29.391  -24.321 1.00 9.67  ? 125  GLY D C   1 
ATOM   8937  O  O   . GLY D  1 125 ? 82.228  28.380  -24.639 1.00 10.54 ? 125  GLY D O   1 
ATOM   8938  N  N   . VAL D  1 126 ? 82.350  30.612  -24.398 1.00 9.85  ? 126  VAL D N   1 
ATOM   8939  C  CA  . VAL D  1 126 ? 81.025  30.826  -24.927 1.00 8.91  ? 126  VAL D CA  1 
ATOM   8940  C  C   . VAL D  1 126 ? 81.273  31.766  -26.099 1.00 9.01  ? 126  VAL D C   1 
ATOM   8941  O  O   . VAL D  1 126 ? 81.781  32.892  -25.913 1.00 8.94  ? 126  VAL D O   1 
ATOM   8942  C  CB  . VAL D  1 126 ? 80.062  31.441  -23.867 1.00 9.38  ? 126  VAL D CB  1 
ATOM   8943  C  CG1 . VAL D  1 126 ? 78.734  31.819  -24.506 1.00 8.85  ? 126  VAL D CG1 1 
ATOM   8944  C  CG2 . VAL D  1 126 ? 79.873  30.456  -22.670 1.00 9.29  ? 126  VAL D CG2 1 
ATOM   8945  N  N   . ILE D  1 127 ? 80.941  31.302  -27.300 1.00 9.52  ? 127  ILE D N   1 
ATOM   8946  C  CA  . ILE D  1 127 ? 81.252  32.043  -28.532 1.00 9.85  ? 127  ILE D CA  1 
ATOM   8947  C  C   . ILE D  1 127 ? 79.964  32.318  -29.283 1.00 9.08  ? 127  ILE D C   1 
ATOM   8948  O  O   . ILE D  1 127 ? 79.105  31.431  -29.415 1.00 9.31  ? 127  ILE D O   1 
ATOM   8949  C  CB  . ILE D  1 127 ? 82.265  31.285  -29.409 1.00 9.67  ? 127  ILE D CB  1 
ATOM   8950  C  CG1 . ILE D  1 127 ? 83.447  30.830  -28.557 1.00 12.79 ? 127  ILE D CG1 1 
ATOM   8951  C  CG2 . ILE D  1 127 ? 82.731  32.158  -30.648 1.00 7.14  ? 127  ILE D CG2 1 
ATOM   8952  C  CD1 . ILE D  1 127 ? 84.390  29.875  -29.310 1.00 17.45 ? 127  ILE D CD1 1 
ATOM   8953  N  N   . VAL D  1 128 ? 79.809  33.557  -29.739 1.00 8.55  ? 128  VAL D N   1 
ATOM   8954  C  CA  . VAL D  1 128 ? 78.531  33.950  -30.330 1.00 7.94  ? 128  VAL D CA  1 
ATOM   8955  C  C   . VAL D  1 128 ? 78.871  34.687  -31.627 1.00 8.14  ? 128  VAL D C   1 
ATOM   8956  O  O   . VAL D  1 128 ? 79.723  35.563  -31.581 1.00 8.64  ? 128  VAL D O   1 
ATOM   8957  C  CB  . VAL D  1 128 ? 77.739  34.878  -29.379 1.00 7.49  ? 128  VAL D CB  1 
ATOM   8958  C  CG1 . VAL D  1 128 ? 76.455  35.378  -30.046 1.00 8.96  ? 128  VAL D CG1 1 
ATOM   8959  C  CG2 . VAL D  1 128 ? 77.393  34.132  -28.049 1.00 8.19  ? 128  VAL D CG2 1 
ATOM   8960  N  N   . PRO D  1 129 ? 78.266  34.350  -32.768 1.00 6.97  ? 129  PRO D N   1 
ATOM   8961  C  CA  . PRO D  1 129 ? 77.290  33.252  -32.943 1.00 7.39  ? 129  PRO D CA  1 
ATOM   8962  C  C   . PRO D  1 129 ? 77.970  31.880  -32.956 1.00 6.56  ? 129  PRO D C   1 
ATOM   8963  O  O   . PRO D  1 129 ? 79.193  31.810  -32.766 1.00 5.67  ? 129  PRO D O   1 
ATOM   8964  C  CB  . PRO D  1 129 ? 76.669  33.544  -34.313 1.00 7.13  ? 129  PRO D CB  1 
ATOM   8965  C  CG  . PRO D  1 129 ? 77.780  34.222  -35.076 1.00 8.20  ? 129  PRO D CG  1 
ATOM   8966  C  CD  . PRO D  1 129 ? 78.527  35.062  -34.032 1.00 7.49  ? 129  PRO D CD  1 
ATOM   8967  N  N   . GLY D  1 130 ? 77.196  30.812  -33.153 1.00 6.24  ? 130  GLY D N   1 
ATOM   8968  C  CA  . GLY D  1 130 ? 77.712  29.462  -32.957 1.00 6.92  ? 130  GLY D CA  1 
ATOM   8969  C  C   . GLY D  1 130 ? 78.368  29.045  -34.254 1.00 7.44  ? 130  GLY D C   1 
ATOM   8970  O  O   . GLY D  1 130 ? 78.155  29.708  -35.287 1.00 7.14  ? 130  GLY D O   1 
ATOM   8971  N  N   . GLY D  1 131 ? 79.124  27.946  -34.196 1.00 8.29  ? 131  GLY D N   1 
ATOM   8972  C  CA  . GLY D  1 131 ? 79.727  27.386  -35.384 1.00 8.91  ? 131  GLY D CA  1 
ATOM   8973  C  C   . GLY D  1 131 ? 81.190  27.701  -35.526 1.00 9.61  ? 131  GLY D C   1 
ATOM   8974  O  O   . GLY D  1 131 ? 81.816  27.217  -36.451 1.00 10.22 ? 131  GLY D O   1 
ATOM   8975  N  N   . PHE D  1 132 ? 81.747  28.518  -34.630 1.00 9.44  ? 132  PHE D N   1 
ATOM   8976  C  CA  . PHE D  1 132 ? 83.178  28.806  -34.708 1.00 8.93  ? 132  PHE D CA  1 
ATOM   8977  C  C   . PHE D  1 132 ? 84.021  27.538  -34.485 1.00 9.15  ? 132  PHE D C   1 
ATOM   8978  O  O   . PHE D  1 132 ? 85.169  27.473  -34.914 1.00 8.94  ? 132  PHE D O   1 
ATOM   8979  C  CB  . PHE D  1 132 ? 83.588  29.865  -33.665 1.00 9.83  ? 132  PHE D CB  1 
ATOM   8980  C  CG  . PHE D  1 132 ? 85.062  30.188  -33.677 1.00 9.52  ? 132  PHE D CG  1 
ATOM   8981  C  CD1 . PHE D  1 132 ? 85.592  31.059  -34.640 1.00 8.48  ? 132  PHE D CD1 1 
ATOM   8982  C  CD2 . PHE D  1 132 ? 85.920  29.619  -32.740 1.00 9.56  ? 132  PHE D CD2 1 
ATOM   8983  C  CE1 . PHE D  1 132 ? 86.957  31.358  -34.663 1.00 10.37 ? 132  PHE D CE1 1 
ATOM   8984  C  CE2 . PHE D  1 132 ? 87.323  29.906  -32.766 1.00 11.79 ? 132  PHE D CE2 1 
ATOM   8985  C  CZ  . PHE D  1 132 ? 87.841  30.778  -33.730 1.00 11.01 ? 132  PHE D CZ  1 
ATOM   8986  N  N   . GLU D  1 133 ? 83.452  26.531  -33.815 1.00 8.14  ? 133  GLU D N   1 
ATOM   8987  C  CA  . GLU D  1 133 ? 84.221  25.348  -33.417 1.00 7.65  ? 133  GLU D CA  1 
ATOM   8988  C  C   . GLU D  1 133 ? 84.831  24.542  -34.604 1.00 7.59  ? 133  GLU D C   1 
ATOM   8989  O  O   . GLU D  1 133 ? 85.736  23.705  -34.405 1.00 7.13  ? 133  GLU D O   1 
ATOM   8990  C  CB  . GLU D  1 133 ? 83.351  24.448  -32.528 1.00 6.91  ? 133  GLU D CB  1 
ATOM   8991  C  CG  . GLU D  1 133 ? 82.148  23.772  -33.221 1.00 5.38  ? 133  GLU D CG  1 
ATOM   8992  C  CD  . GLU D  1 133 ? 80.932  24.692  -33.385 1.00 7.32  ? 133  GLU D CD  1 
ATOM   8993  O  OE1 . GLU D  1 133 ? 80.974  25.878  -32.929 1.00 7.74  ? 133  GLU D OE1 1 
ATOM   8994  O  OE2 . GLU D  1 133 ? 79.936  24.220  -33.951 1.00 7.99  ? 133  GLU D OE2 1 
ATOM   8995  N  N   . ASP D  1 134 ? 84.341  24.766  -35.818 1.00 5.68  ? 134  ASP D N   1 
ATOM   8996  C  CA  . ASP D  1 134 ? 84.919  24.128  -36.999 1.00 7.23  ? 134  ASP D CA  1 
ATOM   8997  C  C   . ASP D  1 134 ? 86.431  24.383  -37.059 1.00 6.68  ? 134  ASP D C   1 
ATOM   8998  O  O   . ASP D  1 134 ? 87.204  23.510  -37.452 1.00 7.66  ? 134  ASP D O   1 
ATOM   8999  C  CB  . ASP D  1 134 ? 84.259  24.629  -38.300 1.00 8.73  ? 134  ASP D CB  1 
ATOM   9000  C  CG  . ASP D  1 134 ? 82.795  24.245  -38.435 1.00 11.57 ? 134  ASP D CG  1 
ATOM   9001  O  OD1 . ASP D  1 134 ? 82.244  23.470  -37.621 1.00 12.09 ? 134  ASP D OD1 1 
ATOM   9002  O  OD2 . ASP D  1 134 ? 82.100  24.755  -39.357 1.00 16.92 ? 134  ASP D OD2 1 
ATOM   9003  N  N   . LEU D  1 135 ? 86.862  25.562  -36.603 1.00 7.75  ? 135  LEU D N   1 
ATOM   9004  C  CA  . LEU D  1 135 ? 88.303  25.861  -36.473 1.00 7.68  ? 135  LEU D CA  1 
ATOM   9005  C  C   . LEU D  1 135 ? 89.077  24.819  -35.662 1.00 7.01  ? 135  LEU D C   1 
ATOM   9006  O  O   . LEU D  1 135 ? 90.178  24.400  -36.075 1.00 7.98  ? 135  LEU D O   1 
ATOM   9007  C  CB  . LEU D  1 135 ? 88.506  27.247  -35.841 1.00 7.99  ? 135  LEU D CB  1 
ATOM   9008  C  CG  . LEU D  1 135 ? 89.915  27.817  -35.594 1.00 8.23  ? 135  LEU D CG  1 
ATOM   9009  C  CD1 . LEU D  1 135 ? 90.524  27.335  -34.307 1.00 15.12 ? 135  LEU D CD1 1 
ATOM   9010  C  CD2 . LEU D  1 135 ? 90.864  27.720  -36.805 1.00 5.29  ? 135  LEU D CD2 1 
ATOM   9011  N  N   . PHE D  1 136 ? 88.546  24.422  -34.502 1.00 7.10  ? 136  PHE D N   1 
ATOM   9012  C  CA  . PHE D  1 136 ? 89.184  23.375  -33.672 1.00 7.32  ? 136  PHE D CA  1 
ATOM   9013  C  C   . PHE D  1 136 ? 89.119  21.972  -34.258 1.00 8.50  ? 136  PHE D C   1 
ATOM   9014  O  O   . PHE D  1 136 ? 90.047  21.188  -34.038 1.00 7.95  ? 136  PHE D O   1 
ATOM   9015  C  CB  . PHE D  1 136 ? 88.617  23.375  -32.245 1.00 7.67  ? 136  PHE D CB  1 
ATOM   9016  C  CG  . PHE D  1 136 ? 88.739  24.696  -31.586 1.00 8.40  ? 136  PHE D CG  1 
ATOM   9017  C  CD1 . PHE D  1 136 ? 89.979  25.142  -31.145 1.00 8.49  ? 136  PHE D CD1 1 
ATOM   9018  C  CD2 . PHE D  1 136 ? 87.637  25.521  -31.454 1.00 7.34  ? 136  PHE D CD2 1 
ATOM   9019  C  CE1 . PHE D  1 136 ? 90.126  26.399  -30.581 1.00 9.44  ? 136  PHE D CE1 1 
ATOM   9020  C  CE2 . PHE D  1 136 ? 87.781  26.787  -30.873 1.00 10.07 ? 136  PHE D CE2 1 
ATOM   9021  C  CZ  . PHE D  1 136 ? 89.024  27.226  -30.440 1.00 10.37 ? 136  PHE D CZ  1 
ATOM   9022  N  N   . TYR D  1 137 ? 88.051  21.625  -34.981 1.00 8.51  ? 137  TYR D N   1 
ATOM   9023  C  CA  . TYR D  1 137 ? 88.098  20.321  -35.667 1.00 8.71  ? 137  TYR D CA  1 
ATOM   9024  C  C   . TYR D  1 137 ? 89.239  20.333  -36.649 1.00 7.38  ? 137  TYR D C   1 
ATOM   9025  O  O   . TYR D  1 137 ? 89.936  19.333  -36.812 1.00 9.59  ? 137  TYR D O   1 
ATOM   9026  C  CB  . TYR D  1 137 ? 86.825  20.028  -36.486 1.00 8.42  ? 137  TYR D CB  1 
ATOM   9027  C  CG  . TYR D  1 137 ? 85.504  20.099  -35.734 1.00 10.72 ? 137  TYR D CG  1 
ATOM   9028  C  CD1 . TYR D  1 137 ? 85.405  19.682  -34.378 1.00 8.99  ? 137  TYR D CD1 1 
ATOM   9029  C  CD2 . TYR D  1 137 ? 84.358  20.572  -36.384 1.00 10.98 ? 137  TYR D CD2 1 
ATOM   9030  C  CE1 . TYR D  1 137 ? 84.188  19.724  -33.700 1.00 9.05  ? 137  TYR D CE1 1 
ATOM   9031  C  CE2 . TYR D  1 137 ? 83.132  20.651  -35.724 1.00 11.27 ? 137  TYR D CE2 1 
ATOM   9032  C  CZ  . TYR D  1 137 ? 83.049  20.205  -34.398 1.00 7.30  ? 137  TYR D CZ  1 
ATOM   9033  O  OH  . TYR D  1 137 ? 81.860  20.316  -33.753 1.00 8.18  ? 137  TYR D OH  1 
ATOM   9034  N  N   . TYR D  1 138 ? 89.390  21.437  -37.371 1.00 6.84  ? 138  TYR D N   1 
ATOM   9035  C  CA  . TYR D  1 138 ? 90.348  21.521  -38.456 1.00 6.33  ? 138  TYR D CA  1 
ATOM   9036  C  C   . TYR D  1 138 ? 91.778  21.453  -37.908 1.00 6.39  ? 138  TYR D C   1 
ATOM   9037  O  O   . TYR D  1 138 ? 92.589  20.612  -38.317 1.00 7.88  ? 138  TYR D O   1 
ATOM   9038  C  CB  . TYR D  1 138 ? 90.128  22.858  -39.192 1.00 5.33  ? 138  TYR D CB  1 
ATOM   9039  C  CG  . TYR D  1 138 ? 90.993  23.122  -40.416 1.00 5.65  ? 138  TYR D CG  1 
ATOM   9040  C  CD1 . TYR D  1 138 ? 90.781  22.425  -41.588 1.00 2.20  ? 138  TYR D CD1 1 
ATOM   9041  C  CD2 . TYR D  1 138 ? 91.956  24.143  -40.430 1.00 5.58  ? 138  TYR D CD2 1 
ATOM   9042  C  CE1 . TYR D  1 138 ? 91.526  22.678  -42.711 1.00 2.50  ? 138  TYR D CE1 1 
ATOM   9043  C  CE2 . TYR D  1 138 ? 92.732  24.399  -41.569 1.00 5.18  ? 138  TYR D CE2 1 
ATOM   9044  C  CZ  . TYR D  1 138 ? 92.490  23.668  -42.714 1.00 3.72  ? 138  TYR D CZ  1 
ATOM   9045  O  OH  . TYR D  1 138 ? 93.183  23.858  -43.868 1.00 2.46  ? 138  TYR D OH  1 
ATOM   9046  N  N   . LEU D  1 139 ? 92.104  22.363  -37.008 1.00 7.15  ? 139  LEU D N   1 
ATOM   9047  C  CA  . LEU D  1 139 ? 93.444  22.440  -36.427 1.00 8.22  ? 139  LEU D CA  1 
ATOM   9048  C  C   . LEU D  1 139 ? 93.768  21.356  -35.398 1.00 8.91  ? 139  LEU D C   1 
ATOM   9049  O  O   . LEU D  1 139 ? 94.968  21.087  -35.138 1.00 9.34  ? 139  LEU D O   1 
ATOM   9050  C  CB  . LEU D  1 139 ? 93.585  23.765  -35.708 1.00 7.77  ? 139  LEU D CB  1 
ATOM   9051  C  CG  . LEU D  1 139 ? 93.700  24.976  -36.629 1.00 9.17  ? 139  LEU D CG  1 
ATOM   9052  C  CD1 . LEU D  1 139 ? 94.037  26.156  -35.715 1.00 10.16 ? 139  LEU D CD1 1 
ATOM   9053  C  CD2 . LEU D  1 139 ? 94.714  24.782  -37.781 1.00 10.77 ? 139  LEU D CD2 1 
ATOM   9054  N  N   . GLY D  1 140 ? 92.725  20.802  -34.762 1.00 9.12  ? 140  GLY D N   1 
ATOM   9055  C  CA  . GLY D  1 140 ? 92.871  19.775  -33.735 1.00 8.48  ? 140  GLY D CA  1 
ATOM   9056  C  C   . GLY D  1 140 ? 93.086  18.369  -34.304 1.00 9.14  ? 140  GLY D C   1 
ATOM   9057  O  O   . GLY D  1 140 ? 92.882  18.100  -35.497 1.00 9.20  ? 140  GLY D O   1 
ATOM   9058  N  N   . THR D  1 141 ? 93.482  17.466  -33.433 1.00 7.80  ? 141  THR D N   1 
ATOM   9059  C  CA  . THR D  1 141 ? 93.601  16.070  -33.748 1.00 6.92  ? 141  THR D CA  1 
ATOM   9060  C  C   . THR D  1 141 ? 92.463  15.384  -32.998 1.00 7.67  ? 141  THR D C   1 
ATOM   9061  O  O   . THR D  1 141 ? 92.250  15.589  -31.770 1.00 7.37  ? 141  THR D O   1 
ATOM   9062  C  CB  . THR D  1 141 ? 94.990  15.530  -33.281 1.00 6.86  ? 141  THR D CB  1 
ATOM   9063  O  OG1 . THR D  1 141 ? 95.987  16.205  -34.027 1.00 7.71  ? 141  THR D OG1 1 
ATOM   9064  C  CG2 . THR D  1 141 ? 95.200  14.041  -33.671 1.00 9.22  ? 141  THR D CG2 1 
ATOM   9065  N  N   . ASN D  1 142 ? 91.730  14.554  -33.722 1.00 7.22  ? 142  ASN D N   1 
ATOM   9066  C  CA  . ASN D  1 142 ? 90.609  13.844  -33.123 1.00 7.60  ? 142  ASN D CA  1 
ATOM   9067  C  C   . ASN D  1 142 ? 91.090  13.139  -31.832 1.00 9.28  ? 142  ASN D C   1 
ATOM   9068  O  O   . ASN D  1 142 ? 92.220  12.638  -31.801 1.00 7.71  ? 142  ASN D O   1 
ATOM   9069  C  CB  . ASN D  1 142 ? 90.055  12.823  -34.142 1.00 7.67  ? 142  ASN D CB  1 
ATOM   9070  C  CG  . ASN D  1 142 ? 91.001  11.654  -34.386 1.00 10.25 ? 142  ASN D CG  1 
ATOM   9071  O  OD1 . ASN D  1 142 ? 90.804  10.543  -33.823 1.00 11.61 ? 142  ASN D OD1 1 
ATOM   9072  N  ND2 . ASN D  1 142 ? 91.959  11.852  -35.256 1.00 8.69  ? 142  ASN D ND2 1 
ATOM   9073  N  N   . ALA D  1 143 ? 90.224  13.059  -30.813 1.00 8.74  ? 143  ALA D N   1 
ATOM   9074  C  CA  . ALA D  1 143 ? 90.552  12.346  -29.577 1.00 9.83  ? 143  ALA D CA  1 
ATOM   9075  C  C   . ALA D  1 143 ? 89.407  11.377  -29.202 1.00 8.19  ? 143  ALA D C   1 
ATOM   9076  O  O   . ALA D  1 143 ? 88.259  11.786  -28.977 1.00 6.20  ? 143  ALA D O   1 
ATOM   9077  C  CB  . ALA D  1 143 ? 90.834  13.324  -28.433 1.00 8.93  ? 143  ALA D CB  1 
ATOM   9078  N  N   . THR D  1 144 ? 89.743  10.094  -29.182 1.00 7.89  ? 144  THR D N   1 
ATOM   9079  C  CA  . THR D  1 144 ? 88.784  9.066   -28.778 1.00 9.02  ? 144  THR D CA  1 
ATOM   9080  C  C   . THR D  1 144 ? 88.534  9.191   -27.256 1.00 8.51  ? 144  THR D C   1 
ATOM   9081  O  O   . THR D  1 144 ? 87.422  9.127   -26.795 1.00 9.69  ? 144  THR D O   1 
ATOM   9082  C  CB  . THR D  1 144 ? 89.385  7.658   -29.109 1.00 9.72  ? 144  THR D CB  1 
ATOM   9083  O  OG1 . THR D  1 144 ? 89.381  7.500   -30.552 1.00 10.78 ? 144  THR D OG1 1 
ATOM   9084  C  CG2 . THR D  1 144 ? 88.422  6.601   -28.648 1.00 12.67 ? 144  THR D CG2 1 
ATOM   9085  N  N   . ASP D  1 145 ? 89.606  9.391   -26.507 1.00 8.76  ? 145  ASP D N   1 
ATOM   9086  C  CA  . ASP D  1 145 ? 89.578  9.550   -25.051 1.00 8.41  ? 145  ASP D CA  1 
ATOM   9087  C  C   . ASP D  1 145 ? 88.558  8.608   -24.358 1.00 7.85  ? 145  ASP D C   1 
ATOM   9088  O  O   . ASP D  1 145 ? 87.599  9.031   -23.722 1.00 8.65  ? 145  ASP D O   1 
ATOM   9089  C  CB  . ASP D  1 145 ? 89.337  11.007  -24.721 1.00 7.47  ? 145  ASP D CB  1 
ATOM   9090  C  CG  . ASP D  1 145 ? 89.526  11.318  -23.247 1.00 7.60  ? 145  ASP D CG  1 
ATOM   9091  O  OD1 . ASP D  1 145 ? 89.932  10.392  -22.486 1.00 6.79  ? 145  ASP D OD1 1 
ATOM   9092  O  OD2 . ASP D  1 145 ? 89.340  12.511  -22.792 1.00 7.79  ? 145  ASP D OD2 1 
ATOM   9093  N  N   . THR D  1 146 ? 88.819  7.324   -24.511 1.00 8.43  ? 146  THR D N   1 
ATOM   9094  C  CA  . THR D  1 146 ? 87.947  6.267   -24.039 1.00 9.57  ? 146  THR D CA  1 
ATOM   9095  C  C   . THR D  1 146 ? 87.560  6.421   -22.576 1.00 8.45  ? 146  THR D C   1 
ATOM   9096  O  O   . THR D  1 146 ? 86.427  6.194   -22.243 1.00 7.23  ? 146  THR D O   1 
ATOM   9097  C  CB  . THR D  1 146 ? 88.650  4.932   -24.235 1.00 8.67  ? 146  THR D CB  1 
ATOM   9098  O  OG1 . THR D  1 146 ? 88.895  4.775   -25.631 1.00 14.18 ? 146  THR D OG1 1 
ATOM   9099  C  CG2 . THR D  1 146 ? 87.780  3.752   -23.830 1.00 12.04 ? 146  THR D CG2 1 
ATOM   9100  N  N   . THR D  1 147 ? 88.516  6.792   -21.711 1.00 6.27  ? 147  THR D N   1 
ATOM   9101  C  CA  . THR D  1 147 ? 88.256  6.897   -20.274 1.00 5.95  ? 147  THR D CA  1 
ATOM   9102  C  C   . THR D  1 147 ? 87.606  8.236   -19.857 1.00 6.51  ? 147  THR D C   1 
ATOM   9103  O  O   . THR D  1 147 ? 87.268  8.434   -18.667 1.00 7.83  ? 147  THR D O   1 
ATOM   9104  C  CB  . THR D  1 147 ? 89.576  6.790   -19.533 1.00 5.94  ? 147  THR D CB  1 
ATOM   9105  O  OG1 . THR D  1 147 ? 90.422  7.896   -19.983 1.00 6.90  ? 147  THR D OG1 1 
ATOM   9106  C  CG2 . THR D  1 147 ? 90.316  5.528   -19.948 1.00 5.04  ? 147  THR D CG2 1 
ATOM   9107  N  N   . HIS D  1 148 ? 87.439  9.153   -20.812 1.00 7.18  ? 148  HIS D N   1 
ATOM   9108  C  CA  . HIS D  1 148 ? 86.865  10.501  -20.506 1.00 6.88  ? 148  HIS D CA  1 
ATOM   9109  C  C   . HIS D  1 148 ? 87.779  11.254  -19.538 1.00 6.96  ? 148  HIS D C   1 
ATOM   9110  O  O   . HIS D  1 148 ? 87.326  12.151  -18.779 1.00 9.13  ? 148  HIS D O   1 
ATOM   9111  C  CB  . HIS D  1 148 ? 85.448  10.372  -19.917 1.00 7.42  ? 148  HIS D CB  1 
ATOM   9112  C  CG  . HIS D  1 148 ? 84.468  9.753   -20.854 1.00 4.89  ? 148  HIS D CG  1 
ATOM   9113  N  ND1 . HIS D  1 148 ? 84.370  8.389   -21.035 1.00 10.06 ? 148  HIS D ND1 1 
ATOM   9114  C  CD2 . HIS D  1 148 ? 83.515  10.310  -21.641 1.00 6.73  ? 148  HIS D CD2 1 
ATOM   9115  C  CE1 . HIS D  1 148 ? 83.414  8.136   -21.907 1.00 8.01  ? 148  HIS D CE1 1 
ATOM   9116  N  NE2 . HIS D  1 148 ? 82.887  9.281   -22.296 1.00 6.75  ? 148  HIS D NE2 1 
ATOM   9117  N  N   . THR D  1 149 ? 89.080  10.981  -19.603 1.00 6.64  ? 149  THR D N   1 
ATOM   9118  C  CA  . THR D  1 149 ? 90.029  11.757  -18.840 1.00 6.95  ? 149  THR D CA  1 
ATOM   9119  C  C   . THR D  1 149 ? 89.977  13.238  -19.233 1.00 7.87  ? 149  THR D C   1 
ATOM   9120  O  O   . THR D  1 149 ? 89.778  13.547  -20.386 1.00 7.09  ? 149  THR D O   1 
ATOM   9121  C  CB  . THR D  1 149 ? 91.484  11.184  -18.931 1.00 7.98  ? 149  THR D CB  1 
ATOM   9122  O  OG1 . THR D  1 149 ? 92.259  11.841  -17.935 1.00 5.66  ? 149  THR D OG1 1 
ATOM   9123  C  CG2 . THR D  1 149 ? 92.212  11.517  -20.287 1.00 8.49  ? 149  THR D CG2 1 
ATOM   9124  N  N   . PRO D  1 150 ? 90.003  14.168  -18.263 1.00 8.99  ? 150  PRO D N   1 
ATOM   9125  C  CA  . PRO D  1 150 ? 89.851  15.600  -18.594 1.00 8.45  ? 150  PRO D CA  1 
ATOM   9126  C  C   . PRO D  1 150 ? 90.780  16.080  -19.718 1.00 8.06  ? 150  PRO D C   1 
ATOM   9127  O  O   . PRO D  1 150 ? 90.280  16.747  -20.622 1.00 7.59  ? 150  PRO D O   1 
ATOM   9128  C  CB  . PRO D  1 150 ? 90.151  16.292  -17.246 1.00 8.31  ? 150  PRO D CB  1 
ATOM   9129  C  CG  . PRO D  1 150 ? 89.372  15.351  -16.278 1.00 8.62  ? 150  PRO D CG  1 
ATOM   9130  C  CD  . PRO D  1 150 ? 89.975  13.958  -16.806 1.00 8.32  ? 150  PRO D CD  1 
ATOM   9131  N  N   . TYR D  1 151 ? 92.083  15.781  -19.623 1.00 7.96  ? 151  TYR D N   1 
ATOM   9132  C  CA  . TYR D  1 151 ? 92.961  15.931  -20.781 1.00 7.40  ? 151  TYR D CA  1 
ATOM   9133  C  C   . TYR D  1 151 ? 93.982  14.820  -20.795 1.00 7.31  ? 151  TYR D C   1 
ATOM   9134  O  O   . TYR D  1 151 ? 94.114  14.074  -19.824 1.00 6.59  ? 151  TYR D O   1 
ATOM   9135  C  CB  . TYR D  1 151 ? 93.675  17.265  -20.740 1.00 6.61  ? 151  TYR D CB  1 
ATOM   9136  C  CG  . TYR D  1 151 ? 94.516  17.549  -19.520 1.00 7.42  ? 151  TYR D CG  1 
ATOM   9137  C  CD1 . TYR D  1 151 ? 95.813  17.045  -19.412 1.00 8.85  ? 151  TYR D CD1 1 
ATOM   9138  C  CD2 . TYR D  1 151 ? 94.054  18.395  -18.520 1.00 7.33  ? 151  TYR D CD2 1 
ATOM   9139  C  CE1 . TYR D  1 151 ? 96.619  17.351  -18.350 1.00 9.07  ? 151  TYR D CE1 1 
ATOM   9140  C  CE2 . TYR D  1 151 ? 94.880  18.715  -17.397 1.00 8.47  ? 151  TYR D CE2 1 
ATOM   9141  C  CZ  . TYR D  1 151 ? 96.163  18.178  -17.347 1.00 8.86  ? 151  TYR D CZ  1 
ATOM   9142  O  OH  . TYR D  1 151 ? 97.024  18.473  -16.316 1.00 8.03  ? 151  TYR D OH  1 
ATOM   9143  N  N   . ILE D  1 152 ? 94.742  14.717  -21.880 1.00 8.32  ? 152  ILE D N   1 
ATOM   9144  C  CA  . ILE D  1 152 ? 95.631  13.560  -22.041 1.00 7.93  ? 152  ILE D CA  1 
ATOM   9145  C  C   . ILE D  1 152 ? 96.893  13.866  -21.262 1.00 10.29 ? 152  ILE D C   1 
ATOM   9146  O  O   . ILE D  1 152 ? 97.514  14.906  -21.474 1.00 9.94  ? 152  ILE D O   1 
ATOM   9147  C  CB  . ILE D  1 152 ? 95.975  13.320  -23.543 1.00 8.37  ? 152  ILE D CB  1 
ATOM   9148  C  CG1 . ILE D  1 152 ? 94.717  13.308  -24.403 1.00 9.62  ? 152  ILE D CG1 1 
ATOM   9149  C  CG2 . ILE D  1 152 ? 96.772  12.011  -23.741 1.00 8.06  ? 152  ILE D CG2 1 
ATOM   9150  C  CD1 . ILE D  1 152 ? 93.637  12.260  -24.092 1.00 10.58 ? 152  ILE D CD1 1 
ATOM   9151  N  N   . PRO D  1 153 ? 97.280  12.985  -20.338 1.00 11.69 ? 153  PRO D N   1 
ATOM   9152  C  CA  . PRO D  1 153 ? 98.496  13.248  -19.540 1.00 13.70 ? 153  PRO D CA  1 
ATOM   9153  C  C   . PRO D  1 153 ? 99.743  13.201  -20.433 1.00 16.20 ? 153  PRO D C   1 
ATOM   9154  O  O   . PRO D  1 153 ? 99.791  12.430  -21.377 1.00 16.45 ? 153  PRO D O   1 
ATOM   9155  C  CB  . PRO D  1 153 ? 98.534  12.086  -18.513 1.00 14.24 ? 153  PRO D CB  1 
ATOM   9156  C  CG  . PRO D  1 153 ? 97.296  11.292  -18.717 1.00 12.82 ? 153  PRO D CG  1 
ATOM   9157  C  CD  . PRO D  1 153 ? 96.622  11.705  -20.004 1.00 10.80 ? 153  PRO D CD  1 
ATOM   9158  N  N   . SER D  1 154 ? 100.760 14.001  -20.127 1.00 20.51 ? 154  SER D N   1 
ATOM   9159  C  CA  . SER D  1 154 ? 102.068 13.836  -20.797 1.00 23.35 ? 154  SER D CA  1 
ATOM   9160  C  C   . SER D  1 154 ? 103.176 14.529  -20.007 1.00 24.24 ? 154  SER D C   1 
ATOM   9161  O  O   . SER D  1 154 ? 102.922 15.562  -19.365 1.00 25.63 ? 154  SER D O   1 
ATOM   9162  C  CB  . SER D  1 154 ? 102.018 14.397  -22.219 1.00 24.56 ? 154  SER D CB  1 
ATOM   9163  O  OG  . SER D  1 154 ? 101.594 15.776  -22.202 1.00 27.61 ? 154  SER D OG  1 
ATOM   9164  N  N   . SER D  1 159 ? 109.845 25.039  -25.659 1.00 30.60 ? 159  SER D N   1 
ATOM   9165  C  CA  . SER D  1 159 ? 108.400 25.253  -25.489 1.00 30.58 ? 159  SER D CA  1 
ATOM   9166  C  C   . SER D  1 159 ? 107.820 26.376  -26.400 1.00 29.78 ? 159  SER D C   1 
ATOM   9167  O  O   . SER D  1 159 ? 107.777 27.573  -26.022 1.00 29.73 ? 159  SER D O   1 
ATOM   9168  C  CB  . SER D  1 159 ? 108.029 25.444  -24.004 1.00 30.91 ? 159  SER D CB  1 
ATOM   9169  O  OG  . SER D  1 159 ? 106.717 24.948  -23.724 1.00 33.01 ? 159  SER D OG  1 
ATOM   9170  N  N   . SER D  1 160 ? 107.404 25.963  -27.609 1.00 28.12 ? 160  SER D N   1 
ATOM   9171  C  CA  . SER D  1 160 ? 106.784 26.845  -28.597 1.00 26.61 ? 160  SER D CA  1 
ATOM   9172  C  C   . SER D  1 160 ? 105.350 27.135  -28.160 1.00 25.08 ? 160  SER D C   1 
ATOM   9173  O  O   . SER D  1 160 ? 104.703 26.283  -27.529 1.00 25.20 ? 160  SER D O   1 
ATOM   9174  C  CB  . SER D  1 160 ? 106.764 26.179  -29.995 1.00 26.78 ? 160  SER D CB  1 
ATOM   9175  O  OG  . SER D  1 160 ? 107.846 26.602  -30.836 1.00 28.76 ? 160  SER D OG  1 
ATOM   9176  N  N   . THR D  1 161 ? 104.841 28.314  -28.515 1.00 22.63 ? 161  THR D N   1 
ATOM   9177  C  CA  . THR D  1 161 ? 103.429 28.606  -28.360 1.00 20.48 ? 161  THR D CA  1 
ATOM   9178  C  C   . THR D  1 161 ? 102.566 27.421  -28.832 1.00 20.87 ? 161  THR D C   1 
ATOM   9179  O  O   . THR D  1 161 ? 102.828 26.848  -29.885 1.00 20.91 ? 161  THR D O   1 
ATOM   9180  C  CB  . THR D  1 161 ? 103.076 29.842  -29.183 1.00 20.63 ? 161  THR D CB  1 
ATOM   9181  O  OG1 . THR D  1 161 ? 103.760 30.993  -28.657 1.00 18.18 ? 161  THR D OG1 1 
ATOM   9182  C  CG2 . THR D  1 161 ? 101.603 30.179  -29.014 1.00 16.72 ? 161  THR D CG2 1 
ATOM   9183  N  N   . THR D  1 162 ? 101.540 27.057  -28.053 1.00 20.50 ? 162  THR D N   1 
ATOM   9184  C  CA  . THR D  1 162 ? 100.603 26.000  -28.459 1.00 19.62 ? 162  THR D CA  1 
ATOM   9185  C  C   . THR D  1 162 ? 99.785  26.407  -29.686 1.00 18.67 ? 162  THR D C   1 
ATOM   9186  O  O   . THR D  1 162 ? 99.436  27.589  -29.870 1.00 17.35 ? 162  THR D O   1 
ATOM   9187  C  CB  . THR D  1 162 ? 99.609  25.608  -27.303 1.00 20.23 ? 162  THR D CB  1 
ATOM   9188  O  OG1 . THR D  1 162 ? 100.307 24.933  -26.239 1.00 23.68 ? 162  THR D OG1 1 
ATOM   9189  C  CG2 . THR D  1 162 ? 98.654  24.542  -27.772 1.00 18.08 ? 162  THR D CG2 1 
ATOM   9190  N  N   . GLY D  1 163 ? 99.455  25.400  -30.496 1.00 18.23 ? 163  GLY D N   1 
ATOM   9191  C  CA  . GLY D  1 163 ? 98.569  25.581  -31.622 1.00 17.59 ? 163  GLY D CA  1 
ATOM   9192  C  C   . GLY D  1 163 ? 99.311  25.932  -32.895 1.00 17.15 ? 163  GLY D C   1 
ATOM   9193  O  O   . GLY D  1 163 ? 100.468 25.484  -33.087 1.00 17.28 ? 163  GLY D O   1 
ATOM   9194  N  N   . PRO D  1 164 ? 98.656  26.702  -33.781 1.00 16.27 ? 164  PRO D N   1 
ATOM   9195  C  CA  . PRO D  1 164 ? 99.213  26.917  -35.118 1.00 15.63 ? 164  PRO D CA  1 
ATOM   9196  C  C   . PRO D  1 164 ? 100.457 27.811  -35.036 1.00 15.78 ? 164  PRO D C   1 
ATOM   9197  O  O   . PRO D  1 164 ? 100.503 28.722  -34.187 1.00 15.45 ? 164  PRO D O   1 
ATOM   9198  C  CB  . PRO D  1 164 ? 98.057  27.578  -35.905 1.00 15.83 ? 164  PRO D CB  1 
ATOM   9199  C  CG  . PRO D  1 164 ? 97.157  28.253  -34.867 1.00 15.06 ? 164  PRO D CG  1 
ATOM   9200  C  CD  . PRO D  1 164 ? 97.357  27.401  -33.590 1.00 15.80 ? 164  PRO D CD  1 
ATOM   9201  N  N   . ASP D  1 165 ? 101.458 27.509  -35.858 1.00 14.94 ? 165  ASP D N   1 
ATOM   9202  C  CA  . ASP D  1 165 ? 102.631 28.375  -35.983 1.00 15.68 ? 165  ASP D CA  1 
ATOM   9203  C  C   . ASP D  1 165 ? 102.266 29.691  -36.711 1.00 15.91 ? 165  ASP D C   1 
ATOM   9204  O  O   . ASP D  1 165 ? 101.090 29.908  -37.082 1.00 15.27 ? 165  ASP D O   1 
ATOM   9205  C  CB  . ASP D  1 165 ? 103.866 27.633  -36.555 1.00 14.64 ? 165  ASP D CB  1 
ATOM   9206  C  CG  . ASP D  1 165 ? 103.684 27.118  -37.993 1.00 14.92 ? 165  ASP D CG  1 
ATOM   9207  O  OD1 . ASP D  1 165 ? 102.724 27.486  -38.694 1.00 11.09 ? 165  ASP D OD1 1 
ATOM   9208  O  OD2 . ASP D  1 165 ? 104.520 26.348  -38.509 1.00 13.12 ? 165  ASP D OD2 1 
ATOM   9209  N  N   . SER D  1 166 ? 103.241 30.578  -36.865 1.00 16.88 ? 166  SER D N   1 
ATOM   9210  C  CA  . SER D  1 166 ? 102.939 31.925  -37.349 1.00 17.35 ? 166  SER D CA  1 
ATOM   9211  C  C   . SER D  1 166 ? 102.449 31.897  -38.821 1.00 17.74 ? 166  SER D C   1 
ATOM   9212  O  O   . SER D  1 166 ? 101.473 32.604  -39.160 1.00 17.79 ? 166  SER D O   1 
ATOM   9213  C  CB  . SER D  1 166 ? 104.105 32.903  -37.065 1.00 17.10 ? 166  SER D CB  1 
ATOM   9214  O  OG  . SER D  1 166 ? 105.236 32.605  -37.865 1.00 19.24 ? 166  SER D OG  1 
ATOM   9215  N  N   . SER D  1 167 ? 103.066 31.035  -39.649 1.00 17.38 ? 167  SER D N   1 
ATOM   9216  C  CA  . SER D  1 167 ? 102.571 30.782  -41.020 1.00 17.46 ? 167  SER D CA  1 
ATOM   9217  C  C   . SER D  1 167 ? 101.120 30.233  -41.040 1.00 17.23 ? 167  SER D C   1 
ATOM   9218  O  O   . SER D  1 167 ? 100.239 30.796  -41.697 1.00 17.63 ? 167  SER D O   1 
ATOM   9219  C  CB  . SER D  1 167 ? 103.504 29.852  -41.797 1.00 17.44 ? 167  SER D CB  1 
ATOM   9220  O  OG  . SER D  1 167 ? 104.751 30.477  -42.059 1.00 18.09 ? 167  SER D OG  1 
ATOM   9221  N  N   . THR D  1 168 ? 100.876 29.147  -40.310 1.00 16.49 ? 168  THR D N   1 
ATOM   9222  C  CA  . THR D  1 168 ? 99.546  28.526  -40.267 1.00 15.83 ? 168  THR D CA  1 
ATOM   9223  C  C   . THR D  1 168 ? 98.451  29.493  -39.773 1.00 15.78 ? 168  THR D C   1 
ATOM   9224  O  O   . THR D  1 168 ? 97.419  29.625  -40.436 1.00 15.51 ? 168  THR D O   1 
ATOM   9225  C  CB  . THR D  1 168 ? 99.560  27.212  -39.434 1.00 15.67 ? 168  THR D CB  1 
ATOM   9226  O  OG1 . THR D  1 168 ? 100.488 26.281  -40.015 1.00 15.52 ? 168  THR D OG1 1 
ATOM   9227  C  CG2 . THR D  1 168 ? 98.222  26.483  -39.514 1.00 15.26 ? 168  THR D CG2 1 
ATOM   9228  N  N   . ILE D  1 169 ? 98.672  30.179  -38.645 1.00 15.24 ? 169  ILE D N   1 
ATOM   9229  C  CA  . ILE D  1 169 ? 97.611  31.022  -38.062 1.00 14.64 ? 169  ILE D CA  1 
ATOM   9230  C  C   . ILE D  1 169 ? 97.293  32.259  -38.948 1.00 16.02 ? 169  ILE D C   1 
ATOM   9231  O  O   . ILE D  1 169 ? 96.279  32.966  -38.716 1.00 15.93 ? 169  ILE D O   1 
ATOM   9232  C  CB  . ILE D  1 169 ? 97.957  31.487  -36.624 1.00 14.75 ? 169  ILE D CB  1 
ATOM   9233  C  CG1 . ILE D  1 169 ? 96.665  31.903  -35.901 1.00 11.72 ? 169  ILE D CG1 1 
ATOM   9234  C  CG2 . ILE D  1 169 ? 99.028  32.640  -36.681 1.00 11.52 ? 169  ILE D CG2 1 
ATOM   9235  C  CD1 . ILE D  1 169 ? 96.750  32.013  -34.410 1.00 11.24 ? 169  ILE D CD1 1 
ATOM   9236  N  N   . SER D  1 170 ? 98.182  32.539  -39.913 1.00 16.89 ? 170  SER D N   1 
ATOM   9237  C  CA  . SER D  1 170 ? 97.964  33.606  -40.899 1.00 17.50 ? 170  SER D CA  1 
ATOM   9238  C  C   . SER D  1 170 ? 97.144  33.114  -42.137 1.00 17.37 ? 170  SER D C   1 
ATOM   9239  O  O   . SER D  1 170 ? 96.888  33.903  -43.066 1.00 17.49 ? 170  SER D O   1 
ATOM   9240  C  CB  . SER D  1 170 ? 99.309  34.224  -41.327 1.00 17.21 ? 170  SER D CB  1 
ATOM   9241  O  OG  . SER D  1 170 ? 100.095 34.569  -40.190 1.00 20.46 ? 170  SER D OG  1 
ATOM   9242  N  N   . THR D  1 171 ? 96.739  31.835  -42.140 1.00 16.67 ? 171  THR D N   1 
ATOM   9243  C  CA  . THR D  1 171 ? 96.014  31.222  -43.275 1.00 16.19 ? 171  THR D CA  1 
ATOM   9244  C  C   . THR D  1 171 ? 94.532  30.885  -42.963 1.00 15.16 ? 171  THR D C   1 
ATOM   9245  O  O   . THR D  1 171 ? 93.830  30.326  -43.809 1.00 14.84 ? 171  THR D O   1 
ATOM   9246  C  CB  . THR D  1 171 ? 96.775  29.955  -43.791 1.00 16.81 ? 171  THR D CB  1 
ATOM   9247  O  OG1 . THR D  1 171 ? 98.033  30.352  -44.373 1.00 17.73 ? 171  THR D OG1 1 
ATOM   9248  C  CG2 . THR D  1 171 ? 96.019  29.265  -45.008 1.00 19.01 ? 171  THR D CG2 1 
ATOM   9249  N  N   . LEU D  1 172 ? 94.062  31.312  -41.787 1.00 12.97 ? 172  LEU D N   1 
ATOM   9250  C  CA  . LEU D  1 172 ? 92.780  30.918  -41.214 1.00 11.59 ? 172  LEU D CA  1 
ATOM   9251  C  C   . LEU D  1 172 ? 91.653  31.965  -41.293 1.00 10.98 ? 172  LEU D C   1 
ATOM   9252  O  O   . LEU D  1 172 ? 90.704  31.918  -40.511 1.00 9.62  ? 172  LEU D O   1 
ATOM   9253  C  CB  . LEU D  1 172 ? 93.003  30.558  -39.731 1.00 11.82 ? 172  LEU D CB  1 
ATOM   9254  C  CG  . LEU D  1 172 ? 94.114  29.535  -39.462 1.00 13.46 ? 172  LEU D CG  1 
ATOM   9255  C  CD1 . LEU D  1 172 ? 94.347  29.394  -37.952 1.00 12.10 ? 172  LEU D CD1 1 
ATOM   9256  C  CD2 . LEU D  1 172 ? 93.740  28.174  -40.100 1.00 13.08 ? 172  LEU D CD2 1 
ATOM   9257  N  N   . GLN D  1 173 ? 91.734  32.905  -42.234 1.00 9.69  ? 173  GLN D N   1 
ATOM   9258  C  CA  . GLN D  1 173 ? 90.719  33.963  -42.267 1.00 9.65  ? 173  GLN D CA  1 
ATOM   9259  C  C   . GLN D  1 173 ? 89.352  33.380  -42.569 1.00 8.70  ? 173  GLN D C   1 
ATOM   9260  O  O   . GLN D  1 173 ? 88.315  33.930  -42.177 1.00 6.71  ? 173  GLN D O   1 
ATOM   9261  C  CB  . GLN D  1 173 ? 91.084  35.000  -43.303 1.00 10.08 ? 173  GLN D CB  1 
ATOM   9262  C  CG  . GLN D  1 173 ? 92.252  35.854  -42.837 1.00 14.58 ? 173  GLN D CG  1 
ATOM   9263  C  CD  . GLN D  1 173 ? 93.190  36.227  -43.952 1.00 22.19 ? 173  GLN D CD  1 
ATOM   9264  O  OE1 . GLN D  1 173 ? 92.749  36.751  -44.982 1.00 28.46 ? 173  GLN D OE1 1 
ATOM   9265  N  NE2 . GLN D  1 173 ? 94.487  35.942  -43.776 1.00 21.43 ? 173  GLN D NE2 1 
ATOM   9266  N  N   . SER D  1 174 ? 89.381  32.239  -43.251 1.00 6.59  ? 174  SER D N   1 
ATOM   9267  C  CA  . SER D  1 174 ? 88.189  31.484  -43.573 1.00 6.98  ? 174  SER D CA  1 
ATOM   9268  C  C   . SER D  1 174 ? 87.405  31.153  -42.308 1.00 6.93  ? 174  SER D C   1 
ATOM   9269  O  O   . SER D  1 174 ? 86.161  31.202  -42.295 1.00 6.25  ? 174  SER D O   1 
ATOM   9270  C  CB  . SER D  1 174 ? 88.625  30.208  -44.313 1.00 7.04  ? 174  SER D CB  1 
ATOM   9271  O  OG  . SER D  1 174 ? 87.516  29.455  -44.679 1.00 7.46  ? 174  SER D OG  1 
ATOM   9272  N  N   . PHE D  1 175 ? 88.141  30.868  -41.219 1.00 6.01  ? 175  PHE D N   1 
ATOM   9273  C  CA  . PHE D  1 175 ? 87.566  30.493  -39.931 1.00 5.19  ? 175  PHE D CA  1 
ATOM   9274  C  C   . PHE D  1 175 ? 87.320  31.699  -39.018 1.00 4.89  ? 175  PHE D C   1 
ATOM   9275  O  O   . PHE D  1 175 ? 87.079  31.545  -37.839 1.00 5.14  ? 175  PHE D O   1 
ATOM   9276  C  CB  . PHE D  1 175 ? 88.497  29.493  -39.223 1.00 5.37  ? 175  PHE D CB  1 
ATOM   9277  C  CG  . PHE D  1 175 ? 88.586  28.153  -39.922 1.00 4.09  ? 175  PHE D CG  1 
ATOM   9278  C  CD1 . PHE D  1 175 ? 87.668  27.157  -39.673 1.00 2.00  ? 175  PHE D CD1 1 
ATOM   9279  C  CD2 . PHE D  1 175 ? 89.596  27.900  -40.837 1.00 3.87  ? 175  PHE D CD2 1 
ATOM   9280  C  CE1 . PHE D  1 175 ? 87.779  25.899  -40.329 1.00 2.00  ? 175  PHE D CE1 1 
ATOM   9281  C  CE2 . PHE D  1 175 ? 89.696  26.677  -41.497 1.00 2.54  ? 175  PHE D CE2 1 
ATOM   9282  C  CZ  . PHE D  1 175 ? 88.792  25.674  -41.221 1.00 2.00  ? 175  PHE D CZ  1 
ATOM   9283  N  N   . ASP D  1 176 ? 87.401  32.905  -39.584 1.00 4.87  ? 176  ASP D N   1 
ATOM   9284  C  CA  . ASP D  1 176 ? 87.346  34.178  -38.812 1.00 3.95  ? 176  ASP D CA  1 
ATOM   9285  C  C   . ASP D  1 176 ? 88.434  34.247  -37.752 1.00 3.66  ? 176  ASP D C   1 
ATOM   9286  O  O   . ASP D  1 176 ? 88.172  34.668  -36.631 1.00 4.65  ? 176  ASP D O   1 
ATOM   9287  C  CB  . ASP D  1 176 ? 85.970  34.333  -38.158 1.00 5.01  ? 176  ASP D CB  1 
ATOM   9288  C  CG  . ASP D  1 176 ? 85.718  35.742  -37.602 1.00 2.65  ? 176  ASP D CG  1 
ATOM   9289  O  OD1 . ASP D  1 176 ? 86.183  36.723  -38.199 1.00 3.83  ? 176  ASP D OD1 1 
ATOM   9290  O  OD2 . ASP D  1 176 ? 85.029  35.936  -36.583 1.00 5.73  ? 176  ASP D OD2 1 
ATOM   9291  N  N   . VAL D  1 177 ? 89.651  33.878  -38.122 1.00 3.26  ? 177  VAL D N   1 
ATOM   9292  C  CA  . VAL D  1 177 ? 90.801  34.066  -37.261 1.00 3.39  ? 177  VAL D CA  1 
ATOM   9293  C  C   . VAL D  1 177 ? 91.795  34.925  -38.014 1.00 3.41  ? 177  VAL D C   1 
ATOM   9294  O  O   . VAL D  1 177 ? 92.209  34.570  -39.099 1.00 2.92  ? 177  VAL D O   1 
ATOM   9295  C  CB  . VAL D  1 177 ? 91.474  32.716  -36.837 1.00 4.94  ? 177  VAL D CB  1 
ATOM   9296  C  CG1 . VAL D  1 177 ? 92.733  33.005  -35.936 1.00 4.31  ? 177  VAL D CG1 1 
ATOM   9297  C  CG2 . VAL D  1 177 ? 90.507  31.886  -36.076 1.00 4.72  ? 177  VAL D CG2 1 
ATOM   9298  N  N   . TYR D  1 178 ? 92.164  36.075  -37.446 1.00 3.86  ? 178  TYR D N   1 
ATOM   9299  C  CA  . TYR D  1 178 ? 93.130  36.955  -38.105 1.00 4.25  ? 178  TYR D CA  1 
ATOM   9300  C  C   . TYR D  1 178 ? 94.310  37.079  -37.195 1.00 3.40  ? 178  TYR D C   1 
ATOM   9301  O  O   . TYR D  1 178 ? 94.155  37.433  -36.038 1.00 2.77  ? 178  TYR D O   1 
ATOM   9302  C  CB  . TYR D  1 178 ? 92.486  38.321  -38.355 1.00 4.88  ? 178  TYR D CB  1 
ATOM   9303  C  CG  . TYR D  1 178 ? 91.321  38.155  -39.305 1.00 6.57  ? 178  TYR D CG  1 
ATOM   9304  C  CD1 . TYR D  1 178 ? 90.072  37.703  -38.864 1.00 6.01  ? 178  TYR D CD1 1 
ATOM   9305  C  CD2 . TYR D  1 178 ? 91.504  38.367  -40.661 1.00 6.38  ? 178  TYR D CD2 1 
ATOM   9306  C  CE1 . TYR D  1 178 ? 89.011  37.480  -39.805 1.00 6.85  ? 178  TYR D CE1 1 
ATOM   9307  C  CE2 . TYR D  1 178 ? 90.485  38.183  -41.563 1.00 7.73  ? 178  TYR D CE2 1 
ATOM   9308  C  CZ  . TYR D  1 178 ? 89.254  37.752  -41.145 1.00 6.64  ? 178  TYR D CZ  1 
ATOM   9309  O  OH  . TYR D  1 178 ? 88.315  37.603  -42.137 1.00 4.80  ? 178  TYR D OH  1 
ATOM   9310  N  N   . ALA D  1 179 ? 95.485  36.757  -37.694 1.00 4.88  ? 179  ALA D N   1 
ATOM   9311  C  CA  . ALA D  1 179 ? 96.715  36.850  -36.906 1.00 6.16  ? 179  ALA D CA  1 
ATOM   9312  C  C   . ALA D  1 179 ? 97.078  38.328  -36.536 1.00 6.73  ? 179  ALA D C   1 
ATOM   9313  O  O   . ALA D  1 179 ? 96.860  39.243  -37.313 1.00 8.11  ? 179  ALA D O   1 
ATOM   9314  C  CB  . ALA D  1 179 ? 97.860  36.191  -37.699 1.00 6.44  ? 179  ALA D CB  1 
ATOM   9315  N  N   . GLU D  1 180 ? 97.657  38.527  -35.358 1.00 7.23  ? 180  GLU D N   1 
ATOM   9316  C  CA  . GLU D  1 180 ? 98.129  39.827  -34.867 1.00 7.62  ? 180  GLU D CA  1 
ATOM   9317  C  C   . GLU D  1 180 ? 99.530  39.558  -34.337 1.00 7.92  ? 180  GLU D C   1 
ATOM   9318  O  O   . GLU D  1 180 ? 99.771  39.538  -33.130 1.00 7.27  ? 180  GLU D O   1 
ATOM   9319  C  CB  . GLU D  1 180 ? 97.244  40.369  -33.728 1.00 6.55  ? 180  GLU D CB  1 
ATOM   9320  C  CG  . GLU D  1 180 ? 95.837  40.787  -34.133 1.00 8.05  ? 180  GLU D CG  1 
ATOM   9321  C  CD  . GLU D  1 180 ? 95.773  41.874  -35.211 1.00 13.49 ? 180  GLU D CD  1 
ATOM   9322  O  OE1 . GLU D  1 180 ? 96.707  42.666  -35.367 1.00 13.71 ? 180  GLU D OE1 1 
ATOM   9323  O  OE2 . GLU D  1 180 ? 94.759  41.931  -35.937 1.00 18.03 ? 180  GLU D OE2 1 
ATOM   9324  N  N   . LEU D  1 181 ? 100.452 39.325  -35.250 1.00 9.02  ? 181  LEU D N   1 
ATOM   9325  C  CA  . LEU D  1 181 ? 101.747 38.797  -34.870 1.00 11.16 ? 181  LEU D CA  1 
ATOM   9326  C  C   . LEU D  1 181 ? 102.629 39.905  -34.302 1.00 11.17 ? 181  LEU D C   1 
ATOM   9327  O  O   . LEU D  1 181 ? 103.659 39.618  -33.662 1.00 11.65 ? 181  LEU D O   1 
ATOM   9328  C  CB  . LEU D  1 181 ? 102.427 38.111  -36.074 1.00 12.38 ? 181  LEU D CB  1 
ATOM   9329  C  CG  . LEU D  1 181 ? 101.785 36.861  -36.724 1.00 14.03 ? 181  LEU D CG  1 
ATOM   9330  C  CD1 . LEU D  1 181 ? 102.714 36.364  -37.801 1.00 17.04 ? 181  LEU D CD1 1 
ATOM   9331  C  CD2 . LEU D  1 181 ? 101.474 35.718  -35.745 1.00 16.22 ? 181  LEU D CD2 1 
ATOM   9332  N  N   . SER D  1 182 ? 102.232 41.161  -34.537 1.00 10.36 ? 182  SER D N   1 
ATOM   9333  C  CA  . SER D  1 182 ? 102.944 42.299  -33.949 1.00 10.35 ? 182  SER D CA  1 
ATOM   9334  C  C   . SER D  1 182 ? 102.486 42.618  -32.491 1.00 8.87  ? 182  SER D C   1 
ATOM   9335  O  O   . SER D  1 182 ? 103.058 43.483  -31.820 1.00 8.58  ? 182  SER D O   1 
ATOM   9336  C  CB  . SER D  1 182 ? 102.851 43.535  -34.871 1.00 11.88 ? 182  SER D CB  1 
ATOM   9337  O  OG  . SER D  1 182 ? 101.607 44.229  -34.684 1.00 15.98 ? 182  SER D OG  1 
ATOM   9338  N  N   . PHE D  1 183 ? 101.449 41.938  -32.014 1.00 6.53  ? 183  PHE D N   1 
ATOM   9339  C  CA  . PHE D  1 183 ? 100.961 42.152  -30.641 1.00 5.86  ? 183  PHE D CA  1 
ATOM   9340  C  C   . PHE D  1 183 ? 101.941 41.529  -29.656 1.00 5.82  ? 183  PHE D C   1 
ATOM   9341  O  O   . PHE D  1 183 ? 102.344 40.382  -29.826 1.00 6.02  ? 183  PHE D O   1 
ATOM   9342  C  CB  . PHE D  1 183 ? 99.550  41.546  -30.496 1.00 4.96  ? 183  PHE D CB  1 
ATOM   9343  C  CG  . PHE D  1 183 ? 98.939  41.627  -29.088 1.00 5.43  ? 183  PHE D CG  1 
ATOM   9344  C  CD1 . PHE D  1 183 ? 98.222  42.764  -28.704 1.00 8.84  ? 183  PHE D CD1 1 
ATOM   9345  C  CD2 . PHE D  1 183 ? 99.015  40.555  -28.195 1.00 4.16  ? 183  PHE D CD2 1 
ATOM   9346  C  CE1 . PHE D  1 183 ? 97.604  42.820  -27.450 1.00 8.75  ? 183  PHE D CE1 1 
ATOM   9347  C  CE2 . PHE D  1 183 ? 98.416  40.605  -26.934 1.00 7.70  ? 183  PHE D CE2 1 
ATOM   9348  C  CZ  . PHE D  1 183 ? 97.697  41.746  -26.564 1.00 9.88  ? 183  PHE D CZ  1 
ATOM   9349  N  N   . THR D  1 184 ? 102.322 42.285  -28.626 1.00 5.59  ? 184  THR D N   1 
ATOM   9350  C  CA  . THR D  1 184 ? 103.194 41.783  -27.575 1.00 5.84  ? 184  THR D CA  1 
ATOM   9351  C  C   . THR D  1 184 ? 102.410 41.668  -26.258 1.00 5.87  ? 184  THR D C   1 
ATOM   9352  O  O   . THR D  1 184 ? 102.070 42.700  -25.636 1.00 5.73  ? 184  THR D O   1 
ATOM   9353  C  CB  . THR D  1 184 ? 104.441 42.715  -27.400 1.00 6.55  ? 184  THR D CB  1 
ATOM   9354  O  OG1 . THR D  1 184 ? 105.187 42.786  -28.629 1.00 6.13  ? 184  THR D OG1 1 
ATOM   9355  C  CG2 . THR D  1 184 ? 105.423 42.133  -26.384 1.00 7.37  ? 184  THR D CG2 1 
ATOM   9356  N  N   . PRO D  1 185 ? 102.082 40.437  -25.818 1.00 5.11  ? 185  PRO D N   1 
ATOM   9357  C  CA  . PRO D  1 185 ? 101.432 40.271  -24.494 1.00 5.73  ? 185  PRO D CA  1 
ATOM   9358  C  C   . PRO D  1 185 ? 102.269 40.953  -23.399 1.00 5.89  ? 185  PRO D C   1 
ATOM   9359  O  O   . PRO D  1 185 ? 103.467 40.701  -23.318 1.00 4.03  ? 185  PRO D O   1 
ATOM   9360  C  CB  . PRO D  1 185 ? 101.404 38.760  -24.299 1.00 6.14  ? 185  PRO D CB  1 
ATOM   9361  C  CG  . PRO D  1 185 ? 101.267 38.222  -25.740 1.00 4.81  ? 185  PRO D CG  1 
ATOM   9362  C  CD  . PRO D  1 185 ? 102.269 39.145  -26.505 1.00 4.70  ? 185  PRO D CD  1 
ATOM   9363  N  N   . ARG D  1 186 ? 101.644 41.799  -22.574 1.00 5.58  ? 186  ARG D N   1 
ATOM   9364  C  CA  . ARG D  1 186 ? 102.426 42.583  -21.613 1.00 6.49  ? 186  ARG D CA  1 
ATOM   9365  C  C   . ARG D  1 186 ? 102.932 41.675  -20.517 1.00 7.07  ? 186  ARG D C   1 
ATOM   9366  O  O   . ARG D  1 186 ? 102.273 40.675  -20.169 1.00 7.09  ? 186  ARG D O   1 
ATOM   9367  C  CB  . ARG D  1 186 ? 101.657 43.774  -21.035 1.00 4.93  ? 186  ARG D CB  1 
ATOM   9368  C  CG  . ARG D  1 186 ? 100.361 43.454  -20.304 1.00 4.87  ? 186  ARG D CG  1 
ATOM   9369  C  CD  . ARG D  1 186 ? 99.581  44.714  -19.899 1.00 4.60  ? 186  ARG D CD  1 
ATOM   9370  N  NE  . ARG D  1 186 ? 100.442 45.743  -19.258 1.00 5.86  ? 186  ARG D NE  1 
ATOM   9371  C  CZ  . ARG D  1 186 ? 100.266 47.052  -19.407 1.00 7.37  ? 186  ARG D CZ  1 
ATOM   9372  N  NH1 . ARG D  1 186 ? 99.268  47.497  -20.162 1.00 6.94  ? 186  ARG D NH1 1 
ATOM   9373  N  NH2 . ARG D  1 186 ? 101.081 47.923  -18.780 1.00 7.28  ? 186  ARG D NH2 1 
ATOM   9374  N  N   . THR D  1 187 ? 104.093 42.025  -19.986 1.00 6.94  ? 187  THR D N   1 
ATOM   9375  C  CA  . THR D  1 187 ? 104.817 41.100  -19.118 1.00 9.11  ? 187  THR D CA  1 
ATOM   9376  C  C   . THR D  1 187 ? 105.146 41.736  -17.757 1.00 9.53  ? 187  THR D C   1 
ATOM   9377  O  O   . THR D  1 187 ? 106.139 41.382  -17.116 1.00 9.56  ? 187  THR D O   1 
ATOM   9378  C  CB  . THR D  1 187 ? 106.105 40.624  -19.807 1.00 9.32  ? 187  THR D CB  1 
ATOM   9379  O  OG1 . THR D  1 187 ? 106.771 41.742  -20.370 1.00 9.10  ? 187  THR D OG1 1 
ATOM   9380  C  CG2 . THR D  1 187 ? 105.775 39.784  -21.038 1.00 10.93 ? 187  THR D CG2 1 
ATOM   9381  N  N   . ASP D  1 188 ? 104.295 42.673  -17.347 1.00 9.05  ? 188  ASP D N   1 
ATOM   9382  C  CA  . ASP D  1 188 ? 104.446 43.367  -16.089 1.00 8.64  ? 188  ASP D CA  1 
ATOM   9383  C  C   . ASP D  1 188 ? 103.287 43.038  -15.156 1.00 7.73  ? 188  ASP D C   1 
ATOM   9384  O  O   . ASP D  1 188 ? 102.894 43.848  -14.309 1.00 7.32  ? 188  ASP D O   1 
ATOM   9385  C  CB  . ASP D  1 188 ? 104.605 44.867  -16.330 1.00 7.20  ? 188  ASP D CB  1 
ATOM   9386  C  CG  . ASP D  1 188 ? 103.438 45.470  -17.066 1.00 9.76  ? 188  ASP D CG  1 
ATOM   9387  O  OD1 . ASP D  1 188 ? 102.542 44.723  -17.585 1.00 8.78  ? 188  ASP D OD1 1 
ATOM   9388  O  OD2 . ASP D  1 188 ? 103.335 46.709  -17.201 1.00 9.20  ? 188  ASP D OD2 1 
ATOM   9389  N  N   . THR D  1 189 ? 102.745 41.834  -15.301 1.00 7.95  ? 189  THR D N   1 
ATOM   9390  C  CA  . THR D  1 189 ? 101.666 41.352  -14.435 1.00 7.27  ? 189  THR D CA  1 
ATOM   9391  C  C   . THR D  1 189 ? 102.154 41.341  -12.994 1.00 8.15  ? 189  THR D C   1 
ATOM   9392  O  O   . THR D  1 189 ? 103.289 40.931  -12.700 1.00 7.50  ? 189  THR D O   1 
ATOM   9393  C  CB  . THR D  1 189 ? 101.251 39.922  -14.819 1.00 7.14  ? 189  THR D CB  1 
ATOM   9394  O  OG1 . THR D  1 189 ? 101.009 39.839  -16.230 1.00 9.83  ? 189  THR D OG1 1 
ATOM   9395  C  CG2 . THR D  1 189 ? 99.886  39.566  -14.217 1.00 5.43  ? 189  THR D CG2 1 
ATOM   9396  N  N   . VAL D  1 190 ? 101.306 41.812  -12.082 1.00 7.44  ? 190  VAL D N   1 
ATOM   9397  C  CA  . VAL D  1 190 ? 101.598 41.719  -10.665 1.00 7.65  ? 190  VAL D CA  1 
ATOM   9398  C  C   . VAL D  1 190 ? 100.282 41.501  -9.991  1.00 6.86  ? 190  VAL D C   1 
ATOM   9399  O  O   . VAL D  1 190 ? 99.268  42.162  -10.329 1.00 6.42  ? 190  VAL D O   1 
ATOM   9400  C  CB  . VAL D  1 190 ? 102.193 43.025  -10.065 1.00 7.82  ? 190  VAL D CB  1 
ATOM   9401  C  CG1 . VAL D  1 190 ? 102.447 42.803  -8.557  1.00 10.95 ? 190  VAL D CG1 1 
ATOM   9402  C  CG2 . VAL D  1 190 ? 103.458 43.414  -10.745 1.00 10.17 ? 190  VAL D CG2 1 
ATOM   9403  N  N   . ASN D  1 191 ? 100.258 40.521  -9.081  1.00 6.57  ? 191  ASN D N   1 
ATOM   9404  C  CA  . ASN D  1 191 ? 99.039  40.132  -8.411  1.00 7.65  ? 191  ASN D CA  1 
ATOM   9405  C  C   . ASN D  1 191 ? 97.904  39.840  -9.403  1.00 7.77  ? 191  ASN D C   1 
ATOM   9406  O  O   . ASN D  1 191 ? 96.734  40.149  -9.141  1.00 7.45  ? 191  ASN D O   1 
ATOM   9407  C  CB  . ASN D  1 191 ? 98.566  41.208  -7.376  1.00 8.60  ? 191  ASN D CB  1 
ATOM   9408  C  CG  . ASN D  1 191 ? 99.526  41.425  -6.253  1.00 10.78 ? 191  ASN D CG  1 
ATOM   9409  O  OD1 . ASN D  1 191 ? 100.321 40.543  -5.885  1.00 9.78  ? 191  ASN D OD1 1 
ATOM   9410  N  ND2 . ASN D  1 191 ? 99.501  42.660  -5.720  1.00 15.56 ? 191  ASN D ND2 1 
ATOM   9411  N  N   . GLY D  1 192 ? 98.232  39.224  -10.532 1.00 5.63  ? 192  GLY D N   1 
ATOM   9412  C  CA  . GLY D  1 192 ? 97.205  38.687  -11.410 1.00 5.28  ? 192  GLY D CA  1 
ATOM   9413  C  C   . GLY D  1 192 ? 96.616  39.757  -12.316 1.00 5.89  ? 192  GLY D C   1 
ATOM   9414  O  O   . GLY D  1 192 ? 95.605  39.506  -12.963 1.00 5.61  ? 192  GLY D O   1 
ATOM   9415  N  N   . THR D  1 193 ? 97.230  40.931  -12.372 1.00 5.37  ? 193  THR D N   1 
ATOM   9416  C  CA  . THR D  1 193 ? 96.756  41.944  -13.323 1.00 4.00  ? 193  THR D CA  1 
ATOM   9417  C  C   . THR D  1 193 ? 97.804  42.917  -13.886 1.00 5.02  ? 193  THR D C   1 
ATOM   9418  O  O   . THR D  1 193 ? 98.865  43.152  -13.264 1.00 4.24  ? 193  THR D O   1 
ATOM   9419  C  CB  . THR D  1 193 ? 95.543  42.700  -12.643 1.00 4.51  ? 193  THR D CB  1 
ATOM   9420  O  OG1 . THR D  1 193 ? 94.839  43.505  -13.601 1.00 4.88  ? 193  THR D OG1 1 
ATOM   9421  C  CG2 . THR D  1 193 ? 96.072  43.701  -11.561 1.00 2.71  ? 193  THR D CG2 1 
ATOM   9422  N  N   . ALA D  1 194 ? 97.488  43.514  -15.060 1.00 3.41  ? 194  ALA D N   1 
ATOM   9423  C  CA  . ALA D  1 194 ? 98.178  44.718  -15.558 1.00 4.73  ? 194  ALA D CA  1 
ATOM   9424  C  C   . ALA D  1 194 ? 97.226  45.405  -16.525 1.00 4.92  ? 194  ALA D C   1 
ATOM   9425  O  O   . ALA D  1 194 ? 96.352  44.715  -17.082 1.00 8.18  ? 194  ALA D O   1 
ATOM   9426  C  CB  . ALA D  1 194 ? 99.536  44.410  -16.213 1.00 4.09  ? 194  ALA D CB  1 
ATOM   9427  N  N   . PRO D  1 195 ? 97.257  46.740  -16.656 1.00 5.78  ? 195  PRO D N   1 
ATOM   9428  C  CA  . PRO D  1 195 ? 98.187  47.647  -15.957 1.00 5.05  ? 195  PRO D CA  1 
ATOM   9429  C  C   . PRO D  1 195 ? 97.890  47.812  -14.459 1.00 6.20  ? 195  PRO D C   1 
ATOM   9430  O  O   . PRO D  1 195 ? 96.881  47.276  -13.990 1.00 7.14  ? 195  PRO D O   1 
ATOM   9431  C  CB  . PRO D  1 195 ? 97.949  48.984  -16.679 1.00 5.51  ? 195  PRO D CB  1 
ATOM   9432  C  CG  . PRO D  1 195 ? 96.437  48.903  -17.011 1.00 5.06  ? 195  PRO D CG  1 
ATOM   9433  C  CD  . PRO D  1 195 ? 96.300  47.486  -17.501 1.00 5.20  ? 195  PRO D CD  1 
ATOM   9434  N  N   . ALA D  1 196 ? 98.769  48.508  -13.714 1.00 6.39  ? 196  ALA D N   1 
ATOM   9435  C  CA  . ALA D  1 196 ? 98.611  48.636  -12.249 1.00 7.71  ? 196  ALA D CA  1 
ATOM   9436  C  C   . ALA D  1 196 ? 97.265  49.250  -11.795 1.00 9.18  ? 196  ALA D C   1 
ATOM   9437  O  O   . ALA D  1 196 ? 96.704  48.831  -10.784 1.00 10.58 ? 196  ALA D O   1 
ATOM   9438  C  CB  . ALA D  1 196 ? 99.815  49.413  -11.602 1.00 6.53  ? 196  ALA D CB  1 
ATOM   9439  N  N   . ASN D  1 197 ? 96.739  50.210  -12.540 1.00 10.25 ? 197  ASN D N   1 
ATOM   9440  C  CA  . ASN D  1 197 ? 95.514  50.917  -12.107 1.00 12.21 ? 197  ASN D CA  1 
ATOM   9441  C  C   . ASN D  1 197 ? 94.256  50.164  -12.570 1.00 12.46 ? 197  ASN D C   1 
ATOM   9442  O  O   . ASN D  1 197 ? 93.479  50.643  -13.429 1.00 15.26 ? 197  ASN D O   1 
ATOM   9443  C  CB  . ASN D  1 197 ? 95.505  52.354  -12.653 1.00 12.71 ? 197  ASN D CB  1 
ATOM   9444  C  CG  . ASN D  1 197 ? 95.092  52.438  -14.138 1.00 17.25 ? 197  ASN D CG  1 
ATOM   9445  O  OD1 . ASN D  1 197 ? 95.492  51.606  -14.969 1.00 23.38 ? 197  ASN D OD1 1 
ATOM   9446  N  ND2 . ASN D  1 197 ? 94.319  53.465  -14.479 1.00 18.95 ? 197  ASN D ND2 1 
ATOM   9447  N  N   . THR D  1 198 ? 94.128  48.948  -12.091 1.00 10.00 ? 198  THR D N   1 
ATOM   9448  C  CA  . THR D  1 198 ? 92.991  48.131  -12.368 1.00 9.31  ? 198  THR D CA  1 
ATOM   9449  C  C   . THR D  1 198 ? 92.599  47.521  -11.048 1.00 8.60  ? 198  THR D C   1 
ATOM   9450  O  O   . THR D  1 198 ? 93.312  47.634  -10.044 1.00 7.76  ? 198  THR D O   1 
ATOM   9451  C  CB  . THR D  1 198 ? 93.306  46.993  -13.362 1.00 8.78  ? 198  THR D CB  1 
ATOM   9452  O  OG1 . THR D  1 198 ? 94.482  46.312  -12.928 1.00 9.23  ? 198  THR D OG1 1 
ATOM   9453  C  CG2 . THR D  1 198 ? 93.653  47.549  -14.753 1.00 7.71  ? 198  THR D CG2 1 
ATOM   9454  N  N   . VAL D  1 199 ? 91.490  46.820  -11.069 1.00 8.06  ? 199  VAL D N   1 
ATOM   9455  C  CA  . VAL D  1 199 ? 90.941  46.256  -9.867  1.00 7.88  ? 199  VAL D CA  1 
ATOM   9456  C  C   . VAL D  1 199 ? 90.677  44.790  -10.239 1.00 7.20  ? 199  VAL D C   1 
ATOM   9457  O  O   . VAL D  1 199 ? 89.946  44.507  -11.192 1.00 7.15  ? 199  VAL D O   1 
ATOM   9458  C  CB  . VAL D  1 199 ? 89.649  47.019  -9.450  1.00 7.54  ? 199  VAL D CB  1 
ATOM   9459  C  CG1 . VAL D  1 199 ? 88.899  46.243  -8.387  1.00 7.83  ? 199  VAL D CG1 1 
ATOM   9460  C  CG2 . VAL D  1 199 ? 89.995  48.529  -8.990  1.00 8.65  ? 199  VAL D CG2 1 
ATOM   9461  N  N   . TRP D  1 200 ? 91.303  43.872  -9.513  1.00 7.11  ? 200  TRP D N   1 
ATOM   9462  C  CA  . TRP D  1 200 ? 91.190  42.440  -9.818  1.00 7.67  ? 200  TRP D CA  1 
ATOM   9463  C  C   . TRP D  1 200 ? 91.261  41.674  -8.473  1.00 8.22  ? 200  TRP D C   1 
ATOM   9464  O  O   . TRP D  1 200 ? 92.327  41.680  -7.804  1.00 6.64  ? 200  TRP D O   1 
ATOM   9465  C  CB  . TRP D  1 200 ? 92.302  41.965  -10.784 1.00 8.05  ? 200  TRP D CB  1 
ATOM   9466  C  CG  . TRP D  1 200 ? 92.040  40.577  -11.334 1.00 6.23  ? 200  TRP D CG  1 
ATOM   9467  C  CD1 . TRP D  1 200 ? 92.837  39.479  -11.236 1.00 6.32  ? 200  TRP D CD1 1 
ATOM   9468  C  CD2 . TRP D  1 200 ? 90.884  40.168  -12.055 1.00 4.16  ? 200  TRP D CD2 1 
ATOM   9469  N  NE1 . TRP D  1 200 ? 92.251  38.417  -11.873 1.00 5.88  ? 200  TRP D NE1 1 
ATOM   9470  C  CE2 . TRP D  1 200 ? 91.050  38.813  -12.384 1.00 7.75  ? 200  TRP D CE2 1 
ATOM   9471  C  CE3 . TRP D  1 200 ? 89.739  40.847  -12.520 1.00 5.92  ? 200  TRP D CE3 1 
ATOM   9472  C  CZ2 . TRP D  1 200 ? 90.070  38.074  -13.090 1.00 7.24  ? 200  TRP D CZ2 1 
ATOM   9473  C  CZ3 . TRP D  1 200 ? 88.782  40.125  -13.220 1.00 5.36  ? 200  TRP D CZ3 1 
ATOM   9474  C  CH2 . TRP D  1 200 ? 88.964  38.756  -13.521 1.00 7.69  ? 200  TRP D CH2 1 
ATOM   9475  N  N   . HIS D  1 201 ? 90.112  41.113  -8.063  1.00 8.37  ? 201  HIS D N   1 
ATOM   9476  C  CA  . HIS D  1 201 ? 89.914  40.436  -6.769  1.00 9.95  ? 201  HIS D CA  1 
ATOM   9477  C  C   . HIS D  1 201 ? 90.134  41.361  -5.539  1.00 10.88 ? 201  HIS D C   1 
ATOM   9478  O  O   . HIS D  1 201 ? 90.363  40.884  -4.405  1.00 11.03 ? 201  HIS D O   1 
ATOM   9479  C  CB  . HIS D  1 201 ? 90.799  39.195  -6.650  1.00 10.17 ? 201  HIS D CB  1 
ATOM   9480  C  CG  . HIS D  1 201 ? 90.353  38.060  -7.512  1.00 10.62 ? 201  HIS D CG  1 
ATOM   9481  N  ND1 . HIS D  1 201 ? 89.473  37.089  -7.072  1.00 9.66  ? 201  HIS D ND1 1 
ATOM   9482  C  CD2 . HIS D  1 201 ? 90.674  37.730  -8.789  1.00 10.58 ? 201  HIS D CD2 1 
ATOM   9483  C  CE1 . HIS D  1 201 ? 89.266  36.216  -8.043  1.00 8.11  ? 201  HIS D CE1 1 
ATOM   9484  N  NE2 . HIS D  1 201 ? 89.964  36.590  -9.100  1.00 7.23  ? 201  HIS D NE2 1 
ATOM   9485  N  N   . THR D  1 202 ? 90.067  42.675  -5.759  1.00 10.89 ? 202  THR D N   1 
ATOM   9486  C  CA  . THR D  1 202 ? 90.321  43.604  -4.671  1.00 12.32 ? 202  THR D CA  1 
ATOM   9487  C  C   . THR D  1 202 ? 89.245  44.662  -4.543  1.00 12.17 ? 202  THR D C   1 
ATOM   9488  O  O   . THR D  1 202 ? 89.422  45.605  -3.788  1.00 12.71 ? 202  THR D O   1 
ATOM   9489  C  CB  . THR D  1 202 ? 91.701  44.317  -4.861  1.00 12.41 ? 202  THR D CB  1 
ATOM   9490  O  OG1 . THR D  1 202 ? 91.753  44.903  -6.168  1.00 13.78 ? 202  THR D OG1 1 
ATOM   9491  C  CG2 . THR D  1 202 ? 92.932  43.282  -4.847  1.00 14.01 ? 202  THR D CG2 1 
ATOM   9492  N  N   . GLY D  1 203 ? 88.147  44.532  -5.273  1.00 11.61 ? 203  GLY D N   1 
ATOM   9493  C  CA  . GLY D  1 203 ? 87.146  45.606  -5.280  1.00 9.55  ? 203  GLY D CA  1 
ATOM   9494  C  C   . GLY D  1 203 ? 86.177  45.278  -6.397  1.00 9.79  ? 203  GLY D C   1 
ATOM   9495  O  O   . GLY D  1 203 ? 86.389  44.288  -7.115  1.00 8.13  ? 203  GLY D O   1 
ATOM   9496  N  N   . ALA D  1 204 ? 85.119  46.071  -6.537  1.00 8.74  ? 204  ALA D N   1 
ATOM   9497  C  CA  . ALA D  1 204 ? 84.087  45.747  -7.508  1.00 9.46  ? 204  ALA D CA  1 
ATOM   9498  C  C   . ALA D  1 204 ? 84.555  45.959  -8.952  1.00 8.56  ? 204  ALA D C   1 
ATOM   9499  O  O   . ALA D  1 204 ? 85.415  46.819  -9.199  1.00 10.08 ? 204  ALA D O   1 
ATOM   9500  C  CB  . ALA D  1 204 ? 82.838  46.553  -7.201  1.00 9.22  ? 204  ALA D CB  1 
ATOM   9501  N  N   . ASN D  1 205 ? 84.073  45.115  -9.878  1.00 8.24  ? 205  ASN D N   1 
ATOM   9502  C  CA  . ASN D  1 205 ? 84.242  45.354  -11.325 1.00 8.72  ? 205  ASN D CA  1 
ATOM   9503  C  C   . ASN D  1 205 ? 82.954  45.744  -11.951 1.00 7.90  ? 205  ASN D C   1 
ATOM   9504  O  O   . ASN D  1 205 ? 81.915  45.231  -11.522 1.00 8.53  ? 205  ASN D O   1 
ATOM   9505  C  CB  . ASN D  1 205 ? 84.756  44.087  -12.031 1.00 9.32  ? 205  ASN D CB  1 
ATOM   9506  C  CG  . ASN D  1 205 ? 86.010  43.546  -11.381 1.00 8.57  ? 205  ASN D CG  1 
ATOM   9507  O  OD1 . ASN D  1 205 ? 86.074  42.366  -10.965 1.00 6.90  ? 205  ASN D OD1 1 
ATOM   9508  N  ND2 . ASN D  1 205 ? 87.000  44.410  -11.239 1.00 6.98  ? 205  ASN D ND2 1 
ATOM   9509  N  N   . ALA D  1 206 ? 82.997  46.635  -12.947 1.00 7.37  ? 206  ALA D N   1 
ATOM   9510  C  CA  . ALA D  1 206 ? 81.793  46.935  -13.745 1.00 7.59  ? 206  ALA D CA  1 
ATOM   9511  C  C   . ALA D  1 206 ? 81.902  46.326  -15.130 1.00 7.90  ? 206  ALA D C   1 
ATOM   9512  O  O   . ALA D  1 206 ? 83.004  46.160  -15.635 1.00 7.23  ? 206  ALA D O   1 
ATOM   9513  C  CB  . ALA D  1 206 ? 81.528  48.483  -13.827 1.00 5.37  ? 206  ALA D CB  1 
ATOM   9514  N  N   . LEU D  1 207 ? 80.769  45.949  -15.739 1.00 8.00  ? 207  LEU D N   1 
ATOM   9515  C  CA  . LEU D  1 207 ? 80.771  45.670  -17.191 1.00 7.36  ? 207  LEU D CA  1 
ATOM   9516  C  C   . LEU D  1 207 ? 81.163  46.895  -17.957 1.00 6.47  ? 207  LEU D C   1 
ATOM   9517  O  O   . LEU D  1 207 ? 80.775  48.000  -17.574 1.00 7.60  ? 207  LEU D O   1 
ATOM   9518  C  CB  . LEU D  1 207 ? 79.371  45.271  -17.653 1.00 6.38  ? 207  LEU D CB  1 
ATOM   9519  C  CG  . LEU D  1 207 ? 79.010  43.806  -17.311 1.00 9.87  ? 207  LEU D CG  1 
ATOM   9520  C  CD1 . LEU D  1 207 ? 78.783  43.658  -15.820 1.00 10.79 ? 207  LEU D CD1 1 
ATOM   9521  C  CD2 . LEU D  1 207 ? 77.731  43.417  -18.055 1.00 7.36  ? 207  LEU D CD2 1 
ATOM   9522  N  N   . ALA D  1 208 ? 81.921  46.726  -19.036 1.00 6.60  ? 208  ALA D N   1 
ATOM   9523  C  CA  . ALA D  1 208 ? 82.293  47.845  -19.898 1.00 7.80  ? 208  ALA D CA  1 
ATOM   9524  C  C   . ALA D  1 208 ? 81.058  48.612  -20.355 1.00 8.39  ? 208  ALA D C   1 
ATOM   9525  O  O   . ALA D  1 208 ? 80.092  48.021  -20.838 1.00 8.44  ? 208  ALA D O   1 
ATOM   9526  C  CB  . ALA D  1 208 ? 83.089  47.354  -21.115 1.00 7.80  ? 208  ALA D CB  1 
ATOM   9527  N  N   . SER D  1 209 ? 81.071  49.928  -20.195 1.00 8.69  ? 209  SER D N   1 
ATOM   9528  C  CA  . SER D  1 209 ? 79.955  50.715  -20.704 1.00 9.55  ? 209  SER D CA  1 
ATOM   9529  C  C   . SER D  1 209 ? 80.142  51.057  -22.198 1.00 11.28 ? 209  SER D C   1 
ATOM   9530  O  O   . SER D  1 209 ? 79.200  51.486  -22.887 1.00 11.78 ? 209  SER D O   1 
ATOM   9531  C  CB  . SER D  1 209 ? 79.728  51.945  -19.823 1.00 10.63 ? 209  SER D CB  1 
ATOM   9532  O  OG  . SER D  1 209 ? 80.837  52.828  -19.815 1.00 7.76  ? 209  SER D OG  1 
ATOM   9533  N  N   . THR D  1 210 ? 81.369  50.875  -22.685 1.00 11.64 ? 210  THR D N   1 
ATOM   9534  C  CA  . THR D  1 210 ? 81.761  51.198  -24.056 1.00 12.08 ? 210  THR D CA  1 
ATOM   9535  C  C   . THR D  1 210 ? 81.755  49.871  -24.822 1.00 12.29 ? 210  THR D C   1 
ATOM   9536  O  O   . THR D  1 210 ? 82.488  48.957  -24.445 1.00 11.74 ? 210  THR D O   1 
ATOM   9537  C  CB  . THR D  1 210 ? 83.194  51.799  -23.994 1.00 12.06 ? 210  THR D CB  1 
ATOM   9538  O  OG1 . THR D  1 210 ? 83.171  53.090  -23.339 1.00 14.92 ? 210  THR D OG1 1 
ATOM   9539  C  CG2 . THR D  1 210 ? 83.790  52.063  -25.406 1.00 12.95 ? 210  THR D CG2 1 
ATOM   9540  N  N   . ALA D  1 211 ? 80.903  49.736  -25.842 1.00 11.78 ? 211  ALA D N   1 
ATOM   9541  C  CA  . ALA D  1 211 ? 80.849  48.490  -26.613 1.00 12.69 ? 211  ALA D CA  1 
ATOM   9542  C  C   . ALA D  1 211 ? 82.131  48.358  -27.448 1.00 12.14 ? 211  ALA D C   1 
ATOM   9543  O  O   . ALA D  1 211 ? 82.684  49.361  -27.899 1.00 10.30 ? 211  ALA D O   1 
ATOM   9544  C  CB  . ALA D  1 211 ? 79.658  48.473  -27.519 1.00 13.70 ? 211  ALA D CB  1 
ATOM   9545  N  N   . GLY D  1 212 ? 82.588  47.129  -27.665 1.00 11.62 ? 212  GLY D N   1 
ATOM   9546  C  CA  . GLY D  1 212 ? 83.839  46.934  -28.394 1.00 10.94 ? 212  GLY D CA  1 
ATOM   9547  C  C   . GLY D  1 212 ? 85.045  46.789  -27.465 1.00 11.18 ? 212  GLY D C   1 
ATOM   9548  O  O   . GLY D  1 212 ? 86.093  46.326  -27.886 1.00 10.91 ? 212  GLY D O   1 
ATOM   9549  N  N   . ASP D  1 213 ? 84.912  47.190  -26.196 1.00 10.05 ? 213  ASP D N   1 
ATOM   9550  C  CA  . ASP D  1 213 ? 86.044  47.116  -25.262 1.00 8.38  ? 213  ASP D CA  1 
ATOM   9551  C  C   . ASP D  1 213 ? 86.006  45.824  -24.492 1.00 7.37  ? 213  ASP D C   1 
ATOM   9552  O  O   . ASP D  1 213 ? 84.966  45.443  -23.975 1.00 5.72  ? 213  ASP D O   1 
ATOM   9553  C  CB  . ASP D  1 213 ? 85.946  48.212  -24.202 1.00 7.99  ? 213  ASP D CB  1 
ATOM   9554  C  CG  . ASP D  1 213 ? 86.390  49.552  -24.706 1.00 12.63 ? 213  ASP D CG  1 
ATOM   9555  O  OD1 . ASP D  1 213 ? 86.767  49.676  -25.898 1.00 13.40 ? 213  ASP D OD1 1 
ATOM   9556  O  OD2 . ASP D  1 213 ? 86.438  50.523  -23.943 1.00 12.12 ? 213  ASP D OD2 1 
ATOM   9557  N  N   . PRO D  1 214 ? 87.162  45.214  -24.301 1.00 6.16  ? 214  PRO D N   1 
ATOM   9558  C  CA  . PRO D  1 214 ? 87.232  44.039  -23.432 1.00 6.56  ? 214  PRO D CA  1 
ATOM   9559  C  C   . PRO D  1 214 ? 87.034  44.407  -21.941 1.00 5.99  ? 214  PRO D C   1 
ATOM   9560  O  O   . PRO D  1 214 ? 87.212  45.546  -21.559 1.00 6.80  ? 214  PRO D O   1 
ATOM   9561  C  CB  . PRO D  1 214 ? 88.647  43.515  -23.667 1.00 6.33  ? 214  PRO D CB  1 
ATOM   9562  C  CG  . PRO D  1 214 ? 89.446  44.743  -23.964 1.00 5.94  ? 214  PRO D CG  1 
ATOM   9563  C  CD  . PRO D  1 214 ? 88.482  45.593  -24.867 1.00 5.69  ? 214  PRO D CD  1 
ATOM   9564  N  N   . TYR D  1 215 ? 86.625  43.445  -21.119 1.00 5.58  ? 215  TYR D N   1 
ATOM   9565  C  CA  . TYR D  1 215 ? 86.525  43.708  -19.669 1.00 6.78  ? 215  TYR D CA  1 
ATOM   9566  C  C   . TYR D  1 215 ? 86.528  42.410  -18.926 1.00 7.46  ? 215  TYR D C   1 
ATOM   9567  O  O   . TYR D  1 215 ? 86.186  41.355  -19.501 1.00 6.64  ? 215  TYR D O   1 
ATOM   9568  C  CB  . TYR D  1 215 ? 85.269  44.508  -19.306 1.00 5.96  ? 215  TYR D CB  1 
ATOM   9569  C  CG  . TYR D  1 215 ? 83.959  43.885  -19.793 1.00 6.21  ? 215  TYR D CG  1 
ATOM   9570  C  CD1 . TYR D  1 215 ? 83.514  44.108  -21.078 1.00 7.25  ? 215  TYR D CD1 1 
ATOM   9571  C  CD2 . TYR D  1 215 ? 83.183  43.104  -18.952 1.00 6.36  ? 215  TYR D CD2 1 
ATOM   9572  C  CE1 . TYR D  1 215 ? 82.343  43.543  -21.543 1.00 8.57  ? 215  TYR D CE1 1 
ATOM   9573  C  CE2 . TYR D  1 215 ? 81.982  42.556  -19.388 1.00 10.00 ? 215  TYR D CE2 1 
ATOM   9574  C  CZ  . TYR D  1 215 ? 81.568  42.794  -20.681 1.00 9.49  ? 215  TYR D CZ  1 
ATOM   9575  O  OH  . TYR D  1 215 ? 80.379  42.306  -21.142 1.00 8.98  ? 215  TYR D OH  1 
ATOM   9576  N  N   . PHE D  1 216 ? 86.889  42.508  -17.646 1.00 8.25  ? 216  PHE D N   1 
ATOM   9577  C  CA  . PHE D  1 216 ? 86.991  41.331  -16.795 1.00 7.93  ? 216  PHE D CA  1 
ATOM   9578  C  C   . PHE D  1 216 ? 86.163  41.474  -15.507 1.00 8.33  ? 216  PHE D C   1 
ATOM   9579  O  O   . PHE D  1 216 ? 86.016  42.591  -14.961 1.00 9.82  ? 216  PHE D O   1 
ATOM   9580  C  CB  . PHE D  1 216 ? 88.459  41.102  -16.448 1.00 7.89  ? 216  PHE D CB  1 
ATOM   9581  C  CG  . PHE D  1 216 ? 89.350  41.191  -17.623 1.00 7.03  ? 216  PHE D CG  1 
ATOM   9582  C  CD1 . PHE D  1 216 ? 89.688  42.438  -18.159 1.00 6.20  ? 216  PHE D CD1 1 
ATOM   9583  C  CD2 . PHE D  1 216 ? 89.827  40.036  -18.230 1.00 4.80  ? 216  PHE D CD2 1 
ATOM   9584  C  CE1 . PHE D  1 216 ? 90.517  42.511  -19.257 1.00 7.42  ? 216  PHE D CE1 1 
ATOM   9585  C  CE2 . PHE D  1 216 ? 90.648  40.126  -19.362 1.00 5.25  ? 216  PHE D CE2 1 
ATOM   9586  C  CZ  . PHE D  1 216 ? 90.978  41.343  -19.871 1.00 8.15  ? 216  PHE D CZ  1 
ATOM   9587  N  N   . ILE D  1 217 ? 85.606  40.364  -15.058 1.00 7.95  ? 217  ILE D N   1 
ATOM   9588  C  CA  . ILE D  1 217 ? 84.839  40.348  -13.802 1.00 8.09  ? 217  ILE D CA  1 
ATOM   9589  C  C   . ILE D  1 217 ? 85.312  39.216  -12.908 1.00 7.98  ? 217  ILE D C   1 
ATOM   9590  O  O   . ILE D  1 217 ? 85.180  38.022  -13.264 1.00 8.62  ? 217  ILE D O   1 
ATOM   9591  C  CB  . ILE D  1 217 ? 83.334  40.253  -14.079 1.00 7.71  ? 217  ILE D CB  1 
ATOM   9592  C  CG1 . ILE D  1 217 ? 82.888  41.499  -14.892 1.00 9.86  ? 217  ILE D CG1 1 
ATOM   9593  C  CG2 . ILE D  1 217 ? 82.552  40.191  -12.729 1.00 6.38  ? 217  ILE D CG2 1 
ATOM   9594  C  CD1 . ILE D  1 217 ? 81.522  41.326  -15.528 1.00 16.49 ? 217  ILE D CD1 1 
ATOM   9595  N  N   . ALA D  1 218 ? 85.866  39.580  -11.750 1.00 8.24  ? 218  ALA D N   1 
ATOM   9596  C  CA  . ALA D  1 218 ? 86.403  38.574  -10.828 1.00 8.33  ? 218  ALA D CA  1 
ATOM   9597  C  C   . ALA D  1 218 ? 85.212  37.938  -10.069 1.00 8.87  ? 218  ALA D C   1 
ATOM   9598  O  O   . ALA D  1 218 ? 84.179  38.594  -9.856  1.00 7.81  ? 218  ALA D O   1 
ATOM   9599  C  CB  . ALA D  1 218 ? 87.386  39.194  -9.873  1.00 9.19  ? 218  ALA D CB  1 
ATOM   9600  N  N   . ASN D  1 219 ? 85.342  36.654  -9.708  1.00 8.32  ? 219  ASN D N   1 
ATOM   9601  C  CA  . ASN D  1 219 ? 84.265  35.910  -9.057  1.00 9.11  ? 219  ASN D CA  1 
ATOM   9602  C  C   . ASN D  1 219 ? 83.632  36.628  -7.862  1.00 8.41  ? 219  ASN D C   1 
ATOM   9603  O  O   . ASN D  1 219 ? 84.268  36.835  -6.849  1.00 9.00  ? 219  ASN D O   1 
ATOM   9604  C  CB  . ASN D  1 219 ? 84.800  34.500  -8.646  1.00 9.18  ? 219  ASN D CB  1 
ATOM   9605  C  CG  . ASN D  1 219 ? 83.713  33.563  -8.206  1.00 11.94 ? 219  ASN D CG  1 
ATOM   9606  O  OD1 . ASN D  1 219 ? 82.533  33.760  -8.498  1.00 14.76 ? 219  ASN D OD1 1 
ATOM   9607  N  ND2 . ASN D  1 219 ? 84.107  32.516  -7.505  1.00 15.27 ? 219  ASN D ND2 1 
ATOM   9608  N  N   . GLY D  1 220 ? 82.378  37.042  -7.997  1.00 8.83  ? 220  GLY D N   1 
ATOM   9609  C  CA  . GLY D  1 220 ? 81.667  37.608  -6.878  1.00 8.17  ? 220  GLY D CA  1 
ATOM   9610  C  C   . GLY D  1 220 ? 81.687  39.118  -6.853  1.00 7.56  ? 220  GLY D C   1 
ATOM   9611  O  O   . GLY D  1 220 ? 81.017  39.696  -6.012  1.00 7.91  ? 220  GLY D O   1 
ATOM   9612  N  N   . TRP D  1 221 ? 82.482  39.729  -7.731  1.00 8.34  ? 221  TRP D N   1 
ATOM   9613  C  CA  . TRP D  1 221 ? 82.810  41.182  -7.623  1.00 7.18  ? 221  TRP D CA  1 
ATOM   9614  C  C   . TRP D  1 221 ? 82.071  42.106  -8.590  1.00 7.77  ? 221  TRP D C   1 
ATOM   9615  O  O   . TRP D  1 221 ? 82.262  43.382  -8.546  1.00 6.72  ? 221  TRP D O   1 
ATOM   9616  C  CB  . TRP D  1 221 ? 84.300  41.409  -7.820  1.00 8.11  ? 221  TRP D CB  1 
ATOM   9617  C  CG  . TRP D  1 221 ? 85.212  40.942  -6.652  1.00 8.54  ? 221  TRP D CG  1 
ATOM   9618  C  CD1 . TRP D  1 221 ? 86.011  39.805  -6.604  1.00 10.83 ? 221  TRP D CD1 1 
ATOM   9619  C  CD2 . TRP D  1 221 ? 85.416  41.612  -5.414  1.00 9.08  ? 221  TRP D CD2 1 
ATOM   9620  N  NE1 . TRP D  1 221 ? 86.679  39.734  -5.406  1.00 8.32  ? 221  TRP D NE1 1 
ATOM   9621  C  CE2 . TRP D  1 221 ? 86.339  40.843  -4.659  1.00 8.12  ? 221  TRP D CE2 1 
ATOM   9622  C  CE3 . TRP D  1 221 ? 84.895  42.793  -4.841  1.00 5.15  ? 221  TRP D CE3 1 
ATOM   9623  C  CZ2 . TRP D  1 221 ? 86.751  41.225  -3.391  1.00 11.03 ? 221  TRP D CZ2 1 
ATOM   9624  C  CZ3 . TRP D  1 221 ? 85.297  43.163  -3.581  1.00 6.16  ? 221  TRP D CZ3 1 
ATOM   9625  C  CH2 . TRP D  1 221 ? 86.224  42.402  -2.863  1.00 6.40  ? 221  TRP D CH2 1 
ATOM   9626  N  N   . GLY D  1 222 ? 81.255  41.507  -9.474  1.00 6.95  ? 222  GLY D N   1 
ATOM   9627  C  CA  . GLY D  1 222 ? 80.522  42.261  -10.473 1.00 7.05  ? 222  GLY D CA  1 
ATOM   9628  C  C   . GLY D  1 222 ? 79.148  42.631  -9.938  1.00 8.02  ? 222  GLY D C   1 
ATOM   9629  O  O   . GLY D  1 222 ? 78.849  42.343  -8.778  1.00 8.10  ? 222  GLY D O   1 
ATOM   9630  N  N   . PRO D  1 223 ? 78.336  43.324  -10.733 1.00 8.90  ? 223  PRO D N   1 
ATOM   9631  C  CA  . PRO D  1 223 ? 76.999  43.736  -10.266 1.00 8.84  ? 223  PRO D CA  1 
ATOM   9632  C  C   . PRO D  1 223 ? 76.110  42.479  -10.129 1.00 8.09  ? 223  PRO D C   1 
ATOM   9633  O  O   . PRO D  1 223 ? 76.303  41.520  -10.875 1.00 8.78  ? 223  PRO D O   1 
ATOM   9634  C  CB  . PRO D  1 223 ? 76.518  44.708  -11.395 1.00 8.58  ? 223  PRO D CB  1 
ATOM   9635  C  CG  . PRO D  1 223 ? 77.237  44.201  -12.619 1.00 11.19 ? 223  PRO D CG  1 
ATOM   9636  C  CD  . PRO D  1 223 ? 78.600  43.752  -12.123 1.00 8.24  ? 223  PRO D CD  1 
ATOM   9637  N  N   . LYS D  1 224 ? 75.191  42.473  -9.171  1.00 8.87  ? 224  LYS D N   1 
ATOM   9638  C  CA  . LYS D  1 224 ? 74.337  41.312  -8.875  1.00 8.41  ? 224  LYS D CA  1 
ATOM   9639  C  C   . LYS D  1 224 ? 72.918  41.800  -8.625  1.00 8.99  ? 224  LYS D C   1 
ATOM   9640  O  O   . LYS D  1 224 ? 72.701  42.952  -8.265  1.00 8.59  ? 224  LYS D O   1 
ATOM   9641  C  CB  . LYS D  1 224 ? 74.840  40.590  -7.624  1.00 8.96  ? 224  LYS D CB  1 
ATOM   9642  C  CG  . LYS D  1 224 ? 76.219  39.904  -7.766  1.00 8.70  ? 224  LYS D CG  1 
ATOM   9643  C  CD  . LYS D  1 224 ? 76.689  39.435  -6.383  1.00 9.55  ? 224  LYS D CD  1 
ATOM   9644  C  CE  . LYS D  1 224 ? 77.316  40.599  -5.595  1.00 10.85 ? 224  LYS D CE  1 
ATOM   9645  N  NZ  . LYS D  1 224 ? 78.546  40.973  -6.373  1.00 12.56 ? 224  LYS D NZ  1 
ATOM   9646  N  N   . TYR D  1 225 ? 71.935  40.951  -8.890  1.00 9.72  ? 225  TYR D N   1 
ATOM   9647  C  CA  . TYR D  1 225 ? 70.518  41.357  -8.784  1.00 9.34  ? 225  TYR D CA  1 
ATOM   9648  C  C   . TYR D  1 225 ? 69.873  40.204  -8.082  1.00 9.48  ? 225  TYR D C   1 
ATOM   9649  O  O   . TYR D  1 225 ? 70.097  39.056  -8.504  1.00 8.17  ? 225  TYR D O   1 
ATOM   9650  C  CB  . TYR D  1 225 ? 69.867  41.603  -10.171 1.00 10.39 ? 225  TYR D CB  1 
ATOM   9651  C  CG  . TYR D  1 225 ? 70.514  42.764  -10.875 1.00 11.69 ? 225  TYR D CG  1 
ATOM   9652  C  CD1 . TYR D  1 225 ? 71.684  42.576  -11.625 1.00 14.71 ? 225  TYR D CD1 1 
ATOM   9653  C  CD2 . TYR D  1 225 ? 70.022  44.076  -10.706 1.00 14.09 ? 225  TYR D CD2 1 
ATOM   9654  C  CE1 . TYR D  1 225 ? 72.331  43.662  -12.213 1.00 16.98 ? 225  TYR D CE1 1 
ATOM   9655  C  CE2 . TYR D  1 225 ? 70.659  45.171  -11.299 1.00 16.94 ? 225  TYR D CE2 1 
ATOM   9656  C  CZ  . TYR D  1 225 ? 71.814  44.942  -12.054 1.00 19.39 ? 225  TYR D CZ  1 
ATOM   9657  O  OH  . TYR D  1 225 ? 72.461  45.991  -12.638 1.00 22.27 ? 225  TYR D OH  1 
ATOM   9658  N  N   . LEU D  1 226 ? 69.124  40.508  -7.015  1.00 7.75  ? 226  LEU D N   1 
ATOM   9659  C  CA  . LEU D  1 226 ? 68.329  39.493  -6.337  1.00 8.05  ? 226  LEU D CA  1 
ATOM   9660  C  C   . LEU D  1 226 ? 66.916  39.418  -6.931  1.00 7.43  ? 226  LEU D C   1 
ATOM   9661  O  O   . LEU D  1 226 ? 66.211  40.397  -6.949  1.00 8.48  ? 226  LEU D O   1 
ATOM   9662  C  CB  . LEU D  1 226 ? 68.231  39.792  -4.831  1.00 6.49  ? 226  LEU D CB  1 
ATOM   9663  C  CG  . LEU D  1 226 ? 67.440  38.737  -4.034  1.00 5.76  ? 226  LEU D CG  1 
ATOM   9664  C  CD1 . LEU D  1 226 ? 68.276  37.422  -3.977  1.00 5.96  ? 226  LEU D CD1 1 
ATOM   9665  C  CD2 . LEU D  1 226 ? 67.151  39.277  -2.638  1.00 5.81  ? 226  LEU D CD2 1 
ATOM   9666  N  N   . ASN D  1 227 ? 66.516  38.252  -7.385  1.00 6.48  ? 227  ASN D N   1 
ATOM   9667  C  CA  . ASN D  1 227 ? 65.149  38.001  -7.764  1.00 7.24  ? 227  ASN D CA  1 
ATOM   9668  C  C   . ASN D  1 227 ? 64.495  37.090  -6.707  1.00 6.87  ? 227  ASN D C   1 
ATOM   9669  O  O   . ASN D  1 227 ? 65.038  36.036  -6.363  1.00 6.05  ? 227  ASN D O   1 
ATOM   9670  C  CB  . ASN D  1 227 ? 65.064  37.375  -9.169  1.00 6.15  ? 227  ASN D CB  1 
ATOM   9671  C  CG  . ASN D  1 227 ? 63.612  37.140  -9.597  1.00 8.45  ? 227  ASN D CG  1 
ATOM   9672  O  OD1 . ASN D  1 227 ? 62.956  36.228  -9.099  1.00 9.76  ? 227  ASN D OD1 1 
ATOM   9673  N  ND2 . ASN D  1 227 ? 63.097  37.987  -10.497 1.00 3.30  ? 227  ASN D ND2 1 
ATOM   9674  N  N   . SER D  1 228 ? 63.383  37.544  -6.165  1.00 6.16  ? 228  SER D N   1 
ATOM   9675  C  CA  . SER D  1 228 ? 62.685  36.878  -5.063  1.00 7.99  ? 228  SER D CA  1 
ATOM   9676  C  C   . SER D  1 228 ? 61.340  36.258  -5.488  1.00 7.73  ? 228  SER D C   1 
ATOM   9677  O  O   . SER D  1 228 ? 60.499  35.945  -4.627  1.00 7.33  ? 228  SER D O   1 
ATOM   9678  C  CB  . SER D  1 228 ? 62.415  37.889  -3.925  1.00 8.79  ? 228  SER D CB  1 
ATOM   9679  O  OG  . SER D  1 228 ? 63.660  38.419  -3.483  1.00 14.95 ? 228  SER D OG  1 
ATOM   9680  N  N   . GLN D  1 229 ? 61.116  36.111  -6.788  1.00 7.47  ? 229  GLN D N   1 
ATOM   9681  C  CA  . GLN D  1 229 ? 59.787  35.704  -7.281  1.00 8.63  ? 229  GLN D CA  1 
ATOM   9682  C  C   . GLN D  1 229 ? 59.532  34.194  -7.184  1.00 8.87  ? 229  GLN D C   1 
ATOM   9683  O  O   . GLN D  1 229 ? 58.382  33.737  -7.036  1.00 7.36  ? 229  GLN D O   1 
ATOM   9684  C  CB  . GLN D  1 229 ? 59.648  36.120  -8.745  1.00 10.23 ? 229  GLN D CB  1 
ATOM   9685  C  CG  . GLN D  1 229 ? 59.754  37.639  -8.975  1.00 10.02 ? 229  GLN D CG  1 
ATOM   9686  C  CD  . GLN D  1 229 ? 59.558  37.972  -10.435 1.00 12.08 ? 229  GLN D CD  1 
ATOM   9687  O  OE1 . GLN D  1 229 ? 60.519  38.097  -11.196 1.00 10.20 ? 229  GLN D OE1 1 
ATOM   9688  N  NE2 . GLN D  1 229 ? 58.309  38.092  -10.835 1.00 12.94 ? 229  GLN D NE2 1 
ATOM   9689  N  N   . TYR D  1 230 ? 60.595  33.403  -7.307  1.00 8.87  ? 230  TYR D N   1 
ATOM   9690  C  CA  . TYR D  1 230 ? 60.408  31.940  -7.304  1.00 8.92  ? 230  TYR D CA  1 
ATOM   9691  C  C   . TYR D  1 230 ? 61.425  31.275  -6.422  1.00 8.38  ? 230  TYR D C   1 
ATOM   9692  O  O   . TYR D  1 230 ? 62.199  30.434  -6.863  1.00 8.58  ? 230  TYR D O   1 
ATOM   9693  C  CB  . TYR D  1 230 ? 60.432  31.365  -8.720  1.00 9.58  ? 230  TYR D CB  1 
ATOM   9694  C  CG  . TYR D  1 230 ? 59.790  32.264  -9.767  1.00 10.92 ? 230  TYR D CG  1 
ATOM   9695  C  CD1 . TYR D  1 230 ? 58.440  32.219  -9.991  1.00 9.09  ? 230  TYR D CD1 1 
ATOM   9696  C  CD2 . TYR D  1 230 ? 60.556  33.144  -10.531 1.00 12.34 ? 230  TYR D CD2 1 
ATOM   9697  C  CE1 . TYR D  1 230 ? 57.858  33.013  -10.938 1.00 14.66 ? 230  TYR D CE1 1 
ATOM   9698  C  CE2 . TYR D  1 230 ? 59.968  33.958  -11.492 1.00 13.75 ? 230  TYR D CE2 1 
ATOM   9699  C  CZ  . TYR D  1 230 ? 58.628  33.886  -11.683 1.00 14.46 ? 230  TYR D CZ  1 
ATOM   9700  O  OH  . TYR D  1 230 ? 58.014  34.680  -12.633 1.00 17.80 ? 230  TYR D OH  1 
ATOM   9701  N  N   . GLY D  1 231 ? 61.424  31.668  -5.157  1.00 8.06  ? 231  GLY D N   1 
ATOM   9702  C  CA  . GLY D  1 231 ? 62.575  31.410  -4.316  1.00 7.56  ? 231  GLY D CA  1 
ATOM   9703  C  C   . GLY D  1 231 ? 63.567  32.502  -4.626  1.00 7.31  ? 231  GLY D C   1 
ATOM   9704  O  O   . GLY D  1 231 ? 63.212  33.564  -5.187  1.00 8.36  ? 231  GLY D O   1 
ATOM   9705  N  N   . TYR D  1 232 ? 64.803  32.308  -4.209  1.00 7.44  ? 232  TYR D N   1 
ATOM   9706  C  CA  . TYR D  1 232 ? 65.780  33.364  -4.375  1.00 6.64  ? 232  TYR D CA  1 
ATOM   9707  C  C   . TYR D  1 232 ? 66.738  33.003  -5.467  1.00 7.68  ? 232  TYR D C   1 
ATOM   9708  O  O   . TYR D  1 232 ? 67.260  31.878  -5.519  1.00 4.93  ? 232  TYR D O   1 
ATOM   9709  C  CB  . TYR D  1 232 ? 66.577  33.617  -3.089  1.00 7.17  ? 232  TYR D CB  1 
ATOM   9710  C  CG  . TYR D  1 232 ? 65.828  34.353  -2.001  1.00 6.86  ? 232  TYR D CG  1 
ATOM   9711  C  CD1 . TYR D  1 232 ? 65.159  35.552  -2.260  1.00 7.82  ? 232  TYR D CD1 1 
ATOM   9712  C  CD2 . TYR D  1 232 ? 65.849  33.877  -0.706  1.00 7.00  ? 232  TYR D CD2 1 
ATOM   9713  C  CE1 . TYR D  1 232 ? 64.503  36.241  -1.247  1.00 5.93  ? 232  TYR D CE1 1 
ATOM   9714  C  CE2 . TYR D  1 232 ? 65.209  34.544  0.308   1.00 7.90  ? 232  TYR D CE2 1 
ATOM   9715  C  CZ  . TYR D  1 232 ? 64.524  35.727  0.024   1.00 7.00  ? 232  TYR D CZ  1 
ATOM   9716  O  OH  . TYR D  1 232 ? 63.908  36.384  1.057   1.00 4.52  ? 232  TYR D OH  1 
ATOM   9717  N  N   . GLN D  1 233 ? 66.983  33.974  -6.349  1.00 7.18  ? 233  GLN D N   1 
ATOM   9718  C  CA  . GLN D  1 233 ? 67.975  33.771  -7.392  1.00 8.01  ? 233  GLN D CA  1 
ATOM   9719  C  C   . GLN D  1 233 ? 68.777  35.043  -7.558  1.00 8.10  ? 233  GLN D C   1 
ATOM   9720  O  O   . GLN D  1 233 ? 68.212  36.155  -7.545  1.00 7.60  ? 233  GLN D O   1 
ATOM   9721  C  CB  . GLN D  1 233 ? 67.294  33.389  -8.731  1.00 9.08  ? 233  GLN D CB  1 
ATOM   9722  C  CG  . GLN D  1 233 ? 66.560  32.017  -8.692  1.00 7.15  ? 233  GLN D CG  1 
ATOM   9723  C  CD  . GLN D  1 233 ? 65.827  31.675  -9.953  1.00 7.13  ? 233  GLN D CD  1 
ATOM   9724  O  OE1 . GLN D  1 233 ? 64.593  31.960  -10.103 1.00 8.05  ? 233  GLN D OE1 1 
ATOM   9725  N  NE2 . GLN D  1 233 ? 66.535  31.104  -10.876 1.00 4.45  ? 233  GLN D NE2 1 
ATOM   9726  N  N   . ILE D  1 234 ? 70.098  34.877  -7.631  1.00 7.63  ? 234  ILE D N   1 
ATOM   9727  C  CA  . ILE D  1 234 ? 70.983  36.025  -7.826  1.00 8.37  ? 234  ILE D CA  1 
ATOM   9728  C  C   . ILE D  1 234 ? 71.595  35.912  -9.198  1.00 8.53  ? 234  ILE D C   1 
ATOM   9729  O  O   . ILE D  1 234 ? 72.328  34.941  -9.491  1.00 10.52 ? 234  ILE D O   1 
ATOM   9730  C  CB  . ILE D  1 234 ? 72.093  36.089  -6.763  1.00 7.28  ? 234  ILE D CB  1 
ATOM   9731  C  CG1 . ILE D  1 234 ? 71.461  36.081  -5.362  1.00 6.87  ? 234  ILE D CG1 1 
ATOM   9732  C  CG2 . ILE D  1 234 ? 73.015  37.342  -7.014  1.00 8.03  ? 234  ILE D CG2 1 
ATOM   9733  C  CD1 . ILE D  1 234 ? 72.461  35.757  -4.131  1.00 4.71  ? 234  ILE D CD1 1 
ATOM   9734  N  N   . VAL D  1 235 ? 71.315  36.917  -10.036 1.00 8.86  ? 235  VAL D N   1 
ATOM   9735  C  CA  . VAL D  1 235 ? 71.916  36.947  -11.365 1.00 8.83  ? 235  VAL D CA  1 
ATOM   9736  C  C   . VAL D  1 235 ? 73.144  37.838  -11.334 1.00 9.10  ? 235  VAL D C   1 
ATOM   9737  O  O   . VAL D  1 235 ? 73.046  38.965  -10.826 1.00 8.95  ? 235  VAL D O   1 
ATOM   9738  C  CB  . VAL D  1 235 ? 70.939  37.532  -12.373 1.00 9.69  ? 235  VAL D CB  1 
ATOM   9739  C  CG1 . VAL D  1 235 ? 71.640  37.557  -13.802 1.00 7.81  ? 235  VAL D CG1 1 
ATOM   9740  C  CG2 . VAL D  1 235 ? 69.636  36.685  -12.363 1.00 6.24  ? 235  VAL D CG2 1 
ATOM   9741  N  N   . ALA D  1 236 ? 74.282  37.334  -11.839 1.00 9.29  ? 236  ALA D N   1 
ATOM   9742  C  CA  . ALA D  1 236 ? 75.479  38.185  -11.982 1.00 9.49  ? 236  ALA D CA  1 
ATOM   9743  C  C   . ALA D  1 236 ? 75.749  38.382  -13.474 1.00 8.71  ? 236  ALA D C   1 
ATOM   9744  O  O   . ALA D  1 236 ? 76.305  37.483  -14.116 1.00 8.13  ? 236  ALA D O   1 
ATOM   9745  C  CB  . ALA D  1 236 ? 76.673  37.552  -11.288 1.00 8.24  ? 236  ALA D CB  1 
ATOM   9746  N  N   . PRO D  1 237 ? 75.283  39.486  -14.050 1.00 8.50  ? 237  PRO D N   1 
ATOM   9747  C  CA  . PRO D  1 237 ? 75.439  39.702  -15.503 1.00 9.69  ? 237  PRO D CA  1 
ATOM   9748  C  C   . PRO D  1 237 ? 76.919  39.710  -15.928 1.00 9.77  ? 237  PRO D C   1 
ATOM   9749  O  O   . PRO D  1 237 ? 77.752  40.257  -15.206 1.00 10.17 ? 237  PRO D O   1 
ATOM   9750  C  CB  . PRO D  1 237 ? 74.773  41.072  -15.721 1.00 8.81  ? 237  PRO D CB  1 
ATOM   9751  C  CG  . PRO D  1 237 ? 73.739  41.159  -14.599 1.00 10.67 ? 237  PRO D CG  1 
ATOM   9752  C  CD  . PRO D  1 237 ? 74.495  40.569  -13.416 1.00 8.19  ? 237  PRO D CD  1 
ATOM   9753  N  N   . PHE D  1 238 ? 77.232  39.091  -17.067 1.00 9.13  ? 238  PHE D N   1 
ATOM   9754  C  CA  . PHE D  1 238 ? 78.560  39.175  -17.663 1.00 9.10  ? 238  PHE D CA  1 
ATOM   9755  C  C   . PHE D  1 238 ? 78.478  39.953  -18.995 1.00 9.69  ? 238  PHE D C   1 
ATOM   9756  O  O   . PHE D  1 238 ? 79.399  40.728  -19.311 1.00 8.69  ? 238  PHE D O   1 
ATOM   9757  C  CB  . PHE D  1 238 ? 79.143  37.788  -17.980 1.00 8.77  ? 238  PHE D CB  1 
ATOM   9758  C  CG  . PHE D  1 238 ? 79.569  36.991  -16.764 1.00 9.79  ? 238  PHE D CG  1 
ATOM   9759  C  CD1 . PHE D  1 238 ? 79.878  37.619  -15.554 1.00 12.87 ? 238  PHE D CD1 1 
ATOM   9760  C  CD2 . PHE D  1 238 ? 79.663  35.611  -16.824 1.00 10.85 ? 238  PHE D CD2 1 
ATOM   9761  C  CE1 . PHE D  1 238 ? 80.281  36.874  -14.425 1.00 10.87 ? 238  PHE D CE1 1 
ATOM   9762  C  CE2 . PHE D  1 238 ? 80.069  34.836  -15.678 1.00 10.02 ? 238  PHE D CE2 1 
ATOM   9763  C  CZ  . PHE D  1 238 ? 80.388  35.497  -14.479 1.00 13.23 ? 238  PHE D CZ  1 
ATOM   9764  N  N   . VAL D  1 239 ? 77.417  39.691  -19.769 1.00 7.94  ? 239  VAL D N   1 
ATOM   9765  C  CA  . VAL D  1 239 ? 77.147  40.407  -21.059 1.00 8.84  ? 239  VAL D CA  1 
ATOM   9766  C  C   . VAL D  1 239 ? 75.662  40.792  -21.091 1.00 8.63  ? 239  VAL D C   1 
ATOM   9767  O  O   . VAL D  1 239 ? 74.800  39.946  -20.840 1.00 8.54  ? 239  VAL D O   1 
ATOM   9768  C  CB  . VAL D  1 239 ? 77.442  39.513  -22.310 1.00 8.94  ? 239  VAL D CB  1 
ATOM   9769  C  CG1 . VAL D  1 239 ? 76.959  40.220  -23.662 1.00 7.66  ? 239  VAL D CG1 1 
ATOM   9770  C  CG2 . VAL D  1 239 ? 78.934  39.093  -22.381 1.00 9.32  ? 239  VAL D CG2 1 
ATOM   9771  N  N   . THR D  1 240 ? 75.363  42.056  -21.395 1.00 8.39  ? 240  THR D N   1 
ATOM   9772  C  CA  . THR D  1 240 ? 73.987  42.479  -21.612 1.00 8.21  ? 240  THR D CA  1 
ATOM   9773  C  C   . THR D  1 240 ? 73.869  43.061  -23.022 1.00 8.47  ? 240  THR D C   1 
ATOM   9774  O  O   . THR D  1 240 ? 74.867  43.060  -23.757 1.00 8.02  ? 240  THR D O   1 
ATOM   9775  C  CB  . THR D  1 240 ? 73.570  43.544  -20.583 1.00 8.52  ? 240  THR D CB  1 
ATOM   9776  O  OG1 . THR D  1 240 ? 74.332  44.744  -20.801 1.00 6.04  ? 240  THR D OG1 1 
ATOM   9777  C  CG2 . THR D  1 240 ? 73.932  43.083  -19.140 1.00 6.71  ? 240  THR D CG2 1 
ATOM   9778  N  N   . ALA D  1 241 ? 72.694  43.588  -23.391 1.00 8.00  ? 241  ALA D N   1 
ATOM   9779  C  CA  . ALA D  1 241 ? 72.553  44.209  -24.724 1.00 8.57  ? 241  ALA D CA  1 
ATOM   9780  C  C   . ALA D  1 241 ? 73.603  45.326  -24.953 1.00 8.52  ? 241  ALA D C   1 
ATOM   9781  O  O   . ALA D  1 241 ? 74.083  45.524  -26.075 1.00 9.04  ? 241  ALA D O   1 
ATOM   9782  C  CB  . ALA D  1 241 ? 71.096  44.778  -24.980 1.00 7.62  ? 241  ALA D CB  1 
ATOM   9783  N  N   . THR D  1 242 ? 73.926  46.076  -23.894 1.00 8.15  ? 242  THR D N   1 
ATOM   9784  C  CA  . THR D  1 242 ? 74.926  47.134  -24.011 1.00 8.03  ? 242  THR D CA  1 
ATOM   9785  C  C   . THR D  1 242 ? 76.224  46.607  -24.689 1.00 8.11  ? 242  THR D C   1 
ATOM   9786  O  O   . THR D  1 242 ? 76.729  47.213  -25.638 1.00 8.21  ? 242  THR D O   1 
ATOM   9787  C  CB  . THR D  1 242 ? 75.216  47.734  -22.630 1.00 8.36  ? 242  THR D CB  1 
ATOM   9788  O  OG1 . THR D  1 242 ? 74.050  48.442  -22.163 1.00 10.29 ? 242  THR D OG1 1 
ATOM   9789  C  CG2 . THR D  1 242 ? 76.314  48.832  -22.744 1.00 5.46  ? 242  THR D CG2 1 
ATOM   9790  N  N   . GLN D  1 243 ? 76.741  45.483  -24.222 1.00 7.09  ? 243  GLN D N   1 
ATOM   9791  C  CA  . GLN D  1 243 ? 77.975  44.908  -24.776 1.00 7.23  ? 243  GLN D CA  1 
ATOM   9792  C  C   . GLN D  1 243 ? 77.762  44.014  -26.029 1.00 8.24  ? 243  GLN D C   1 
ATOM   9793  O  O   . GLN D  1 243 ? 78.595  44.059  -26.969 1.00 8.86  ? 243  GLN D O   1 
ATOM   9794  C  CB  . GLN D  1 243 ? 78.736  44.118  -23.670 1.00 6.96  ? 243  GLN D CB  1 
ATOM   9795  C  CG  . GLN D  1 243 ? 79.091  45.042  -22.434 1.00 6.96  ? 243  GLN D CG  1 
ATOM   9796  C  CD  . GLN D  1 243 ? 77.913  45.218  -21.483 1.00 9.56  ? 243  GLN D CD  1 
ATOM   9797  O  OE1 . GLN D  1 243 ? 77.005  44.345  -21.421 1.00 9.09  ? 243  GLN D OE1 1 
ATOM   9798  N  NE2 . GLN D  1 243 ? 77.908  46.344  -20.737 1.00 7.71  ? 243  GLN D NE2 1 
ATOM   9799  N  N   . ALA D  1 244 ? 76.680  43.217  -26.035 1.00 7.47  ? 244  ALA D N   1 
ATOM   9800  C  CA  . ALA D  1 244 ? 76.316  42.319  -27.167 1.00 7.54  ? 244  ALA D CA  1 
ATOM   9801  C  C   . ALA D  1 244 ? 75.984  43.062  -28.469 1.00 8.60  ? 244  ALA D C   1 
ATOM   9802  O  O   . ALA D  1 244 ? 76.326  42.603  -29.576 1.00 9.44  ? 244  ALA D O   1 
ATOM   9803  C  CB  . ALA D  1 244 ? 75.123  41.389  -26.772 1.00 6.76  ? 244  ALA D CB  1 
ATOM   9804  N  N   . GLN D  1 245 ? 75.296  44.193  -28.349 1.00 8.80  ? 245  GLN D N   1 
ATOM   9805  C  CA  . GLN D  1 245 ? 74.798  44.926  -29.530 1.00 9.13  ? 245  GLN D CA  1 
ATOM   9806  C  C   . GLN D  1 245 ? 74.163  43.936  -30.483 1.00 9.35  ? 245  GLN D C   1 
ATOM   9807  O  O   . GLN D  1 245 ? 73.376  43.085  -30.051 1.00 9.09  ? 245  GLN D O   1 
ATOM   9808  C  CB  . GLN D  1 245 ? 75.915  45.700  -30.202 1.00 9.66  ? 245  GLN D CB  1 
ATOM   9809  C  CG  . GLN D  1 245 ? 76.527  46.698  -29.258 1.00 13.15 ? 245  GLN D CG  1 
ATOM   9810  C  CD  . GLN D  1 245 ? 77.709  47.417  -29.881 1.00 19.69 ? 245  GLN D CD  1 
ATOM   9811  O  OE1 . GLN D  1 245 ? 78.795  46.816  -30.075 1.00 20.29 ? 245  GLN D OE1 1 
ATOM   9812  N  NE2 . GLN D  1 245 ? 77.522  48.705  -30.187 1.00 17.78 ? 245  GLN D NE2 1 
ATOM   9813  N  N   . ASP D  1 246 ? 74.540  43.978  -31.754 1.00 8.42  ? 246  ASP D N   1 
ATOM   9814  C  CA  . ASP D  1 246 ? 73.863  43.121  -32.718 1.00 9.56  ? 246  ASP D CA  1 
ATOM   9815  C  C   . ASP D  1 246 ? 74.147  41.614  -32.562 1.00 9.09  ? 246  ASP D C   1 
ATOM   9816  O  O   . ASP D  1 246 ? 73.434  40.801  -33.158 1.00 8.40  ? 246  ASP D O   1 
ATOM   9817  C  CB  . ASP D  1 246 ? 74.213  43.577  -34.123 1.00 9.16  ? 246  ASP D CB  1 
ATOM   9818  C  CG  . ASP D  1 246 ? 75.695  43.694  -34.294 1.00 12.14 ? 246  ASP D CG  1 
ATOM   9819  O  OD1 . ASP D  1 246 ? 76.332  44.520  -33.564 1.00 12.73 ? 246  ASP D OD1 1 
ATOM   9820  O  OD2 . ASP D  1 246 ? 76.305  42.978  -35.094 1.00 12.02 ? 246  ASP D OD2 1 
ATOM   9821  N  N   . THR D  1 247 ? 75.159  41.205  -31.785 1.00 8.34  ? 247  THR D N   1 
ATOM   9822  C  CA  . THR D  1 247 ? 75.276  39.764  -31.501 1.00 8.64  ? 247  THR D CA  1 
ATOM   9823  C  C   . THR D  1 247 ? 74.115  39.234  -30.630 1.00 9.29  ? 247  THR D C   1 
ATOM   9824  O  O   . THR D  1 247 ? 73.884  37.996  -30.555 1.00 7.71  ? 247  THR D O   1 
ATOM   9825  C  CB  . THR D  1 247 ? 76.655  39.340  -30.892 1.00 9.17  ? 247  THR D CB  1 
ATOM   9826  O  OG1 . THR D  1 247 ? 76.812  39.954  -29.602 1.00 10.02 ? 247  THR D OG1 1 
ATOM   9827  C  CG2 . THR D  1 247 ? 77.839  39.891  -31.700 1.00 9.46  ? 247  THR D CG2 1 
ATOM   9828  N  N   . ASN D  1 248 ? 73.388  40.143  -29.956 1.00 9.41  ? 248  ASN D N   1 
ATOM   9829  C  CA  . ASN D  1 248 ? 72.045  39.801  -29.482 1.00 9.73  ? 248  ASN D CA  1 
ATOM   9830  C  C   . ASN D  1 248 ? 72.014  38.567  -28.558 1.00 9.49  ? 248  ASN D C   1 
ATOM   9831  O  O   . ASN D  1 248 ? 71.405  37.538  -28.878 1.00 7.97  ? 248  ASN D O   1 
ATOM   9832  C  CB  . ASN D  1 248 ? 71.151  39.595  -30.733 1.00 10.38 ? 248  ASN D CB  1 
ATOM   9833  C  CG  . ASN D  1 248 ? 69.677  39.390  -30.411 1.00 15.76 ? 248  ASN D CG  1 
ATOM   9834  O  OD1 . ASN D  1 248 ? 69.177  39.896  -29.400 1.00 14.95 ? 248  ASN D OD1 1 
ATOM   9835  N  ND2 . ASN D  1 248 ? 68.971  38.625  -31.303 1.00 20.13 ? 248  ASN D ND2 1 
ATOM   9836  N  N   . TYR D  1 249 ? 72.694  38.644  -27.418 1.00 8.14  ? 249  TYR D N   1 
ATOM   9837  C  CA  . TYR D  1 249 ? 72.639  37.578  -26.439 1.00 7.87  ? 249  TYR D CA  1 
ATOM   9838  C  C   . TYR D  1 249 ? 72.887  38.175  -25.066 1.00 8.80  ? 249  TYR D C   1 
ATOM   9839  O  O   . TYR D  1 249 ? 73.239  39.361  -24.949 1.00 7.15  ? 249  TYR D O   1 
ATOM   9840  C  CB  . TYR D  1 249 ? 73.679  36.478  -26.740 1.00 7.10  ? 249  TYR D CB  1 
ATOM   9841  C  CG  . TYR D  1 249 ? 75.135  36.889  -26.486 1.00 5.93  ? 249  TYR D CG  1 
ATOM   9842  C  CD1 . TYR D  1 249 ? 75.812  37.751  -27.369 1.00 7.42  ? 249  TYR D CD1 1 
ATOM   9843  C  CD2 . TYR D  1 249 ? 75.827  36.383  -25.391 1.00 3.93  ? 249  TYR D CD2 1 
ATOM   9844  C  CE1 . TYR D  1 249 ? 77.165  38.074  -27.160 1.00 3.97  ? 249  TYR D CE1 1 
ATOM   9845  C  CE2 . TYR D  1 249 ? 77.150  36.715  -25.162 1.00 6.40  ? 249  TYR D CE2 1 
ATOM   9846  C  CZ  . TYR D  1 249 ? 77.791  37.590  -26.018 1.00 6.00  ? 249  TYR D CZ  1 
ATOM   9847  O  OH  . TYR D  1 249 ? 79.102  37.867  -25.778 1.00 5.93  ? 249  TYR D OH  1 
ATOM   9848  N  N   . THR D  1 250 ? 72.720  37.344  -24.035 1.00 8.85  ? 250  THR D N   1 
ATOM   9849  C  CA  . THR D  1 250 ? 73.134  37.700  -22.702 1.00 8.77  ? 250  THR D CA  1 
ATOM   9850  C  C   . THR D  1 250 ? 73.878  36.493  -22.119 1.00 9.46  ? 250  THR D C   1 
ATOM   9851  O  O   . THR D  1 250 ? 73.735  35.339  -22.574 1.00 8.88  ? 250  THR D O   1 
ATOM   9852  C  CB  . THR D  1 250 ? 71.914  38.025  -21.806 1.00 9.27  ? 250  THR D CB  1 
ATOM   9853  O  OG1 . THR D  1 250 ? 71.014  36.889  -21.832 1.00 8.99  ? 250  THR D OG1 1 
ATOM   9854  C  CG2 . THR D  1 250 ? 71.099  39.227  -22.345 1.00 7.05  ? 250  THR D CG2 1 
ATOM   9855  N  N   . LEU D  1 251 ? 74.670  36.786  -21.096 1.00 9.52  ? 251  LEU D N   1 
ATOM   9856  C  CA  . LEU D  1 251 ? 75.503  35.808  -20.452 1.00 8.33  ? 251  LEU D CA  1 
ATOM   9857  C  C   . LEU D  1 251 ? 75.588  36.264  -19.016 1.00 8.60  ? 251  LEU D C   1 
ATOM   9858  O  O   . LEU D  1 251 ? 75.750  37.455  -18.746 1.00 7.88  ? 251  LEU D O   1 
ATOM   9859  C  CB  . LEU D  1 251 ? 76.897  35.787  -21.108 1.00 6.22  ? 251  LEU D CB  1 
ATOM   9860  C  CG  . LEU D  1 251 ? 77.866  34.797  -20.510 1.00 8.15  ? 251  LEU D CG  1 
ATOM   9861  C  CD1 . LEU D  1 251 ? 77.372  33.449  -21.017 1.00 8.49  ? 251  LEU D CD1 1 
ATOM   9862  C  CD2 . LEU D  1 251 ? 79.335  35.076  -21.010 1.00 5.23  ? 251  LEU D CD2 1 
ATOM   9863  N  N   . SER D  1 252 ? 75.491  35.313  -18.089 1.00 8.80  ? 252  SER D N   1 
ATOM   9864  C  CA  . SER D  1 252 ? 75.545  35.627  -16.655 1.00 9.49  ? 252  SER D CA  1 
ATOM   9865  C  C   . SER D  1 252 ? 75.846  34.361  -15.838 1.00 9.21  ? 252  SER D C   1 
ATOM   9866  O  O   . SER D  1 252 ? 75.909  33.277  -16.412 1.00 9.28  ? 252  SER D O   1 
ATOM   9867  C  CB  . SER D  1 252 ? 74.219  36.161  -16.219 1.00 8.08  ? 252  SER D CB  1 
ATOM   9868  O  OG  . SER D  1 252 ? 73.249  35.168  -16.496 1.00 14.64 ? 252  SER D OG  1 
ATOM   9869  N  N   . THR D  1 253 ? 76.051  34.487  -14.514 1.00 9.89  ? 253  THR D N   1 
ATOM   9870  C  CA  . THR D  1 253 ? 75.779  33.335  -13.638 1.00 9.76  ? 253  THR D CA  1 
ATOM   9871  C  C   . THR D  1 253 ? 74.425  33.552  -12.957 1.00 9.81  ? 253  THR D C   1 
ATOM   9872  O  O   . THR D  1 253 ? 73.975  34.680  -12.820 1.00 8.57  ? 253  THR D O   1 
ATOM   9873  C  CB  . THR D  1 253 ? 76.842  33.085  -12.568 1.00 9.55  ? 253  THR D CB  1 
ATOM   9874  O  OG1 . THR D  1 253 ? 77.053  34.284  -11.807 1.00 12.40 ? 253  THR D OG1 1 
ATOM   9875  C  CG2 . THR D  1 253 ? 78.173  32.761  -13.230 1.00 10.23 ? 253  THR D CG2 1 
ATOM   9876  N  N   . ILE D  1 254 ? 73.774  32.444  -12.592 1.00 9.51  ? 254  ILE D N   1 
ATOM   9877  C  CA  . ILE D  1 254 ? 72.542  32.534  -11.835 1.00 9.05  ? 254  ILE D CA  1 
ATOM   9878  C  C   . ILE D  1 254 ? 72.784  31.597  -10.675 1.00 10.02 ? 254  ILE D C   1 
ATOM   9879  O  O   . ILE D  1 254 ? 73.120  30.413  -10.871 1.00 9.68  ? 254  ILE D O   1 
ATOM   9880  C  CB  . ILE D  1 254 ? 71.332  32.056  -12.615 1.00 8.21  ? 254  ILE D CB  1 
ATOM   9881  C  CG1 . ILE D  1 254 ? 71.123  32.946  -13.857 1.00 7.25  ? 254  ILE D CG1 1 
ATOM   9882  C  CG2 . ILE D  1 254 ? 70.087  32.052  -11.629 1.00 6.95  ? 254  ILE D CG2 1 
ATOM   9883  C  CD1 . ILE D  1 254 ? 69.998  32.410  -14.883 1.00 7.51  ? 254  ILE D CD1 1 
ATOM   9884  N  N   . SER D  1 255 ? 72.702  32.169  -9.473  1.00 9.20  ? 255  SER D N   1 
ATOM   9885  C  CA  . SER D  1 255 ? 72.850  31.397  -8.228  1.00 10.12 ? 255  SER D CA  1 
ATOM   9886  C  C   . SER D  1 255 ? 71.438  31.244  -7.688  1.00 9.70  ? 255  SER D C   1 
ATOM   9887  O  O   . SER D  1 255 ? 70.627  32.146  -7.911  1.00 9.71  ? 255  SER D O   1 
ATOM   9888  C  CB  . SER D  1 255 ? 73.699  32.169  -7.236  1.00 9.98  ? 255  SER D CB  1 
ATOM   9889  O  OG  . SER D  1 255 ? 75.007  32.438  -7.761  1.00 11.27 ? 255  SER D OG  1 
ATOM   9890  N  N   . MET D  1 256 ? 71.147  30.104  -7.056  1.00 10.12 ? 256  MET D N   1 
ATOM   9891  C  CA  . MET D  1 256 ? 69.756  29.705  -6.671  1.00 11.16 ? 256  MET D CA  1 
ATOM   9892  C  C   . MET D  1 256 ? 69.687  29.115  -5.285  1.00 9.93  ? 256  MET D C   1 
ATOM   9893  O  O   . MET D  1 256 ? 70.545  28.302  -4.931  1.00 10.42 ? 256  MET D O   1 
ATOM   9894  C  CB  . MET D  1 256 ? 69.194  28.642  -7.614  1.00 12.06 ? 256  MET D CB  1 
ATOM   9895  C  CG  . MET D  1 256 ? 69.498  28.899  -9.059  1.00 15.90 ? 256  MET D CG  1 
ATOM   9896  S  SD  . MET D  1 256 ? 69.172  27.363  -9.911  1.00 14.51 ? 256  MET D SD  1 
ATOM   9897  C  CE  . MET D  1 256 ? 69.872  27.877  -11.498 1.00 13.25 ? 256  MET D CE  1 
ATOM   9898  N  N   . SER D  1 257 ? 68.654  29.486  -4.525  1.00 7.57  ? 257  SER D N   1 
ATOM   9899  C  CA  . SER D  1 257 ? 68.268  28.750  -3.325  1.00 6.53  ? 257  SER D CA  1 
ATOM   9900  C  C   . SER D  1 257 ? 67.420  27.567  -3.787  1.00 6.61  ? 257  SER D C   1 
ATOM   9901  O  O   . SER D  1 257 ? 67.176  27.401  -4.996  1.00 7.15  ? 257  SER D O   1 
ATOM   9902  C  CB  . SER D  1 257 ? 67.396  29.636  -2.406  1.00 5.17  ? 257  SER D CB  1 
ATOM   9903  O  OG  . SER D  1 257 ? 66.172  29.907  -3.051  1.00 4.94  ? 257  SER D OG  1 
ATOM   9904  N  N   . THR D  1 258 ? 66.912  26.786  -2.843  1.00 6.59  ? 258  THR D N   1 
ATOM   9905  C  CA  . THR D  1 258 ? 65.885  25.827  -3.183  1.00 7.63  ? 258  THR D CA  1 
ATOM   9906  C  C   . THR D  1 258 ? 64.583  26.608  -3.415  1.00 7.91  ? 258  THR D C   1 
ATOM   9907  O  O   . THR D  1 258 ? 64.473  27.783  -3.062  1.00 8.06  ? 258  THR D O   1 
ATOM   9908  C  CB  . THR D  1 258 ? 65.659  24.823  -2.060  1.00 7.74  ? 258  THR D CB  1 
ATOM   9909  O  OG1 . THR D  1 258 ? 65.383  25.521  -0.835  1.00 5.73  ? 258  THR D OG1 1 
ATOM   9910  C  CG2 . THR D  1 258 ? 66.897  23.965  -1.817  1.00 9.37  ? 258  THR D CG2 1 
ATOM   9911  N  N   . THR D  1 259 ? 63.611  25.934  -3.985  1.00 8.98  ? 259  THR D N   1 
ATOM   9912  C  CA  . THR D  1 259 ? 62.290  26.507  -4.187  1.00 8.62  ? 259  THR D CA  1 
ATOM   9913  C  C   . THR D  1 259 ? 61.465  26.052  -2.997  1.00 10.04 ? 259  THR D C   1 
ATOM   9914  O  O   . THR D  1 259 ? 61.267  24.840  -2.840  1.00 10.04 ? 259  THR D O   1 
ATOM   9915  C  CB  . THR D  1 259 ? 61.641  25.928  -5.465  1.00 8.67  ? 259  THR D CB  1 
ATOM   9916  O  OG1 . THR D  1 259 ? 62.395  26.327  -6.616  1.00 7.98  ? 259  THR D OG1 1 
ATOM   9917  C  CG2 . THR D  1 259 ? 60.248  26.594  -5.702  1.00 6.50  ? 259  THR D CG2 1 
ATOM   9918  N  N   . PRO D  1 260 ? 60.916  26.976  -2.202  1.00 10.46 ? 260  PRO D N   1 
ATOM   9919  C  CA  . PRO D  1 260 ? 60.143  26.566  -1.026  1.00 11.40 ? 260  PRO D CA  1 
ATOM   9920  C  C   . PRO D  1 260 ? 58.897  25.849  -1.511  1.00 12.96 ? 260  PRO D C   1 
ATOM   9921  O  O   . PRO D  1 260 ? 58.517  26.081  -2.664  1.00 12.45 ? 260  PRO D O   1 
ATOM   9922  C  CB  . PRO D  1 260 ? 59.765  27.896  -0.377  1.00 12.40 ? 260  PRO D CB  1 
ATOM   9923  C  CG  . PRO D  1 260 ? 60.693  28.854  -0.902  1.00 11.47 ? 260  PRO D CG  1 
ATOM   9924  C  CD  . PRO D  1 260 ? 60.949  28.438  -2.348  1.00 10.49 ? 260  PRO D CD  1 
ATOM   9925  N  N   . SER D  1 261 ? 58.291  25.018  -0.655  1.00 13.91 ? 261  SER D N   1 
ATOM   9926  C  CA  . SER D  1 261 ? 57.179  24.142  -1.009  1.00 15.72 ? 261  SER D CA  1 
ATOM   9927  C  C   . SER D  1 261 ? 55.902  24.910  -1.292  1.00 15.75 ? 261  SER D C   1 
ATOM   9928  O  O   . SER D  1 261 ? 55.001  24.380  -1.936  1.00 16.74 ? 261  SER D O   1 
ATOM   9929  C  CB  . SER D  1 261 ? 56.883  23.156  0.118   1.00 15.71 ? 261  SER D CB  1 
ATOM   9930  O  OG  . SER D  1 261 ? 56.272  23.848  1.216   1.00 18.99 ? 261  SER D OG  1 
ATOM   9931  N  N   . THR D  1 262 ? 55.823  26.139  -0.804  1.00 15.53 ? 262  THR D N   1 
ATOM   9932  C  CA  . THR D  1 262 ? 54.675  26.983  -1.104  1.00 15.32 ? 262  THR D CA  1 
ATOM   9933  C  C   . THR D  1 262 ? 54.737  27.640  -2.480  1.00 14.33 ? 262  THR D C   1 
ATOM   9934  O  O   . THR D  1 262 ? 53.752  28.184  -2.930  1.00 14.45 ? 262  THR D O   1 
ATOM   9935  C  CB  . THR D  1 262 ? 54.516  28.083  -0.038  1.00 15.36 ? 262  THR D CB  1 
ATOM   9936  O  OG1 . THR D  1 262 ? 55.793  28.685  0.214   1.00 16.34 ? 262  THR D OG1 1 
ATOM   9937  C  CG2 . THR D  1 262 ? 54.100  27.479  1.302   1.00 17.58 ? 262  THR D CG2 1 
ATOM   9938  N  N   . VAL D  1 263 ? 55.895  27.620  -3.133  1.00 13.43 ? 263  VAL D N   1 
ATOM   9939  C  CA  . VAL D  1 263 ? 56.073  28.310  -4.412  1.00 12.83 ? 263  VAL D CA  1 
ATOM   9940  C  C   . VAL D  1 263 ? 56.025  27.265  -5.550  1.00 11.45 ? 263  VAL D C   1 
ATOM   9941  O  O   . VAL D  1 263 ? 56.668  26.229  -5.465  1.00 11.27 ? 263  VAL D O   1 
ATOM   9942  C  CB  . VAL D  1 263 ? 57.410  29.104  -4.395  1.00 13.39 ? 263  VAL D CB  1 
ATOM   9943  C  CG1 . VAL D  1 263 ? 57.783  29.622  -5.786  1.00 14.42 ? 263  VAL D CG1 1 
ATOM   9944  C  CG2 . VAL D  1 263 ? 57.342  30.247  -3.349  1.00 14.36 ? 263  VAL D CG2 1 
ATOM   9945  N  N   . THR D  1 264 ? 55.222  27.521  -6.574  1.00 11.24 ? 264  THR D N   1 
ATOM   9946  C  CA  . THR D  1 264 ? 55.209  26.698  -7.781  1.00 10.37 ? 264  THR D CA  1 
ATOM   9947  C  C   . THR D  1 264 ? 56.457  26.995  -8.621  1.00 10.47 ? 264  THR D C   1 
ATOM   9948  O  O   . THR D  1 264 ? 56.767  28.164  -8.883  1.00 10.46 ? 264  THR D O   1 
ATOM   9949  C  CB  . THR D  1 264 ? 53.972  26.997  -8.606  1.00 12.02 ? 264  THR D CB  1 
ATOM   9950  O  OG1 . THR D  1 264 ? 52.793  26.635  -7.857  1.00 11.91 ? 264  THR D OG1 1 
ATOM   9951  C  CG2 . THR D  1 264 ? 53.940  26.078  -9.834  1.00 11.12 ? 264  THR D CG2 1 
ATOM   9952  N  N   . VAL D  1 265 ? 57.173  25.945  -9.026  1.00 9.68  ? 265  VAL D N   1 
ATOM   9953  C  CA  . VAL D  1 265 ? 58.310  26.115  -9.926  1.00 9.49  ? 265  VAL D CA  1 
ATOM   9954  C  C   . VAL D  1 265 ? 57.681  26.620  -11.243 1.00 10.12 ? 265  VAL D C   1 
ATOM   9955  O  O   . VAL D  1 265 ? 56.750  26.007  -11.784 1.00 9.52  ? 265  VAL D O   1 
ATOM   9956  C  CB  . VAL D  1 265 ? 59.099  24.797  -10.120 1.00 9.44  ? 265  VAL D CB  1 
ATOM   9957  C  CG1 . VAL D  1 265 ? 60.153  24.944  -11.253 1.00 7.82  ? 265  VAL D CG1 1 
ATOM   9958  C  CG2 . VAL D  1 265 ? 59.728  24.331  -8.787  1.00 9.00  ? 265  VAL D CG2 1 
ATOM   9959  N  N   . PRO D  1 266 ? 58.142  27.764  -11.728 1.00 9.91  ? 266  PRO D N   1 
ATOM   9960  C  CA  . PRO D  1 266 ? 57.581  28.349  -12.954 1.00 10.05 ? 266  PRO D CA  1 
ATOM   9961  C  C   . PRO D  1 266 ? 57.962  27.563  -14.221 1.00 9.97  ? 266  PRO D C   1 
ATOM   9962  O  O   . PRO D  1 266 ? 58.956  26.802  -14.255 1.00 9.42  ? 266  PRO D O   1 
ATOM   9963  C  CB  . PRO D  1 266 ? 58.180  29.762  -12.975 1.00 9.82  ? 266  PRO D CB  1 
ATOM   9964  C  CG  . PRO D  1 266 ? 59.461  29.630  -12.189 1.00 11.72 ? 266  PRO D CG  1 
ATOM   9965  C  CD  . PRO D  1 266 ? 59.178  28.598  -11.106 1.00 10.46 ? 266  PRO D CD  1 
ATOM   9966  N  N   . THR D  1 267 ? 57.164  27.760  -15.248 1.00 9.17  ? 267  THR D N   1 
ATOM   9967  C  CA  . THR D  1 267 ? 57.469  27.251  -16.576 1.00 9.76  ? 267  THR D CA  1 
ATOM   9968  C  C   . THR D  1 267 ? 57.824  28.424  -17.461 1.00 9.76  ? 267  THR D C   1 
ATOM   9969  O  O   . THR D  1 267 ? 57.033  29.347  -17.601 1.00 9.68  ? 267  THR D O   1 
ATOM   9970  C  CB  . THR D  1 267 ? 56.255  26.542  -17.161 1.00 10.50 ? 267  THR D CB  1 
ATOM   9971  O  OG1 . THR D  1 267 ? 55.958  25.386  -16.366 1.00 9.73  ? 267  THR D OG1 1 
ATOM   9972  C  CG2 . THR D  1 267 ? 56.584  26.001  -18.544 1.00 10.66 ? 267  THR D CG2 1 
ATOM   9973  N  N   . TRP D  1 268 ? 58.998  28.349  -18.080 1.00 8.41  ? 268  TRP D N   1 
ATOM   9974  C  CA  . TRP D  1 268 ? 59.570  29.425  -18.882 1.00 9.25  ? 268  TRP D CA  1 
ATOM   9975  C  C   . TRP D  1 268 ? 59.492  29.062  -20.360 1.00 9.96  ? 268  TRP D C   1 
ATOM   9976  O  O   . TRP D  1 268 ? 59.529  27.896  -20.679 1.00 10.77 ? 268  TRP D O   1 
ATOM   9977  C  CB  . TRP D  1 268 ? 61.050  29.597  -18.487 1.00 9.40  ? 268  TRP D CB  1 
ATOM   9978  C  CG  . TRP D  1 268 ? 61.219  30.076  -17.088 1.00 9.03  ? 268  TRP D CG  1 
ATOM   9979  C  CD1 . TRP D  1 268 ? 61.685  29.347  -16.018 1.00 12.25 ? 268  TRP D CD1 1 
ATOM   9980  C  CD2 . TRP D  1 268 ? 61.042  31.407  -16.624 1.00 9.38  ? 268  TRP D CD2 1 
ATOM   9981  N  NE1 . TRP D  1 268 ? 61.752  30.150  -14.899 1.00 10.87 ? 268  TRP D NE1 1 
ATOM   9982  C  CE2 . TRP D  1 268 ? 61.356  31.418  -15.244 1.00 9.49  ? 268  TRP D CE2 1 
ATOM   9983  C  CE3 . TRP D  1 268 ? 60.593  32.602  -17.227 1.00 11.13 ? 268  TRP D CE3 1 
ATOM   9984  C  CZ2 . TRP D  1 268 ? 61.267  32.578  -14.455 1.00 8.74  ? 268  TRP D CZ2 1 
ATOM   9985  C  CZ3 . TRP D  1 268 ? 60.515  33.758  -16.453 1.00 13.62 ? 268  TRP D CZ3 1 
ATOM   9986  C  CH2 . TRP D  1 268 ? 60.848  33.737  -15.078 1.00 9.98  ? 268  TRP D CH2 1 
ATOM   9987  N  N   . SER D  1 269 ? 59.378  30.064  -21.236 1.00 10.25 ? 269  SER D N   1 
ATOM   9988  C  CA  . SER D  1 269 ? 59.501  29.915  -22.678 1.00 10.43 ? 269  SER D CA  1 
ATOM   9989  C  C   . SER D  1 269 ? 60.141  31.202  -23.188 1.00 10.84 ? 269  SER D C   1 
ATOM   9990  O  O   . SER D  1 269 ? 59.681  32.299  -22.847 1.00 10.91 ? 269  SER D O   1 
ATOM   9991  C  CB  . SER D  1 269 ? 58.104  29.778  -23.319 1.00 11.73 ? 269  SER D CB  1 
ATOM   9992  O  OG  . SER D  1 269 ? 58.212  29.088  -24.532 1.00 13.57 ? 269  SER D OG  1 
ATOM   9993  N  N   . PHE D  1 270 ? 61.184  31.088  -24.003 1.00 9.99  ? 270  PHE D N   1 
ATOM   9994  C  CA  . PHE D  1 270 ? 61.845  32.264  -24.575 1.00 10.40 ? 270  PHE D CA  1 
ATOM   9995  C  C   . PHE D  1 270 ? 62.071  32.025  -26.044 1.00 10.00 ? 270  PHE D C   1 
ATOM   9996  O  O   . PHE D  1 270 ? 62.186  30.856  -26.442 1.00 9.64  ? 270  PHE D O   1 
ATOM   9997  C  CB  . PHE D  1 270 ? 63.178  32.575  -23.861 1.00 9.12  ? 270  PHE D CB  1 
ATOM   9998  C  CG  . PHE D  1 270 ? 63.001  32.965  -22.449 1.00 10.74 ? 270  PHE D CG  1 
ATOM   9999  C  CD1 . PHE D  1 270 ? 62.503  34.229  -22.118 1.00 12.65 ? 270  PHE D CD1 1 
ATOM   10000 C  CD2 . PHE D  1 270 ? 63.248  32.049  -21.425 1.00 9.76  ? 270  PHE D CD2 1 
ATOM   10001 C  CE1 . PHE D  1 270 ? 62.312  34.583  -20.784 1.00 12.72 ? 270  PHE D CE1 1 
ATOM   10002 C  CE2 . PHE D  1 270 ? 63.051  32.406  -20.090 1.00 8.70  ? 270  PHE D CE2 1 
ATOM   10003 C  CZ  . PHE D  1 270 ? 62.596  33.654  -19.775 1.00 10.14 ? 270  PHE D CZ  1 
ATOM   10004 N  N   . PRO D  1 271 ? 62.070  33.088  -26.866 1.00 10.50 ? 271  PRO D N   1 
ATOM   10005 C  CA  . PRO D  1 271 ? 62.192  32.904  -28.320 1.00 10.26 ? 271  PRO D CA  1 
ATOM   10006 C  C   . PRO D  1 271 ? 63.554  32.399  -28.787 1.00 9.89  ? 271  PRO D C   1 
ATOM   10007 O  O   . PRO D  1 271 ? 63.572  31.634  -29.743 1.00 11.30 ? 271  PRO D O   1 
ATOM   10008 C  CB  . PRO D  1 271 ? 61.913  34.306  -28.879 1.00 10.77 ? 271  PRO D CB  1 
ATOM   10009 C  CG  . PRO D  1 271 ? 62.179  35.244  -27.755 1.00 11.02 ? 271  PRO D CG  1 
ATOM   10010 C  CD  . PRO D  1 271 ? 61.774  34.507  -26.525 1.00 11.65 ? 271  PRO D CD  1 
ATOM   10011 N  N   . GLY D  1 272 ? 64.650  32.827  -28.167 1.00 8.75  ? 272  GLY D N   1 
ATOM   10012 C  CA  . GLY D  1 272 ? 65.972  32.325  -28.507 1.00 7.98  ? 272  GLY D CA  1 
ATOM   10013 C  C   . GLY D  1 272 ? 66.361  31.140  -27.658 1.00 6.93  ? 272  GLY D C   1 
ATOM   10014 O  O   . GLY D  1 272 ? 65.921  30.972  -26.509 1.00 7.85  ? 272  GLY D O   1 
ATOM   10015 N  N   . ALA D  1 273 ? 67.219  30.306  -28.220 1.00 7.51  ? 273  ALA D N   1 
ATOM   10016 C  CA  . ALA D  1 273 ? 67.779  29.184  -27.456 1.00 8.00  ? 273  ALA D CA  1 
ATOM   10017 C  C   . ALA D  1 273 ? 68.529  29.681  -26.211 1.00 8.33  ? 273  ALA D C   1 
ATOM   10018 O  O   . ALA D  1 273 ? 69.044  30.792  -26.198 1.00 9.64  ? 273  ALA D O   1 
ATOM   10019 C  CB  . ALA D  1 273 ? 68.722  28.398  -28.348 1.00 8.36  ? 273  ALA D CB  1 
ATOM   10020 N  N   . CYS D  1 274 ? 68.639  28.858  -25.179 1.00 8.10  ? 274  CYS D N   1 
ATOM   10021 C  CA  . CYS D  1 274 ? 69.539  29.215  -24.083 1.00 8.73  ? 274  CYS D CA  1 
ATOM   10022 C  C   . CYS D  1 274 ? 70.157  27.955  -23.590 1.00 9.33  ? 274  CYS D C   1 
ATOM   10023 O  O   . CYS D  1 274 ? 69.687  26.863  -23.956 1.00 9.46  ? 274  CYS D O   1 
ATOM   10024 C  CB  . CYS D  1 274 ? 68.796  29.935  -22.952 1.00 8.53  ? 274  CYS D CB  1 
ATOM   10025 S  SG  . CYS D  1 274 ? 67.454  29.033  -22.118 1.00 10.03 ? 274  CYS D SG  1 
ATOM   10026 N  N   . ALA D  1 275 ? 71.151  28.085  -22.714 1.00 8.37  ? 275  ALA D N   1 
ATOM   10027 C  CA  . ALA D  1 275 ? 71.793  26.920  -22.141 1.00 8.95  ? 275  ALA D CA  1 
ATOM   10028 C  C   . ALA D  1 275 ? 72.478  27.306  -20.831 1.00 9.90  ? 275  ALA D C   1 
ATOM   10029 O  O   . ALA D  1 275 ? 72.694  28.486  -20.555 1.00 10.44 ? 275  ALA D O   1 
ATOM   10030 C  CB  . ALA D  1 275 ? 72.860  26.317  -23.141 1.00 8.54  ? 275  ALA D CB  1 
ATOM   10031 N  N   . PHE D  1 276 ? 72.777  26.316  -20.000 1.00 9.63  ? 276  PHE D N   1 
ATOM   10032 C  CA  . PHE D  1 276 ? 73.573  26.590  -18.817 1.00 10.07 ? 276  PHE D CA  1 
ATOM   10033 C  C   . PHE D  1 276 ? 74.476  25.412  -18.498 1.00 10.18 ? 276  PHE D C   1 
ATOM   10034 O  O   . PHE D  1 276 ? 74.184  24.262  -18.886 1.00 10.38 ? 276  PHE D O   1 
ATOM   10035 C  CB  . PHE D  1 276 ? 72.698  27.010  -17.598 1.00 11.02 ? 276  PHE D CB  1 
ATOM   10036 C  CG  . PHE D  1 276 ? 71.716  25.949  -17.116 1.00 11.29 ? 276  PHE D CG  1 
ATOM   10037 C  CD1 . PHE D  1 276 ? 72.124  25.000  -16.164 1.00 10.13 ? 276  PHE D CD1 1 
ATOM   10038 C  CD2 . PHE D  1 276 ? 70.382  25.966  -17.558 1.00 11.71 ? 276  PHE D CD2 1 
ATOM   10039 C  CE1 . PHE D  1 276 ? 71.252  24.021  -15.672 1.00 10.77 ? 276  PHE D CE1 1 
ATOM   10040 C  CE2 . PHE D  1 276 ? 69.461  24.990  -17.091 1.00 10.99 ? 276  PHE D CE2 1 
ATOM   10041 C  CZ  . PHE D  1 276 ? 69.912  24.004  -16.133 1.00 8.33  ? 276  PHE D CZ  1 
ATOM   10042 N  N   . GLN D  1 277 ? 75.590  25.726  -17.828 1.00 9.43  ? 277  GLN D N   1 
ATOM   10043 C  CA  . GLN D  1 277 ? 76.466  24.715  -17.320 1.00 8.40  ? 277  GLN D CA  1 
ATOM   10044 C  C   . GLN D  1 277 ? 76.523  24.882  -15.797 1.00 7.80  ? 277  GLN D C   1 
ATOM   10045 O  O   . GLN D  1 277 ? 76.788  25.981  -15.311 1.00 7.88  ? 277  GLN D O   1 
ATOM   10046 C  CB  . GLN D  1 277 ? 77.872  24.875  -17.907 1.00 8.18  ? 277  GLN D CB  1 
ATOM   10047 C  CG  . GLN D  1 277 ? 78.851  23.814  -17.371 1.00 6.44  ? 277  GLN D CG  1 
ATOM   10048 C  CD  . GLN D  1 277 ? 80.291  24.052  -17.861 1.00 10.27 ? 277  GLN D CD  1 
ATOM   10049 O  OE1 . GLN D  1 277 ? 80.830  25.161  -17.669 1.00 12.73 ? 277  GLN D OE1 1 
ATOM   10050 N  NE2 . GLN D  1 277 ? 80.927  23.028  -18.419 1.00 9.89  ? 277  GLN D NE2 1 
ATOM   10051 N  N   . VAL D  1 278 ? 76.271  23.814  -15.061 1.00 6.64  ? 278  VAL D N   1 
ATOM   10052 C  CA  . VAL D  1 278 ? 76.319  23.910  -13.598 1.00 8.50  ? 278  VAL D CA  1 
ATOM   10053 C  C   . VAL D  1 278 ? 77.763  24.140  -13.151 1.00 8.97  ? 278  VAL D C   1 
ATOM   10054 O  O   . VAL D  1 278 ? 78.636  23.396  -13.563 1.00 8.33  ? 278  VAL D O   1 
ATOM   10055 C  CB  . VAL D  1 278 ? 75.807  22.622  -12.941 1.00 7.40  ? 278  VAL D CB  1 
ATOM   10056 C  CG1 . VAL D  1 278 ? 75.929  22.677  -11.378 1.00 7.56  ? 278  VAL D CG1 1 
ATOM   10057 C  CG2 . VAL D  1 278 ? 74.338  22.359  -13.372 1.00 8.12  ? 278  VAL D CG2 1 
ATOM   10058 N  N   . GLN D  1 279 ? 78.007  25.199  -12.351 1.00 9.44  ? 279  GLN D N   1 
ATOM   10059 C  CA  . GLN D  1 279 ? 79.298  25.359  -11.677 1.00 9.41  ? 279  GLN D CA  1 
ATOM   10060 C  C   . GLN D  1 279 ? 79.368  24.667  -10.304 1.00 10.11 ? 279  GLN D C   1 
ATOM   10061 O  O   . GLN D  1 279 ? 80.339  23.928  -10.006 1.00 9.86  ? 279  GLN D O   1 
ATOM   10062 C  CB  . GLN D  1 279 ? 79.657  26.825  -11.556 1.00 8.82  ? 279  GLN D CB  1 
ATOM   10063 C  CG  . GLN D  1 279 ? 79.663  27.514  -12.946 1.00 10.24 ? 279  GLN D CG  1 
ATOM   10064 C  CD  . GLN D  1 279 ? 80.547  26.796  -13.976 1.00 10.00 ? 279  GLN D CD  1 
ATOM   10065 O  OE1 . GLN D  1 279 ? 81.721  26.525  -13.715 1.00 8.55  ? 279  GLN D OE1 1 
ATOM   10066 N  NE2 . GLN D  1 279 ? 79.954  26.438  -15.137 1.00 10.22 ? 279  GLN D NE2 1 
ATOM   10067 N  N   . GLU D  1 280 ? 78.363  24.914  -9.464  1.00 8.49  ? 280  GLU D N   1 
ATOM   10068 C  CA  . GLU D  1 280 ? 78.345  24.365  -8.123  1.00 9.21  ? 280  GLU D CA  1 
ATOM   10069 C  C   . GLU D  1 280 ? 76.870  23.951  -7.889  1.00 9.21  ? 280  GLU D C   1 
ATOM   10070 O  O   . GLU D  1 280 ? 75.973  24.665  -8.298  1.00 9.56  ? 280  GLU D O   1 
ATOM   10071 C  CB  . GLU D  1 280 ? 78.773  25.456  -7.134  1.00 7.72  ? 280  GLU D CB  1 
ATOM   10072 C  CG  . GLU D  1 280 ? 78.671  25.087  -5.692  1.00 13.08 ? 280  GLU D CG  1 
ATOM   10073 C  CD  . GLU D  1 280 ? 79.012  26.219  -4.727  1.00 13.38 ? 280  GLU D CD  1 
ATOM   10074 O  OE1 . GLU D  1 280 ? 79.277  27.392  -5.100  1.00 17.57 ? 280  GLU D OE1 1 
ATOM   10075 O  OE2 . GLU D  1 280 ? 78.958  25.906  -3.535  1.00 21.32 ? 280  GLU D OE2 1 
ATOM   10076 N  N   . GLY D  1 281 ? 76.664  22.799  -7.256  1.00 7.92  ? 281  GLY D N   1 
ATOM   10077 C  CA  . GLY D  1 281 ? 75.334  22.467  -6.765  1.00 7.87  ? 281  GLY D CA  1 
ATOM   10078 C  C   . GLY D  1 281 ? 74.705  21.396  -7.645  1.00 7.27  ? 281  GLY D C   1 
ATOM   10079 O  O   . GLY D  1 281 ? 75.384  20.740  -8.444  1.00 5.46  ? 281  GLY D O   1 
ATOM   10080 N  N   . ARG D  1 282 ? 73.380  21.281  -7.538  1.00 7.31  ? 282  ARG D N   1 
ATOM   10081 C  CA  . ARG D  1 282 ? 72.641  20.190  -8.163  1.00 5.93  ? 282  ARG D CA  1 
ATOM   10082 C  C   . ARG D  1 282 ? 71.355  20.819  -8.609  1.00 6.72  ? 282  ARG D C   1 
ATOM   10083 O  O   . ARG D  1 282 ? 70.526  21.227  -7.769  1.00 6.95  ? 282  ARG D O   1 
ATOM   10084 C  CB  . ARG D  1 282 ? 72.380  19.066  -7.128  1.00 5.67  ? 282  ARG D CB  1 
ATOM   10085 C  CG  . ARG D  1 282 ? 73.695  18.565  -6.466  1.00 5.71  ? 282  ARG D CG  1 
ATOM   10086 C  CD  . ARG D  1 282 ? 73.495  17.410  -5.502  1.00 9.06  ? 282  ARG D CD  1 
ATOM   10087 N  NE  . ARG D  1 282 ? 72.739  17.752  -4.298  1.00 8.54  ? 282  ARG D NE  1 
ATOM   10088 C  CZ  . ARG D  1 282 ? 71.525  17.273  -4.019  1.00 10.63 ? 282  ARG D CZ  1 
ATOM   10089 N  NH1 . ARG D  1 282 ? 70.903  16.459  -4.856  1.00 9.64  ? 282  ARG D NH1 1 
ATOM   10090 N  NH2 . ARG D  1 282 ? 70.931  17.597  -2.886  1.00 7.66  ? 282  ARG D NH2 1 
ATOM   10091 N  N   . VAL D  1 283 ? 71.192  20.934  -9.923  1.00 6.83  ? 283  VAL D N   1 
ATOM   10092 C  CA  . VAL D  1 283 ? 70.014  21.570  -10.522 1.00 6.95  ? 283  VAL D CA  1 
ATOM   10093 C  C   . VAL D  1 283 ? 69.205  20.570  -11.322 1.00 7.05  ? 283  VAL D C   1 
ATOM   10094 O  O   . VAL D  1 283 ? 69.740  19.854  -12.169 1.00 8.59  ? 283  VAL D O   1 
ATOM   10095 C  CB  . VAL D  1 283 ? 70.474  22.722  -11.492 1.00 6.88  ? 283  VAL D CB  1 
ATOM   10096 C  CG1 . VAL D  1 283 ? 69.265  23.466  -12.127 1.00 3.65  ? 283  VAL D CG1 1 
ATOM   10097 C  CG2 . VAL D  1 283 ? 71.351  23.698  -10.744 1.00 6.65  ? 283  VAL D CG2 1 
ATOM   10098 N  N   . VAL D  1 284 ? 67.897  20.558  -11.122 1.00 8.04  ? 284  VAL D N   1 
ATOM   10099 C  CA  . VAL D  1 284 ? 67.035  19.694  -11.901 1.00 6.93  ? 284  VAL D CA  1 
ATOM   10100 C  C   . VAL D  1 284 ? 66.429  20.516  -13.045 1.00 8.86  ? 284  VAL D C   1 
ATOM   10101 O  O   . VAL D  1 284 ? 65.913  21.608  -12.823 1.00 9.50  ? 284  VAL D O   1 
ATOM   10102 C  CB  . VAL D  1 284 ? 65.910  19.099  -11.059 1.00 6.08  ? 284  VAL D CB  1 
ATOM   10103 C  CG1 . VAL D  1 284 ? 64.988  18.252  -11.916 1.00 6.12  ? 284  VAL D CG1 1 
ATOM   10104 C  CG2 . VAL D  1 284 ? 66.484  18.257  -9.936  1.00 8.24  ? 284  VAL D CG2 1 
ATOM   10105 N  N   . VAL D  1 285 ? 66.522  19.974  -14.254 1.00 8.92  ? 285  VAL D N   1 
ATOM   10106 C  CA  . VAL D  1 285 ? 65.964  20.613  -15.439 1.00 9.44  ? 285  VAL D CA  1 
ATOM   10107 C  C   . VAL D  1 285 ? 64.926  19.676  -16.049 1.00 8.69  ? 285  VAL D C   1 
ATOM   10108 O  O   . VAL D  1 285 ? 65.103  18.458  -16.030 1.00 8.53  ? 285  VAL D O   1 
ATOM   10109 C  CB  . VAL D  1 285 ? 67.104  21.018  -16.443 1.00 9.37  ? 285  VAL D CB  1 
ATOM   10110 C  CG1 . VAL D  1 285 ? 67.631  19.819  -17.261 1.00 7.44  ? 285  VAL D CG1 1 
ATOM   10111 C  CG2 . VAL D  1 285 ? 66.626  22.195  -17.366 1.00 11.93 ? 285  VAL D CG2 1 
ATOM   10112 N  N   . GLN D  1 286 ? 63.844  20.258  -16.574 1.00 8.58  ? 286  GLN D N   1 
ATOM   10113 C  CA  . GLN D  1 286 ? 62.746  19.517  -17.239 1.00 9.44  ? 286  GLN D CA  1 
ATOM   10114 C  C   . GLN D  1 286 ? 62.385  20.334  -18.468 1.00 9.82  ? 286  GLN D C   1 
ATOM   10115 O  O   . GLN D  1 286 ? 61.992  21.533  -18.351 1.00 10.73 ? 286  GLN D O   1 
ATOM   10116 C  CB  . GLN D  1 286 ? 61.538  19.347  -16.299 1.00 9.03  ? 286  GLN D CB  1 
ATOM   10117 C  CG  . GLN D  1 286 ? 60.318  18.627  -16.949 1.00 11.49 ? 286  GLN D CG  1 
ATOM   10118 C  CD  . GLN D  1 286 ? 59.231  18.174  -15.981 1.00 15.39 ? 286  GLN D CD  1 
ATOM   10119 O  OE1 . GLN D  1 286 ? 59.310  18.410  -14.763 1.00 15.67 ? 286  GLN D OE1 1 
ATOM   10120 N  NE2 . GLN D  1 286 ? 58.197  17.514  -16.526 1.00 13.23 ? 286  GLN D NE2 1 
ATOM   10121 N  N   . ILE D  1 287 ? 62.565  19.720  -19.640 1.00 9.49  ? 287  ILE D N   1 
ATOM   10122 C  CA  . ILE D  1 287 ? 62.559  20.442  -20.914 1.00 9.44  ? 287  ILE D CA  1 
ATOM   10123 C  C   . ILE D  1 287 ? 61.639  19.681  -21.857 1.00 10.35 ? 287  ILE D C   1 
ATOM   10124 O  O   . ILE D  1 287 ? 61.843  18.497  -22.076 1.00 9.37  ? 287  ILE D O   1 
ATOM   10125 C  CB  . ILE D  1 287 ? 63.981  20.580  -21.564 1.00 10.09 ? 287  ILE D CB  1 
ATOM   10126 C  CG1 . ILE D  1 287 ? 65.026  21.178  -20.596 1.00 9.69  ? 287  ILE D CG1 1 
ATOM   10127 C  CG2 . ILE D  1 287 ? 63.870  21.490  -22.805 1.00 7.31  ? 287  ILE D CG2 1 
ATOM   10128 C  CD1 . ILE D  1 287 ? 66.522  20.949  -21.049 1.00 8.95  ? 287  ILE D CD1 1 
ATOM   10129 N  N   . GLY D  1 288 ? 60.611  20.372  -22.357 1.00 10.23 ? 288  GLY D N   1 
ATOM   10130 C  CA  . GLY D  1 288 ? 59.656  19.809  -23.275 1.00 10.51 ? 288  GLY D CA  1 
ATOM   10131 C  C   . GLY D  1 288 ? 59.002  18.634  -22.599 1.00 12.22 ? 288  GLY D C   1 
ATOM   10132 O  O   . GLY D  1 288 ? 58.659  18.715  -21.411 1.00 12.57 ? 288  GLY D O   1 
ATOM   10133 N  N   . ASP D  1 289 ? 58.901  17.530  -23.331 1.00 12.16 ? 289  ASP D N   1 
ATOM   10134 C  CA  . ASP D  1 289 ? 58.296  16.301  -22.812 1.00 13.86 ? 289  ASP D CA  1 
ATOM   10135 C  C   . ASP D  1 289 ? 59.293  15.250  -22.313 1.00 12.87 ? 289  ASP D C   1 
ATOM   10136 O  O   . ASP D  1 289 ? 58.917  14.105  -22.042 1.00 12.09 ? 289  ASP D O   1 
ATOM   10137 C  CB  . ASP D  1 289 ? 57.392  15.715  -23.875 1.00 14.92 ? 289  ASP D CB  1 
ATOM   10138 C  CG  . ASP D  1 289 ? 56.311  16.675  -24.263 1.00 20.22 ? 289  ASP D CG  1 
ATOM   10139 O  OD1 . ASP D  1 289 ? 55.374  16.882  -23.435 1.00 26.07 ? 289  ASP D OD1 1 
ATOM   10140 O  OD2 . ASP D  1 289 ? 56.344  17.310  -25.344 1.00 25.59 ? 289  ASP D OD2 1 
ATOM   10141 N  N   . TYR D  1 290 ? 60.551  15.661  -22.156 1.00 11.78 ? 290  TYR D N   1 
ATOM   10142 C  CA  . TYR D  1 290 ? 61.602  14.757  -21.709 1.00 11.63 ? 290  TYR D CA  1 
ATOM   10143 C  C   . TYR D  1 290 ? 61.518  14.583  -20.199 1.00 12.06 ? 290  TYR D C   1 
ATOM   10144 O  O   . TYR D  1 290 ? 60.958  15.423  -19.514 1.00 10.55 ? 290  TYR D O   1 
ATOM   10145 C  CB  . TYR D  1 290 ? 62.979  15.341  -22.065 1.00 10.57 ? 290  TYR D CB  1 
ATOM   10146 C  CG  . TYR D  1 290 ? 63.342  15.230  -23.534 1.00 10.83 ? 290  TYR D CG  1 
ATOM   10147 C  CD1 . TYR D  1 290 ? 62.935  16.208  -24.443 1.00 11.24 ? 290  TYR D CD1 1 
ATOM   10148 C  CD2 . TYR D  1 290 ? 64.045  14.125  -24.023 1.00 9.07  ? 290  TYR D CD2 1 
ATOM   10149 C  CE1 . TYR D  1 290 ? 63.270  16.132  -25.768 1.00 11.39 ? 290  TYR D CE1 1 
ATOM   10150 C  CE2 . TYR D  1 290 ? 64.383  14.041  -25.350 1.00 8.66  ? 290  TYR D CE2 1 
ATOM   10151 C  CZ  . TYR D  1 290 ? 63.986  15.053  -26.222 1.00 13.49 ? 290  TYR D CZ  1 
ATOM   10152 O  OH  . TYR D  1 290 ? 64.308  14.995  -27.556 1.00 17.31 ? 290  TYR D OH  1 
ATOM   10153 N  N   . ALA D  1 291 ? 62.091  13.493  -19.675 1.00 12.68 ? 291  ALA D N   1 
ATOM   10154 C  CA  . ALA D  1 291 ? 62.115  13.276  -18.232 1.00 12.23 ? 291  ALA D CA  1 
ATOM   10155 C  C   . ALA D  1 291 ? 63.010  14.324  -17.597 1.00 12.93 ? 291  ALA D C   1 
ATOM   10156 O  O   . ALA D  1 291 ? 64.009  14.751  -18.203 1.00 12.74 ? 291  ALA D O   1 
ATOM   10157 C  CB  . ALA D  1 291 ? 62.612  11.838  -17.894 1.00 12.49 ? 291  ALA D CB  1 
ATOM   10158 N  N   . ALA D  1 292 ? 62.645  14.759  -16.391 1.00 12.14 ? 292  ALA D N   1 
ATOM   10159 C  CA  . ALA D  1 292 ? 63.511  15.639  -15.591 1.00 12.38 ? 292  ALA D CA  1 
ATOM   10160 C  C   . ALA D  1 292 ? 64.858  14.976  -15.233 1.00 12.92 ? 292  ALA D C   1 
ATOM   10161 O  O   . ALA D  1 292 ? 64.897  13.817  -14.831 1.00 14.90 ? 292  ALA D O   1 
ATOM   10162 C  CB  . ALA D  1 292 ? 62.783  16.042  -14.330 1.00 11.86 ? 292  ALA D CB  1 
ATOM   10163 N  N   . THR D  1 293 ? 65.948  15.738  -15.316 1.00 13.01 ? 293  THR D N   1 
ATOM   10164 C  CA  . THR D  1 293 ? 67.286  15.212  -15.108 1.00 13.02 ? 293  THR D CA  1 
ATOM   10165 C  C   . THR D  1 293 ? 67.995  16.122  -14.141 1.00 10.06 ? 293  THR D C   1 
ATOM   10166 O  O   . THR D  1 293 ? 67.884  17.327  -14.282 1.00 10.37 ? 293  THR D O   1 
ATOM   10167 C  CB  . THR D  1 293 ? 68.034  15.228  -16.457 1.00 13.35 ? 293  THR D CB  1 
ATOM   10168 O  OG1 . THR D  1 293 ? 67.393  14.288  -17.320 1.00 18.45 ? 293  THR D OG1 1 
ATOM   10169 C  CG2 . THR D  1 293 ? 69.407  14.652  -16.322 1.00 16.89 ? 293  THR D CG2 1 
ATOM   10170 N  N   . GLU D  1 294 ? 68.700  15.553  -13.175 1.00 8.48  ? 294  GLU D N   1 
ATOM   10171 C  CA  . GLU D  1 294 ? 69.473  16.347  -12.251 1.00 8.07  ? 294  GLU D CA  1 
ATOM   10172 C  C   . GLU D  1 294 ? 70.915  16.516  -12.767 1.00 8.79  ? 294  GLU D C   1 
ATOM   10173 O  O   . GLU D  1 294 ? 71.549  15.540  -13.140 1.00 9.77  ? 294  GLU D O   1 
ATOM   10174 C  CB  . GLU D  1 294 ? 69.469  15.756  -10.827 1.00 8.11  ? 294  GLU D CB  1 
ATOM   10175 C  CG  . GLU D  1 294 ? 70.039  16.723  -9.763  1.00 5.36  ? 294  GLU D CG  1 
ATOM   10176 C  CD  . GLU D  1 294 ? 70.175  16.042  -8.404  1.00 13.44 ? 294  GLU D CD  1 
ATOM   10177 O  OE1 . GLU D  1 294 ? 69.254  15.288  -7.938  1.00 14.38 ? 294  GLU D OE1 1 
ATOM   10178 O  OE2 . GLU D  1 294 ? 71.241  16.171  -7.837  1.00 15.42 ? 294  GLU D OE2 1 
ATOM   10179 N  N   . LEU D  1 295 ? 71.399  17.750  -12.777 1.00 7.86  ? 295  LEU D N   1 
ATOM   10180 C  CA  . LEU D  1 295 ? 72.731  18.055  -13.272 1.00 8.90  ? 295  LEU D CA  1 
ATOM   10181 C  C   . LEU D  1 295 ? 73.665  18.375  -12.121 1.00 9.75  ? 295  LEU D C   1 
ATOM   10182 O  O   . LEU D  1 295 ? 73.224  19.022  -11.151 1.00 9.37  ? 295  LEU D O   1 
ATOM   10183 C  CB  . LEU D  1 295 ? 72.716  19.256  -14.238 1.00 8.98  ? 295  LEU D CB  1 
ATOM   10184 C  CG  . LEU D  1 295 ? 72.329  19.009  -15.711 1.00 10.40 ? 295  LEU D CG  1 
ATOM   10185 C  CD1 . LEU D  1 295 ? 70.909  18.615  -15.871 1.00 11.06 ? 295  LEU D CD1 1 
ATOM   10186 C  CD2 . LEU D  1 295 ? 72.571  20.352  -16.524 1.00 9.50  ? 295  LEU D CD2 1 
ATOM   10187 N  N   . GLY D  1 296 ? 74.938  17.989  -12.284 1.00 6.20  ? 296  GLY D N   1 
ATOM   10188 C  CA  . GLY D  1 296 ? 76.000  18.254  -11.313 1.00 7.48  ? 296  GLY D CA  1 
ATOM   10189 C  C   . GLY D  1 296 ? 77.120  19.069  -11.982 1.00 7.69  ? 296  GLY D C   1 
ATOM   10190 O  O   . GLY D  1 296 ? 76.947  19.618  -13.078 1.00 8.39  ? 296  GLY D O   1 
ATOM   10191 N  N   . SER D  1 297 ? 78.279  19.156  -11.341 1.00 8.22  ? 297  SER D N   1 
ATOM   10192 C  CA  . SER D  1 297 ? 79.262  20.134  -11.791 1.00 9.26  ? 297  SER D CA  1 
ATOM   10193 C  C   . SER D  1 297 ? 79.710  19.900  -13.243 1.00 8.43  ? 297  SER D C   1 
ATOM   10194 O  O   . SER D  1 297 ? 79.948  18.768  -13.670 1.00 7.04  ? 297  SER D O   1 
ATOM   10195 C  CB  . SER D  1 297 ? 80.463  20.209  -10.865 1.00 10.83 ? 297  SER D CB  1 
ATOM   10196 O  OG  . SER D  1 297 ? 81.029  18.955  -10.668 1.00 14.02 ? 297  SER D OG  1 
ATOM   10197 N  N   . GLY D  1 298 ? 79.741  20.997  -13.991 1.00 7.13  ? 298  GLY D N   1 
ATOM   10198 C  CA  . GLY D  1 298 ? 80.166  20.951  -15.392 1.00 7.06  ? 298  GLY D CA  1 
ATOM   10199 C  C   . GLY D  1 298 ? 79.133  20.387  -16.389 1.00 8.58  ? 298  GLY D C   1 
ATOM   10200 O  O   . GLY D  1 298 ? 79.397  20.467  -17.577 1.00 8.57  ? 298  GLY D O   1 
ATOM   10201 N  N   . ASP D  1 299 ? 78.031  19.771  -15.920 1.00 6.81  ? 299  ASP D N   1 
ATOM   10202 C  CA  . ASP D  1 299 ? 76.989  19.261  -16.796 1.00 7.55  ? 299  ASP D CA  1 
ATOM   10203 C  C   . ASP D  1 299 ? 76.240  20.455  -17.451 1.00 7.90  ? 299  ASP D C   1 
ATOM   10204 O  O   . ASP D  1 299 ? 76.119  21.512  -16.844 1.00 9.33  ? 299  ASP D O   1 
ATOM   10205 C  CB  . ASP D  1 299 ? 75.948  18.440  -16.029 1.00 5.39  ? 299  ASP D CB  1 
ATOM   10206 C  CG  . ASP D  1 299 ? 76.471  17.188  -15.461 1.00 8.08  ? 299  ASP D CG  1 
ATOM   10207 O  OD1 . ASP D  1 299 ? 77.568  16.662  -15.874 1.00 4.22  ? 299  ASP D OD1 1 
ATOM   10208 O  OD2 . ASP D  1 299 ? 75.798  16.605  -14.571 1.00 6.37  ? 299  ASP D OD2 1 
ATOM   10209 N  N   . VAL D  1 300 ? 75.791  20.251  -18.694 1.00 7.64  ? 300  VAL D N   1 
ATOM   10210 C  CA  . VAL D  1 300 ? 75.224  21.266  -19.576 1.00 7.73  ? 300  VAL D CA  1 
ATOM   10211 C  C   . VAL D  1 300 ? 73.813  20.847  -20.016 1.00 7.02  ? 300  VAL D C   1 
ATOM   10212 O  O   . VAL D  1 300 ? 73.580  19.708  -20.433 1.00 7.72  ? 300  VAL D O   1 
ATOM   10213 C  CB  . VAL D  1 300 ? 76.112  21.524  -20.831 1.00 7.29  ? 300  VAL D CB  1 
ATOM   10214 C  CG1 . VAL D  1 300 ? 75.451  22.585  -21.766 1.00 8.17  ? 300  VAL D CG1 1 
ATOM   10215 C  CG2 . VAL D  1 300 ? 77.535  22.032  -20.440 1.00 5.18  ? 300  VAL D CG2 1 
ATOM   10216 N  N   . ALA D  1 301 ? 72.904  21.799  -19.942 1.00 7.54  ? 301  ALA D N   1 
ATOM   10217 C  CA  . ALA D  1 301 ? 71.524  21.653  -20.443 1.00 7.23  ? 301  ALA D CA  1 
ATOM   10218 C  C   . ALA D  1 301 ? 71.342  22.629  -21.576 1.00 8.18  ? 301  ALA D C   1 
ATOM   10219 O  O   . ALA D  1 301 ? 71.729  23.800  -21.460 1.00 8.96  ? 301  ALA D O   1 
ATOM   10220 C  CB  . ALA D  1 301 ? 70.522  21.976  -19.297 1.00 6.44  ? 301  ALA D CB  1 
ATOM   10221 N  N   . PHE D  1 302 ? 70.754  22.168  -22.661 1.00 6.88  ? 302  PHE D N   1 
ATOM   10222 C  CA  . PHE D  1 302 ? 70.470  23.029  -23.794 1.00 6.78  ? 302  PHE D CA  1 
ATOM   10223 C  C   . PHE D  1 302 ? 68.963  23.081  -24.007 1.00 6.10  ? 302  PHE D C   1 
ATOM   10224 O  O   . PHE D  1 302 ? 68.286  22.021  -24.087 1.00 5.87  ? 302  PHE D O   1 
ATOM   10225 C  CB  . PHE D  1 302 ? 71.109  22.500  -25.099 1.00 7.14  ? 302  PHE D CB  1 
ATOM   10226 C  CG  . PHE D  1 302 ? 70.749  23.331  -26.267 1.00 7.18  ? 302  PHE D CG  1 
ATOM   10227 C  CD1 . PHE D  1 302 ? 71.393  24.558  -26.472 1.00 9.59  ? 302  PHE D CD1 1 
ATOM   10228 C  CD2 . PHE D  1 302 ? 69.713  22.942  -27.128 1.00 7.81  ? 302  PHE D CD2 1 
ATOM   10229 C  CE1 . PHE D  1 302 ? 71.000  25.401  -27.512 1.00 5.65  ? 302  PHE D CE1 1 
ATOM   10230 C  CE2 . PHE D  1 302 ? 69.304  23.796  -28.143 1.00 7.94  ? 302  PHE D CE2 1 
ATOM   10231 C  CZ  . PHE D  1 302 ? 69.955  25.025  -28.345 1.00 7.29  ? 302  PHE D CZ  1 
ATOM   10232 N  N   . ILE D  1 303 ? 68.428  24.295  -24.172 1.00 6.93  ? 303  ILE D N   1 
ATOM   10233 C  CA  . ILE D  1 303 ? 66.992  24.466  -24.373 1.00 5.29  ? 303  ILE D CA  1 
ATOM   10234 C  C   . ILE D  1 303 ? 66.706  25.241  -25.664 1.00 6.82  ? 303  ILE D C   1 
ATOM   10235 O  O   . ILE D  1 303 ? 67.023  26.455  -25.727 1.00 7.03  ? 303  ILE D O   1 
ATOM   10236 C  CB  . ILE D  1 303 ? 66.349  25.304  -23.192 1.00 6.57  ? 303  ILE D CB  1 
ATOM   10237 C  CG1 . ILE D  1 303 ? 66.574  24.653  -21.840 1.00 6.20  ? 303  ILE D CG1 1 
ATOM   10238 C  CG2 . ILE D  1 303 ? 64.852  25.412  -23.423 1.00 3.40  ? 303  ILE D CG2 1 
ATOM   10239 C  CD1 . ILE D  1 303 ? 67.835  25.128  -21.126 1.00 10.66 ? 303  ILE D CD1 1 
ATOM   10240 N  N   . PRO D  1 304 ? 66.097  24.608  -26.660 1.00 7.32  ? 304  PRO D N   1 
ATOM   10241 C  CA  . PRO D  1 304 ? 65.754  25.299  -27.904 1.00 6.67  ? 304  PRO D CA  1 
ATOM   10242 C  C   . PRO D  1 304 ? 64.797  26.470  -27.634 1.00 7.32  ? 304  PRO D C   1 
ATOM   10243 O  O   . PRO D  1 304 ? 63.946  26.316  -26.757 1.00 7.19  ? 304  PRO D O   1 
ATOM   10244 C  CB  . PRO D  1 304 ? 64.979  24.236  -28.700 1.00 8.43  ? 304  PRO D CB  1 
ATOM   10245 C  CG  . PRO D  1 304 ? 65.482  22.890  -28.139 1.00 7.29  ? 304  PRO D CG  1 
ATOM   10246 C  CD  . PRO D  1 304 ? 65.670  23.187  -26.683 1.00 7.07  ? 304  PRO D CD  1 
ATOM   10247 N  N   . GLY D  1 305 ? 64.908  27.554  -28.397 1.00 7.39  ? 305  GLY D N   1 
ATOM   10248 C  CA  . GLY D  1 305 ? 63.937  28.640  -28.348 1.00 7.60  ? 305  GLY D CA  1 
ATOM   10249 C  C   . GLY D  1 305 ? 62.530  28.111  -28.520 1.00 8.03  ? 305  GLY D C   1 
ATOM   10250 O  O   . GLY D  1 305 ? 62.290  27.189  -29.331 1.00 6.98  ? 305  GLY D O   1 
ATOM   10251 N  N   . GLY D  1 306 ? 61.600  28.685  -27.765 1.00 7.95  ? 306  GLY D N   1 
ATOM   10252 C  CA  . GLY D  1 306 ? 60.201  28.337  -27.893 1.00 8.66  ? 306  GLY D CA  1 
ATOM   10253 C  C   . GLY D  1 306 ? 59.838  27.032  -27.183 1.00 8.19  ? 306  GLY D C   1 
ATOM   10254 O  O   . GLY D  1 306 ? 58.680  26.647  -27.188 1.00 9.38  ? 306  GLY D O   1 
ATOM   10255 N  N   . VAL D  1 307 ? 60.800  26.342  -26.585 1.00 8.00  ? 307  VAL D N   1 
ATOM   10256 C  CA  . VAL D  1 307 ? 60.460  25.101  -25.881 1.00 7.90  ? 307  VAL D CA  1 
ATOM   10257 C  C   . VAL D  1 307 ? 60.294  25.368  -24.374 1.00 7.51  ? 307  VAL D C   1 
ATOM   10258 O  O   . VAL D  1 307 ? 61.117  26.080  -23.773 1.00 6.24  ? 307  VAL D O   1 
ATOM   10259 C  CB  . VAL D  1 307 ? 61.511  24.004  -26.147 1.00 7.76  ? 307  VAL D CB  1 
ATOM   10260 C  CG1 . VAL D  1 307 ? 61.337  22.817  -25.171 1.00 7.78  ? 307  VAL D CG1 1 
ATOM   10261 C  CG2 . VAL D  1 307 ? 61.434  23.595  -27.629 1.00 8.99  ? 307  VAL D CG2 1 
ATOM   10262 N  N   . GLU D  1 308 ? 59.219  24.845  -23.772 1.00 7.00  ? 308  GLU D N   1 
ATOM   10263 C  CA  . GLU D  1 308 ? 58.984  25.097  -22.348 1.00 8.01  ? 308  GLU D CA  1 
ATOM   10264 C  C   . GLU D  1 308 ? 59.973  24.345  -21.439 1.00 8.60  ? 308  GLU D C   1 
ATOM   10265 O  O   . GLU D  1 308 ? 60.354  23.184  -21.740 1.00 7.99  ? 308  GLU D O   1 
ATOM   10266 C  CB  . GLU D  1 308 ? 57.562  24.767  -21.992 1.00 8.98  ? 308  GLU D CB  1 
ATOM   10267 C  CG  . GLU D  1 308 ? 56.610  25.845  -22.450 1.00 12.57 ? 308  GLU D CG  1 
ATOM   10268 C  CD  . GLU D  1 308 ? 55.170  25.458  -22.210 1.00 18.49 ? 308  GLU D CD  1 
ATOM   10269 O  OE1 . GLU D  1 308 ? 54.887  24.250  -22.050 1.00 20.18 ? 308  GLU D OE1 1 
ATOM   10270 O  OE2 . GLU D  1 308 ? 54.329  26.382  -22.187 1.00 22.99 ? 308  GLU D OE2 1 
ATOM   10271 N  N   . PHE D  1 309 ? 60.405  25.015  -20.363 1.00 6.90  ? 309  PHE D N   1 
ATOM   10272 C  CA  . PHE D  1 309 ? 61.316  24.399  -19.404 1.00 8.78  ? 309  PHE D CA  1 
ATOM   10273 C  C   . PHE D  1 309 ? 61.022  24.809  -17.982 1.00 8.34  ? 309  PHE D C   1 
ATOM   10274 O  O   . PHE D  1 309 ? 60.461  25.879  -17.745 1.00 9.93  ? 309  PHE D O   1 
ATOM   10275 C  CB  . PHE D  1 309 ? 62.821  24.601  -19.738 1.00 7.82  ? 309  PHE D CB  1 
ATOM   10276 C  CG  . PHE D  1 309 ? 63.306  26.011  -19.652 1.00 9.06  ? 309  PHE D CG  1 
ATOM   10277 C  CD1 . PHE D  1 309 ? 63.010  26.936  -20.661 1.00 8.27  ? 309  PHE D CD1 1 
ATOM   10278 C  CD2 . PHE D  1 309 ? 64.139  26.404  -18.607 1.00 8.77  ? 309  PHE D CD2 1 
ATOM   10279 C  CE1 . PHE D  1 309 ? 63.526  28.230  -20.612 1.00 8.13  ? 309  PHE D CE1 1 
ATOM   10280 C  CE2 . PHE D  1 309 ? 64.622  27.707  -18.522 1.00 12.52 ? 309  PHE D CE2 1 
ATOM   10281 C  CZ  . PHE D  1 309 ? 64.303  28.639  -19.520 1.00 5.28  ? 309  PHE D CZ  1 
ATOM   10282 N  N   . LYS D  1 310 ? 61.392  23.931  -17.063 1.00 8.88  ? 310  LYS D N   1 
ATOM   10283 C  CA  . LYS D  1 310 ? 61.356  24.202  -15.633 1.00 9.32  ? 310  LYS D CA  1 
ATOM   10284 C  C   . LYS D  1 310 ? 62.697  23.849  -15.096 1.00 9.62  ? 310  LYS D C   1 
ATOM   10285 O  O   . LYS D  1 310 ? 63.348  22.878  -15.561 1.00 10.12 ? 310  LYS D O   1 
ATOM   10286 C  CB  . LYS D  1 310 ? 60.335  23.301  -14.948 1.00 9.77  ? 310  LYS D CB  1 
ATOM   10287 C  CG  . LYS D  1 310 ? 58.879  23.654  -15.245 1.00 12.56 ? 310  LYS D CG  1 
ATOM   10288 C  CD  . LYS D  1 310 ? 57.914  22.542  -14.779 1.00 17.17 ? 310  LYS D CD  1 
ATOM   10289 C  CE  . LYS D  1 310 ? 57.842  22.472  -13.269 1.00 21.44 ? 310  LYS D CE  1 
ATOM   10290 N  NZ  . LYS D  1 310 ? 56.468  22.094  -12.768 1.00 24.34 ? 310  LYS D NZ  1 
ATOM   10291 N  N   . TYR D  1 311 ? 63.152  24.620  -14.119 1.00 9.20  ? 311  TYR D N   1 
ATOM   10292 C  CA  . TYR D  1 311 ? 64.390  24.248  -13.429 1.00 8.80  ? 311  TYR D CA  1 
ATOM   10293 C  C   . TYR D  1 311 ? 64.273  24.628  -11.947 1.00 9.05  ? 311  TYR D C   1 
ATOM   10294 O  O   . TYR D  1 311 ? 63.527  25.561  -11.585 1.00 8.93  ? 311  TYR D O   1 
ATOM   10295 C  CB  . TYR D  1 311 ? 65.638  24.884  -14.087 1.00 7.92  ? 311  TYR D CB  1 
ATOM   10296 C  CG  . TYR D  1 311 ? 65.734  26.358  -13.800 1.00 7.65  ? 311  TYR D CG  1 
ATOM   10297 C  CD1 . TYR D  1 311 ? 65.029  27.260  -14.588 1.00 6.27  ? 311  TYR D CD1 1 
ATOM   10298 C  CD2 . TYR D  1 311 ? 66.486  26.851  -12.699 1.00 8.57  ? 311  TYR D CD2 1 
ATOM   10299 C  CE1 . TYR D  1 311 ? 65.060  28.597  -14.339 1.00 7.93  ? 311  TYR D CE1 1 
ATOM   10300 C  CE2 . TYR D  1 311 ? 66.518  28.237  -12.428 1.00 8.88  ? 311  TYR D CE2 1 
ATOM   10301 C  CZ  . TYR D  1 311 ? 65.791  29.097  -13.272 1.00 4.49  ? 311  TYR D CZ  1 
ATOM   10302 O  OH  . TYR D  1 311 ? 65.751  30.490  -13.086 1.00 7.66  ? 311  TYR D OH  1 
ATOM   10303 N  N   . TYR D  1 312 ? 64.990  23.889  -11.102 1.00 9.06  ? 312  TYR D N   1 
ATOM   10304 C  CA  . TYR D  1 312 ? 65.076  24.223  -9.696  1.00 9.33  ? 312  TYR D CA  1 
ATOM   10305 C  C   . TYR D  1 312 ? 66.330  23.606  -9.110  1.00 10.13 ? 312  TYR D C   1 
ATOM   10306 O  O   . TYR D  1 312 ? 66.957  22.677  -9.691  1.00 10.09 ? 312  TYR D O   1 
ATOM   10307 C  CB  . TYR D  1 312 ? 63.830  23.743  -8.915  1.00 8.93  ? 312  TYR D CB  1 
ATOM   10308 C  CG  . TYR D  1 312 ? 63.606  22.274  -8.905  1.00 7.77  ? 312  TYR D CG  1 
ATOM   10309 C  CD1 . TYR D  1 312 ? 64.149  21.444  -7.879  1.00 7.21  ? 312  TYR D CD1 1 
ATOM   10310 C  CD2 . TYR D  1 312 ? 62.807  21.664  -9.906  1.00 5.70  ? 312  TYR D CD2 1 
ATOM   10311 C  CE1 . TYR D  1 312 ? 63.909  20.037  -7.898  1.00 10.04 ? 312  TYR D CE1 1 
ATOM   10312 C  CE2 . TYR D  1 312 ? 62.570  20.302  -9.918  1.00 8.09  ? 312  TYR D CE2 1 
ATOM   10313 C  CZ  . TYR D  1 312 ? 63.132  19.492  -8.918  1.00 9.77  ? 312  TYR D CZ  1 
ATOM   10314 O  OH  . TYR D  1 312 ? 62.875  18.125  -8.954  1.00 11.66 ? 312  TYR D OH  1 
ATOM   10315 N  N   . SER D  1 313 ? 66.701  24.120  -7.946  1.00 9.99  ? 313  SER D N   1 
ATOM   10316 C  CA  . SER D  1 313 ? 67.876  23.618  -7.263  1.00 9.97  ? 313  SER D CA  1 
ATOM   10317 C  C   . SER D  1 313 ? 67.482  22.584  -6.205  1.00 9.41  ? 313  SER D C   1 
ATOM   10318 O  O   . SER D  1 313 ? 66.644  22.842  -5.325  1.00 8.95  ? 313  SER D O   1 
ATOM   10319 C  CB  . SER D  1 313 ? 68.660  24.771  -6.645  1.00 9.89  ? 313  SER D CB  1 
ATOM   10320 O  OG  . SER D  1 313 ? 69.860  24.289  -6.083  1.00 6.73  ? 313  SER D OG  1 
ATOM   10321 N  N   . GLU D  1 314 ? 68.085  21.407  -6.307  1.00 8.07  ? 314  GLU D N   1 
ATOM   10322 C  CA  . GLU D  1 314 ? 67.979  20.404  -5.270  1.00 8.95  ? 314  GLU D CA  1 
ATOM   10323 C  C   . GLU D  1 314 ? 68.984  20.758  -4.162  1.00 8.21  ? 314  GLU D C   1 
ATOM   10324 O  O   . GLU D  1 314 ? 68.718  20.577  -2.981  1.00 8.45  ? 314  GLU D O   1 
ATOM   10325 C  CB  . GLU D  1 314 ? 68.251  19.031  -5.916  1.00 10.44 ? 314  GLU D CB  1 
ATOM   10326 C  CG  . GLU D  1 314 ? 67.982  17.847  -5.094  1.00 15.36 ? 314  GLU D CG  1 
ATOM   10327 C  CD  . GLU D  1 314 ? 66.533  17.746  -4.674  1.00 20.59 ? 314  GLU D CD  1 
ATOM   10328 O  OE1 . GLU D  1 314 ? 65.650  18.215  -5.416  1.00 22.97 ? 314  GLU D OE1 1 
ATOM   10329 O  OE2 . GLU D  1 314 ? 66.292  17.209  -3.577  1.00 23.03 ? 314  GLU D OE2 1 
ATOM   10330 N  N   . ALA D  1 315 ? 70.131  21.293  -4.536  1.00 6.31  ? 315  ALA D N   1 
ATOM   10331 C  CA  . ALA D  1 315 ? 71.110  21.677  -3.512  1.00 6.35  ? 315  ALA D CA  1 
ATOM   10332 C  C   . ALA D  1 315 ? 70.619  22.954  -2.851  1.00 5.75  ? 315  ALA D C   1 
ATOM   10333 O  O   . ALA D  1 315 ? 69.883  23.715  -3.474  1.00 6.32  ? 315  ALA D O   1 
ATOM   10334 C  CB  . ALA D  1 315 ? 72.511  21.931  -4.111  1.00 6.08  ? 315  ALA D CB  1 
ATOM   10335 N  N   . TYR D  1 316 ? 71.017  23.178  -1.604  1.00 5.10  ? 316  TYR D N   1 
ATOM   10336 C  CA  . TYR D  1 316 ? 70.611  24.377  -0.901  1.00 6.53  ? 316  TYR D CA  1 
ATOM   10337 C  C   . TYR D  1 316 ? 71.132  25.632  -1.574  1.00 7.67  ? 316  TYR D C   1 
ATOM   10338 O  O   . TYR D  1 316 ? 70.521  26.684  -1.444  1.00 8.09  ? 316  TYR D O   1 
ATOM   10339 C  CB  . TYR D  1 316 ? 71.053  24.342  0.572   1.00 4.17  ? 316  TYR D CB  1 
ATOM   10340 C  CG  . TYR D  1 316 ? 70.288  23.347  1.412   1.00 2.38  ? 316  TYR D CG  1 
ATOM   10341 C  CD1 . TYR D  1 316 ? 68.862  23.382  1.483   1.00 2.35  ? 316  TYR D CD1 1 
ATOM   10342 C  CD2 . TYR D  1 316 ? 70.954  22.387  2.161   1.00 2.31  ? 316  TYR D CD2 1 
ATOM   10343 C  CE1 . TYR D  1 316 ? 68.138  22.448  2.261   1.00 4.95  ? 316  TYR D CE1 1 
ATOM   10344 C  CE2 . TYR D  1 316 ? 70.237  21.453  2.910   1.00 5.13  ? 316  TYR D CE2 1 
ATOM   10345 C  CZ  . TYR D  1 316 ? 68.827  21.497  2.976   1.00 3.95  ? 316  TYR D CZ  1 
ATOM   10346 O  OH  . TYR D  1 316 ? 68.153  20.572  3.770   1.00 6.57  ? 316  TYR D OH  1 
ATOM   10347 N  N   . PHE D  1 317 ? 72.262  25.510  -2.267  1.00 8.51  ? 317  PHE D N   1 
ATOM   10348 C  CA  . PHE D  1 317 ? 72.797  26.609  -3.095  1.00 7.90  ? 317  PHE D CA  1 
ATOM   10349 C  C   . PHE D  1 317 ? 73.398  26.021  -4.373  1.00 8.96  ? 317  PHE D C   1 
ATOM   10350 O  O   . PHE D  1 317 ? 74.268  25.140  -4.318  1.00 9.08  ? 317  PHE D O   1 
ATOM   10351 C  CB  . PHE D  1 317 ? 73.843  27.406  -2.306  1.00 7.06  ? 317  PHE D CB  1 
ATOM   10352 C  CG  . PHE D  1 317 ? 74.572  28.465  -3.116  1.00 6.83  ? 317  PHE D CG  1 
ATOM   10353 C  CD1 . PHE D  1 317 ? 75.700  28.101  -3.869  1.00 7.47  ? 317  PHE D CD1 1 
ATOM   10354 C  CD2 . PHE D  1 317 ? 74.194  29.808  -3.080  1.00 8.79  ? 317  PHE D CD2 1 
ATOM   10355 C  CE1 . PHE D  1 317 ? 76.432  29.064  -4.627  1.00 9.85  ? 317  PHE D CE1 1 
ATOM   10356 C  CE2 . PHE D  1 317 ? 74.951  30.790  -3.799  1.00 10.74 ? 317  PHE D CE2 1 
ATOM   10357 C  CZ  . PHE D  1 317 ? 76.047  30.396  -4.582  1.00 9.57  ? 317  PHE D CZ  1 
ATOM   10358 N  N   . SER D  1 318 ? 72.963  26.514  -5.519  1.00 8.53  ? 318  SER D N   1 
ATOM   10359 C  CA  . SER D  1 318 ? 73.577  26.122  -6.803  1.00 8.51  ? 318  SER D CA  1 
ATOM   10360 C  C   . SER D  1 318 ? 73.946  27.358  -7.559  1.00 9.16  ? 318  SER D C   1 
ATOM   10361 O  O   . SER D  1 318 ? 73.390  28.436  -7.322  1.00 8.84  ? 318  SER D O   1 
ATOM   10362 C  CB  . SER D  1 318 ? 72.645  25.264  -7.657  1.00 8.01  ? 318  SER D CB  1 
ATOM   10363 O  OG  . SER D  1 318 ? 72.305  24.097  -6.958  1.00 9.07  ? 318  SER D OG  1 
ATOM   10364 N  N   . LYS D  1 319 ? 74.947  27.209  -8.418  1.00 9.58  ? 319  LYS D N   1 
ATOM   10365 C  CA  . LYS D  1 319 ? 75.364  28.299  -9.277  1.00 8.60  ? 319  LYS D CA  1 
ATOM   10366 C  C   . LYS D  1 319 ? 75.625  27.769  -10.676 1.00 8.68  ? 319  LYS D C   1 
ATOM   10367 O  O   . LYS D  1 319 ? 76.395  26.823  -10.841 1.00 8.53  ? 319  LYS D O   1 
ATOM   10368 C  CB  . LYS D  1 319 ? 76.628  29.024  -8.717  1.00 7.67  ? 319  LYS D CB  1 
ATOM   10369 C  CG  . LYS D  1 319 ? 77.105  30.222  -9.647  1.00 9.16  ? 319  LYS D CG  1 
ATOM   10370 C  CD  . LYS D  1 319 ? 78.378  30.973  -9.146  1.00 13.13 ? 319  LYS D CD  1 
ATOM   10371 C  CE  . LYS D  1 319 ? 79.657  30.189  -9.538  1.00 13.48 ? 319  LYS D CE  1 
ATOM   10372 N  NZ  . LYS D  1 319 ? 80.934  30.972  -9.196  1.00 13.74 ? 319  LYS D NZ  1 
ATOM   10373 N  N   . VAL D  1 320 ? 75.043  28.431  -11.677 1.00 8.40  ? 320  VAL D N   1 
ATOM   10374 C  CA  . VAL D  1 320 ? 75.215  28.028  -13.050 1.00 8.13  ? 320  VAL D CA  1 
ATOM   10375 C  C   . VAL D  1 320 ? 75.738  29.163  -13.935 1.00 9.63  ? 320  VAL D C   1 
ATOM   10376 O  O   . VAL D  1 320 ? 75.498  30.344  -13.654 1.00 8.97  ? 320  VAL D O   1 
ATOM   10377 C  CB  . VAL D  1 320 ? 73.908  27.481  -13.665 1.00 8.35  ? 320  VAL D CB  1 
ATOM   10378 C  CG1 . VAL D  1 320 ? 73.254  26.435  -12.798 1.00 4.89  ? 320  VAL D CG1 1 
ATOM   10379 C  CG2 . VAL D  1 320 ? 72.887  28.648  -14.024 1.00 5.97  ? 320  VAL D CG2 1 
ATOM   10380 N  N   . LEU D  1 321 ? 76.458  28.789  -14.989 1.00 9.61  ? 321  LEU D N   1 
ATOM   10381 C  CA  . LEU D  1 321 ? 76.814  29.712  -16.062 1.00 9.24  ? 321  LEU D CA  1 
ATOM   10382 C  C   . LEU D  1 321 ? 75.701  29.664  -17.146 1.00 10.16 ? 321  LEU D C   1 
ATOM   10383 O  O   . LEU D  1 321 ? 75.373  28.594  -17.660 1.00 9.23  ? 321  LEU D O   1 
ATOM   10384 C  CB  . LEU D  1 321 ? 78.170  29.361  -16.660 1.00 8.61  ? 321  LEU D CB  1 
ATOM   10385 C  CG  . LEU D  1 321 ? 78.660  30.253  -17.796 1.00 11.59 ? 321  LEU D CG  1 
ATOM   10386 C  CD1 . LEU D  1 321 ? 79.008  31.694  -17.339 1.00 8.28  ? 321  LEU D CD1 1 
ATOM   10387 C  CD2 . LEU D  1 321 ? 79.885  29.500  -18.441 1.00 9.78  ? 321  LEU D CD2 1 
ATOM   10388 N  N   . PHE D  1 322 ? 75.149  30.833  -17.467 1.00 7.80  ? 322  PHE D N   1 
ATOM   10389 C  CA  . PHE D  1 322 ? 73.948  30.877  -18.288 1.00 8.96  ? 322  PHE D CA  1 
ATOM   10390 C  C   . PHE D  1 322 ? 74.137  31.729  -19.531 1.00 7.89  ? 322  PHE D C   1 
ATOM   10391 O  O   . PHE D  1 322 ? 74.526  32.891  -19.409 1.00 9.18  ? 322  PHE D O   1 
ATOM   10392 C  CB  . PHE D  1 322 ? 72.829  31.528  -17.489 1.00 7.64  ? 322  PHE D CB  1 
ATOM   10393 C  CG  . PHE D  1 322 ? 71.579  31.715  -18.307 1.00 8.69  ? 322  PHE D CG  1 
ATOM   10394 C  CD1 . PHE D  1 322 ? 70.724  30.646  -18.518 1.00 6.71  ? 322  PHE D CD1 1 
ATOM   10395 C  CD2 . PHE D  1 322 ? 71.268  32.941  -18.866 1.00 8.81  ? 322  PHE D CD2 1 
ATOM   10396 C  CE1 . PHE D  1 322 ? 69.593  30.761  -19.342 1.00 4.68  ? 322  PHE D CE1 1 
ATOM   10397 C  CE2 . PHE D  1 322 ? 70.122  33.085  -19.642 1.00 8.63  ? 322  PHE D CE2 1 
ATOM   10398 C  CZ  . PHE D  1 322 ? 69.279  32.001  -19.878 1.00 8.44  ? 322  PHE D CZ  1 
ATOM   10399 N  N   . VAL D  1 323 ? 73.781  31.205  -20.692 1.00 7.24  ? 323  VAL D N   1 
ATOM   10400 C  CA  . VAL D  1 323 ? 73.818  31.990  -21.945 1.00 7.65  ? 323  VAL D CA  1 
ATOM   10401 C  C   . VAL D  1 323 ? 72.475  31.884  -22.631 1.00 8.02  ? 323  VAL D C   1 
ATOM   10402 O  O   . VAL D  1 323 ? 71.818  30.814  -22.550 1.00 7.81  ? 323  VAL D O   1 
ATOM   10403 C  CB  . VAL D  1 323 ? 74.955  31.511  -22.879 1.00 8.59  ? 323  VAL D CB  1 
ATOM   10404 C  CG1 . VAL D  1 323 ? 74.718  30.116  -23.297 1.00 10.35 ? 323  VAL D CG1 1 
ATOM   10405 C  CG2 . VAL D  1 323 ? 75.075  32.396  -24.135 1.00 7.66  ? 323  VAL D CG2 1 
ATOM   10406 N  N   . SER D  1 324 ? 72.074  32.993  -23.272 1.00 7.25  ? 324  SER D N   1 
ATOM   10407 C  CA  . SER D  1 324 ? 70.805  33.113  -23.940 1.00 8.15  ? 324  SER D CA  1 
ATOM   10408 C  C   . SER D  1 324 ? 70.953  33.930  -25.204 1.00 8.77  ? 324  SER D C   1 
ATOM   10409 O  O   . SER D  1 324 ? 71.558  35.020  -25.193 1.00 8.45  ? 324  SER D O   1 
ATOM   10410 C  CB  . SER D  1 324 ? 69.717  33.759  -23.050 1.00 6.66  ? 324  SER D CB  1 
ATOM   10411 O  OG  . SER D  1 324 ? 68.606  34.159  -23.841 1.00 5.95  ? 324  SER D OG  1 
ATOM   10412 N  N   . SER D  1 325 ? 70.346  33.408  -26.270 1.00 7.69  ? 325  SER D N   1 
ATOM   10413 C  CA  . SER D  1 325 ? 70.214  34.149  -27.505 1.00 8.21  ? 325  SER D CA  1 
ATOM   10414 C  C   . SER D  1 325 ? 68.975  35.034  -27.392 1.00 7.83  ? 325  SER D C   1 
ATOM   10415 O  O   . SER D  1 325 ? 67.873  34.558  -27.008 1.00 8.07  ? 325  SER D O   1 
ATOM   10416 C  CB  . SER D  1 325 ? 70.109  33.208  -28.712 1.00 7.35  ? 325  SER D CB  1 
ATOM   10417 O  OG  . SER D  1 325 ? 69.814  33.950  -29.917 1.00 11.64 ? 325  SER D OG  1 
ATOM   10418 N  N   . GLY D  1 326 ? 69.158  36.299  -27.725 1.00 8.55  ? 326  GLY D N   1 
ATOM   10419 C  CA  . GLY D  1 326 ? 68.077  37.298  -27.711 1.00 8.88  ? 326  GLY D CA  1 
ATOM   10420 C  C   . GLY D  1 326 ? 68.416  38.312  -26.652 1.00 11.19 ? 326  GLY D C   1 
ATOM   10421 O  O   . GLY D  1 326 ? 69.449  38.185  -25.980 1.00 10.62 ? 326  GLY D O   1 
ATOM   10422 N  N   . SER D  1 327 ? 67.592  39.358  -26.526 1.00 11.48 ? 327  SER D N   1 
ATOM   10423 C  CA  . SER D  1 327 ? 67.930  40.411  -25.580 1.00 12.94 ? 327  SER D CA  1 
ATOM   10424 C  C   . SER D  1 327 ? 67.214  40.204  -24.231 1.00 13.06 ? 327  SER D C   1 
ATOM   10425 O  O   . SER D  1 327 ? 67.567  40.841  -23.246 1.00 11.72 ? 327  SER D O   1 
ATOM   10426 C  CB  . SER D  1 327 ? 67.608  41.789  -26.168 1.00 12.40 ? 327  SER D CB  1 
ATOM   10427 O  OG  . SER D  1 327 ? 66.242  41.841  -26.521 1.00 16.04 ? 327  SER D OG  1 
ATOM   10428 N  N   . ASP D  1 328 ? 66.248  39.285  -24.194 1.00 13.72 ? 328  ASP D N   1 
ATOM   10429 C  CA  . ASP D  1 328 ? 65.325  39.201  -23.062 1.00 14.45 ? 328  ASP D CA  1 
ATOM   10430 C  C   . ASP D  1 328 ? 65.041  37.788  -22.576 1.00 13.25 ? 328  ASP D C   1 
ATOM   10431 O  O   . ASP D  1 328 ? 63.890  37.445  -22.291 1.00 13.68 ? 328  ASP D O   1 
ATOM   10432 C  CB  . ASP D  1 328 ? 64.020  39.889  -23.440 1.00 16.54 ? 328  ASP D CB  1 
ATOM   10433 C  CG  . ASP D  1 328 ? 64.136  41.391  -23.378 1.00 21.86 ? 328  ASP D CG  1 
ATOM   10434 O  OD1 . ASP D  1 328 ? 64.447  41.889  -22.267 1.00 27.74 ? 328  ASP D OD1 1 
ATOM   10435 O  OD2 . ASP D  1 328 ? 63.962  42.144  -24.374 1.00 27.15 ? 328  ASP D OD2 1 
ATOM   10436 N  N   . GLY D  1 329 ? 66.087  36.974  -22.495 1.00 11.66 ? 329  GLY D N   1 
ATOM   10437 C  CA  . GLY D  1 329 ? 66.002  35.597  -22.014 1.00 10.71 ? 329  GLY D CA  1 
ATOM   10438 C  C   . GLY D  1 329 ? 65.942  35.544  -20.481 1.00 10.30 ? 329  GLY D C   1 
ATOM   10439 O  O   . GLY D  1 329 ? 65.793  36.606  -19.811 1.00 9.06  ? 329  GLY D O   1 
ATOM   10440 N  N   . LEU D  1 330 ? 66.063  34.321  -19.931 1.00 8.25  ? 330  LEU D N   1 
ATOM   10441 C  CA  . LEU D  1 330 ? 65.836  34.105  -18.499 1.00 7.75  ? 330  LEU D CA  1 
ATOM   10442 C  C   . LEU D  1 330 ? 66.562  35.090  -17.563 1.00 8.44  ? 330  LEU D C   1 
ATOM   10443 O  O   . LEU D  1 330 ? 65.945  35.638  -16.644 1.00 7.72  ? 330  LEU D O   1 
ATOM   10444 C  CB  . LEU D  1 330 ? 66.248  32.709  -18.109 1.00 7.72  ? 330  LEU D CB  1 
ATOM   10445 C  CG  . LEU D  1 330 ? 66.049  32.326  -16.631 1.00 8.23  ? 330  LEU D CG  1 
ATOM   10446 C  CD1 . LEU D  1 330 ? 64.528  32.416  -16.216 1.00 6.56  ? 330  LEU D CD1 1 
ATOM   10447 C  CD2 . LEU D  1 330 ? 66.667  30.952  -16.412 1.00 6.48  ? 330  LEU D CD2 1 
ATOM   10448 N  N   . ASP D  1 331 ? 67.869  35.271  -17.767 1.00 7.61  ? 331  ASP D N   1 
ATOM   10449 C  CA  . ASP D  1 331 ? 68.639  36.088  -16.832 1.00 8.60  ? 331  ASP D CA  1 
ATOM   10450 C  C   . ASP D  1 331 ? 68.185  37.532  -16.754 1.00 8.60  ? 331  ASP D C   1 
ATOM   10451 O  O   . ASP D  1 331 ? 68.044  38.078  -15.649 1.00 9.71  ? 331  ASP D O   1 
ATOM   10452 C  CB  . ASP D  1 331 ? 70.175  35.917  -17.020 1.00 8.46  ? 331  ASP D CB  1 
ATOM   10453 C  CG  . ASP D  1 331 ? 70.684  36.368  -18.414 1.00 12.23 ? 331  ASP D CG  1 
ATOM   10454 O  OD1 . ASP D  1 331 ? 69.843  36.514  -19.356 1.00 9.57  ? 331  ASP D OD1 1 
ATOM   10455 O  OD2 . ASP D  1 331 ? 71.911  36.580  -18.629 1.00 11.56 ? 331  ASP D OD2 1 
ATOM   10456 N  N   . GLN D  1 332 ? 67.955  38.135  -17.912 1.00 7.37  ? 332  GLN D N   1 
ATOM   10457 C  CA  . GLN D  1 332 ? 67.465  39.509  -18.017 1.00 9.27  ? 332  GLN D CA  1 
ATOM   10458 C  C   . GLN D  1 332 ? 66.082  39.631  -17.409 1.00 9.12  ? 332  GLN D C   1 
ATOM   10459 O  O   . GLN D  1 332 ? 65.716  40.668  -16.822 1.00 7.56  ? 332  GLN D O   1 
ATOM   10460 C  CB  . GLN D  1 332 ? 67.382  39.960  -19.498 1.00 7.93  ? 332  GLN D CB  1 
ATOM   10461 C  CG  . GLN D  1 332 ? 67.285  41.505  -19.717 1.00 10.38 ? 332  GLN D CG  1 
ATOM   10462 C  CD  . GLN D  1 332 ? 68.409  42.302  -19.041 1.00 13.63 ? 332  GLN D CD  1 
ATOM   10463 O  OE1 . GLN D  1 332 ? 69.577  42.065  -19.290 1.00 15.97 ? 332  GLN D OE1 1 
ATOM   10464 N  NE2 . GLN D  1 332 ? 68.046  43.215  -18.172 1.00 13.59 ? 332  GLN D NE2 1 
ATOM   10465 N  N   . ASN D  1 333 ? 65.291  38.578  -17.594 1.00 8.78  ? 333  ASN D N   1 
ATOM   10466 C  CA  . ASN D  1 333 ? 63.947  38.556  -17.055 1.00 10.02 ? 333  ASN D CA  1 
ATOM   10467 C  C   . ASN D  1 333 ? 63.994  38.591  -15.524 1.00 9.44  ? 333  ASN D C   1 
ATOM   10468 O  O   . ASN D  1 333 ? 63.255  39.341  -14.882 1.00 8.28  ? 333  ASN D O   1 
ATOM   10469 C  CB  . ASN D  1 333 ? 63.188  37.313  -17.575 1.00 9.75  ? 333  ASN D CB  1 
ATOM   10470 C  CG  . ASN D  1 333 ? 61.781  37.264  -17.088 1.00 11.61 ? 333  ASN D CG  1 
ATOM   10471 O  OD1 . ASN D  1 333 ? 61.556  37.152  -15.881 1.00 13.32 ? 333  ASN D OD1 1 
ATOM   10472 N  ND2 . ASN D  1 333 ? 60.800  37.380  -18.007 1.00 7.18  ? 333  ASN D ND2 1 
ATOM   10473 N  N   . LEU D  1 334 ? 64.920  37.820  -14.962 1.00 10.09 ? 334  LEU D N   1 
ATOM   10474 C  CA  . LEU D  1 334 ? 65.026  37.728  -13.521 1.00 9.76  ? 334  LEU D CA  1 
ATOM   10475 C  C   . LEU D  1 334 ? 65.595  39.007  -12.956 1.00 9.35  ? 334  LEU D C   1 
ATOM   10476 O  O   . LEU D  1 334 ? 65.163  39.451  -11.884 1.00 10.31 ? 334  LEU D O   1 
ATOM   10477 C  CB  . LEU D  1 334 ? 65.900  36.539  -13.101 1.00 9.84  ? 334  LEU D CB  1 
ATOM   10478 C  CG  . LEU D  1 334 ? 65.303  35.146  -13.344 1.00 11.66 ? 334  LEU D CG  1 
ATOM   10479 C  CD1 . LEU D  1 334 ? 66.325  34.097  -12.930 1.00 9.72  ? 334  LEU D CD1 1 
ATOM   10480 C  CD2 . LEU D  1 334 ? 63.954  34.904  -12.630 1.00 9.76  ? 334  LEU D CD2 1 
ATOM   10481 N  N   . VAL D  1 335 ? 66.554  39.605  -13.664 1.00 8.71  ? 335  VAL D N   1 
ATOM   10482 C  CA  . VAL D  1 335 ? 67.084  40.917  -13.271 1.00 8.04  ? 335  VAL D CA  1 
ATOM   10483 C  C   . VAL D  1 335 ? 65.970  41.967  -13.279 1.00 8.49  ? 335  VAL D C   1 
ATOM   10484 O  O   . VAL D  1 335 ? 65.748  42.680  -12.300 1.00 7.67  ? 335  VAL D O   1 
ATOM   10485 C  CB  . VAL D  1 335 ? 68.254  41.363  -14.230 1.00 7.92  ? 335  VAL D CB  1 
ATOM   10486 C  CG1 . VAL D  1 335 ? 68.692  42.794  -13.968 1.00 8.08  ? 335  VAL D CG1 1 
ATOM   10487 C  CG2 . VAL D  1 335 ? 69.432  40.430  -14.036 1.00 5.25  ? 335  VAL D CG2 1 
ATOM   10488 N  N   . ASN D  1 336 ? 65.239  42.032  -14.382 1.00 8.88  ? 336  ASN D N   1 
ATOM   10489 C  CA  . ASN D  1 336 ? 64.172  43.014  -14.529 1.00 8.01  ? 336  ASN D CA  1 
ATOM   10490 C  C   . ASN D  1 336 ? 63.126  42.882  -13.435 1.00 8.04  ? 336  ASN D C   1 
ATOM   10491 O  O   . ASN D  1 336 ? 62.462  43.871  -13.064 1.00 6.00  ? 336  ASN D O   1 
ATOM   10492 C  CB  . ASN D  1 336 ? 63.496  42.845  -15.881 1.00 8.70  ? 336  ASN D CB  1 
ATOM   10493 C  CG  . ASN D  1 336 ? 64.382  43.316  -17.052 1.00 10.49 ? 336  ASN D CG  1 
ATOM   10494 O  OD1 . ASN D  1 336 ? 64.071  43.062  -18.222 1.00 18.19 ? 336  ASN D OD1 1 
ATOM   10495 N  ND2 . ASN D  1 336 ? 65.437  44.035  -16.744 1.00 10.41 ? 336  ASN D ND2 1 
ATOM   10496 N  N   . GLY D  1 337 ? 62.960  41.667  -12.919 1.00 6.44  ? 337  GLY D N   1 
ATOM   10497 C  CA  . GLY D  1 337 ? 61.904  41.444  -11.939 1.00 6.82  ? 337  GLY D CA  1 
ATOM   10498 C  C   . GLY D  1 337 ? 62.467  41.468  -10.542 1.00 6.93  ? 337  GLY D C   1 
ATOM   10499 O  O   . GLY D  1 337 ? 61.750  41.130  -9.564  1.00 7.21  ? 337  GLY D O   1 
ATOM   10500 N  N   . GLY D  1 338 ? 63.743  41.874  -10.454 1.00 5.93  ? 338  GLY D N   1 
ATOM   10501 C  CA  . GLY D  1 338 ? 64.548  41.786  -9.241  1.00 6.62  ? 338  GLY D CA  1 
ATOM   10502 C  C   . GLY D  1 338 ? 65.002  43.160  -8.769  1.00 8.33  ? 338  GLY D C   1 
ATOM   10503 O  O   . GLY D  1 338 ? 64.373  44.181  -9.122  1.00 6.82  ? 338  GLY D O   1 
ATOM   10504 N  N   . GLU D  1 339 ? 66.053  43.205  -7.956  1.00 8.62  ? 339  GLU D N   1 
ATOM   10505 C  CA  . GLU D  1 339 ? 66.523  44.465  -7.378  1.00 9.65  ? 339  GLU D CA  1 
ATOM   10506 C  C   . GLU D  1 339 ? 68.023  44.357  -7.274  1.00 10.84 ? 339  GLU D C   1 
ATOM   10507 O  O   . GLU D  1 339 ? 68.552  43.233  -7.205  1.00 10.53 ? 339  GLU D O   1 
ATOM   10508 C  CB  . GLU D  1 339 ? 65.939  44.660  -5.959  1.00 11.02 ? 339  GLU D CB  1 
ATOM   10509 C  CG  . GLU D  1 339 ? 66.235  43.455  -5.035  1.00 14.74 ? 339  GLU D CG  1 
ATOM   10510 C  CD  . GLU D  1 339 ? 65.502  43.493  -3.714  1.00 23.14 ? 339  GLU D CD  1 
ATOM   10511 O  OE1 . GLU D  1 339 ? 65.648  44.483  -2.947  1.00 25.24 ? 339  GLU D OE1 1 
ATOM   10512 O  OE2 . GLU D  1 339 ? 64.763  42.528  -3.444  1.00 26.60 ? 339  GLU D OE2 1 
ATOM   10513 N  N   . GLU D  1 340 ? 68.729  45.487  -7.227  1.00 10.83 ? 340  GLU D N   1 
ATOM   10514 C  CA  . GLU D  1 340 ? 70.186  45.415  -7.070  1.00 12.08 ? 340  GLU D CA  1 
ATOM   10515 C  C   . GLU D  1 340 ? 70.466  44.766  -5.741  1.00 10.98 ? 340  GLU D C   1 
ATOM   10516 O  O   . GLU D  1 340 ? 69.726  44.973  -4.787  1.00 9.85  ? 340  GLU D O   1 
ATOM   10517 C  CB  . GLU D  1 340 ? 70.831  46.806  -7.114  1.00 13.40 ? 340  GLU D CB  1 
ATOM   10518 C  CG  . GLU D  1 340 ? 70.589  47.494  -8.451  1.00 18.27 ? 340  GLU D CG  1 
ATOM   10519 C  CD  . GLU D  1 340 ? 71.223  48.871  -8.525  1.00 25.28 ? 340  GLU D CD  1 
ATOM   10520 O  OE1 . GLU D  1 340 ? 71.328  49.540  -7.464  1.00 24.15 ? 340  GLU D OE1 1 
ATOM   10521 O  OE2 . GLU D  1 340 ? 71.605  49.261  -9.655  1.00 27.34 ? 340  GLU D OE2 1 
ATOM   10522 N  N   . TRP D  1 341 ? 71.533  43.993  -5.678  1.00 10.38 ? 341  TRP D N   1 
ATOM   10523 C  CA  . TRP D  1 341 ? 71.806  43.201  -4.498  1.00 10.72 ? 341  TRP D CA  1 
ATOM   10524 C  C   . TRP D  1 341 ? 73.301  43.174  -4.281  1.00 11.82 ? 341  TRP D C   1 
ATOM   10525 O  O   . TRP D  1 341 ? 74.045  43.000  -5.241  1.00 13.91 ? 341  TRP D O   1 
ATOM   10526 C  CB  . TRP D  1 341 ? 71.240  41.791  -4.722  1.00 10.58 ? 341  TRP D CB  1 
ATOM   10527 C  CG  . TRP D  1 341 ? 71.381  40.903  -3.564  1.00 10.13 ? 341  TRP D CG  1 
ATOM   10528 C  CD1 . TRP D  1 341 ? 72.186  39.819  -3.475  1.00 8.70  ? 341  TRP D CD1 1 
ATOM   10529 C  CD2 . TRP D  1 341 ? 70.715  41.025  -2.313  1.00 9.45  ? 341  TRP D CD2 1 
ATOM   10530 N  NE1 . TRP D  1 341 ? 72.029  39.233  -2.250  1.00 8.05  ? 341  TRP D NE1 1 
ATOM   10531 C  CE2 . TRP D  1 341 ? 71.140  39.970  -1.515  1.00 8.67  ? 341  TRP D CE2 1 
ATOM   10532 C  CE3 . TRP D  1 341 ? 69.783  41.951  -1.780  1.00 10.31 ? 341  TRP D CE3 1 
ATOM   10533 C  CZ2 . TRP D  1 341 ? 70.690  39.791  -0.205  1.00 11.00 ? 341  TRP D CZ2 1 
ATOM   10534 C  CZ3 . TRP D  1 341 ? 69.323  41.764  -0.507  1.00 11.57 ? 341  TRP D CZ3 1 
ATOM   10535 C  CH2 . TRP D  1 341 ? 69.782  40.678  0.277   1.00 9.09  ? 341  TRP D CH2 1 
ATOM   10536 N  N   . SER D  1 342 ? 73.773  43.354  -3.054  1.00 10.84 ? 342  SER D N   1 
ATOM   10537 C  CA  . SER D  1 342 ? 75.217  43.519  -2.884  1.00 12.54 ? 342  SER D CA  1 
ATOM   10538 C  C   . SER D  1 342 ? 75.923  42.307  -2.300  1.00 13.58 ? 342  SER D C   1 
ATOM   10539 O  O   . SER D  1 342 ? 77.021  42.454  -1.738  1.00 16.95 ? 342  SER D O   1 
ATOM   10540 C  CB  . SER D  1 342 ? 75.522  44.738  -2.017  1.00 11.92 ? 342  SER D CB  1 
ATOM   10541 O  OG  A SER D  1 342 ? 75.160  45.929  -2.708  0.50 14.08 ? 342  SER D OG  1 
ATOM   10542 O  OG  B SER D  1 342 ? 75.074  44.508  -0.705  0.50 11.39 ? 342  SER D OG  1 
ATOM   10543 N  N   . SER D  1 343 ? 75.320  41.126  -2.392  1.00 11.84 ? 343  SER D N   1 
ATOM   10544 C  CA  . SER D  1 343 ? 75.952  39.964  -1.830  1.00 10.77 ? 343  SER D CA  1 
ATOM   10545 C  C   . SER D  1 343 ? 75.835  38.764  -2.768  1.00 9.69  ? 343  SER D C   1 
ATOM   10546 O  O   . SER D  1 343 ? 74.892  38.689  -3.578  1.00 9.70  ? 343  SER D O   1 
ATOM   10547 C  CB  . SER D  1 343 ? 75.325  39.653  -0.472  1.00 10.03 ? 343  SER D CB  1 
ATOM   10548 O  OG  . SER D  1 343 ? 75.996  38.562  0.133   1.00 10.28 ? 343  SER D OG  1 
ATOM   10549 N  N   . VAL D  1 344 ? 76.809  37.862  -2.705  1.00 9.14  ? 344  VAL D N   1 
ATOM   10550 C  CA  . VAL D  1 344 ? 76.686  36.560  -3.389  1.00 8.68  ? 344  VAL D CA  1 
ATOM   10551 C  C   . VAL D  1 344 ? 75.745  35.568  -2.667  1.00 8.84  ? 344  VAL D C   1 
ATOM   10552 O  O   . VAL D  1 344 ? 75.410  34.485  -3.220  1.00 8.71  ? 344  VAL D O   1 
ATOM   10553 C  CB  . VAL D  1 344 ? 78.070  35.853  -3.632  1.00 8.70  ? 344  VAL D CB  1 
ATOM   10554 C  CG1 . VAL D  1 344 ? 78.878  36.544  -4.727  1.00 10.03 ? 344  VAL D CG1 1 
ATOM   10555 C  CG2 . VAL D  1 344 ? 78.852  35.689  -2.307  1.00 8.14  ? 344  VAL D CG2 1 
ATOM   10556 N  N   . SER D  1 345 ? 75.374  35.894  -1.436  1.00 7.82  ? 345  SER D N   1 
ATOM   10557 C  CA  . SER D  1 345 ? 74.471  35.065  -0.681  1.00 8.31  ? 345  SER D CA  1 
ATOM   10558 C  C   . SER D  1 345 ? 73.095  35.700  -0.694  1.00 8.69  ? 345  SER D C   1 
ATOM   10559 O  O   . SER D  1 345 ? 73.009  36.930  -0.732  1.00 8.82  ? 345  SER D O   1 
ATOM   10560 C  CB  . SER D  1 345 ? 74.966  35.001  0.753   1.00 10.04 ? 345  SER D CB  1 
ATOM   10561 O  OG  . SER D  1 345 ? 75.898  33.938  0.845   1.00 12.63 ? 345  SER D OG  1 
ATOM   10562 N  N   . PHE D  1 346 ? 72.033  34.889  -0.692  1.00 8.03  ? 346  PHE D N   1 
ATOM   10563 C  CA  . PHE D  1 346 ? 70.667  35.420  -0.637  1.00 6.98  ? 346  PHE D CA  1 
ATOM   10564 C  C   . PHE D  1 346 ? 70.214  35.594  0.831   1.00 6.44  ? 346  PHE D C   1 
ATOM   10565 O  O   . PHE D  1 346 ? 70.938  35.180  1.746   1.00 7.63  ? 346  PHE D O   1 
ATOM   10566 C  CB  . PHE D  1 346 ? 69.711  34.534  -1.486  1.00 7.99  ? 346  PHE D CB  1 
ATOM   10567 C  CG  . PHE D  1 346 ? 69.899  33.035  -1.280  1.00 8.30  ? 346  PHE D CG  1 
ATOM   10568 C  CD1 . PHE D  1 346 ? 69.381  32.408  -0.152  1.00 7.44  ? 346  PHE D CD1 1 
ATOM   10569 C  CD2 . PHE D  1 346 ? 70.583  32.266  -2.230  1.00 4.80  ? 346  PHE D CD2 1 
ATOM   10570 C  CE1 . PHE D  1 346 ? 69.528  31.035  0.061   1.00 7.84  ? 346  PHE D CE1 1 
ATOM   10571 C  CE2 . PHE D  1 346 ? 70.788  30.844  -2.045  1.00 8.10  ? 346  PHE D CE2 1 
ATOM   10572 C  CZ  . PHE D  1 346 ? 70.266  30.226  -0.885  1.00 8.58  ? 346  PHE D CZ  1 
ATOM   10573 N  N   . PRO D  1 347 ? 69.071  36.232  1.092   1.00 5.33  ? 347  PRO D N   1 
ATOM   10574 C  CA  . PRO D  1 347 ? 68.632  36.444  2.477   1.00 5.96  ? 347  PRO D CA  1 
ATOM   10575 C  C   . PRO D  1 347 ? 68.421  35.146  3.270   1.00 5.73  ? 347  PRO D C   1 
ATOM   10576 O  O   . PRO D  1 347 ? 68.146  34.111  2.668   1.00 6.67  ? 347  PRO D O   1 
ATOM   10577 C  CB  . PRO D  1 347 ? 67.332  37.252  2.312   1.00 6.53  ? 347  PRO D CB  1 
ATOM   10578 C  CG  . PRO D  1 347 ? 67.476  37.911  1.003   1.00 4.44  ? 347  PRO D CG  1 
ATOM   10579 C  CD  . PRO D  1 347 ? 68.171  36.903  0.131   1.00 4.55  ? 347  PRO D CD  1 
ATOM   10580 N  N   . ALA D  1 348 ? 68.575  35.223  4.585   1.00 5.36  ? 348  ALA D N   1 
ATOM   10581 C  CA  . ALA D  1 348 ? 68.485  34.059  5.464   1.00 4.97  ? 348  ALA D CA  1 
ATOM   10582 C  C   . ALA D  1 348 ? 67.048  33.667  5.704   1.00 5.49  ? 348  ALA D C   1 
ATOM   10583 O  O   . ALA D  1 348 ? 66.792  32.537  6.139   1.00 4.13  ? 348  ALA D O   1 
ATOM   10584 C  CB  . ALA D  1 348 ? 69.196  34.343  6.822   1.00 4.84  ? 348  ALA D CB  1 
ATOM   10585 N  N   . ASP D  1 349 ? 66.113  34.594  5.437   1.00 4.74  ? 349  ASP D N   1 
ATOM   10586 C  CA  . ASP D  1 349 ? 64.696  34.295  5.567   1.00 6.05  ? 349  ASP D CA  1 
ATOM   10587 C  C   . ASP D  1 349 ? 63.953  34.417  4.248   1.00 5.92  ? 349  ASP D C   1 
ATOM   10588 O  O   . ASP D  1 349 ? 64.312  35.251  3.399   1.00 5.49  ? 349  ASP D O   1 
ATOM   10589 C  CB  . ASP D  1 349 ? 64.030  35.252  6.554   1.00 7.85  ? 349  ASP D CB  1 
ATOM   10590 C  CG  . ASP D  1 349 ? 64.802  35.409  7.841   1.00 9.93  ? 349  ASP D CG  1 
ATOM   10591 O  OD1 . ASP D  1 349 ? 64.881  34.446  8.622   1.00 7.75  ? 349  ASP D OD1 1 
ATOM   10592 O  OD2 . ASP D  1 349 ? 65.360  36.474  8.133   1.00 14.26 ? 349  ASP D OD2 1 
ATOM   10593 N  N   . TRP D  1 350 ? 62.887  33.627  4.090   1.00 5.73  ? 350  TRP D N   1 
ATOM   10594 C  CA  . TRP D  1 350 ? 62.033  33.702  2.891   1.00 5.67  ? 350  TRP D CA  1 
ATOM   10595 C  C   . TRP D  1 350 ? 61.219  35.005  2.919   1.00 7.29  ? 350  TRP D C   1 
ATOM   10596 O  O   . TRP D  1 350 ? 60.745  35.374  1.839   1.00 8.76  ? 350  TRP D O   1 
ATOM   10597 C  CB  . TRP D  1 350 ? 61.058  32.528  2.833   1.00 5.75  ? 350  TRP D CB  1 
ATOM   10598 C  CG  . TRP D  1 350 ? 61.733  31.181  2.731   1.00 5.94  ? 350  TRP D CG  1 
ATOM   10599 C  CD1 . TRP D  1 350 ? 61.708  30.203  3.677   1.00 8.83  ? 350  TRP D CD1 1 
ATOM   10600 C  CD2 . TRP D  1 350 ? 62.605  30.691  1.679   1.00 9.26  ? 350  TRP D CD2 1 
ATOM   10601 N  NE1 . TRP D  1 350 ? 62.473  29.126  3.283   1.00 7.31  ? 350  TRP D NE1 1 
ATOM   10602 C  CE2 . TRP D  1 350 ? 63.010  29.375  2.051   1.00 7.74  ? 350  TRP D CE2 1 
ATOM   10603 C  CE3 . TRP D  1 350 ? 63.032  31.192  0.433   1.00 5.31  ? 350  TRP D CE3 1 
ATOM   10604 C  CZ2 . TRP D  1 350 ? 63.843  28.576  1.249   1.00 6.55  ? 350  TRP D CZ2 1 
ATOM   10605 C  CZ3 . TRP D  1 350 ? 63.867  30.400  -0.360  1.00 5.53  ? 350  TRP D CZ3 1 
ATOM   10606 C  CH2 . TRP D  1 350 ? 64.282  29.104  0.068   1.00 5.96  ? 350  TRP D CH2 1 
ATOM   10607 O  OXT . TRP D  1 350 ? 61.044  35.625  3.992   1.00 5.56  ? 350  TRP D OXT 1 
HETATM 10608 C  C1  . NAG E  2 .   ? 50.984  3.947   80.765  1.00 26.82 ? 1351 NAG A C1  1 
HETATM 10609 C  C2  . NAG E  2 .   ? 49.555  4.514   80.718  1.00 29.34 ? 1351 NAG A C2  1 
HETATM 10610 C  C3  . NAG E  2 .   ? 49.031  4.918   82.114  1.00 33.25 ? 1351 NAG A C3  1 
HETATM 10611 C  C4  . NAG E  2 .   ? 49.289  3.806   83.148  1.00 34.53 ? 1351 NAG A C4  1 
HETATM 10612 C  C5  . NAG E  2 .   ? 50.788  3.450   83.103  1.00 34.81 ? 1351 NAG A C5  1 
HETATM 10613 C  C6  . NAG E  2 .   ? 51.226  2.407   84.120  1.00 36.33 ? 1351 NAG A C6  1 
HETATM 10614 C  C7  . NAG E  2 .   ? 49.046  5.474   78.548  1.00 30.69 ? 1351 NAG A C7  1 
HETATM 10615 C  C8  . NAG E  2 .   ? 48.879  6.731   77.757  1.00 30.42 ? 1351 NAG A C8  1 
HETATM 10616 N  N2  . NAG E  2 .   ? 49.460  5.645   79.800  1.00 29.59 ? 1351 NAG A N2  1 
HETATM 10617 O  O3  . NAG E  2 .   ? 47.652  5.222   82.023  1.00 33.95 ? 1351 NAG A O3  1 
HETATM 10618 O  O4  . NAG E  2 .   ? 48.946  4.249   84.445  1.00 39.13 ? 1351 NAG A O4  1 
HETATM 10619 O  O5  . NAG E  2 .   ? 51.077  2.968   81.795  1.00 32.23 ? 1351 NAG A O5  1 
HETATM 10620 O  O6  . NAG E  2 .   ? 50.420  1.279   83.830  1.00 39.39 ? 1351 NAG A O6  1 
HETATM 10621 O  O7  . NAG E  2 .   ? 48.823  4.362   78.034  1.00 28.06 ? 1351 NAG A O7  1 
HETATM 10622 C  C1  . NAG F  2 .   ? 69.050  -8.933  52.639  1.00 19.24 ? 1352 NAG A C1  1 
HETATM 10623 C  C2  . NAG F  2 .   ? 68.253  -10.215 52.278  1.00 25.89 ? 1352 NAG A C2  1 
HETATM 10624 C  C3  . NAG F  2 .   ? 68.767  -10.950 51.014  1.00 25.79 ? 1352 NAG A C3  1 
HETATM 10625 C  C4  . NAG F  2 .   ? 68.807  -9.944  49.864  1.00 24.65 ? 1352 NAG A C4  1 
HETATM 10626 C  C5  . NAG F  2 .   ? 69.544  -8.657  50.316  1.00 24.28 ? 1352 NAG A C5  1 
HETATM 10627 C  C6  . NAG F  2 .   ? 69.425  -7.564  49.260  1.00 23.32 ? 1352 NAG A C6  1 
HETATM 10628 C  C7  . NAG F  2 .   ? 67.246  -11.318 54.182  1.00 26.48 ? 1352 NAG A C7  1 
HETATM 10629 C  C8  . NAG F  2 .   ? 67.345  -12.465 55.149  1.00 25.90 ? 1352 NAG A C8  1 
HETATM 10630 N  N2  . NAG F  2 .   ? 68.300  -11.128 53.400  1.00 25.51 ? 1352 NAG A N2  1 
HETATM 10631 O  O3  . NAG F  2 .   ? 67.949  -12.070 50.698  1.00 28.89 ? 1352 NAG A O3  1 
HETATM 10632 O  O4  . NAG F  2 .   ? 69.507  -10.439 48.741  1.00 24.18 ? 1352 NAG A O4  1 
HETATM 10633 O  O5  . NAG F  2 .   ? 68.996  -8.081  51.508  1.00 22.17 ? 1352 NAG A O5  1 
HETATM 10634 O  O6  . NAG F  2 .   ? 70.459  -6.648  49.572  1.00 25.50 ? 1352 NAG A O6  1 
HETATM 10635 O  O7  . NAG F  2 .   ? 66.239  -10.620 54.118  1.00 30.23 ? 1352 NAG A O7  1 
HETATM 10636 C  C1  . NAG G  2 .   ? 68.663  -10.994 47.708  1.00 27.53 ? 1353 NAG A C1  1 
HETATM 10637 C  C2  . NAG G  2 .   ? 69.397  -10.947 46.371  1.00 29.19 ? 1353 NAG A C2  1 
HETATM 10638 C  C3  . NAG G  2 .   ? 68.515  -11.524 45.267  1.00 32.63 ? 1353 NAG A C3  1 
HETATM 10639 C  C4  . NAG G  2 .   ? 68.010  -12.921 45.657  1.00 35.15 ? 1353 NAG A C4  1 
HETATM 10640 C  C5  . NAG G  2 .   ? 67.441  -12.958 47.093  1.00 32.37 ? 1353 NAG A C5  1 
HETATM 10641 C  C6  . NAG G  2 .   ? 67.195  -14.393 47.568  1.00 32.35 ? 1353 NAG A C6  1 
HETATM 10642 C  C7  . NAG G  2 .   ? 71.002  -9.143  46.046  1.00 28.59 ? 1353 NAG A C7  1 
HETATM 10643 C  C8  . NAG G  2 .   ? 71.201  -7.776  45.451  1.00 26.09 ? 1353 NAG A C8  1 
HETATM 10644 N  N2  . NAG G  2 .   ? 69.743  -9.572  46.029  1.00 27.92 ? 1353 NAG A N2  1 
HETATM 10645 O  O3  . NAG G  2 .   ? 69.216  -11.503 44.031  1.00 31.42 ? 1353 NAG A O3  1 
HETATM 10646 O  O4  . NAG G  2 .   ? 66.971  -13.239 44.767  1.00 39.78 ? 1353 NAG A O4  1 
HETATM 10647 O  O5  . NAG G  2 .   ? 68.348  -12.332 47.986  1.00 28.35 ? 1353 NAG A O5  1 
HETATM 10648 O  O6  . NAG G  2 .   ? 68.438  -15.082 47.754  1.00 33.08 ? 1353 NAG A O6  1 
HETATM 10649 O  O7  . NAG G  2 .   ? 71.960  -9.773  46.524  1.00 24.84 ? 1353 NAG A O7  1 
HETATM 10650 C  C1  . BMA H  3 .   ? 67.236  -14.504 44.146  1.00 45.62 ? 1357 BMA A C1  1 
HETATM 10651 C  C2  . BMA H  3 .   ? 65.937  -15.087 43.579  1.00 47.17 ? 1357 BMA A C2  1 
HETATM 10652 C  C3  . BMA H  3 .   ? 66.217  -16.379 42.774  1.00 49.62 ? 1357 BMA A C3  1 
HETATM 10653 C  C4  . BMA H  3 .   ? 67.399  -16.183 41.826  1.00 50.92 ? 1357 BMA A C4  1 
HETATM 10654 C  C5  . BMA H  3 .   ? 68.589  -15.629 42.622  1.00 51.90 ? 1357 BMA A C5  1 
HETATM 10655 C  C6  . BMA H  3 .   ? 69.827  -15.378 41.777  1.00 54.87 ? 1357 BMA A C6  1 
HETATM 10656 O  O2  . BMA H  3 .   ? 65.290  -14.081 42.820  1.00 48.17 ? 1357 BMA A O2  1 
HETATM 10657 O  O3  . BMA H  3 .   ? 65.072  -16.899 42.097  1.00 48.70 ? 1357 BMA A O3  1 
HETATM 10658 O  O4  . BMA H  3 .   ? 67.749  -17.416 41.256  1.00 53.19 ? 1357 BMA A O4  1 
HETATM 10659 O  O5  . BMA H  3 .   ? 68.213  -14.375 43.148  1.00 48.85 ? 1357 BMA A O5  1 
HETATM 10660 O  O6  . BMA H  3 .   ? 69.428  -14.493 40.750  1.00 58.35 ? 1357 BMA A O6  1 
HETATM 10661 C  C1  . MAN I  4 .   ? 70.399  -14.517 39.687  1.00 60.51 ? 1358 MAN A C1  1 
HETATM 10662 C  C2  . MAN I  4 .   ? 70.131  -13.283 38.834  1.00 62.09 ? 1358 MAN A C2  1 
HETATM 10663 C  C3  . MAN I  4 .   ? 68.852  -13.507 38.019  1.00 62.80 ? 1358 MAN A C3  1 
HETATM 10664 C  C4  . MAN I  4 .   ? 68.930  -14.777 37.177  1.00 62.08 ? 1358 MAN A C4  1 
HETATM 10665 C  C5  . MAN I  4 .   ? 69.255  -15.973 38.086  1.00 61.88 ? 1358 MAN A C5  1 
HETATM 10666 C  C6  . MAN I  4 .   ? 69.411  -17.301 37.323  1.00 61.97 ? 1358 MAN A C6  1 
HETATM 10667 O  O2  . MAN I  4 .   ? 71.257  -13.015 38.023  1.00 60.60 ? 1358 MAN A O2  1 
HETATM 10668 O  O3  . MAN I  4 .   ? 68.621  -12.401 37.185  1.00 65.65 ? 1358 MAN A O3  1 
HETATM 10669 O  O4  . MAN I  4 .   ? 67.688  -14.918 36.532  1.00 61.22 ? 1358 MAN A O4  1 
HETATM 10670 O  O5  . MAN I  4 .   ? 70.408  -15.701 38.891  1.00 61.39 ? 1358 MAN A O5  1 
HETATM 10671 O  O6  . MAN I  4 .   ? 70.702  -17.492 36.773  1.00 61.63 ? 1358 MAN A O6  1 
HETATM 10672 C  C1  . MAN J  4 .   ? 67.387  -11.751 37.532  1.00 67.35 ? 1359 MAN A C1  1 
HETATM 10673 C  C2  . MAN J  4 .   ? 66.832  -11.154 36.241  1.00 68.43 ? 1359 MAN A C2  1 
HETATM 10674 C  C3  . MAN J  4 .   ? 67.804  -10.077 35.719  1.00 68.46 ? 1359 MAN A C3  1 
HETATM 10675 C  C4  . MAN J  4 .   ? 68.208  -9.066  36.822  1.00 68.50 ? 1359 MAN A C4  1 
HETATM 10676 C  C5  . MAN J  4 .   ? 68.566  -9.780  38.148  1.00 67.90 ? 1359 MAN A C5  1 
HETATM 10677 C  C6  . MAN J  4 .   ? 68.808  -8.829  39.326  1.00 67.77 ? 1359 MAN A C6  1 
HETATM 10678 O  O2  . MAN J  4 .   ? 65.528  -10.656 36.478  1.00 69.48 ? 1359 MAN A O2  1 
HETATM 10679 O  O3  . MAN J  4 .   ? 67.286  -9.466  34.544  1.00 68.47 ? 1359 MAN A O3  1 
HETATM 10680 O  O4  . MAN J  4 .   ? 69.292  -8.238  36.407  1.00 67.83 ? 1359 MAN A O4  1 
HETATM 10681 O  O5  . MAN J  4 .   ? 67.571  -10.733 38.501  1.00 68.00 ? 1359 MAN A O5  1 
HETATM 10682 O  O6  . MAN J  4 .   ? 70.149  -8.965  39.744  1.00 68.18 ? 1359 MAN A O6  1 
HETATM 10683 C  C1  . NAG K  2 .   ? 45.458  20.833  71.075  1.00 26.10 ? 1354 NAG A C1  1 
HETATM 10684 C  C2  . NAG K  2 .   ? 44.476  21.320  72.160  1.00 32.95 ? 1354 NAG A C2  1 
HETATM 10685 C  C3  . NAG K  2 .   ? 43.896  22.718  71.887  1.00 33.38 ? 1354 NAG A C3  1 
HETATM 10686 C  C4  . NAG K  2 .   ? 44.949  23.703  71.364  1.00 30.99 ? 1354 NAG A C4  1 
HETATM 10687 C  C5  . NAG K  2 .   ? 45.807  23.050  70.267  1.00 26.48 ? 1354 NAG A C5  1 
HETATM 10688 C  C6  . NAG K  2 .   ? 46.953  23.958  69.777  1.00 22.45 ? 1354 NAG A C6  1 
HETATM 10689 C  C7  . NAG K  2 .   ? 43.247  19.810  73.559  1.00 39.75 ? 1354 NAG A C7  1 
HETATM 10690 C  C8  . NAG K  2 .   ? 42.109  18.835  73.761  1.00 41.24 ? 1354 NAG A C8  1 
HETATM 10691 N  N2  . NAG K  2 .   ? 43.348  20.414  72.372  1.00 35.25 ? 1354 NAG A N2  1 
HETATM 10692 O  O3  . NAG K  2 .   ? 43.312  23.186  73.094  1.00 34.07 ? 1354 NAG A O3  1 
HETATM 10693 O  O4  . NAG K  2 .   ? 44.320  24.853  70.864  1.00 32.83 ? 1354 NAG A O4  1 
HETATM 10694 O  O5  . NAG K  2 .   ? 46.377  21.907  70.856  1.00 23.14 ? 1354 NAG A O5  1 
HETATM 10695 O  O6  . NAG K  2 .   ? 47.849  24.270  70.834  1.00 20.92 ? 1354 NAG A O6  1 
HETATM 10696 O  O7  . NAG K  2 .   ? 44.044  20.014  74.480  1.00 41.04 ? 1354 NAG A O7  1 
HETATM 10697 C  C1  . NAG L  2 .   ? 48.584  -8.905  77.478  1.00 35.24 ? 1355 NAG A C1  1 
HETATM 10698 C  C2  . NAG L  2 .   ? 47.148  -8.410  77.810  1.00 36.50 ? 1355 NAG A C2  1 
HETATM 10699 C  C3  . NAG L  2 .   ? 46.941  -8.442  79.339  1.00 40.23 ? 1355 NAG A C3  1 
HETATM 10700 C  C4  . NAG L  2 .   ? 47.208  -9.854  79.897  1.00 41.18 ? 1355 NAG A C4  1 
HETATM 10701 C  C5  . NAG L  2 .   ? 48.570  -10.384 79.409  1.00 40.33 ? 1355 NAG A C5  1 
HETATM 10702 C  C6  . NAG L  2 .   ? 48.726  -11.870 79.770  1.00 44.36 ? 1355 NAG A C6  1 
HETATM 10703 C  C7  . NAG L  2 .   ? 45.771  -6.701  76.619  1.00 31.39 ? 1355 NAG A C7  1 
HETATM 10704 C  C8  . NAG L  2 .   ? 45.760  -5.423  75.875  1.00 37.02 ? 1355 NAG A C8  1 
HETATM 10705 N  N2  . NAG L  2 .   ? 46.876  -7.042  77.310  1.00 36.84 ? 1355 NAG A N2  1 
HETATM 10706 O  O3  . NAG L  2 .   ? 45.670  -7.916  79.725  1.00 40.07 ? 1355 NAG A O3  1 
HETATM 10707 O  O4  . NAG L  2 .   ? 47.162  -9.908  81.314  1.00 42.19 ? 1355 NAG A O4  1 
HETATM 10708 O  O5  . NAG L  2 .   ? 48.724  -10.221 77.991  1.00 37.56 ? 1355 NAG A O5  1 
HETATM 10709 O  O6  . NAG L  2 .   ? 49.998  -12.129 80.345  1.00 46.55 ? 1355 NAG A O6  1 
HETATM 10710 O  O7  . NAG L  2 .   ? 44.774  -7.378  76.559  1.00 28.74 ? 1355 NAG A O7  1 
HETATM 10711 C  C1  . NAG M  2 .   ? 80.372  21.679  83.812  1.00 26.20 ? 1356 NAG A C1  1 
HETATM 10712 C  C2  . NAG M  2 .   ? 80.407  21.007  85.202  1.00 30.09 ? 1356 NAG A C2  1 
HETATM 10713 C  C3  . NAG M  2 .   ? 81.869  20.770  85.647  1.00 32.97 ? 1356 NAG A C3  1 
HETATM 10714 C  C4  . NAG M  2 .   ? 82.707  20.002  84.583  1.00 35.33 ? 1356 NAG A C4  1 
HETATM 10715 C  C5  . NAG M  2 .   ? 82.607  20.774  83.260  1.00 35.89 ? 1356 NAG A C5  1 
HETATM 10716 C  C6  . NAG M  2 .   ? 83.379  20.164  82.068  1.00 36.23 ? 1356 NAG A C6  1 
HETATM 10717 C  C7  . NAG M  2 .   ? 80.027  22.908  86.727  1.00 31.99 ? 1356 NAG A C7  1 
HETATM 10718 C  C8  . NAG M  2 .   ? 79.476  23.284  88.084  1.00 30.19 ? 1356 NAG A C8  1 
HETATM 10719 N  N2  . NAG M  2 .   ? 79.607  21.743  86.204  1.00 27.42 ? 1356 NAG A N2  1 
HETATM 10720 O  O3  . NAG M  2 .   ? 81.821  20.063  86.855  1.00 33.84 ? 1356 NAG A O3  1 
HETATM 10721 O  O4  . NAG M  2 .   ? 84.073  19.882  84.973  1.00 39.02 ? 1356 NAG A O4  1 
HETATM 10722 O  O5  . NAG M  2 .   ? 81.223  20.974  82.903  1.00 35.77 ? 1356 NAG A O5  1 
HETATM 10723 O  O6  . NAG M  2 .   ? 82.765  20.575  80.839  1.00 35.99 ? 1356 NAG A O6  1 
HETATM 10724 O  O7  . NAG M  2 .   ? 80.831  23.674  86.145  1.00 34.30 ? 1356 NAG A O7  1 
HETATM 10725 C  C1  . KMP N  5 .   ? 69.013  8.475   79.787  1.00 13.70 ? 1360 KMP A C1  1 
HETATM 10726 C  C2  . KMP N  5 .   ? 67.633  8.488   79.449  1.00 13.29 ? 1360 KMP A C2  1 
HETATM 10727 C  C3  . KMP N  5 .   ? 67.256  8.653   78.027  1.00 16.03 ? 1360 KMP A C3  1 
HETATM 10728 C  C4  . KMP N  5 .   ? 68.299  8.871   77.016  1.00 15.35 ? 1360 KMP A C4  1 
HETATM 10729 C  C5  . KMP N  5 .   ? 69.612  8.872   77.430  1.00 14.04 ? 1360 KMP A C5  1 
HETATM 10730 C  C6  . KMP N  5 .   ? 69.970  8.683   78.770  1.00 13.07 ? 1360 KMP A C6  1 
HETATM 10731 C  C9  . KMP N  5 .   ? 65.846  8.677   77.557  1.00 17.76 ? 1360 KMP A C9  1 
HETATM 10732 C  C10 . KMP N  5 .   ? 65.568  8.882   76.124  1.00 19.37 ? 1360 KMP A C10 1 
HETATM 10733 C  C11 . KMP N  5 .   ? 66.598  9.071   75.236  1.00 16.30 ? 1360 KMP A C11 1 
HETATM 10734 C  C14 . KMP N  5 .   ? 66.496  9.672   73.840  1.00 15.07 ? 1360 KMP A C14 1 
HETATM 10735 C  C15 . KMP N  5 .   ? 67.674  10.137  73.250  1.00 14.18 ? 1360 KMP A C15 1 
HETATM 10736 C  C16 . KMP N  5 .   ? 67.720  10.693  71.982  1.00 11.80 ? 1360 KMP A C16 1 
HETATM 10737 C  C17 . KMP N  5 .   ? 66.492  10.786  71.303  1.00 13.17 ? 1360 KMP A C17 1 
HETATM 10738 C  C18 . KMP N  5 .   ? 65.307  10.310  71.867  1.00 13.64 ? 1360 KMP A C18 1 
HETATM 10739 C  C19 . KMP N  5 .   ? 65.289  9.767   73.147  1.00 15.38 ? 1360 KMP A C19 1 
HETATM 10740 O  O12 . KMP N  5 .   ? 67.957  9.033   75.712  1.00 15.34 ? 1360 KMP A O12 1 
HETATM 10741 O  O13 . KMP N  5 .   ? 64.991  8.537   78.418  1.00 19.99 ? 1360 KMP A O13 1 
HETATM 10742 O  O24 . KMP N  5 .   ? 66.462  11.296  70.092  1.00 13.57 ? 1360 KMP A O24 1 
HETATM 10743 O  O27 . KMP N  5 .   ? 64.293  8.850   75.723  1.00 20.13 ? 1360 KMP A O27 1 
HETATM 10744 O  O29 . KMP N  5 .   ? 71.275  8.693   79.011  1.00 13.50 ? 1360 KMP A O29 1 
HETATM 10745 O  O30 . KMP N  5 .   ? 66.667  8.308   80.365  1.00 16.56 ? 1360 KMP A O30 1 
HETATM 10746 CU CU  . CU  O  6 .   ? 63.164  7.220   75.841  1.00 9.41  ? 1361 CU  A CU  1 
HETATM 10747 C  C1  . MPD P  7 .   ? 69.013  2.932   53.439  1.00 31.41 ? 1362 MPD A C1  1 
HETATM 10748 C  C2  . MPD P  7 .   ? 69.470  1.516   53.676  1.00 31.85 ? 1362 MPD A C2  1 
HETATM 10749 O  O2  . MPD P  7 .   ? 68.475  0.510   53.279  1.00 34.69 ? 1362 MPD A O2  1 
HETATM 10750 C  CM  . MPD P  7 .   ? 70.544  1.398   52.618  1.00 25.91 ? 1362 MPD A CM  1 
HETATM 10751 C  C3  . MPD P  7 .   ? 70.054  1.347   55.099  1.00 29.85 ? 1362 MPD A C3  1 
HETATM 10752 C  C4  . MPD P  7 .   ? 69.322  0.940   56.433  1.00 29.15 ? 1362 MPD A C4  1 
HETATM 10753 O  O4  . MPD P  7 .   ? 68.563  2.004   57.073  1.00 20.48 ? 1362 MPD A O4  1 
HETATM 10754 C  C5  . MPD P  7 .   ? 68.532  -0.383  56.373  1.00 23.11 ? 1362 MPD A C5  1 
HETATM 10755 C  C1  . NAG Q  2 .   ? 103.917 22.104  21.681  1.00 23.90 ? 1351 NAG B C1  1 
HETATM 10756 C  C2  . NAG Q  2 .   ? 104.518 20.725  21.931  1.00 28.46 ? 1351 NAG B C2  1 
HETATM 10757 C  C3  . NAG Q  2 .   ? 104.417 20.325  23.406  1.00 33.63 ? 1351 NAG B C3  1 
HETATM 10758 C  C4  . NAG Q  2 .   ? 104.940 21.416  24.331  1.00 32.80 ? 1351 NAG B C4  1 
HETATM 10759 C  C5  . NAG Q  2 .   ? 104.156 22.687  23.970  1.00 31.74 ? 1351 NAG B C5  1 
HETATM 10760 C  C6  . NAG Q  2 .   ? 104.533 23.863  24.860  1.00 32.91 ? 1351 NAG B C6  1 
HETATM 10761 C  C7  . NAG Q  2 .   ? 104.291 19.093  20.119  1.00 32.71 ? 1351 NAG B C7  1 
HETATM 10762 C  C8  . NAG Q  2 .   ? 103.469 17.936  19.644  1.00 31.64 ? 1351 NAG B C8  1 
HETATM 10763 N  N2  . NAG Q  2 .   ? 103.795 19.714  21.199  1.00 29.91 ? 1351 NAG B N2  1 
HETATM 10764 O  O3  . NAG Q  2 .   ? 105.082 19.096  23.596  1.00 34.96 ? 1351 NAG B O3  1 
HETATM 10765 O  O4  . NAG Q  2 .   ? 104.769 21.054  25.699  1.00 35.78 ? 1351 NAG B O4  1 
HETATM 10766 O  O5  . NAG Q  2 .   ? 104.442 23.032  22.620  1.00 25.49 ? 1351 NAG B O5  1 
HETATM 10767 O  O6  . NAG Q  2 .   ? 105.868 24.273  24.649  1.00 32.57 ? 1351 NAG B O6  1 
HETATM 10768 O  O7  . NAG Q  2 .   ? 105.334 19.409  19.521  1.00 33.74 ? 1351 NAG B O7  1 
HETATM 10769 C  C1  . NAG R  2 .   ? 104.345 37.851  -10.393 1.00 21.31 ? 1352 NAG B C1  1 
HETATM 10770 C  C2  . NAG R  2 .   ? 105.870 37.910  -10.657 1.00 24.23 ? 1352 NAG B C2  1 
HETATM 10771 C  C3  . NAG R  2 .   ? 106.153 38.369  -12.091 1.00 25.06 ? 1352 NAG B C3  1 
HETATM 10772 C  C4  . NAG R  2 .   ? 105.433 37.501  -13.124 1.00 25.78 ? 1352 NAG B C4  1 
HETATM 10773 C  C5  . NAG R  2 .   ? 103.947 37.521  -12.781 1.00 24.32 ? 1352 NAG B C5  1 
HETATM 10774 C  C6  . NAG R  2 .   ? 103.174 36.515  -13.648 1.00 24.69 ? 1352 NAG B C6  1 
HETATM 10775 C  C7  . NAG R  2 .   ? 107.125 38.505  -8.655  1.00 24.67 ? 1352 NAG B C7  1 
HETATM 10776 C  C8  . NAG R  2 .   ? 107.769 39.609  -7.861  1.00 28.85 ? 1352 NAG B C8  1 
HETATM 10777 N  N2  . NAG R  2 .   ? 106.463 38.872  -9.737  1.00 25.02 ? 1352 NAG B N2  1 
HETATM 10778 O  O3  . NAG R  2 .   ? 107.532 38.329  -12.322 1.00 22.55 ? 1352 NAG B O3  1 
HETATM 10779 O  O4  . NAG R  2 .   ? 105.537 38.081  -14.399 1.00 29.09 ? 1352 NAG B O4  1 
HETATM 10780 O  O5  . NAG R  2 .   ? 103.711 37.143  -11.427 1.00 22.87 ? 1352 NAG B O5  1 
HETATM 10781 O  O6  . NAG R  2 .   ? 101.778 36.845  -13.597 1.00 22.26 ? 1352 NAG B O6  1 
HETATM 10782 O  O7  . NAG R  2 .   ? 107.233 37.329  -8.312  1.00 31.97 ? 1352 NAG B O7  1 
HETATM 10783 C  C1  . NAG S  2 .   ? 106.513 37.490  -15.281 1.00 32.73 ? 1353 NAG B C1  1 
HETATM 10784 C  C2  . NAG S  2 .   ? 106.053 37.775  -16.703 1.00 32.34 ? 1353 NAG B C2  1 
HETATM 10785 C  C3  . NAG S  2 .   ? 107.054 37.175  -17.701 1.00 35.28 ? 1353 NAG B C3  1 
HETATM 10786 C  C4  . NAG S  2 .   ? 108.460 37.713  -17.412 1.00 39.13 ? 1353 NAG B C4  1 
HETATM 10787 C  C5  . NAG S  2 .   ? 108.835 37.774  -15.931 1.00 37.94 ? 1353 NAG B C5  1 
HETATM 10788 C  C6  . NAG S  2 .   ? 109.848 38.901  -15.751 1.00 34.15 ? 1353 NAG B C6  1 
HETATM 10789 C  C7  . NAG S  2 .   ? 103.661 37.846  -17.104 1.00 26.69 ? 1353 NAG B C7  1 
HETATM 10790 C  C8  . NAG S  2 .   ? 102.567 37.003  -17.661 1.00 24.31 ? 1353 NAG B C8  1 
HETATM 10791 N  N2  . NAG S  2 .   ? 104.768 37.155  -16.932 1.00 28.78 ? 1353 NAG B N2  1 
HETATM 10792 O  O3  . NAG S  2 .   ? 106.695 37.639  -18.982 1.00 31.72 ? 1353 NAG B O3  1 
HETATM 10793 O  O4  . NAG S  2 .   ? 109.462 36.991  -18.118 1.00 44.35 ? 1353 NAG B O4  1 
HETATM 10794 O  O5  . NAG S  2 .   ? 107.761 38.113  -15.070 1.00 36.40 ? 1353 NAG B O5  1 
HETATM 10795 O  O6  . NAG S  2 .   ? 110.470 38.532  -14.552 1.00 40.72 ? 1353 NAG B O6  1 
HETATM 10796 O  O7  . NAG S  2 .   ? 103.511 39.048  -16.864 1.00 25.56 ? 1353 NAG B O7  1 
HETATM 10797 C  C1  . BMA T  3 .   ? 110.360 37.908  -18.785 1.00 46.10 ? 1356 BMA B C1  1 
HETATM 10798 C  C2  . BMA T  3 .   ? 111.484 37.069  -19.372 1.00 47.72 ? 1356 BMA B C2  1 
HETATM 10799 C  C3  . BMA T  3 .   ? 112.430 37.903  -20.245 1.00 48.58 ? 1356 BMA B C3  1 
HETATM 10800 C  C4  . BMA T  3 .   ? 111.703 38.894  -21.173 1.00 50.16 ? 1356 BMA B C4  1 
HETATM 10801 C  C5  . BMA T  3 .   ? 110.524 39.650  -20.501 1.00 50.96 ? 1356 BMA B C5  1 
HETATM 10802 C  C6  . BMA T  3 .   ? 109.673 40.416  -21.548 1.00 54.38 ? 1356 BMA B C6  1 
HETATM 10803 O  O2  . BMA T  3 .   ? 110.887 35.989  -20.062 1.00 46.38 ? 1356 BMA B O2  1 
HETATM 10804 O  O3  . BMA T  3 .   ? 113.302 37.049  -20.951 1.00 49.77 ? 1356 BMA B O3  1 
HETATM 10805 O  O4  . BMA T  3 .   ? 112.613 39.841  -21.707 1.00 47.43 ? 1356 BMA B O4  1 
HETATM 10806 O  O5  . BMA T  3 .   ? 109.711 38.750  -19.742 1.00 48.48 ? 1356 BMA B O5  1 
HETATM 10807 O  O6  . BMA T  3 .   ? 109.571 39.590  -22.710 1.00 59.28 ? 1356 BMA B O6  1 
HETATM 10808 C  C1  . MAN U  4 .   ? 108.684 39.972  -23.795 1.00 61.41 ? 1357 MAN B C1  1 
HETATM 10809 C  C2  . MAN U  4 .   ? 108.105 38.668  -24.374 1.00 62.59 ? 1357 MAN B C2  1 
HETATM 10810 C  C3  . MAN U  4 .   ? 109.249 37.775  -24.908 1.00 62.74 ? 1357 MAN B C3  1 
HETATM 10811 C  C4  . MAN U  4 .   ? 110.109 38.543  -25.938 1.00 62.92 ? 1357 MAN B C4  1 
HETATM 10812 C  C5  . MAN U  4 .   ? 110.454 39.966  -25.436 1.00 63.79 ? 1357 MAN B C5  1 
HETATM 10813 C  C6  . MAN U  4 .   ? 111.075 40.822  -26.542 1.00 64.81 ? 1357 MAN B C6  1 
HETATM 10814 O  O2  . MAN U  4 .   ? 107.143 38.956  -25.371 1.00 63.05 ? 1357 MAN B O2  1 
HETATM 10815 O  O3  . MAN U  4 .   ? 108.796 36.501  -25.355 1.00 62.75 ? 1357 MAN B O3  1 
HETATM 10816 O  O4  . MAN U  4 .   ? 111.310 37.837  -26.185 1.00 61.39 ? 1357 MAN B O4  1 
HETATM 10817 O  O5  . MAN U  4 .   ? 109.342 40.669  -24.846 1.00 62.80 ? 1357 MAN B O5  1 
HETATM 10818 O  O6  . MAN U  4 .   ? 111.398 42.096  -26.020 1.00 65.73 ? 1357 MAN B O6  1 
HETATM 10819 C  C1  . NAG V  2 .   ? 95.393  5.118   14.950  1.00 24.69 ? 1354 NAG B C1  1 
HETATM 10820 C  C2  . NAG V  2 .   ? 95.577  4.262   16.224  1.00 31.88 ? 1354 NAG B C2  1 
HETATM 10821 C  C3  . NAG V  2 .   ? 94.988  2.841   16.122  1.00 33.48 ? 1354 NAG B C3  1 
HETATM 10822 C  C4  . NAG V  2 .   ? 93.619  2.847   15.429  1.00 29.90 ? 1354 NAG B C4  1 
HETATM 10823 C  C5  . NAG V  2 .   ? 93.627  3.749   14.200  1.00 24.74 ? 1354 NAG B C5  1 
HETATM 10824 C  C6  . NAG V  2 .   ? 92.247  3.724   13.560  1.00 23.81 ? 1354 NAG B C6  1 
HETATM 10825 C  C7  . NAG V  2 .   ? 97.455  4.705   17.647  1.00 41.79 ? 1354 NAG B C7  1 
HETATM 10826 C  C8  . NAG V  2 .   ? 98.959  4.744   17.736  1.00 42.87 ? 1354 NAG B C8  1 
HETATM 10827 N  N2  . NAG V  2 .   ? 96.983  4.158   16.533  1.00 38.85 ? 1354 NAG B N2  1 
HETATM 10828 O  O3  . NAG V  2 .   ? 94.902  2.172   17.396  1.00 36.66 ? 1354 NAG B O3  1 
HETATM 10829 O  O4  . NAG V  2 .   ? 93.277  1.532   15.010  1.00 31.37 ? 1354 NAG B O4  1 
HETATM 10830 O  O5  . NAG V  2 .   ? 94.001  5.066   14.584  1.00 23.17 ? 1354 NAG B O5  1 
HETATM 10831 O  O6  . NAG V  2 .   ? 91.428  4.576   14.315  1.00 22.66 ? 1354 NAG B O6  1 
HETATM 10832 O  O7  . NAG V  2 .   ? 96.700  5.139   18.540  1.00 43.08 ? 1354 NAG B O7  1 
HETATM 10833 C  C1  . NAG W  2 .   ? 72.775  26.959  20.543  1.00 31.93 ? 1355 NAG B C1  1 
HETATM 10834 C  C2  . NAG W  2 .   ? 71.932  27.227  21.814  1.00 38.69 ? 1355 NAG B C2  1 
HETATM 10835 C  C3  . NAG W  2 .   ? 72.282  26.203  22.892  1.00 40.55 ? 1355 NAG B C3  1 
HETATM 10836 C  C4  . NAG W  2 .   ? 72.163  24.792  22.343  1.00 42.46 ? 1355 NAG B C4  1 
HETATM 10837 C  C5  . NAG W  2 .   ? 72.994  24.658  21.066  1.00 41.44 ? 1355 NAG B C5  1 
HETATM 10838 C  C6  . NAG W  2 .   ? 72.798  23.306  20.416  1.00 41.34 ? 1355 NAG B C6  1 
HETATM 10839 C  C7  . NAG W  2 .   ? 71.416  29.471  22.801  1.00 44.24 ? 1355 NAG B C7  1 
HETATM 10840 C  C8  . NAG W  2 .   ? 72.024  30.542  23.676  1.00 42.51 ? 1355 NAG B C8  1 
HETATM 10841 N  N2  . NAG W  2 .   ? 72.262  28.533  22.377  1.00 41.95 ? 1355 NAG B N2  1 
HETATM 10842 O  O3  . NAG W  2 .   ? 71.397  26.325  23.994  1.00 42.12 ? 1355 NAG B O3  1 
HETATM 10843 O  O4  . NAG W  2 .   ? 72.566  23.864  23.316  1.00 42.40 ? 1355 NAG B O4  1 
HETATM 10844 O  O5  . NAG W  2 .   ? 72.544  25.631  20.139  1.00 37.78 ? 1355 NAG B O5  1 
HETATM 10845 O  O6  . NAG W  2 .   ? 71.431  23.225  20.080  1.00 42.88 ? 1355 NAG B O6  1 
HETATM 10846 O  O7  . NAG W  2 .   ? 70.220  29.492  22.501  1.00 47.09 ? 1355 NAG B O7  1 
HETATM 10847 C  C1  . KMP X  5 .   ? 88.746  32.134  17.110  1.00 18.58 ? 1358 KMP B C1  1 
HETATM 10848 C  C2  . KMP X  5 .   ? 89.651  31.067  17.113  1.00 18.65 ? 1358 KMP B C2  1 
HETATM 10849 C  C3  . KMP X  5 .   ? 89.807  30.327  15.846  1.00 19.10 ? 1358 KMP B C3  1 
HETATM 10850 C  C4  . KMP X  5 .   ? 89.026  30.759  14.675  1.00 15.60 ? 1358 KMP B C4  1 
HETATM 10851 C  C5  . KMP X  5 .   ? 88.148  31.817  14.734  1.00 17.05 ? 1358 KMP B C5  1 
HETATM 10852 C  C6  . KMP X  5 .   ? 88.012  32.489  15.938  1.00 18.02 ? 1358 KMP B C6  1 
HETATM 10853 C  C9  . KMP X  5 .   ? 90.731  29.176  15.677  1.00 18.91 ? 1358 KMP B C9  1 
HETATM 10854 C  C10 . KMP X  5 .   ? 90.802  28.532  14.382  1.00 19.95 ? 1358 KMP B C10 1 
HETATM 10855 C  C11 . KMP X  5 .   ? 90.069  28.977  13.360  1.00 17.25 ? 1358 KMP B C11 1 
HETATM 10856 C  C14 . KMP X  5 .   ? 89.803  28.178  12.124  1.00 20.05 ? 1358 KMP B C14 1 
HETATM 10857 C  C15 . KMP X  5 .   ? 88.754  28.598  11.317  1.00 17.02 ? 1358 KMP B C15 1 
HETATM 10858 C  C16 . KMP X  5 .   ? 88.451  27.913  10.140  1.00 20.23 ? 1358 KMP B C16 1 
HETATM 10859 C  C17 . KMP X  5 .   ? 89.183  26.791  9.780   1.00 17.98 ? 1358 KMP B C17 1 
HETATM 10860 C  C18 . KMP X  5 .   ? 90.218  26.356  10.604  1.00 18.72 ? 1358 KMP B C18 1 
HETATM 10861 C  C19 . KMP X  5 .   ? 90.556  27.046  11.751  1.00 16.88 ? 1358 KMP B C19 1 
HETATM 10862 O  O12 . KMP X  5 .   ? 89.172  30.079  13.523  1.00 19.97 ? 1358 KMP B O12 1 
HETATM 10863 O  O13 . KMP X  5 .   ? 91.401  28.761  16.614  1.00 21.69 ? 1358 KMP B O13 1 
HETATM 10864 O  O24 . KMP X  5 .   ? 88.876  26.120  8.661   1.00 21.46 ? 1358 KMP B O24 1 
HETATM 10865 O  O27 . KMP X  5 .   ? 91.632  27.507  14.221  1.00 21.40 ? 1358 KMP B O27 1 
HETATM 10866 O  O29 . KMP X  5 .   ? 87.177  33.505  15.954  1.00 16.23 ? 1358 KMP B O29 1 
HETATM 10867 O  O30 . KMP X  5 .   ? 90.365  30.717  18.196  1.00 18.19 ? 1358 KMP B O30 1 
HETATM 10868 CU CU  . CU  Y  6 .   ? 93.739  27.790  14.560  1.00 10.45 ? 1359 CU  B CU  1 
HETATM 10869 C  C1  . MPD Z  7 .   ? 91.490  34.600  -6.464  1.00 36.36 ? 1360 MPD B C1  1 
HETATM 10870 C  C2  . MPD Z  7 .   ? 92.950  34.996  -6.518  1.00 37.88 ? 1360 MPD B C2  1 
HETATM 10871 O  O2  . MPD Z  7 .   ? 93.235  36.402  -6.322  1.00 39.92 ? 1360 MPD B O2  1 
HETATM 10872 C  CM  . MPD Z  7 .   ? 93.450  34.456  -5.212  1.00 34.33 ? 1360 MPD B CM  1 
HETATM 10873 C  C3  . MPD Z  7 .   ? 93.659  34.434  -7.784  1.00 35.47 ? 1360 MPD B C3  1 
HETATM 10874 C  C4  . MPD Z  7 .   ? 93.804  35.155  -9.178  1.00 34.51 ? 1360 MPD B C4  1 
HETATM 10875 O  O4  . MPD Z  7 .   ? 92.679  34.965  -10.047 1.00 24.54 ? 1360 MPD B O4  1 
HETATM 10876 C  C5  . MPD Z  7 .   ? 94.319  36.606  -9.229  1.00 28.21 ? 1360 MPD B C5  1 
HETATM 10877 C  C1  . MPD AA 7 .   ? 95.788  30.263  -8.921  1.00 38.68 ? 1361 MPD B C1  1 
HETATM 10878 C  C2  . MPD AA 7 .   ? 96.186  31.715  -8.684  1.00 39.37 ? 1361 MPD B C2  1 
HETATM 10879 O  O2  . MPD AA 7 .   ? 97.617  32.008  -8.728  1.00 43.96 ? 1361 MPD B O2  1 
HETATM 10880 C  CM  . MPD AA 7 .   ? 95.631  32.363  -9.919  1.00 35.41 ? 1361 MPD B CM  1 
HETATM 10881 C  C3  . MPD AA 7 .   ? 95.527  32.274  -7.396  1.00 37.23 ? 1361 MPD B C3  1 
HETATM 10882 C  C4  . MPD AA 7 .   ? 96.181  32.414  -5.974  1.00 36.45 ? 1361 MPD B C4  1 
HETATM 10883 O  O4  . MPD AA 7 .   ? 95.876  31.260  -5.161  1.00 26.14 ? 1361 MPD B O4  1 
HETATM 10884 C  C5  . MPD AA 7 .   ? 97.673  32.826  -5.857  1.00 28.47 ? 1361 MPD B C5  1 
HETATM 10885 C  C1  . NAG BA 2 .   ? 92.455  -1.045  29.952  1.00 27.28 ? 1351 NAG C C1  1 
HETATM 10886 C  C2  . NAG BA 2 .   ? 93.943  -0.706  30.046  1.00 33.22 ? 1351 NAG C C2  1 
HETATM 10887 C  C3  . NAG BA 2 .   ? 94.566  -0.617  28.647  1.00 35.77 ? 1351 NAG C C3  1 
HETATM 10888 C  C4  . NAG BA 2 .   ? 94.233  -1.859  27.817  1.00 38.90 ? 1351 NAG C C4  1 
HETATM 10889 C  C5  . NAG BA 2 .   ? 92.712  -2.031  27.811  1.00 36.15 ? 1351 NAG C C5  1 
HETATM 10890 C  C6  . NAG BA 2 .   ? 92.239  -3.201  26.958  1.00 39.02 ? 1351 NAG C C6  1 
HETATM 10891 C  C7  . NAG BA 2 .   ? 94.505  0.664   32.035  1.00 30.44 ? 1351 NAG C C7  1 
HETATM 10892 C  C8  . NAG BA 2 .   ? 94.641  2.050   32.611  1.00 34.45 ? 1351 NAG C C8  1 
HETATM 10893 N  N2  . NAG BA 2 .   ? 94.131  0.554   30.761  1.00 31.20 ? 1351 NAG C N2  1 
HETATM 10894 O  O3  . NAG BA 2 .   ? 95.957  -0.415  28.811  1.00 37.12 ? 1351 NAG C O3  1 
HETATM 10895 O  O4  . NAG BA 2 .   ? 94.665  -1.732  26.468  1.00 43.47 ? 1351 NAG C O4  1 
HETATM 10896 O  O5  . NAG BA 2 .   ? 92.288  -2.201  29.155  1.00 32.43 ? 1351 NAG C O5  1 
HETATM 10897 O  O6  . NAG BA 2 .   ? 92.751  -4.392  27.509  1.00 40.22 ? 1351 NAG C O6  1 
HETATM 10898 O  O7  . NAG BA 2 .   ? 94.735  -0.290  32.742  1.00 31.74 ? 1351 NAG C O7  1 
HETATM 10899 C  C1  . NAG CA 2 .   ? 73.963  -8.310  59.683  1.00 19.19 ? 1352 NAG C C1  1 
HETATM 10900 C  C2  . NAG CA 2 .   ? 74.838  -9.460  60.184  1.00 25.47 ? 1352 NAG C C2  1 
HETATM 10901 C  C3  . NAG CA 2 .   ? 74.449  -9.818  61.625  1.00 27.44 ? 1352 NAG C C3  1 
HETATM 10902 C  C4  . NAG CA 2 .   ? 74.410  -8.625  62.578  1.00 23.01 ? 1352 NAG C C4  1 
HETATM 10903 C  C5  . NAG CA 2 .   ? 73.568  -7.528  61.903  1.00 22.07 ? 1352 NAG C C5  1 
HETATM 10904 C  C6  . NAG CA 2 .   ? 73.535  -6.292  62.805  1.00 19.92 ? 1352 NAG C C6  1 
HETATM 10905 C  C7  . NAG CA 2 .   ? 75.635  -11.233 58.674  1.00 34.17 ? 1352 NAG C C7  1 
HETATM 10906 C  C8  . NAG CA 2 .   ? 75.353  -12.566 58.040  1.00 36.71 ? 1352 NAG C C8  1 
HETATM 10907 N  N2  . NAG CA 2 .   ? 74.651  -10.630 59.351  1.00 29.26 ? 1352 NAG C N2  1 
HETATM 10908 O  O3  . NAG CA 2 .   ? 75.296  -10.839 62.135  1.00 22.21 ? 1352 NAG C O3  1 
HETATM 10909 O  O4  . NAG CA 2 .   ? 73.694  -8.988  63.759  1.00 24.56 ? 1352 NAG C O4  1 
HETATM 10910 O  O5  . NAG CA 2 .   ? 74.117  -7.243  60.613  1.00 19.29 ? 1352 NAG C O5  1 
HETATM 10911 O  O6  . NAG CA 2 .   ? 72.613  -5.437  62.170  1.00 21.92 ? 1352 NAG C O6  1 
HETATM 10912 O  O7  . NAG CA 2 .   ? 76.747  -10.769 58.539  1.00 34.38 ? 1352 NAG C O7  1 
HETATM 10913 C  C1  . NAG DA 2 .   ? 74.540  -9.262  64.878  1.00 25.01 ? 1353 NAG C C1  1 
HETATM 10914 C  C2  . NAG DA 2 .   ? 73.807  -8.948  66.175  1.00 24.32 ? 1353 NAG C C2  1 
HETATM 10915 C  C3  . NAG DA 2 .   ? 74.683  -9.315  67.356  1.00 25.66 ? 1353 NAG C C3  1 
HETATM 10916 C  C4  . NAG DA 2 .   ? 75.148  -10.755 67.247  1.00 27.77 ? 1353 NAG C C4  1 
HETATM 10917 C  C5  . NAG DA 2 .   ? 75.777  -11.023 65.882  1.00 28.36 ? 1353 NAG C C5  1 
HETATM 10918 C  C6  . NAG DA 2 .   ? 76.200  -12.483 65.685  1.00 28.74 ? 1353 NAG C C6  1 
HETATM 10919 C  C7  . NAG DA 2 .   ? 72.178  -7.117  66.169  1.00 21.61 ? 1353 NAG C C7  1 
HETATM 10920 C  C8  . NAG DA 2 .   ? 72.009  -5.624  66.339  1.00 21.06 ? 1353 NAG C C8  1 
HETATM 10921 N  N2  . NAG DA 2 .   ? 73.422  -7.554  66.322  1.00 23.12 ? 1353 NAG C N2  1 
HETATM 10922 O  O3  . NAG DA 2 .   ? 73.974  -9.085  68.552  1.00 23.22 ? 1353 NAG C O3  1 
HETATM 10923 O  O4  . NAG DA 2 .   ? 76.149  -10.887 68.206  1.00 33.29 ? 1353 NAG C O4  1 
HETATM 10924 O  O5  . NAG DA 2 .   ? 74.796  -10.666 64.913  1.00 29.65 ? 1353 NAG C O5  1 
HETATM 10925 O  O6  . NAG DA 2 .   ? 75.069  -13.335 65.539  1.00 30.42 ? 1353 NAG C O6  1 
HETATM 10926 O  O7  . NAG DA 2 .   ? 71.194  -7.811  65.926  1.00 21.33 ? 1353 NAG C O7  1 
HETATM 10927 C  C1  . BMA EA 3 .   ? 75.887  -12.063 68.969  1.00 36.34 ? 1356 BMA C C1  1 
HETATM 10928 C  C2  . BMA EA 3 .   ? 77.173  -12.470 69.689  1.00 38.15 ? 1356 BMA C C2  1 
HETATM 10929 C  C3  . BMA EA 3 .   ? 76.929  -13.667 70.609  1.00 41.23 ? 1356 BMA C C3  1 
HETATM 10930 C  C4  . BMA EA 3 .   ? 75.696  -13.413 71.474  1.00 41.77 ? 1356 BMA C C4  1 
HETATM 10931 C  C5  . BMA EA 3 .   ? 74.517  -12.963 70.591  1.00 42.76 ? 1356 BMA C C5  1 
HETATM 10932 C  C6  . BMA EA 3 .   ? 73.292  -12.586 71.405  1.00 43.12 ? 1356 BMA C C6  1 
HETATM 10933 O  O2  . BMA EA 3 .   ? 77.572  -11.333 70.399  1.00 35.06 ? 1356 BMA C O2  1 
HETATM 10934 O  O3  . BMA EA 3 .   ? 78.067  -14.012 71.399  1.00 41.08 ? 1356 BMA C O3  1 
HETATM 10935 O  O4  . BMA EA 3 .   ? 75.373  -14.608 72.153  1.00 42.07 ? 1356 BMA C O4  1 
HETATM 10936 O  O5  . BMA EA 3 .   ? 74.865  -11.803 69.867  1.00 38.54 ? 1356 BMA C O5  1 
HETATM 10937 O  O6  . BMA EA 3 .   ? 73.679  -11.508 72.230  1.00 44.25 ? 1356 BMA C O6  1 
HETATM 10938 C  C1  . MAN FA 4 .   ? 72.642  -11.220 73.199  1.00 47.04 ? 1357 MAN C C1  1 
HETATM 10939 C  C2  . MAN FA 4 .   ? 73.071  -9.938  73.922  1.00 46.24 ? 1357 MAN C C2  1 
HETATM 10940 C  C3  . MAN FA 4 .   ? 74.305  -10.226 74.788  1.00 44.88 ? 1357 MAN C C3  1 
HETATM 10941 C  C4  . MAN FA 4 .   ? 74.029  -11.381 75.755  1.00 45.65 ? 1357 MAN C C4  1 
HETATM 10942 C  C5  . MAN FA 4 .   ? 73.538  -12.604 74.942  1.00 47.69 ? 1357 MAN C C5  1 
HETATM 10943 C  C6  . MAN FA 4 .   ? 73.357  -13.905 75.744  1.00 47.93 ? 1357 MAN C C6  1 
HETATM 10944 O  O2  . MAN FA 4 .   ? 71.982  -9.447  74.682  1.00 46.78 ? 1357 MAN C O2  1 
HETATM 10945 O  O3  . MAN FA 4 .   ? 74.802  -9.072  75.433  1.00 44.10 ? 1357 MAN C O3  1 
HETATM 10946 O  O4  . MAN FA 4 .   ? 75.245  -11.700 76.392  1.00 43.15 ? 1357 MAN C O4  1 
HETATM 10947 O  O5  . MAN FA 4 .   ? 72.381  -12.267 74.145  1.00 49.51 ? 1357 MAN C O5  1 
HETATM 10948 O  O6  . MAN FA 4 .   ? 72.221  -13.916 76.594  1.00 48.98 ? 1357 MAN C O6  1 
HETATM 10949 C  C1  . NAG GA 2 .   ? 98.109  17.351  36.391  1.00 30.70 ? 1354 NAG C C1  1 
HETATM 10950 C  C2  . NAG GA 2 .   ? 99.196  17.574  35.295  1.00 36.67 ? 1354 NAG C C2  1 
HETATM 10951 C  C3  . NAG GA 2 .   ? 99.767  19.000  35.143  1.00 38.12 ? 1354 NAG C C3  1 
HETATM 10952 C  C4  . NAG GA 2 .   ? 98.751  20.089  35.429  1.00 35.66 ? 1354 NAG C C4  1 
HETATM 10953 C  C5  . NAG GA 2 .   ? 97.785  19.683  36.551  1.00 33.93 ? 1354 NAG C C5  1 
HETATM 10954 C  C6  . NAG GA 2 .   ? 96.737  20.800  36.722  1.00 28.75 ? 1354 NAG C C6  1 
HETATM 10955 C  C7  . NAG GA 2 .   ? 100.596 15.730  34.717  1.00 45.58 ? 1354 NAG C C7  1 
HETATM 10956 C  C8  . NAG GA 2 .   ? 101.674 14.780  35.170  1.00 46.34 ? 1354 NAG C C8  1 
HETATM 10957 N  N2  . NAG GA 2 .   ? 100.327 16.717  35.563  1.00 41.36 ? 1354 NAG C N2  1 
HETATM 10958 O  O3  . NAG GA 2 .   ? 100.349 19.222  33.857  1.00 40.45 ? 1354 NAG C O3  1 
HETATM 10959 O  O4  . NAG GA 2 .   ? 99.470  21.238  35.841  1.00 37.53 ? 1354 NAG C O4  1 
HETATM 10960 O  O5  . NAG GA 2 .   ? 97.171  18.416  36.292  1.00 29.97 ? 1354 NAG C O5  1 
HETATM 10961 O  O6  . NAG GA 2 .   ? 95.670  20.549  35.839  1.00 29.61 ? 1354 NAG C O6  1 
HETATM 10962 O  O7  . NAG GA 2 .   ? 100.017 15.614  33.625  1.00 47.47 ? 1354 NAG C O7  1 
HETATM 10963 C  C1  . NAG HA 2 .   ? 68.788  18.351  23.467  1.00 34.91 ? 1355 NAG C C1  1 
HETATM 10964 C  C2  . NAG HA 2 .   ? 68.326  18.810  22.079  1.00 42.07 ? 1355 NAG C C2  1 
HETATM 10965 C  C3  . NAG HA 2 .   ? 69.488  19.279  21.224  1.00 43.92 ? 1355 NAG C C3  1 
HETATM 10966 C  C4  . NAG HA 2 .   ? 70.561  20.017  22.010  1.00 44.06 ? 1355 NAG C C4  1 
HETATM 10967 C  C5  . NAG HA 2 .   ? 70.849  19.268  23.339  1.00 44.99 ? 1355 NAG C C5  1 
HETATM 10968 C  C6  . NAG HA 2 .   ? 72.035  19.683  24.248  1.00 47.24 ? 1355 NAG C C6  1 
HETATM 10969 C  C7  . NAG HA 2 .   ? 66.497  17.960  20.784  1.00 47.99 ? 1355 NAG C C7  1 
HETATM 10970 C  C8  . NAG HA 2 .   ? 65.917  16.814  20.001  1.00 48.53 ? 1355 NAG C C8  1 
HETATM 10971 N  N2  . NAG HA 2 .   ? 67.677  17.742  21.342  1.00 44.90 ? 1355 NAG C N2  1 
HETATM 10972 O  O3  . NAG HA 2 .   ? 68.941  20.056  20.185  1.00 47.91 ? 1355 NAG C O3  1 
HETATM 10973 O  O4  . NAG HA 2 .   ? 71.641  20.042  21.127  1.00 45.37 ? 1355 NAG C O4  1 
HETATM 10974 O  O5  . NAG HA 2 .   ? 69.631  19.327  24.056  1.00 39.67 ? 1355 NAG C O5  1 
HETATM 10975 O  O6  . NAG HA 2 .   ? 72.576  18.639  25.073  1.00 49.55 ? 1355 NAG C O6  1 
HETATM 10976 O  O7  . NAG HA 2 .   ? 65.905  19.040  20.907  1.00 49.49 ? 1355 NAG C O7  1 
HETATM 10977 C  C1  . KMP IA 5 .   ? 74.528  3.862   30.029  1.00 19.02 ? 1358 KMP C C1  1 
HETATM 10978 C  C2  . KMP IA 5 .   ? 75.891  3.930   30.328  1.00 17.28 ? 1358 KMP C C2  1 
HETATM 10979 C  C3  . KMP IA 5 .   ? 76.248  4.431   31.666  1.00 17.70 ? 1358 KMP C C3  1 
HETATM 10980 C  C4  . KMP IA 5 .   ? 75.169  4.830   32.602  1.00 17.74 ? 1358 KMP C C4  1 
HETATM 10981 C  C5  . KMP IA 5 .   ? 73.838  4.725   32.225  1.00 17.11 ? 1358 KMP C C5  1 
HETATM 10982 C  C6  . KMP IA 5 .   ? 73.527  4.249   30.947  1.00 18.88 ? 1358 KMP C C6  1 
HETATM 10983 C  C9  . KMP IA 5 .   ? 77.655  4.580   32.107  1.00 20.05 ? 1358 KMP C C9  1 
HETATM 10984 C  C10 . KMP IA 5 .   ? 77.896  5.079   33.454  1.00 18.92 ? 1358 KMP C C10 1 
HETATM 10985 C  C11 . KMP IA 5 .   ? 76.875  5.428   34.274  1.00 18.17 ? 1358 KMP C C11 1 
HETATM 10986 C  C14 . KMP IA 5 .   ? 76.975  6.283   35.530  1.00 20.35 ? 1358 KMP C C14 1 
HETATM 10987 C  C15 . KMP IA 5 .   ? 75.788  6.913   35.942  1.00 20.48 ? 1358 KMP C C15 1 
HETATM 10988 C  C16 . KMP IA 5 .   ? 75.761  7.701   37.094  1.00 21.80 ? 1358 KMP C C16 1 
HETATM 10989 C  C17 . KMP IA 5 .   ? 76.932  7.923   37.846  1.00 20.44 ? 1358 KMP C C17 1 
HETATM 10990 C  C18 . KMP IA 5 .   ? 78.135  7.315   37.429  1.00 20.35 ? 1358 KMP C C18 1 
HETATM 10991 C  C19 . KMP IA 5 .   ? 78.146  6.485   36.296  1.00 19.59 ? 1358 KMP C C19 1 
HETATM 10992 O  O12 . KMP IA 5 .   ? 75.501  5.307   33.834  1.00 19.03 ? 1358 KMP C O12 1 
HETATM 10993 O  O13 . KMP IA 5 .   ? 78.557  4.254   31.340  1.00 23.28 ? 1358 KMP C O13 1 
HETATM 10994 O  O24 . KMP IA 5 .   ? 76.887  8.690   38.949  1.00 18.18 ? 1358 KMP C O24 1 
HETATM 10995 O  O27 . KMP IA 5 .   ? 79.156  5.166   33.856  1.00 17.99 ? 1358 KMP C O27 1 
HETATM 10996 O  O29 . KMP IA 5 .   ? 72.250  4.103   30.607  1.00 20.57 ? 1358 KMP C O29 1 
HETATM 10997 O  O30 . KMP IA 5 .   ? 76.826  3.544   29.441  1.00 17.39 ? 1358 KMP C O30 1 
HETATM 10998 CU CU  . CU  JA 6 .   ? 80.219  3.352   34.057  1.00 11.17 ? 1359 CU  C CU  1 
HETATM 10999 C  C1  . MPD KA 7 .   ? 74.039  3.407   56.953  1.00 35.39 ? 1360 MPD C C1  1 
HETATM 11000 C  C2  . MPD KA 7 .   ? 73.694  1.939   56.759  1.00 38.73 ? 1360 MPD C C2  1 
HETATM 11001 O  O2  . MPD KA 7 .   ? 74.803  1.031   57.038  1.00 42.82 ? 1360 MPD C O2  1 
HETATM 11002 C  CM  . MPD KA 7 .   ? 72.707  1.672   57.880  1.00 35.01 ? 1360 MPD C CM  1 
HETATM 11003 C  C3  . MPD KA 7 .   ? 73.077  1.698   55.350  1.00 34.78 ? 1360 MPD C C3  1 
HETATM 11004 C  C4  . MPD KA 7 .   ? 73.727  0.896   54.180  1.00 32.63 ? 1360 MPD C C4  1 
HETATM 11005 O  O4  . MPD KA 7 .   ? 74.618  1.712   53.372  1.00 24.91 ? 1360 MPD C O4  1 
HETATM 11006 C  C5  . MPD KA 7 .   ? 74.321  -0.480  54.564  1.00 26.65 ? 1360 MPD C C5  1 
HETATM 11007 C  C1  . NAG LA 2 .   ? 86.066  44.665  -37.113 1.00 30.08 ? 1351 NAG D C1  1 
HETATM 11008 C  C2  . NAG LA 2 .   ? 84.568  44.959  -37.374 1.00 38.48 ? 1351 NAG D C2  1 
HETATM 11009 C  C3  . NAG LA 2 .   ? 84.133  44.676  -38.825 1.00 41.46 ? 1351 NAG D C3  1 
HETATM 11010 C  C4  . NAG LA 2 .   ? 85.075  45.339  -39.828 1.00 41.86 ? 1351 NAG D C4  1 
HETATM 11011 C  C5  . NAG LA 2 .   ? 86.524  44.911  -39.500 1.00 40.01 ? 1351 NAG D C5  1 
HETATM 11012 C  C6  . NAG LA 2 .   ? 87.554  45.654  -40.347 1.00 42.69 ? 1351 NAG D C6  1 
HETATM 11013 C  C7  . NAG LA 2 .   ? 83.100  45.015  -35.422 1.00 40.17 ? 1351 NAG D C7  1 
HETATM 11014 C  C8  . NAG LA 2 .   ? 81.716  44.640  -34.999 1.00 38.86 ? 1351 NAG D C8  1 
HETATM 11015 N  N2  . NAG LA 2 .   ? 83.675  44.298  -36.422 1.00 37.95 ? 1351 NAG D N2  1 
HETATM 11016 O  O3  . NAG LA 2 .   ? 82.799  45.084  -39.030 1.00 42.58 ? 1351 NAG D O3  1 
HETATM 11017 O  O4  . NAG LA 2 .   ? 84.660  45.016  -41.153 1.00 44.72 ? 1351 NAG D O4  1 
HETATM 11018 O  O5  . NAG LA 2 .   ? 86.893  45.201  -38.137 1.00 35.65 ? 1351 NAG D O5  1 
HETATM 11019 O  O6  . NAG LA 2 .   ? 88.382  46.417  -39.478 1.00 41.45 ? 1351 NAG D O6  1 
HETATM 11020 O  O7  . NAG LA 2 .   ? 83.661  45.965  -34.834 1.00 38.51 ? 1351 NAG D O7  1 
HETATM 11021 C  C1  . NAG MA 2 .   ? 100.030 42.711  -4.392  1.00 22.54 ? 1352 NAG D C1  1 
HETATM 11022 C  C2  . NAG MA 2 .   ? 100.396 44.200  -4.152  1.00 26.75 ? 1352 NAG D C2  1 
HETATM 11023 C  C3  . NAG MA 2 .   ? 100.828 44.417  -2.688  1.00 28.50 ? 1352 NAG D C3  1 
HETATM 11024 C  C4  . NAG MA 2 .   ? 99.881  43.757  -1.694  1.00 23.54 ? 1352 NAG D C4  1 
HETATM 11025 C  C5  . NAG MA 2 .   ? 99.584  42.315  -2.123  1.00 23.85 ? 1352 NAG D C5  1 
HETATM 11026 C  C6  . NAG MA 2 .   ? 98.566  41.683  -1.189  1.00 22.87 ? 1352 NAG D C6  1 
HETATM 11027 C  C7  . NAG MA 2 .   ? 101.334 45.496  -6.002  1.00 31.11 ? 1352 NAG D C7  1 
HETATM 11028 C  C8  . NAG MA 2 .   ? 102.519 46.186  -6.622  1.00 33.17 ? 1352 NAG D C8  1 
HETATM 11029 N  N2  . NAG MA 2 .   ? 101.520 44.619  -4.998  1.00 29.86 ? 1352 NAG D N2  1 
HETATM 11030 O  O3  . NAG MA 2 .   ? 100.976 45.813  -2.450  1.00 28.29 ? 1352 NAG D O3  1 
HETATM 11031 O  O4  . NAG MA 2 .   ? 100.423 43.740  -0.372  1.00 25.85 ? 1352 NAG D O4  1 
HETATM 11032 O  O5  . NAG MA 2 .   ? 99.062  42.271  -3.447  1.00 20.95 ? 1352 NAG D O5  1 
HETATM 11033 O  O6  . NAG MA 2 .   ? 98.376  40.349  -1.602  1.00 21.33 ? 1352 NAG D O6  1 
HETATM 11034 O  O7  . NAG MA 2 .   ? 100.222 45.766  -6.393  1.00 29.96 ? 1352 NAG D O7  1 
HETATM 11035 C  C1  . NAG NA 2 .   ? 99.956  44.782  0.488   1.00 25.97 ? 1353 NAG D C1  1 
HETATM 11036 C  C2  . NAG NA 2 .   ? 100.000 44.232  1.927   1.00 26.29 ? 1353 NAG D C2  1 
HETATM 11037 C  C3  . NAG NA 2 .   ? 99.734  45.366  2.921   1.00 29.33 ? 1353 NAG D C3  1 
HETATM 11038 C  C4  . NAG NA 2 .   ? 100.637 46.583  2.663   1.00 32.79 ? 1353 NAG D C4  1 
HETATM 11039 C  C5  . NAG NA 2 .   ? 100.576 47.016  1.182   1.00 33.47 ? 1353 NAG D C5  1 
HETATM 11040 C  C6  . NAG NA 2 .   ? 101.561 48.157  0.844   1.00 34.15 ? 1353 NAG D C6  1 
HETATM 11041 C  C7  . NAG NA 2 .   ? 99.628  41.827  2.360   1.00 20.38 ? 1353 NAG D C7  1 
HETATM 11042 C  C8  . NAG NA 2 .   ? 98.717  40.639  2.650   1.00 19.86 ? 1353 NAG D C8  1 
HETATM 11043 N  N2  . NAG NA 2 .   ? 99.131  43.052  2.193   1.00 18.85 ? 1353 NAG D N2  1 
HETATM 11044 O  O3  . NAG NA 2 .   ? 99.970  44.840  4.212   1.00 31.48 ? 1353 NAG D O3  1 
HETATM 11045 O  O4  . NAG NA 2 .   ? 100.381 47.653  3.587   1.00 34.97 ? 1353 NAG D O4  1 
HETATM 11046 O  O5  . NAG NA 2 .   ? 100.840 45.890  0.346   1.00 31.25 ? 1353 NAG D O5  1 
HETATM 11047 O  O6  . NAG NA 2 .   ? 102.911 47.707  1.024   1.00 35.60 ? 1353 NAG D O6  1 
HETATM 11048 O  O7  . NAG NA 2 .   ? 100.812 41.556  2.329   1.00 18.65 ? 1353 NAG D O7  1 
HETATM 11049 C  C1  . NAG OA 2 .   ? 92.945  10.768  -35.251 1.00 22.57 ? 1354 NAG D C1  1 
HETATM 11050 C  C2  . NAG OA 2 .   ? 93.851  10.847  -36.519 1.00 25.22 ? 1354 NAG D C2  1 
HETATM 11051 C  C3  . NAG OA 2 .   ? 95.129  9.964   -36.456 1.00 28.17 ? 1354 NAG D C3  1 
HETATM 11052 C  C4  . NAG OA 2 .   ? 95.856  10.026  -35.096 1.00 30.95 ? 1354 NAG D C4  1 
HETATM 11053 C  C5  . NAG OA 2 .   ? 94.848  9.901   -33.969 1.00 28.55 ? 1354 NAG D C5  1 
HETATM 11054 C  C6  . NAG OA 2 .   ? 95.459  10.098  -32.577 1.00 32.29 ? 1354 NAG D C6  1 
HETATM 11055 C  C7  . NAG OA 2 .   ? 92.613  9.479   -38.211 1.00 26.10 ? 1354 NAG D C7  1 
HETATM 11056 C  C8  . NAG OA 2 .   ? 92.278  9.420   -39.664 1.00 24.88 ? 1354 NAG D C8  1 
HETATM 11057 N  N2  . NAG OA 2 .   ? 93.068  10.672  -37.763 1.00 22.44 ? 1354 NAG D N2  1 
HETATM 11058 O  O3  . NAG OA 2 .   ? 96.049  10.413  -37.439 1.00 29.45 ? 1354 NAG D O3  1 
HETATM 11059 O  O4  . NAG OA 2 .   ? 96.959  9.104   -34.980 1.00 32.90 ? 1354 NAG D O4  1 
HETATM 11060 O  O5  . NAG OA 2 .   ? 93.871  10.920  -34.168 1.00 28.57 ? 1354 NAG D O5  1 
HETATM 11061 O  O6  . NAG OA 2 .   ? 94.420  10.054  -31.611 1.00 36.21 ? 1354 NAG D O6  1 
HETATM 11062 O  O7  . NAG OA 2 .   ? 92.419  8.474   -37.482 1.00 30.21 ? 1354 NAG D O7  1 
HETATM 11063 C  C1  . NAG PA 2 .   ? 67.557  38.447  -31.025 1.00 28.55 ? 1355 NAG D C1  1 
HETATM 11064 C  C2  . NAG PA 2 .   ? 66.733  38.831  -32.289 1.00 35.41 ? 1355 NAG D C2  1 
HETATM 11065 C  C3  . NAG PA 2 .   ? 65.264  38.388  -32.230 1.00 35.42 ? 1355 NAG D C3  1 
HETATM 11066 C  C4  . NAG PA 2 .   ? 65.170  36.912  -31.851 1.00 34.68 ? 1355 NAG D C4  1 
HETATM 11067 C  C5  . NAG PA 2 .   ? 65.937  36.722  -30.540 1.00 32.37 ? 1355 NAG D C5  1 
HETATM 11068 C  C6  . NAG PA 2 .   ? 65.930  35.270  -30.096 1.00 31.21 ? 1355 NAG D C6  1 
HETATM 11069 C  C7  . NAG PA 2 .   ? 67.641  40.604  -33.606 1.00 42.94 ? 1355 NAG D C7  1 
HETATM 11070 C  C8  . NAG PA 2 .   ? 68.105  42.046  -33.615 1.00 46.12 ? 1355 NAG D C8  1 
HETATM 11071 N  N2  . NAG PA 2 .   ? 66.824  40.246  -32.618 1.00 39.29 ? 1355 NAG D N2  1 
HETATM 11072 O  O3  . NAG PA 2 .   ? 64.656  38.556  -33.499 1.00 37.27 ? 1355 NAG D O3  1 
HETATM 11073 O  O4  . NAG PA 2 .   ? 63.814  36.549  -31.702 1.00 36.53 ? 1355 NAG D O4  1 
HETATM 11074 O  O5  . NAG PA 2 .   ? 67.282  37.064  -30.791 1.00 27.37 ? 1355 NAG D O5  1 
HETATM 11075 O  O6  . NAG PA 2 .   ? 66.685  34.506  -31.020 1.00 30.40 ? 1355 NAG D O6  1 
HETATM 11076 O  O7  . NAG PA 2 .   ? 68.014  39.796  -34.471 1.00 44.83 ? 1355 NAG D O7  1 
HETATM 11077 C  C1  . KMP QA 5 .   ? 93.903  28.497  -32.594 1.00 12.87 ? 1356 KMP D C1  1 
HETATM 11078 C  C2  . KMP QA 5 .   ? 92.941  29.493  -32.599 1.00 15.99 ? 1356 KMP D C2  1 
HETATM 11079 C  C3  . KMP QA 5 .   ? 92.175  29.752  -31.364 1.00 15.43 ? 1356 KMP D C3  1 
HETATM 11080 C  C4  . KMP QA 5 .   ? 92.474  28.924  -30.168 1.00 16.51 ? 1356 KMP D C4  1 
HETATM 11081 C  C5  . KMP QA 5 .   ? 93.455  27.935  -30.232 1.00 14.94 ? 1356 KMP D C5  1 
HETATM 11082 C  C6  . KMP QA 5 .   ? 94.150  27.745  -31.435 1.00 15.89 ? 1356 KMP D C6  1 
HETATM 11083 C  C9  . KMP QA 5 .   ? 91.122  30.821  -31.307 1.00 18.69 ? 1356 KMP D C9  1 
HETATM 11084 C  C10 . KMP QA 5 .   ? 90.418  30.986  -30.026 1.00 16.02 ? 1356 KMP D C10 1 
HETATM 11085 C  C11 . KMP QA 5 .   ? 90.734  30.194  -28.965 1.00 16.96 ? 1356 KMP D C11 1 
HETATM 11086 C  C14 . KMP QA 5 .   ? 89.891  29.990  -27.721 1.00 18.52 ? 1356 KMP D C14 1 
HETATM 11087 C  C15 . KMP QA 5 .   ? 90.188  28.862  -26.911 1.00 16.29 ? 1356 KMP D C15 1 
HETATM 11088 C  C16 . KMP QA 5 .   ? 89.479  28.569  -25.734 1.00 15.75 ? 1356 KMP D C16 1 
HETATM 11089 C  C17 . KMP QA 5 .   ? 88.432  29.438  -25.348 1.00 18.57 ? 1356 KMP D C17 1 
HETATM 11090 C  C18 . KMP QA 5 .   ? 88.140  30.549  -26.160 1.00 18.43 ? 1356 KMP D C18 1 
HETATM 11091 C  C19 . KMP QA 5 .   ? 88.835  30.835  -27.346 1.00 19.65 ? 1356 KMP D C19 1 
HETATM 11092 O  O12 . KMP QA 5 .   ? 91.767  29.143  -29.044 1.00 16.42 ? 1356 KMP D O12 1 
HETATM 11093 O  O13 . KMP QA 5 .   ? 90.877  31.500  -32.324 1.00 17.57 ? 1356 KMP D O13 1 
HETATM 11094 O  O24 . KMP QA 5 .   ? 87.696  29.212  -24.204 1.00 17.41 ? 1356 KMP D O24 1 
HETATM 11095 O  O27 . KMP QA 5 .   ? 89.486  31.958  -29.955 1.00 17.01 ? 1356 KMP D O27 1 
HETATM 11096 O  O29 . KMP QA 5 .   ? 95.108  26.824  -31.490 1.00 14.40 ? 1356 KMP D O29 1 
HETATM 11097 O  O30 . KMP QA 5 .   ? 92.701  30.209  -33.688 1.00 16.41 ? 1356 KMP D O30 1 
HETATM 11098 CU CU  . CU  RA 6 .   ? 90.085  33.958  -30.057 1.00 11.06 ? 1357 CU  D CU  1 
HETATM 11099 O  O   . HOH SA 8 .   ? 71.061  40.768  65.490  1.00 36.36 ? 2001 HOH A O   1 
HETATM 11100 O  O   . HOH SA 8 .   ? 67.292  42.945  69.261  1.00 30.66 ? 2002 HOH A O   1 
HETATM 11101 O  O   . HOH SA 8 .   ? 64.081  41.561  78.651  1.00 31.21 ? 2003 HOH A O   1 
HETATM 11102 O  O   . HOH SA 8 .   ? 66.044  39.943  64.318  1.00 24.23 ? 2004 HOH A O   1 
HETATM 11103 O  O   . HOH SA 8 .   ? 73.252  35.702  61.866  1.00 37.15 ? 2005 HOH A O   1 
HETATM 11104 O  O   . HOH SA 8 .   ? 69.386  35.423  72.966  1.00 36.46 ? 2006 HOH A O   1 
HETATM 11105 O  O   . HOH SA 8 .   ? 77.630  32.675  71.706  1.00 35.53 ? 2007 HOH A O   1 
HETATM 11106 O  O   . HOH SA 8 .   ? 62.566  39.272  76.816  1.00 40.15 ? 2008 HOH A O   1 
HETATM 11107 O  O   . HOH SA 8 .   ? 55.562  37.656  68.696  1.00 38.38 ? 2009 HOH A O   1 
HETATM 11108 O  O   . HOH SA 8 .   ? 72.940  37.537  73.628  1.00 46.33 ? 2010 HOH A O   1 
HETATM 11109 O  O   . HOH SA 8 .   ? 68.494  37.420  63.590  1.00 21.18 ? 2011 HOH A O   1 
HETATM 11110 O  O   . HOH SA 8 .   ? 71.736  37.821  55.785  1.00 45.58 ? 2012 HOH A O   1 
HETATM 11111 O  O   . HOH SA 8 .   ? 64.812  37.095  77.500  1.00 42.48 ? 2013 HOH A O   1 
HETATM 11112 O  O   . HOH SA 8 .   ? 77.059  34.101  67.248  1.00 35.21 ? 2014 HOH A O   1 
HETATM 11113 O  O   . HOH SA 8 .   ? 73.716  34.671  64.673  1.00 42.28 ? 2015 HOH A O   1 
HETATM 11114 O  O   . HOH SA 8 .   ? 71.317  34.117  71.881  1.00 37.24 ? 2016 HOH A O   1 
HETATM 11115 O  O   . HOH SA 8 .   ? 74.062  31.760  65.553  0.50 10.68 ? 2017 HOH A O   1 
HETATM 11116 O  O   . HOH SA 8 .   ? 76.795  30.180  72.194  0.50 11.36 ? 2018 HOH A O   1 
HETATM 11117 O  O   . HOH SA 8 .   ? 55.165  35.545  70.676  1.00 29.92 ? 2019 HOH A O   1 
HETATM 11118 O  O   . HOH SA 8 .   ? 50.418  17.579  79.098  1.00 32.98 ? 2020 HOH A O   1 
HETATM 11119 O  O   . HOH SA 8 .   ? 72.402  32.478  74.662  1.00 31.60 ? 2021 HOH A O   1 
HETATM 11120 O  O   . HOH SA 8 .   ? 75.623  29.979  74.903  1.00 23.59 ? 2022 HOH A O   1 
HETATM 11121 O  O   . HOH SA 8 .   ? 70.391  36.452  58.213  1.00 44.54 ? 2023 HOH A O   1 
HETATM 11122 O  O   . HOH SA 8 .   ? 67.794  31.394  76.570  1.00 39.24 ? 2024 HOH A O   1 
HETATM 11123 O  O   . HOH SA 8 .   ? 67.208  27.088  76.287  1.00 16.59 ? 2025 HOH A O   1 
HETATM 11124 O  O   . HOH SA 8 .   ? 49.602  -0.252  54.171  1.00 32.98 ? 2026 HOH A O   1 
HETATM 11125 O  O   . HOH SA 8 .   ? 65.061  34.336  76.474  1.00 26.00 ? 2027 HOH A O   1 
HETATM 11126 O  O   . HOH SA 8 .   ? 63.291  36.624  79.616  1.00 53.09 ? 2028 HOH A O   1 
HETATM 11127 O  O   . HOH SA 8 .   ? 64.533  32.991  83.233  1.00 34.74 ? 2029 HOH A O   1 
HETATM 11128 O  O   . HOH SA 8 .   ? 62.115  29.551  81.455  1.00 26.97 ? 2030 HOH A O   1 
HETATM 11129 O  O   . HOH SA 8 .   ? 60.161  37.949  73.672  1.00 28.05 ? 2031 HOH A O   1 
HETATM 11130 O  O   . HOH SA 8 .   ? 83.189  15.240  76.843  1.00 29.50 ? 2032 HOH A O   1 
HETATM 11131 O  O   . HOH SA 8 .   ? 51.793  -16.104 76.938  1.00 43.94 ? 2033 HOH A O   1 
HETATM 11132 O  O   . HOH SA 8 .   ? 56.467  36.552  72.506  1.00 32.34 ? 2034 HOH A O   1 
HETATM 11133 O  O   . HOH SA 8 .   ? 56.157  32.197  77.653  1.00 22.92 ? 2035 HOH A O   1 
HETATM 11134 O  O   . HOH SA 8 .   ? 64.017  37.477  73.857  1.00 25.93 ? 2036 HOH A O   1 
HETATM 11135 O  O   . HOH SA 8 .   ? 54.462  28.772  78.973  1.00 35.59 ? 2037 HOH A O   1 
HETATM 11136 O  O   . HOH SA 8 .   ? 49.145  26.212  75.491  1.00 40.09 ? 2038 HOH A O   1 
HETATM 11137 O  O   . HOH SA 8 .   ? 52.830  24.301  81.793  1.00 38.35 ? 2039 HOH A O   1 
HETATM 11138 O  O   . HOH SA 8 .   ? 48.495  20.478  76.683  1.00 30.30 ? 2040 HOH A O   1 
HETATM 11139 O  O   . HOH SA 8 .   ? 52.060  20.037  78.637  1.00 24.58 ? 2041 HOH A O   1 
HETATM 11140 O  O   . HOH SA 8 .   ? 54.853  28.770  82.098  1.00 41.80 ? 2042 HOH A O   1 
HETATM 11141 O  O   . HOH SA 8 .   ? 72.259  35.094  59.618  1.00 29.40 ? 2043 HOH A O   1 
HETATM 11142 O  O   . HOH SA 8 .   ? 71.041  32.945  56.198  1.00 20.17 ? 2044 HOH A O   1 
HETATM 11143 O  O   . HOH SA 8 .   ? 73.277  33.186  61.594  1.00 21.71 ? 2045 HOH A O   1 
HETATM 11144 O  O   . HOH SA 8 .   ? 85.291  18.347  79.073  1.00 42.94 ? 2046 HOH A O   1 
HETATM 11145 O  O   . HOH SA 8 .   ? 75.330  26.459  61.966  1.00 11.91 ? 2047 HOH A O   1 
HETATM 11146 O  O   . HOH SA 8 .   ? 84.601  2.454   65.516  1.00 30.73 ? 2048 HOH A O   1 
HETATM 11147 O  O   . HOH SA 8 .   ? 77.646  23.740  69.828  1.00 15.25 ? 2049 HOH A O   1 
HETATM 11148 O  O   . HOH SA 8 .   ? 71.950  30.229  66.114  1.00 11.20 ? 2050 HOH A O   1 
HETATM 11149 O  O   . HOH SA 8 .   ? 50.327  8.471   83.871  1.00 30.43 ? 2051 HOH A O   1 
HETATM 11150 O  O   . HOH SA 8 .   ? 68.385  -14.609 57.897  1.00 30.97 ? 2052 HOH A O   1 
HETATM 11151 O  O   . HOH SA 8 .   ? 50.156  15.381  76.831  1.00 24.24 ? 2053 HOH A O   1 
HETATM 11152 O  O   . HOH SA 8 .   ? 58.634  16.572  82.904  1.00 29.48 ? 2054 HOH A O   1 
HETATM 11153 O  O   . HOH SA 8 .   ? 64.458  28.300  79.835  1.00 18.22 ? 2055 HOH A O   1 
HETATM 11154 O  O   . HOH SA 8 .   ? 48.000  2.142   54.758  1.00 28.00 ? 2056 HOH A O   1 
HETATM 11155 O  O   . HOH SA 8 .   ? 47.739  5.593   53.410  1.00 28.45 ? 2057 HOH A O   1 
HETATM 11156 O  O   . HOH SA 8 .   ? 79.623  13.462  79.475  1.00 38.26 ? 2058 HOH A O   1 
HETATM 11157 O  O   . HOH SA 8 .   ? 51.045  15.095  37.606  1.00 40.72 ? 2059 HOH A O   1 
HETATM 11158 O  O   . HOH SA 8 .   ? 81.655  13.656  75.157  1.00 20.36 ? 2060 HOH A O   1 
HETATM 11159 O  O   . HOH SA 8 .   ? 78.673  11.743  81.205  1.00 29.85 ? 2061 HOH A O   1 
HETATM 11160 O  O   . HOH SA 8 .   ? 56.034  -6.476  79.702  1.00 45.29 ? 2062 HOH A O   1 
HETATM 11161 O  O   . HOH SA 8 .   ? 79.361  6.702   75.126  1.00 35.33 ? 2063 HOH A O   1 
HETATM 11162 O  O   . HOH SA 8 .   ? 52.387  -13.493 76.009  1.00 46.84 ? 2064 HOH A O   1 
HETATM 11163 O  O   . HOH SA 8 .   ? 76.202  5.932   72.396  1.00 16.49 ? 2065 HOH A O   1 
HETATM 11164 O  O   . HOH SA 8 .   ? 68.704  25.816  74.155  1.00 11.02 ? 2066 HOH A O   1 
HETATM 11165 O  O   . HOH SA 8 .   ? 48.916  11.270  82.185  1.00 48.11 ? 2067 HOH A O   1 
HETATM 11166 O  O   . HOH SA 8 .   ? 72.169  18.788  66.486  1.00 13.41 ? 2068 HOH A O   1 
HETATM 11167 O  O   . HOH SA 8 .   ? 64.637  27.136  77.365  1.00 21.86 ? 2069 HOH A O   1 
HETATM 11168 O  O   . HOH SA 8 .   ? 57.216  29.313  78.584  1.00 22.98 ? 2070 HOH A O   1 
HETATM 11169 O  O   . HOH SA 8 .   ? 60.511  30.704  72.369  1.00 20.55 ? 2071 HOH A O   1 
HETATM 11170 O  O   . HOH SA 8 .   ? 52.807  27.035  73.130  1.00 13.22 ? 2072 HOH A O   1 
HETATM 11171 O  O   . HOH SA 8 .   ? 51.508  27.982  75.457  1.00 30.28 ? 2073 HOH A O   1 
HETATM 11172 O  O   . HOH SA 8 .   ? 51.271  25.058  78.984  1.00 34.95 ? 2074 HOH A O   1 
HETATM 11173 O  O   . HOH SA 8 .   ? 51.576  23.348  75.470  1.00 23.63 ? 2075 HOH A O   1 
HETATM 11174 O  O   . HOH SA 8 .   ? 51.314  20.688  76.107  1.00 18.48 ? 2076 HOH A O   1 
HETATM 11175 O  O   . HOH SA 8 .   ? 58.093  28.615  81.437  1.00 25.05 ? 2077 HOH A O   1 
HETATM 11176 O  O   . HOH SA 8 .   ? 51.961  19.376  73.921  1.00 18.34 ? 2078 HOH A O   1 
HETATM 11177 O  O   . HOH SA 8 .   ? 60.845  22.333  81.303  1.00 25.07 ? 2079 HOH A O   1 
HETATM 11178 O  O   . HOH SA 8 .   ? 59.797  17.180  76.167  1.00 17.59 ? 2080 HOH A O   1 
HETATM 11179 O  O   . HOH SA 8 .   ? 82.326  19.243  77.133  1.00 25.30 ? 2081 HOH A O   1 
HETATM 11180 O  O   . HOH SA 8 .   ? 82.540  16.834  80.043  1.00 37.76 ? 2082 HOH A O   1 
HETATM 11181 O  O   . HOH SA 8 .   ? 73.721  17.768  68.965  1.00 15.93 ? 2083 HOH A O   1 
HETATM 11182 O  O   . HOH SA 8 .   ? 78.055  6.916   70.909  1.00 14.50 ? 2084 HOH A O   1 
HETATM 11183 O  O   . HOH SA 8 .   ? 84.186  -0.055  65.397  1.00 34.40 ? 2085 HOH A O   1 
HETATM 11184 O  O   . HOH SA 8 .   ? 82.818  6.545   65.349  1.00 14.40 ? 2086 HOH A O   1 
HETATM 11185 O  O   . HOH SA 8 .   ? 81.871  5.567   71.147  1.00 27.62 ? 2087 HOH A O   1 
HETATM 11186 O  O   . HOH SA 8 .   ? 84.402  2.320   72.459  1.00 47.67 ? 2088 HOH A O   1 
HETATM 11187 O  O   . HOH SA 8 .   ? 81.020  3.712   73.481  1.00 46.36 ? 2089 HOH A O   1 
HETATM 11188 O  O   . HOH SA 8 .   ? 77.596  -3.911  69.414  1.00 30.36 ? 2090 HOH A O   1 
HETATM 11189 O  O   . HOH SA 8 .   ? 58.963  6.630   95.656  1.00 44.67 ? 2091 HOH A O   1 
HETATM 11190 O  O   . HOH SA 8 .   ? 67.186  -13.646 60.477  1.00 22.09 ? 2092 HOH A O   1 
HETATM 11191 O  O   . HOH SA 8 .   ? 69.010  -15.344 63.962  1.00 25.78 ? 2093 HOH A O   1 
HETATM 11192 O  O   . HOH SA 8 .   ? 53.242  8.426   85.295  1.00 33.89 ? 2094 HOH A O   1 
HETATM 11193 O  O   . HOH SA 8 .   ? 50.141  7.903   81.129  1.00 39.46 ? 2095 HOH A O   1 
HETATM 11194 O  O   . HOH SA 8 .   ? 52.066  12.313  88.127  1.00 37.95 ? 2096 HOH A O   1 
HETATM 11195 O  O   . HOH SA 8 .   ? 51.292  13.419  78.366  1.00 23.26 ? 2097 HOH A O   1 
HETATM 11196 O  O   . HOH SA 8 .   ? 57.792  7.148   74.775  1.00 15.69 ? 2098 HOH A O   1 
HETATM 11197 O  O   . HOH SA 8 .   ? 57.590  17.443  80.334  1.00 17.82 ? 2099 HOH A O   1 
HETATM 11198 O  O   . HOH SA 8 .   ? 54.716  -5.543  57.684  1.00 32.44 ? 2100 HOH A O   1 
HETATM 11199 O  O   . HOH SA 8 .   ? 56.459  -4.743  50.862  1.00 35.75 ? 2101 HOH A O   1 
HETATM 11200 O  O   . HOH SA 8 .   ? 52.811  -1.919  49.261  1.00 41.05 ? 2102 HOH A O   1 
HETATM 11201 O  O   . HOH SA 8 .   ? 55.662  0.844   46.916  1.00 38.34 ? 2103 HOH A O   1 
HETATM 11202 O  O   . HOH SA 8 .   ? 49.527  4.196   54.533  1.00 14.41 ? 2104 HOH A O   1 
HETATM 11203 O  O   . HOH SA 8 .   ? 52.296  -1.725  59.833  1.00 35.20 ? 2105 HOH A O   1 
HETATM 11204 O  O   . HOH SA 8 .   ? 47.378  2.927   57.859  1.00 17.49 ? 2106 HOH A O   1 
HETATM 11205 O  O   . HOH SA 8 .   ? 49.363  -1.381  59.218  1.00 25.28 ? 2107 HOH A O   1 
HETATM 11206 O  O   . HOH SA 8 .   ? 48.224  7.291   57.772  1.00 11.82 ? 2108 HOH A O   1 
HETATM 11207 O  O   . HOH SA 8 .   ? 51.886  -4.413  64.729  1.00 35.54 ? 2109 HOH A O   1 
HETATM 11208 O  O   . HOH SA 8 .   ? 72.702  16.870  58.596  1.00 33.96 ? 2110 HOH A O   1 
HETATM 11209 O  O   . HOH SA 8 .   ? 70.770  18.319  57.764  1.00 45.81 ? 2111 HOH A O   1 
HETATM 11210 O  O   . HOH SA 8 .   ? 68.388  14.574  57.056  1.00 15.27 ? 2112 HOH A O   1 
HETATM 11211 O  O   . HOH SA 8 .   ? 58.526  10.728  51.805  1.00 16.70 ? 2113 HOH A O   1 
HETATM 11212 O  O   . HOH SA 8 .   ? 55.912  3.090   48.373  1.00 32.11 ? 2114 HOH A O   1 
HETATM 11213 O  O   . HOH SA 8 .   ? 72.610  7.674   56.589  1.00 12.86 ? 2115 HOH A O   1 
HETATM 11214 O  O   . HOH SA 8 .   ? 74.890  9.988   56.561  1.00 14.46 ? 2116 HOH A O   1 
HETATM 11215 O  O   . HOH SA 8 .   ? 47.262  12.008  57.267  1.00 29.53 ? 2117 HOH A O   1 
HETATM 11216 O  O   . HOH SA 8 .   ? 49.074  16.631  39.830  1.00 42.31 ? 2118 HOH A O   1 
HETATM 11217 O  O   . HOH SA 8 .   ? 56.702  26.346  49.654  1.00 22.20 ? 2119 HOH A O   1 
HETATM 11218 O  O   . HOH SA 8 .   ? 73.271  -1.917  66.902  1.00 29.61 ? 2120 HOH A O   1 
HETATM 11219 O  O   . HOH SA 8 .   ? 45.178  11.472  59.150  1.00 40.74 ? 2121 HOH A O   1 
HETATM 11220 O  O   . HOH SA 8 .   ? 60.842  -8.250  74.204  1.00 24.40 ? 2122 HOH A O   1 
HETATM 11221 O  O   . HOH SA 8 .   ? 46.581  6.018   74.113  1.00 42.97 ? 2123 HOH A O   1 
HETATM 11222 O  O   . HOH SA 8 .   ? 55.778  -4.034  69.903  1.00 14.91 ? 2124 HOH A O   1 
HETATM 11223 O  O   . HOH SA 8 .   ? 49.518  -0.715  72.641  1.00 34.14 ? 2125 HOH A O   1 
HETATM 11224 O  O   . HOH SA 8 .   ? 48.312  18.509  75.381  1.00 33.88 ? 2126 HOH A O   1 
HETATM 11225 O  O   . HOH SA 8 .   ? 55.576  -4.559  77.382  1.00 39.99 ? 2127 HOH A O   1 
HETATM 11226 O  O   . HOH SA 8 .   ? 52.273  -10.713 78.818  1.00 47.11 ? 2128 HOH A O   1 
HETATM 11227 O  O   . HOH SA 8 .   ? 53.452  -10.130 76.366  1.00 44.00 ? 2129 HOH A O   1 
HETATM 11228 O  O   . HOH SA 8 .   ? 57.982  13.071  50.741  1.00 13.14 ? 2130 HOH A O   1 
HETATM 11229 O  O   . HOH SA 8 .   ? 54.358  -3.497  67.332  1.00 32.76 ? 2131 HOH A O   1 
HETATM 11230 O  O   . HOH SA 8 .   ? 59.402  33.168  46.656  1.00 28.68 ? 2132 HOH A O   1 
HETATM 11231 O  O   . HOH SA 8 .   ? 55.437  -12.024 69.825  1.00 41.09 ? 2133 HOH A O   1 
HETATM 11232 O  O   . HOH SA 8 .   ? 52.630  -9.570  68.278  1.00 36.82 ? 2134 HOH A O   1 
HETATM 11233 O  O   . HOH SA 8 .   ? 59.283  -10.281 70.761  1.00 21.97 ? 2135 HOH A O   1 
HETATM 11234 O  O   . HOH SA 8 .   ? 46.932  32.423  49.807  1.00 31.10 ? 2136 HOH A O   1 
HETATM 11235 O  O   . HOH SA 8 .   ? 56.157  -8.088  62.606  1.00 36.60 ? 2137 HOH A O   1 
HETATM 11236 O  O   . HOH SA 8 .   ? 54.994  -6.009  66.671  1.00 20.02 ? 2138 HOH A O   1 
HETATM 11237 O  O   . HOH SA 8 .   ? 45.367  34.402  66.244  1.00 28.58 ? 2139 HOH A O   1 
HETATM 11238 O  O   . HOH SA 8 .   ? 56.111  -2.347  62.829  1.00 24.62 ? 2140 HOH A O   1 
HETATM 11239 O  O   . HOH SA 8 .   ? 56.057  -4.305  61.235  1.00 27.44 ? 2141 HOH A O   1 
HETATM 11240 O  O   . HOH SA 8 .   ? 68.542  6.361   54.359  1.00 13.43 ? 2142 HOH A O   1 
HETATM 11241 O  O   . HOH SA 8 .   ? 72.148  12.974  55.512  1.00 25.08 ? 2143 HOH A O   1 
HETATM 11242 O  O   . HOH SA 8 .   ? 68.729  12.350  53.293  1.00 23.79 ? 2144 HOH A O   1 
HETATM 11243 O  O   . HOH SA 8 .   ? 53.870  38.939  65.986  1.00 35.23 ? 2145 HOH A O   1 
HETATM 11244 O  O   . HOH SA 8 .   ? 62.758  11.722  55.745  1.00 14.03 ? 2146 HOH A O   1 
HETATM 11245 O  O   . HOH SA 8 .   ? 60.976  40.979  53.118  1.00 35.04 ? 2147 HOH A O   1 
HETATM 11246 O  O   . HOH SA 8 .   ? 70.772  34.863  52.667  0.50 26.86 ? 2148 HOH A O   1 
HETATM 11247 O  O   . HOH SA 8 .   ? 52.870  34.577  71.562  1.00 44.16 ? 2149 HOH A O   1 
HETATM 11248 O  O   . HOH SA 8 .   ? 50.301  11.308  79.387  1.00 32.06 ? 2150 HOH A O   1 
HETATM 11249 O  O   . HOH SA 8 .   ? 50.662  5.229   74.120  1.00 15.95 ? 2151 HOH A O   1 
HETATM 11250 O  O   . HOH SA 8 .   ? 51.174  7.666   73.631  1.00 14.61 ? 2152 HOH A O   1 
HETATM 11251 O  O   . HOH SA 8 .   ? 53.323  -1.090  76.393  1.00 42.21 ? 2153 HOH A O   1 
HETATM 11252 O  O   . HOH SA 8 .   ? 49.692  1.361   78.290  1.00 28.10 ? 2154 HOH A O   1 
HETATM 11253 O  O   . HOH SA 8 .   ? 62.223  31.434  44.169  1.00 24.24 ? 2155 HOH A O   1 
HETATM 11254 O  O   . HOH SA 8 .   ? 68.034  36.124  45.518  1.00 43.64 ? 2156 HOH A O   1 
HETATM 11255 O  O   . HOH SA 8 .   ? 57.869  4.826   76.301  1.00 12.15 ? 2157 HOH A O   1 
HETATM 11256 O  O   . HOH SA 8 .   ? 56.416  -1.892  77.291  1.00 29.24 ? 2158 HOH A O   1 
HETATM 11257 O  O   . HOH SA 8 .   ? 59.804  -4.162  78.717  1.00 34.25 ? 2159 HOH A O   1 
HETATM 11258 O  O   . HOH SA 8 .   ? 41.559  14.839  64.057  1.00 40.02 ? 2160 HOH A O   1 
HETATM 11259 O  O   . HOH SA 8 .   ? 76.549  0.108   66.834  1.00 25.88 ? 2161 HOH A O   1 
HETATM 11260 O  O   . HOH SA 8 .   ? 74.149  0.324   65.567  1.00 29.50 ? 2162 HOH A O   1 
HETATM 11261 O  O   . HOH SA 8 .   ? 42.101  24.680  61.054  1.00 30.49 ? 2163 HOH A O   1 
HETATM 11262 O  O   . HOH SA 8 .   ? 75.149  3.599   71.241  1.00 16.40 ? 2164 HOH A O   1 
HETATM 11263 O  O   . HOH SA 8 .   ? 76.552  -0.569  64.226  1.00 49.30 ? 2165 HOH A O   1 
HETATM 11264 O  O   . HOH SA 8 .   ? 75.005  -2.912  59.270  1.00 36.58 ? 2166 HOH A O   1 
HETATM 11265 O  O   . HOH SA 8 .   ? 76.355  6.968   57.471  1.00 17.72 ? 2167 HOH A O   1 
HETATM 11266 O  O   . HOH SA 8 .   ? 48.088  10.865  41.541  1.00 28.97 ? 2168 HOH A O   1 
HETATM 11267 O  O   . HOH SA 8 .   ? 77.556  13.414  64.495  1.00 13.33 ? 2169 HOH A O   1 
HETATM 11268 O  O   . HOH SA 8 .   ? 77.020  10.822  58.558  1.00 38.32 ? 2170 HOH A O   1 
HETATM 11269 O  O   . HOH SA 8 .   ? 81.364  13.839  58.266  1.00 16.63 ? 2171 HOH A O   1 
HETATM 11270 O  O   . HOH SA 8 .   ? 78.030  13.174  57.373  1.00 15.32 ? 2172 HOH A O   1 
HETATM 11271 O  O   . HOH SA 8 .   ? 53.517  14.284  37.775  1.00 33.84 ? 2173 HOH A O   1 
HETATM 11272 O  O   . HOH SA 8 .   ? 56.251  15.070  32.933  1.00 36.25 ? 2174 HOH A O   1 
HETATM 11273 O  O   . HOH SA 8 .   ? 55.334  23.941  29.243  1.00 39.00 ? 2175 HOH A O   1 
HETATM 11274 O  O   . HOH SA 8 .   ? 51.495  22.270  31.290  1.00 39.88 ? 2176 HOH A O   1 
HETATM 11275 O  O   . HOH SA 8 .   ? 55.035  27.151  33.152  1.00 29.66 ? 2177 HOH A O   1 
HETATM 11276 O  O   . HOH SA 8 .   ? 69.221  17.668  64.968  1.00 16.09 ? 2178 HOH A O   1 
HETATM 11277 O  O   . HOH SA 8 .   ? 54.774  19.927  79.671  1.00 29.52 ? 2179 HOH A O   1 
HETATM 11278 O  O   . HOH SA 8 .   ? 71.837  -16.615 53.368  1.00 42.26 ? 2180 HOH A O   1 
HETATM 11279 O  O   . HOH SA 8 .   ? 60.066  20.205  82.712  1.00 32.87 ? 2181 HOH A O   1 
HETATM 11280 O  O   . HOH SA 8 .   ? 64.398  23.591  79.346  1.00 14.00 ? 2182 HOH A O   1 
HETATM 11281 O  O   . HOH SA 8 .   ? 74.724  14.354  86.066  1.00 19.81 ? 2183 HOH A O   1 
HETATM 11282 O  O   . HOH SA 8 .   ? 77.087  13.207  82.478  1.00 24.85 ? 2184 HOH A O   1 
HETATM 11283 O  O   . HOH SA 8 .   ? 77.231  15.188  85.348  1.00 27.07 ? 2185 HOH A O   1 
HETATM 11284 O  O   . HOH SA 8 .   ? 79.169  25.128  79.873  1.00 33.23 ? 2186 HOH A O   1 
HETATM 11285 O  O   . HOH SA 8 .   ? 80.560  18.179  78.984  1.00 15.86 ? 2187 HOH A O   1 
HETATM 11286 O  O   . HOH SA 8 .   ? 79.533  27.945  74.600  1.00 21.42 ? 2188 HOH A O   1 
HETATM 11287 O  O   . HOH SA 8 .   ? 83.017  21.512  75.629  1.00 28.57 ? 2189 HOH A O   1 
HETATM 11288 O  O   . HOH SA 8 .   ? 78.715  25.771  71.606  1.00 12.08 ? 2190 HOH A O   1 
HETATM 11289 O  O   . HOH SA 8 .   ? 81.460  29.411  71.139  1.00 27.85 ? 2191 HOH A O   1 
HETATM 11290 O  O   . HOH SA 8 .   ? 82.480  26.035  64.008  1.00 18.39 ? 2192 HOH A O   1 
HETATM 11291 O  O   . HOH SA 8 .   ? 82.357  28.203  66.140  1.00 32.72 ? 2193 HOH A O   1 
HETATM 11292 O  O   . HOH SA 8 .   ? 78.834  28.481  72.259  1.00 24.53 ? 2194 HOH A O   1 
HETATM 11293 O  O   . HOH SA 8 .   ? 84.354  9.798   64.276  1.00 32.40 ? 2195 HOH A O   1 
HETATM 11294 O  O   . HOH SA 8 .   ? 80.321  14.537  72.650  1.00 14.72 ? 2196 HOH A O   1 
HETATM 11295 O  O   . HOH SA 8 .   ? 82.361  11.616  71.782  1.00 21.26 ? 2197 HOH A O   1 
HETATM 11296 O  O   . HOH SA 8 .   ? 83.687  12.352  74.282  1.00 28.10 ? 2198 HOH A O   1 
HETATM 11297 O  O   . HOH SA 8 .   ? 84.208  10.369  70.642  1.00 28.39 ? 2199 HOH A O   1 
HETATM 11298 O  O   . HOH SA 8 .   ? 85.185  6.615   68.362  1.00 37.02 ? 2200 HOH A O   1 
HETATM 11299 O  O   . HOH SA 8 .   ? 82.300  1.226   71.536  1.00 29.64 ? 2201 HOH A O   1 
HETATM 11300 O  O   . HOH SA 8 .   ? 83.369  2.354   75.040  1.00 42.96 ? 2202 HOH A O   1 
HETATM 11301 O  O   . HOH SA 8 .   ? 76.256  -2.306  80.427  1.00 36.24 ? 2203 HOH A O   1 
HETATM 11302 O  O   . HOH SA 8 .   ? 75.181  -2.437  75.941  1.00 20.29 ? 2204 HOH A O   1 
HETATM 11303 O  O   . HOH SA 8 .   ? 77.118  3.411   74.163  1.00 26.97 ? 2205 HOH A O   1 
HETATM 11304 O  O   . HOH SA 8 .   ? 71.640  4.133   80.352  1.00 25.20 ? 2206 HOH A O   1 
HETATM 11305 O  O   . HOH SA 8 .   ? 75.266  3.757   90.966  1.00 35.29 ? 2207 HOH A O   1 
HETATM 11306 O  O   . HOH SA 8 .   ? 72.681  -4.696  85.757  1.00 33.17 ? 2208 HOH A O   1 
HETATM 11307 O  O   . HOH SA 8 .   ? 74.322  -0.943  84.964  1.00 40.59 ? 2209 HOH A O   1 
HETATM 11308 O  O   . HOH SA 8 .   ? 67.883  1.575   92.115  1.00 32.48 ? 2210 HOH A O   1 
HETATM 11309 O  O   . HOH SA 8 .   ? 73.965  0.015   88.485  1.00 41.41 ? 2211 HOH A O   1 
HETATM 11310 O  O   . HOH SA 8 .   ? 63.325  5.090   86.818  1.00 22.62 ? 2212 HOH A O   1 
HETATM 11311 O  O   . HOH SA 8 .   ? 64.379  -1.631  87.888  1.00 36.71 ? 2213 HOH A O   1 
HETATM 11312 O  O   . HOH SA 8 .   ? 65.384  11.394  90.204  1.00 30.50 ? 2214 HOH A O   1 
HETATM 11313 O  O   . HOH SA 8 .   ? 67.628  9.921   90.812  1.00 24.26 ? 2215 HOH A O   1 
HETATM 11314 O  O   . HOH SA 8 .   ? 65.901  9.173   93.043  1.00 27.23 ? 2216 HOH A O   1 
HETATM 11315 O  O   . HOH SA 8 .   ? 62.661  10.217  90.493  1.00 22.88 ? 2217 HOH A O   1 
HETATM 11316 O  O   . HOH SA 8 .   ? 61.361  4.313   90.245  1.00 34.49 ? 2218 HOH A O   1 
HETATM 11317 O  O   . HOH SA 8 .   ? 59.630  7.660   93.036  1.00 33.10 ? 2219 HOH A O   1 
HETATM 11318 O  O   . HOH SA 8 .   ? 57.001  12.208  86.069  1.00 33.23 ? 2220 HOH A O   1 
HETATM 11319 O  O   . HOH SA 8 .   ? 62.130  6.426   90.186  1.00 19.67 ? 2221 HOH A O   1 
HETATM 11320 O  O   . HOH SA 8 .   ? 57.996  10.819  90.867  1.00 30.99 ? 2222 HOH A O   1 
HETATM 11321 O  O   . HOH SA 8 .   ? 62.130  14.525  82.181  1.00 14.27 ? 2223 HOH A O   1 
HETATM 11322 O  O   . HOH SA 8 .   ? 55.651  9.664   84.896  1.00 22.98 ? 2224 HOH A O   1 
HETATM 11323 O  O   . HOH SA 8 .   ? 60.023  0.386   85.856  1.00 35.61 ? 2225 HOH A O   1 
HETATM 11324 O  O   . HOH SA 8 .   ? 61.987  2.715   87.260  1.00 22.33 ? 2226 HOH A O   1 
HETATM 11325 O  O   . HOH SA 8 .   ? 63.508  -2.641  85.421  1.00 26.19 ? 2227 HOH A O   1 
HETATM 11326 O  O   . HOH SA 8 .   ? 59.527  -6.942  84.375  1.00 38.31 ? 2228 HOH A O   1 
HETATM 11327 O  O   . HOH SA 8 .   ? 60.673  -8.333  78.199  1.00 42.50 ? 2229 HOH A O   1 
HETATM 11328 O  O   . HOH SA 8 .   ? 61.617  -4.965  82.551  1.00 37.62 ? 2230 HOH A O   1 
HETATM 11329 O  O   . HOH SA 8 .   ? 65.407  -10.597 72.760  1.00 43.52 ? 2231 HOH A O   1 
HETATM 11330 O  O   . HOH SA 8 .   ? 62.784  -8.864  76.231  1.00 21.58 ? 2232 HOH A O   1 
HETATM 11331 O  O   . HOH SA 8 .   ? 60.176  -12.558 67.286  1.00 39.30 ? 2233 HOH A O   1 
HETATM 11332 O  O   . HOH SA 8 .   ? 69.093  -11.233 71.946  1.00 36.82 ? 2234 HOH A O   1 
HETATM 11333 O  O   . HOH SA 8 .   ? 72.544  -12.377 64.591  1.00 25.93 ? 2235 HOH A O   1 
HETATM 11334 O  O   . HOH SA 8 .   ? 69.523  -13.793 61.788  1.00 25.37 ? 2236 HOH A O   1 
HETATM 11335 O  O   . HOH SA 8 .   ? 65.886  -11.458 61.097  1.00 28.45 ? 2237 HOH A O   1 
HETATM 11336 O  O   . HOH SA 8 .   ? 63.937  -12.605 62.685  1.00 25.30 ? 2238 HOH A O   1 
HETATM 11337 O  O   . HOH SA 8 .   ? 71.204  -11.751 62.167  1.00 22.62 ? 2239 HOH A O   1 
HETATM 11338 O  O   . HOH SA 8 .   ? 65.584  -7.293  53.169  1.00 28.33 ? 2240 HOH A O   1 
HETATM 11339 O  O   . HOH SA 8 .   ? 65.345  -9.332  59.088  1.00 30.81 ? 2241 HOH A O   1 
HETATM 11340 O  O   . HOH SA 8 .   ? 63.908  -9.200  56.610  1.00 22.78 ? 2242 HOH A O   1 
HETATM 11341 O  O   . HOH SA 8 .   ? 56.917  -3.817  58.738  1.00 17.27 ? 2243 HOH A O   1 
HETATM 11342 O  O   . HOH SA 8 .   ? 58.808  -1.049  59.423  1.00 17.99 ? 2244 HOH A O   1 
HETATM 11343 O  O   . HOH SA 8 .   ? 65.566  -4.381  55.124  1.00 21.39 ? 2245 HOH A O   1 
HETATM 11344 O  O   . HOH SA 8 .   ? 64.430  -1.583  47.953  1.00 30.31 ? 2246 HOH A O   1 
HETATM 11345 O  O   . HOH SA 8 .   ? 61.457  -2.755  47.045  1.00 35.14 ? 2247 HOH A O   1 
HETATM 11346 O  O   . HOH SA 8 .   ? 57.861  -3.767  47.810  1.00 33.28 ? 2248 HOH A O   1 
HETATM 11347 O  O   . HOH SA 8 .   ? 59.072  -5.830  51.371  1.00 29.70 ? 2249 HOH A O   1 
HETATM 11348 O  O   . HOH SA 8 .   ? 62.377  -5.547  54.543  1.00 20.06 ? 2250 HOH A O   1 
HETATM 11349 O  O   . HOH SA 8 .   ? 55.348  -1.430  48.713  1.00 26.51 ? 2251 HOH A O   1 
HETATM 11350 O  O   . HOH SA 8 .   ? 54.675  -2.958  52.381  1.00 21.87 ? 2252 HOH A O   1 
HETATM 11351 O  O   . HOH SA 8 .   ? 51.846  3.309   53.298  1.00 23.56 ? 2253 HOH A O   1 
HETATM 11352 O  O   . HOH SA 8 .   ? 60.302  0.518   54.081  1.00 16.24 ? 2254 HOH A O   1 
HETATM 11353 O  O   . HOH SA 8 .   ? 55.855  -1.454  57.632  1.00 21.00 ? 2255 HOH A O   1 
HETATM 11354 O  O   . HOH SA 8 .   ? 52.811  -0.157  61.359  1.00 45.36 ? 2256 HOH A O   1 
HETATM 11355 O  O   . HOH SA 8 .   ? 53.313  -1.134  56.489  1.00 35.55 ? 2257 HOH A O   1 
HETATM 11356 O  O   . HOH SA 8 .   ? 48.072  0.945   59.660  1.00 16.18 ? 2258 HOH A O   1 
HETATM 11357 O  O   . HOH SA 8 .   ? 49.317  4.630   57.233  1.00 15.67 ? 2259 HOH A O   1 
HETATM 11358 O  O   . HOH SA 8 .   ? 49.476  -0.893  63.659  1.00 23.83 ? 2260 HOH A O   1 
HETATM 11359 O  O   . HOH SA 8 .   ? 44.865  3.264   70.869  1.00 20.46 ? 2261 HOH A O   1 
HETATM 11360 O  O   . HOH SA 8 .   ? 51.827  1.447   74.485  1.00 24.59 ? 2262 HOH A O   1 
HETATM 11361 O  O   . HOH SA 8 .   ? 48.012  -0.416  65.903  1.00 19.09 ? 2263 HOH A O   1 
HETATM 11362 O  O   . HOH SA 8 .   ? 50.889  4.470   67.475  1.00 11.81 ? 2264 HOH A O   1 
HETATM 11363 O  O   . HOH SA 8 .   ? 54.342  -2.109  65.083  1.00 36.39 ? 2265 HOH A O   1 
HETATM 11364 O  O   . HOH SA 8 .   ? 52.362  -0.587  64.076  1.00 36.22 ? 2266 HOH A O   1 
HETATM 11365 O  O   . HOH SA 8 .   ? 55.593  0.794   59.444  1.00 33.07 ? 2267 HOH A O   1 
HETATM 11366 O  O   . HOH SA 8 .   ? 56.651  -0.321  61.267  1.00 20.81 ? 2268 HOH A O   1 
HETATM 11367 O  O   . HOH SA 8 .   ? 60.899  8.381   56.963  1.00 12.08 ? 2269 HOH A O   1 
HETATM 11368 O  O   . HOH SA 8 .   ? 64.455  7.609   49.990  1.00 17.56 ? 2270 HOH A O   1 
HETATM 11369 O  O   . HOH SA 8 .   ? 61.121  11.468  52.055  1.00 20.44 ? 2271 HOH A O   1 
HETATM 11370 O  O   . HOH SA 8 .   ? 59.707  9.382   54.799  1.00 10.53 ? 2272 HOH A O   1 
HETATM 11371 O  O   . HOH SA 8 .   ? 57.632  5.020   47.741  1.00 23.76 ? 2273 HOH A O   1 
HETATM 11372 O  O   . HOH SA 8 .   ? 54.384  4.025   50.205  1.00 39.38 ? 2274 HOH A O   1 
HETATM 11373 O  O   . HOH SA 8 .   ? 57.387  8.779   53.811  1.00 14.98 ? 2275 HOH A O   1 
HETATM 11374 O  O   . HOH SA 8 .   ? 55.006  9.078   55.391  1.00 11.54 ? 2276 HOH A O   1 
HETATM 11375 O  O   . HOH SA 8 .   ? 55.040  5.751   47.610  1.00 37.24 ? 2277 HOH A O   1 
HETATM 11376 O  O   . HOH SA 8 .   ? 48.991  8.829   50.414  1.00 37.56 ? 2278 HOH A O   1 
HETATM 11377 O  O   . HOH SA 8 .   ? 48.588  9.484   56.331  1.00 20.71 ? 2279 HOH A O   1 
HETATM 11378 O  O   . HOH SA 8 .   ? 45.469  23.832  50.104  1.00 18.91 ? 2280 HOH A O   1 
HETATM 11379 O  O   . HOH SA 8 .   ? 51.292  23.974  48.105  1.00 14.14 ? 2281 HOH A O   1 
HETATM 11380 O  O   . HOH SA 8 .   ? 48.515  19.331  40.544  1.00 28.91 ? 2282 HOH A O   1 
HETATM 11381 O  O   . HOH SA 8 .   ? 47.395  29.944  46.357  1.00 34.44 ? 2283 HOH A O   1 
HETATM 11382 O  O   . HOH SA 8 .   ? 41.739  28.684  46.818  1.00 26.89 ? 2284 HOH A O   1 
HETATM 11383 O  O   . HOH SA 8 .   ? 44.661  29.809  48.206  1.00 35.40 ? 2285 HOH A O   1 
HETATM 11384 O  O   . HOH SA 8 .   ? 55.871  25.216  47.335  1.00 28.04 ? 2286 HOH A O   1 
HETATM 11385 O  O   . HOH SA 8 .   ? 50.967  14.585  60.010  1.00 16.66 ? 2287 HOH A O   1 
HETATM 11386 O  O   . HOH SA 8 .   ? 44.075  6.226   68.516  1.00 24.19 ? 2288 HOH A O   1 
HETATM 11387 O  O   . HOH SA 8 .   ? 45.204  8.895   60.435  1.00 23.30 ? 2289 HOH A O   1 
HETATM 11388 O  O   . HOH SA 8 .   ? 50.614  6.406   69.591  1.00 14.60 ? 2290 HOH A O   1 
HETATM 11389 O  O   . HOH SA 8 .   ? 49.329  8.767   71.878  1.00 12.46 ? 2291 HOH A O   1 
HETATM 11390 O  O   . HOH SA 8 .   ? 47.216  7.154   60.266  1.00 18.04 ? 2292 HOH A O   1 
HETATM 11391 O  O   . HOH SA 8 .   ? 43.590  6.875   72.450  1.00 48.98 ? 2293 HOH A O   1 
HETATM 11392 O  O   . HOH SA 8 .   ? 43.271  15.749  71.951  1.00 33.50 ? 2294 HOH A O   1 
HETATM 11393 O  O   . HOH SA 8 .   ? 45.148  14.311  68.407  1.00 23.56 ? 2295 HOH A O   1 
HETATM 11394 O  O   . HOH SA 8 .   ? 50.890  16.994  74.496  1.00 22.03 ? 2296 HOH A O   1 
HETATM 11395 O  O   . HOH SA 8 .   ? 50.262  19.784  72.004  1.00 24.21 ? 2297 HOH A O   1 
HETATM 11396 O  O   . HOH SA 8 .   ? 47.047  15.553  66.132  1.00 20.83 ? 2298 HOH A O   1 
HETATM 11397 O  O   . HOH SA 8 .   ? 57.983  15.146  52.540  1.00 11.50 ? 2299 HOH A O   1 
HETATM 11398 O  O   . HOH SA 8 .   ? 60.370  11.995  54.511  1.00 9.62  ? 2300 HOH A O   1 
HETATM 11399 O  O   . HOH SA 8 .   ? 57.775  33.557  44.283  1.00 29.07 ? 2301 HOH A O   1 
HETATM 11400 O  O   . HOH SA 8 .   ? 54.360  29.140  48.571  1.00 17.83 ? 2302 HOH A O   1 
HETATM 11401 O  O   . HOH SA 8 .   ? 55.439  34.810  44.483  1.00 21.08 ? 2303 HOH A O   1 
HETATM 11402 O  O   . HOH SA 8 .   ? 48.245  33.418  44.923  1.00 33.51 ? 2304 HOH A O   1 
HETATM 11403 O  O   . HOH SA 8 .   ? 48.609  31.962  47.545  1.00 23.73 ? 2305 HOH A O   1 
HETATM 11404 O  O   . HOH SA 8 .   ? 55.001  36.030  47.318  1.00 32.67 ? 2306 HOH A O   1 
HETATM 11405 O  O   . HOH SA 8 .   ? 54.010  30.300  53.641  1.00 11.59 ? 2307 HOH A O   1 
HETATM 11406 O  O   . HOH SA 8 .   ? 50.006  38.875  56.203  1.00 37.61 ? 2308 HOH A O   1 
HETATM 11407 O  O   . HOH SA 8 .   ? 44.616  32.128  62.031  1.00 14.09 ? 2309 HOH A O   1 
HETATM 11408 O  O   . HOH SA 8 .   ? 47.880  35.957  64.063  1.00 36.99 ? 2310 HOH A O   1 
HETATM 11409 O  O   . HOH SA 8 .   ? 46.041  32.202  65.139  1.00 17.15 ? 2311 HOH A O   1 
HETATM 11410 O  O   . HOH SA 8 .   ? 46.418  30.491  69.989  1.00 40.08 ? 2312 HOH A O   1 
HETATM 11411 O  O   . HOH SA 8 .   ? 49.142  27.905  71.541  1.00 26.38 ? 2313 HOH A O   1 
HETATM 11412 O  O   . HOH SA 8 .   ? 51.074  25.823  71.422  1.00 16.82 ? 2314 HOH A O   1 
HETATM 11413 O  O   . HOH SA 8 .   ? 71.738  18.163  53.913  1.00 38.11 ? 2315 HOH A O   1 
HETATM 11414 O  O   . HOH SA 8 .   ? 66.645  14.900  51.696  1.00 20.31 ? 2316 HOH A O   1 
HETATM 11415 O  O   . HOH SA 8 .   ? 71.251  24.188  52.420  1.00 35.53 ? 2317 HOH A O   1 
HETATM 11416 O  O   . HOH SA 8 .   ? 67.976  27.587  44.006  1.00 17.86 ? 2318 HOH A O   1 
HETATM 11417 O  O   . HOH SA 8 .   ? 56.821  39.262  52.668  1.00 32.20 ? 2319 HOH A O   1 
HETATM 11418 O  O   . HOH SA 8 .   ? 58.935  36.408  53.046  1.00 32.38 ? 2320 HOH A O   1 
HETATM 11419 O  O   . HOH SA 8 .   ? 54.757  39.112  57.858  1.00 35.56 ? 2321 HOH A O   1 
HETATM 11420 O  O   . HOH SA 8 .   ? 58.195  40.485  58.870  1.00 23.83 ? 2322 HOH A O   1 
HETATM 11421 O  O   . HOH SA 8 .   ? 57.396  39.720  65.517  1.00 37.75 ? 2323 HOH A O   1 
HETATM 11422 O  O   . HOH SA 8 .   ? 59.448  38.742  70.025  1.00 42.30 ? 2324 HOH A O   1 
HETATM 11423 O  O   . HOH SA 8 .   ? 65.193  39.868  61.809  1.00 21.81 ? 2325 HOH A O   1 
HETATM 11424 O  O   . HOH SA 8 .   ? 61.611  35.607  60.098  1.00 17.52 ? 2326 HOH A O   1 
HETATM 11425 O  O   . HOH SA 8 .   ? 62.055  40.751  55.540  1.00 31.44 ? 2327 HOH A O   1 
HETATM 11426 O  O   . HOH SA 8 .   ? 67.186  37.316  61.013  1.00 25.01 ? 2328 HOH A O   1 
HETATM 11427 O  O   . HOH SA 8 .   ? 70.034  33.200  49.176  1.00 35.24 ? 2329 HOH A O   1 
HETATM 11428 O  O   . HOH SA 8 .   ? 72.112  30.567  50.784  1.00 25.81 ? 2330 HOH A O   1 
HETATM 11429 O  O   . HOH SA 8 .   ? 70.002  28.778  53.480  1.00 26.90 ? 2331 HOH A O   1 
HETATM 11430 O  O   . HOH SA 8 .   ? 69.182  34.762  55.861  1.00 17.51 ? 2332 HOH A O   1 
HETATM 11431 O  O   . HOH SA 8 .   ? 73.771  24.253  58.297  1.00 9.45  ? 2333 HOH A O   1 
HETATM 11432 O  O   . HOH SA 8 .   ? 73.632  26.713  59.731  1.00 13.00 ? 2334 HOH A O   1 
HETATM 11433 O  O   . HOH SA 8 .   ? 52.557  28.324  65.147  1.00 12.22 ? 2335 HOH A O   1 
HETATM 11434 O  O   . HOH SA 8 .   ? 50.578  34.711  69.930  1.00 25.96 ? 2336 HOH A O   1 
HETATM 11435 O  O   . HOH SA 8 .   ? 51.622  31.553  71.784  1.00 25.15 ? 2337 HOH A O   1 
HETATM 11436 O  O   . HOH SA 8 .   ? 52.830  29.132  71.308  1.00 21.78 ? 2338 HOH A O   1 
HETATM 11437 O  O   . HOH SA 8 .   ? 50.394  37.555  68.157  1.00 45.09 ? 2339 HOH A O   1 
HETATM 11438 O  O   . HOH SA 8 .   ? 47.175  36.143  67.251  1.00 43.37 ? 2340 HOH A O   1 
HETATM 11439 O  O   . HOH SA 8 .   ? 49.645  37.624  65.114  1.00 40.01 ? 2341 HOH A O   1 
HETATM 11440 O  O   . HOH SA 8 .   ? 51.200  30.444  63.859  1.00 18.01 ? 2342 HOH A O   1 
HETATM 11441 O  O   . HOH SA 8 .   ? 52.086  39.534  62.196  1.00 37.94 ? 2343 HOH A O   1 
HETATM 11442 O  O   . HOH SA 8 .   ? 51.958  37.868  64.061  1.00 29.07 ? 2344 HOH A O   1 
HETATM 11443 O  O   . HOH SA 8 .   ? 52.585  40.282  53.731  1.00 33.86 ? 2345 HOH A O   1 
HETATM 11444 O  O   . HOH SA 8 .   ? 53.085  40.144  49.856  1.00 40.70 ? 2346 HOH A O   1 
HETATM 11445 O  O   . HOH SA 8 .   ? 54.744  28.375  51.116  1.00 21.34 ? 2347 HOH A O   1 
HETATM 11446 O  O   . HOH SA 8 .   ? 52.551  27.051  52.357  1.00 16.93 ? 2348 HOH A O   1 
HETATM 11447 O  O   . HOH SA 8 .   ? 61.586  37.259  51.439  1.00 30.92 ? 2349 HOH A O   1 
HETATM 11448 O  O   . HOH SA 8 .   ? 58.225  27.445  48.182  1.00 11.45 ? 2350 HOH A O   1 
HETATM 11449 O  O   . HOH SA 8 .   ? 60.225  30.262  46.086  1.00 15.11 ? 2351 HOH A O   1 
HETATM 11450 O  O   . HOH SA 8 .   ? 65.721  34.756  44.583  1.00 41.66 ? 2352 HOH A O   1 
HETATM 11451 O  O   . HOH SA 8 .   ? 69.538  33.719  46.608  1.00 50.34 ? 2353 HOH A O   1 
HETATM 11452 O  O   . HOH SA 8 .   ? 64.637  30.554  44.120  1.00 26.94 ? 2354 HOH A O   1 
HETATM 11453 O  O   . HOH SA 8 .   ? 68.759  31.661  45.772  1.00 36.39 ? 2355 HOH A O   1 
HETATM 11454 O  O   . HOH SA 8 .   ? 64.754  28.905  37.169  1.00 31.03 ? 2356 HOH A O   1 
HETATM 11455 O  O   . HOH SA 8 .   ? 61.148  24.203  42.346  1.00 12.38 ? 2357 HOH A O   1 
HETATM 11456 O  O   . HOH SA 8 .   ? 67.818  29.406  42.014  1.00 28.29 ? 2358 HOH A O   1 
HETATM 11457 O  O   . HOH SA 8 .   ? 68.212  21.355  47.364  1.00 16.14 ? 2359 HOH A O   1 
HETATM 11458 O  O   . HOH SA 8 .   ? 65.385  12.494  51.253  1.00 15.25 ? 2360 HOH A O   1 
HETATM 11459 O  O   . HOH SA 8 .   ? 66.888  12.907  55.001  1.00 22.46 ? 2361 HOH A O   1 
HETATM 11460 O  O   . HOH SA 8 .   ? 50.320  24.635  64.727  1.00 12.18 ? 2362 HOH A O   1 
HETATM 11461 O  O   . HOH SA 8 .   ? 50.497  23.881  73.238  1.00 28.58 ? 2363 HOH A O   1 
HETATM 11462 O  O   . HOH SA 8 .   ? 47.762  24.376  65.743  1.00 19.37 ? 2364 HOH A O   1 
HETATM 11463 O  O   . HOH SA 8 .   ? 49.046  19.970  64.165  1.00 18.73 ? 2365 HOH A O   1 
HETATM 11464 O  O   . HOH SA 8 .   ? 43.209  16.270  62.314  1.00 46.41 ? 2366 HOH A O   1 
HETATM 11465 O  O   . HOH SA 8 .   ? 43.811  21.076  67.867  1.00 26.97 ? 2367 HOH A O   1 
HETATM 11466 O  O   . HOH SA 8 .   ? 41.761  19.584  69.154  1.00 51.10 ? 2368 HOH A O   1 
HETATM 11467 O  O   . HOH SA 8 .   ? 45.463  22.945  65.335  1.00 27.12 ? 2369 HOH A O   1 
HETATM 11468 O  O   . HOH SA 8 .   ? 51.388  24.456  62.087  1.00 11.11 ? 2370 HOH A O   1 
HETATM 11469 O  O   . HOH SA 8 .   ? 48.698  14.568  58.436  1.00 30.10 ? 2371 HOH A O   1 
HETATM 11470 O  O   . HOH SA 8 .   ? 45.693  14.232  61.903  1.00 34.19 ? 2372 HOH A O   1 
HETATM 11471 O  O   . HOH SA 8 .   ? 44.874  12.977  56.887  1.00 39.74 ? 2373 HOH A O   1 
HETATM 11472 O  O   . HOH SA 8 .   ? 43.299  22.467  54.396  1.00 27.97 ? 2374 HOH A O   1 
HETATM 11473 O  O   . HOH SA 8 .   ? 43.818  24.971  53.853  0.50 23.31 ? 2375 HOH A O   1 
HETATM 11474 O  O   . HOH SA 8 .   ? 44.617  24.831  60.336  0.50 12.06 ? 2376 HOH A O   1 
HETATM 11475 O  O   . HOH SA 8 .   ? 45.661  24.975  52.552  0.50 16.83 ? 2377 HOH A O   1 
HETATM 11476 O  O   . HOH SA 8 .   ? 43.761  21.262  59.415  1.00 50.07 ? 2378 HOH A O   1 
HETATM 11477 O  O   . HOH SA 8 .   ? 44.249  14.491  51.317  1.00 35.73 ? 2379 HOH A O   1 
HETATM 11478 O  O   . HOH SA 8 .   ? 42.283  22.185  57.308  1.00 35.85 ? 2380 HOH A O   1 
HETATM 11479 O  O   . HOH SA 8 .   ? 42.462  22.214  47.964  1.00 21.47 ? 2381 HOH A O   1 
HETATM 11480 O  O   . HOH SA 8 .   ? 41.940  15.215  46.795  1.00 43.30 ? 2382 HOH A O   1 
HETATM 11481 O  O   . HOH SA 8 .   ? 47.677  18.304  44.581  1.00 18.54 ? 2383 HOH A O   1 
HETATM 11482 O  O   . HOH SA 8 .   ? 45.255  14.477  40.338  1.00 41.00 ? 2384 HOH A O   1 
HETATM 11483 O  O   . HOH SA 8 .   ? 44.654  7.515   52.721  1.00 54.93 ? 2385 HOH A O   1 
HETATM 11484 O  O   . HOH SA 8 .   ? 45.403  10.700  44.260  1.00 43.62 ? 2386 HOH A O   1 
HETATM 11485 O  O   . HOH SA 8 .   ? 43.424  12.073  47.175  1.00 29.78 ? 2387 HOH A O   1 
HETATM 11486 O  O   . HOH SA 8 .   ? 43.011  9.743   46.202  1.00 54.18 ? 2388 HOH A O   1 
HETATM 11487 O  O   . HOH SA 8 .   ? 44.679  5.164   50.930  1.00 47.79 ? 2389 HOH A O   1 
HETATM 11488 O  O   . HOH SA 8 .   ? 51.792  7.705   49.122  1.00 26.92 ? 2390 HOH A O   1 
HETATM 11489 O  O   . HOH SA 8 .   ? 52.719  10.281  41.441  1.00 47.96 ? 2391 HOH A O   1 
HETATM 11490 O  O   . HOH SA 8 .   ? 57.638  7.072   46.423  1.00 33.92 ? 2392 HOH A O   1 
HETATM 11491 O  O   . HOH SA 8 .   ? 50.292  9.440   42.576  1.00 30.71 ? 2393 HOH A O   1 
HETATM 11492 O  O   . HOH SA 8 .   ? 57.464  6.339   42.806  1.00 39.72 ? 2394 HOH A O   1 
HETATM 11493 O  O   . HOH SA 8 .   ? 57.833  8.470   41.347  1.00 17.20 ? 2395 HOH A O   1 
HETATM 11494 O  O   . HOH SA 8 .   ? 59.772  14.186  49.051  1.00 14.36 ? 2396 HOH A O   1 
HETATM 11495 O  O   . HOH SA 8 .   ? 55.322  15.439  35.770  1.00 20.50 ? 2397 HOH A O   1 
HETATM 11496 O  O   . HOH SA 8 .   ? 55.966  22.885  31.889  1.00 28.07 ? 2398 HOH A O   1 
HETATM 11497 O  O   . HOH SA 8 .   ? 55.519  19.914  29.369  1.00 33.47 ? 2399 HOH A O   1 
HETATM 11498 O  O   . HOH SA 8 .   ? 53.648  17.384  35.051  1.00 23.48 ? 2400 HOH A O   1 
HETATM 11499 O  O   . HOH SA 8 .   ? 52.095  24.013  33.362  1.00 29.22 ? 2401 HOH A O   1 
HETATM 11500 O  O   . HOH SA 8 .   ? 54.672  24.418  33.688  1.00 16.78 ? 2402 HOH A O   1 
HETATM 11501 O  O   . HOH SA 8 .   ? 48.514  4.190   75.006  1.00 27.35 ? 2403 HOH A O   1 
HETATM 11502 O  O   . HOH SA 8 .   ? 70.464  -4.723  47.997  1.00 24.57 ? 2404 HOH A O   1 
HETATM 11503 O  O   . HOH SA 8 .   ? 71.732  -6.426  52.045  1.00 23.12 ? 2405 HOH A O   1 
HETATM 11504 O  O   . HOH SA 8 .   ? 70.442  -13.504 52.888  1.00 36.61 ? 2406 HOH A O   1 
HETATM 11505 O  O   . HOH SA 8 .   ? 70.752  -13.947 48.792  1.00 35.54 ? 2407 HOH A O   1 
HETATM 11506 O  O   . HOH SA 8 .   ? 46.606  26.797  72.305  1.00 43.44 ? 2408 HOH A O   1 
HETATM 11507 O  O   . HOH SA 8 .   ? 49.237  -5.169  77.317  1.00 41.66 ? 2409 HOH A O   1 
HETATM 11508 O  O   . HOH SA 8 .   ? 45.962  -4.489  78.706  1.00 34.56 ? 2410 HOH A O   1 
HETATM 11509 O  O   . HOH SA 8 .   ? 61.667  -16.320 43.427  1.00 46.24 ? 2411 HOH A O   1 
HETATM 11510 O  O   . HOH SA 8 .   ? 72.288  -10.777 38.948  1.00 30.25 ? 2412 HOH A O   1 
HETATM 11511 O  O   . HOH SA 8 .   ? 71.975  -19.325 34.601  1.00 43.84 ? 2413 HOH A O   1 
HETATM 11512 O  O   . HOH SA 8 .   ? 67.940  -6.069  35.612  1.00 32.82 ? 2414 HOH A O   1 
HETATM 11513 O  O   . HOH SA 8 .   ? 67.945  13.477  69.656  1.00 12.98 ? 2415 HOH A O   1 
HETATM 11514 O  O   . HOH SA 8 .   ? 72.839  7.949   77.049  1.00 18.99 ? 2416 HOH A O   1 
HETATM 11515 O  O   . HOH TA 8 .   ? 67.077  6.401   7.432   1.00 51.21 ? 2001 HOH B O   1 
HETATM 11516 O  O   . HOH TA 8 .   ? 67.640  24.514  8.813   1.00 22.03 ? 2002 HOH B O   1 
HETATM 11517 O  O   . HOH TA 8 .   ? 71.360  14.900  16.748  1.00 38.05 ? 2003 HOH B O   1 
HETATM 11518 O  O   . HOH TA 8 .   ? 67.622  21.789  9.046   0.50 11.16 ? 2004 HOH B O   1 
HETATM 11519 O  O   . HOH TA 8 .   ? 69.120  17.390  3.202   1.00 20.92 ? 2005 HOH B O   1 
HETATM 11520 O  O   . HOH TA 8 .   ? 68.827  15.402  10.836  1.00 23.10 ? 2006 HOH B O   1 
HETATM 11521 O  O   . HOH TA 8 .   ? 70.043  6.503   13.971  1.00 41.55 ? 2007 HOH B O   1 
HETATM 11522 O  O   . HOH TA 8 .   ? 68.636  17.629  12.742  1.00 25.34 ? 2008 HOH B O   1 
HETATM 11523 O  O   . HOH TA 8 .   ? 71.283  14.382  12.965  1.00 25.88 ? 2009 HOH B O   1 
HETATM 11524 O  O   . HOH TA 8 .   ? 68.390  21.461  11.840  1.00 29.90 ? 2010 HOH B O   1 
HETATM 11525 O  O   . HOH TA 8 .   ? 70.977  21.947  15.684  1.00 32.70 ? 2011 HOH B O   1 
HETATM 11526 O  O   . HOH TA 8 .   ? 76.035  23.738  18.732  1.00 35.94 ? 2012 HOH B O   1 
HETATM 11527 O  O   . HOH TA 8 .   ? 71.858  15.086  21.592  1.00 35.24 ? 2013 HOH B O   1 
HETATM 11528 O  O   . HOH TA 8 .   ? 76.648  12.983  22.147  1.00 16.16 ? 2014 HOH B O   1 
HETATM 11529 O  O   . HOH TA 8 .   ? 70.412  10.354  18.303  1.00 33.38 ? 2015 HOH B O   1 
HETATM 11530 O  O   . HOH TA 8 .   ? 71.914  12.249  16.522  1.00 31.46 ? 2016 HOH B O   1 
HETATM 11531 O  O   . HOH TA 8 .   ? 77.843  9.872   13.234  1.00 16.14 ? 2017 HOH B O   1 
HETATM 11532 O  O   . HOH TA 8 .   ? 72.267  5.353   14.918  1.00 31.76 ? 2018 HOH B O   1 
HETATM 11533 O  O   . HOH TA 8 .   ? 79.063  7.214   19.243  1.00 29.88 ? 2019 HOH B O   1 
HETATM 11534 O  O   . HOH TA 8 .   ? 70.448  9.191   14.155  1.00 35.69 ? 2020 HOH B O   1 
HETATM 11535 O  O   . HOH TA 8 .   ? 88.697  10.124  22.368  1.00 33.73 ? 2021 HOH B O   1 
HETATM 11536 O  O   . HOH TA 8 .   ? 93.466  12.940  21.271  1.00 32.84 ? 2022 HOH B O   1 
HETATM 11537 O  O   . HOH TA 8 .   ? 92.727  8.762   20.041  1.00 30.46 ? 2023 HOH B O   1 
HETATM 11538 O  O   . HOH TA 8 .   ? 81.897  34.843  23.291  1.00 35.16 ? 2024 HOH B O   1 
HETATM 11539 O  O   . HOH TA 8 .   ? 69.048  15.277  -0.029  1.00 29.20 ? 2025 HOH B O   1 
HETATM 11540 O  O   . HOH TA 8 .   ? 71.048  12.640  -4.726  1.00 16.68 ? 2026 HOH B O   1 
HETATM 11541 O  O   . HOH TA 8 .   ? 68.529  12.638  -1.339  1.00 31.73 ? 2027 HOH B O   1 
HETATM 11542 O  O   . HOH TA 8 .   ? 72.688  21.091  -0.582  1.00 15.08 ? 2028 HOH B O   1 
HETATM 11543 O  O   . HOH TA 8 .   ? 80.414  41.780  4.949   1.00 28.79 ? 2029 HOH B O   1 
HETATM 11544 O  O   . HOH TA 8 .   ? 84.273  45.002  4.561   1.00 53.85 ? 2030 HOH B O   1 
HETATM 11545 O  O   . HOH TA 8 .   ? 72.281  26.214  6.518   1.00 17.44 ? 2031 HOH B O   1 
HETATM 11546 O  O   . HOH TA 8 .   ? 71.587  17.164  4.506   1.00 14.33 ? 2032 HOH B O   1 
HETATM 11547 O  O   . HOH TA 8 .   ? 69.840  27.196  15.356  1.00 22.68 ? 2033 HOH B O   1 
HETATM 11548 O  O   . HOH TA 8 .   ? 67.686  24.631  13.029  1.00 40.26 ? 2034 HOH B O   1 
HETATM 11549 O  O   . HOH TA 8 .   ? 95.614  13.488  19.012  1.00 28.90 ? 2035 HOH B O   1 
HETATM 11550 O  O   . HOH TA 8 .   ? 93.234  17.175  22.911  1.00 36.47 ? 2036 HOH B O   1 
HETATM 11551 O  O   . HOH TA 8 .   ? 88.282  18.888  22.986  1.00 34.39 ? 2037 HOH B O   1 
HETATM 11552 O  O   . HOH TA 8 .   ? 90.739  15.832  22.844  1.00 31.77 ? 2038 HOH B O   1 
HETATM 11553 O  O   . HOH TA 8 .   ? 76.188  21.077  20.211  1.00 46.36 ? 2039 HOH B O   1 
HETATM 11554 O  O   . HOH TA 8 .   ? 75.491  25.550  17.363  1.00 20.62 ? 2040 HOH B O   1 
HETATM 11555 O  O   . HOH TA 8 .   ? 76.385  16.564  19.093  1.00 23.25 ? 2041 HOH B O   1 
HETATM 11556 O  O   . HOH TA 8 .   ? 75.857  18.215  15.468  1.00 26.53 ? 2042 HOH B O   1 
HETATM 11557 O  O   . HOH TA 8 .   ? 110.452 16.994  -3.540  1.00 34.58 ? 2043 HOH B O   1 
HETATM 11558 O  O   . HOH TA 8 .   ? 72.581  26.540  15.310  1.00 16.14 ? 2044 HOH B O   1 
HETATM 11559 O  O   . HOH TA 8 .   ? 73.766  33.920  14.294  1.00 18.66 ? 2045 HOH B O   1 
HETATM 11560 O  O   . HOH TA 8 .   ? 77.373  36.906  13.806  1.00 29.72 ? 2046 HOH B O   1 
HETATM 11561 O  O   . HOH TA 8 .   ? 74.651  36.975  11.621  1.00 33.44 ? 2047 HOH B O   1 
HETATM 11562 O  O   . HOH TA 8 .   ? 76.674  36.837  10.121  1.00 13.89 ? 2048 HOH B O   1 
HETATM 11563 O  O   . HOH TA 8 .   ? 83.473  39.564  10.087  1.00 20.55 ? 2049 HOH B O   1 
HETATM 11564 O  O   . HOH TA 8 .   ? 77.240  34.864  8.104   1.00 19.56 ? 2050 HOH B O   1 
HETATM 11565 O  O   . HOH TA 8 .   ? 118.292 28.174  15.414  1.00 45.76 ? 2051 HOH B O   1 
HETATM 11566 O  O   . HOH TA 8 .   ? 115.567 33.490  17.550  1.00 46.24 ? 2052 HOH B O   1 
HETATM 11567 O  O   . HOH TA 8 .   ? 118.791 33.351  19.380  1.00 37.25 ? 2053 HOH B O   1 
HETATM 11568 O  O   . HOH TA 8 .   ? 86.469  37.411  8.241   1.00 14.65 ? 2054 HOH B O   1 
HETATM 11569 O  O   . HOH TA 8 .   ? 76.218  19.464  12.961  1.00 14.97 ? 2055 HOH B O   1 
HETATM 11570 O  O   . HOH TA 8 .   ? 80.064  24.721  4.047   1.00 18.43 ? 2056 HOH B O   1 
HETATM 11571 O  O   . HOH TA 8 .   ? 107.383 21.939  16.402  1.00 33.50 ? 2057 HOH B O   1 
HETATM 11572 O  O   . HOH TA 8 .   ? 77.400  16.375  16.730  1.00 25.10 ? 2058 HOH B O   1 
HETATM 11573 O  O   . HOH TA 8 .   ? 80.691  9.474   19.718  1.00 19.78 ? 2059 HOH B O   1 
HETATM 11574 O  O   . HOH TA 8 .   ? 85.746  6.905   15.573  1.00 14.90 ? 2060 HOH B O   1 
HETATM 11575 O  O   . HOH TA 8 .   ? 88.760  8.753   18.078  1.00 24.13 ? 2061 HOH B O   1 
HETATM 11576 O  O   . HOH TA 8 .   ? 90.465  12.205  20.695  1.00 25.79 ? 2062 HOH B O   1 
HETATM 11577 O  O   . HOH TA 8 .   ? 90.864  10.391  18.534  1.00 21.89 ? 2063 HOH B O   1 
HETATM 11578 O  O   . HOH TA 8 .   ? 87.128  14.497  22.978  1.00 28.04 ? 2064 HOH B O   1 
HETATM 11579 O  O   . HOH TA 8 .   ? 91.910  11.435  16.161  1.00 15.81 ? 2065 HOH B O   1 
HETATM 11580 O  O   . HOH TA 8 .   ? 88.337  18.884  16.180  1.00 48.19 ? 2066 HOH B O   1 
HETATM 11581 O  O   . HOH TA 8 .   ? 84.050  36.639  21.646  1.00 36.79 ? 2067 HOH B O   1 
HETATM 11582 O  O   . HOH TA 8 .   ? 64.512  26.662  10.691  1.00 37.44 ? 2068 HOH B O   1 
HETATM 11583 O  O   . HOH TA 8 .   ? 79.418  26.982  6.063   1.00 18.88 ? 2069 HOH B O   1 
HETATM 11584 O  O   . HOH TA 8 .   ? 84.598  37.823  6.462   1.00 16.04 ? 2070 HOH B O   1 
HETATM 11585 O  O   . HOH TA 8 .   ? 82.268  40.260  0.075   1.00 16.74 ? 2071 HOH B O   1 
HETATM 11586 O  O   . HOH TA 8 .   ? 83.254  41.655  5.806   1.00 32.56 ? 2072 HOH B O   1 
HETATM 11587 O  O   . HOH TA 8 .   ? 87.203  45.590  -1.011  1.00 35.37 ? 2073 HOH B O   1 
HETATM 11588 O  O   . HOH TA 8 .   ? 82.935  42.815  2.211   1.00 40.75 ? 2074 HOH B O   1 
HETATM 11589 O  O   . HOH TA 8 .   ? 85.809  46.126  2.839   1.00 41.60 ? 2075 HOH B O   1 
HETATM 11590 O  O   . HOH TA 8 .   ? 88.318  47.592  1.000   1.00 42.40 ? 2076 HOH B O   1 
HETATM 11591 O  O   . HOH TA 8 .   ? 88.996  37.927  7.327   1.00 14.87 ? 2077 HOH B O   1 
HETATM 11592 O  O   . HOH TA 8 .   ? 86.773  34.560  13.658  1.00 16.87 ? 2078 HOH B O   1 
HETATM 11593 O  O   . HOH TA 8 .   ? 99.045  25.492  16.083  1.00 15.06 ? 2079 HOH B O   1 
HETATM 11594 O  O   . HOH TA 8 .   ? 101.337 18.996  22.413  1.00 25.37 ? 2080 HOH B O   1 
HETATM 11595 O  O   . HOH TA 8 .   ? 107.271 43.868  -0.972  1.00 35.38 ? 2081 HOH B O   1 
HETATM 11596 O  O   . HOH TA 8 .   ? 97.824  17.013  28.440  1.00 40.33 ? 2082 HOH B O   1 
HETATM 11597 O  O   . HOH TA 8 .   ? 96.333  15.667  20.256  1.00 27.28 ? 2083 HOH B O   1 
HETATM 11598 O  O   . HOH TA 8 .   ? 94.043  16.506  25.801  1.00 43.52 ? 2084 HOH B O   1 
HETATM 11599 O  O   . HOH TA 8 .   ? 89.246  18.220  20.765  1.00 21.51 ? 2085 HOH B O   1 
HETATM 11600 O  O   . HOH TA 8 .   ? 97.535  23.523  14.737  1.00 17.74 ? 2086 HOH B O   1 
HETATM 11601 O  O   . HOH TA 8 .   ? 108.977 29.189  -12.352 1.00 41.96 ? 2087 HOH B O   1 
HETATM 11602 O  O   . HOH TA 8 .   ? 109.484 25.317  -8.691  1.00 29.46 ? 2088 HOH B O   1 
HETATM 11603 O  O   . HOH TA 8 .   ? 106.804 15.811  -3.361  1.00 37.94 ? 2089 HOH B O   1 
HETATM 11604 O  O   . HOH TA 8 .   ? 108.954 19.133  -5.003  1.00 43.43 ? 2090 HOH B O   1 
HETATM 11605 O  O   . HOH TA 8 .   ? 105.145 12.985  0.340   1.00 31.40 ? 2091 HOH B O   1 
HETATM 11606 O  O   . HOH TA 8 .   ? 82.502  22.268  -3.743  0.50 26.32 ? 2092 HOH B O   1 
HETATM 11607 O  O   . HOH TA 8 .   ? 83.338  24.907  -5.728  0.50 15.30 ? 2093 HOH B O   1 
HETATM 11608 O  O   . HOH TA 8 .   ? 82.282  24.787  -3.903  0.50 20.28 ? 2094 HOH B O   1 
HETATM 11609 O  O   . HOH TA 8 .   ? 96.411  17.124  -7.438  1.00 18.25 ? 2095 HOH B O   1 
HETATM 11610 O  O   . HOH TA 8 .   ? 105.599 12.482  -6.766  1.00 51.83 ? 2096 HOH B O   1 
HETATM 11611 O  O   . HOH TA 8 .   ? 85.916  30.402  -6.483  1.00 14.56 ? 2097 HOH B O   1 
HETATM 11612 O  O   . HOH TA 8 .   ? 89.119  30.325  -6.139  1.00 16.68 ? 2098 HOH B O   1 
HETATM 11613 O  O   . HOH TA 8 .   ? 102.107 9.011   0.531   1.00 34.38 ? 2099 HOH B O   1 
HETATM 11614 O  O   . HOH TA 8 .   ? 86.162  5.204   -8.324  1.00 25.30 ? 2100 HOH B O   1 
HETATM 11615 O  O   . HOH TA 8 .   ? 95.096  39.532  3.127   1.00 28.04 ? 2101 HOH B O   1 
HETATM 11616 O  O   . HOH TA 8 .   ? 97.996  4.201   -20.886 1.00 42.44 ? 2102 HOH B O   1 
HETATM 11617 O  O   . HOH TA 8 .   ? 106.588 36.249  12.689  1.00 27.16 ? 2103 HOH B O   1 
HETATM 11618 O  O   . HOH TA 8 .   ? 110.035 35.826  13.631  1.00 33.48 ? 2104 HOH B O   1 
HETATM 11619 O  O   . HOH TA 8 .   ? 110.570 25.166  14.755  1.00 28.76 ? 2105 HOH B O   1 
HETATM 11620 O  O   . HOH TA 8 .   ? 117.764 31.172  17.009  1.00 53.68 ? 2106 HOH B O   1 
HETATM 11621 O  O   . HOH TA 8 .   ? 117.254 28.936  18.689  1.00 57.88 ? 2107 HOH B O   1 
HETATM 11622 O  O   . HOH TA 8 .   ? 112.424 27.300  15.342  1.00 42.10 ? 2108 HOH B O   1 
HETATM 11623 O  O   . HOH TA 8 .   ? 95.194  14.933  -8.154  1.00 12.61 ? 2109 HOH B O   1 
HETATM 11624 O  O   . HOH TA 8 .   ? 108.323 26.747  8.025   1.00 18.77 ? 2110 HOH B O   1 
HETATM 11625 O  O   . HOH TA 8 .   ? 109.790 28.854  6.882   1.00 15.67 ? 2111 HOH B O   1 
HETATM 11626 O  O   . HOH TA 8 .   ? 113.673 30.605  5.256   1.00 36.29 ? 2112 HOH B O   1 
HETATM 11627 O  O   . HOH TA 8 .   ? 107.508 28.927  9.705   1.00 12.03 ? 2113 HOH B O   1 
HETATM 11628 O  O   . HOH TA 8 .   ? 108.225 37.271  10.989  1.00 31.28 ? 2114 HOH B O   1 
HETATM 11629 O  O   . HOH TA 8 .   ? 87.663  -2.821  12.197  1.00 43.38 ? 2115 HOH B O   1 
HETATM 11630 O  O   . HOH TA 8 .   ? 108.418 27.269  1.328   1.00 34.00 ? 2116 HOH B O   1 
HETATM 11631 O  O   . HOH TA 8 .   ? 104.425 26.724  -0.778  1.00 19.64 ? 2117 HOH B O   1 
HETATM 11632 O  O   . HOH TA 8 .   ? 106.723 26.344  2.973   1.00 29.31 ? 2118 HOH B O   1 
HETATM 11633 O  O   . HOH TA 8 .   ? 85.445  26.244  -6.769  1.00 32.58 ? 2119 HOH B O   1 
HETATM 11634 O  O   . HOH TA 8 .   ? 88.397  23.645  -8.216  1.00 24.30 ? 2120 HOH B O   1 
HETATM 11635 O  O   . HOH TA 8 .   ? 92.913  27.679  -7.413  1.00 15.91 ? 2121 HOH B O   1 
HETATM 11636 O  O   . HOH TA 8 .   ? 92.444  20.174  -4.432  1.00 13.79 ? 2122 HOH B O   1 
HETATM 11637 O  O   . HOH TA 8 .   ? 71.908  6.341   -5.973  1.00 33.51 ? 2123 HOH B O   1 
HETATM 11638 O  O   . HOH TA 8 .   ? 80.072  1.714   14.332  1.00 26.36 ? 2124 HOH B O   1 
HETATM 11639 O  O   . HOH TA 8 .   ? 78.130  -2.167  9.825   1.00 31.64 ? 2125 HOH B O   1 
HETATM 11640 O  O   . HOH TA 8 .   ? 103.784 19.840  15.597  1.00 14.87 ? 2126 HOH B O   1 
HETATM 11641 O  O   . HOH TA 8 .   ? 101.677 18.509  14.963  1.00 19.09 ? 2127 HOH B O   1 
HETATM 11642 O  O   . HOH TA 8 .   ? 98.899  16.469  21.068  1.00 29.62 ? 2128 HOH B O   1 
HETATM 11643 O  O   . HOH TA 8 .   ? 106.774 22.349  19.364  1.00 28.94 ? 2129 HOH B O   1 
HETATM 11644 O  O   . HOH TA 8 .   ? 104.827 29.701  16.869  1.00 28.44 ? 2130 HOH B O   1 
HETATM 11645 O  O   . HOH TA 8 .   ? 95.187  0.781   11.433  1.00 43.68 ? 2131 HOH B O   1 
HETATM 11646 O  O   . HOH TA 8 .   ? 92.310  43.184  1.838   1.00 31.73 ? 2132 HOH B O   1 
HETATM 11647 O  O   . HOH TA 8 .   ? 95.305  42.803  7.311   1.00 38.49 ? 2133 HOH B O   1 
HETATM 11648 O  O   . HOH TA 8 .   ? 92.963  38.425  2.097   1.00 26.10 ? 2134 HOH B O   1 
HETATM 11649 O  O   . HOH TA 8 .   ? 91.173  40.422  2.031   1.00 44.26 ? 2135 HOH B O   1 
HETATM 11650 O  O   . HOH TA 8 .   ? 95.885  39.684  -4.679  1.00 43.21 ? 2136 HOH B O   1 
HETATM 11651 O  O   . HOH TA 8 .   ? 104.108 7.291   -14.960 1.00 24.69 ? 2137 HOH B O   1 
HETATM 11652 O  O   . HOH TA 8 .   ? 87.134  33.738  -6.231  1.00 19.72 ? 2138 HOH B O   1 
HETATM 11653 O  O   . HOH TA 8 .   ? 78.676  32.977  -6.152  1.00 16.53 ? 2139 HOH B O   1 
HETATM 11654 O  O   . HOH TA 8 .   ? 96.608  8.969   -25.178 1.00 27.21 ? 2140 HOH B O   1 
HETATM 11655 O  O   . HOH TA 8 .   ? 88.821  -0.168  -24.127 1.00 39.91 ? 2141 HOH B O   1 
HETATM 11656 O  O   . HOH TA 8 .   ? 80.726  31.895  0.811   1.00 13.55 ? 2142 HOH B O   1 
HETATM 11657 O  O   . HOH TA 8 .   ? 82.777  23.062  3.291   1.00 12.28 ? 2143 HOH B O   1 
HETATM 11658 O  O   . HOH TA 8 .   ? 89.109  14.454  21.041  1.00 19.24 ? 2144 HOH B O   1 
HETATM 11659 O  O   . HOH TA 8 .   ? 79.791  20.832  23.386  1.00 25.38 ? 2145 HOH B O   1 
HETATM 11660 O  O   . HOH TA 8 .   ? 82.733  18.272  24.601  1.00 20.18 ? 2146 HOH B O   1 
HETATM 11661 O  O   . HOH TA 8 .   ? 85.586  19.072  22.742  1.00 28.97 ? 2147 HOH B O   1 
HETATM 11662 O  O   . HOH TA 8 .   ? 81.107  18.564  20.843  1.00 26.34 ? 2148 HOH B O   1 
HETATM 11663 O  O   . HOH TA 8 .   ? 76.420  28.048  20.396  1.00 33.66 ? 2149 HOH B O   1 
HETATM 11664 O  O   . HOH TA 8 .   ? 79.633  18.743  18.703  1.00 30.05 ? 2150 HOH B O   1 
HETATM 11665 O  O   . HOH TA 8 .   ? 79.115  35.185  18.391  1.00 24.73 ? 2151 HOH B O   1 
HETATM 11666 O  O   . HOH TA 8 .   ? 83.303  35.808  19.183  1.00 30.09 ? 2152 HOH B O   1 
HETATM 11667 O  O   . HOH TA 8 .   ? 77.890  31.479  21.903  1.00 39.25 ? 2153 HOH B O   1 
HETATM 11668 O  O   . HOH TA 8 .   ? 70.399  32.959  17.663  1.00 36.00 ? 2154 HOH B O   1 
HETATM 11669 O  O   . HOH TA 8 .   ? 69.809  28.815  19.792  1.00 33.10 ? 2155 HOH B O   1 
HETATM 11670 O  O   . HOH TA 8 .   ? 73.770  31.299  20.493  1.00 24.41 ? 2156 HOH B O   1 
HETATM 11671 O  O   . HOH TA 8 .   ? 69.349  33.018  13.543  1.00 30.56 ? 2157 HOH B O   1 
HETATM 11672 O  O   . HOH TA 8 .   ? 67.240  25.953  10.978  1.00 21.74 ? 2158 HOH B O   1 
HETATM 11673 O  O   . HOH TA 8 .   ? 64.621  32.224  12.626  1.00 38.51 ? 2159 HOH B O   1 
HETATM 11674 O  O   . HOH TA 8 .   ? 68.914  29.372  16.596  1.00 35.73 ? 2160 HOH B O   1 
HETATM 11675 O  O   . HOH TA 8 .   ? 69.958  26.032  7.908   1.00 16.27 ? 2161 HOH B O   1 
HETATM 11676 O  O   . HOH TA 8 .   ? 69.715  32.997  10.594  1.00 23.88 ? 2162 HOH B O   1 
HETATM 11677 O  O   . HOH TA 8 .   ? 65.337  25.506  7.131   1.00 26.74 ? 2163 HOH B O   1 
HETATM 11678 O  O   . HOH TA 8 .   ? 79.548  39.507  -0.517  1.00 26.97 ? 2164 HOH B O   1 
HETATM 11679 O  O   . HOH TA 8 .   ? 78.072  37.802  6.536   1.00 22.58 ? 2165 HOH B O   1 
HETATM 11680 O  O   . HOH TA 8 .   ? 76.608  39.191  8.728   1.00 31.31 ? 2166 HOH B O   1 
HETATM 11681 O  O   . HOH TA 8 .   ? 73.611  39.759  9.773   1.00 38.24 ? 2167 HOH B O   1 
HETATM 11682 O  O   . HOH TA 8 .   ? 78.149  39.993  4.784   1.00 26.70 ? 2168 HOH B O   1 
HETATM 11683 O  O   . HOH TA 8 .   ? 92.472  45.563  11.382  1.00 32.18 ? 2169 HOH B O   1 
HETATM 11684 O  O   . HOH TA 8 .   ? 84.346  46.324  8.405   1.00 48.29 ? 2170 HOH B O   1 
HETATM 11685 O  O   . HOH TA 8 .   ? 84.541  45.163  12.109  1.00 48.44 ? 2171 HOH B O   1 
HETATM 11686 O  O   . HOH TA 8 .   ? 85.814  44.429  6.518   1.00 34.61 ? 2172 HOH B O   1 
HETATM 11687 O  O   . HOH TA 8 .   ? 85.142  42.378  13.714  1.00 46.65 ? 2173 HOH B O   1 
HETATM 11688 O  O   . HOH TA 8 .   ? 92.895  42.779  11.500  1.00 24.92 ? 2174 HOH B O   1 
HETATM 11689 O  O   . HOH TA 8 .   ? 87.603  40.018  9.681   1.00 24.73 ? 2175 HOH B O   1 
HETATM 11690 O  O   . HOH TA 8 .   ? 89.839  36.854  16.951  1.00 30.17 ? 2176 HOH B O   1 
HETATM 11691 O  O   . HOH TA 8 .   ? 89.205  40.921  17.421  1.00 33.12 ? 2177 HOH B O   1 
HETATM 11692 O  O   . HOH TA 8 .   ? 86.646  42.249  26.073  1.00 42.87 ? 2178 HOH B O   1 
HETATM 11693 O  O   . HOH TA 8 .   ? 90.688  43.164  24.428  1.00 51.95 ? 2179 HOH B O   1 
HETATM 11694 O  O   . HOH TA 8 .   ? 91.705  37.853  29.107  1.00 39.76 ? 2180 HOH B O   1 
HETATM 11695 O  O   . HOH TA 8 .   ? 85.333  39.103  22.164  1.00 43.18 ? 2181 HOH B O   1 
HETATM 11696 O  O   . HOH TA 8 .   ? 88.260  39.812  28.085  1.00 55.24 ? 2182 HOH B O   1 
HETATM 11697 O  O   . HOH TA 8 .   ? 94.274  31.824  24.813  1.00 26.47 ? 2183 HOH B O   1 
HETATM 11698 O  O   . HOH TA 8 .   ? 89.329  28.995  27.310  1.00 41.51 ? 2184 HOH B O   1 
HETATM 11699 O  O   . HOH TA 8 .   ? 86.882  30.922  28.544  1.00 45.66 ? 2185 HOH B O   1 
HETATM 11700 O  O   . HOH TA 8 .   ? 90.693  29.171  29.347  1.00 32.12 ? 2186 HOH B O   1 
HETATM 11701 O  O   . HOH TA 8 .   ? 93.060  30.742  28.670  1.00 47.05 ? 2187 HOH B O   1 
HETATM 11702 O  O   . HOH TA 8 .   ? 92.805  31.783  30.994  1.00 42.13 ? 2188 HOH B O   1 
HETATM 11703 O  O   . HOH TA 8 .   ? 91.696  23.506  30.649  1.00 31.03 ? 2189 HOH B O   1 
HETATM 11704 O  O   . HOH TA 8 .   ? 88.304  23.571  21.299  1.00 24.81 ? 2190 HOH B O   1 
HETATM 11705 O  O   . HOH TA 8 .   ? 96.220  22.425  25.104  1.00 22.36 ? 2191 HOH B O   1 
HETATM 11706 O  O   . HOH TA 8 .   ? 96.553  32.498  25.625  1.00 27.96 ? 2192 HOH B O   1 
HETATM 11707 O  O   . HOH TA 8 .   ? 104.106 34.549  17.562  1.00 34.35 ? 2193 HOH B O   1 
HETATM 11708 O  O   . HOH TA 8 .   ? 100.429 42.650  17.392  1.00 36.78 ? 2194 HOH B O   1 
HETATM 11709 O  O   . HOH TA 8 .   ? 99.957  36.752  23.289  1.00 28.65 ? 2195 HOH B O   1 
HETATM 11710 O  O   . HOH TA 8 .   ? 102.832 36.432  20.937  1.00 31.88 ? 2196 HOH B O   1 
HETATM 11711 O  O   . HOH TA 8 .   ? 105.727 38.259  14.053  1.00 25.10 ? 2197 HOH B O   1 
HETATM 11712 O  O   . HOH TA 8 .   ? 105.877 40.860  9.885   1.00 31.71 ? 2198 HOH B O   1 
HETATM 11713 O  O   . HOH TA 8 .   ? 101.929 43.954  14.892  1.00 44.71 ? 2199 HOH B O   1 
HETATM 11714 O  O   . HOH TA 8 .   ? 100.438 42.819  9.709   1.00 22.78 ? 2200 HOH B O   1 
HETATM 11715 O  O   . HOH TA 8 .   ? 106.332 42.365  6.174   1.00 32.93 ? 2201 HOH B O   1 
HETATM 11716 O  O   . HOH TA 8 .   ? 104.045 45.168  0.661   1.00 31.44 ? 2202 HOH B O   1 
HETATM 11717 O  O   . HOH TA 8 .   ? 110.164 41.675  2.901   1.00 43.76 ? 2203 HOH B O   1 
HETATM 11718 O  O   . HOH TA 8 .   ? 109.390 39.546  0.228   1.00 37.61 ? 2204 HOH B O   1 
HETATM 11719 O  O   . HOH TA 8 .   ? 104.153 43.318  -1.414  1.00 27.79 ? 2205 HOH B O   1 
HETATM 11720 O  O   . HOH TA 8 .   ? 105.157 34.647  -8.778  1.00 25.39 ? 2206 HOH B O   1 
HETATM 11721 O  O   . HOH TA 8 .   ? 99.675  38.978  -3.618  1.00 19.43 ? 2207 HOH B O   1 
HETATM 11722 O  O   . HOH TA 8 .   ? 106.861 37.200  -2.049  1.00 43.49 ? 2208 HOH B O   1 
HETATM 11723 O  O   . HOH TA 8 .   ? 111.362 38.300  0.627   1.00 30.21 ? 2209 HOH B O   1 
HETATM 11724 O  O   . HOH TA 8 .   ? 111.327 30.352  2.550   1.00 31.13 ? 2210 HOH B O   1 
HETATM 11725 O  O   . HOH TA 8 .   ? 107.822 26.837  -1.527  1.00 20.17 ? 2211 HOH B O   1 
HETATM 11726 O  O   . HOH TA 8 .   ? 103.149 32.990  -6.826  1.00 23.19 ? 2212 HOH B O   1 
HETATM 11727 O  O   . HOH TA 8 .   ? 102.755 25.667  -6.219  1.00 15.72 ? 2213 HOH B O   1 
HETATM 11728 O  O   . HOH TA 8 .   ? 102.356 28.998  -13.308 0.50 8.79  ? 2214 HOH B O   1 
HETATM 11729 O  O   . HOH TA 8 .   ? 106.361 29.265  -13.445 1.00 48.81 ? 2215 HOH B O   1 
HETATM 11730 O  O   . HOH TA 8 .   ? 108.635 28.557  -8.978  1.00 38.65 ? 2216 HOH B O   1 
HETATM 11731 O  O   . HOH TA 8 .   ? 105.936 31.112  -6.722  1.00 28.98 ? 2217 HOH B O   1 
HETATM 11732 O  O   . HOH TA 8 .   ? 108.367 24.997  -12.196 1.00 38.23 ? 2218 HOH B O   1 
HETATM 11733 O  O   . HOH TA 8 .   ? 109.275 23.408  -6.822  1.00 21.71 ? 2219 HOH B O   1 
HETATM 11734 O  O   . HOH TA 8 .   ? 108.016 22.080  -10.372 1.00 27.12 ? 2220 HOH B O   1 
HETATM 11735 O  O   . HOH TA 8 .   ? 106.288 17.661  -4.935  1.00 49.48 ? 2221 HOH B O   1 
HETATM 11736 O  O   . HOH TA 8 .   ? 106.736 24.204  -1.949  1.00 24.75 ? 2222 HOH B O   1 
HETATM 11737 O  O   . HOH TA 8 .   ? 108.696 21.815  -2.720  1.00 39.76 ? 2223 HOH B O   1 
HETATM 11738 O  O   . HOH TA 8 .   ? 107.768 21.814  2.011   1.00 41.77 ? 2224 HOH B O   1 
HETATM 11739 O  O   . HOH TA 8 .   ? 105.618 22.933  0.079   1.00 39.94 ? 2225 HOH B O   1 
HETATM 11740 O  O   . HOH TA 8 .   ? 106.215 15.225  -0.529  1.00 27.80 ? 2226 HOH B O   1 
HETATM 11741 O  O   . HOH TA 8 .   ? 114.097 16.940  3.784   1.00 34.88 ? 2227 HOH B O   1 
HETATM 11742 O  O   . HOH TA 8 .   ? 110.145 17.940  2.604   1.00 50.22 ? 2228 HOH B O   1 
HETATM 11743 O  O   . HOH TA 8 .   ? 112.546 15.965  8.114   1.00 37.70 ? 2229 HOH B O   1 
HETATM 11744 O  O   . HOH TA 8 .   ? 110.414 20.034  6.256   1.00 40.41 ? 2230 HOH B O   1 
HETATM 11745 O  O   . HOH TA 8 .   ? 105.802 23.539  15.226  1.00 18.79 ? 2231 HOH B O   1 
HETATM 11746 O  O   . HOH TA 8 .   ? 109.273 21.621  13.056  1.00 28.13 ? 2232 HOH B O   1 
HETATM 11747 O  O   . HOH TA 8 .   ? 104.977 19.040  8.897   1.00 17.33 ? 2233 HOH B O   1 
HETATM 11748 O  O   . HOH TA 8 .   ? 112.544 22.961  9.795   1.00 39.37 ? 2234 HOH B O   1 
HETATM 11749 O  O   . HOH TA 8 .   ? 105.034 24.908  1.471   1.00 21.06 ? 2235 HOH B O   1 
HETATM 11750 O  O   . HOH TA 8 .   ? 95.998  21.510  -2.997  1.00 12.69 ? 2236 HOH B O   1 
HETATM 11751 O  O   . HOH TA 8 .   ? 95.125  23.208  -10.717 1.00 16.00 ? 2237 HOH B O   1 
HETATM 11752 O  O   . HOH TA 8 .   ? 94.302  18.710  -7.719  1.00 15.60 ? 2238 HOH B O   1 
HETATM 11753 O  O   . HOH TA 8 .   ? 101.890 19.314  -11.461 0.50 15.23 ? 2239 HOH B O   1 
HETATM 11754 O  O   . HOH TA 8 .   ? 96.341  19.553  -4.894  1.00 11.69 ? 2240 HOH B O   1 
HETATM 11755 O  O   . HOH TA 8 .   ? 104.270 17.796  -7.846  1.00 34.27 ? 2241 HOH B O   1 
HETATM 11756 O  O   . HOH TA 8 .   ? 104.025 19.339  -9.926  1.00 31.24 ? 2242 HOH B O   1 
HETATM 11757 O  O   . HOH TA 8 .   ? 98.400  18.156  -5.356  1.00 12.07 ? 2243 HOH B O   1 
HETATM 11758 O  O   . HOH TA 8 .   ? 99.557  16.266  -3.334  1.00 15.60 ? 2244 HOH B O   1 
HETATM 11759 O  O   . HOH TA 8 .   ? 102.884 16.654  -10.651 0.50 20.03 ? 2245 HOH B O   1 
HETATM 11760 O  O   . HOH TA 8 .   ? 103.669 13.377  -8.278  1.00 32.11 ? 2246 HOH B O   1 
HETATM 11761 O  O   . HOH TA 8 .   ? 103.259 11.457  -0.610  1.00 26.21 ? 2247 HOH B O   1 
HETATM 11762 O  O   . HOH TA 8 .   ? 98.896  2.795   -11.407 1.00 20.37 ? 2248 HOH B O   1 
HETATM 11763 O  O   . HOH TA 8 .   ? 91.087  -1.168  -13.174 1.00 21.83 ? 2249 HOH B O   1 
HETATM 11764 O  O   . HOH TA 8 .   ? 97.918  1.804   -15.260 1.00 39.10 ? 2250 HOH B O   1 
HETATM 11765 O  O   . HOH TA 8 .   ? 92.764  -4.805  -9.580  1.00 39.20 ? 2251 HOH B O   1 
HETATM 11766 O  O   . HOH TA 8 .   ? 93.930  -1.609  -2.978  1.00 22.19 ? 2252 HOH B O   1 
HETATM 11767 O  O   . HOH TA 8 .   ? 87.767  -6.295  -5.462  1.00 36.64 ? 2253 HOH B O   1 
HETATM 11768 O  O   . HOH TA 8 .   ? 87.873  4.445   -10.265 1.00 17.63 ? 2254 HOH B O   1 
HETATM 11769 O  O   . HOH TA 8 .   ? 91.585  2.264   -8.803  1.00 13.37 ? 2255 HOH B O   1 
HETATM 11770 O  O   . HOH TA 8 .   ? 97.891  2.930   -17.684 1.00 40.71 ? 2256 HOH B O   1 
HETATM 11771 O  O   . HOH TA 8 .   ? 97.529  10.738  2.601   1.00 16.32 ? 2257 HOH B O   1 
HETATM 11772 O  O   . HOH TA 8 .   ? 108.372 12.844  10.844  1.00 43.24 ? 2258 HOH B O   1 
HETATM 11773 O  O   . HOH TA 8 .   ? 103.799 17.984  11.161  1.00 17.46 ? 2259 HOH B O   1 
HETATM 11774 O  O   . HOH TA 8 .   ? 105.636 12.683  3.183   1.00 25.85 ? 2260 HOH B O   1 
HETATM 11775 O  O   . HOH TA 8 .   ? 102.604 15.948  14.046  1.00 23.09 ? 2261 HOH B O   1 
HETATM 11776 O  O   . HOH TA 8 .   ? 100.786 8.594   11.840  1.00 34.97 ? 2262 HOH B O   1 
HETATM 11777 O  O   . HOH TA 8 .   ? 98.347  8.136   18.565  1.00 36.20 ? 2263 HOH B O   1 
HETATM 11778 O  O   . HOH TA 8 .   ? 97.971  12.050  20.098  1.00 35.53 ? 2264 HOH B O   1 
HETATM 11779 O  O   . HOH TA 8 .   ? 94.568  12.024  16.804  1.00 21.91 ? 2265 HOH B O   1 
HETATM 11780 O  O   . HOH TA 8 .   ? 99.224  8.791   9.493   1.00 25.95 ? 2266 HOH B O   1 
HETATM 11781 O  O   . HOH TA 8 .   ? 94.060  18.160  -5.153  1.00 13.33 ? 2267 HOH B O   1 
HETATM 11782 O  O   . HOH TA 8 .   ? 93.258  13.854  -6.340  1.00 11.81 ? 2268 HOH B O   1 
HETATM 11783 O  O   . HOH TA 8 .   ? 85.753  1.325   -8.853  1.00 20.85 ? 2269 HOH B O   1 
HETATM 11784 O  O   . HOH TA 8 .   ? 81.421  3.031   -16.461 1.00 43.02 ? 2270 HOH B O   1 
HETATM 11785 O  O   . HOH TA 8 .   ? 88.627  -2.464  -18.586 1.00 35.68 ? 2271 HOH B O   1 
HETATM 11786 O  O   . HOH TA 8 .   ? 84.981  0.388   -20.058 1.00 29.81 ? 2272 HOH B O   1 
HETATM 11787 O  O   . HOH TA 8 .   ? 89.774  -6.898  -16.008 1.00 25.38 ? 2273 HOH B O   1 
HETATM 11788 O  O   . HOH TA 8 .   ? 87.022  -8.541  -13.057 1.00 23.50 ? 2274 HOH B O   1 
HETATM 11789 O  O   . HOH TA 8 .   ? 81.450  -4.719  -16.898 1.00 17.95 ? 2275 HOH B O   1 
HETATM 11790 O  O   . HOH TA 8 .   ? 86.358  -5.618  -7.723  1.00 30.46 ? 2276 HOH B O   1 
HETATM 11791 O  O   . HOH TA 8 .   ? 86.544  -6.168  -10.409 1.00 29.50 ? 2277 HOH B O   1 
HETATM 11792 O  O   . HOH TA 8 .   ? 80.017  -8.386  -10.050 1.00 30.00 ? 2278 HOH B O   1 
HETATM 11793 O  O   . HOH TA 8 .   ? 79.807  -2.788  -9.908  1.00 25.79 ? 2279 HOH B O   1 
HETATM 11794 O  O   . HOH TA 8 .   ? 82.382  -5.177  -4.167  1.00 28.64 ? 2280 HOH B O   1 
HETATM 11795 O  O   . HOH TA 8 .   ? 86.253  -5.679  -2.837  1.00 40.40 ? 2281 HOH B O   1 
HETATM 11796 O  O   . HOH TA 8 .   ? 90.663  -3.395  7.870   1.00 38.82 ? 2282 HOH B O   1 
HETATM 11797 O  O   . HOH TA 8 .   ? 89.546  -3.053  3.276   1.00 34.35 ? 2283 HOH B O   1 
HETATM 11798 O  O   . HOH TA 8 .   ? 87.387  -0.438  14.048  1.00 37.75 ? 2284 HOH B O   1 
HETATM 11799 O  O   . HOH TA 8 .   ? 87.563  3.122   14.939  1.00 29.14 ? 2285 HOH B O   1 
HETATM 11800 O  O   . HOH TA 8 .   ? 85.802  3.997   8.006   1.00 18.94 ? 2286 HOH B O   1 
HETATM 11801 O  O   . HOH TA 8 .   ? 87.962  6.105   14.403  1.00 18.04 ? 2287 HOH B O   1 
HETATM 11802 O  O   . HOH TA 8 .   ? 86.812  22.757  -4.354  1.00 18.07 ? 2288 HOH B O   1 
HETATM 11803 O  O   . HOH TA 8 .   ? 84.821  21.997  -12.512 1.00 36.03 ? 2289 HOH B O   1 
HETATM 11804 O  O   . HOH TA 8 .   ? 88.115  20.543  -9.213  1.00 23.16 ? 2290 HOH B O   1 
HETATM 11805 O  O   . HOH TA 8 .   ? 77.684  17.862  -8.354  1.00 32.47 ? 2291 HOH B O   1 
HETATM 11806 O  O   . HOH TA 8 .   ? 78.505  11.292  -16.311 1.00 17.48 ? 2292 HOH B O   1 
HETATM 11807 O  O   . HOH TA 8 .   ? 72.462  -0.086  -4.345  1.00 40.85 ? 2293 HOH B O   1 
HETATM 11808 O  O   . HOH TA 8 .   ? 76.857  0.988   -4.849  1.00 31.80 ? 2294 HOH B O   1 
HETATM 11809 O  O   . HOH TA 8 .   ? 74.455  3.735   1.920   1.00 24.13 ? 2295 HOH B O   1 
HETATM 11810 O  O   . HOH TA 8 .   ? 77.625  -2.645  1.564   1.00 41.64 ? 2296 HOH B O   1 
HETATM 11811 O  O   . HOH TA 8 .   ? 69.720  5.648   10.872  1.00 35.03 ? 2297 HOH B O   1 
HETATM 11812 O  O   . HOH TA 8 .   ? 73.206  2.972   12.048  1.00 34.43 ? 2298 HOH B O   1 
HETATM 11813 O  O   . HOH TA 8 .   ? 73.622  -0.892  1.771   1.00 24.08 ? 2299 HOH B O   1 
HETATM 11814 O  O   . HOH TA 8 .   ? 69.558  4.370   -3.414  1.00 39.91 ? 2300 HOH B O   1 
HETATM 11815 O  O   . HOH TA 8 .   ? 71.192  1.085   -2.296  1.00 34.58 ? 2301 HOH B O   1 
HETATM 11816 O  O   . HOH TA 8 .   ? 70.572  7.211   1.771   1.00 43.57 ? 2302 HOH B O   1 
HETATM 11817 O  O   . HOH TA 8 .   ? 69.313  10.043  -1.478  1.00 32.44 ? 2303 HOH B O   1 
HETATM 11818 O  O   . HOH TA 8 .   ? 75.356  13.986  -7.573  1.00 19.71 ? 2304 HOH B O   1 
HETATM 11819 O  O   . HOH TA 8 .   ? 71.003  9.962   -4.416  1.00 20.26 ? 2305 HOH B O   1 
HETATM 11820 O  O   . HOH TA 8 .   ? 72.234  10.158  -11.415 1.00 36.39 ? 2306 HOH B O   1 
HETATM 11821 O  O   . HOH TA 8 .   ? 73.146  7.665   -9.096  1.00 34.79 ? 2307 HOH B O   1 
HETATM 11822 O  O   . HOH TA 8 .   ? 72.834  13.946  -10.455 1.00 27.24 ? 2308 HOH B O   1 
HETATM 11823 O  O   . HOH TA 8 .   ? 75.691  20.698  -3.847  1.00 13.49 ? 2309 HOH B O   1 
HETATM 11824 O  O   . HOH TA 8 .   ? 73.985  19.210  -2.282  1.00 13.13 ? 2310 HOH B O   1 
HETATM 11825 O  O   . HOH TA 8 .   ? 84.196  5.204   13.917  1.00 18.95 ? 2311 HOH B O   1 
HETATM 11826 O  O   . HOH TA 8 .   ? 82.985  3.013   14.722  1.00 27.69 ? 2312 HOH B O   1 
HETATM 11827 O  O   . HOH TA 8 .   ? 80.901  -4.303  9.214   1.00 35.27 ? 2313 HOH B O   1 
HETATM 11828 O  O   . HOH TA 8 .   ? 85.412  1.248   7.300   1.00 20.70 ? 2314 HOH B O   1 
HETATM 11829 O  O   . HOH TA 8 .   ? 77.883  -4.235  5.679   1.00 38.14 ? 2315 HOH B O   1 
HETATM 11830 O  O   . HOH TA 8 .   ? 79.437  -2.994  7.680   1.00 28.07 ? 2316 HOH B O   1 
HETATM 11831 O  O   . HOH TA 8 .   ? 75.962  -2.650  -3.897  1.00 33.03 ? 2317 HOH B O   1 
HETATM 11832 O  O   . HOH TA 8 .   ? 78.109  -6.733  -2.997  1.00 46.29 ? 2318 HOH B O   1 
HETATM 11833 O  O   . HOH TA 8 .   ? 79.898  -3.638  -6.131  1.00 31.98 ? 2319 HOH B O   1 
HETATM 11834 O  O   . HOH TA 8 .   ? 87.958  2.109   -4.773  1.00 16.72 ? 2320 HOH B O   1 
HETATM 11835 O  O   . HOH TA 8 .   ? 84.446  1.347   -3.502  1.00 18.29 ? 2321 HOH B O   1 
HETATM 11836 O  O   . HOH TA 8 .   ? 85.616  2.785   -6.425  1.00 20.70 ? 2322 HOH B O   1 
HETATM 11837 O  O   . HOH TA 8 .   ? 74.541  1.740   -6.285  1.00 35.90 ? 2323 HOH B O   1 
HETATM 11838 O  O   . HOH TA 8 .   ? 84.165  5.042   -10.124 1.00 14.62 ? 2324 HOH B O   1 
HETATM 11839 O  O   . HOH TA 8 .   ? 81.434  4.402   -12.398 1.00 18.37 ? 2325 HOH B O   1 
HETATM 11840 O  O   . HOH TA 8 .   ? 73.901  9.543   -13.968 1.00 33.90 ? 2326 HOH B O   1 
HETATM 11841 O  O   . HOH TA 8 .   ? 76.686  3.507   -13.247 1.00 34.44 ? 2327 HOH B O   1 
HETATM 11842 O  O   . HOH TA 8 .   ? 78.645  6.952   -15.048 1.00 19.32 ? 2328 HOH B O   1 
HETATM 11843 O  O   . HOH TA 8 .   ? 80.331  13.282  -16.086 1.00 12.99 ? 2329 HOH B O   1 
HETATM 11844 O  O   . HOH TA 8 .   ? 77.483  9.697   -17.935 1.00 22.49 ? 2330 HOH B O   1 
HETATM 11845 O  O   . HOH TA 8 .   ? 82.751  16.183  -13.424 1.00 14.95 ? 2331 HOH B O   1 
HETATM 11846 O  O   . HOH TA 8 .   ? 90.766  20.738  -9.387  1.00 15.95 ? 2332 HOH B O   1 
HETATM 11847 O  O   . HOH TA 8 .   ? 88.973  22.107  -6.095  1.00 20.80 ? 2333 HOH B O   1 
HETATM 11848 O  O   . HOH TA 8 .   ? 90.055  4.800   7.718   1.00 15.27 ? 2334 HOH B O   1 
HETATM 11849 O  O   . HOH TA 8 .   ? 92.947  9.460   14.549  1.00 20.14 ? 2335 HOH B O   1 
HETATM 11850 O  O   . HOH TA 8 .   ? 89.744  7.091   16.198  1.00 27.13 ? 2336 HOH B O   1 
HETATM 11851 O  O   . HOH TA 8 .   ? 91.760  3.354   9.328   1.00 20.74 ? 2337 HOH B O   1 
HETATM 11852 O  O   . HOH TA 8 .   ? 94.457  6.661   7.286   1.00 20.86 ? 2338 HOH B O   1 
HETATM 11853 O  O   . HOH TA 8 .   ? 95.358  -0.050  4.118   1.00 30.32 ? 2339 HOH B O   1 
HETATM 11854 O  O   . HOH TA 8 .   ? 100.617 -0.893  5.565   1.00 46.87 ? 2340 HOH B O   1 
HETATM 11855 O  O   . HOH TA 8 .   ? 94.574  2.628   9.528   1.00 24.74 ? 2341 HOH B O   1 
HETATM 11856 O  O   . HOH TA 8 .   ? 98.105  -1.268  5.070   1.00 40.02 ? 2342 HOH B O   1 
HETATM 11857 O  O   . HOH TA 8 .   ? 93.859  -0.428  7.358   1.00 33.59 ? 2343 HOH B O   1 
HETATM 11858 O  O   . HOH TA 8 .   ? 101.372 2.676   4.627   1.00 33.63 ? 2344 HOH B O   1 
HETATM 11859 O  O   . HOH TA 8 .   ? 89.475  4.925   5.093   1.00 14.33 ? 2345 HOH B O   1 
HETATM 11860 O  O   . HOH TA 8 .   ? 99.165  8.779   1.546   1.00 30.31 ? 2346 HOH B O   1 
HETATM 11861 O  O   . HOH TA 8 .   ? 101.036 7.851   5.347   1.00 34.36 ? 2347 HOH B O   1 
HETATM 11862 O  O   . HOH TA 8 .   ? 97.481  -1.430  -0.886  1.00 30.37 ? 2348 HOH B O   1 
HETATM 11863 O  O   . HOH TA 8 .   ? 103.259 3.153   -3.423  1.00 26.65 ? 2349 HOH B O   1 
HETATM 11864 O  O   . HOH TA 8 .   ? 99.567  -2.516  -1.807  1.00 32.80 ? 2350 HOH B O   1 
HETATM 11865 O  O   . HOH TA 8 .   ? 103.747 0.711   -2.420  1.00 37.01 ? 2351 HOH B O   1 
HETATM 11866 O  O   . HOH TA 8 .   ? 99.954  -3.321  -4.006  1.00 53.98 ? 2352 HOH B O   1 
HETATM 11867 O  O   . HOH TA 8 .   ? 98.280  -2.708  -6.755  1.00 42.52 ? 2353 HOH B O   1 
HETATM 11868 O  O   . HOH TA 8 .   ? 97.404  0.269   -9.319  1.00 16.27 ? 2354 HOH B O   1 
HETATM 11869 O  O   . HOH TA 8 .   ? 102.226 -0.189  -5.681  1.00 22.50 ? 2355 HOH B O   1 
HETATM 11870 O  O   . HOH TA 8 .   ? 105.297 -1.556  -7.843  1.00 36.61 ? 2356 HOH B O   1 
HETATM 11871 O  O   . HOH TA 8 .   ? 106.172 0.523   -6.713  1.00 25.20 ? 2357 HOH B O   1 
HETATM 11872 O  O   . HOH TA 8 .   ? 103.052 5.782   -12.867 1.00 28.50 ? 2358 HOH B O   1 
HETATM 11873 O  O   . HOH TA 8 .   ? 106.159 11.655  -4.611  1.00 37.50 ? 2359 HOH B O   1 
HETATM 11874 O  O   . HOH TA 8 .   ? 106.267 6.413   -11.237 1.00 33.54 ? 2360 HOH B O   1 
HETATM 11875 O  O   . HOH TA 8 .   ? 108.741 7.927   -9.642  1.00 14.37 ? 2361 HOH B O   1 
HETATM 11876 O  O   . HOH TA 8 .   ? 105.634 10.600  -11.778 1.00 33.98 ? 2362 HOH B O   1 
HETATM 11877 O  O   . HOH TA 8 .   ? 103.945 9.979   -14.479 1.00 29.08 ? 2363 HOH B O   1 
HETATM 11878 O  O   . HOH TA 8 .   ? 101.116 17.831  -12.563 0.50 20.64 ? 2364 HOH B O   1 
HETATM 11879 O  O   . HOH TA 8 .   ? 99.798  15.803  -17.486 1.00 18.49 ? 2365 HOH B O   1 
HETATM 11880 O  O   . HOH TA 8 .   ? 93.153  14.998  -10.159 1.00 10.64 ? 2366 HOH B O   1 
HETATM 11881 O  O   . HOH TA 8 .   ? 96.848  8.482   -22.055 1.00 19.10 ? 2367 HOH B O   1 
HETATM 11882 O  O   . HOH TA 8 .   ? 91.217  3.075   -25.601 1.00 34.59 ? 2368 HOH B O   1 
HETATM 11883 O  O   . HOH TA 8 .   ? 91.413  6.686   -25.836 1.00 14.61 ? 2369 HOH B O   1 
HETATM 11884 O  O   . HOH TA 8 .   ? 96.586  5.669   -22.487 1.00 27.06 ? 2370 HOH B O   1 
HETATM 11885 O  O   . HOH TA 8 .   ? 94.614  7.708   -26.766 1.00 46.44 ? 2371 HOH B O   1 
HETATM 11886 O  O   . HOH TA 8 .   ? 91.000  1.725   -23.474 1.00 26.53 ? 2372 HOH B O   1 
HETATM 11887 O  O   . HOH TA 8 .   ? 94.894  -2.014  -19.507 1.00 39.60 ? 2373 HOH B O   1 
HETATM 11888 O  O   . HOH TA 8 .   ? 93.095  0.285   -16.335 1.00 40.80 ? 2374 HOH B O   1 
HETATM 11889 O  O   . HOH TA 8 .   ? 85.213  3.070   -21.869 1.00 33.30 ? 2375 HOH B O   1 
HETATM 11890 O  O   . HOH TA 8 .   ? 96.793  1.488   -20.893 1.00 44.38 ? 2376 HOH B O   1 
HETATM 11891 O  O   . HOH TA 8 .   ? 106.003 19.129  16.913  1.00 27.64 ? 2377 HOH B O   1 
HETATM 11892 O  O   . HOH TA 8 .   ? 108.235 19.831  20.132  1.00 41.42 ? 2378 HOH B O   1 
HETATM 11893 O  O   . HOH TA 8 .   ? 100.591 34.704  -14.683 1.00 28.18 ? 2379 HOH B O   1 
HETATM 11894 O  O   . HOH TA 8 .   ? 106.701 41.647  -10.290 1.00 31.59 ? 2380 HOH B O   1 
HETATM 11895 O  O   . HOH TA 8 .   ? 97.352  1.746   19.228  1.00 44.96 ? 2381 HOH B O   1 
HETATM 11896 O  O   . HOH TA 8 .   ? 97.301  0.638   16.896  1.00 49.01 ? 2382 HOH B O   1 
HETATM 11897 O  O   . HOH TA 8 .   ? 92.339  6.371   16.630  1.00 47.86 ? 2383 HOH B O   1 
HETATM 11898 O  O   . HOH TA 8 .   ? 70.929  21.836  23.990  1.00 29.99 ? 2384 HOH B O   1 
HETATM 11899 O  O   . HOH TA 8 .   ? 69.452  24.789  18.587  1.00 34.92 ? 2385 HOH B O   1 
HETATM 11900 O  O   . HOH TA 8 .   ? 72.033  24.730  17.423  1.00 43.56 ? 2386 HOH B O   1 
HETATM 11901 O  O   . HOH TA 8 .   ? 86.317  25.933  8.039   1.00 14.84 ? 2387 HOH B O   1 
HETATM 11902 O  O   . HOH UA 8 .   ? 80.302  39.501  37.021  1.00 40.82 ? 2001 HOH C O   1 
HETATM 11903 O  O   . HOH UA 8 .   ? 78.268  39.647  30.509  1.00 51.65 ? 2002 HOH C O   1 
HETATM 11904 O  O   . HOH UA 8 .   ? 77.104  37.479  40.469  0.50 14.17 ? 2003 HOH C O   1 
HETATM 11905 O  O   . HOH UA 8 .   ? 74.004  33.670  34.843  1.00 37.37 ? 2004 HOH C O   1 
HETATM 11906 O  O   . HOH UA 8 .   ? 65.698  27.962  29.465  1.00 46.79 ? 2005 HOH C O   1 
HETATM 11907 O  O   . HOH UA 8 .   ? 56.980  3.970   34.439  1.00 37.50 ? 2006 HOH C O   1 
HETATM 11908 O  O   . HOH UA 8 .   ? 79.445  23.342  24.279  1.00 19.88 ? 2007 HOH C O   1 
HETATM 11909 O  O   . HOH UA 8 .   ? 72.656  29.968  32.933  1.00 33.71 ? 2008 HOH C O   1 
HETATM 11910 O  O   . HOH UA 8 .   ? 66.421  26.981  33.556  1.00 34.95 ? 2009 HOH C O   1 
HETATM 11911 O  O   . HOH UA 8 .   ? 69.564  29.586  40.002  0.50 11.63 ? 2010 HOH C O   1 
HETATM 11912 O  O   . HOH UA 8 .   ? 58.374  5.478   29.533  1.00 46.82 ? 2011 HOH C O   1 
HETATM 11913 O  O   . HOH UA 8 .   ? 71.340  28.557  31.109  1.00 21.86 ? 2012 HOH C O   1 
HETATM 11914 O  O   . HOH UA 8 .   ? 75.446  28.987  31.387  1.00 27.22 ? 2013 HOH C O   1 
HETATM 11915 O  O   . HOH UA 8 .   ? 68.007  26.395  31.228  1.00 19.45 ? 2014 HOH C O   1 
HETATM 11916 O  O   . HOH UA 8 .   ? 56.506  2.683   37.416  1.00 46.57 ? 2015 HOH C O   1 
HETATM 11917 O  O   . HOH UA 8 .   ? 55.739  0.650   44.317  1.00 57.08 ? 2016 HOH C O   1 
HETATM 11918 O  O   . HOH UA 8 .   ? 75.684  26.148  28.375  1.00 36.58 ? 2017 HOH C O   1 
HETATM 11919 O  O   . HOH UA 8 .   ? 75.954  22.906  29.911  1.00 19.12 ? 2018 HOH C O   1 
HETATM 11920 O  O   . HOH UA 8 .   ? 91.031  13.666  24.625  1.00 33.47 ? 2019 HOH C O   1 
HETATM 11921 O  O   . HOH UA 8 .   ? 76.755  27.268  23.600  1.00 34.55 ? 2020 HOH C O   1 
HETATM 11922 O  O   . HOH UA 8 .   ? 76.363  28.548  27.872  1.00 39.64 ? 2021 HOH C O   1 
HETATM 11923 O  O   . HOH UA 8 .   ? 78.704  31.407  26.581  1.00 34.75 ? 2022 HOH C O   1 
HETATM 11924 O  O   . HOH UA 8 .   ? 77.744  30.789  24.208  1.00 27.29 ? 2023 HOH C O   1 
HETATM 11925 O  O   . HOH UA 8 .   ? 81.649  24.843  24.187  1.00 16.30 ? 2024 HOH C O   1 
HETATM 11926 O  O   . HOH UA 8 .   ? 78.260  29.989  28.623  1.00 23.10 ? 2025 HOH C O   1 
HETATM 11927 O  O   . HOH UA 8 .   ? 82.971  27.088  33.336  1.00 15.33 ? 2026 HOH C O   1 
HETATM 11928 O  O   . HOH UA 8 .   ? 82.772  34.352  30.878  1.00 25.60 ? 2027 HOH C O   1 
HETATM 11929 O  O   . HOH UA 8 .   ? 60.045  11.360  31.530  1.00 26.70 ? 2028 HOH C O   1 
HETATM 11930 O  O   . HOH UA 8 .   ? 60.278  7.945   30.010  1.00 46.49 ? 2029 HOH C O   1 
HETATM 11931 O  O   . HOH UA 8 .   ? 87.142  27.236  27.919  1.00 26.61 ? 2030 HOH C O   1 
HETATM 11932 O  O   . HOH UA 8 .   ? 86.369  33.962  33.267  1.00 35.10 ? 2031 HOH C O   1 
HETATM 11933 O  O   . HOH UA 8 .   ? 76.288  34.599  33.904  1.00 37.08 ? 2032 HOH C O   1 
HETATM 11934 O  O   . HOH UA 8 .   ? 78.917  32.834  30.797  1.00 29.98 ? 2033 HOH C O   1 
HETATM 11935 O  O   . HOH UA 8 .   ? 94.811  16.096  30.335  1.00 37.92 ? 2034 HOH C O   1 
HETATM 11936 O  O   . HOH UA 8 .   ? 92.738  13.271  28.670  1.00 32.70 ? 2035 HOH C O   1 
HETATM 11937 O  O   . HOH UA 8 .   ? 89.606  17.518  24.696  1.00 30.59 ? 2036 HOH C O   1 
HETATM 11938 O  O   . HOH UA 8 .   ? 72.629  32.173  48.654  1.00 16.62 ? 2037 HOH C O   1 
HETATM 11939 O  O   . HOH UA 8 .   ? 71.672  33.684  45.238  1.00 31.17 ? 2038 HOH C O   1 
HETATM 11940 O  O   . HOH UA 8 .   ? 70.253  31.362  43.366  1.00 22.08 ? 2039 HOH C O   1 
HETATM 11941 O  O   . HOH UA 8 .   ? 54.446  4.018   37.501  1.00 49.69 ? 2040 HOH C O   1 
HETATM 11942 O  O   . HOH UA 8 .   ? 68.284  24.940  44.341  1.00 12.33 ? 2041 HOH C O   1 
HETATM 11943 O  O   . HOH UA 8 .   ? 59.038  4.303   39.047  1.00 38.37 ? 2042 HOH C O   1 
HETATM 11944 O  O   . HOH UA 8 .   ? 58.457  0.830   44.831  1.00 32.76 ? 2043 HOH C O   1 
HETATM 11945 O  O   . HOH UA 8 .   ? 58.656  3.344   46.032  1.00 34.57 ? 2044 HOH C O   1 
HETATM 11946 O  O   . HOH UA 8 .   ? 57.774  3.927   41.269  1.00 36.54 ? 2045 HOH C O   1 
HETATM 11947 O  O   . HOH UA 8 .   ? 59.170  -0.845  40.950  1.00 37.12 ? 2046 HOH C O   1 
HETATM 11948 O  O   . HOH UA 8 .   ? 55.258  -1.970  44.187  1.00 44.12 ? 2047 HOH C O   1 
HETATM 11949 O  O   . HOH UA 8 .   ? 57.538  0.360   37.503  1.00 46.29 ? 2048 HOH C O   1 
HETATM 11950 O  O   . HOH UA 8 .   ? 65.909  20.881  36.951  1.00 14.23 ? 2049 HOH C O   1 
HETATM 11951 O  O   . HOH UA 8 .   ? 71.543  27.831  39.587  1.00 11.45 ? 2050 HOH C O   1 
HETATM 11952 O  O   . HOH UA 8 .   ? 65.177  23.324  28.309  1.00 32.30 ? 2051 HOH C O   1 
HETATM 11953 O  O   . HOH UA 8 .   ? 69.753  22.867  28.039  0.50 21.09 ? 2052 HOH C O   1 
HETATM 11954 O  O   . HOH UA 8 .   ? 91.955  10.257  27.936  1.00 26.19 ? 2053 HOH C O   1 
HETATM 11955 O  O   . HOH UA 8 .   ? 93.299  11.251  31.352  1.00 34.19 ? 2054 HOH C O   1 
HETATM 11956 O  O   . HOH UA 8 .   ? 88.790  12.408  26.238  1.00 38.16 ? 2055 HOH C O   1 
HETATM 11957 O  O   . HOH UA 8 .   ? 71.281  24.376  27.982  0.50 29.16 ? 2056 HOH C O   1 
HETATM 11958 O  O   . HOH UA 8 .   ? 70.856  18.064  27.319  1.00 19.98 ? 2057 HOH C O   1 
HETATM 11959 O  O   . HOH UA 8 .   ? 78.121  23.181  26.684  1.00 22.18 ? 2058 HOH C O   1 
HETATM 11960 O  O   . HOH UA 8 .   ? 95.414  0.755   55.958  1.00 37.32 ? 2059 HOH C O   1 
HETATM 11961 O  O   . HOH UA 8 .   ? 97.664  6.165   53.034  1.00 40.78 ? 2060 HOH C O   1 
HETATM 11962 O  O   . HOH UA 8 .   ? 67.703  19.391  28.484  1.00 16.05 ? 2061 HOH C O   1 
HETATM 11963 O  O   . HOH UA 8 .   ? 70.459  15.183  52.050  1.00 42.15 ? 2062 HOH C O   1 
HETATM 11964 O  O   . HOH UA 8 .   ? 62.772  13.824  29.110  1.00 15.61 ? 2063 HOH C O   1 
HETATM 11965 O  O   . HOH UA 8 .   ? 61.781  10.113  33.537  1.00 15.61 ? 2064 HOH C O   1 
HETATM 11966 O  O   . HOH UA 8 .   ? 59.969  6.601   32.717  1.00 39.33 ? 2065 HOH C O   1 
HETATM 11967 O  O   . HOH UA 8 .   ? 64.705  7.336   28.091  1.00 37.73 ? 2066 HOH C O   1 
HETATM 11968 O  O   . HOH UA 8 .   ? 66.515  4.471   27.356  1.00 35.74 ? 2067 HOH C O   1 
HETATM 11969 O  O   . HOH UA 8 .   ? 64.067  3.253   34.752  1.00 23.71 ? 2068 HOH C O   1 
HETATM 11970 O  O   . HOH UA 8 .   ? 63.102  11.273  35.714  1.00 15.01 ? 2069 HOH C O   1 
HETATM 11971 O  O   . HOH UA 8 .   ? 84.942  36.182  56.419  1.00 45.42 ? 2070 HOH C O   1 
HETATM 11972 O  O   . HOH UA 8 .   ? 67.033  2.772   37.543  1.00 18.77 ? 2071 HOH C O   1 
HETATM 11973 O  O   . HOH UA 8 .   ? 74.419  14.891  55.930  1.00 35.32 ? 2072 HOH C O   1 
HETATM 11974 O  O   . HOH UA 8 .   ? 88.592  32.146  34.450  1.00 26.84 ? 2073 HOH C O   1 
HETATM 11975 O  O   . HOH UA 8 .   ? 74.759  21.901  32.295  1.00 15.02 ? 2074 HOH C O   1 
HETATM 11976 O  O   . HOH UA 8 .   ? 71.311  16.504  41.189  1.00 11.49 ? 2075 HOH C O   1 
HETATM 11977 O  O   . HOH UA 8 .   ? 78.675  22.937  29.335  1.00 20.72 ? 2076 HOH C O   1 
HETATM 11978 O  O   . HOH UA 8 .   ? 86.455  24.652  27.708  1.00 19.16 ? 2077 HOH C O   1 
HETATM 11979 O  O   . HOH UA 8 .   ? 90.609  23.336  33.106  1.00 18.82 ? 2078 HOH C O   1 
HETATM 11980 O  O   . HOH UA 8 .   ? 91.787  19.309  31.139  1.00 25.43 ? 2079 HOH C O   1 
HETATM 11981 O  O   . HOH UA 8 .   ? 90.965  15.442  28.815  1.00 24.21 ? 2080 HOH C O   1 
HETATM 11982 O  O   . HOH UA 8 .   ? 91.995  16.367  31.059  1.00 22.83 ? 2081 HOH C O   1 
HETATM 11983 O  O   . HOH UA 8 .   ? 87.383  15.896  25.494  1.00 26.91 ? 2082 HOH C O   1 
HETATM 11984 O  O   . HOH UA 8 .   ? 84.825  16.459  25.488  1.00 24.88 ? 2083 HOH C O   1 
HETATM 11985 O  O   . HOH UA 8 .   ? 91.510  15.460  33.455  1.00 22.76 ? 2084 HOH C O   1 
HETATM 11986 O  O   . HOH UA 8 .   ? 84.876  16.693  22.259  1.00 26.07 ? 2085 HOH C O   1 
HETATM 11987 O  O   . HOH UA 8 .   ? 76.457  15.669  21.665  1.00 17.14 ? 2086 HOH C O   1 
HETATM 11988 O  O   . HOH UA 8 .   ? 77.696  19.908  22.095  1.00 34.01 ? 2087 HOH C O   1 
HETATM 11989 O  O   . HOH UA 8 .   ? 60.737  18.351  25.741  1.00 37.52 ? 2088 HOH C O   1 
HETATM 11990 O  O   . HOH UA 8 .   ? 69.726  15.198  38.988  1.00 17.44 ? 2089 HOH C O   1 
HETATM 11991 O  O   . HOH UA 8 .   ? 55.558  6.411   38.563  1.00 41.25 ? 2090 HOH C O   1 
HETATM 11992 O  O   . HOH UA 8 .   ? 55.534  6.544   33.366  1.00 50.99 ? 2091 HOH C O   1 
HETATM 11993 O  O   . HOH UA 8 .   ? 65.241  4.206   38.776  1.00 19.18 ? 2092 HOH C O   1 
HETATM 11994 O  O   . HOH UA 8 .   ? 59.727  2.787   41.808  1.00 37.16 ? 2093 HOH C O   1 
HETATM 11995 O  O   . HOH UA 8 .   ? 61.293  2.673   38.705  1.00 22.41 ? 2094 HOH C O   1 
HETATM 11996 O  O   . HOH UA 8 .   ? 60.509  4.862   44.298  1.00 15.70 ? 2095 HOH C O   1 
HETATM 11997 O  O   . HOH UA 8 .   ? 59.073  -1.770  45.755  1.00 32.17 ? 2096 HOH C O   1 
HETATM 11998 O  O   . HOH UA 8 .   ? 60.946  -1.409  39.097  1.00 29.84 ? 2097 HOH C O   1 
HETATM 11999 O  O   . HOH UA 8 .   ? 70.446  3.988   32.594  1.00 18.70 ? 2098 HOH C O   1 
HETATM 12000 O  O   . HOH UA 8 .   ? 87.379  8.338   25.705  1.00 27.37 ? 2099 HOH C O   1 
HETATM 12001 O  O   . HOH UA 8 .   ? 87.079  11.905  23.928  1.00 26.00 ? 2100 HOH C O   1 
HETATM 12002 O  O   . HOH UA 8 .   ? 88.673  5.123   18.281  1.00 43.59 ? 2101 HOH C O   1 
HETATM 12003 O  O   . HOH UA 8 .   ? 71.911  -0.158  30.082  1.00 29.48 ? 2102 HOH C O   1 
HETATM 12004 O  O   . HOH UA 8 .   ? 78.712  -14.196 41.440  1.00 31.51 ? 2103 HOH C O   1 
HETATM 12005 O  O   . HOH UA 8 .   ? 73.742  -15.007 51.311  1.00 30.09 ? 2104 HOH C O   1 
HETATM 12006 O  O   . HOH UA 8 .   ? 76.605  -14.173 55.389  1.00 38.79 ? 2105 HOH C O   1 
HETATM 12007 O  O   . HOH UA 8 .   ? 93.455  2.955   29.357  1.00 39.96 ? 2106 HOH C O   1 
HETATM 12008 O  O   . HOH UA 8 .   ? 92.312  8.962   30.115  1.00 25.33 ? 2107 HOH C O   1 
HETATM 12009 O  O   . HOH UA 8 .   ? 85.586  12.352  27.886  1.00 24.49 ? 2108 HOH C O   1 
HETATM 12010 O  O   . HOH UA 8 .   ? 85.645  3.362   35.102  1.00 18.95 ? 2109 HOH C O   1 
HETATM 12011 O  O   . HOH UA 8 .   ? 87.191  -3.983  60.499  1.00 36.28 ? 2110 HOH C O   1 
HETATM 12012 O  O   . HOH UA 8 .   ? 91.712  -0.185  57.231  1.00 34.30 ? 2111 HOH C O   1 
HETATM 12013 O  O   . HOH UA 8 .   ? 93.851  3.728   55.518  1.00 26.94 ? 2112 HOH C O   1 
HETATM 12014 O  O   . HOH UA 8 .   ? 96.328  0.368   53.273  1.00 36.15 ? 2113 HOH C O   1 
HETATM 12015 O  O   . HOH UA 8 .   ? 97.192  3.741   49.964  1.00 30.90 ? 2114 HOH C O   1 
HETATM 12016 O  O   . HOH UA 8 .   ? 95.265  6.604   51.806  1.00 18.24 ? 2115 HOH C O   1 
HETATM 12017 O  O   . HOH UA 8 .   ? 75.063  13.905  51.190  1.00 18.77 ? 2116 HOH C O   1 
HETATM 12018 O  O   . HOH UA 8 .   ? 70.600  15.918  48.806  0.50 11.97 ? 2117 HOH C O   1 
HETATM 12019 O  O   . HOH UA 8 .   ? 72.448  17.186  49.105  0.50 30.72 ? 2118 HOH C O   1 
HETATM 12020 O  O   . HOH UA 8 .   ? 84.906  11.010  57.001  1.00 24.16 ? 2119 HOH C O   1 
HETATM 12021 O  O   . HOH UA 8 .   ? 87.543  4.112   61.525  1.00 34.21 ? 2120 HOH C O   1 
HETATM 12022 O  O   . HOH UA 8 .   ? 84.597  4.880   64.106  1.00 34.67 ? 2121 HOH C O   1 
HETATM 12023 O  O   . HOH UA 8 .   ? 86.813  5.666   65.140  1.00 41.89 ? 2122 HOH C O   1 
HETATM 12024 O  O   . HOH UA 8 .   ? 68.420  9.506   52.388  1.00 16.37 ? 2123 HOH C O   1 
HETATM 12025 O  O   . HOH UA 8 .   ? 95.839  11.267  51.313  1.00 25.39 ? 2124 HOH C O   1 
HETATM 12026 O  O   . HOH UA 8 .   ? 98.484  23.928  62.002  1.00 32.49 ? 2125 HOH C O   1 
HETATM 12027 O  O   . HOH UA 8 .   ? 70.072  -4.167  44.384  1.00 30.41 ? 2126 HOH C O   1 
HETATM 12028 O  O   . HOH UA 8 .   ? 101.774 4.004   44.022  1.00 34.05 ? 2127 HOH C O   1 
HETATM 12029 O  O   . HOH UA 8 .   ? 97.713  9.606   50.252  1.00 46.90 ? 2128 HOH C O   1 
HETATM 12030 O  O   . HOH UA 8 .   ? 82.076  -11.726 38.412  1.00 24.65 ? 2129 HOH C O   1 
HETATM 12031 O  O   . HOH UA 8 .   ? 87.469  -6.605  41.969  1.00 18.41 ? 2130 HOH C O   1 
HETATM 12032 O  O   . HOH UA 8 .   ? 88.332  -14.403 41.281  1.00 40.03 ? 2131 HOH C O   1 
HETATM 12033 O  O   . HOH UA 8 .   ? 94.627  -15.551 36.487  1.00 46.21 ? 2132 HOH C O   1 
HETATM 12034 O  O   . HOH UA 8 .   ? 85.418  13.483  57.659  1.00 14.48 ? 2133 HOH C O   1 
HETATM 12035 O  O   . HOH UA 8 .   ? 89.052  -5.916  44.118  1.00 34.54 ? 2134 HOH C O   1 
HETATM 12036 O  O   . HOH UA 8 .   ? 84.586  34.331  57.931  1.00 35.41 ? 2135 HOH C O   1 
HETATM 12037 O  O   . HOH UA 8 .   ? 87.985  -8.039  45.147  1.00 25.17 ? 2136 HOH C O   1 
HETATM 12038 O  O   . HOH UA 8 .   ? 87.990  -12.860 48.721  1.00 36.64 ? 2137 HOH C O   1 
HETATM 12039 O  O   . HOH UA 8 .   ? 90.338  -11.069 44.728  1.00 43.58 ? 2138 HOH C O   1 
HETATM 12040 O  O   . HOH UA 8 .   ? 98.046  28.390  37.528  1.00 36.13 ? 2139 HOH C O   1 
HETATM 12041 O  O   . HOH UA 8 .   ? 87.071  -5.538  50.322  1.00 32.33 ? 2140 HOH C O   1 
HETATM 12042 O  O   . HOH UA 8 .   ? 87.016  -3.929  48.537  1.00 26.21 ? 2141 HOH C O   1 
HETATM 12043 O  O   . HOH UA 8 .   ? 74.612  12.289  55.222  1.00 28.35 ? 2142 HOH C O   1 
HETATM 12044 O  O   . HOH UA 8 .   ? 70.713  7.295   52.791  1.00 15.77 ? 2143 HOH C O   1 
HETATM 12045 O  O   . HOH UA 8 .   ? 71.114  12.426  52.988  1.00 26.05 ? 2144 HOH C O   1 
HETATM 12046 O  O   . HOH UA 8 .   ? 74.710  6.469   55.140  1.00 14.55 ? 2145 HOH C O   1 
HETATM 12047 O  O   . HOH UA 8 .   ? 82.295  8.001   52.342  1.00 15.72 ? 2146 HOH C O   1 
HETATM 12048 O  O   . HOH UA 8 .   ? 71.723  33.365  52.494  0.50 28.18 ? 2147 HOH C O   1 
HETATM 12049 O  O   . HOH UA 8 .   ? 71.663  26.954  53.094  1.00 22.07 ? 2148 HOH C O   1 
HETATM 12050 O  O   . HOH UA 8 .   ? 77.730  35.791  51.288  1.00 43.68 ? 2149 HOH C O   1 
HETATM 12051 O  O   . HOH UA 8 .   ? 92.246  33.915  35.120  1.00 33.94 ? 2150 HOH C O   1 
HETATM 12052 O  O   . HOH UA 8 .   ? 92.354  3.667   36.400  1.00 18.42 ? 2151 HOH C O   1 
HETATM 12053 O  O   . HOH UA 8 .   ? 93.412  6.225   30.001  1.00 28.71 ? 2152 HOH C O   1 
HETATM 12054 O  O   . HOH UA 8 .   ? 92.507  1.099   36.088  1.00 20.89 ? 2153 HOH C O   1 
HETATM 12055 O  O   . HOH UA 8 .   ? 90.761  35.773  37.743  1.00 29.59 ? 2154 HOH C O   1 
HETATM 12056 O  O   . HOH UA 8 .   ? 91.084  37.724  41.430  1.00 39.00 ? 2155 HOH C O   1 
HETATM 12057 O  O   . HOH UA 8 .   ? 82.056  32.961  60.654  1.00 29.06 ? 2156 HOH C O   1 
HETATM 12058 O  O   . HOH UA 8 .   ? 77.718  32.817  63.357  1.00 34.31 ? 2157 HOH C O   1 
HETATM 12059 O  O   . HOH UA 8 .   ? 85.745  0.728   34.109  1.00 20.08 ? 2158 HOH C O   1 
HETATM 12060 O  O   . HOH UA 8 .   ? 69.246  -1.812  44.982  1.00 29.60 ? 2159 HOH C O   1 
HETATM 12061 O  O   . HOH UA 8 .   ? 68.253  0.846   39.057  1.00 17.46 ? 2160 HOH C O   1 
HETATM 12062 O  O   . HOH UA 8 .   ? 66.841  -1.663  44.028  1.00 32.65 ? 2161 HOH C O   1 
HETATM 12063 O  O   . HOH UA 8 .   ? 67.936  -3.568  52.138  1.00 38.19 ? 2162 HOH C O   1 
HETATM 12064 O  O   . HOH UA 8 .   ? 70.551  -2.903  52.402  1.00 44.20 ? 2163 HOH C O   1 
HETATM 12065 O  O   . HOH UA 8 .   ? 67.018  6.522   52.215  1.00 15.65 ? 2164 HOH C O   1 
HETATM 12066 O  O   . HOH UA 8 .   ? 62.114  13.117  50.124  1.00 13.68 ? 2165 HOH C O   1 
HETATM 12067 O  O   . HOH UA 8 .   ? 65.837  11.707  44.113  1.00 12.61 ? 2166 HOH C O   1 
HETATM 12068 O  O   . HOH UA 8 .   ? 90.252  17.019  70.077  1.00 27.75 ? 2167 HOH C O   1 
HETATM 12069 O  O   . HOH UA 8 .   ? 88.669  30.321  72.545  1.00 31.83 ? 2168 HOH C O   1 
HETATM 12070 O  O   . HOH UA 8 .   ? 74.213  15.687  42.856  1.00 15.84 ? 2169 HOH C O   1 
HETATM 12071 O  O   . HOH UA 8 .   ? 88.352  14.710  27.877  1.00 18.60 ? 2170 HOH C O   1 
HETATM 12072 O  O   . HOH UA 8 .   ? 83.418  14.185  25.050  1.00 33.43 ? 2171 HOH C O   1 
HETATM 12073 O  O   . HOH UA 8 .   ? 75.089  -3.779  65.210  1.00 38.37 ? 2172 HOH C O   1 
HETATM 12074 O  O   . HOH UA 8 .   ? 78.313  17.243  22.776  1.00 22.05 ? 2173 HOH C O   1 
HETATM 12075 O  O   . HOH UA 8 .   ? 82.343  16.752  22.499  1.00 25.03 ? 2174 HOH C O   1 
HETATM 12076 O  O   . HOH UA 8 .   ? 80.314  17.920  25.789  1.00 29.75 ? 2175 HOH C O   1 
HETATM 12077 O  O   . HOH UA 8 .   ? 75.409  20.733  22.536  1.00 46.29 ? 2176 HOH C O   1 
HETATM 12078 O  O   . HOH UA 8 .   ? 72.737  -6.581  72.254  1.00 42.02 ? 2177 HOH C O   1 
HETATM 12079 O  O   . HOH UA 8 .   ? 69.443  11.727  22.864  1.00 29.77 ? 2178 HOH C O   1 
HETATM 12080 O  O   . HOH UA 8 .   ? 78.460  19.499  27.439  1.00 30.30 ? 2179 HOH C O   1 
HETATM 12081 O  O   . HOH UA 8 .   ? 70.147  5.831   17.708  1.00 44.37 ? 2180 HOH C O   1 
HETATM 12082 O  O   . HOH UA 8 .   ? 66.236  8.540   26.108  1.00 24.73 ? 2181 HOH C O   1 
HETATM 12083 O  O   . HOH UA 8 .   ? 66.234  14.932  23.497  1.00 28.60 ? 2182 HOH C O   1 
HETATM 12084 O  O   . HOH UA 8 .   ? 62.598  16.067  24.720  1.00 29.11 ? 2183 HOH C O   1 
HETATM 12085 O  O   . HOH UA 8 .   ? 65.477  20.874  27.620  1.00 25.98 ? 2184 HOH C O   1 
HETATM 12086 O  O   . HOH UA 8 .   ? 63.435  19.849  26.359  1.00 35.96 ? 2185 HOH C O   1 
HETATM 12087 O  O   . HOH UA 8 .   ? 60.682  17.875  28.647  1.00 25.83 ? 2186 HOH C O   1 
HETATM 12088 O  O   . HOH UA 8 .   ? 63.757  24.232  31.407  1.00 22.35 ? 2187 HOH C O   1 
HETATM 12089 O  O   . HOH UA 8 .   ? 60.374  17.733  31.829  1.00 29.29 ? 2188 HOH C O   1 
HETATM 12090 O  O   . HOH UA 8 .   ? 64.856  22.592  35.021  1.00 10.80 ? 2189 HOH C O   1 
HETATM 12091 O  O   . HOH UA 8 .   ? 62.141  26.437  34.666  1.00 25.80 ? 2190 HOH C O   1 
HETATM 12092 O  O   . HOH UA 8 .   ? 58.589  20.425  32.299  1.00 17.89 ? 2191 HOH C O   1 
HETATM 12093 O  O   . HOH UA 8 .   ? 64.732  25.185  33.778  1.00 26.38 ? 2192 HOH C O   1 
HETATM 12094 O  O   . HOH UA 8 .   ? 59.224  7.923   44.617  1.00 29.96 ? 2193 HOH C O   1 
HETATM 12095 O  O   . HOH UA 8 .   ? 61.039  8.734   37.237  1.00 15.74 ? 2194 HOH C O   1 
HETATM 12096 O  O   . HOH UA 8 .   ? 59.161  7.483   38.624  1.00 30.21 ? 2195 HOH C O   1 
HETATM 12097 O  O   . HOH UA 8 .   ? 59.511  8.579   34.606  1.00 25.59 ? 2196 HOH C O   1 
HETATM 12098 O  O   . HOH UA 8 .   ? 56.613  7.650   36.856  1.00 47.32 ? 2197 HOH C O   1 
HETATM 12099 O  O   . HOH UA 8 .   ? 66.012  -0.134  36.307  1.00 26.19 ? 2198 HOH C O   1 
HETATM 12100 O  O   . HOH UA 8 .   ? 68.007  0.158   23.709  1.00 38.87 ? 2199 HOH C O   1 
HETATM 12101 O  O   . HOH UA 8 .   ? 68.612  -6.317  26.423  1.00 36.44 ? 2200 HOH C O   1 
HETATM 12102 O  O   . HOH UA 8 .   ? 68.996  -6.177  22.788  1.00 37.23 ? 2201 HOH C O   1 
HETATM 12103 O  O   . HOH UA 8 .   ? 76.422  3.891   18.240  1.00 45.29 ? 2202 HOH C O   1 
HETATM 12104 O  O   . HOH UA 8 .   ? 86.743  4.005   21.589  1.00 40.53 ? 2203 HOH C O   1 
HETATM 12105 O  O   . HOH UA 8 .   ? 85.726  6.139   18.157  1.00 27.48 ? 2204 HOH C O   1 
HETATM 12106 O  O   . HOH UA 8 .   ? 85.221  9.169   24.494  1.00 31.29 ? 2205 HOH C O   1 
HETATM 12107 O  O   . HOH UA 8 .   ? 81.533  9.477   26.716  1.00 22.74 ? 2206 HOH C O   1 
HETATM 12108 O  O   . HOH UA 8 .   ? 79.951  -0.618  23.826  1.00 25.90 ? 2207 HOH C O   1 
HETATM 12109 O  O   . HOH UA 8 .   ? 87.988  4.004   24.908  1.00 26.81 ? 2208 HOH C O   1 
HETATM 12110 O  O   . HOH UA 8 .   ? 81.071  -3.133  23.736  1.00 33.90 ? 2209 HOH C O   1 
HETATM 12111 O  O   . HOH UA 8 .   ? 79.548  -8.080  26.246  1.00 32.45 ? 2210 HOH C O   1 
HETATM 12112 O  O   . HOH UA 8 .   ? 81.484  -9.775  29.478  1.00 27.89 ? 2211 HOH C O   1 
HETATM 12113 O  O   . HOH UA 8 .   ? 79.973  -12.213 36.507  1.00 33.13 ? 2212 HOH C O   1 
HETATM 12114 O  O   . HOH UA 8 .   ? 83.663  -14.264 46.239  1.00 29.74 ? 2213 HOH C O   1 
HETATM 12115 O  O   . HOH UA 8 .   ? 81.784  -15.549 47.828  1.00 23.28 ? 2214 HOH C O   1 
HETATM 12116 O  O   . HOH UA 8 .   ? 76.258  -14.704 43.891  1.00 40.66 ? 2215 HOH C O   1 
HETATM 12117 O  O   . HOH UA 8 .   ? 74.257  -13.862 40.770  1.00 49.77 ? 2216 HOH C O   1 
HETATM 12118 O  O   . HOH UA 8 .   ? 77.518  -16.542 48.222  1.00 35.90 ? 2217 HOH C O   1 
HETATM 12119 O  O   . HOH UA 8 .   ? 76.817  -14.161 52.320  1.00 37.24 ? 2218 HOH C O   1 
HETATM 12120 O  O   . HOH UA 8 .   ? 72.051  -12.930 50.516  1.00 29.88 ? 2219 HOH C O   1 
HETATM 12121 O  O   . HOH UA 8 .   ? 77.758  -7.074  58.362  1.00 50.54 ? 2220 HOH C O   1 
HETATM 12122 O  O   . HOH UA 8 .   ? 71.553  -5.672  59.690  1.00 16.53 ? 2221 HOH C O   1 
HETATM 12123 O  O   . HOH UA 8 .   ? 77.869  -10.808 52.341  1.00 43.41 ? 2222 HOH C O   1 
HETATM 12124 O  O   . HOH UA 8 .   ? 86.018  -11.925 51.966  1.00 31.03 ? 2223 HOH C O   1 
HETATM 12125 O  O   . HOH UA 8 .   ? 80.919  -14.986 50.719  1.00 40.93 ? 2224 HOH C O   1 
HETATM 12126 O  O   . HOH UA 8 .   ? 86.351  -9.385  52.649  1.00 41.61 ? 2225 HOH C O   1 
HETATM 12127 O  O   . HOH UA 8 .   ? 86.294  -4.600  53.069  1.00 22.64 ? 2226 HOH C O   1 
HETATM 12128 O  O   . HOH UA 8 .   ? 84.261  -1.740  51.739  1.00 17.76 ? 2227 HOH C O   1 
HETATM 12129 O  O   . HOH UA 8 .   ? 77.744  -4.511  56.609  1.00 30.79 ? 2228 HOH C O   1 
HETATM 12130 O  O   . HOH UA 8 .   ? 78.601  -0.452  63.021  1.00 33.26 ? 2229 HOH C O   1 
HETATM 12131 O  O   . HOH UA 8 .   ? 80.321  -5.303  57.311  1.00 28.10 ? 2230 HOH C O   1 
HETATM 12132 O  O   . HOH UA 8 .   ? 85.410  -2.211  63.886  1.00 34.43 ? 2231 HOH C O   1 
HETATM 12133 O  O   . HOH UA 8 .   ? 88.394  -2.507  58.695  1.00 26.48 ? 2232 HOH C O   1 
HETATM 12134 O  O   . HOH UA 8 .   ? 87.809  -0.697  62.256  1.00 31.99 ? 2233 HOH C O   1 
HETATM 12135 O  O   . HOH UA 8 .   ? 87.251  -2.099  53.571  1.00 24.61 ? 2234 HOH C O   1 
HETATM 12136 O  O   . HOH UA 8 .   ? 91.615  3.161   56.887  1.00 26.56 ? 2235 HOH C O   1 
HETATM 12137 O  O   . HOH UA 8 .   ? 82.998  0.599   56.580  1.00 17.68 ? 2236 HOH C O   1 
HETATM 12138 O  O   . HOH UA 8 .   ? 88.114  -0.127  51.303  1.00 39.18 ? 2237 HOH C O   1 
HETATM 12139 O  O   . HOH UA 8 .   ? 90.519  -1.592  55.393  1.00 42.17 ? 2238 HOH C O   1 
HETATM 12140 O  O   . HOH UA 8 .   ? 94.117  4.175   52.800  1.00 23.98 ? 2239 HOH C O   1 
HETATM 12141 O  O   . HOH UA 8 .   ? 95.363  2.166   51.325  1.00 26.26 ? 2240 HOH C O   1 
HETATM 12142 O  O   . HOH UA 8 .   ? 94.378  -1.484  50.002  1.00 43.55 ? 2241 HOH C O   1 
HETATM 12143 O  O   . HOH UA 8 .   ? 99.667  0.833   42.435  1.00 34.69 ? 2242 HOH C O   1 
HETATM 12144 O  O   . HOH UA 8 .   ? 94.514  -3.581  39.522  1.00 36.85 ? 2243 HOH C O   1 
HETATM 12145 O  O   . HOH UA 8 .   ? 91.199  -2.592  36.668  1.00 24.84 ? 2244 HOH C O   1 
HETATM 12146 O  O   . HOH UA 8 .   ? 93.933  -2.828  46.343  1.00 36.43 ? 2245 HOH C O   1 
HETATM 12147 O  O   . HOH UA 8 .   ? 92.572  1.523   42.897  1.00 19.08 ? 2246 HOH C O   1 
HETATM 12148 O  O   . HOH UA 8 .   ? 91.763  -4.363  46.657  1.00 44.21 ? 2247 HOH C O   1 
HETATM 12149 O  O   . HOH UA 8 .   ? 86.608  -1.491  49.700  1.00 25.54 ? 2248 HOH C O   1 
HETATM 12150 O  O   . HOH UA 8 .   ? 82.054  11.684  56.662  1.00 20.31 ? 2249 HOH C O   1 
HETATM 12151 O  O   . HOH UA 8 .   ? 78.730  8.288   59.364  1.00 20.29 ? 2250 HOH C O   1 
HETATM 12152 O  O   . HOH UA 8 .   ? 85.620  5.954   62.005  1.00 28.17 ? 2251 HOH C O   1 
HETATM 12153 O  O   . HOH UA 8 .   ? 83.473  9.193   54.258  1.00 16.27 ? 2252 HOH C O   1 
HETATM 12154 O  O   . HOH UA 8 .   ? 89.563  4.379   58.213  1.00 54.04 ? 2253 HOH C O   1 
HETATM 12155 O  O   . HOH UA 8 .   ? 85.928  8.564   55.376  1.00 18.28 ? 2254 HOH C O   1 
HETATM 12156 O  O   . HOH UA 8 .   ? 89.062  6.988   61.257  1.00 38.41 ? 2255 HOH C O   1 
HETATM 12157 O  O   . HOH UA 8 .   ? 94.338  9.052   59.225  1.00 31.96 ? 2256 HOH C O   1 
HETATM 12158 O  O   . HOH UA 8 .   ? 94.904  8.815   52.889  1.00 32.32 ? 2257 HOH C O   1 
HETATM 12159 O  O   . HOH UA 8 .   ? 92.289  24.730  58.398  1.00 18.53 ? 2258 HOH C O   1 
HETATM 12160 O  O   . HOH UA 8 .   ? 93.406  27.923  62.820  1.00 29.19 ? 2259 HOH C O   1 
HETATM 12161 O  O   . HOH UA 8 .   ? 95.088  21.549  66.341  1.00 31.04 ? 2260 HOH C O   1 
HETATM 12162 O  O   . HOH UA 8 .   ? 97.355  21.969  60.620  1.00 16.91 ? 2261 HOH C O   1 
HETATM 12163 O  O   . HOH UA 8 .   ? 95.994  19.806  62.771  1.00 23.01 ? 2262 HOH C O   1 
HETATM 12164 O  O   . HOH UA 8 .   ? 96.211  30.945  59.004  1.00 37.39 ? 2263 HOH C O   1 
HETATM 12165 O  O   . HOH UA 8 .   ? 87.513  26.387  58.789  0.50 9.29  ? 2264 HOH C O   1 
HETATM 12166 O  O   . HOH UA 8 .   ? 92.961  21.933  70.198  1.00 45.24 ? 2265 HOH C O   1 
HETATM 12167 O  O   . HOH UA 8 .   ? 87.133  26.622  56.132  0.50 7.53  ? 2266 HOH C O   1 
HETATM 12168 O  O   . HOH UA 8 .   ? 88.367  8.748   53.812  1.00 14.42 ? 2267 HOH C O   1 
HETATM 12169 O  O   . HOH UA 8 .   ? 99.126  9.155   46.890  1.00 44.12 ? 2268 HOH C O   1 
HETATM 12170 O  O   . HOH UA 8 .   ? 98.058  7.608   48.649  1.00 34.41 ? 2269 HOH C O   1 
HETATM 12171 O  O   . HOH UA 8 .   ? 99.675  3.434   42.493  1.00 35.66 ? 2270 HOH C O   1 
HETATM 12172 O  O   . HOH UA 8 .   ? 101.315 5.280   46.486  1.00 41.29 ? 2271 HOH C O   1 
HETATM 12173 O  O   . HOH UA 8 .   ? 94.550  4.762   37.733  1.00 24.72 ? 2272 HOH C O   1 
HETATM 12174 O  O   . HOH UA 8 .   ? 93.263  3.147   40.613  1.00 21.85 ? 2273 HOH C O   1 
HETATM 12175 O  O   . HOH UA 8 .   ? 96.196  5.714   49.104  1.00 22.29 ? 2274 HOH C O   1 
HETATM 12176 O  O   . HOH UA 8 .   ? 98.120  11.574  40.082  1.00 29.21 ? 2275 HOH C O   1 
HETATM 12177 O  O   . HOH UA 8 .   ? 97.818  3.537   33.855  1.00 40.34 ? 2276 HOH C O   1 
HETATM 12178 O  O   . HOH UA 8 .   ? 92.759  12.978  33.368  1.00 24.18 ? 2277 HOH C O   1 
HETATM 12179 O  O   . HOH UA 8 .   ? 96.281  12.848  42.127  1.00 29.42 ? 2278 HOH C O   1 
HETATM 12180 O  O   . HOH UA 8 .   ? 85.449  15.428  55.478  1.00 14.83 ? 2279 HOH C O   1 
HETATM 12181 O  O   . HOH UA 8 .   ? 83.053  11.707  54.078  1.00 14.76 ? 2280 HOH C O   1 
HETATM 12182 O  O   . HOH UA 8 .   ? 83.653  15.204  59.043  1.00 14.99 ? 2281 HOH C O   1 
HETATM 12183 O  O   . HOH UA 8 .   ? 86.066  27.038  57.208  0.50 2.74  ? 2282 HOH C O   1 
HETATM 12184 O  O   . HOH UA 8 .   ? 85.879  34.635  60.274  1.00 38.64 ? 2283 HOH C O   1 
HETATM 12185 O  O   . HOH UA 8 .   ? 89.505  29.707  56.811  1.00 22.57 ? 2284 HOH C O   1 
HETATM 12186 O  O   . HOH UA 8 .   ? 85.449  28.309  57.611  0.50 3.31  ? 2285 HOH C O   1 
HETATM 12187 O  O   . HOH UA 8 .   ? 85.789  33.358  66.773  1.00 41.28 ? 2286 HOH C O   1 
HETATM 12188 O  O   . HOH UA 8 .   ? 88.240  35.985  59.908  1.00 36.72 ? 2287 HOH C O   1 
HETATM 12189 O  O   . HOH UA 8 .   ? 95.556  33.957  59.936  1.00 39.45 ? 2288 HOH C O   1 
HETATM 12190 O  O   . HOH UA 8 .   ? 89.169  36.716  56.834  1.00 32.28 ? 2289 HOH C O   1 
HETATM 12191 O  O   . HOH UA 8 .   ? 90.266  36.854  53.899  1.00 37.51 ? 2290 HOH C O   1 
HETATM 12192 O  O   . HOH UA 8 .   ? 93.166  36.014  52.088  1.00 21.41 ? 2291 HOH C O   1 
HETATM 12193 O  O   . HOH UA 8 .   ? 89.856  30.164  51.633  1.00 22.30 ? 2292 HOH C O   1 
HETATM 12194 O  O   . HOH UA 8 .   ? 94.382  37.859  48.291  1.00 47.31 ? 2293 HOH C O   1 
HETATM 12195 O  O   . HOH UA 8 .   ? 96.216  33.909  51.804  1.00 32.37 ? 2294 HOH C O   1 
HETATM 12196 O  O   . HOH UA 8 .   ? 98.109  28.624  40.677  1.00 36.86 ? 2295 HOH C O   1 
HETATM 12197 O  O   . HOH UA 8 .   ? 97.741  28.378  46.625  1.00 24.04 ? 2296 HOH C O   1 
HETATM 12198 O  O   . HOH UA 8 .   ? 99.091  26.327  44.096  1.00 35.86 ? 2297 HOH C O   1 
HETATM 12199 O  O   . HOH UA 8 .   ? 94.609  24.229  34.017  1.00 32.93 ? 2298 HOH C O   1 
HETATM 12200 O  O   . HOH UA 8 .   ? 96.613  27.078  35.403  1.00 35.26 ? 2299 HOH C O   1 
HETATM 12201 O  O   . HOH UA 8 .   ? 91.175  25.849  40.793  1.00 16.58 ? 2300 HOH C O   1 
HETATM 12202 O  O   . HOH UA 8 .   ? 92.348  22.126  34.929  1.00 20.51 ? 2301 HOH C O   1 
HETATM 12203 O  O   . HOH UA 8 .   ? 76.641  15.063  56.487  1.00 23.77 ? 2302 HOH C O   1 
HETATM 12204 O  O   . HOH UA 8 .   ? 72.639  23.394  54.132  1.00 34.87 ? 2303 HOH C O   1 
HETATM 12205 O  O   . HOH UA 8 .   ? 87.220  39.239  50.668  1.00 39.41 ? 2304 HOH C O   1 
HETATM 12206 O  O   . HOH UA 8 .   ? 89.078  35.876  45.474  1.00 33.39 ? 2305 HOH C O   1 
HETATM 12207 O  O   . HOH UA 8 .   ? 86.889  36.250  37.840  1.00 45.19 ? 2306 HOH C O   1 
HETATM 12208 O  O   . HOH UA 8 .   ? 80.493  36.598  34.341  1.00 44.32 ? 2307 HOH C O   1 
HETATM 12209 O  O   . HOH UA 8 .   ? 85.675  38.399  44.420  1.00 32.23 ? 2308 HOH C O   1 
HETATM 12210 O  O   . HOH UA 8 .   ? 82.189  34.423  44.136  1.00 27.45 ? 2309 HOH C O   1 
HETATM 12211 O  O   . HOH UA 8 .   ? 79.052  38.414  40.952  0.50 22.35 ? 2310 HOH C O   1 
HETATM 12212 O  O   . HOH UA 8 .   ? 77.485  35.936  43.067  1.00 45.43 ? 2311 HOH C O   1 
HETATM 12213 O  O   . HOH UA 8 .   ? 76.740  34.698  53.880  1.00 33.48 ? 2312 HOH C O   1 
HETATM 12214 O  O   . HOH UA 8 .   ? 73.866  33.892  55.778  1.00 35.11 ? 2313 HOH C O   1 
HETATM 12215 O  O   . HOH UA 8 .   ? 74.554  34.111  48.755  1.00 21.15 ? 2314 HOH C O   1 
HETATM 12216 O  O   . HOH UA 8 .   ? 73.524  28.682  52.364  1.00 19.06 ? 2315 HOH C O   1 
HETATM 12217 O  O   . HOH UA 8 .   ? 71.815  30.855  54.539  1.00 34.73 ? 2316 HOH C O   1 
HETATM 12218 O  O   . HOH UA 8 .   ? 69.710  23.362  48.243  1.00 13.76 ? 2317 HOH C O   1 
HETATM 12219 O  O   . HOH UA 8 .   ? 70.041  25.433  46.405  1.00 16.86 ? 2318 HOH C O   1 
HETATM 12220 O  O   . HOH UA 8 .   ? 93.248  31.487  35.061  1.00 32.41 ? 2319 HOH C O   1 
HETATM 12221 O  O   . HOH UA 8 .   ? 91.719  27.939  33.821  1.00 24.61 ? 2320 HOH C O   1 
HETATM 12222 O  O   . HOH UA 8 .   ? 90.469  25.546  34.472  1.00 18.65 ? 2321 HOH C O   1 
HETATM 12223 O  O   . HOH UA 8 .   ? 92.740  27.987  41.482  1.00 21.04 ? 2322 HOH C O   1 
HETATM 12224 O  O   . HOH UA 8 .   ? 92.289  35.174  39.881  1.00 29.10 ? 2323 HOH C O   1 
HETATM 12225 O  O   . HOH UA 8 .   ? 84.793  33.252  50.561  1.00 33.74 ? 2324 HOH C O   1 
HETATM 12226 O  O   . HOH UA 8 .   ? 86.428  36.359  53.431  1.00 34.88 ? 2325 HOH C O   1 
HETATM 12227 O  O   . HOH UA 8 .   ? 89.074  28.434  54.354  1.00 24.60 ? 2326 HOH C O   1 
HETATM 12228 O  O   . HOH UA 8 .   ? 91.075  26.956  53.541  1.00 19.41 ? 2327 HOH C O   1 
HETATM 12229 O  O   . HOH UA 8 .   ? 82.489  37.217  52.187  1.00 37.90 ? 2328 HOH C O   1 
HETATM 12230 O  O   . HOH UA 8 .   ? 83.430  31.279  59.240  1.00 15.23 ? 2329 HOH C O   1 
HETATM 12231 O  O   . HOH UA 8 .   ? 74.868  32.898  59.195  1.00 41.29 ? 2330 HOH C O   1 
HETATM 12232 O  O   . HOH UA 8 .   ? 75.752  29.237  61.801  1.00 15.12 ? 2331 HOH C O   1 
HETATM 12233 O  O   . HOH UA 8 .   ? 79.264  31.726  61.141  1.00 23.04 ? 2332 HOH C O   1 
HETATM 12234 O  O   . HOH UA 8 .   ? 75.724  31.338  63.275  1.00 16.48 ? 2333 HOH C O   1 
HETATM 12235 O  O   . HOH UA 8 .   ? 75.396  22.383  59.630  1.00 17.54 ? 2334 HOH C O   1 
HETATM 12236 O  O   . HOH UA 8 .   ? 76.467  12.983  53.392  1.00 23.63 ? 2335 HOH C O   1 
HETATM 12237 O  O   . HOH UA 8 .   ? 80.554  11.704  53.006  1.00 17.39 ? 2336 HOH C O   1 
HETATM 12238 O  O   . HOH UA 8 .   ? 94.493  17.799  43.269  1.00 16.07 ? 2337 HOH C O   1 
HETATM 12239 O  O   . HOH UA 8 .   ? 93.351  22.245  41.745  1.00 18.80 ? 2338 HOH C O   1 
HETATM 12240 O  O   . HOH UA 8 .   ? 95.704  21.756  40.820  1.00 18.23 ? 2339 HOH C O   1 
HETATM 12241 O  O   . HOH UA 8 .   ? 93.249  16.148  35.647  1.00 19.81 ? 2340 HOH C O   1 
HETATM 12242 O  O   . HOH UA 8 .   ? 93.124  19.751  33.386  1.00 38.07 ? 2341 HOH C O   1 
HETATM 12243 O  O   . HOH UA 8 .   ? 99.967  18.025  39.424  1.00 29.80 ? 2342 HOH C O   1 
HETATM 12244 O  O   . HOH UA 8 .   ? 97.996  13.899  44.723  1.00 33.59 ? 2343 HOH C O   1 
HETATM 12245 O  O   . HOH UA 8 .   ? 98.082  20.598  41.539  1.00 21.42 ? 2344 HOH C O   1 
HETATM 12246 O  O   . HOH UA 8 .   ? 99.361  22.295  46.944  1.00 35.07 ? 2345 HOH C O   1 
HETATM 12247 O  O   . HOH UA 8 .   ? 92.211  22.746  44.231  1.00 19.61 ? 2346 HOH C O   1 
HETATM 12248 O  O   . HOH UA 8 .   ? 92.451  13.410  48.403  1.00 24.22 ? 2347 HOH C O   1 
HETATM 12249 O  O   . HOH UA 8 .   ? 94.783  13.366  49.805  1.00 25.51 ? 2348 HOH C O   1 
HETATM 12250 O  O   . HOH UA 8 .   ? 97.662  12.343  46.483  1.00 30.93 ? 2349 HOH C O   1 
HETATM 12251 O  O   . HOH UA 8 .   ? 100.332 22.200  52.458  1.00 34.35 ? 2350 HOH C O   1 
HETATM 12252 O  O   . HOH UA 8 .   ? 98.235  24.879  53.752  1.00 31.18 ? 2351 HOH C O   1 
HETATM 12253 O  O   . HOH UA 8 .   ? 101.473 20.659  49.844  1.00 37.36 ? 2352 HOH C O   1 
HETATM 12254 O  O   . HOH UA 8 .   ? 101.574 18.429  58.280  1.00 36.96 ? 2353 HOH C O   1 
HETATM 12255 O  O   . HOH UA 8 .   ? 100.866 22.913  58.759  1.00 37.38 ? 2354 HOH C O   1 
HETATM 12256 O  O   . HOH UA 8 .   ? 98.629  19.979  62.484  1.00 35.00 ? 2355 HOH C O   1 
HETATM 12257 O  O   . HOH UA 8 .   ? 99.647  9.487   57.240  1.00 34.63 ? 2356 HOH C O   1 
HETATM 12258 O  O   . HOH UA 8 .   ? 99.929  12.763  61.249  1.00 35.42 ? 2357 HOH C O   1 
HETATM 12259 O  O   . HOH UA 8 .   ? 91.676  8.409   60.161  1.00 30.87 ? 2358 HOH C O   1 
HETATM 12260 O  O   . HOH UA 8 .   ? 90.677  12.178  67.193  1.00 41.44 ? 2359 HOH C O   1 
HETATM 12261 O  O   . HOH UA 8 .   ? 93.134  11.426  66.152  1.00 31.50 ? 2360 HOH C O   1 
HETATM 12262 O  O   . HOH UA 8 .   ? 85.470  10.719  67.717  1.00 20.17 ? 2361 HOH C O   1 
HETATM 12263 O  O   . HOH UA 8 .   ? 80.953  15.697  62.961  1.00 33.61 ? 2362 HOH C O   1 
HETATM 12264 O  O   . HOH UA 8 .   ? 88.078  18.726  71.944  1.00 21.58 ? 2363 HOH C O   1 
HETATM 12265 O  O   . HOH UA 8 .   ? 89.880  20.561  72.296  1.00 20.31 ? 2364 HOH C O   1 
HETATM 12266 O  O   . HOH UA 8 .   ? 87.692  26.405  74.569  1.00 25.83 ? 2365 HOH C O   1 
HETATM 12267 O  O   . HOH UA 8 .   ? 85.052  24.082  74.557  1.00 16.96 ? 2366 HOH C O   1 
HETATM 12268 O  O   . HOH UA 8 .   ? 91.711  27.284  72.810  1.00 26.50 ? 2367 HOH C O   1 
HETATM 12269 O  O   . HOH UA 8 .   ? 84.403  30.166  68.873  1.00 36.28 ? 2368 HOH C O   1 
HETATM 12270 O  O   . HOH UA 8 .   ? 88.972  27.693  72.499  1.00 23.72 ? 2369 HOH C O   1 
HETATM 12271 O  O   . HOH UA 8 .   ? 94.860  -0.048  35.339  1.00 32.62 ? 2370 HOH C O   1 
HETATM 12272 O  O   . HOH UA 8 .   ? 94.184  -2.643  35.466  1.00 40.36 ? 2371 HOH C O   1 
HETATM 12273 O  O   . HOH UA 8 .   ? 73.018  -3.123  63.418  1.00 25.12 ? 2372 HOH C O   1 
HETATM 12274 O  O   . HOH UA 8 .   ? 72.817  -12.615 60.033  1.00 27.85 ? 2373 HOH C O   1 
HETATM 12275 O  O   . HOH UA 8 .   ? 75.778  -6.139  66.368  1.00 31.61 ? 2374 HOH C O   1 
HETATM 12276 O  O   . HOH UA 8 .   ? 95.584  17.965  33.283  1.00 49.20 ? 2375 HOH C O   1 
HETATM 12277 O  O   . HOH UA 8 .   ? 74.220  17.321  22.437  1.00 39.52 ? 2376 HOH C O   1 
HETATM 12278 O  O   . HOH UA 8 .   ? 69.415  20.396  26.909  1.00 37.54 ? 2377 HOH C O   1 
HETATM 12279 O  O   . HOH UA 8 .   ? 70.621  -7.621  73.544  1.00 26.21 ? 2378 HOH C O   1 
HETATM 12280 O  O   . HOH UA 8 .   ? 72.659  -13.175 79.651  0.50 20.62 ? 2379 HOH C O   1 
HETATM 12281 O  O   . HOH UA 8 .   ? 71.415  -14.411 78.906  0.50 22.04 ? 2380 HOH C O   1 
HETATM 12282 O  O   . HOH UA 8 .   ? 75.331  10.700  38.708  1.00 19.40 ? 2381 HOH C O   1 
HETATM 12283 O  O   . HOH VA 8 .   ? 63.330  11.757  -21.480 1.00 36.95 ? 2001 HOH D O   1 
HETATM 12284 O  O   . HOH VA 8 .   ? 73.919  8.835   -19.457 1.00 36.00 ? 2002 HOH D O   1 
HETATM 12285 O  O   . HOH VA 8 .   ? 79.713  6.361   -25.725 1.00 39.73 ? 2003 HOH D O   1 
HETATM 12286 O  O   . HOH VA 8 .   ? 74.596  7.116   -25.657 1.00 39.36 ? 2004 HOH D O   1 
HETATM 12287 O  O   . HOH VA 8 .   ? 73.867  13.297  -33.763 0.50 23.86 ? 2005 HOH D O   1 
HETATM 12288 O  O   . HOH VA 8 .   ? 76.432  18.701  -38.252 1.00 26.66 ? 2006 HOH D O   1 
HETATM 12289 O  O   . HOH VA 8 .   ? 74.963  10.667  -27.895 1.00 23.80 ? 2007 HOH D O   1 
HETATM 12290 O  O   . HOH VA 8 .   ? 74.530  8.238   -23.275 1.00 39.20 ? 2008 HOH D O   1 
HETATM 12291 O  O   . HOH VA 8 .   ? 81.206  8.571   -26.028 1.00 18.05 ? 2009 HOH D O   1 
HETATM 12292 O  O   . HOH VA 8 .   ? 76.390  10.389  -20.481 0.50 9.73  ? 2010 HOH D O   1 
HETATM 12293 O  O   . HOH VA 8 .   ? 66.614  24.321  -36.461 1.00 28.98 ? 2011 HOH D O   1 
HETATM 12294 O  O   . HOH VA 8 .   ? 73.919  13.387  -29.873 1.00 34.02 ? 2012 HOH D O   1 
HETATM 12295 O  O   . HOH VA 8 .   ? 80.978  9.526   -28.673 1.00 21.95 ? 2013 HOH D O   1 
HETATM 12296 O  O   . HOH VA 8 .   ? 77.179  10.403  -29.771 1.00 19.85 ? 2014 HOH D O   1 
HETATM 12297 O  O   . HOH VA 8 .   ? 76.306  15.444  -33.571 0.50 18.39 ? 2015 HOH D O   1 
HETATM 12298 O  O   . HOH VA 8 .   ? 78.482  17.685  -31.833 1.00 17.59 ? 2016 HOH D O   1 
HETATM 12299 O  O   . HOH VA 8 .   ? 73.913  19.559  -38.747 1.00 27.83 ? 2017 HOH D O   1 
HETATM 12300 O  O   . HOH VA 8 .   ? 72.028  14.139  -33.500 0.50 7.71  ? 2018 HOH D O   1 
HETATM 12301 O  O   . HOH VA 8 .   ? 94.318  11.556  -28.063 1.00 34.71 ? 2019 HOH D O   1 
HETATM 12302 O  O   . HOH VA 8 .   ? 96.765  12.895  -30.522 1.00 28.25 ? 2020 HOH D O   1 
HETATM 12303 O  O   . HOH VA 8 .   ? 65.129  15.183  -32.076 1.00 28.10 ? 2021 HOH D O   1 
HETATM 12304 O  O   . HOH VA 8 .   ? 97.526  13.909  -27.336 1.00 25.10 ? 2022 HOH D O   1 
HETATM 12305 O  O   . HOH VA 8 .   ? 63.580  19.462  -31.827 1.00 33.67 ? 2023 HOH D O   1 
HETATM 12306 O  O   . HOH VA 8 .   ? 68.180  22.071  -36.275 1.00 27.56 ? 2024 HOH D O   1 
HETATM 12307 O  O   . HOH VA 8 .   ? 68.479  12.746  -31.491 1.00 31.55 ? 2025 HOH D O   1 
HETATM 12308 O  O   . HOH VA 8 .   ? 98.277  36.433  -7.686  1.00 38.06 ? 2026 HOH D O   1 
HETATM 12309 O  O   . HOH VA 8 .   ? 66.893  27.490  -34.777 1.00 35.44 ? 2027 HOH D O   1 
HETATM 12310 O  O   . HOH VA 8 .   ? 71.330  35.347  -35.863 1.00 34.56 ? 2028 HOH D O   1 
HETATM 12311 O  O   . HOH VA 8 .   ? 74.537  33.187  -36.949 1.00 24.60 ? 2029 HOH D O   1 
HETATM 12312 O  O   . HOH VA 8 .   ? 71.519  10.153  -15.805 1.00 32.99 ? 2030 HOH D O   1 
HETATM 12313 O  O   . HOH VA 8 .   ? 74.174  10.500  -17.201 1.00 22.89 ? 2031 HOH D O   1 
HETATM 12314 O  O   . HOH VA 8 .   ? 71.369  12.617  -12.528 1.00 18.89 ? 2032 HOH D O   1 
HETATM 12315 O  O   . HOH VA 8 .   ? 101.540 17.686  -16.429 1.00 42.11 ? 2033 HOH D O   1 
HETATM 12316 O  O   . HOH VA 8 .   ? 105.693 23.190  -18.268 1.00 47.40 ? 2034 HOH D O   1 
HETATM 12317 O  O   . HOH VA 8 .   ? 110.486 23.083  -16.525 1.00 37.56 ? 2035 HOH D O   1 
HETATM 12318 O  O   . HOH VA 8 .   ? 105.022 36.278  -23.295 1.00 42.51 ? 2036 HOH D O   1 
HETATM 12319 O  O   . HOH VA 8 .   ? 85.784  12.820  -22.774 1.00 12.05 ? 2037 HOH D O   1 
HETATM 12320 O  O   . HOH VA 8 .   ? 76.554  12.857  -21.401 1.00 10.32 ? 2038 HOH D O   1 
HETATM 12321 O  O   . HOH VA 8 .   ? 75.260  35.997  -37.427 1.00 39.74 ? 2039 HOH D O   1 
HETATM 12322 O  O   . HOH VA 8 .   ? 81.768  30.369  -39.144 1.00 31.92 ? 2040 HOH D O   1 
HETATM 12323 O  O   . HOH VA 8 .   ? 78.944  16.375  -39.312 1.00 29.17 ? 2041 HOH D O   1 
HETATM 12324 O  O   . HOH VA 8 .   ? 76.822  18.195  -35.731 1.00 18.45 ? 2042 HOH D O   1 
HETATM 12325 O  O   . HOH VA 8 .   ? 75.524  48.266  -11.265 1.00 35.55 ? 2043 HOH D O   1 
HETATM 12326 O  O   . HOH VA 8 .   ? 94.329  13.548  -30.032 1.00 11.20 ? 2044 HOH D O   1 
HETATM 12327 O  O   . HOH VA 8 .   ? 97.398  16.968  -29.739 1.00 30.72 ? 2045 HOH D O   1 
HETATM 12328 O  O   . HOH VA 8 .   ? 97.095  16.081  -25.843 1.00 13.94 ? 2046 HOH D O   1 
HETATM 12329 O  O   . HOH VA 8 .   ? 100.984 16.934  -26.796 1.00 40.38 ? 2047 HOH D O   1 
HETATM 12330 O  O   . HOH VA 8 .   ? 97.841  18.712  -31.835 1.00 37.81 ? 2048 HOH D O   1 
HETATM 12331 O  O   . HOH VA 8 .   ? 100.672 48.493  -25.936 1.00 37.41 ? 2049 HOH D O   1 
HETATM 12332 O  O   . HOH VA 8 .   ? 100.497 46.186  -31.287 1.00 37.80 ? 2050 HOH D O   1 
HETATM 12333 O  O   . HOH VA 8 .   ? 69.997  48.839  -18.951 1.00 38.91 ? 2051 HOH D O   1 
HETATM 12334 O  O   . HOH VA 8 .   ? 95.109  16.837  -23.868 1.00 12.93 ? 2052 HOH D O   1 
HETATM 12335 O  O   . HOH VA 8 .   ? 100.724 22.354  -25.417 1.00 32.76 ? 2053 HOH D O   1 
HETATM 12336 O  O   . HOH VA 8 .   ? 97.892  17.439  -22.182 1.00 20.60 ? 2054 HOH D O   1 
HETATM 12337 O  O   . HOH VA 8 .   ? 92.029  52.289  -21.400 1.00 35.33 ? 2055 HOH D O   1 
HETATM 12338 O  O   . HOH VA 8 .   ? 98.648  25.625  -23.502 1.00 15.41 ? 2056 HOH D O   1 
HETATM 12339 O  O   . HOH VA 8 .   ? 86.083  22.357  -9.153  1.00 43.54 ? 2057 HOH D O   1 
HETATM 12340 O  O   . HOH VA 8 .   ? 79.870  17.535  -29.444 1.00 11.30 ? 2058 HOH D O   1 
HETATM 12341 O  O   . HOH VA 8 .   ? 85.126  20.329  -20.270 1.00 15.26 ? 2059 HOH D O   1 
HETATM 12342 O  O   . HOH VA 8 .   ? 78.007  19.752  -33.876 1.00 26.66 ? 2060 HOH D O   1 
HETATM 12343 O  O   . HOH VA 8 .   ? 99.659  35.014  -9.828  0.50 25.27 ? 2061 HOH D O   1 
HETATM 12344 O  O   . HOH VA 8 .   ? 71.087  22.949  -36.777 1.00 25.85 ? 2062 HOH D O   1 
HETATM 12345 O  O   . HOH VA 8 .   ? 60.190  27.639  6.346   1.00 34.91 ? 2063 HOH D O   1 
HETATM 12346 O  O   . HOH VA 8 .   ? 70.306  20.389  -30.017 1.00 14.09 ? 2064 HOH D O   1 
HETATM 12347 O  O   . HOH VA 8 .   ? 68.465  28.441  -32.256 1.00 18.88 ? 2065 HOH D O   1 
HETATM 12348 O  O   . HOH VA 8 .   ? 70.949  31.542  -34.557 1.00 25.63 ? 2066 HOH D O   1 
HETATM 12349 O  O   . HOH VA 8 .   ? 72.731  33.483  -34.898 1.00 25.71 ? 2067 HOH D O   1 
HETATM 12350 O  O   . HOH VA 8 .   ? 73.466  22.474  -39.272 1.00 24.42 ? 2068 HOH D O   1 
HETATM 12351 O  O   . HOH VA 8 .   ? 78.223  23.674  -39.179 1.00 26.84 ? 2069 HOH D O   1 
HETATM 12352 O  O   . HOH VA 8 .   ? 73.635  34.181  -32.232 1.00 19.34 ? 2070 HOH D O   1 
HETATM 12353 O  O   . HOH VA 8 .   ? 80.881  29.667  -32.311 1.00 21.64 ? 2071 HOH D O   1 
HETATM 12354 O  O   . HOH VA 8 .   ? 85.208  5.356   -26.916 1.00 33.95 ? 2072 HOH D O   1 
HETATM 12355 O  O   . HOH VA 8 .   ? 86.378  0.993   -26.172 1.00 39.92 ? 2073 HOH D O   1 
HETATM 12356 O  O   . HOH VA 8 .   ? 87.383  19.701  -22.104 1.00 18.00 ? 2074 HOH D O   1 
HETATM 12357 O  O   . HOH VA 8 .   ? 98.553  23.681  -21.788 1.00 21.55 ? 2075 HOH D O   1 
HETATM 12358 O  O   . HOH VA 8 .   ? 102.556 10.368  -18.404 1.00 46.73 ? 2076 HOH D O   1 
HETATM 12359 O  O   . HOH VA 8 .   ? 106.070 13.345  -21.716 1.00 48.27 ? 2077 HOH D O   1 
HETATM 12360 O  O   . HOH VA 8 .   ? 103.547 21.466  -17.738 1.00 36.63 ? 2078 HOH D O   1 
HETATM 12361 O  O   . HOH VA 8 .   ? 100.581 20.855  -15.311 1.00 14.78 ? 2079 HOH D O   1 
HETATM 12362 O  O   . HOH VA 8 .   ? 101.434 26.597  -24.670 1.00 30.89 ? 2080 HOH D O   1 
HETATM 12363 O  O   . HOH VA 8 .   ? 105.226 34.667  -26.337 1.00 31.47 ? 2081 HOH D O   1 
HETATM 12364 O  O   . HOH VA 8 .   ? 107.484 24.396  -16.567 1.00 46.08 ? 2082 HOH D O   1 
HETATM 12365 O  O   . HOH VA 8 .   ? 105.456 24.074  -20.785 1.00 28.11 ? 2083 HOH D O   1 
HETATM 12366 O  O   . HOH VA 8 .   ? 99.236  28.089  -22.539 1.00 16.87 ? 2084 HOH D O   1 
HETATM 12367 O  O   . HOH VA 8 .   ? 95.911  26.271  -28.930 1.00 22.95 ? 2085 HOH D O   1 
HETATM 12368 O  O   . HOH VA 8 .   ? 92.360  34.277  -47.912 1.00 38.21 ? 2086 HOH D O   1 
HETATM 12369 O  O   . HOH VA 8 .   ? 99.013  52.283  -18.415 0.50 23.33 ? 2087 HOH D O   1 
HETATM 12370 O  O   . HOH VA 8 .   ? 105.994 44.354  -23.314 1.00 40.89 ? 2088 HOH D O   1 
HETATM 12371 O  O   . HOH VA 8 .   ? 78.587  37.986  -36.239 1.00 32.92 ? 2089 HOH D O   1 
HETATM 12372 O  O   . HOH VA 8 .   ? 77.808  36.453  -38.324 1.00 34.56 ? 2090 HOH D O   1 
HETATM 12373 O  O   . HOH VA 8 .   ? 78.847  33.827  -38.884 1.00 49.68 ? 2091 HOH D O   1 
HETATM 12374 O  O   . HOH VA 8 .   ? 80.461  30.740  -36.830 1.00 23.72 ? 2092 HOH D O   1 
HETATM 12375 O  O   . HOH VA 8 .   ? 86.193  38.062  -30.229 1.00 19.10 ? 2093 HOH D O   1 
HETATM 12376 O  O   . HOH VA 8 .   ? 75.894  46.400  -15.759 1.00 20.78 ? 2094 HOH D O   1 
HETATM 12377 O  O   . HOH VA 8 .   ? 78.411  47.923  -12.013 1.00 29.28 ? 2095 HOH D O   1 
HETATM 12378 O  O   . HOH VA 8 .   ? 86.041  47.885  -32.449 1.00 41.90 ? 2096 HOH D O   1 
HETATM 12379 O  O   . HOH VA 8 .   ? 82.988  23.604  -14.869 1.00 52.94 ? 2097 HOH D O   1 
HETATM 12380 O  O   . HOH VA 8 .   ? 78.663  36.983  -8.405  1.00 17.39 ? 2098 HOH D O   1 
HETATM 12381 O  O   . HOH VA 8 .   ? 77.748  44.830  -5.513  1.00 39.46 ? 2099 HOH D O   1 
HETATM 12382 O  O   . HOH VA 8 .   ? 90.791  25.141  -9.165  1.00 16.55 ? 2100 HOH D O   1 
HETATM 12383 O  O   . HOH VA 8 .   ? 71.729  43.646  -16.399 1.00 24.81 ? 2101 HOH D O   1 
HETATM 12384 O  O   . HOH VA 8 .   ? 60.025  33.327  -1.629  0.50 20.83 ? 2102 HOH D O   1 
HETATM 12385 O  O   . HOH VA 8 .   ? 71.369  48.871  -25.988 1.00 45.33 ? 2103 HOH D O   1 
HETATM 12386 O  O   . HOH VA 8 .   ? 72.030  46.500  -18.058 1.00 35.05 ? 2104 HOH D O   1 
HETATM 12387 O  O   . HOH VA 8 .   ? 99.485  49.399  -27.964 1.00 31.85 ? 2105 HOH D O   1 
HETATM 12388 O  O   . HOH VA 8 .   ? 97.698  46.809  -30.303 1.00 49.14 ? 2106 HOH D O   1 
HETATM 12389 O  O   . HOH VA 8 .   ? 99.445  46.175  -26.904 1.00 26.96 ? 2107 HOH D O   1 
HETATM 12390 O  O   . HOH VA 8 .   ? 88.760  51.154  -29.707 1.00 32.89 ? 2108 HOH D O   1 
HETATM 12391 O  O   . HOH VA 8 .   ? 91.139  46.534  -31.838 1.00 36.95 ? 2109 HOH D O   1 
HETATM 12392 O  O   . HOH VA 8 .   ? 91.428  52.868  -29.710 1.00 36.22 ? 2110 HOH D O   1 
HETATM 12393 O  O   . HOH VA 8 .   ? 76.349  36.013  -7.665  1.00 15.44 ? 2111 HOH D O   1 
HETATM 12394 O  O   . HOH VA 8 .   ? 89.953  48.493  -22.678 1.00 22.46 ? 2112 HOH D O   1 
HETATM 12395 O  O   . HOH VA 8 .   ? 87.377  54.081  -27.017 1.00 57.23 ? 2113 HOH D O   1 
HETATM 12396 O  O   . HOH VA 8 .   ? 61.485  21.664  -5.939  1.00 31.87 ? 2114 HOH D O   1 
HETATM 12397 O  O   . HOH VA 8 .   ? 92.062  47.395  -24.424 1.00 19.45 ? 2115 HOH D O   1 
HETATM 12398 O  O   . HOH VA 8 .   ? 92.232  49.629  -21.583 1.00 18.23 ? 2116 HOH D O   1 
HETATM 12399 O  O   . HOH VA 8 .   ? 61.047  25.854  2.358   1.00 39.81 ? 2117 HOH D O   1 
HETATM 12400 O  O   . HOH VA 8 .   ? 101.336 46.889  -23.239 1.00 34.45 ? 2118 HOH D O   1 
HETATM 12401 O  O   . HOH VA 8 .   ? 98.995  49.146  -23.759 1.00 31.86 ? 2119 HOH D O   1 
HETATM 12402 O  O   . HOH VA 8 .   ? 93.309  50.548  -17.116 1.00 29.77 ? 2120 HOH D O   1 
HETATM 12403 O  O   . HOH VA 8 .   ? 54.577  30.973  -12.509 1.00 35.78 ? 2121 HOH D O   1 
HETATM 12404 O  O   . HOH VA 8 .   ? 63.844  28.908  -33.236 1.00 33.07 ? 2122 HOH D O   1 
HETATM 12405 O  O   . HOH VA 8 .   ? 89.525  46.797  -18.024 1.00 22.26 ? 2123 HOH D O   1 
HETATM 12406 O  O   . HOH VA 8 .   ? 89.150  43.970  -14.030 1.00 21.57 ? 2124 HOH D O   1 
HETATM 12407 O  O   . HOH VA 8 .   ? 84.476  28.457  -7.704  1.00 20.82 ? 2125 HOH D O   1 
HETATM 12408 O  O   . HOH VA 8 .   ? 88.851  32.420  -7.951  1.00 15.81 ? 2126 HOH D O   1 
HETATM 12409 O  O   . HOH VA 8 .   ? 91.019  28.420  -9.394  1.00 10.97 ? 2127 HOH D O   1 
HETATM 12410 O  O   . HOH VA 8 .   ? 86.615  25.403  -9.129  1.00 27.05 ? 2128 HOH D O   1 
HETATM 12411 O  O   . HOH VA 8 .   ? 81.466  33.001  -11.254 1.00 15.86 ? 2129 HOH D O   1 
HETATM 12412 O  O   . HOH VA 8 .   ? 75.558  16.266  -8.405  1.00 16.93 ? 2130 HOH D O   1 
HETATM 12413 O  O   . HOH VA 8 .   ? 83.197  44.799  -30.987 1.00 26.38 ? 2131 HOH D O   1 
HETATM 12414 O  O   . HOH VA 8 .   ? 81.666  43.000  -30.514 1.00 20.33 ? 2132 HOH D O   1 
HETATM 12415 O  O   . HOH VA 8 .   ? 87.098  48.473  -36.703 1.00 41.89 ? 2133 HOH D O   1 
HETATM 12416 O  O   . HOH VA 8 .   ? 89.790  47.918  -34.568 0.50 13.79 ? 2134 HOH D O   1 
HETATM 12417 O  O   . HOH VA 8 .   ? 63.909  21.283  -2.760  1.00 28.17 ? 2135 HOH D O   1 
HETATM 12418 O  O   . HOH VA 8 .   ? 88.529  39.494  -31.525 1.00 16.71 ? 2136 HOH D O   1 
HETATM 12419 O  O   . HOH VA 8 .   ? 96.889  43.757  -32.142 1.00 38.78 ? 2137 HOH D O   1 
HETATM 12420 O  O   . HOH VA 8 .   ? 93.226  44.847  -31.993 1.00 32.07 ? 2138 HOH D O   1 
HETATM 12421 O  O   . HOH VA 8 .   ? 99.662  31.878  -17.117 1.00 41.31 ? 2139 HOH D O   1 
HETATM 12422 O  O   . HOH VA 8 .   ? 104.101 30.362  -16.421 1.00 42.62 ? 2140 HOH D O   1 
HETATM 12423 O  O   . HOH VA 8 .   ? 101.596 30.069  -14.771 0.50 23.01 ? 2141 HOH D O   1 
HETATM 12424 O  O   . HOH VA 8 .   ? 101.178 33.002  -10.151 0.50 25.07 ? 2142 HOH D O   1 
HETATM 12425 O  O   . HOH VA 8 .   ? 59.446  39.634  -6.094  1.00 37.37 ? 2143 HOH D O   1 
HETATM 12426 O  O   . HOH VA 8 .   ? 69.410  46.149  -0.861  1.00 41.33 ? 2144 HOH D O   1 
HETATM 12427 O  O   . HOH VA 8 .   ? 94.200  26.035  -9.229  1.00 16.51 ? 2145 HOH D O   1 
HETATM 12428 O  O   . HOH VA 8 .   ? 80.369  42.945  2.577   1.00 35.87 ? 2146 HOH D O   1 
HETATM 12429 O  O   . HOH VA 8 .   ? 92.422  17.611  -9.708  1.00 16.92 ? 2147 HOH D O   1 
HETATM 12430 O  O   . HOH VA 8 .   ? 91.895  20.070  -16.465 1.00 17.35 ? 2148 HOH D O   1 
HETATM 12431 O  O   . HOH VA 8 .   ? 69.592  38.116  8.507   1.00 41.04 ? 2149 HOH D O   1 
HETATM 12432 O  O   . HOH VA 8 .   ? 59.950  30.238  6.835   1.00 24.46 ? 2150 HOH D O   1 
HETATM 12433 O  O   . HOH VA 8 .   ? 85.402  23.294  -14.572 0.50 18.28 ? 2151 HOH D O   1 
HETATM 12434 O  O   . HOH VA 8 .   ? 83.569  23.390  -19.387 1.00 15.20 ? 2152 HOH D O   1 
HETATM 12435 O  O   . HOH VA 8 .   ? 76.740  31.540  -37.168 1.00 29.01 ? 2153 HOH D O   1 
HETATM 12436 O  O   . HOH VA 8 .   ? 83.708  28.576  -38.788 1.00 29.60 ? 2154 HOH D O   1 
HETATM 12437 O  O   . HOH VA 8 .   ? 94.923  41.732  1.261   1.00 41.56 ? 2155 HOH D O   1 
HETATM 12438 O  O   . HOH VA 8 .   ? 81.283  23.118  -40.923 1.00 18.43 ? 2156 HOH D O   1 
HETATM 12439 O  O   . HOH VA 8 .   ? 80.001  22.342  -37.575 1.00 18.36 ? 2157 HOH D O   1 
HETATM 12440 O  O   . HOH VA 8 .   ? 83.071  26.536  -40.580 1.00 29.80 ? 2158 HOH D O   1 
HETATM 12441 O  O   . HOH VA 8 .   ? 79.850  26.104  -38.685 1.00 25.22 ? 2159 HOH D O   1 
HETATM 12442 O  O   . HOH VA 8 .   ? 91.647  18.079  -37.574 1.00 18.01 ? 2160 HOH D O   1 
HETATM 12443 O  O   . HOH VA 8 .   ? 80.053  21.594  -34.947 1.00 14.24 ? 2161 HOH D O   1 
HETATM 12444 O  O   . HOH VA 8 .   ? 95.125  19.687  -38.127 1.00 19.92 ? 2162 HOH D O   1 
HETATM 12445 O  O   . HOH VA 8 .   ? 96.414  19.053  -33.918 1.00 26.10 ? 2163 HOH D O   1 
HETATM 12446 O  O   . HOH VA 8 .   ? 96.153  17.647  -36.711 1.00 28.38 ? 2164 HOH D O   1 
HETATM 12447 O  O   . HOH VA 8 .   ? 88.505  9.693   -32.446 1.00 32.33 ? 2165 HOH D O   1 
HETATM 12448 O  O   . HOH VA 8 .   ? 92.413  8.494   -32.859 1.00 37.86 ? 2166 HOH D O   1 
HETATM 12449 O  O   . HOH VA 8 .   ? 85.105  7.910   -27.582 1.00 17.34 ? 2167 HOH D O   1 
HETATM 12450 O  O   . HOH VA 8 .   ? 92.223  9.653   -27.031 1.00 24.10 ? 2168 HOH D O   1 
HETATM 12451 O  O   . HOH VA 8 .   ? 85.438  10.487  -24.527 1.00 13.28 ? 2169 HOH D O   1 
HETATM 12452 O  O   . HOH VA 8 .   ? 84.261  5.990   -23.895 1.00 23.66 ? 2170 HOH D O   1 
HETATM 12453 O  O   . HOH VA 8 .   ? 86.925  3.647   -27.374 1.00 31.09 ? 2171 HOH D O   1 
HETATM 12454 O  O   . HOH VA 8 .   ? 85.839  8.227   -16.507 1.00 14.48 ? 2172 HOH D O   1 
HETATM 12455 O  O   . HOH VA 8 .   ? 84.775  6.355   -19.180 1.00 33.74 ? 2173 HOH D O   1 
HETATM 12456 O  O   . HOH VA 8 .   ? 83.637  8.337   -25.414 1.00 18.75 ? 2174 HOH D O   1 
HETATM 12457 O  O   . HOH VA 8 .   ? 98.781  17.786  -14.430 1.00 32.24 ? 2175 HOH D O   1 
HETATM 12458 O  O   . HOH VA 8 .   ? 106.262 15.118  -19.434 1.00 45.65 ? 2176 HOH D O   1 
HETATM 12459 O  O   . HOH VA 8 .   ? 102.092 13.837  -17.445 1.00 39.35 ? 2177 HOH D O   1 
HETATM 12460 O  O   . HOH VA 8 .   ? 102.191 18.815  -19.983 1.00 23.45 ? 2178 HOH D O   1 
HETATM 12461 O  O   . HOH VA 8 .   ? 100.200 16.821  -20.525 1.00 29.83 ? 2179 HOH D O   1 
HETATM 12462 O  O   . HOH VA 8 .   ? 99.226  15.557  -24.398 1.00 25.91 ? 2180 HOH D O   1 
HETATM 12463 O  O   . HOH VA 8 .   ? 107.913 29.834  -23.831 1.00 45.93 ? 2181 HOH D O   1 
HETATM 12464 O  O   . HOH VA 8 .   ? 107.100 22.789  -25.928 1.00 40.04 ? 2182 HOH D O   1 
HETATM 12465 O  O   . HOH VA 8 .   ? 110.079 27.116  -22.440 1.00 59.48 ? 2183 HOH D O   1 
HETATM 12466 O  O   . HOH VA 8 .   ? 104.609 31.540  -26.189 1.00 24.59 ? 2184 HOH D O   1 
HETATM 12467 O  O   . HOH VA 8 .   ? 98.921  29.227  -32.051 1.00 20.28 ? 2185 HOH D O   1 
HETATM 12468 O  O   . HOH VA 8 .   ? 101.026 25.356  -37.451 1.00 31.50 ? 2186 HOH D O   1 
HETATM 12469 O  O   . HOH VA 8 .   ? 105.631 30.354  -35.064 1.00 41.55 ? 2187 HOH D O   1 
HETATM 12470 O  O   . HOH VA 8 .   ? 105.827 29.681  -38.788 1.00 43.00 ? 2188 HOH D O   1 
HETATM 12471 O  O   . HOH VA 8 .   ? 101.832 32.382  -43.925 1.00 34.59 ? 2189 HOH D O   1 
HETATM 12472 O  O   . HOH VA 8 .   ? 104.108 33.395  -42.474 1.00 49.01 ? 2190 HOH D O   1 
HETATM 12473 O  O   . HOH VA 8 .   ? 94.617  34.237  -40.435 1.00 33.02 ? 2191 HOH D O   1 
HETATM 12474 O  O   . HOH VA 8 .   ? 100.824 37.528  -40.185 1.00 41.30 ? 2192 HOH D O   1 
HETATM 12475 O  O   . HOH VA 8 .   ? 94.423  32.468  -46.392 1.00 38.37 ? 2193 HOH D O   1 
HETATM 12476 O  O   . HOH VA 8 .   ? 91.364  30.702  -44.699 1.00 32.10 ? 2194 HOH D O   1 
HETATM 12477 O  O   . HOH VA 8 .   ? 93.851  33.593  -44.143 1.00 27.78 ? 2195 HOH D O   1 
HETATM 12478 O  O   . HOH VA 8 .   ? 85.739  29.118  -37.319 1.00 17.35 ? 2196 HOH D O   1 
HETATM 12479 O  O   . HOH VA 8 .   ? 85.707  37.006  -40.914 1.00 24.98 ? 2197 HOH D O   1 
HETATM 12480 O  O   . HOH VA 8 .   ? 95.661  39.917  -39.895 1.00 31.65 ? 2198 HOH D O   1 
HETATM 12481 O  O   . HOH VA 8 .   ? 95.733  36.487  -40.792 1.00 31.61 ? 2199 HOH D O   1 
HETATM 12482 O  O   . HOH VA 8 .   ? 100.029 39.742  -38.190 1.00 32.42 ? 2200 HOH D O   1 
HETATM 12483 O  O   . HOH VA 8 .   ? 106.061 40.458  -29.790 1.00 37.79 ? 2201 HOH D O   1 
HETATM 12484 O  O   . HOH VA 8 .   ? 101.382 44.996  -28.728 1.00 26.38 ? 2202 HOH D O   1 
HETATM 12485 O  O   . HOH VA 8 .   ? 100.138 50.754  -19.443 0.50 22.72 ? 2203 HOH D O   1 
HETATM 12486 O  O   . HOH VA 8 .   ? 100.615 50.306  -21.666 0.50 23.32 ? 2204 HOH D O   1 
HETATM 12487 O  O   . HOH VA 8 .   ? 102.871 48.129  -21.708 1.00 40.04 ? 2205 HOH D O   1 
HETATM 12488 O  O   . HOH VA 8 .   ? 107.757 44.414  -18.673 1.00 34.51 ? 2206 HOH D O   1 
HETATM 12489 O  O   . HOH VA 8 .   ? 105.123 44.645  -20.591 1.00 40.31 ? 2207 HOH D O   1 
HETATM 12490 O  O   . HOH VA 8 .   ? 107.024 40.802  -14.783 1.00 40.89 ? 2208 HOH D O   1 
HETATM 12491 O  O   . HOH VA 8 .   ? 104.627 46.839  -20.107 1.00 40.30 ? 2209 HOH D O   1 
HETATM 12492 O  O   . HOH VA 8 .   ? 105.318 48.213  -16.298 1.00 44.23 ? 2210 HOH D O   1 
HETATM 12493 O  O   . HOH VA 8 .   ? 105.603 41.949  -12.918 1.00 30.92 ? 2211 HOH D O   1 
HETATM 12494 O  O   . HOH VA 8 .   ? 100.642 38.223  -11.300 1.00 20.11 ? 2212 HOH D O   1 
HETATM 12495 O  O   . HOH VA 8 .   ? 100.183 45.488  -12.750 1.00 36.41 ? 2213 HOH D O   1 
HETATM 12496 O  O   . HOH VA 8 .   ? 101.192 49.218  -14.807 1.00 39.59 ? 2214 HOH D O   1 
HETATM 12497 O  O   . HOH VA 8 .   ? 97.023  53.101  -10.490 1.00 34.40 ? 2215 HOH D O   1 
HETATM 12498 O  O   . HOH VA 8 .   ? 97.031  52.443  -17.395 0.50 14.69 ? 2216 HOH D O   1 
HETATM 12499 O  O   . HOH VA 8 .   ? 91.124  51.056  -15.747 1.00 33.89 ? 2217 HOH D O   1 
HETATM 12500 O  O   . HOH VA 8 .   ? 89.696  47.312  -13.297 1.00 22.69 ? 2218 HOH D O   1 
HETATM 12501 O  O   . HOH VA 8 .   ? 95.053  42.080  -7.984  1.00 21.61 ? 2219 HOH D O   1 
HETATM 12502 O  O   . HOH VA 8 .   ? 90.542  41.435  -1.712  1.00 36.17 ? 2220 HOH D O   1 
HETATM 12503 O  O   . HOH VA 8 .   ? 93.547  45.005  -7.921  1.00 30.65 ? 2221 HOH D O   1 
HETATM 12504 O  O   . HOH VA 8 .   ? 87.844  42.535  -8.889  1.00 16.51 ? 2222 HOH D O   1 
HETATM 12505 O  O   . HOH VA 8 .   ? 85.567  45.354  -15.215 1.00 18.75 ? 2223 HOH D O   1 
HETATM 12506 O  O   . HOH VA 8 .   ? 77.862  49.181  -18.198 1.00 35.31 ? 2224 HOH D O   1 
HETATM 12507 O  O   . HOH VA 8 .   ? 78.444  47.120  -14.685 1.00 18.39 ? 2225 HOH D O   1 
HETATM 12508 O  O   . HOH VA 8 .   ? 81.100  54.472  -21.889 1.00 43.10 ? 2226 HOH D O   1 
HETATM 12509 O  O   . HOH VA 8 .   ? 76.908  52.355  -22.233 1.00 30.53 ? 2227 HOH D O   1 
HETATM 12510 O  O   . HOH VA 8 .   ? 78.993  52.089  -26.106 1.00 35.87 ? 2228 HOH D O   1 
HETATM 12511 O  O   . HOH VA 8 .   ? 87.049  46.341  -30.300 1.00 29.20 ? 2229 HOH D O   1 
HETATM 12512 O  O   . HOH VA 8 .   ? 86.291  50.076  -21.272 1.00 30.00 ? 2230 HOH D O   1 
HETATM 12513 O  O   . HOH VA 8 .   ? 82.333  45.995  -24.293 1.00 17.19 ? 2231 HOH D O   1 
HETATM 12514 O  O   . HOH VA 8 .   ? 88.325  47.788  -20.732 1.00 27.81 ? 2232 HOH D O   1 
HETATM 12515 O  O   . HOH VA 8 .   ? 87.919  45.187  -16.663 1.00 15.76 ? 2233 HOH D O   1 
HETATM 12516 O  O   . HOH VA 8 .   ? 83.244  36.367  -12.583 1.00 12.31 ? 2234 HOH D O   1 
HETATM 12517 O  O   . HOH VA 8 .   ? 79.839  34.534  -8.044  1.00 24.33 ? 2235 HOH D O   1 
HETATM 12518 O  O   . HOH VA 8 .   ? 84.166  35.052  -4.727  1.00 16.40 ? 2236 HOH D O   1 
HETATM 12519 O  O   . HOH VA 8 .   ? 80.948  41.746  -3.876  1.00 32.63 ? 2237 HOH D O   1 
HETATM 12520 O  O   . HOH VA 8 .   ? 81.227  36.949  -10.695 1.00 13.60 ? 2238 HOH D O   1 
HETATM 12521 O  O   . HOH VA 8 .   ? 79.692  45.145  -8.040  1.00 51.14 ? 2239 HOH D O   1 
HETATM 12522 O  O   . HOH VA 8 .   ? 79.835  39.126  -10.309 1.00 16.28 ? 2240 HOH D O   1 
HETATM 12523 O  O   . HOH VA 8 .   ? 78.309  40.446  -12.386 1.00 13.16 ? 2241 HOH D O   1 
HETATM 12524 O  O   . HOH VA 8 .   ? 73.725  45.871  -8.463  1.00 41.60 ? 2242 HOH D O   1 
HETATM 12525 O  O   . HOH VA 8 .   ? 79.006  43.114  -4.363  1.00 33.08 ? 2243 HOH D O   1 
HETATM 12526 O  O   . HOH VA 8 .   ? 74.065  44.724  -14.960 1.00 28.06 ? 2244 HOH D O   1 
HETATM 12527 O  O   . HOH VA 8 .   ? 63.304  33.801  -8.063  1.00 20.04 ? 2245 HOH D O   1 
HETATM 12528 O  O   . HOH VA 8 .   ? 63.481  39.845  -0.993  1.00 32.26 ? 2246 HOH D O   1 
HETATM 12529 O  O   . HOH VA 8 .   ? 59.544  33.409  -4.000  0.50 10.75 ? 2247 HOH D O   1 
HETATM 12530 O  O   . HOH VA 8 .   ? 55.795  32.449  -8.154  1.00 37.42 ? 2248 HOH D O   1 
HETATM 12531 O  O   . HOH VA 8 .   ? 65.185  29.833  -6.540  1.00 40.88 ? 2249 HOH D O   1 
HETATM 12532 O  O   . HOH VA 8 .   ? 61.717  28.365  -8.500  1.00 23.04 ? 2250 HOH D O   1 
HETATM 12533 O  O   . HOH VA 8 .   ? 73.433  47.845  -27.602 1.00 32.22 ? 2251 HOH D O   1 
HETATM 12534 O  O   . HOH VA 8 .   ? 71.955  46.676  -21.496 1.00 39.75 ? 2252 HOH D O   1 
HETATM 12535 O  O   . HOH VA 8 .   ? 76.174  50.137  -26.270 1.00 37.13 ? 2253 HOH D O   1 
HETATM 12536 O  O   . HOH VA 8 .   ? 72.981  49.993  -23.729 1.00 44.70 ? 2254 HOH D O   1 
HETATM 12537 O  O   . HOH VA 8 .   ? 73.796  47.418  -19.618 1.00 31.26 ? 2255 HOH D O   1 
HETATM 12538 O  O   . HOH VA 8 .   ? 76.041  47.092  -18.586 1.00 24.41 ? 2256 HOH D O   1 
HETATM 12539 O  O   . HOH VA 8 .   ? 81.054  45.056  -26.616 1.00 22.40 ? 2257 HOH D O   1 
HETATM 12540 O  O   . HOH VA 8 .   ? 79.904  47.415  -32.764 1.00 36.02 ? 2258 HOH D O   1 
HETATM 12541 O  O   . HOH VA 8 .   ? 71.654  43.176  -27.940 1.00 33.38 ? 2259 HOH D O   1 
HETATM 12542 O  O   . HOH VA 8 .   ? 79.284  44.261  -29.651 1.00 19.48 ? 2260 HOH D O   1 
HETATM 12543 O  O   . HOH VA 8 .   ? 71.081  41.464  -34.532 1.00 32.34 ? 2261 HOH D O   1 
HETATM 12544 O  O   . HOH VA 8 .   ? 74.904  36.549  -32.780 1.00 16.78 ? 2262 HOH D O   1 
HETATM 12545 O  O   . HOH VA 8 .   ? 70.336  36.968  -33.278 1.00 36.06 ? 2263 HOH D O   1 
HETATM 12546 O  O   . HOH VA 8 .   ? 71.627  41.244  -25.546 1.00 26.60 ? 2264 HOH D O   1 
HETATM 12547 O  O   . HOH VA 8 .   ? 79.440  34.653  -10.679 1.00 15.42 ? 2265 HOH D O   1 
HETATM 12548 O  O   . HOH VA 8 .   ? 76.023  34.006  -5.841  1.00 16.24 ? 2266 HOH D O   1 
HETATM 12549 O  O   . HOH VA 8 .   ? 75.161  34.455  -9.705  1.00 16.64 ? 2267 HOH D O   1 
HETATM 12550 O  O   . HOH VA 8 .   ? 65.353  26.566  -7.090  1.00 18.87 ? 2268 HOH D O   1 
HETATM 12551 O  O   . HOH VA 8 .   ? 64.439  23.634  1.475   1.00 35.87 ? 2269 HOH D O   1 
HETATM 12552 O  O   . HOH VA 8 .   ? 59.889  22.814  -3.983  1.00 31.64 ? 2270 HOH D O   1 
HETATM 12553 O  O   . HOH VA 8 .   ? 59.739  23.952  1.408   1.00 45.36 ? 2271 HOH D O   1 
HETATM 12554 O  O   . HOH VA 8 .   ? 54.975  25.648  -13.657 1.00 23.76 ? 2272 HOH D O   1 
HETATM 12555 O  O   . HOH VA 8 .   ? 61.708  27.078  -13.643 1.00 24.84 ? 2273 HOH D O   1 
HETATM 12556 O  O   . HOH VA 8 .   ? 55.754  30.384  -19.347 1.00 31.73 ? 2274 HOH D O   1 
HETATM 12557 O  O   . HOH VA 8 .   ? 55.062  29.574  -15.027 1.00 32.03 ? 2275 HOH D O   1 
HETATM 12558 O  O   . HOH VA 8 .   ? 59.186  34.878  -23.375 1.00 35.68 ? 2276 HOH D O   1 
HETATM 12559 O  O   . HOH VA 8 .   ? 58.823  31.851  -26.549 1.00 37.87 ? 2277 HOH D O   1 
HETATM 12560 O  O   . HOH VA 8 .   ? 58.382  33.620  -20.436 1.00 37.75 ? 2278 HOH D O   1 
HETATM 12561 O  O   . HOH VA 8 .   ? 62.483  28.651  -24.169 1.00 20.41 ? 2279 HOH D O   1 
HETATM 12562 O  O   . HOH VA 8 .   ? 65.203  30.845  -32.227 1.00 32.67 ? 2280 HOH D O   1 
HETATM 12563 O  O   . HOH VA 8 .   ? 61.168  30.651  -30.961 1.00 26.08 ? 2281 HOH D O   1 
HETATM 12564 O  O   . HOH VA 8 .   ? 65.250  28.708  -24.849 1.00 16.31 ? 2282 HOH D O   1 
HETATM 12565 O  O   . HOH VA 8 .   ? 67.694  30.648  -31.031 1.00 20.67 ? 2283 HOH D O   1 
HETATM 12566 O  O   . HOH VA 8 .   ? 82.626  25.681  -9.092  1.00 42.71 ? 2284 HOH D O   1 
HETATM 12567 O  O   . HOH VA 8 .   ? 81.312  21.680  -8.206  1.00 40.82 ? 2285 HOH D O   1 
HETATM 12568 O  O   . HOH VA 8 .   ? 82.414  22.632  -12.474 1.00 41.62 ? 2286 HOH D O   1 
HETATM 12569 O  O   . HOH VA 8 .   ? 83.397  26.929  -11.570 1.00 25.60 ? 2287 HOH D O   1 
HETATM 12570 O  O   . HOH VA 8 .   ? 80.786  28.467  -6.844  1.00 21.32 ? 2288 HOH D O   1 
HETATM 12571 O  O   . HOH VA 8 .   ? 70.336  19.500  -0.613  1.00 22.56 ? 2289 HOH D O   1 
HETATM 12572 O  O   . HOH VA 8 .   ? 58.640  16.881  -19.433 1.00 29.91 ? 2290 HOH D O   1 
HETATM 12573 O  O   . HOH VA 8 .   ? 57.928  21.147  -19.202 1.00 39.77 ? 2291 HOH D O   1 
HETATM 12574 O  O   . HOH VA 8 .   ? 60.048  17.856  -26.087 1.00 28.97 ? 2292 HOH D O   1 
HETATM 12575 O  O   . HOH VA 8 .   ? 63.752  17.175  -18.912 1.00 32.35 ? 2293 HOH D O   1 
HETATM 12576 O  O   . HOH VA 8 .   ? 60.178  13.739  -15.352 1.00 33.08 ? 2294 HOH D O   1 
HETATM 12577 O  O   . HOH VA 8 .   ? 66.102  13.183  -19.110 1.00 42.93 ? 2295 HOH D O   1 
HETATM 12578 O  O   . HOH VA 8 .   ? 69.056  12.813  -13.065 1.00 23.69 ? 2296 HOH D O   1 
HETATM 12579 O  O   . HOH VA 8 .   ? 68.841  13.699  -5.850  1.00 31.84 ? 2297 HOH D O   1 
HETATM 12580 O  O   . HOH VA 8 .   ? 66.549  15.016  -8.474  1.00 28.34 ? 2298 HOH D O   1 
HETATM 12581 O  O   . HOH VA 8 .   ? 72.627  13.877  -6.458  1.00 25.61 ? 2299 HOH D O   1 
HETATM 12582 O  O   . HOH VA 8 .   ? 73.240  16.298  -9.505  1.00 22.57 ? 2300 HOH D O   1 
HETATM 12583 O  O   . HOH VA 8 .   ? 80.101  16.045  -12.693 1.00 11.35 ? 2301 HOH D O   1 
HETATM 12584 O  O   . HOH VA 8 .   ? 78.556  14.734  -14.438 1.00 12.51 ? 2302 HOH D O   1 
HETATM 12585 O  O   . HOH VA 8 .   ? 60.337  25.544  -30.347 1.00 33.86 ? 2303 HOH D O   1 
HETATM 12586 O  O   . HOH VA 8 .   ? 63.924  26.321  -31.532 1.00 25.53 ? 2304 HOH D O   1 
HETATM 12587 O  O   . HOH VA 8 .   ? 66.444  27.022  -30.726 1.00 16.06 ? 2305 HOH D O   1 
HETATM 12588 O  O   . HOH VA 8 .   ? 55.956  21.946  -23.057 1.00 36.07 ? 2306 HOH D O   1 
HETATM 12589 O  O   . HOH VA 8 .   ? 57.440  22.942  -25.131 1.00 28.60 ? 2307 HOH D O   1 
HETATM 12590 O  O   . HOH VA 8 .   ? 57.041  19.557  -13.029 1.00 37.30 ? 2308 HOH D O   1 
HETATM 12591 O  O   . HOH VA 8 .   ? 62.875  28.102  -10.915 1.00 24.93 ? 2309 HOH D O   1 
HETATM 12592 O  O   . HOH VA 8 .   ? 62.943  30.431  -12.137 1.00 17.59 ? 2310 HOH D O   1 
HETATM 12593 O  O   . HOH VA 8 .   ? 64.076  23.139  -4.886  1.00 22.24 ? 2311 HOH D O   1 
HETATM 12594 O  O   . HOH VA 8 .   ? 64.608  16.611  -7.051  1.00 40.17 ? 2312 HOH D O   1 
HETATM 12595 O  O   . HOH VA 8 .   ? 62.757  18.968  -4.374  1.00 32.14 ? 2313 HOH D O   1 
HETATM 12596 O  O   . HOH VA 8 .   ? 68.274  15.921  -2.831  1.00 35.97 ? 2314 HOH D O   1 
HETATM 12597 O  O   . HOH VA 8 .   ? 66.098  20.139  -1.976  1.00 29.91 ? 2315 HOH D O   1 
HETATM 12598 O  O   . HOH VA 8 .   ? 68.096  26.915  -0.209  1.00 14.83 ? 2316 HOH D O   1 
HETATM 12599 O  O   . HOH VA 8 .   ? 65.686  21.581  5.553   1.00 37.15 ? 2317 HOH D O   1 
HETATM 12600 O  O   . HOH VA 8 .   ? 68.752  18.382  1.136   1.00 26.70 ? 2318 HOH D O   1 
HETATM 12601 O  O   . HOH VA 8 .   ? 75.794  23.326  -3.087  1.00 22.52 ? 2319 HOH D O   1 
HETATM 12602 O  O   . HOH VA 8 .   ? 81.462  31.033  -6.474  1.00 16.98 ? 2320 HOH D O   1 
HETATM 12603 O  O   . HOH VA 8 .   ? 82.997  29.118  -9.766  1.00 26.31 ? 2321 HOH D O   1 
HETATM 12604 O  O   . HOH VA 8 .   ? 68.882  36.778  -23.579 1.00 21.56 ? 2322 HOH D O   1 
HETATM 12605 O  O   . HOH VA 8 .   ? 66.405  32.739  -24.420 1.00 17.65 ? 2323 HOH D O   1 
HETATM 12606 O  O   . HOH VA 8 .   ? 69.244  32.437  -32.474 1.00 31.77 ? 2324 HOH D O   1 
HETATM 12607 O  O   . HOH VA 8 .   ? 71.690  35.513  -30.862 1.00 25.10 ? 2325 HOH D O   1 
HETATM 12608 O  O   . HOH VA 8 .   ? 65.376  34.785  -26.043 1.00 17.54 ? 2326 HOH D O   1 
HETATM 12609 O  O   . HOH VA 8 .   ? 65.792  39.829  -28.400 1.00 32.75 ? 2327 HOH D O   1 
HETATM 12610 O  O   . HOH VA 8 .   ? 63.409  40.416  -20.143 1.00 52.83 ? 2328 HOH D O   1 
HETATM 12611 O  O   . HOH VA 8 .   ? 64.968  44.123  -21.086 1.00 32.72 ? 2329 HOH D O   1 
HETATM 12612 O  O   . HOH VA 8 .   ? 64.769  37.487  -25.680 1.00 21.14 ? 2330 HOH D O   1 
HETATM 12613 O  O   . HOH VA 8 .   ? 66.319  32.116  -21.692 1.00 16.39 ? 2331 HOH D O   1 
HETATM 12614 O  O   . HOH VA 8 .   ? 72.955  39.355  -18.327 1.00 15.58 ? 2332 HOH D O   1 
HETATM 12615 O  O   . HOH VA 8 .   ? 70.226  43.099  -21.685 1.00 23.49 ? 2333 HOH D O   1 
HETATM 12616 O  O   . HOH VA 8 .   ? 71.360  41.317  -17.431 1.00 23.47 ? 2334 HOH D O   1 
HETATM 12617 O  O   . HOH VA 8 .   ? 60.888  40.456  -15.515 1.00 27.22 ? 2335 HOH D O   1 
HETATM 12618 O  O   . HOH VA 8 .   ? 59.883  37.128  -13.793 1.00 29.01 ? 2336 HOH D O   1 
HETATM 12619 O  O   . HOH VA 8 .   ? 59.521  42.777  -14.350 1.00 32.21 ? 2337 HOH D O   1 
HETATM 12620 O  O   . HOH VA 8 .   ? 59.244  41.399  -9.869  1.00 31.15 ? 2338 HOH D O   1 
HETATM 12621 O  O   . HOH VA 8 .   ? 62.008  39.821  -7.187  1.00 23.54 ? 2339 HOH D O   1 
HETATM 12622 O  O   . HOH VA 8 .   ? 61.736  44.750  -10.219 1.00 29.62 ? 2340 HOH D O   1 
HETATM 12623 O  O   . HOH VA 8 .   ? 64.372  40.747  -4.884  1.00 24.77 ? 2341 HOH D O   1 
HETATM 12624 O  O   . HOH VA 8 .   ? 67.501  48.170  -7.890  1.00 33.99 ? 2342 HOH D O   1 
HETATM 12625 O  O   . HOH VA 8 .   ? 68.136  46.157  -3.333  1.00 36.86 ? 2343 HOH D O   1 
HETATM 12626 O  O   . HOH VA 8 .   ? 75.600  44.217  -6.928  1.00 25.68 ? 2344 HOH D O   1 
HETATM 12627 O  O   . HOH VA 8 .   ? 71.997  44.567  -1.136  1.00 37.20 ? 2345 HOH D O   1 
HETATM 12628 O  O   . HOH VA 8 .   ? 79.822  44.611  -1.215  1.00 48.80 ? 2346 HOH D O   1 
HETATM 12629 O  O   . HOH VA 8 .   ? 78.780  41.491  0.766   1.00 39.05 ? 2347 HOH D O   1 
HETATM 12630 O  O   . HOH VA 8 .   ? 77.059  40.099  1.920   1.00 26.15 ? 2348 HOH D O   1 
HETATM 12631 O  O   . HOH VA 8 .   ? 69.188  37.729  5.762   1.00 26.32 ? 2349 HOH D O   1 
HETATM 12632 O  O   . HOH VA 8 .   ? 66.778  32.433  9.402   1.00 23.14 ? 2350 HOH D O   1 
HETATM 12633 O  O   . HOH VA 8 .   ? 66.559  37.491  5.824   1.00 24.65 ? 2351 HOH D O   1 
HETATM 12634 O  O   . HOH VA 8 .   ? 63.326  32.493  8.828   1.00 22.24 ? 2352 HOH D O   1 
HETATM 12635 O  O   . HOH VA 8 .   ? 64.467  34.743  11.402  1.00 33.63 ? 2353 HOH D O   1 
HETATM 12636 O  O   . HOH VA 8 .   ? 60.444  34.663  6.572   1.00 34.38 ? 2354 HOH D O   1 
HETATM 12637 O  O   . HOH VA 8 .   ? 61.787  32.272  6.682   1.00 24.66 ? 2355 HOH D O   1 
HETATM 12638 O  O   . HOH VA 8 .   ? 82.784  46.809  -32.708 1.00 40.00 ? 2356 HOH D O   1 
HETATM 12639 O  O   . HOH VA 8 .   ? 96.494  39.356  -0.175  1.00 22.95 ? 2357 HOH D O   1 
HETATM 12640 O  O   . HOH VA 8 .   ? 96.646  43.876  2.021   1.00 37.06 ? 2358 HOH D O   1 
HETATM 12641 O  O   . HOH VA 8 .   ? 92.874  5.970   -36.051 1.00 25.01 ? 2359 HOH D O   1 
HETATM 12642 O  O   . HOH VA 8 .   ? 95.267  9.224   -40.375 1.00 36.19 ? 2360 HOH D O   1 
HETATM 12643 O  O   . HOH VA 8 .   ? 92.417  9.098   -30.240 1.00 30.97 ? 2361 HOH D O   1 
HETATM 12644 O  O   . HOH VA 8 .   ? 63.366  33.883  -32.644 1.00 41.03 ? 2362 HOH D O   1 
HETATM 12645 O  O   . HOH VA 8 .   ? 87.072  26.654  -23.864 1.00 16.88 ? 2363 HOH D O   1 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   ASP 1   1   ?   ?   ?   A . n 
A 1 2   THR 2   2   ?   ?   ?   A . n 
A 1 3   SER 3   3   3   SER SER A . n 
A 1 4   SER 4   4   4   SER SER A . n 
A 1 5   LEU 5   5   5   LEU LEU A . n 
A 1 6   ILE 6   6   6   ILE ILE A . n 
A 1 7   VAL 7   7   7   VAL VAL A . n 
A 1 8   GLU 8   8   8   GLU GLU A . n 
A 1 9   ASP 9   9   9   ASP ASP A . n 
A 1 10  ALA 10  10  10  ALA ALA A . n 
A 1 11  PRO 11  11  11  PRO PRO A . n 
A 1 12  ASP 12  12  12  ASP ASP A . n 
A 1 13  HIS 13  13  13  HIS HIS A . n 
A 1 14  VAL 14  14  14  VAL VAL A . n 
A 1 15  ARG 15  15  15  ARG ARG A . n 
A 1 16  PRO 16  16  16  PRO PRO A . n 
A 1 17  TYR 17  17  17  TYR TYR A . n 
A 1 18  VAL 18  18  18  VAL VAL A . n 
A 1 19  ILE 19  19  19  ILE ILE A . n 
A 1 20  ARG 20  20  20  ARG ARG A . n 
A 1 21  HIS 21  21  21  HIS HIS A . n 
A 1 22  TYR 22  22  22  TYR TYR A . n 
A 1 23  SER 23  23  23  SER SER A . n 
A 1 24  HIS 24  24  24  HIS HIS A . n 
A 1 25  ALA 25  25  25  ALA ALA A . n 
A 1 26  ARG 26  26  26  ARG ARG A . n 
A 1 27  ALA 27  27  27  ALA ALA A . n 
A 1 28  VAL 28  28  28  VAL VAL A . n 
A 1 29  THR 29  29  29  THR THR A . n 
A 1 30  VAL 30  30  30  VAL VAL A . n 
A 1 31  ASP 31  31  31  ASP ASP A . n 
A 1 32  THR 32  32  32  THR THR A . n 
A 1 33  GLN 33  33  33  GLN GLN A . n 
A 1 34  LEU 34  34  34  LEU LEU A . n 
A 1 35  TYR 35  35  35  TYR TYR A . n 
A 1 36  ARG 36  36  36  ARG ARG A . n 
A 1 37  PHE 37  37  37  PHE PHE A . n 
A 1 38  TYR 38  38  38  TYR TYR A . n 
A 1 39  VAL 39  39  39  VAL VAL A . n 
A 1 40  THR 40  40  40  THR THR A . n 
A 1 41  GLY 41  41  41  GLY GLY A . n 
A 1 42  PRO 42  42  42  PRO PRO A . n 
A 1 43  SER 43  43  43  SER SER A . n 
A 1 44  SER 44  44  44  SER SER A . n 
A 1 45  GLY 45  45  45  GLY GLY A . n 
A 1 46  TYR 46  46  46  TYR TYR A . n 
A 1 47  ALA 47  47  47  ALA ALA A . n 
A 1 48  PHE 48  48  48  PHE PHE A . n 
A 1 49  THR 49  49  49  THR THR A . n 
A 1 50  LEU 50  50  50  LEU LEU A . n 
A 1 51  MET 51  51  51  MET MET A . n 
A 1 52  GLY 52  52  52  GLY GLY A . n 
A 1 53  THR 53  53  53  THR THR A . n 
A 1 54  ASN 54  54  54  ASN ASN A . n 
A 1 55  ALA 55  55  55  ALA ALA A . n 
A 1 56  PRO 56  56  56  PRO PRO A . n 
A 1 57  HIS 57  57  57  HIS HIS A . n 
A 1 58  SER 58  58  58  SER SER A . n 
A 1 59  ASP 59  59  59  ASP ASP A . n 
A 1 60  ALA 60  60  60  ALA ALA A . n 
A 1 61  LEU 61  61  61  LEU LEU A . n 
A 1 62  GLY 62  62  62  GLY GLY A . n 
A 1 63  VAL 63  63  63  VAL VAL A . n 
A 1 64  LEU 64  64  64  LEU LEU A . n 
A 1 65  PRO 65  65  65  PRO PRO A . n 
A 1 66  HIS 66  66  66  HIS HIS A . n 
A 1 67  ILE 67  67  67  ILE ILE A . n 
A 1 68  HIS 68  68  68  HIS HIS A . n 
A 1 69  GLN 69  69  69  GLN GLN A . n 
A 1 70  LYS 70  70  70  LYS LYS A . n 
A 1 71  HIS 71  71  71  HIS HIS A . n 
A 1 72  TYR 72  72  72  TYR TYR A . n 
A 1 73  GLU 73  73  73  GLU GLU A . n 
A 1 74  ASN 74  74  74  ASN ASN A . n 
A 1 75  PHE 75  75  75  PHE PHE A . n 
A 1 76  TYR 76  76  76  TYR TYR A . n 
A 1 77  CYS 77  77  77  CYS CYS A . n 
A 1 78  ASN 78  78  78  ASN ASN A . n 
A 1 79  LYS 79  79  79  LYS LYS A . n 
A 1 80  GLY 80  80  80  GLY GLY A . n 
A 1 81  SER 81  81  81  SER SER A . n 
A 1 82  PHE 82  82  82  PHE PHE A . n 
A 1 83  GLN 83  83  83  GLN GLN A . n 
A 1 84  LEU 84  84  84  LEU LEU A . n 
A 1 85  TRP 85  85  85  TRP TRP A . n 
A 1 86  ALA 86  86  86  ALA ALA A . n 
A 1 87  GLN 87  87  87  GLN GLN A . n 
A 1 88  SER 88  88  88  SER SER A . n 
A 1 89  GLY 89  89  89  GLY GLY A . n 
A 1 90  ASN 90  90  90  ASN ASN A . n 
A 1 91  GLU 91  91  91  GLU GLU A . n 
A 1 92  THR 92  92  92  THR THR A . n 
A 1 93  GLN 93  93  93  GLN GLN A . n 
A 1 94  GLN 94  94  94  GLN GLN A . n 
A 1 95  THR 95  95  95  THR THR A . n 
A 1 96  ARG 96  96  96  ARG ARG A . n 
A 1 97  VAL 97  97  97  VAL VAL A . n 
A 1 98  LEU 98  98  98  LEU LEU A . n 
A 1 99  SER 99  99  99  SER SER A . n 
A 1 100 SER 100 100 100 SER SER A . n 
A 1 101 GLY 101 101 101 GLY GLY A . n 
A 1 102 ASP 102 102 102 ASP ASP A . n 
A 1 103 TYR 103 103 103 TYR TYR A . n 
A 1 104 GLY 104 104 104 GLY GLY A . n 
A 1 105 SER 105 105 105 SER SER A . n 
A 1 106 VAL 106 106 106 VAL VAL A . n 
A 1 107 PRO 107 107 107 PRO PRO A . n 
A 1 108 ARG 108 108 108 ARG ARG A . n 
A 1 109 ASN 109 109 109 ASN ASN A . n 
A 1 110 VAL 110 110 110 VAL VAL A . n 
A 1 111 THR 111 111 111 THR THR A . n 
A 1 112 HIS 112 112 112 HIS HIS A . n 
A 1 113 THR 113 113 113 THR THR A . n 
A 1 114 PHE 114 114 114 PHE PHE A . n 
A 1 115 GLN 115 115 115 GLN GLN A . n 
A 1 116 ILE 116 116 116 ILE ILE A . n 
A 1 117 GLN 117 117 117 GLN GLN A . n 
A 1 118 ASP 118 118 118 ASP ASP A . n 
A 1 119 PRO 119 119 119 PRO PRO A . n 
A 1 120 ASP 120 120 120 ASP ASP A . n 
A 1 121 THR 121 121 121 THR THR A . n 
A 1 122 GLU 122 122 122 GLU GLU A . n 
A 1 123 MET 123 123 123 MET MET A . n 
A 1 124 THR 124 124 124 THR THR A . n 
A 1 125 GLY 125 125 125 GLY GLY A . n 
A 1 126 VAL 126 126 126 VAL VAL A . n 
A 1 127 ILE 127 127 127 ILE ILE A . n 
A 1 128 VAL 128 128 128 VAL VAL A . n 
A 1 129 PRO 129 129 129 PRO PRO A . n 
A 1 130 GLY 130 130 130 GLY GLY A . n 
A 1 131 GLY 131 131 131 GLY GLY A . n 
A 1 132 PHE 132 132 132 PHE PHE A . n 
A 1 133 GLU 133 133 133 GLU GLU A . n 
A 1 134 ASP 134 134 134 ASP ASP A . n 
A 1 135 LEU 135 135 135 LEU LEU A . n 
A 1 136 PHE 136 136 136 PHE PHE A . n 
A 1 137 TYR 137 137 137 TYR TYR A . n 
A 1 138 TYR 138 138 138 TYR TYR A . n 
A 1 139 LEU 139 139 139 LEU LEU A . n 
A 1 140 GLY 140 140 140 GLY GLY A . n 
A 1 141 THR 141 141 141 THR THR A . n 
A 1 142 ASN 142 142 142 ASN ASN A . n 
A 1 143 ALA 143 143 143 ALA ALA A . n 
A 1 144 THR 144 144 144 THR THR A . n 
A 1 145 ASP 145 145 145 ASP ASP A . n 
A 1 146 THR 146 146 146 THR THR A . n 
A 1 147 THR 147 147 147 THR THR A . n 
A 1 148 HIS 148 148 148 HIS HIS A . n 
A 1 149 THR 149 149 149 THR THR A . n 
A 1 150 PRO 150 150 150 PRO PRO A . n 
A 1 151 TYR 151 151 151 TYR TYR A . n 
A 1 152 ILE 152 152 152 ILE ILE A . n 
A 1 153 PRO 153 153 153 PRO PRO A . n 
A 1 154 SER 154 154 154 SER SER A . n 
A 1 155 SER 155 155 ?   ?   ?   A . n 
A 1 156 SER 156 156 ?   ?   ?   A . n 
A 1 157 ASP 157 157 ?   ?   ?   A . n 
A 1 158 SER 158 158 ?   ?   ?   A . n 
A 1 159 SER 159 159 159 SER SER A . n 
A 1 160 SER 160 160 160 SER SER A . n 
A 1 161 THR 161 161 161 THR THR A . n 
A 1 162 THR 162 162 162 THR THR A . n 
A 1 163 GLY 163 163 163 GLY GLY A . n 
A 1 164 PRO 164 164 164 PRO PRO A . n 
A 1 165 ASP 165 165 165 ASP ASP A . n 
A 1 166 SER 166 166 166 SER SER A . n 
A 1 167 SER 167 167 167 SER SER A . n 
A 1 168 THR 168 168 168 THR THR A . n 
A 1 169 ILE 169 169 169 ILE ILE A . n 
A 1 170 SER 170 170 170 SER SER A . n 
A 1 171 THR 171 171 171 THR THR A . n 
A 1 172 LEU 172 172 172 LEU LEU A . n 
A 1 173 GLN 173 173 173 GLN GLN A . n 
A 1 174 SER 174 174 174 SER SER A . n 
A 1 175 PHE 175 175 175 PHE PHE A . n 
A 1 176 ASP 176 176 176 ASP ASP A . n 
A 1 177 VAL 177 177 177 VAL VAL A . n 
A 1 178 TYR 178 178 178 TYR TYR A . n 
A 1 179 ALA 179 179 179 ALA ALA A . n 
A 1 180 GLU 180 180 180 GLU GLU A . n 
A 1 181 LEU 181 181 181 LEU LEU A . n 
A 1 182 SER 182 182 182 SER SER A . n 
A 1 183 PHE 183 183 183 PHE PHE A . n 
A 1 184 THR 184 184 184 THR THR A . n 
A 1 185 PRO 185 185 185 PRO PRO A . n 
A 1 186 ARG 186 186 186 ARG ARG A . n 
A 1 187 THR 187 187 187 THR THR A . n 
A 1 188 ASP 188 188 188 ASP ASP A . n 
A 1 189 THR 189 189 189 THR THR A . n 
A 1 190 VAL 190 190 190 VAL VAL A . n 
A 1 191 ASN 191 191 191 ASN ASN A . n 
A 1 192 GLY 192 192 192 GLY GLY A . n 
A 1 193 THR 193 193 193 THR THR A . n 
A 1 194 ALA 194 194 194 ALA ALA A . n 
A 1 195 PRO 195 195 195 PRO PRO A . n 
A 1 196 ALA 196 196 196 ALA ALA A . n 
A 1 197 ASN 197 197 197 ASN ASN A . n 
A 1 198 THR 198 198 198 THR THR A . n 
A 1 199 VAL 199 199 199 VAL VAL A . n 
A 1 200 TRP 200 200 200 TRP TRP A . n 
A 1 201 HIS 201 201 201 HIS HIS A . n 
A 1 202 THR 202 202 202 THR THR A . n 
A 1 203 GLY 203 203 203 GLY GLY A . n 
A 1 204 ALA 204 204 204 ALA ALA A . n 
A 1 205 ASN 205 205 205 ASN ASN A . n 
A 1 206 ALA 206 206 206 ALA ALA A . n 
A 1 207 LEU 207 207 207 LEU LEU A . n 
A 1 208 ALA 208 208 208 ALA ALA A . n 
A 1 209 SER 209 209 209 SER SER A . n 
A 1 210 THR 210 210 210 THR THR A . n 
A 1 211 ALA 211 211 211 ALA ALA A . n 
A 1 212 GLY 212 212 212 GLY GLY A . n 
A 1 213 ASP 213 213 213 ASP ASP A . n 
A 1 214 PRO 214 214 214 PRO PRO A . n 
A 1 215 TYR 215 215 215 TYR TYR A . n 
A 1 216 PHE 216 216 216 PHE PHE A . n 
A 1 217 ILE 217 217 217 ILE ILE A . n 
A 1 218 ALA 218 218 218 ALA ALA A . n 
A 1 219 ASN 219 219 219 ASN ASN A . n 
A 1 220 GLY 220 220 220 GLY GLY A . n 
A 1 221 TRP 221 221 221 TRP TRP A . n 
A 1 222 GLY 222 222 222 GLY GLY A . n 
A 1 223 PRO 223 223 223 PRO PRO A . n 
A 1 224 LYS 224 224 224 LYS LYS A . n 
A 1 225 TYR 225 225 225 TYR TYR A . n 
A 1 226 LEU 226 226 226 LEU LEU A . n 
A 1 227 ASN 227 227 227 ASN ASN A . n 
A 1 228 SER 228 228 228 SER SER A . n 
A 1 229 GLN 229 229 229 GLN GLN A . n 
A 1 230 TYR 230 230 230 TYR TYR A . n 
A 1 231 GLY 231 231 231 GLY GLY A . n 
A 1 232 TYR 232 232 232 TYR TYR A . n 
A 1 233 GLN 233 233 233 GLN GLN A . n 
A 1 234 ILE 234 234 234 ILE ILE A . n 
A 1 235 VAL 235 235 235 VAL VAL A . n 
A 1 236 ALA 236 236 236 ALA ALA A . n 
A 1 237 PRO 237 237 237 PRO PRO A . n 
A 1 238 PHE 238 238 238 PHE PHE A . n 
A 1 239 VAL 239 239 239 VAL VAL A . n 
A 1 240 THR 240 240 240 THR THR A . n 
A 1 241 ALA 241 241 241 ALA ALA A . n 
A 1 242 THR 242 242 242 THR THR A . n 
A 1 243 GLN 243 243 243 GLN GLN A . n 
A 1 244 ALA 244 244 244 ALA ALA A . n 
A 1 245 GLN 245 245 245 GLN GLN A . n 
A 1 246 ASP 246 246 246 ASP ASP A . n 
A 1 247 THR 247 247 247 THR THR A . n 
A 1 248 ASN 248 248 248 ASN ASN A . n 
A 1 249 TYR 249 249 249 TYR TYR A . n 
A 1 250 THR 250 250 250 THR THR A . n 
A 1 251 LEU 251 251 251 LEU LEU A . n 
A 1 252 SER 252 252 252 SER SER A . n 
A 1 253 THR 253 253 253 THR THR A . n 
A 1 254 ILE 254 254 254 ILE ILE A . n 
A 1 255 SER 255 255 255 SER SER A . n 
A 1 256 MET 256 256 256 MET MET A . n 
A 1 257 SER 257 257 257 SER SER A . n 
A 1 258 THR 258 258 258 THR THR A . n 
A 1 259 THR 259 259 259 THR THR A . n 
A 1 260 PRO 260 260 260 PRO PRO A . n 
A 1 261 SER 261 261 261 SER SER A . n 
A 1 262 THR 262 262 262 THR THR A . n 
A 1 263 VAL 263 263 263 VAL VAL A . n 
A 1 264 THR 264 264 264 THR THR A . n 
A 1 265 VAL 265 265 265 VAL VAL A . n 
A 1 266 PRO 266 266 266 PRO PRO A . n 
A 1 267 THR 267 267 267 THR THR A . n 
A 1 268 TRP 268 268 268 TRP TRP A . n 
A 1 269 SER 269 269 269 SER SER A . n 
A 1 270 PHE 270 270 270 PHE PHE A . n 
A 1 271 PRO 271 271 271 PRO PRO A . n 
A 1 272 GLY 272 272 272 GLY GLY A . n 
A 1 273 ALA 273 273 273 ALA ALA A . n 
A 1 274 CYS 274 274 274 CYS CYS A . n 
A 1 275 ALA 275 275 275 ALA ALA A . n 
A 1 276 PHE 276 276 276 PHE PHE A . n 
A 1 277 GLN 277 277 277 GLN GLN A . n 
A 1 278 VAL 278 278 278 VAL VAL A . n 
A 1 279 GLN 279 279 279 GLN GLN A . n 
A 1 280 GLU 280 280 280 GLU GLU A . n 
A 1 281 GLY 281 281 281 GLY GLY A . n 
A 1 282 ARG 282 282 282 ARG ARG A . n 
A 1 283 VAL 283 283 283 VAL VAL A . n 
A 1 284 VAL 284 284 284 VAL VAL A . n 
A 1 285 VAL 285 285 285 VAL VAL A . n 
A 1 286 GLN 286 286 286 GLN GLN A . n 
A 1 287 ILE 287 287 287 ILE ILE A . n 
A 1 288 GLY 288 288 288 GLY GLY A . n 
A 1 289 ASP 289 289 289 ASP ASP A . n 
A 1 290 TYR 290 290 290 TYR TYR A . n 
A 1 291 ALA 291 291 291 ALA ALA A . n 
A 1 292 ALA 292 292 292 ALA ALA A . n 
A 1 293 THR 293 293 293 THR THR A . n 
A 1 294 GLU 294 294 294 GLU GLU A . n 
A 1 295 LEU 295 295 295 LEU LEU A . n 
A 1 296 GLY 296 296 296 GLY GLY A . n 
A 1 297 SER 297 297 297 SER SER A . n 
A 1 298 GLY 298 298 298 GLY GLY A . n 
A 1 299 ASP 299 299 299 ASP ASP A . n 
A 1 300 VAL 300 300 300 VAL VAL A . n 
A 1 301 ALA 301 301 301 ALA ALA A . n 
A 1 302 PHE 302 302 302 PHE PHE A . n 
A 1 303 ILE 303 303 303 ILE ILE A . n 
A 1 304 PRO 304 304 304 PRO PRO A . n 
A 1 305 GLY 305 305 305 GLY GLY A . n 
A 1 306 GLY 306 306 306 GLY GLY A . n 
A 1 307 VAL 307 307 307 VAL VAL A . n 
A 1 308 GLU 308 308 308 GLU GLU A . n 
A 1 309 PHE 309 309 309 PHE PHE A . n 
A 1 310 LYS 310 310 310 LYS LYS A . n 
A 1 311 TYR 311 311 311 TYR TYR A . n 
A 1 312 TYR 312 312 312 TYR TYR A . n 
A 1 313 SER 313 313 313 SER SER A . n 
A 1 314 GLU 314 314 314 GLU GLU A . n 
A 1 315 ALA 315 315 315 ALA ALA A . n 
A 1 316 TYR 316 316 316 TYR TYR A . n 
A 1 317 PHE 317 317 317 PHE PHE A . n 
A 1 318 SER 318 318 318 SER SER A . n 
A 1 319 LYS 319 319 319 LYS LYS A . n 
A 1 320 VAL 320 320 320 VAL VAL A . n 
A 1 321 LEU 321 321 321 LEU LEU A . n 
A 1 322 PHE 322 322 322 PHE PHE A . n 
A 1 323 VAL 323 323 323 VAL VAL A . n 
A 1 324 SER 324 324 324 SER SER A . n 
A 1 325 SER 325 325 325 SER SER A . n 
A 1 326 GLY 326 326 326 GLY GLY A . n 
A 1 327 SER 327 327 327 SER SER A . n 
A 1 328 ASP 328 328 328 ASP ASP A . n 
A 1 329 GLY 329 329 329 GLY GLY A . n 
A 1 330 LEU 330 330 330 LEU LEU A . n 
A 1 331 ASP 331 331 331 ASP ASP A . n 
A 1 332 GLN 332 332 332 GLN GLN A . n 
A 1 333 ASN 333 333 333 ASN ASN A . n 
A 1 334 LEU 334 334 334 LEU LEU A . n 
A 1 335 VAL 335 335 335 VAL VAL A . n 
A 1 336 ASN 336 336 336 ASN ASN A . n 
A 1 337 GLY 337 337 337 GLY GLY A . n 
A 1 338 GLY 338 338 338 GLY GLY A . n 
A 1 339 GLU 339 339 339 GLU GLU A . n 
A 1 340 GLU 340 340 340 GLU GLU A . n 
A 1 341 TRP 341 341 341 TRP TRP A . n 
A 1 342 SER 342 342 342 SER SER A . n 
A 1 343 SER 343 343 343 SER SER A . n 
A 1 344 VAL 344 344 344 VAL VAL A . n 
A 1 345 SER 345 345 345 SER SER A . n 
A 1 346 PHE 346 346 346 PHE PHE A . n 
A 1 347 PRO 347 347 347 PRO PRO A . n 
A 1 348 ALA 348 348 348 ALA ALA A . n 
A 1 349 ASP 349 349 349 ASP ASP A . n 
A 1 350 TRP 350 350 350 TRP TRP A . n 
B 1 1   ASP 1   1   ?   ?   ?   B . n 
B 1 2   THR 2   2   ?   ?   ?   B . n 
B 1 3   SER 3   3   3   SER SER B . n 
B 1 4   SER 4   4   4   SER SER B . n 
B 1 5   LEU 5   5   5   LEU LEU B . n 
B 1 6   ILE 6   6   6   ILE ILE B . n 
B 1 7   VAL 7   7   7   VAL VAL B . n 
B 1 8   GLU 8   8   8   GLU GLU B . n 
B 1 9   ASP 9   9   9   ASP ASP B . n 
B 1 10  ALA 10  10  10  ALA ALA B . n 
B 1 11  PRO 11  11  11  PRO PRO B . n 
B 1 12  ASP 12  12  12  ASP ASP B . n 
B 1 13  HIS 13  13  13  HIS HIS B . n 
B 1 14  VAL 14  14  14  VAL VAL B . n 
B 1 15  ARG 15  15  15  ARG ARG B . n 
B 1 16  PRO 16  16  16  PRO PRO B . n 
B 1 17  TYR 17  17  17  TYR TYR B . n 
B 1 18  VAL 18  18  18  VAL VAL B . n 
B 1 19  ILE 19  19  19  ILE ILE B . n 
B 1 20  ARG 20  20  20  ARG ARG B . n 
B 1 21  HIS 21  21  21  HIS HIS B . n 
B 1 22  TYR 22  22  22  TYR TYR B . n 
B 1 23  SER 23  23  23  SER SER B . n 
B 1 24  HIS 24  24  24  HIS HIS B . n 
B 1 25  ALA 25  25  25  ALA ALA B . n 
B 1 26  ARG 26  26  26  ARG ARG B . n 
B 1 27  ALA 27  27  27  ALA ALA B . n 
B 1 28  VAL 28  28  28  VAL VAL B . n 
B 1 29  THR 29  29  29  THR THR B . n 
B 1 30  VAL 30  30  30  VAL VAL B . n 
B 1 31  ASP 31  31  31  ASP ASP B . n 
B 1 32  THR 32  32  32  THR THR B . n 
B 1 33  GLN 33  33  33  GLN GLN B . n 
B 1 34  LEU 34  34  34  LEU LEU B . n 
B 1 35  TYR 35  35  35  TYR TYR B . n 
B 1 36  ARG 36  36  36  ARG ARG B . n 
B 1 37  PHE 37  37  37  PHE PHE B . n 
B 1 38  TYR 38  38  38  TYR TYR B . n 
B 1 39  VAL 39  39  39  VAL VAL B . n 
B 1 40  THR 40  40  40  THR THR B . n 
B 1 41  GLY 41  41  41  GLY GLY B . n 
B 1 42  PRO 42  42  42  PRO PRO B . n 
B 1 43  SER 43  43  43  SER SER B . n 
B 1 44  SER 44  44  44  SER SER B . n 
B 1 45  GLY 45  45  45  GLY GLY B . n 
B 1 46  TYR 46  46  46  TYR TYR B . n 
B 1 47  ALA 47  47  47  ALA ALA B . n 
B 1 48  PHE 48  48  48  PHE PHE B . n 
B 1 49  THR 49  49  49  THR THR B . n 
B 1 50  LEU 50  50  50  LEU LEU B . n 
B 1 51  MET 51  51  51  MET MET B . n 
B 1 52  GLY 52  52  52  GLY GLY B . n 
B 1 53  THR 53  53  53  THR THR B . n 
B 1 54  ASN 54  54  54  ASN ASN B . n 
B 1 55  ALA 55  55  55  ALA ALA B . n 
B 1 56  PRO 56  56  56  PRO PRO B . n 
B 1 57  HIS 57  57  57  HIS HIS B . n 
B 1 58  SER 58  58  58  SER SER B . n 
B 1 59  ASP 59  59  59  ASP ASP B . n 
B 1 60  ALA 60  60  60  ALA ALA B . n 
B 1 61  LEU 61  61  61  LEU LEU B . n 
B 1 62  GLY 62  62  62  GLY GLY B . n 
B 1 63  VAL 63  63  63  VAL VAL B . n 
B 1 64  LEU 64  64  64  LEU LEU B . n 
B 1 65  PRO 65  65  65  PRO PRO B . n 
B 1 66  HIS 66  66  66  HIS HIS B . n 
B 1 67  ILE 67  67  67  ILE ILE B . n 
B 1 68  HIS 68  68  68  HIS HIS B . n 
B 1 69  GLN 69  69  69  GLN GLN B . n 
B 1 70  LYS 70  70  70  LYS LYS B . n 
B 1 71  HIS 71  71  71  HIS HIS B . n 
B 1 72  TYR 72  72  72  TYR TYR B . n 
B 1 73  GLU 73  73  73  GLU GLU B . n 
B 1 74  ASN 74  74  74  ASN ASN B . n 
B 1 75  PHE 75  75  75  PHE PHE B . n 
B 1 76  TYR 76  76  76  TYR TYR B . n 
B 1 77  CYS 77  77  77  CYS CYS B . n 
B 1 78  ASN 78  78  78  ASN ASN B . n 
B 1 79  LYS 79  79  79  LYS LYS B . n 
B 1 80  GLY 80  80  80  GLY GLY B . n 
B 1 81  SER 81  81  81  SER SER B . n 
B 1 82  PHE 82  82  82  PHE PHE B . n 
B 1 83  GLN 83  83  83  GLN GLN B . n 
B 1 84  LEU 84  84  84  LEU LEU B . n 
B 1 85  TRP 85  85  85  TRP TRP B . n 
B 1 86  ALA 86  86  86  ALA ALA B . n 
B 1 87  GLN 87  87  87  GLN GLN B . n 
B 1 88  SER 88  88  88  SER SER B . n 
B 1 89  GLY 89  89  89  GLY GLY B . n 
B 1 90  ASN 90  90  90  ASN ASN B . n 
B 1 91  GLU 91  91  91  GLU GLU B . n 
B 1 92  THR 92  92  92  THR THR B . n 
B 1 93  GLN 93  93  93  GLN GLN B . n 
B 1 94  GLN 94  94  94  GLN GLN B . n 
B 1 95  THR 95  95  95  THR THR B . n 
B 1 96  ARG 96  96  96  ARG ARG B . n 
B 1 97  VAL 97  97  97  VAL VAL B . n 
B 1 98  LEU 98  98  98  LEU LEU B . n 
B 1 99  SER 99  99  99  SER SER B . n 
B 1 100 SER 100 100 100 SER SER B . n 
B 1 101 GLY 101 101 101 GLY GLY B . n 
B 1 102 ASP 102 102 102 ASP ASP B . n 
B 1 103 TYR 103 103 103 TYR TYR B . n 
B 1 104 GLY 104 104 104 GLY GLY B . n 
B 1 105 SER 105 105 105 SER SER B . n 
B 1 106 VAL 106 106 106 VAL VAL B . n 
B 1 107 PRO 107 107 107 PRO PRO B . n 
B 1 108 ARG 108 108 108 ARG ARG B . n 
B 1 109 ASN 109 109 109 ASN ASN B . n 
B 1 110 VAL 110 110 110 VAL VAL B . n 
B 1 111 THR 111 111 111 THR THR B . n 
B 1 112 HIS 112 112 112 HIS HIS B . n 
B 1 113 THR 113 113 113 THR THR B . n 
B 1 114 PHE 114 114 114 PHE PHE B . n 
B 1 115 GLN 115 115 115 GLN GLN B . n 
B 1 116 ILE 116 116 116 ILE ILE B . n 
B 1 117 GLN 117 117 117 GLN GLN B . n 
B 1 118 ASP 118 118 118 ASP ASP B . n 
B 1 119 PRO 119 119 119 PRO PRO B . n 
B 1 120 ASP 120 120 120 ASP ASP B . n 
B 1 121 THR 121 121 121 THR THR B . n 
B 1 122 GLU 122 122 122 GLU GLU B . n 
B 1 123 MET 123 123 123 MET MET B . n 
B 1 124 THR 124 124 124 THR THR B . n 
B 1 125 GLY 125 125 125 GLY GLY B . n 
B 1 126 VAL 126 126 126 VAL VAL B . n 
B 1 127 ILE 127 127 127 ILE ILE B . n 
B 1 128 VAL 128 128 128 VAL VAL B . n 
B 1 129 PRO 129 129 129 PRO PRO B . n 
B 1 130 GLY 130 130 130 GLY GLY B . n 
B 1 131 GLY 131 131 131 GLY GLY B . n 
B 1 132 PHE 132 132 132 PHE PHE B . n 
B 1 133 GLU 133 133 133 GLU GLU B . n 
B 1 134 ASP 134 134 134 ASP ASP B . n 
B 1 135 LEU 135 135 135 LEU LEU B . n 
B 1 136 PHE 136 136 136 PHE PHE B . n 
B 1 137 TYR 137 137 137 TYR TYR B . n 
B 1 138 TYR 138 138 138 TYR TYR B . n 
B 1 139 LEU 139 139 139 LEU LEU B . n 
B 1 140 GLY 140 140 140 GLY GLY B . n 
B 1 141 THR 141 141 141 THR THR B . n 
B 1 142 ASN 142 142 142 ASN ASN B . n 
B 1 143 ALA 143 143 143 ALA ALA B . n 
B 1 144 THR 144 144 144 THR THR B . n 
B 1 145 ASP 145 145 145 ASP ASP B . n 
B 1 146 THR 146 146 146 THR THR B . n 
B 1 147 THR 147 147 147 THR THR B . n 
B 1 148 HIS 148 148 148 HIS HIS B . n 
B 1 149 THR 149 149 149 THR THR B . n 
B 1 150 PRO 150 150 150 PRO PRO B . n 
B 1 151 TYR 151 151 151 TYR TYR B . n 
B 1 152 ILE 152 152 152 ILE ILE B . n 
B 1 153 PRO 153 153 153 PRO PRO B . n 
B 1 154 SER 154 154 154 SER SER B . n 
B 1 155 SER 155 155 ?   ?   ?   B . n 
B 1 156 SER 156 156 ?   ?   ?   B . n 
B 1 157 ASP 157 157 ?   ?   ?   B . n 
B 1 158 SER 158 158 ?   ?   ?   B . n 
B 1 159 SER 159 159 159 SER SER B . n 
B 1 160 SER 160 160 160 SER SER B . n 
B 1 161 THR 161 161 161 THR THR B . n 
B 1 162 THR 162 162 162 THR THR B . n 
B 1 163 GLY 163 163 163 GLY GLY B . n 
B 1 164 PRO 164 164 164 PRO PRO B . n 
B 1 165 ASP 165 165 165 ASP ASP B . n 
B 1 166 SER 166 166 166 SER SER B . n 
B 1 167 SER 167 167 167 SER SER B . n 
B 1 168 THR 168 168 168 THR THR B . n 
B 1 169 ILE 169 169 169 ILE ILE B . n 
B 1 170 SER 170 170 170 SER SER B . n 
B 1 171 THR 171 171 171 THR THR B . n 
B 1 172 LEU 172 172 172 LEU LEU B . n 
B 1 173 GLN 173 173 173 GLN GLN B . n 
B 1 174 SER 174 174 174 SER SER B . n 
B 1 175 PHE 175 175 175 PHE PHE B . n 
B 1 176 ASP 176 176 176 ASP ASP B . n 
B 1 177 VAL 177 177 177 VAL VAL B . n 
B 1 178 TYR 178 178 178 TYR TYR B . n 
B 1 179 ALA 179 179 179 ALA ALA B . n 
B 1 180 GLU 180 180 180 GLU GLU B . n 
B 1 181 LEU 181 181 181 LEU LEU B . n 
B 1 182 SER 182 182 182 SER SER B . n 
B 1 183 PHE 183 183 183 PHE PHE B . n 
B 1 184 THR 184 184 184 THR THR B . n 
B 1 185 PRO 185 185 185 PRO PRO B . n 
B 1 186 ARG 186 186 186 ARG ARG B . n 
B 1 187 THR 187 187 187 THR THR B . n 
B 1 188 ASP 188 188 188 ASP ASP B . n 
B 1 189 THR 189 189 189 THR THR B . n 
B 1 190 VAL 190 190 190 VAL VAL B . n 
B 1 191 ASN 191 191 191 ASN ASN B . n 
B 1 192 GLY 192 192 192 GLY GLY B . n 
B 1 193 THR 193 193 193 THR THR B . n 
B 1 194 ALA 194 194 194 ALA ALA B . n 
B 1 195 PRO 195 195 195 PRO PRO B . n 
B 1 196 ALA 196 196 196 ALA ALA B . n 
B 1 197 ASN 197 197 197 ASN ASN B . n 
B 1 198 THR 198 198 198 THR THR B . n 
B 1 199 VAL 199 199 199 VAL VAL B . n 
B 1 200 TRP 200 200 200 TRP TRP B . n 
B 1 201 HIS 201 201 201 HIS HIS B . n 
B 1 202 THR 202 202 202 THR THR B . n 
B 1 203 GLY 203 203 203 GLY GLY B . n 
B 1 204 ALA 204 204 204 ALA ALA B . n 
B 1 205 ASN 205 205 205 ASN ASN B . n 
B 1 206 ALA 206 206 206 ALA ALA B . n 
B 1 207 LEU 207 207 207 LEU LEU B . n 
B 1 208 ALA 208 208 208 ALA ALA B . n 
B 1 209 SER 209 209 209 SER SER B . n 
B 1 210 THR 210 210 210 THR THR B . n 
B 1 211 ALA 211 211 211 ALA ALA B . n 
B 1 212 GLY 212 212 212 GLY GLY B . n 
B 1 213 ASP 213 213 213 ASP ASP B . n 
B 1 214 PRO 214 214 214 PRO PRO B . n 
B 1 215 TYR 215 215 215 TYR TYR B . n 
B 1 216 PHE 216 216 216 PHE PHE B . n 
B 1 217 ILE 217 217 217 ILE ILE B . n 
B 1 218 ALA 218 218 218 ALA ALA B . n 
B 1 219 ASN 219 219 219 ASN ASN B . n 
B 1 220 GLY 220 220 220 GLY GLY B . n 
B 1 221 TRP 221 221 221 TRP TRP B . n 
B 1 222 GLY 222 222 222 GLY GLY B . n 
B 1 223 PRO 223 223 223 PRO PRO B . n 
B 1 224 LYS 224 224 224 LYS LYS B . n 
B 1 225 TYR 225 225 225 TYR TYR B . n 
B 1 226 LEU 226 226 226 LEU LEU B . n 
B 1 227 ASN 227 227 227 ASN ASN B . n 
B 1 228 SER 228 228 228 SER SER B . n 
B 1 229 GLN 229 229 229 GLN GLN B . n 
B 1 230 TYR 230 230 230 TYR TYR B . n 
B 1 231 GLY 231 231 231 GLY GLY B . n 
B 1 232 TYR 232 232 232 TYR TYR B . n 
B 1 233 GLN 233 233 233 GLN GLN B . n 
B 1 234 ILE 234 234 234 ILE ILE B . n 
B 1 235 VAL 235 235 235 VAL VAL B . n 
B 1 236 ALA 236 236 236 ALA ALA B . n 
B 1 237 PRO 237 237 237 PRO PRO B . n 
B 1 238 PHE 238 238 238 PHE PHE B . n 
B 1 239 VAL 239 239 239 VAL VAL B . n 
B 1 240 THR 240 240 240 THR THR B . n 
B 1 241 ALA 241 241 241 ALA ALA B . n 
B 1 242 THR 242 242 242 THR THR B . n 
B 1 243 GLN 243 243 243 GLN GLN B . n 
B 1 244 ALA 244 244 244 ALA ALA B . n 
B 1 245 GLN 245 245 245 GLN GLN B . n 
B 1 246 ASP 246 246 246 ASP ASP B . n 
B 1 247 THR 247 247 247 THR THR B . n 
B 1 248 ASN 248 248 248 ASN ASN B . n 
B 1 249 TYR 249 249 249 TYR TYR B . n 
B 1 250 THR 250 250 250 THR THR B . n 
B 1 251 LEU 251 251 251 LEU LEU B . n 
B 1 252 SER 252 252 252 SER SER B . n 
B 1 253 THR 253 253 253 THR THR B . n 
B 1 254 ILE 254 254 254 ILE ILE B . n 
B 1 255 SER 255 255 255 SER SER B . n 
B 1 256 MET 256 256 256 MET MET B . n 
B 1 257 SER 257 257 257 SER SER B . n 
B 1 258 THR 258 258 258 THR THR B . n 
B 1 259 THR 259 259 259 THR THR B . n 
B 1 260 PRO 260 260 260 PRO PRO B . n 
B 1 261 SER 261 261 261 SER SER B . n 
B 1 262 THR 262 262 262 THR THR B . n 
B 1 263 VAL 263 263 263 VAL VAL B . n 
B 1 264 THR 264 264 264 THR THR B . n 
B 1 265 VAL 265 265 265 VAL VAL B . n 
B 1 266 PRO 266 266 266 PRO PRO B . n 
B 1 267 THR 267 267 267 THR THR B . n 
B 1 268 TRP 268 268 268 TRP TRP B . n 
B 1 269 SER 269 269 269 SER SER B . n 
B 1 270 PHE 270 270 270 PHE PHE B . n 
B 1 271 PRO 271 271 271 PRO PRO B . n 
B 1 272 GLY 272 272 272 GLY GLY B . n 
B 1 273 ALA 273 273 273 ALA ALA B . n 
B 1 274 CYS 274 274 274 CYS CYS B . n 
B 1 275 ALA 275 275 275 ALA ALA B . n 
B 1 276 PHE 276 276 276 PHE PHE B . n 
B 1 277 GLN 277 277 277 GLN GLN B . n 
B 1 278 VAL 278 278 278 VAL VAL B . n 
B 1 279 GLN 279 279 279 GLN GLN B . n 
B 1 280 GLU 280 280 280 GLU GLU B . n 
B 1 281 GLY 281 281 281 GLY GLY B . n 
B 1 282 ARG 282 282 282 ARG ARG B . n 
B 1 283 VAL 283 283 283 VAL VAL B . n 
B 1 284 VAL 284 284 284 VAL VAL B . n 
B 1 285 VAL 285 285 285 VAL VAL B . n 
B 1 286 GLN 286 286 286 GLN GLN B . n 
B 1 287 ILE 287 287 287 ILE ILE B . n 
B 1 288 GLY 288 288 288 GLY GLY B . n 
B 1 289 ASP 289 289 289 ASP ASP B . n 
B 1 290 TYR 290 290 290 TYR TYR B . n 
B 1 291 ALA 291 291 291 ALA ALA B . n 
B 1 292 ALA 292 292 292 ALA ALA B . n 
B 1 293 THR 293 293 293 THR THR B . n 
B 1 294 GLU 294 294 294 GLU GLU B . n 
B 1 295 LEU 295 295 295 LEU LEU B . n 
B 1 296 GLY 296 296 296 GLY GLY B . n 
B 1 297 SER 297 297 297 SER SER B . n 
B 1 298 GLY 298 298 298 GLY GLY B . n 
B 1 299 ASP 299 299 299 ASP ASP B . n 
B 1 300 VAL 300 300 300 VAL VAL B . n 
B 1 301 ALA 301 301 301 ALA ALA B . n 
B 1 302 PHE 302 302 302 PHE PHE B . n 
B 1 303 ILE 303 303 303 ILE ILE B . n 
B 1 304 PRO 304 304 304 PRO PRO B . n 
B 1 305 GLY 305 305 305 GLY GLY B . n 
B 1 306 GLY 306 306 306 GLY GLY B . n 
B 1 307 VAL 307 307 307 VAL VAL B . n 
B 1 308 GLU 308 308 308 GLU GLU B . n 
B 1 309 PHE 309 309 309 PHE PHE B . n 
B 1 310 LYS 310 310 310 LYS LYS B . n 
B 1 311 TYR 311 311 311 TYR TYR B . n 
B 1 312 TYR 312 312 312 TYR TYR B . n 
B 1 313 SER 313 313 313 SER SER B . n 
B 1 314 GLU 314 314 314 GLU GLU B . n 
B 1 315 ALA 315 315 315 ALA ALA B . n 
B 1 316 TYR 316 316 316 TYR TYR B . n 
B 1 317 PHE 317 317 317 PHE PHE B . n 
B 1 318 SER 318 318 318 SER SER B . n 
B 1 319 LYS 319 319 319 LYS LYS B . n 
B 1 320 VAL 320 320 320 VAL VAL B . n 
B 1 321 LEU 321 321 321 LEU LEU B . n 
B 1 322 PHE 322 322 322 PHE PHE B . n 
B 1 323 VAL 323 323 323 VAL VAL B . n 
B 1 324 SER 324 324 324 SER SER B . n 
B 1 325 SER 325 325 325 SER SER B . n 
B 1 326 GLY 326 326 326 GLY GLY B . n 
B 1 327 SER 327 327 327 SER SER B . n 
B 1 328 ASP 328 328 328 ASP ASP B . n 
B 1 329 GLY 329 329 329 GLY GLY B . n 
B 1 330 LEU 330 330 330 LEU LEU B . n 
B 1 331 ASP 331 331 331 ASP ASP B . n 
B 1 332 GLN 332 332 332 GLN GLN B . n 
B 1 333 ASN 333 333 333 ASN ASN B . n 
B 1 334 LEU 334 334 334 LEU LEU B . n 
B 1 335 VAL 335 335 335 VAL VAL B . n 
B 1 336 ASN 336 336 336 ASN ASN B . n 
B 1 337 GLY 337 337 337 GLY GLY B . n 
B 1 338 GLY 338 338 338 GLY GLY B . n 
B 1 339 GLU 339 339 339 GLU GLU B . n 
B 1 340 GLU 340 340 340 GLU GLU B . n 
B 1 341 TRP 341 341 341 TRP TRP B . n 
B 1 342 SER 342 342 342 SER SER B . n 
B 1 343 SER 343 343 343 SER SER B . n 
B 1 344 VAL 344 344 344 VAL VAL B . n 
B 1 345 SER 345 345 345 SER SER B . n 
B 1 346 PHE 346 346 346 PHE PHE B . n 
B 1 347 PRO 347 347 347 PRO PRO B . n 
B 1 348 ALA 348 348 348 ALA ALA B . n 
B 1 349 ASP 349 349 349 ASP ASP B . n 
B 1 350 TRP 350 350 350 TRP TRP B . n 
C 1 1   ASP 1   1   ?   ?   ?   C . n 
C 1 2   THR 2   2   ?   ?   ?   C . n 
C 1 3   SER 3   3   3   SER SER C . n 
C 1 4   SER 4   4   4   SER SER C . n 
C 1 5   LEU 5   5   5   LEU LEU C . n 
C 1 6   ILE 6   6   6   ILE ILE C . n 
C 1 7   VAL 7   7   7   VAL VAL C . n 
C 1 8   GLU 8   8   8   GLU GLU C . n 
C 1 9   ASP 9   9   9   ASP ASP C . n 
C 1 10  ALA 10  10  10  ALA ALA C . n 
C 1 11  PRO 11  11  11  PRO PRO C . n 
C 1 12  ASP 12  12  12  ASP ASP C . n 
C 1 13  HIS 13  13  13  HIS HIS C . n 
C 1 14  VAL 14  14  14  VAL VAL C . n 
C 1 15  ARG 15  15  15  ARG ARG C . n 
C 1 16  PRO 16  16  16  PRO PRO C . n 
C 1 17  TYR 17  17  17  TYR TYR C . n 
C 1 18  VAL 18  18  18  VAL VAL C . n 
C 1 19  ILE 19  19  19  ILE ILE C . n 
C 1 20  ARG 20  20  20  ARG ARG C . n 
C 1 21  HIS 21  21  21  HIS HIS C . n 
C 1 22  TYR 22  22  22  TYR TYR C . n 
C 1 23  SER 23  23  23  SER SER C . n 
C 1 24  HIS 24  24  24  HIS HIS C . n 
C 1 25  ALA 25  25  25  ALA ALA C . n 
C 1 26  ARG 26  26  26  ARG ARG C . n 
C 1 27  ALA 27  27  27  ALA ALA C . n 
C 1 28  VAL 28  28  28  VAL VAL C . n 
C 1 29  THR 29  29  29  THR THR C . n 
C 1 30  VAL 30  30  30  VAL VAL C . n 
C 1 31  ASP 31  31  31  ASP ASP C . n 
C 1 32  THR 32  32  32  THR THR C . n 
C 1 33  GLN 33  33  33  GLN GLN C . n 
C 1 34  LEU 34  34  34  LEU LEU C . n 
C 1 35  TYR 35  35  35  TYR TYR C . n 
C 1 36  ARG 36  36  36  ARG ARG C . n 
C 1 37  PHE 37  37  37  PHE PHE C . n 
C 1 38  TYR 38  38  38  TYR TYR C . n 
C 1 39  VAL 39  39  39  VAL VAL C . n 
C 1 40  THR 40  40  40  THR THR C . n 
C 1 41  GLY 41  41  41  GLY GLY C . n 
C 1 42  PRO 42  42  42  PRO PRO C . n 
C 1 43  SER 43  43  43  SER SER C . n 
C 1 44  SER 44  44  44  SER SER C . n 
C 1 45  GLY 45  45  45  GLY GLY C . n 
C 1 46  TYR 46  46  46  TYR TYR C . n 
C 1 47  ALA 47  47  47  ALA ALA C . n 
C 1 48  PHE 48  48  48  PHE PHE C . n 
C 1 49  THR 49  49  49  THR THR C . n 
C 1 50  LEU 50  50  50  LEU LEU C . n 
C 1 51  MET 51  51  51  MET MET C . n 
C 1 52  GLY 52  52  52  GLY GLY C . n 
C 1 53  THR 53  53  53  THR THR C . n 
C 1 54  ASN 54  54  54  ASN ASN C . n 
C 1 55  ALA 55  55  55  ALA ALA C . n 
C 1 56  PRO 56  56  56  PRO PRO C . n 
C 1 57  HIS 57  57  57  HIS HIS C . n 
C 1 58  SER 58  58  58  SER SER C . n 
C 1 59  ASP 59  59  59  ASP ASP C . n 
C 1 60  ALA 60  60  60  ALA ALA C . n 
C 1 61  LEU 61  61  61  LEU LEU C . n 
C 1 62  GLY 62  62  62  GLY GLY C . n 
C 1 63  VAL 63  63  63  VAL VAL C . n 
C 1 64  LEU 64  64  64  LEU LEU C . n 
C 1 65  PRO 65  65  65  PRO PRO C . n 
C 1 66  HIS 66  66  66  HIS HIS C . n 
C 1 67  ILE 67  67  67  ILE ILE C . n 
C 1 68  HIS 68  68  68  HIS HIS C . n 
C 1 69  GLN 69  69  69  GLN GLN C . n 
C 1 70  LYS 70  70  70  LYS LYS C . n 
C 1 71  HIS 71  71  71  HIS HIS C . n 
C 1 72  TYR 72  72  72  TYR TYR C . n 
C 1 73  GLU 73  73  73  GLU GLU C . n 
C 1 74  ASN 74  74  74  ASN ASN C . n 
C 1 75  PHE 75  75  75  PHE PHE C . n 
C 1 76  TYR 76  76  76  TYR TYR C . n 
C 1 77  CYS 77  77  77  CYS CYS C . n 
C 1 78  ASN 78  78  78  ASN ASN C . n 
C 1 79  LYS 79  79  79  LYS LYS C . n 
C 1 80  GLY 80  80  80  GLY GLY C . n 
C 1 81  SER 81  81  81  SER SER C . n 
C 1 82  PHE 82  82  82  PHE PHE C . n 
C 1 83  GLN 83  83  83  GLN GLN C . n 
C 1 84  LEU 84  84  84  LEU LEU C . n 
C 1 85  TRP 85  85  85  TRP TRP C . n 
C 1 86  ALA 86  86  86  ALA ALA C . n 
C 1 87  GLN 87  87  87  GLN GLN C . n 
C 1 88  SER 88  88  88  SER SER C . n 
C 1 89  GLY 89  89  89  GLY GLY C . n 
C 1 90  ASN 90  90  90  ASN ASN C . n 
C 1 91  GLU 91  91  91  GLU GLU C . n 
C 1 92  THR 92  92  92  THR THR C . n 
C 1 93  GLN 93  93  93  GLN GLN C . n 
C 1 94  GLN 94  94  94  GLN GLN C . n 
C 1 95  THR 95  95  95  THR THR C . n 
C 1 96  ARG 96  96  96  ARG ARG C . n 
C 1 97  VAL 97  97  97  VAL VAL C . n 
C 1 98  LEU 98  98  98  LEU LEU C . n 
C 1 99  SER 99  99  99  SER SER C . n 
C 1 100 SER 100 100 100 SER SER C . n 
C 1 101 GLY 101 101 101 GLY GLY C . n 
C 1 102 ASP 102 102 102 ASP ASP C . n 
C 1 103 TYR 103 103 103 TYR TYR C . n 
C 1 104 GLY 104 104 104 GLY GLY C . n 
C 1 105 SER 105 105 105 SER SER C . n 
C 1 106 VAL 106 106 106 VAL VAL C . n 
C 1 107 PRO 107 107 107 PRO PRO C . n 
C 1 108 ARG 108 108 108 ARG ARG C . n 
C 1 109 ASN 109 109 109 ASN ASN C . n 
C 1 110 VAL 110 110 110 VAL VAL C . n 
C 1 111 THR 111 111 111 THR THR C . n 
C 1 112 HIS 112 112 112 HIS HIS C . n 
C 1 113 THR 113 113 113 THR THR C . n 
C 1 114 PHE 114 114 114 PHE PHE C . n 
C 1 115 GLN 115 115 115 GLN GLN C . n 
C 1 116 ILE 116 116 116 ILE ILE C . n 
C 1 117 GLN 117 117 117 GLN GLN C . n 
C 1 118 ASP 118 118 118 ASP ASP C . n 
C 1 119 PRO 119 119 119 PRO PRO C . n 
C 1 120 ASP 120 120 120 ASP ASP C . n 
C 1 121 THR 121 121 121 THR THR C . n 
C 1 122 GLU 122 122 122 GLU GLU C . n 
C 1 123 MET 123 123 123 MET MET C . n 
C 1 124 THR 124 124 124 THR THR C . n 
C 1 125 GLY 125 125 125 GLY GLY C . n 
C 1 126 VAL 126 126 126 VAL VAL C . n 
C 1 127 ILE 127 127 127 ILE ILE C . n 
C 1 128 VAL 128 128 128 VAL VAL C . n 
C 1 129 PRO 129 129 129 PRO PRO C . n 
C 1 130 GLY 130 130 130 GLY GLY C . n 
C 1 131 GLY 131 131 131 GLY GLY C . n 
C 1 132 PHE 132 132 132 PHE PHE C . n 
C 1 133 GLU 133 133 133 GLU GLU C . n 
C 1 134 ASP 134 134 134 ASP ASP C . n 
C 1 135 LEU 135 135 135 LEU LEU C . n 
C 1 136 PHE 136 136 136 PHE PHE C . n 
C 1 137 TYR 137 137 137 TYR TYR C . n 
C 1 138 TYR 138 138 138 TYR TYR C . n 
C 1 139 LEU 139 139 139 LEU LEU C . n 
C 1 140 GLY 140 140 140 GLY GLY C . n 
C 1 141 THR 141 141 141 THR THR C . n 
C 1 142 ASN 142 142 142 ASN ASN C . n 
C 1 143 ALA 143 143 143 ALA ALA C . n 
C 1 144 THR 144 144 144 THR THR C . n 
C 1 145 ASP 145 145 145 ASP ASP C . n 
C 1 146 THR 146 146 146 THR THR C . n 
C 1 147 THR 147 147 147 THR THR C . n 
C 1 148 HIS 148 148 148 HIS HIS C . n 
C 1 149 THR 149 149 149 THR THR C . n 
C 1 150 PRO 150 150 150 PRO PRO C . n 
C 1 151 TYR 151 151 151 TYR TYR C . n 
C 1 152 ILE 152 152 152 ILE ILE C . n 
C 1 153 PRO 153 153 153 PRO PRO C . n 
C 1 154 SER 154 154 ?   ?   ?   C . n 
C 1 155 SER 155 155 ?   ?   ?   C . n 
C 1 156 SER 156 156 ?   ?   ?   C . n 
C 1 157 ASP 157 157 ?   ?   ?   C . n 
C 1 158 SER 158 158 ?   ?   ?   C . n 
C 1 159 SER 159 159 159 SER SER C . n 
C 1 160 SER 160 160 160 SER SER C . n 
C 1 161 THR 161 161 161 THR THR C . n 
C 1 162 THR 162 162 162 THR THR C . n 
C 1 163 GLY 163 163 163 GLY GLY C . n 
C 1 164 PRO 164 164 164 PRO PRO C . n 
C 1 165 ASP 165 165 165 ASP ASP C . n 
C 1 166 SER 166 166 166 SER SER C . n 
C 1 167 SER 167 167 167 SER SER C . n 
C 1 168 THR 168 168 168 THR THR C . n 
C 1 169 ILE 169 169 169 ILE ILE C . n 
C 1 170 SER 170 170 170 SER SER C . n 
C 1 171 THR 171 171 171 THR THR C . n 
C 1 172 LEU 172 172 172 LEU LEU C . n 
C 1 173 GLN 173 173 173 GLN GLN C . n 
C 1 174 SER 174 174 174 SER SER C . n 
C 1 175 PHE 175 175 175 PHE PHE C . n 
C 1 176 ASP 176 176 176 ASP ASP C . n 
C 1 177 VAL 177 177 177 VAL VAL C . n 
C 1 178 TYR 178 178 178 TYR TYR C . n 
C 1 179 ALA 179 179 179 ALA ALA C . n 
C 1 180 GLU 180 180 180 GLU GLU C . n 
C 1 181 LEU 181 181 181 LEU LEU C . n 
C 1 182 SER 182 182 182 SER SER C . n 
C 1 183 PHE 183 183 183 PHE PHE C . n 
C 1 184 THR 184 184 184 THR THR C . n 
C 1 185 PRO 185 185 185 PRO PRO C . n 
C 1 186 ARG 186 186 186 ARG ARG C . n 
C 1 187 THR 187 187 187 THR THR C . n 
C 1 188 ASP 188 188 188 ASP ASP C . n 
C 1 189 THR 189 189 189 THR THR C . n 
C 1 190 VAL 190 190 190 VAL VAL C . n 
C 1 191 ASN 191 191 191 ASN ASN C . n 
C 1 192 GLY 192 192 192 GLY GLY C . n 
C 1 193 THR 193 193 193 THR THR C . n 
C 1 194 ALA 194 194 194 ALA ALA C . n 
C 1 195 PRO 195 195 195 PRO PRO C . n 
C 1 196 ALA 196 196 196 ALA ALA C . n 
C 1 197 ASN 197 197 197 ASN ASN C . n 
C 1 198 THR 198 198 198 THR THR C . n 
C 1 199 VAL 199 199 199 VAL VAL C . n 
C 1 200 TRP 200 200 200 TRP TRP C . n 
C 1 201 HIS 201 201 201 HIS HIS C . n 
C 1 202 THR 202 202 202 THR THR C . n 
C 1 203 GLY 203 203 203 GLY GLY C . n 
C 1 204 ALA 204 204 204 ALA ALA C . n 
C 1 205 ASN 205 205 205 ASN ASN C . n 
C 1 206 ALA 206 206 206 ALA ALA C . n 
C 1 207 LEU 207 207 207 LEU LEU C . n 
C 1 208 ALA 208 208 208 ALA ALA C . n 
C 1 209 SER 209 209 209 SER SER C . n 
C 1 210 THR 210 210 210 THR THR C . n 
C 1 211 ALA 211 211 211 ALA ALA C . n 
C 1 212 GLY 212 212 212 GLY GLY C . n 
C 1 213 ASP 213 213 213 ASP ASP C . n 
C 1 214 PRO 214 214 214 PRO PRO C . n 
C 1 215 TYR 215 215 215 TYR TYR C . n 
C 1 216 PHE 216 216 216 PHE PHE C . n 
C 1 217 ILE 217 217 217 ILE ILE C . n 
C 1 218 ALA 218 218 218 ALA ALA C . n 
C 1 219 ASN 219 219 219 ASN ASN C . n 
C 1 220 GLY 220 220 220 GLY GLY C . n 
C 1 221 TRP 221 221 221 TRP TRP C . n 
C 1 222 GLY 222 222 222 GLY GLY C . n 
C 1 223 PRO 223 223 223 PRO PRO C . n 
C 1 224 LYS 224 224 224 LYS LYS C . n 
C 1 225 TYR 225 225 225 TYR TYR C . n 
C 1 226 LEU 226 226 226 LEU LEU C . n 
C 1 227 ASN 227 227 227 ASN ASN C . n 
C 1 228 SER 228 228 228 SER SER C . n 
C 1 229 GLN 229 229 229 GLN GLN C . n 
C 1 230 TYR 230 230 230 TYR TYR C . n 
C 1 231 GLY 231 231 231 GLY GLY C . n 
C 1 232 TYR 232 232 232 TYR TYR C . n 
C 1 233 GLN 233 233 233 GLN GLN C . n 
C 1 234 ILE 234 234 234 ILE ILE C . n 
C 1 235 VAL 235 235 235 VAL VAL C . n 
C 1 236 ALA 236 236 236 ALA ALA C . n 
C 1 237 PRO 237 237 237 PRO PRO C . n 
C 1 238 PHE 238 238 238 PHE PHE C . n 
C 1 239 VAL 239 239 239 VAL VAL C . n 
C 1 240 THR 240 240 240 THR THR C . n 
C 1 241 ALA 241 241 241 ALA ALA C . n 
C 1 242 THR 242 242 242 THR THR C . n 
C 1 243 GLN 243 243 243 GLN GLN C . n 
C 1 244 ALA 244 244 244 ALA ALA C . n 
C 1 245 GLN 245 245 245 GLN GLN C . n 
C 1 246 ASP 246 246 246 ASP ASP C . n 
C 1 247 THR 247 247 247 THR THR C . n 
C 1 248 ASN 248 248 248 ASN ASN C . n 
C 1 249 TYR 249 249 249 TYR TYR C . n 
C 1 250 THR 250 250 250 THR THR C . n 
C 1 251 LEU 251 251 251 LEU LEU C . n 
C 1 252 SER 252 252 252 SER SER C . n 
C 1 253 THR 253 253 253 THR THR C . n 
C 1 254 ILE 254 254 254 ILE ILE C . n 
C 1 255 SER 255 255 255 SER SER C . n 
C 1 256 MET 256 256 256 MET MET C . n 
C 1 257 SER 257 257 257 SER SER C . n 
C 1 258 THR 258 258 258 THR THR C . n 
C 1 259 THR 259 259 259 THR THR C . n 
C 1 260 PRO 260 260 260 PRO PRO C . n 
C 1 261 SER 261 261 261 SER SER C . n 
C 1 262 THR 262 262 262 THR THR C . n 
C 1 263 VAL 263 263 263 VAL VAL C . n 
C 1 264 THR 264 264 264 THR THR C . n 
C 1 265 VAL 265 265 265 VAL VAL C . n 
C 1 266 PRO 266 266 266 PRO PRO C . n 
C 1 267 THR 267 267 267 THR THR C . n 
C 1 268 TRP 268 268 268 TRP TRP C . n 
C 1 269 SER 269 269 269 SER SER C . n 
C 1 270 PHE 270 270 270 PHE PHE C . n 
C 1 271 PRO 271 271 271 PRO PRO C . n 
C 1 272 GLY 272 272 272 GLY GLY C . n 
C 1 273 ALA 273 273 273 ALA ALA C . n 
C 1 274 CYS 274 274 274 CYS CYS C . n 
C 1 275 ALA 275 275 275 ALA ALA C . n 
C 1 276 PHE 276 276 276 PHE PHE C . n 
C 1 277 GLN 277 277 277 GLN GLN C . n 
C 1 278 VAL 278 278 278 VAL VAL C . n 
C 1 279 GLN 279 279 279 GLN GLN C . n 
C 1 280 GLU 280 280 280 GLU GLU C . n 
C 1 281 GLY 281 281 281 GLY GLY C . n 
C 1 282 ARG 282 282 282 ARG ARG C . n 
C 1 283 VAL 283 283 283 VAL VAL C . n 
C 1 284 VAL 284 284 284 VAL VAL C . n 
C 1 285 VAL 285 285 285 VAL VAL C . n 
C 1 286 GLN 286 286 286 GLN GLN C . n 
C 1 287 ILE 287 287 287 ILE ILE C . n 
C 1 288 GLY 288 288 288 GLY GLY C . n 
C 1 289 ASP 289 289 289 ASP ASP C . n 
C 1 290 TYR 290 290 290 TYR TYR C . n 
C 1 291 ALA 291 291 291 ALA ALA C . n 
C 1 292 ALA 292 292 292 ALA ALA C . n 
C 1 293 THR 293 293 293 THR THR C . n 
C 1 294 GLU 294 294 294 GLU GLU C . n 
C 1 295 LEU 295 295 295 LEU LEU C . n 
C 1 296 GLY 296 296 296 GLY GLY C . n 
C 1 297 SER 297 297 297 SER SER C . n 
C 1 298 GLY 298 298 298 GLY GLY C . n 
C 1 299 ASP 299 299 299 ASP ASP C . n 
C 1 300 VAL 300 300 300 VAL VAL C . n 
C 1 301 ALA 301 301 301 ALA ALA C . n 
C 1 302 PHE 302 302 302 PHE PHE C . n 
C 1 303 ILE 303 303 303 ILE ILE C . n 
C 1 304 PRO 304 304 304 PRO PRO C . n 
C 1 305 GLY 305 305 305 GLY GLY C . n 
C 1 306 GLY 306 306 306 GLY GLY C . n 
C 1 307 VAL 307 307 307 VAL VAL C . n 
C 1 308 GLU 308 308 308 GLU GLU C . n 
C 1 309 PHE 309 309 309 PHE PHE C . n 
C 1 310 LYS 310 310 310 LYS LYS C . n 
C 1 311 TYR 311 311 311 TYR TYR C . n 
C 1 312 TYR 312 312 312 TYR TYR C . n 
C 1 313 SER 313 313 313 SER SER C . n 
C 1 314 GLU 314 314 314 GLU GLU C . n 
C 1 315 ALA 315 315 315 ALA ALA C . n 
C 1 316 TYR 316 316 316 TYR TYR C . n 
C 1 317 PHE 317 317 317 PHE PHE C . n 
C 1 318 SER 318 318 318 SER SER C . n 
C 1 319 LYS 319 319 319 LYS LYS C . n 
C 1 320 VAL 320 320 320 VAL VAL C . n 
C 1 321 LEU 321 321 321 LEU LEU C . n 
C 1 322 PHE 322 322 322 PHE PHE C . n 
C 1 323 VAL 323 323 323 VAL VAL C . n 
C 1 324 SER 324 324 324 SER SER C . n 
C 1 325 SER 325 325 325 SER SER C . n 
C 1 326 GLY 326 326 326 GLY GLY C . n 
C 1 327 SER 327 327 327 SER SER C . n 
C 1 328 ASP 328 328 328 ASP ASP C . n 
C 1 329 GLY 329 329 329 GLY GLY C . n 
C 1 330 LEU 330 330 330 LEU LEU C . n 
C 1 331 ASP 331 331 331 ASP ASP C . n 
C 1 332 GLN 332 332 332 GLN GLN C . n 
C 1 333 ASN 333 333 333 ASN ASN C . n 
C 1 334 LEU 334 334 334 LEU LEU C . n 
C 1 335 VAL 335 335 335 VAL VAL C . n 
C 1 336 ASN 336 336 336 ASN ASN C . n 
C 1 337 GLY 337 337 337 GLY GLY C . n 
C 1 338 GLY 338 338 338 GLY GLY C . n 
C 1 339 GLU 339 339 339 GLU GLU C . n 
C 1 340 GLU 340 340 340 GLU GLU C . n 
C 1 341 TRP 341 341 341 TRP TRP C . n 
C 1 342 SER 342 342 342 SER SER C . n 
C 1 343 SER 343 343 343 SER SER C . n 
C 1 344 VAL 344 344 344 VAL VAL C . n 
C 1 345 SER 345 345 345 SER SER C . n 
C 1 346 PHE 346 346 346 PHE PHE C . n 
C 1 347 PRO 347 347 347 PRO PRO C . n 
C 1 348 ALA 348 348 348 ALA ALA C . n 
C 1 349 ASP 349 349 349 ASP ASP C . n 
C 1 350 TRP 350 350 350 TRP TRP C . n 
D 1 1   ASP 1   1   ?   ?   ?   D . n 
D 1 2   THR 2   2   ?   ?   ?   D . n 
D 1 3   SER 3   3   ?   ?   ?   D . n 
D 1 4   SER 4   4   4   SER SER D . n 
D 1 5   LEU 5   5   5   LEU LEU D . n 
D 1 6   ILE 6   6   6   ILE ILE D . n 
D 1 7   VAL 7   7   7   VAL VAL D . n 
D 1 8   GLU 8   8   8   GLU GLU D . n 
D 1 9   ASP 9   9   9   ASP ASP D . n 
D 1 10  ALA 10  10  10  ALA ALA D . n 
D 1 11  PRO 11  11  11  PRO PRO D . n 
D 1 12  ASP 12  12  12  ASP ASP D . n 
D 1 13  HIS 13  13  13  HIS HIS D . n 
D 1 14  VAL 14  14  14  VAL VAL D . n 
D 1 15  ARG 15  15  15  ARG ARG D . n 
D 1 16  PRO 16  16  16  PRO PRO D . n 
D 1 17  TYR 17  17  17  TYR TYR D . n 
D 1 18  VAL 18  18  18  VAL VAL D . n 
D 1 19  ILE 19  19  19  ILE ILE D . n 
D 1 20  ARG 20  20  20  ARG ARG D . n 
D 1 21  HIS 21  21  21  HIS HIS D . n 
D 1 22  TYR 22  22  22  TYR TYR D . n 
D 1 23  SER 23  23  23  SER SER D . n 
D 1 24  HIS 24  24  24  HIS HIS D . n 
D 1 25  ALA 25  25  25  ALA ALA D . n 
D 1 26  ARG 26  26  26  ARG ARG D . n 
D 1 27  ALA 27  27  27  ALA ALA D . n 
D 1 28  VAL 28  28  28  VAL VAL D . n 
D 1 29  THR 29  29  29  THR THR D . n 
D 1 30  VAL 30  30  30  VAL VAL D . n 
D 1 31  ASP 31  31  31  ASP ASP D . n 
D 1 32  THR 32  32  32  THR THR D . n 
D 1 33  GLN 33  33  33  GLN GLN D . n 
D 1 34  LEU 34  34  34  LEU LEU D . n 
D 1 35  TYR 35  35  35  TYR TYR D . n 
D 1 36  ARG 36  36  36  ARG ARG D . n 
D 1 37  PHE 37  37  37  PHE PHE D . n 
D 1 38  TYR 38  38  38  TYR TYR D . n 
D 1 39  VAL 39  39  39  VAL VAL D . n 
D 1 40  THR 40  40  40  THR THR D . n 
D 1 41  GLY 41  41  41  GLY GLY D . n 
D 1 42  PRO 42  42  42  PRO PRO D . n 
D 1 43  SER 43  43  43  SER SER D . n 
D 1 44  SER 44  44  44  SER SER D . n 
D 1 45  GLY 45  45  45  GLY GLY D . n 
D 1 46  TYR 46  46  46  TYR TYR D . n 
D 1 47  ALA 47  47  47  ALA ALA D . n 
D 1 48  PHE 48  48  48  PHE PHE D . n 
D 1 49  THR 49  49  49  THR THR D . n 
D 1 50  LEU 50  50  50  LEU LEU D . n 
D 1 51  MET 51  51  51  MET MET D . n 
D 1 52  GLY 52  52  52  GLY GLY D . n 
D 1 53  THR 53  53  53  THR THR D . n 
D 1 54  ASN 54  54  54  ASN ASN D . n 
D 1 55  ALA 55  55  55  ALA ALA D . n 
D 1 56  PRO 56  56  56  PRO PRO D . n 
D 1 57  HIS 57  57  57  HIS HIS D . n 
D 1 58  SER 58  58  58  SER SER D . n 
D 1 59  ASP 59  59  59  ASP ASP D . n 
D 1 60  ALA 60  60  60  ALA ALA D . n 
D 1 61  LEU 61  61  61  LEU LEU D . n 
D 1 62  GLY 62  62  62  GLY GLY D . n 
D 1 63  VAL 63  63  63  VAL VAL D . n 
D 1 64  LEU 64  64  64  LEU LEU D . n 
D 1 65  PRO 65  65  65  PRO PRO D . n 
D 1 66  HIS 66  66  66  HIS HIS D . n 
D 1 67  ILE 67  67  67  ILE ILE D . n 
D 1 68  HIS 68  68  68  HIS HIS D . n 
D 1 69  GLN 69  69  69  GLN GLN D . n 
D 1 70  LYS 70  70  70  LYS LYS D . n 
D 1 71  HIS 71  71  71  HIS HIS D . n 
D 1 72  TYR 72  72  72  TYR TYR D . n 
D 1 73  GLU 73  73  73  GLU GLU D . n 
D 1 74  ASN 74  74  74  ASN ASN D . n 
D 1 75  PHE 75  75  75  PHE PHE D . n 
D 1 76  TYR 76  76  76  TYR TYR D . n 
D 1 77  CYS 77  77  77  CYS CYS D . n 
D 1 78  ASN 78  78  78  ASN ASN D . n 
D 1 79  LYS 79  79  79  LYS LYS D . n 
D 1 80  GLY 80  80  80  GLY GLY D . n 
D 1 81  SER 81  81  81  SER SER D . n 
D 1 82  PHE 82  82  82  PHE PHE D . n 
D 1 83  GLN 83  83  83  GLN GLN D . n 
D 1 84  LEU 84  84  84  LEU LEU D . n 
D 1 85  TRP 85  85  85  TRP TRP D . n 
D 1 86  ALA 86  86  86  ALA ALA D . n 
D 1 87  GLN 87  87  87  GLN GLN D . n 
D 1 88  SER 88  88  88  SER SER D . n 
D 1 89  GLY 89  89  89  GLY GLY D . n 
D 1 90  ASN 90  90  90  ASN ASN D . n 
D 1 91  GLU 91  91  91  GLU GLU D . n 
D 1 92  THR 92  92  92  THR THR D . n 
D 1 93  GLN 93  93  93  GLN GLN D . n 
D 1 94  GLN 94  94  94  GLN GLN D . n 
D 1 95  THR 95  95  95  THR THR D . n 
D 1 96  ARG 96  96  96  ARG ARG D . n 
D 1 97  VAL 97  97  97  VAL VAL D . n 
D 1 98  LEU 98  98  98  LEU LEU D . n 
D 1 99  SER 99  99  99  SER SER D . n 
D 1 100 SER 100 100 100 SER SER D . n 
D 1 101 GLY 101 101 101 GLY GLY D . n 
D 1 102 ASP 102 102 102 ASP ASP D . n 
D 1 103 TYR 103 103 103 TYR TYR D . n 
D 1 104 GLY 104 104 104 GLY GLY D . n 
D 1 105 SER 105 105 105 SER SER D . n 
D 1 106 VAL 106 106 106 VAL VAL D . n 
D 1 107 PRO 107 107 107 PRO PRO D . n 
D 1 108 ARG 108 108 108 ARG ARG D . n 
D 1 109 ASN 109 109 109 ASN ASN D . n 
D 1 110 VAL 110 110 110 VAL VAL D . n 
D 1 111 THR 111 111 111 THR THR D . n 
D 1 112 HIS 112 112 112 HIS HIS D . n 
D 1 113 THR 113 113 113 THR THR D . n 
D 1 114 PHE 114 114 114 PHE PHE D . n 
D 1 115 GLN 115 115 115 GLN GLN D . n 
D 1 116 ILE 116 116 116 ILE ILE D . n 
D 1 117 GLN 117 117 117 GLN GLN D . n 
D 1 118 ASP 118 118 118 ASP ASP D . n 
D 1 119 PRO 119 119 119 PRO PRO D . n 
D 1 120 ASP 120 120 120 ASP ASP D . n 
D 1 121 THR 121 121 121 THR THR D . n 
D 1 122 GLU 122 122 122 GLU GLU D . n 
D 1 123 MET 123 123 123 MET MET D . n 
D 1 124 THR 124 124 124 THR THR D . n 
D 1 125 GLY 125 125 125 GLY GLY D . n 
D 1 126 VAL 126 126 126 VAL VAL D . n 
D 1 127 ILE 127 127 127 ILE ILE D . n 
D 1 128 VAL 128 128 128 VAL VAL D . n 
D 1 129 PRO 129 129 129 PRO PRO D . n 
D 1 130 GLY 130 130 130 GLY GLY D . n 
D 1 131 GLY 131 131 131 GLY GLY D . n 
D 1 132 PHE 132 132 132 PHE PHE D . n 
D 1 133 GLU 133 133 133 GLU GLU D . n 
D 1 134 ASP 134 134 134 ASP ASP D . n 
D 1 135 LEU 135 135 135 LEU LEU D . n 
D 1 136 PHE 136 136 136 PHE PHE D . n 
D 1 137 TYR 137 137 137 TYR TYR D . n 
D 1 138 TYR 138 138 138 TYR TYR D . n 
D 1 139 LEU 139 139 139 LEU LEU D . n 
D 1 140 GLY 140 140 140 GLY GLY D . n 
D 1 141 THR 141 141 141 THR THR D . n 
D 1 142 ASN 142 142 142 ASN ASN D . n 
D 1 143 ALA 143 143 143 ALA ALA D . n 
D 1 144 THR 144 144 144 THR THR D . n 
D 1 145 ASP 145 145 145 ASP ASP D . n 
D 1 146 THR 146 146 146 THR THR D . n 
D 1 147 THR 147 147 147 THR THR D . n 
D 1 148 HIS 148 148 148 HIS HIS D . n 
D 1 149 THR 149 149 149 THR THR D . n 
D 1 150 PRO 150 150 150 PRO PRO D . n 
D 1 151 TYR 151 151 151 TYR TYR D . n 
D 1 152 ILE 152 152 152 ILE ILE D . n 
D 1 153 PRO 153 153 153 PRO PRO D . n 
D 1 154 SER 154 154 154 SER SER D . n 
D 1 155 SER 155 155 ?   ?   ?   D . n 
D 1 156 SER 156 156 ?   ?   ?   D . n 
D 1 157 ASP 157 157 ?   ?   ?   D . n 
D 1 158 SER 158 158 ?   ?   ?   D . n 
D 1 159 SER 159 159 159 SER SER D . n 
D 1 160 SER 160 160 160 SER SER D . n 
D 1 161 THR 161 161 161 THR THR D . n 
D 1 162 THR 162 162 162 THR THR D . n 
D 1 163 GLY 163 163 163 GLY GLY D . n 
D 1 164 PRO 164 164 164 PRO PRO D . n 
D 1 165 ASP 165 165 165 ASP ASP D . n 
D 1 166 SER 166 166 166 SER SER D . n 
D 1 167 SER 167 167 167 SER SER D . n 
D 1 168 THR 168 168 168 THR THR D . n 
D 1 169 ILE 169 169 169 ILE ILE D . n 
D 1 170 SER 170 170 170 SER SER D . n 
D 1 171 THR 171 171 171 THR THR D . n 
D 1 172 LEU 172 172 172 LEU LEU D . n 
D 1 173 GLN 173 173 173 GLN GLN D . n 
D 1 174 SER 174 174 174 SER SER D . n 
D 1 175 PHE 175 175 175 PHE PHE D . n 
D 1 176 ASP 176 176 176 ASP ASP D . n 
D 1 177 VAL 177 177 177 VAL VAL D . n 
D 1 178 TYR 178 178 178 TYR TYR D . n 
D 1 179 ALA 179 179 179 ALA ALA D . n 
D 1 180 GLU 180 180 180 GLU GLU D . n 
D 1 181 LEU 181 181 181 LEU LEU D . n 
D 1 182 SER 182 182 182 SER SER D . n 
D 1 183 PHE 183 183 183 PHE PHE D . n 
D 1 184 THR 184 184 184 THR THR D . n 
D 1 185 PRO 185 185 185 PRO PRO D . n 
D 1 186 ARG 186 186 186 ARG ARG D . n 
D 1 187 THR 187 187 187 THR THR D . n 
D 1 188 ASP 188 188 188 ASP ASP D . n 
D 1 189 THR 189 189 189 THR THR D . n 
D 1 190 VAL 190 190 190 VAL VAL D . n 
D 1 191 ASN 191 191 191 ASN ASN D . n 
D 1 192 GLY 192 192 192 GLY GLY D . n 
D 1 193 THR 193 193 193 THR THR D . n 
D 1 194 ALA 194 194 194 ALA ALA D . n 
D 1 195 PRO 195 195 195 PRO PRO D . n 
D 1 196 ALA 196 196 196 ALA ALA D . n 
D 1 197 ASN 197 197 197 ASN ASN D . n 
D 1 198 THR 198 198 198 THR THR D . n 
D 1 199 VAL 199 199 199 VAL VAL D . n 
D 1 200 TRP 200 200 200 TRP TRP D . n 
D 1 201 HIS 201 201 201 HIS HIS D . n 
D 1 202 THR 202 202 202 THR THR D . n 
D 1 203 GLY 203 203 203 GLY GLY D . n 
D 1 204 ALA 204 204 204 ALA ALA D . n 
D 1 205 ASN 205 205 205 ASN ASN D . n 
D 1 206 ALA 206 206 206 ALA ALA D . n 
D 1 207 LEU 207 207 207 LEU LEU D . n 
D 1 208 ALA 208 208 208 ALA ALA D . n 
D 1 209 SER 209 209 209 SER SER D . n 
D 1 210 THR 210 210 210 THR THR D . n 
D 1 211 ALA 211 211 211 ALA ALA D . n 
D 1 212 GLY 212 212 212 GLY GLY D . n 
D 1 213 ASP 213 213 213 ASP ASP D . n 
D 1 214 PRO 214 214 214 PRO PRO D . n 
D 1 215 TYR 215 215 215 TYR TYR D . n 
D 1 216 PHE 216 216 216 PHE PHE D . n 
D 1 217 ILE 217 217 217 ILE ILE D . n 
D 1 218 ALA 218 218 218 ALA ALA D . n 
D 1 219 ASN 219 219 219 ASN ASN D . n 
D 1 220 GLY 220 220 220 GLY GLY D . n 
D 1 221 TRP 221 221 221 TRP TRP D . n 
D 1 222 GLY 222 222 222 GLY GLY D . n 
D 1 223 PRO 223 223 223 PRO PRO D . n 
D 1 224 LYS 224 224 224 LYS LYS D . n 
D 1 225 TYR 225 225 225 TYR TYR D . n 
D 1 226 LEU 226 226 226 LEU LEU D . n 
D 1 227 ASN 227 227 227 ASN ASN D . n 
D 1 228 SER 228 228 228 SER SER D . n 
D 1 229 GLN 229 229 229 GLN GLN D . n 
D 1 230 TYR 230 230 230 TYR TYR D . n 
D 1 231 GLY 231 231 231 GLY GLY D . n 
D 1 232 TYR 232 232 232 TYR TYR D . n 
D 1 233 GLN 233 233 233 GLN GLN D . n 
D 1 234 ILE 234 234 234 ILE ILE D . n 
D 1 235 VAL 235 235 235 VAL VAL D . n 
D 1 236 ALA 236 236 236 ALA ALA D . n 
D 1 237 PRO 237 237 237 PRO PRO D . n 
D 1 238 PHE 238 238 238 PHE PHE D . n 
D 1 239 VAL 239 239 239 VAL VAL D . n 
D 1 240 THR 240 240 240 THR THR D . n 
D 1 241 ALA 241 241 241 ALA ALA D . n 
D 1 242 THR 242 242 242 THR THR D . n 
D 1 243 GLN 243 243 243 GLN GLN D . n 
D 1 244 ALA 244 244 244 ALA ALA D . n 
D 1 245 GLN 245 245 245 GLN GLN D . n 
D 1 246 ASP 246 246 246 ASP ASP D . n 
D 1 247 THR 247 247 247 THR THR D . n 
D 1 248 ASN 248 248 248 ASN ASN D . n 
D 1 249 TYR 249 249 249 TYR TYR D . n 
D 1 250 THR 250 250 250 THR THR D . n 
D 1 251 LEU 251 251 251 LEU LEU D . n 
D 1 252 SER 252 252 252 SER SER D . n 
D 1 253 THR 253 253 253 THR THR D . n 
D 1 254 ILE 254 254 254 ILE ILE D . n 
D 1 255 SER 255 255 255 SER SER D . n 
D 1 256 MET 256 256 256 MET MET D . n 
D 1 257 SER 257 257 257 SER SER D . n 
D 1 258 THR 258 258 258 THR THR D . n 
D 1 259 THR 259 259 259 THR THR D . n 
D 1 260 PRO 260 260 260 PRO PRO D . n 
D 1 261 SER 261 261 261 SER SER D . n 
D 1 262 THR 262 262 262 THR THR D . n 
D 1 263 VAL 263 263 263 VAL VAL D . n 
D 1 264 THR 264 264 264 THR THR D . n 
D 1 265 VAL 265 265 265 VAL VAL D . n 
D 1 266 PRO 266 266 266 PRO PRO D . n 
D 1 267 THR 267 267 267 THR THR D . n 
D 1 268 TRP 268 268 268 TRP TRP D . n 
D 1 269 SER 269 269 269 SER SER D . n 
D 1 270 PHE 270 270 270 PHE PHE D . n 
D 1 271 PRO 271 271 271 PRO PRO D . n 
D 1 272 GLY 272 272 272 GLY GLY D . n 
D 1 273 ALA 273 273 273 ALA ALA D . n 
D 1 274 CYS 274 274 274 CYS CYS D . n 
D 1 275 ALA 275 275 275 ALA ALA D . n 
D 1 276 PHE 276 276 276 PHE PHE D . n 
D 1 277 GLN 277 277 277 GLN GLN D . n 
D 1 278 VAL 278 278 278 VAL VAL D . n 
D 1 279 GLN 279 279 279 GLN GLN D . n 
D 1 280 GLU 280 280 280 GLU GLU D . n 
D 1 281 GLY 281 281 281 GLY GLY D . n 
D 1 282 ARG 282 282 282 ARG ARG D . n 
D 1 283 VAL 283 283 283 VAL VAL D . n 
D 1 284 VAL 284 284 284 VAL VAL D . n 
D 1 285 VAL 285 285 285 VAL VAL D . n 
D 1 286 GLN 286 286 286 GLN GLN D . n 
D 1 287 ILE 287 287 287 ILE ILE D . n 
D 1 288 GLY 288 288 288 GLY GLY D . n 
D 1 289 ASP 289 289 289 ASP ASP D . n 
D 1 290 TYR 290 290 290 TYR TYR D . n 
D 1 291 ALA 291 291 291 ALA ALA D . n 
D 1 292 ALA 292 292 292 ALA ALA D . n 
D 1 293 THR 293 293 293 THR THR D . n 
D 1 294 GLU 294 294 294 GLU GLU D . n 
D 1 295 LEU 295 295 295 LEU LEU D . n 
D 1 296 GLY 296 296 296 GLY GLY D . n 
D 1 297 SER 297 297 297 SER SER D . n 
D 1 298 GLY 298 298 298 GLY GLY D . n 
D 1 299 ASP 299 299 299 ASP ASP D . n 
D 1 300 VAL 300 300 300 VAL VAL D . n 
D 1 301 ALA 301 301 301 ALA ALA D . n 
D 1 302 PHE 302 302 302 PHE PHE D . n 
D 1 303 ILE 303 303 303 ILE ILE D . n 
D 1 304 PRO 304 304 304 PRO PRO D . n 
D 1 305 GLY 305 305 305 GLY GLY D . n 
D 1 306 GLY 306 306 306 GLY GLY D . n 
D 1 307 VAL 307 307 307 VAL VAL D . n 
D 1 308 GLU 308 308 308 GLU GLU D . n 
D 1 309 PHE 309 309 309 PHE PHE D . n 
D 1 310 LYS 310 310 310 LYS LYS D . n 
D 1 311 TYR 311 311 311 TYR TYR D . n 
D 1 312 TYR 312 312 312 TYR TYR D . n 
D 1 313 SER 313 313 313 SER SER D . n 
D 1 314 GLU 314 314 314 GLU GLU D . n 
D 1 315 ALA 315 315 315 ALA ALA D . n 
D 1 316 TYR 316 316 316 TYR TYR D . n 
D 1 317 PHE 317 317 317 PHE PHE D . n 
D 1 318 SER 318 318 318 SER SER D . n 
D 1 319 LYS 319 319 319 LYS LYS D . n 
D 1 320 VAL 320 320 320 VAL VAL D . n 
D 1 321 LEU 321 321 321 LEU LEU D . n 
D 1 322 PHE 322 322 322 PHE PHE D . n 
D 1 323 VAL 323 323 323 VAL VAL D . n 
D 1 324 SER 324 324 324 SER SER D . n 
D 1 325 SER 325 325 325 SER SER D . n 
D 1 326 GLY 326 326 326 GLY GLY D . n 
D 1 327 SER 327 327 327 SER SER D . n 
D 1 328 ASP 328 328 328 ASP ASP D . n 
D 1 329 GLY 329 329 329 GLY GLY D . n 
D 1 330 LEU 330 330 330 LEU LEU D . n 
D 1 331 ASP 331 331 331 ASP ASP D . n 
D 1 332 GLN 332 332 332 GLN GLN D . n 
D 1 333 ASN 333 333 333 ASN ASN D . n 
D 1 334 LEU 334 334 334 LEU LEU D . n 
D 1 335 VAL 335 335 335 VAL VAL D . n 
D 1 336 ASN 336 336 336 ASN ASN D . n 
D 1 337 GLY 337 337 337 GLY GLY D . n 
D 1 338 GLY 338 338 338 GLY GLY D . n 
D 1 339 GLU 339 339 339 GLU GLU D . n 
D 1 340 GLU 340 340 340 GLU GLU D . n 
D 1 341 TRP 341 341 341 TRP TRP D . n 
D 1 342 SER 342 342 342 SER SER D . n 
D 1 343 SER 343 343 343 SER SER D . n 
D 1 344 VAL 344 344 344 VAL VAL D . n 
D 1 345 SER 345 345 345 SER SER D . n 
D 1 346 PHE 346 346 346 PHE PHE D . n 
D 1 347 PRO 347 347 347 PRO PRO D . n 
D 1 348 ALA 348 348 348 ALA ALA D . n 
D 1 349 ASP 349 349 349 ASP ASP D . n 
D 1 350 TRP 350 350 350 TRP TRP D . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
E  2 NAG 1   1351 1351 NAG NAG A . 
F  2 NAG 1   1352 1352 NAG NAG A . 
G  2 NAG 2   1353 1353 NAG NAG A . 
H  3 BMA 3   1357 1357 BMA BMA A . 
I  4 MAN 4   1358 1358 MAN MAN A . 
J  4 MAN 5   1359 1359 MAN MAN A . 
K  2 NAG 1   1354 1354 NAG NAG A . 
L  2 NAG 1   1355 1355 NAG NAG A . 
M  2 NAG 1   1356 1356 NAG NAG A . 
N  5 KMP 1   1360 1360 KMP KMP A . 
O  6 CU  1   1361 1361 CU  CU  A . 
P  7 MPD 1   1362 1362 MPD MPD A . 
Q  2 NAG 1   1351 1351 NAG NAG B . 
R  2 NAG 1   1352 1352 NAG NAG B . 
S  2 NAG 2   1353 1353 NAG NAG B . 
T  3 BMA 3   1356 1356 BMA BMA B . 
U  4 MAN 4   1357 1357 MAN MAN B . 
V  2 NAG 1   1354 1354 NAG NAG B . 
W  2 NAG 1   1355 1355 NAG NAG B . 
X  5 KMP 1   1358 1358 KMP KMP B . 
Y  6 CU  1   1359 1359 CU  CU  B . 
Z  7 MPD 1   1360 1360 MPD MPD B . 
AA 7 MPD 1   1361 1361 MPD MPD B . 
BA 2 NAG 1   1351 1351 NAG NAG C . 
CA 2 NAG 1   1352 1352 NAG NAG C . 
DA 2 NAG 2   1353 1353 NAG NAG C . 
EA 3 BMA 3   1356 1356 BMA BMA C . 
FA 4 MAN 4   1357 1357 MAN MAN C . 
GA 2 NAG 1   1354 1354 NAG NAG C . 
HA 2 NAG 1   1355 1355 NAG NAG C . 
IA 5 KMP 1   1358 1358 KMP KMP C . 
JA 6 CU  1   1359 1359 CU  CU  C . 
KA 7 MPD 1   1360 1360 MPD MPD C . 
LA 2 NAG 1   1351 1351 NAG NAG D . 
MA 2 NAG 1   1352 1352 NAG NAG D . 
NA 2 NAG 2   1353 1353 NAG NAG D . 
OA 2 NAG 1   1354 1354 NAG NAG D . 
PA 2 NAG 1   1355 1355 NAG NAG D . 
QA 5 KMP 1   1356 1356 KMP KMP D . 
RA 6 CU  1   1357 1357 CU  CU  D . 
SA 8 HOH 1   2001 2001 HOH HOH A . 
SA 8 HOH 2   2002 2002 HOH HOH A . 
SA 8 HOH 3   2003 2003 HOH HOH A . 
SA 8 HOH 4   2004 2004 HOH HOH A . 
SA 8 HOH 5   2005 2005 HOH HOH A . 
SA 8 HOH 6   2006 2006 HOH HOH A . 
SA 8 HOH 7   2007 2007 HOH HOH A . 
SA 8 HOH 8   2008 2008 HOH HOH A . 
SA 8 HOH 9   2009 2009 HOH HOH A . 
SA 8 HOH 10  2010 2010 HOH HOH A . 
SA 8 HOH 11  2011 2011 HOH HOH A . 
SA 8 HOH 12  2012 2012 HOH HOH A . 
SA 8 HOH 13  2013 2013 HOH HOH A . 
SA 8 HOH 14  2014 2014 HOH HOH A . 
SA 8 HOH 15  2015 2015 HOH HOH A . 
SA 8 HOH 16  2016 2016 HOH HOH A . 
SA 8 HOH 17  2017 2017 HOH HOH A . 
SA 8 HOH 18  2018 2018 HOH HOH A . 
SA 8 HOH 19  2019 2019 HOH HOH A . 
SA 8 HOH 20  2020 2020 HOH HOH A . 
SA 8 HOH 21  2021 2021 HOH HOH A . 
SA 8 HOH 22  2022 2022 HOH HOH A . 
SA 8 HOH 23  2023 2023 HOH HOH A . 
SA 8 HOH 24  2024 2024 HOH HOH A . 
SA 8 HOH 25  2025 2025 HOH HOH A . 
SA 8 HOH 26  2026 2026 HOH HOH A . 
SA 8 HOH 27  2027 2027 HOH HOH A . 
SA 8 HOH 28  2028 2028 HOH HOH A . 
SA 8 HOH 29  2029 2029 HOH HOH A . 
SA 8 HOH 30  2030 2030 HOH HOH A . 
SA 8 HOH 31  2031 2031 HOH HOH A . 
SA 8 HOH 32  2032 2032 HOH HOH A . 
SA 8 HOH 33  2033 2033 HOH HOH A . 
SA 8 HOH 34  2034 2034 HOH HOH A . 
SA 8 HOH 35  2035 2035 HOH HOH A . 
SA 8 HOH 36  2036 2036 HOH HOH A . 
SA 8 HOH 37  2037 2037 HOH HOH A . 
SA 8 HOH 38  2038 2038 HOH HOH A . 
SA 8 HOH 39  2039 2039 HOH HOH A . 
SA 8 HOH 40  2040 2040 HOH HOH A . 
SA 8 HOH 41  2041 2041 HOH HOH A . 
SA 8 HOH 42  2042 2042 HOH HOH A . 
SA 8 HOH 43  2043 2043 HOH HOH A . 
SA 8 HOH 44  2044 2044 HOH HOH A . 
SA 8 HOH 45  2045 2045 HOH HOH A . 
SA 8 HOH 46  2046 2046 HOH HOH A . 
SA 8 HOH 47  2047 2047 HOH HOH A . 
SA 8 HOH 48  2048 2048 HOH HOH A . 
SA 8 HOH 49  2049 2049 HOH HOH A . 
SA 8 HOH 50  2050 2050 HOH HOH A . 
SA 8 HOH 51  2051 2051 HOH HOH A . 
SA 8 HOH 52  2052 2052 HOH HOH A . 
SA 8 HOH 53  2053 2053 HOH HOH A . 
SA 8 HOH 54  2054 2054 HOH HOH A . 
SA 8 HOH 55  2055 2055 HOH HOH A . 
SA 8 HOH 56  2056 2056 HOH HOH A . 
SA 8 HOH 57  2057 2057 HOH HOH A . 
SA 8 HOH 58  2058 2058 HOH HOH A . 
SA 8 HOH 59  2059 2059 HOH HOH A . 
SA 8 HOH 60  2060 2060 HOH HOH A . 
SA 8 HOH 61  2061 2061 HOH HOH A . 
SA 8 HOH 62  2062 2062 HOH HOH A . 
SA 8 HOH 63  2063 2063 HOH HOH A . 
SA 8 HOH 64  2064 2064 HOH HOH A . 
SA 8 HOH 65  2065 2065 HOH HOH A . 
SA 8 HOH 66  2066 2066 HOH HOH A . 
SA 8 HOH 67  2067 2067 HOH HOH A . 
SA 8 HOH 68  2068 2068 HOH HOH A . 
SA 8 HOH 69  2069 2069 HOH HOH A . 
SA 8 HOH 70  2070 2070 HOH HOH A . 
SA 8 HOH 71  2071 2071 HOH HOH A . 
SA 8 HOH 72  2072 2072 HOH HOH A . 
SA 8 HOH 73  2073 2073 HOH HOH A . 
SA 8 HOH 74  2074 2074 HOH HOH A . 
SA 8 HOH 75  2075 2075 HOH HOH A . 
SA 8 HOH 76  2076 2076 HOH HOH A . 
SA 8 HOH 77  2077 2077 HOH HOH A . 
SA 8 HOH 78  2078 2078 HOH HOH A . 
SA 8 HOH 79  2079 2079 HOH HOH A . 
SA 8 HOH 80  2080 2080 HOH HOH A . 
SA 8 HOH 81  2081 2081 HOH HOH A . 
SA 8 HOH 82  2082 2082 HOH HOH A . 
SA 8 HOH 83  2083 2083 HOH HOH A . 
SA 8 HOH 84  2084 2084 HOH HOH A . 
SA 8 HOH 85  2085 2085 HOH HOH A . 
SA 8 HOH 86  2086 2086 HOH HOH A . 
SA 8 HOH 87  2087 2087 HOH HOH A . 
SA 8 HOH 88  2088 2088 HOH HOH A . 
SA 8 HOH 89  2089 2089 HOH HOH A . 
SA 8 HOH 90  2090 2090 HOH HOH A . 
SA 8 HOH 91  2091 2091 HOH HOH A . 
SA 8 HOH 92  2092 2092 HOH HOH A . 
SA 8 HOH 93  2093 2093 HOH HOH A . 
SA 8 HOH 94  2094 2094 HOH HOH A . 
SA 8 HOH 95  2095 2095 HOH HOH A . 
SA 8 HOH 96  2096 2096 HOH HOH A . 
SA 8 HOH 97  2097 2097 HOH HOH A . 
SA 8 HOH 98  2098 2098 HOH HOH A . 
SA 8 HOH 99  2099 2099 HOH HOH A . 
SA 8 HOH 100 2100 2100 HOH HOH A . 
SA 8 HOH 101 2101 2101 HOH HOH A . 
SA 8 HOH 102 2102 2102 HOH HOH A . 
SA 8 HOH 103 2103 2103 HOH HOH A . 
SA 8 HOH 104 2104 2104 HOH HOH A . 
SA 8 HOH 105 2105 2105 HOH HOH A . 
SA 8 HOH 106 2106 2106 HOH HOH A . 
SA 8 HOH 107 2107 2107 HOH HOH A . 
SA 8 HOH 108 2108 2108 HOH HOH A . 
SA 8 HOH 109 2109 2109 HOH HOH A . 
SA 8 HOH 110 2110 2110 HOH HOH A . 
SA 8 HOH 111 2111 2111 HOH HOH A . 
SA 8 HOH 112 2112 2112 HOH HOH A . 
SA 8 HOH 113 2113 2113 HOH HOH A . 
SA 8 HOH 114 2114 2114 HOH HOH A . 
SA 8 HOH 115 2115 2115 HOH HOH A . 
SA 8 HOH 116 2116 2116 HOH HOH A . 
SA 8 HOH 117 2117 2117 HOH HOH A . 
SA 8 HOH 118 2118 2118 HOH HOH A . 
SA 8 HOH 119 2119 2119 HOH HOH A . 
SA 8 HOH 120 2120 2120 HOH HOH A . 
SA 8 HOH 121 2121 2121 HOH HOH A . 
SA 8 HOH 122 2122 2122 HOH HOH A . 
SA 8 HOH 123 2123 2123 HOH HOH A . 
SA 8 HOH 124 2124 2124 HOH HOH A . 
SA 8 HOH 125 2125 2125 HOH HOH A . 
SA 8 HOH 126 2126 2126 HOH HOH A . 
SA 8 HOH 127 2127 2127 HOH HOH A . 
SA 8 HOH 128 2128 2128 HOH HOH A . 
SA 8 HOH 129 2129 2129 HOH HOH A . 
SA 8 HOH 130 2130 2130 HOH HOH A . 
SA 8 HOH 131 2131 2131 HOH HOH A . 
SA 8 HOH 132 2132 2132 HOH HOH A . 
SA 8 HOH 133 2133 2133 HOH HOH A . 
SA 8 HOH 134 2134 2134 HOH HOH A . 
SA 8 HOH 135 2135 2135 HOH HOH A . 
SA 8 HOH 136 2136 2136 HOH HOH A . 
SA 8 HOH 137 2137 2137 HOH HOH A . 
SA 8 HOH 138 2138 2138 HOH HOH A . 
SA 8 HOH 139 2139 2139 HOH HOH A . 
SA 8 HOH 140 2140 2140 HOH HOH A . 
SA 8 HOH 141 2141 2141 HOH HOH A . 
SA 8 HOH 142 2142 2142 HOH HOH A . 
SA 8 HOH 143 2143 2143 HOH HOH A . 
SA 8 HOH 144 2144 2144 HOH HOH A . 
SA 8 HOH 145 2145 2145 HOH HOH A . 
SA 8 HOH 146 2146 2146 HOH HOH A . 
SA 8 HOH 147 2147 2147 HOH HOH A . 
SA 8 HOH 148 2148 2148 HOH HOH A . 
SA 8 HOH 149 2149 2149 HOH HOH A . 
SA 8 HOH 150 2150 2150 HOH HOH A . 
SA 8 HOH 151 2151 2151 HOH HOH A . 
SA 8 HOH 152 2152 2152 HOH HOH A . 
SA 8 HOH 153 2153 2153 HOH HOH A . 
SA 8 HOH 154 2154 2154 HOH HOH A . 
SA 8 HOH 155 2155 2155 HOH HOH A . 
SA 8 HOH 156 2156 2156 HOH HOH A . 
SA 8 HOH 157 2157 2157 HOH HOH A . 
SA 8 HOH 158 2158 2158 HOH HOH A . 
SA 8 HOH 159 2159 2159 HOH HOH A . 
SA 8 HOH 160 2160 2160 HOH HOH A . 
SA 8 HOH 161 2161 2161 HOH HOH A . 
SA 8 HOH 162 2162 2162 HOH HOH A . 
SA 8 HOH 163 2163 2163 HOH HOH A . 
SA 8 HOH 164 2164 2164 HOH HOH A . 
SA 8 HOH 165 2165 2165 HOH HOH A . 
SA 8 HOH 166 2166 2166 HOH HOH A . 
SA 8 HOH 167 2167 2167 HOH HOH A . 
SA 8 HOH 168 2168 2168 HOH HOH A . 
SA 8 HOH 169 2169 2169 HOH HOH A . 
SA 8 HOH 170 2170 2170 HOH HOH A . 
SA 8 HOH 171 2171 2171 HOH HOH A . 
SA 8 HOH 172 2172 2172 HOH HOH A . 
SA 8 HOH 173 2173 2173 HOH HOH A . 
SA 8 HOH 174 2174 2174 HOH HOH A . 
SA 8 HOH 175 2175 2175 HOH HOH A . 
SA 8 HOH 176 2176 2176 HOH HOH A . 
SA 8 HOH 177 2177 2177 HOH HOH A . 
SA 8 HOH 178 2178 2178 HOH HOH A . 
SA 8 HOH 179 2179 2179 HOH HOH A . 
SA 8 HOH 180 2180 2180 HOH HOH A . 
SA 8 HOH 181 2181 2181 HOH HOH A . 
SA 8 HOH 182 2182 2182 HOH HOH A . 
SA 8 HOH 183 2183 2183 HOH HOH A . 
SA 8 HOH 184 2184 2184 HOH HOH A . 
SA 8 HOH 185 2185 2185 HOH HOH A . 
SA 8 HOH 186 2186 2186 HOH HOH A . 
SA 8 HOH 187 2187 2187 HOH HOH A . 
SA 8 HOH 188 2188 2188 HOH HOH A . 
SA 8 HOH 189 2189 2189 HOH HOH A . 
SA 8 HOH 190 2190 2190 HOH HOH A . 
SA 8 HOH 191 2191 2191 HOH HOH A . 
SA 8 HOH 192 2192 2192 HOH HOH A . 
SA 8 HOH 193 2193 2193 HOH HOH A . 
SA 8 HOH 194 2194 2194 HOH HOH A . 
SA 8 HOH 195 2195 2195 HOH HOH A . 
SA 8 HOH 196 2196 2196 HOH HOH A . 
SA 8 HOH 197 2197 2197 HOH HOH A . 
SA 8 HOH 198 2198 2198 HOH HOH A . 
SA 8 HOH 199 2199 2199 HOH HOH A . 
SA 8 HOH 200 2200 2200 HOH HOH A . 
SA 8 HOH 201 2201 2201 HOH HOH A . 
SA 8 HOH 202 2202 2202 HOH HOH A . 
SA 8 HOH 203 2203 2203 HOH HOH A . 
SA 8 HOH 204 2204 2204 HOH HOH A . 
SA 8 HOH 205 2205 2205 HOH HOH A . 
SA 8 HOH 206 2206 2206 HOH HOH A . 
SA 8 HOH 207 2207 2207 HOH HOH A . 
SA 8 HOH 208 2208 2208 HOH HOH A . 
SA 8 HOH 209 2209 2209 HOH HOH A . 
SA 8 HOH 210 2210 2210 HOH HOH A . 
SA 8 HOH 211 2211 2211 HOH HOH A . 
SA 8 HOH 212 2212 2212 HOH HOH A . 
SA 8 HOH 213 2213 2213 HOH HOH A . 
SA 8 HOH 214 2214 2214 HOH HOH A . 
SA 8 HOH 215 2215 2215 HOH HOH A . 
SA 8 HOH 216 2216 2216 HOH HOH A . 
SA 8 HOH 217 2217 2217 HOH HOH A . 
SA 8 HOH 218 2218 2218 HOH HOH A . 
SA 8 HOH 219 2219 2219 HOH HOH A . 
SA 8 HOH 220 2220 2220 HOH HOH A . 
SA 8 HOH 221 2221 2221 HOH HOH A . 
SA 8 HOH 222 2222 2222 HOH HOH A . 
SA 8 HOH 223 2223 2223 HOH HOH A . 
SA 8 HOH 224 2224 2224 HOH HOH A . 
SA 8 HOH 225 2225 2225 HOH HOH A . 
SA 8 HOH 226 2226 2226 HOH HOH A . 
SA 8 HOH 227 2227 2227 HOH HOH A . 
SA 8 HOH 228 2228 2228 HOH HOH A . 
SA 8 HOH 229 2229 2229 HOH HOH A . 
SA 8 HOH 230 2230 2230 HOH HOH A . 
SA 8 HOH 231 2231 2231 HOH HOH A . 
SA 8 HOH 232 2232 2232 HOH HOH A . 
SA 8 HOH 233 2233 2233 HOH HOH A . 
SA 8 HOH 234 2234 2234 HOH HOH A . 
SA 8 HOH 235 2235 2235 HOH HOH A . 
SA 8 HOH 236 2236 2236 HOH HOH A . 
SA 8 HOH 237 2237 2237 HOH HOH A . 
SA 8 HOH 238 2238 2238 HOH HOH A . 
SA 8 HOH 239 2239 2239 HOH HOH A . 
SA 8 HOH 240 2240 2240 HOH HOH A . 
SA 8 HOH 241 2241 2241 HOH HOH A . 
SA 8 HOH 242 2242 2242 HOH HOH A . 
SA 8 HOH 243 2243 2243 HOH HOH A . 
SA 8 HOH 244 2244 2244 HOH HOH A . 
SA 8 HOH 245 2245 2245 HOH HOH A . 
SA 8 HOH 246 2246 2246 HOH HOH A . 
SA 8 HOH 247 2247 2247 HOH HOH A . 
SA 8 HOH 248 2248 2248 HOH HOH A . 
SA 8 HOH 249 2249 2249 HOH HOH A . 
SA 8 HOH 250 2250 2250 HOH HOH A . 
SA 8 HOH 251 2251 2251 HOH HOH A . 
SA 8 HOH 252 2252 2252 HOH HOH A . 
SA 8 HOH 253 2253 2253 HOH HOH A . 
SA 8 HOH 254 2254 2254 HOH HOH A . 
SA 8 HOH 255 2255 2255 HOH HOH A . 
SA 8 HOH 256 2256 2256 HOH HOH A . 
SA 8 HOH 257 2257 2257 HOH HOH A . 
SA 8 HOH 258 2258 2258 HOH HOH A . 
SA 8 HOH 259 2259 2259 HOH HOH A . 
SA 8 HOH 260 2260 2260 HOH HOH A . 
SA 8 HOH 261 2261 2261 HOH HOH A . 
SA 8 HOH 262 2262 2262 HOH HOH A . 
SA 8 HOH 263 2263 2263 HOH HOH A . 
SA 8 HOH 264 2264 2264 HOH HOH A . 
SA 8 HOH 265 2265 2265 HOH HOH A . 
SA 8 HOH 266 2266 2266 HOH HOH A . 
SA 8 HOH 267 2267 2267 HOH HOH A . 
SA 8 HOH 268 2268 2268 HOH HOH A . 
SA 8 HOH 269 2269 2269 HOH HOH A . 
SA 8 HOH 270 2270 2270 HOH HOH A . 
SA 8 HOH 271 2271 2271 HOH HOH A . 
SA 8 HOH 272 2272 2272 HOH HOH A . 
SA 8 HOH 273 2273 2273 HOH HOH A . 
SA 8 HOH 274 2274 2274 HOH HOH A . 
SA 8 HOH 275 2275 2275 HOH HOH A . 
SA 8 HOH 276 2276 2276 HOH HOH A . 
SA 8 HOH 277 2277 2277 HOH HOH A . 
SA 8 HOH 278 2278 2278 HOH HOH A . 
SA 8 HOH 279 2279 2279 HOH HOH A . 
SA 8 HOH 280 2280 2280 HOH HOH A . 
SA 8 HOH 281 2281 2281 HOH HOH A . 
SA 8 HOH 282 2282 2282 HOH HOH A . 
SA 8 HOH 283 2283 2283 HOH HOH A . 
SA 8 HOH 284 2284 2284 HOH HOH A . 
SA 8 HOH 285 2285 2285 HOH HOH A . 
SA 8 HOH 286 2286 2286 HOH HOH A . 
SA 8 HOH 287 2287 2287 HOH HOH A . 
SA 8 HOH 288 2288 2288 HOH HOH A . 
SA 8 HOH 289 2289 2289 HOH HOH A . 
SA 8 HOH 290 2290 2290 HOH HOH A . 
SA 8 HOH 291 2291 2291 HOH HOH A . 
SA 8 HOH 292 2292 2292 HOH HOH A . 
SA 8 HOH 293 2293 2293 HOH HOH A . 
SA 8 HOH 294 2294 2294 HOH HOH A . 
SA 8 HOH 295 2295 2295 HOH HOH A . 
SA 8 HOH 296 2296 2296 HOH HOH A . 
SA 8 HOH 297 2297 2297 HOH HOH A . 
SA 8 HOH 298 2298 2298 HOH HOH A . 
SA 8 HOH 299 2299 2299 HOH HOH A . 
SA 8 HOH 300 2300 2300 HOH HOH A . 
SA 8 HOH 301 2301 2301 HOH HOH A . 
SA 8 HOH 302 2302 2302 HOH HOH A . 
SA 8 HOH 303 2303 2303 HOH HOH A . 
SA 8 HOH 304 2304 2304 HOH HOH A . 
SA 8 HOH 305 2305 2305 HOH HOH A . 
SA 8 HOH 306 2306 2306 HOH HOH A . 
SA 8 HOH 307 2307 2307 HOH HOH A . 
SA 8 HOH 308 2308 2308 HOH HOH A . 
SA 8 HOH 309 2309 2309 HOH HOH A . 
SA 8 HOH 310 2310 2310 HOH HOH A . 
SA 8 HOH 311 2311 2311 HOH HOH A . 
SA 8 HOH 312 2312 2312 HOH HOH A . 
SA 8 HOH 313 2313 2313 HOH HOH A . 
SA 8 HOH 314 2314 2314 HOH HOH A . 
SA 8 HOH 315 2315 2315 HOH HOH A . 
SA 8 HOH 316 2316 2316 HOH HOH A . 
SA 8 HOH 317 2317 2317 HOH HOH A . 
SA 8 HOH 318 2318 2318 HOH HOH A . 
SA 8 HOH 319 2319 2319 HOH HOH A . 
SA 8 HOH 320 2320 2320 HOH HOH A . 
SA 8 HOH 321 2321 2321 HOH HOH A . 
SA 8 HOH 322 2322 2322 HOH HOH A . 
SA 8 HOH 323 2323 2323 HOH HOH A . 
SA 8 HOH 324 2324 2324 HOH HOH A . 
SA 8 HOH 325 2325 2325 HOH HOH A . 
SA 8 HOH 326 2326 2326 HOH HOH A . 
SA 8 HOH 327 2327 2327 HOH HOH A . 
SA 8 HOH 328 2328 2328 HOH HOH A . 
SA 8 HOH 329 2329 2329 HOH HOH A . 
SA 8 HOH 330 2330 2330 HOH HOH A . 
SA 8 HOH 331 2331 2331 HOH HOH A . 
SA 8 HOH 332 2332 2332 HOH HOH A . 
SA 8 HOH 333 2333 2333 HOH HOH A . 
SA 8 HOH 334 2334 2334 HOH HOH A . 
SA 8 HOH 335 2335 2335 HOH HOH A . 
SA 8 HOH 336 2336 2336 HOH HOH A . 
SA 8 HOH 337 2337 2337 HOH HOH A . 
SA 8 HOH 338 2338 2338 HOH HOH A . 
SA 8 HOH 339 2339 2339 HOH HOH A . 
SA 8 HOH 340 2340 2340 HOH HOH A . 
SA 8 HOH 341 2341 2341 HOH HOH A . 
SA 8 HOH 342 2342 2342 HOH HOH A . 
SA 8 HOH 343 2343 2343 HOH HOH A . 
SA 8 HOH 344 2344 2344 HOH HOH A . 
SA 8 HOH 345 2345 2345 HOH HOH A . 
SA 8 HOH 346 2346 2346 HOH HOH A . 
SA 8 HOH 347 2347 2347 HOH HOH A . 
SA 8 HOH 348 2348 2348 HOH HOH A . 
SA 8 HOH 349 2349 2349 HOH HOH A . 
SA 8 HOH 350 2350 2350 HOH HOH A . 
SA 8 HOH 351 2351 2351 HOH HOH A . 
SA 8 HOH 352 2352 2352 HOH HOH A . 
SA 8 HOH 353 2353 2353 HOH HOH A . 
SA 8 HOH 354 2354 2354 HOH HOH A . 
SA 8 HOH 355 2355 2355 HOH HOH A . 
SA 8 HOH 356 2356 2356 HOH HOH A . 
SA 8 HOH 357 2357 2357 HOH HOH A . 
SA 8 HOH 358 2358 2358 HOH HOH A . 
SA 8 HOH 359 2359 2359 HOH HOH A . 
SA 8 HOH 360 2360 2360 HOH HOH A . 
SA 8 HOH 361 2361 2361 HOH HOH A . 
SA 8 HOH 362 2362 2362 HOH HOH A . 
SA 8 HOH 363 2363 2363 HOH HOH A . 
SA 8 HOH 364 2364 2364 HOH HOH A . 
SA 8 HOH 365 2365 2365 HOH HOH A . 
SA 8 HOH 366 2366 2366 HOH HOH A . 
SA 8 HOH 367 2367 2367 HOH HOH A . 
SA 8 HOH 368 2368 2368 HOH HOH A . 
SA 8 HOH 369 2369 2369 HOH HOH A . 
SA 8 HOH 370 2370 2370 HOH HOH A . 
SA 8 HOH 371 2371 2371 HOH HOH A . 
SA 8 HOH 372 2372 2372 HOH HOH A . 
SA 8 HOH 373 2373 2373 HOH HOH A . 
SA 8 HOH 374 2374 2374 HOH HOH A . 
SA 8 HOH 375 2375 2375 HOH HOH A . 
SA 8 HOH 376 2376 2376 HOH HOH A . 
SA 8 HOH 377 2377 2377 HOH HOH A . 
SA 8 HOH 378 2378 2378 HOH HOH A . 
SA 8 HOH 379 2379 2379 HOH HOH A . 
SA 8 HOH 380 2380 2380 HOH HOH A . 
SA 8 HOH 381 2381 2381 HOH HOH A . 
SA 8 HOH 382 2382 2382 HOH HOH A . 
SA 8 HOH 383 2383 2383 HOH HOH A . 
SA 8 HOH 384 2384 2384 HOH HOH A . 
SA 8 HOH 385 2385 2385 HOH HOH A . 
SA 8 HOH 386 2386 2386 HOH HOH A . 
SA 8 HOH 387 2387 2387 HOH HOH A . 
SA 8 HOH 388 2388 2388 HOH HOH A . 
SA 8 HOH 389 2389 2389 HOH HOH A . 
SA 8 HOH 390 2390 2390 HOH HOH A . 
SA 8 HOH 391 2391 2391 HOH HOH A . 
SA 8 HOH 392 2392 2392 HOH HOH A . 
SA 8 HOH 393 2393 2393 HOH HOH A . 
SA 8 HOH 394 2394 2394 HOH HOH A . 
SA 8 HOH 395 2395 2395 HOH HOH A . 
SA 8 HOH 396 2396 2396 HOH HOH A . 
SA 8 HOH 397 2397 2397 HOH HOH A . 
SA 8 HOH 398 2398 2398 HOH HOH A . 
SA 8 HOH 399 2399 2399 HOH HOH A . 
SA 8 HOH 400 2400 2400 HOH HOH A . 
SA 8 HOH 401 2401 2401 HOH HOH A . 
SA 8 HOH 402 2402 2402 HOH HOH A . 
SA 8 HOH 403 2403 2403 HOH HOH A . 
SA 8 HOH 404 2404 2404 HOH HOH A . 
SA 8 HOH 405 2405 2405 HOH HOH A . 
SA 8 HOH 406 2406 2406 HOH HOH A . 
SA 8 HOH 407 2407 2407 HOH HOH A . 
SA 8 HOH 408 2408 2408 HOH HOH A . 
SA 8 HOH 409 2409 2409 HOH HOH A . 
SA 8 HOH 410 2410 2410 HOH HOH A . 
SA 8 HOH 411 2411 2411 HOH HOH A . 
SA 8 HOH 412 2412 2412 HOH HOH A . 
SA 8 HOH 413 2413 2413 HOH HOH A . 
SA 8 HOH 414 2414 2414 HOH HOH A . 
SA 8 HOH 415 2415 2415 HOH HOH A . 
SA 8 HOH 416 2416 2416 HOH HOH A . 
TA 8 HOH 1   2001 2001 HOH HOH B . 
TA 8 HOH 2   2002 2002 HOH HOH B . 
TA 8 HOH 3   2003 2003 HOH HOH B . 
TA 8 HOH 4   2004 2004 HOH HOH B . 
TA 8 HOH 5   2005 2005 HOH HOH B . 
TA 8 HOH 6   2006 2006 HOH HOH B . 
TA 8 HOH 7   2007 2007 HOH HOH B . 
TA 8 HOH 8   2008 2008 HOH HOH B . 
TA 8 HOH 9   2009 2009 HOH HOH B . 
TA 8 HOH 10  2010 2010 HOH HOH B . 
TA 8 HOH 11  2011 2011 HOH HOH B . 
TA 8 HOH 12  2012 2012 HOH HOH B . 
TA 8 HOH 13  2013 2013 HOH HOH B . 
TA 8 HOH 14  2014 2014 HOH HOH B . 
TA 8 HOH 15  2015 2015 HOH HOH B . 
TA 8 HOH 16  2016 2016 HOH HOH B . 
TA 8 HOH 17  2017 2017 HOH HOH B . 
TA 8 HOH 18  2018 2018 HOH HOH B . 
TA 8 HOH 19  2019 2019 HOH HOH B . 
TA 8 HOH 20  2020 2020 HOH HOH B . 
TA 8 HOH 21  2021 2021 HOH HOH B . 
TA 8 HOH 22  2022 2022 HOH HOH B . 
TA 8 HOH 23  2023 2023 HOH HOH B . 
TA 8 HOH 24  2024 2024 HOH HOH B . 
TA 8 HOH 25  2025 2025 HOH HOH B . 
TA 8 HOH 26  2026 2026 HOH HOH B . 
TA 8 HOH 27  2027 2027 HOH HOH B . 
TA 8 HOH 28  2028 2028 HOH HOH B . 
TA 8 HOH 29  2029 2029 HOH HOH B . 
TA 8 HOH 30  2030 2030 HOH HOH B . 
TA 8 HOH 31  2031 2031 HOH HOH B . 
TA 8 HOH 32  2032 2032 HOH HOH B . 
TA 8 HOH 33  2033 2033 HOH HOH B . 
TA 8 HOH 34  2034 2034 HOH HOH B . 
TA 8 HOH 35  2035 2035 HOH HOH B . 
TA 8 HOH 36  2036 2036 HOH HOH B . 
TA 8 HOH 37  2037 2037 HOH HOH B . 
TA 8 HOH 38  2038 2038 HOH HOH B . 
TA 8 HOH 39  2039 2039 HOH HOH B . 
TA 8 HOH 40  2040 2040 HOH HOH B . 
TA 8 HOH 41  2041 2041 HOH HOH B . 
TA 8 HOH 42  2042 2042 HOH HOH B . 
TA 8 HOH 43  2043 2043 HOH HOH B . 
TA 8 HOH 44  2044 2044 HOH HOH B . 
TA 8 HOH 45  2045 2045 HOH HOH B . 
TA 8 HOH 46  2046 2046 HOH HOH B . 
TA 8 HOH 47  2047 2047 HOH HOH B . 
TA 8 HOH 48  2048 2048 HOH HOH B . 
TA 8 HOH 49  2049 2049 HOH HOH B . 
TA 8 HOH 50  2050 2050 HOH HOH B . 
TA 8 HOH 51  2051 2051 HOH HOH B . 
TA 8 HOH 52  2052 2052 HOH HOH B . 
TA 8 HOH 53  2053 2053 HOH HOH B . 
TA 8 HOH 54  2054 2054 HOH HOH B . 
TA 8 HOH 55  2055 2055 HOH HOH B . 
TA 8 HOH 56  2056 2056 HOH HOH B . 
TA 8 HOH 57  2057 2057 HOH HOH B . 
TA 8 HOH 58  2058 2058 HOH HOH B . 
TA 8 HOH 59  2059 2059 HOH HOH B . 
TA 8 HOH 60  2060 2060 HOH HOH B . 
TA 8 HOH 61  2061 2061 HOH HOH B . 
TA 8 HOH 62  2062 2062 HOH HOH B . 
TA 8 HOH 63  2063 2063 HOH HOH B . 
TA 8 HOH 64  2064 2064 HOH HOH B . 
TA 8 HOH 65  2065 2065 HOH HOH B . 
TA 8 HOH 66  2066 2066 HOH HOH B . 
TA 8 HOH 67  2067 2067 HOH HOH B . 
TA 8 HOH 68  2068 2068 HOH HOH B . 
TA 8 HOH 69  2069 2069 HOH HOH B . 
TA 8 HOH 70  2070 2070 HOH HOH B . 
TA 8 HOH 71  2071 2071 HOH HOH B . 
TA 8 HOH 72  2072 2072 HOH HOH B . 
TA 8 HOH 73  2073 2073 HOH HOH B . 
TA 8 HOH 74  2074 2074 HOH HOH B . 
TA 8 HOH 75  2075 2075 HOH HOH B . 
TA 8 HOH 76  2076 2076 HOH HOH B . 
TA 8 HOH 77  2077 2077 HOH HOH B . 
TA 8 HOH 78  2078 2078 HOH HOH B . 
TA 8 HOH 79  2079 2079 HOH HOH B . 
TA 8 HOH 80  2080 2080 HOH HOH B . 
TA 8 HOH 81  2081 2081 HOH HOH B . 
TA 8 HOH 82  2082 2082 HOH HOH B . 
TA 8 HOH 83  2083 2083 HOH HOH B . 
TA 8 HOH 84  2084 2084 HOH HOH B . 
TA 8 HOH 85  2085 2085 HOH HOH B . 
TA 8 HOH 86  2086 2086 HOH HOH B . 
TA 8 HOH 87  2087 2087 HOH HOH B . 
TA 8 HOH 88  2088 2088 HOH HOH B . 
TA 8 HOH 89  2089 2089 HOH HOH B . 
TA 8 HOH 90  2090 2090 HOH HOH B . 
TA 8 HOH 91  2091 2091 HOH HOH B . 
TA 8 HOH 92  2092 2092 HOH HOH B . 
TA 8 HOH 93  2093 2093 HOH HOH B . 
TA 8 HOH 94  2094 2094 HOH HOH B . 
TA 8 HOH 95  2095 2095 HOH HOH B . 
TA 8 HOH 96  2096 2096 HOH HOH B . 
TA 8 HOH 97  2097 2097 HOH HOH B . 
TA 8 HOH 98  2098 2098 HOH HOH B . 
TA 8 HOH 99  2099 2099 HOH HOH B . 
TA 8 HOH 100 2100 2100 HOH HOH B . 
TA 8 HOH 101 2101 2101 HOH HOH B . 
TA 8 HOH 102 2102 2102 HOH HOH B . 
TA 8 HOH 103 2103 2103 HOH HOH B . 
TA 8 HOH 104 2104 2104 HOH HOH B . 
TA 8 HOH 105 2105 2105 HOH HOH B . 
TA 8 HOH 106 2106 2106 HOH HOH B . 
TA 8 HOH 107 2107 2107 HOH HOH B . 
TA 8 HOH 108 2108 2108 HOH HOH B . 
TA 8 HOH 109 2109 2109 HOH HOH B . 
TA 8 HOH 110 2110 2110 HOH HOH B . 
TA 8 HOH 111 2111 2111 HOH HOH B . 
TA 8 HOH 112 2112 2112 HOH HOH B . 
TA 8 HOH 113 2113 2113 HOH HOH B . 
TA 8 HOH 114 2114 2114 HOH HOH B . 
TA 8 HOH 115 2115 2115 HOH HOH B . 
TA 8 HOH 116 2116 2116 HOH HOH B . 
TA 8 HOH 117 2117 2117 HOH HOH B . 
TA 8 HOH 118 2118 2118 HOH HOH B . 
TA 8 HOH 119 2119 2119 HOH HOH B . 
TA 8 HOH 120 2120 2120 HOH HOH B . 
TA 8 HOH 121 2121 2121 HOH HOH B . 
TA 8 HOH 122 2122 2122 HOH HOH B . 
TA 8 HOH 123 2123 2123 HOH HOH B . 
TA 8 HOH 124 2124 2124 HOH HOH B . 
TA 8 HOH 125 2125 2125 HOH HOH B . 
TA 8 HOH 126 2126 2126 HOH HOH B . 
TA 8 HOH 127 2127 2127 HOH HOH B . 
TA 8 HOH 128 2128 2128 HOH HOH B . 
TA 8 HOH 129 2129 2129 HOH HOH B . 
TA 8 HOH 130 2130 2130 HOH HOH B . 
TA 8 HOH 131 2131 2131 HOH HOH B . 
TA 8 HOH 132 2132 2132 HOH HOH B . 
TA 8 HOH 133 2133 2133 HOH HOH B . 
TA 8 HOH 134 2134 2134 HOH HOH B . 
TA 8 HOH 135 2135 2135 HOH HOH B . 
TA 8 HOH 136 2136 2136 HOH HOH B . 
TA 8 HOH 137 2137 2137 HOH HOH B . 
TA 8 HOH 138 2138 2138 HOH HOH B . 
TA 8 HOH 139 2139 2139 HOH HOH B . 
TA 8 HOH 140 2140 2140 HOH HOH B . 
TA 8 HOH 141 2141 2141 HOH HOH B . 
TA 8 HOH 142 2142 2142 HOH HOH B . 
TA 8 HOH 143 2143 2143 HOH HOH B . 
TA 8 HOH 144 2144 2144 HOH HOH B . 
TA 8 HOH 145 2145 2145 HOH HOH B . 
TA 8 HOH 146 2146 2146 HOH HOH B . 
TA 8 HOH 147 2147 2147 HOH HOH B . 
TA 8 HOH 148 2148 2148 HOH HOH B . 
TA 8 HOH 149 2149 2149 HOH HOH B . 
TA 8 HOH 150 2150 2150 HOH HOH B . 
TA 8 HOH 151 2151 2151 HOH HOH B . 
TA 8 HOH 152 2152 2152 HOH HOH B . 
TA 8 HOH 153 2153 2153 HOH HOH B . 
TA 8 HOH 154 2154 2154 HOH HOH B . 
TA 8 HOH 155 2155 2155 HOH HOH B . 
TA 8 HOH 156 2156 2156 HOH HOH B . 
TA 8 HOH 157 2157 2157 HOH HOH B . 
TA 8 HOH 158 2158 2158 HOH HOH B . 
TA 8 HOH 159 2159 2159 HOH HOH B . 
TA 8 HOH 160 2160 2160 HOH HOH B . 
TA 8 HOH 161 2161 2161 HOH HOH B . 
TA 8 HOH 162 2162 2162 HOH HOH B . 
TA 8 HOH 163 2163 2163 HOH HOH B . 
TA 8 HOH 164 2164 2164 HOH HOH B . 
TA 8 HOH 165 2165 2165 HOH HOH B . 
TA 8 HOH 166 2166 2166 HOH HOH B . 
TA 8 HOH 167 2167 2167 HOH HOH B . 
TA 8 HOH 168 2168 2168 HOH HOH B . 
TA 8 HOH 169 2169 2169 HOH HOH B . 
TA 8 HOH 170 2170 2170 HOH HOH B . 
TA 8 HOH 171 2171 2171 HOH HOH B . 
TA 8 HOH 172 2172 2172 HOH HOH B . 
TA 8 HOH 173 2173 2173 HOH HOH B . 
TA 8 HOH 174 2174 2174 HOH HOH B . 
TA 8 HOH 175 2175 2175 HOH HOH B . 
TA 8 HOH 176 2176 2176 HOH HOH B . 
TA 8 HOH 177 2177 2177 HOH HOH B . 
TA 8 HOH 178 2178 2178 HOH HOH B . 
TA 8 HOH 179 2179 2179 HOH HOH B . 
TA 8 HOH 180 2180 2180 HOH HOH B . 
TA 8 HOH 181 2181 2181 HOH HOH B . 
TA 8 HOH 182 2182 2182 HOH HOH B . 
TA 8 HOH 183 2183 2183 HOH HOH B . 
TA 8 HOH 184 2184 2184 HOH HOH B . 
TA 8 HOH 185 2185 2185 HOH HOH B . 
TA 8 HOH 186 2186 2186 HOH HOH B . 
TA 8 HOH 187 2187 2187 HOH HOH B . 
TA 8 HOH 188 2188 2188 HOH HOH B . 
TA 8 HOH 189 2189 2189 HOH HOH B . 
TA 8 HOH 190 2190 2190 HOH HOH B . 
TA 8 HOH 191 2191 2191 HOH HOH B . 
TA 8 HOH 192 2192 2192 HOH HOH B . 
TA 8 HOH 193 2193 2193 HOH HOH B . 
TA 8 HOH 194 2194 2194 HOH HOH B . 
TA 8 HOH 195 2195 2195 HOH HOH B . 
TA 8 HOH 196 2196 2196 HOH HOH B . 
TA 8 HOH 197 2197 2197 HOH HOH B . 
TA 8 HOH 198 2198 2198 HOH HOH B . 
TA 8 HOH 199 2199 2199 HOH HOH B . 
TA 8 HOH 200 2200 2200 HOH HOH B . 
TA 8 HOH 201 2201 2201 HOH HOH B . 
TA 8 HOH 202 2202 2202 HOH HOH B . 
TA 8 HOH 203 2203 2203 HOH HOH B . 
TA 8 HOH 204 2204 2204 HOH HOH B . 
TA 8 HOH 205 2205 2205 HOH HOH B . 
TA 8 HOH 206 2206 2206 HOH HOH B . 
TA 8 HOH 207 2207 2207 HOH HOH B . 
TA 8 HOH 208 2208 2208 HOH HOH B . 
TA 8 HOH 209 2209 2209 HOH HOH B . 
TA 8 HOH 210 2210 2210 HOH HOH B . 
TA 8 HOH 211 2211 2211 HOH HOH B . 
TA 8 HOH 212 2212 2212 HOH HOH B . 
TA 8 HOH 213 2213 2213 HOH HOH B . 
TA 8 HOH 214 2214 2214 HOH HOH B . 
TA 8 HOH 215 2215 2215 HOH HOH B . 
TA 8 HOH 216 2216 2216 HOH HOH B . 
TA 8 HOH 217 2217 2217 HOH HOH B . 
TA 8 HOH 218 2218 2218 HOH HOH B . 
TA 8 HOH 219 2219 2219 HOH HOH B . 
TA 8 HOH 220 2220 2220 HOH HOH B . 
TA 8 HOH 221 2221 2221 HOH HOH B . 
TA 8 HOH 222 2222 2222 HOH HOH B . 
TA 8 HOH 223 2223 2223 HOH HOH B . 
TA 8 HOH 224 2224 2224 HOH HOH B . 
TA 8 HOH 225 2225 2225 HOH HOH B . 
TA 8 HOH 226 2226 2226 HOH HOH B . 
TA 8 HOH 227 2227 2227 HOH HOH B . 
TA 8 HOH 228 2228 2228 HOH HOH B . 
TA 8 HOH 229 2229 2229 HOH HOH B . 
TA 8 HOH 230 2230 2230 HOH HOH B . 
TA 8 HOH 231 2231 2231 HOH HOH B . 
TA 8 HOH 232 2232 2232 HOH HOH B . 
TA 8 HOH 233 2233 2233 HOH HOH B . 
TA 8 HOH 234 2234 2234 HOH HOH B . 
TA 8 HOH 235 2235 2235 HOH HOH B . 
TA 8 HOH 236 2236 2236 HOH HOH B . 
TA 8 HOH 237 2237 2237 HOH HOH B . 
TA 8 HOH 238 2238 2238 HOH HOH B . 
TA 8 HOH 239 2239 2239 HOH HOH B . 
TA 8 HOH 240 2240 2240 HOH HOH B . 
TA 8 HOH 241 2241 2241 HOH HOH B . 
TA 8 HOH 242 2242 2242 HOH HOH B . 
TA 8 HOH 243 2243 2243 HOH HOH B . 
TA 8 HOH 244 2244 2244 HOH HOH B . 
TA 8 HOH 245 2245 2245 HOH HOH B . 
TA 8 HOH 246 2246 2246 HOH HOH B . 
TA 8 HOH 247 2247 2247 HOH HOH B . 
TA 8 HOH 248 2248 2248 HOH HOH B . 
TA 8 HOH 249 2249 2249 HOH HOH B . 
TA 8 HOH 250 2250 2250 HOH HOH B . 
TA 8 HOH 251 2251 2251 HOH HOH B . 
TA 8 HOH 252 2252 2252 HOH HOH B . 
TA 8 HOH 253 2253 2253 HOH HOH B . 
TA 8 HOH 254 2254 2254 HOH HOH B . 
TA 8 HOH 255 2255 2255 HOH HOH B . 
TA 8 HOH 256 2256 2256 HOH HOH B . 
TA 8 HOH 257 2257 2257 HOH HOH B . 
TA 8 HOH 258 2258 2258 HOH HOH B . 
TA 8 HOH 259 2259 2259 HOH HOH B . 
TA 8 HOH 260 2260 2260 HOH HOH B . 
TA 8 HOH 261 2261 2261 HOH HOH B . 
TA 8 HOH 262 2262 2262 HOH HOH B . 
TA 8 HOH 263 2263 2263 HOH HOH B . 
TA 8 HOH 264 2264 2264 HOH HOH B . 
TA 8 HOH 265 2265 2265 HOH HOH B . 
TA 8 HOH 266 2266 2266 HOH HOH B . 
TA 8 HOH 267 2267 2267 HOH HOH B . 
TA 8 HOH 268 2268 2268 HOH HOH B . 
TA 8 HOH 269 2269 2269 HOH HOH B . 
TA 8 HOH 270 2270 2270 HOH HOH B . 
TA 8 HOH 271 2271 2271 HOH HOH B . 
TA 8 HOH 272 2272 2272 HOH HOH B . 
TA 8 HOH 273 2273 2273 HOH HOH B . 
TA 8 HOH 274 2274 2274 HOH HOH B . 
TA 8 HOH 275 2275 2275 HOH HOH B . 
TA 8 HOH 276 2276 2276 HOH HOH B . 
TA 8 HOH 277 2277 2277 HOH HOH B . 
TA 8 HOH 278 2278 2278 HOH HOH B . 
TA 8 HOH 279 2279 2279 HOH HOH B . 
TA 8 HOH 280 2280 2280 HOH HOH B . 
TA 8 HOH 281 2281 2281 HOH HOH B . 
TA 8 HOH 282 2282 2282 HOH HOH B . 
TA 8 HOH 283 2283 2283 HOH HOH B . 
TA 8 HOH 284 2284 2284 HOH HOH B . 
TA 8 HOH 285 2285 2285 HOH HOH B . 
TA 8 HOH 286 2286 2286 HOH HOH B . 
TA 8 HOH 287 2287 2287 HOH HOH B . 
TA 8 HOH 288 2288 2288 HOH HOH B . 
TA 8 HOH 289 2289 2289 HOH HOH B . 
TA 8 HOH 290 2290 2290 HOH HOH B . 
TA 8 HOH 291 2291 2291 HOH HOH B . 
TA 8 HOH 292 2292 2292 HOH HOH B . 
TA 8 HOH 293 2293 2293 HOH HOH B . 
TA 8 HOH 294 2294 2294 HOH HOH B . 
TA 8 HOH 295 2295 2295 HOH HOH B . 
TA 8 HOH 296 2296 2296 HOH HOH B . 
TA 8 HOH 297 2297 2297 HOH HOH B . 
TA 8 HOH 298 2298 2298 HOH HOH B . 
TA 8 HOH 299 2299 2299 HOH HOH B . 
TA 8 HOH 300 2300 2300 HOH HOH B . 
TA 8 HOH 301 2301 2301 HOH HOH B . 
TA 8 HOH 302 2302 2302 HOH HOH B . 
TA 8 HOH 303 2303 2303 HOH HOH B . 
TA 8 HOH 304 2304 2304 HOH HOH B . 
TA 8 HOH 305 2305 2305 HOH HOH B . 
TA 8 HOH 306 2306 2306 HOH HOH B . 
TA 8 HOH 307 2307 2307 HOH HOH B . 
TA 8 HOH 308 2308 2308 HOH HOH B . 
TA 8 HOH 309 2309 2309 HOH HOH B . 
TA 8 HOH 310 2310 2310 HOH HOH B . 
TA 8 HOH 311 2311 2311 HOH HOH B . 
TA 8 HOH 312 2312 2312 HOH HOH B . 
TA 8 HOH 313 2313 2313 HOH HOH B . 
TA 8 HOH 314 2314 2314 HOH HOH B . 
TA 8 HOH 315 2315 2315 HOH HOH B . 
TA 8 HOH 316 2316 2316 HOH HOH B . 
TA 8 HOH 317 2317 2317 HOH HOH B . 
TA 8 HOH 318 2318 2318 HOH HOH B . 
TA 8 HOH 319 2319 2319 HOH HOH B . 
TA 8 HOH 320 2320 2320 HOH HOH B . 
TA 8 HOH 321 2321 2321 HOH HOH B . 
TA 8 HOH 322 2322 2322 HOH HOH B . 
TA 8 HOH 323 2323 2323 HOH HOH B . 
TA 8 HOH 324 2324 2324 HOH HOH B . 
TA 8 HOH 325 2325 2325 HOH HOH B . 
TA 8 HOH 326 2326 2326 HOH HOH B . 
TA 8 HOH 327 2327 2327 HOH HOH B . 
TA 8 HOH 328 2328 2328 HOH HOH B . 
TA 8 HOH 329 2329 2329 HOH HOH B . 
TA 8 HOH 330 2330 2330 HOH HOH B . 
TA 8 HOH 331 2331 2331 HOH HOH B . 
TA 8 HOH 332 2332 2332 HOH HOH B . 
TA 8 HOH 333 2333 2333 HOH HOH B . 
TA 8 HOH 334 2334 2334 HOH HOH B . 
TA 8 HOH 335 2335 2335 HOH HOH B . 
TA 8 HOH 336 2336 2336 HOH HOH B . 
TA 8 HOH 337 2337 2337 HOH HOH B . 
TA 8 HOH 338 2338 2338 HOH HOH B . 
TA 8 HOH 339 2339 2339 HOH HOH B . 
TA 8 HOH 340 2340 2340 HOH HOH B . 
TA 8 HOH 341 2341 2341 HOH HOH B . 
TA 8 HOH 342 2342 2342 HOH HOH B . 
TA 8 HOH 343 2343 2343 HOH HOH B . 
TA 8 HOH 344 2344 2344 HOH HOH B . 
TA 8 HOH 345 2345 2345 HOH HOH B . 
TA 8 HOH 346 2346 2346 HOH HOH B . 
TA 8 HOH 347 2347 2347 HOH HOH B . 
TA 8 HOH 348 2348 2348 HOH HOH B . 
TA 8 HOH 349 2349 2349 HOH HOH B . 
TA 8 HOH 350 2350 2350 HOH HOH B . 
TA 8 HOH 351 2351 2351 HOH HOH B . 
TA 8 HOH 352 2352 2352 HOH HOH B . 
TA 8 HOH 353 2353 2353 HOH HOH B . 
TA 8 HOH 354 2354 2354 HOH HOH B . 
TA 8 HOH 355 2355 2355 HOH HOH B . 
TA 8 HOH 356 2356 2356 HOH HOH B . 
TA 8 HOH 357 2357 2357 HOH HOH B . 
TA 8 HOH 358 2358 2358 HOH HOH B . 
TA 8 HOH 359 2359 2359 HOH HOH B . 
TA 8 HOH 360 2360 2360 HOH HOH B . 
TA 8 HOH 361 2361 2361 HOH HOH B . 
TA 8 HOH 362 2362 2362 HOH HOH B . 
TA 8 HOH 363 2363 2363 HOH HOH B . 
TA 8 HOH 364 2364 2364 HOH HOH B . 
TA 8 HOH 365 2365 2365 HOH HOH B . 
TA 8 HOH 366 2366 2366 HOH HOH B . 
TA 8 HOH 367 2367 2367 HOH HOH B . 
TA 8 HOH 368 2368 2368 HOH HOH B . 
TA 8 HOH 369 2369 2369 HOH HOH B . 
TA 8 HOH 370 2370 2370 HOH HOH B . 
TA 8 HOH 371 2371 2371 HOH HOH B . 
TA 8 HOH 372 2372 2372 HOH HOH B . 
TA 8 HOH 373 2373 2373 HOH HOH B . 
TA 8 HOH 374 2374 2374 HOH HOH B . 
TA 8 HOH 375 2375 2375 HOH HOH B . 
TA 8 HOH 376 2376 2376 HOH HOH B . 
TA 8 HOH 377 2377 2377 HOH HOH B . 
TA 8 HOH 378 2378 2378 HOH HOH B . 
TA 8 HOH 379 2379 2379 HOH HOH B . 
TA 8 HOH 380 2380 2380 HOH HOH B . 
TA 8 HOH 381 2381 2381 HOH HOH B . 
TA 8 HOH 382 2382 2382 HOH HOH B . 
TA 8 HOH 383 2383 2383 HOH HOH B . 
TA 8 HOH 384 2384 2384 HOH HOH B . 
TA 8 HOH 385 2385 2385 HOH HOH B . 
TA 8 HOH 386 2386 2386 HOH HOH B . 
TA 8 HOH 387 2387 2387 HOH HOH B . 
UA 8 HOH 1   2001 2001 HOH HOH C . 
UA 8 HOH 2   2002 2002 HOH HOH C . 
UA 8 HOH 3   2003 2003 HOH HOH C . 
UA 8 HOH 4   2004 2004 HOH HOH C . 
UA 8 HOH 5   2005 2005 HOH HOH C . 
UA 8 HOH 6   2006 2006 HOH HOH C . 
UA 8 HOH 7   2007 2007 HOH HOH C . 
UA 8 HOH 8   2008 2008 HOH HOH C . 
UA 8 HOH 9   2009 2009 HOH HOH C . 
UA 8 HOH 10  2010 2010 HOH HOH C . 
UA 8 HOH 11  2011 2011 HOH HOH C . 
UA 8 HOH 12  2012 2012 HOH HOH C . 
UA 8 HOH 13  2013 2013 HOH HOH C . 
UA 8 HOH 14  2014 2014 HOH HOH C . 
UA 8 HOH 15  2015 2015 HOH HOH C . 
UA 8 HOH 16  2016 2016 HOH HOH C . 
UA 8 HOH 17  2017 2017 HOH HOH C . 
UA 8 HOH 18  2018 2018 HOH HOH C . 
UA 8 HOH 19  2019 2019 HOH HOH C . 
UA 8 HOH 20  2020 2020 HOH HOH C . 
UA 8 HOH 21  2021 2021 HOH HOH C . 
UA 8 HOH 22  2022 2022 HOH HOH C . 
UA 8 HOH 23  2023 2023 HOH HOH C . 
UA 8 HOH 24  2024 2024 HOH HOH C . 
UA 8 HOH 25  2025 2025 HOH HOH C . 
UA 8 HOH 26  2026 2026 HOH HOH C . 
UA 8 HOH 27  2027 2027 HOH HOH C . 
UA 8 HOH 28  2028 2028 HOH HOH C . 
UA 8 HOH 29  2029 2029 HOH HOH C . 
UA 8 HOH 30  2030 2030 HOH HOH C . 
UA 8 HOH 31  2031 2031 HOH HOH C . 
UA 8 HOH 32  2032 2032 HOH HOH C . 
UA 8 HOH 33  2033 2033 HOH HOH C . 
UA 8 HOH 34  2034 2034 HOH HOH C . 
UA 8 HOH 35  2035 2035 HOH HOH C . 
UA 8 HOH 36  2036 2036 HOH HOH C . 
UA 8 HOH 37  2037 2037 HOH HOH C . 
UA 8 HOH 38  2038 2038 HOH HOH C . 
UA 8 HOH 39  2039 2039 HOH HOH C . 
UA 8 HOH 40  2040 2040 HOH HOH C . 
UA 8 HOH 41  2041 2041 HOH HOH C . 
UA 8 HOH 42  2042 2042 HOH HOH C . 
UA 8 HOH 43  2043 2043 HOH HOH C . 
UA 8 HOH 44  2044 2044 HOH HOH C . 
UA 8 HOH 45  2045 2045 HOH HOH C . 
UA 8 HOH 46  2046 2046 HOH HOH C . 
UA 8 HOH 47  2047 2047 HOH HOH C . 
UA 8 HOH 48  2048 2048 HOH HOH C . 
UA 8 HOH 49  2049 2049 HOH HOH C . 
UA 8 HOH 50  2050 2050 HOH HOH C . 
UA 8 HOH 51  2051 2051 HOH HOH C . 
UA 8 HOH 52  2052 2052 HOH HOH C . 
UA 8 HOH 53  2053 2053 HOH HOH C . 
UA 8 HOH 54  2054 2054 HOH HOH C . 
UA 8 HOH 55  2055 2055 HOH HOH C . 
UA 8 HOH 56  2056 2056 HOH HOH C . 
UA 8 HOH 57  2057 2057 HOH HOH C . 
UA 8 HOH 58  2058 2058 HOH HOH C . 
UA 8 HOH 59  2059 2059 HOH HOH C . 
UA 8 HOH 60  2060 2060 HOH HOH C . 
UA 8 HOH 61  2061 2061 HOH HOH C . 
UA 8 HOH 62  2062 2062 HOH HOH C . 
UA 8 HOH 63  2063 2063 HOH HOH C . 
UA 8 HOH 64  2064 2064 HOH HOH C . 
UA 8 HOH 65  2065 2065 HOH HOH C . 
UA 8 HOH 66  2066 2066 HOH HOH C . 
UA 8 HOH 67  2067 2067 HOH HOH C . 
UA 8 HOH 68  2068 2068 HOH HOH C . 
UA 8 HOH 69  2069 2069 HOH HOH C . 
UA 8 HOH 70  2070 2070 HOH HOH C . 
UA 8 HOH 71  2071 2071 HOH HOH C . 
UA 8 HOH 72  2072 2072 HOH HOH C . 
UA 8 HOH 73  2073 2073 HOH HOH C . 
UA 8 HOH 74  2074 2074 HOH HOH C . 
UA 8 HOH 75  2075 2075 HOH HOH C . 
UA 8 HOH 76  2076 2076 HOH HOH C . 
UA 8 HOH 77  2077 2077 HOH HOH C . 
UA 8 HOH 78  2078 2078 HOH HOH C . 
UA 8 HOH 79  2079 2079 HOH HOH C . 
UA 8 HOH 80  2080 2080 HOH HOH C . 
UA 8 HOH 81  2081 2081 HOH HOH C . 
UA 8 HOH 82  2082 2082 HOH HOH C . 
UA 8 HOH 83  2083 2083 HOH HOH C . 
UA 8 HOH 84  2084 2084 HOH HOH C . 
UA 8 HOH 85  2085 2085 HOH HOH C . 
UA 8 HOH 86  2086 2086 HOH HOH C . 
UA 8 HOH 87  2087 2087 HOH HOH C . 
UA 8 HOH 88  2088 2088 HOH HOH C . 
UA 8 HOH 89  2089 2089 HOH HOH C . 
UA 8 HOH 90  2090 2090 HOH HOH C . 
UA 8 HOH 91  2091 2091 HOH HOH C . 
UA 8 HOH 92  2092 2092 HOH HOH C . 
UA 8 HOH 93  2093 2093 HOH HOH C . 
UA 8 HOH 94  2094 2094 HOH HOH C . 
UA 8 HOH 95  2095 2095 HOH HOH C . 
UA 8 HOH 96  2096 2096 HOH HOH C . 
UA 8 HOH 97  2097 2097 HOH HOH C . 
UA 8 HOH 98  2098 2098 HOH HOH C . 
UA 8 HOH 99  2099 2099 HOH HOH C . 
UA 8 HOH 100 2100 2100 HOH HOH C . 
UA 8 HOH 101 2101 2101 HOH HOH C . 
UA 8 HOH 102 2102 2102 HOH HOH C . 
UA 8 HOH 103 2103 2103 HOH HOH C . 
UA 8 HOH 104 2104 2104 HOH HOH C . 
UA 8 HOH 105 2105 2105 HOH HOH C . 
UA 8 HOH 106 2106 2106 HOH HOH C . 
UA 8 HOH 107 2107 2107 HOH HOH C . 
UA 8 HOH 108 2108 2108 HOH HOH C . 
UA 8 HOH 109 2109 2109 HOH HOH C . 
UA 8 HOH 110 2110 2110 HOH HOH C . 
UA 8 HOH 111 2111 2111 HOH HOH C . 
UA 8 HOH 112 2112 2112 HOH HOH C . 
UA 8 HOH 113 2113 2113 HOH HOH C . 
UA 8 HOH 114 2114 2114 HOH HOH C . 
UA 8 HOH 115 2115 2115 HOH HOH C . 
UA 8 HOH 116 2116 2116 HOH HOH C . 
UA 8 HOH 117 2117 2117 HOH HOH C . 
UA 8 HOH 118 2118 2118 HOH HOH C . 
UA 8 HOH 119 2119 2119 HOH HOH C . 
UA 8 HOH 120 2120 2120 HOH HOH C . 
UA 8 HOH 121 2121 2121 HOH HOH C . 
UA 8 HOH 122 2122 2122 HOH HOH C . 
UA 8 HOH 123 2123 2123 HOH HOH C . 
UA 8 HOH 124 2124 2124 HOH HOH C . 
UA 8 HOH 125 2125 2125 HOH HOH C . 
UA 8 HOH 126 2126 2126 HOH HOH C . 
UA 8 HOH 127 2127 2127 HOH HOH C . 
UA 8 HOH 128 2128 2128 HOH HOH C . 
UA 8 HOH 129 2129 2129 HOH HOH C . 
UA 8 HOH 130 2130 2130 HOH HOH C . 
UA 8 HOH 131 2131 2131 HOH HOH C . 
UA 8 HOH 132 2132 2132 HOH HOH C . 
UA 8 HOH 133 2133 2133 HOH HOH C . 
UA 8 HOH 134 2134 2134 HOH HOH C . 
UA 8 HOH 135 2135 2135 HOH HOH C . 
UA 8 HOH 136 2136 2136 HOH HOH C . 
UA 8 HOH 137 2137 2137 HOH HOH C . 
UA 8 HOH 138 2138 2138 HOH HOH C . 
UA 8 HOH 139 2139 2139 HOH HOH C . 
UA 8 HOH 140 2140 2140 HOH HOH C . 
UA 8 HOH 141 2141 2141 HOH HOH C . 
UA 8 HOH 142 2142 2142 HOH HOH C . 
UA 8 HOH 143 2143 2143 HOH HOH C . 
UA 8 HOH 144 2144 2144 HOH HOH C . 
UA 8 HOH 145 2145 2145 HOH HOH C . 
UA 8 HOH 146 2146 2146 HOH HOH C . 
UA 8 HOH 147 2147 2147 HOH HOH C . 
UA 8 HOH 148 2148 2148 HOH HOH C . 
UA 8 HOH 149 2149 2149 HOH HOH C . 
UA 8 HOH 150 2150 2150 HOH HOH C . 
UA 8 HOH 151 2151 2151 HOH HOH C . 
UA 8 HOH 152 2152 2152 HOH HOH C . 
UA 8 HOH 153 2153 2153 HOH HOH C . 
UA 8 HOH 154 2154 2154 HOH HOH C . 
UA 8 HOH 155 2155 2155 HOH HOH C . 
UA 8 HOH 156 2156 2156 HOH HOH C . 
UA 8 HOH 157 2157 2157 HOH HOH C . 
UA 8 HOH 158 2158 2158 HOH HOH C . 
UA 8 HOH 159 2159 2159 HOH HOH C . 
UA 8 HOH 160 2160 2160 HOH HOH C . 
UA 8 HOH 161 2161 2161 HOH HOH C . 
UA 8 HOH 162 2162 2162 HOH HOH C . 
UA 8 HOH 163 2163 2163 HOH HOH C . 
UA 8 HOH 164 2164 2164 HOH HOH C . 
UA 8 HOH 165 2165 2165 HOH HOH C . 
UA 8 HOH 166 2166 2166 HOH HOH C . 
UA 8 HOH 167 2167 2167 HOH HOH C . 
UA 8 HOH 168 2168 2168 HOH HOH C . 
UA 8 HOH 169 2169 2169 HOH HOH C . 
UA 8 HOH 170 2170 2170 HOH HOH C . 
UA 8 HOH 171 2171 2171 HOH HOH C . 
UA 8 HOH 172 2172 2172 HOH HOH C . 
UA 8 HOH 173 2173 2173 HOH HOH C . 
UA 8 HOH 174 2174 2174 HOH HOH C . 
UA 8 HOH 175 2175 2175 HOH HOH C . 
UA 8 HOH 176 2176 2176 HOH HOH C . 
UA 8 HOH 177 2177 2177 HOH HOH C . 
UA 8 HOH 178 2178 2178 HOH HOH C . 
UA 8 HOH 179 2179 2179 HOH HOH C . 
UA 8 HOH 180 2180 2180 HOH HOH C . 
UA 8 HOH 181 2181 2181 HOH HOH C . 
UA 8 HOH 182 2182 2182 HOH HOH C . 
UA 8 HOH 183 2183 2183 HOH HOH C . 
UA 8 HOH 184 2184 2184 HOH HOH C . 
UA 8 HOH 185 2185 2185 HOH HOH C . 
UA 8 HOH 186 2186 2186 HOH HOH C . 
UA 8 HOH 187 2187 2187 HOH HOH C . 
UA 8 HOH 188 2188 2188 HOH HOH C . 
UA 8 HOH 189 2189 2189 HOH HOH C . 
UA 8 HOH 190 2190 2190 HOH HOH C . 
UA 8 HOH 191 2191 2191 HOH HOH C . 
UA 8 HOH 192 2192 2192 HOH HOH C . 
UA 8 HOH 193 2193 2193 HOH HOH C . 
UA 8 HOH 194 2194 2194 HOH HOH C . 
UA 8 HOH 195 2195 2195 HOH HOH C . 
UA 8 HOH 196 2196 2196 HOH HOH C . 
UA 8 HOH 197 2197 2197 HOH HOH C . 
UA 8 HOH 198 2198 2198 HOH HOH C . 
UA 8 HOH 199 2199 2199 HOH HOH C . 
UA 8 HOH 200 2200 2200 HOH HOH C . 
UA 8 HOH 201 2201 2201 HOH HOH C . 
UA 8 HOH 202 2202 2202 HOH HOH C . 
UA 8 HOH 203 2203 2203 HOH HOH C . 
UA 8 HOH 204 2204 2204 HOH HOH C . 
UA 8 HOH 205 2205 2205 HOH HOH C . 
UA 8 HOH 206 2206 2206 HOH HOH C . 
UA 8 HOH 207 2207 2207 HOH HOH C . 
UA 8 HOH 208 2208 2208 HOH HOH C . 
UA 8 HOH 209 2209 2209 HOH HOH C . 
UA 8 HOH 210 2210 2210 HOH HOH C . 
UA 8 HOH 211 2211 2211 HOH HOH C . 
UA 8 HOH 212 2212 2212 HOH HOH C . 
UA 8 HOH 213 2213 2213 HOH HOH C . 
UA 8 HOH 214 2214 2214 HOH HOH C . 
UA 8 HOH 215 2215 2215 HOH HOH C . 
UA 8 HOH 216 2216 2216 HOH HOH C . 
UA 8 HOH 217 2217 2217 HOH HOH C . 
UA 8 HOH 218 2218 2218 HOH HOH C . 
UA 8 HOH 219 2219 2219 HOH HOH C . 
UA 8 HOH 220 2220 2220 HOH HOH C . 
UA 8 HOH 221 2221 2221 HOH HOH C . 
UA 8 HOH 222 2222 2222 HOH HOH C . 
UA 8 HOH 223 2223 2223 HOH HOH C . 
UA 8 HOH 224 2224 2224 HOH HOH C . 
UA 8 HOH 225 2225 2225 HOH HOH C . 
UA 8 HOH 226 2226 2226 HOH HOH C . 
UA 8 HOH 227 2227 2227 HOH HOH C . 
UA 8 HOH 228 2228 2228 HOH HOH C . 
UA 8 HOH 229 2229 2229 HOH HOH C . 
UA 8 HOH 230 2230 2230 HOH HOH C . 
UA 8 HOH 231 2231 2231 HOH HOH C . 
UA 8 HOH 232 2232 2232 HOH HOH C . 
UA 8 HOH 233 2233 2233 HOH HOH C . 
UA 8 HOH 234 2234 2234 HOH HOH C . 
UA 8 HOH 235 2235 2235 HOH HOH C . 
UA 8 HOH 236 2236 2236 HOH HOH C . 
UA 8 HOH 237 2237 2237 HOH HOH C . 
UA 8 HOH 238 2238 2238 HOH HOH C . 
UA 8 HOH 239 2239 2239 HOH HOH C . 
UA 8 HOH 240 2240 2240 HOH HOH C . 
UA 8 HOH 241 2241 2241 HOH HOH C . 
UA 8 HOH 242 2242 2242 HOH HOH C . 
UA 8 HOH 243 2243 2243 HOH HOH C . 
UA 8 HOH 244 2244 2244 HOH HOH C . 
UA 8 HOH 245 2245 2245 HOH HOH C . 
UA 8 HOH 246 2246 2246 HOH HOH C . 
UA 8 HOH 247 2247 2247 HOH HOH C . 
UA 8 HOH 248 2248 2248 HOH HOH C . 
UA 8 HOH 249 2249 2249 HOH HOH C . 
UA 8 HOH 250 2250 2250 HOH HOH C . 
UA 8 HOH 251 2251 2251 HOH HOH C . 
UA 8 HOH 252 2252 2252 HOH HOH C . 
UA 8 HOH 253 2253 2253 HOH HOH C . 
UA 8 HOH 254 2254 2254 HOH HOH C . 
UA 8 HOH 255 2255 2255 HOH HOH C . 
UA 8 HOH 256 2256 2256 HOH HOH C . 
UA 8 HOH 257 2257 2257 HOH HOH C . 
UA 8 HOH 258 2258 2258 HOH HOH C . 
UA 8 HOH 259 2259 2259 HOH HOH C . 
UA 8 HOH 260 2260 2260 HOH HOH C . 
UA 8 HOH 261 2261 2261 HOH HOH C . 
UA 8 HOH 262 2262 2262 HOH HOH C . 
UA 8 HOH 263 2263 2263 HOH HOH C . 
UA 8 HOH 264 2264 2264 HOH HOH C . 
UA 8 HOH 265 2265 2265 HOH HOH C . 
UA 8 HOH 266 2266 2266 HOH HOH C . 
UA 8 HOH 267 2267 2267 HOH HOH C . 
UA 8 HOH 268 2268 2268 HOH HOH C . 
UA 8 HOH 269 2269 2269 HOH HOH C . 
UA 8 HOH 270 2270 2270 HOH HOH C . 
UA 8 HOH 271 2271 2271 HOH HOH C . 
UA 8 HOH 272 2272 2272 HOH HOH C . 
UA 8 HOH 273 2273 2273 HOH HOH C . 
UA 8 HOH 274 2274 2274 HOH HOH C . 
UA 8 HOH 275 2275 2275 HOH HOH C . 
UA 8 HOH 276 2276 2276 HOH HOH C . 
UA 8 HOH 277 2277 2277 HOH HOH C . 
UA 8 HOH 278 2278 2278 HOH HOH C . 
UA 8 HOH 279 2279 2279 HOH HOH C . 
UA 8 HOH 280 2280 2280 HOH HOH C . 
UA 8 HOH 281 2281 2281 HOH HOH C . 
UA 8 HOH 282 2282 2282 HOH HOH C . 
UA 8 HOH 283 2283 2283 HOH HOH C . 
UA 8 HOH 284 2284 2284 HOH HOH C . 
UA 8 HOH 285 2285 2285 HOH HOH C . 
UA 8 HOH 286 2286 2286 HOH HOH C . 
UA 8 HOH 287 2287 2287 HOH HOH C . 
UA 8 HOH 288 2288 2288 HOH HOH C . 
UA 8 HOH 289 2289 2289 HOH HOH C . 
UA 8 HOH 290 2290 2290 HOH HOH C . 
UA 8 HOH 291 2291 2291 HOH HOH C . 
UA 8 HOH 292 2292 2292 HOH HOH C . 
UA 8 HOH 293 2293 2293 HOH HOH C . 
UA 8 HOH 294 2294 2294 HOH HOH C . 
UA 8 HOH 295 2295 2295 HOH HOH C . 
UA 8 HOH 296 2296 2296 HOH HOH C . 
UA 8 HOH 297 2297 2297 HOH HOH C . 
UA 8 HOH 298 2298 2298 HOH HOH C . 
UA 8 HOH 299 2299 2299 HOH HOH C . 
UA 8 HOH 300 2300 2300 HOH HOH C . 
UA 8 HOH 301 2301 2301 HOH HOH C . 
UA 8 HOH 302 2302 2302 HOH HOH C . 
UA 8 HOH 303 2303 2303 HOH HOH C . 
UA 8 HOH 304 2304 2304 HOH HOH C . 
UA 8 HOH 305 2305 2305 HOH HOH C . 
UA 8 HOH 306 2306 2306 HOH HOH C . 
UA 8 HOH 307 2307 2307 HOH HOH C . 
UA 8 HOH 308 2308 2308 HOH HOH C . 
UA 8 HOH 309 2309 2309 HOH HOH C . 
UA 8 HOH 310 2310 2310 HOH HOH C . 
UA 8 HOH 311 2311 2311 HOH HOH C . 
UA 8 HOH 312 2312 2312 HOH HOH C . 
UA 8 HOH 313 2313 2313 HOH HOH C . 
UA 8 HOH 314 2314 2314 HOH HOH C . 
UA 8 HOH 315 2315 2315 HOH HOH C . 
UA 8 HOH 316 2316 2316 HOH HOH C . 
UA 8 HOH 317 2317 2317 HOH HOH C . 
UA 8 HOH 318 2318 2318 HOH HOH C . 
UA 8 HOH 319 2319 2319 HOH HOH C . 
UA 8 HOH 320 2320 2320 HOH HOH C . 
UA 8 HOH 321 2321 2321 HOH HOH C . 
UA 8 HOH 322 2322 2322 HOH HOH C . 
UA 8 HOH 323 2323 2323 HOH HOH C . 
UA 8 HOH 324 2324 2324 HOH HOH C . 
UA 8 HOH 325 2325 2325 HOH HOH C . 
UA 8 HOH 326 2326 2326 HOH HOH C . 
UA 8 HOH 327 2327 2327 HOH HOH C . 
UA 8 HOH 328 2328 2328 HOH HOH C . 
UA 8 HOH 329 2329 2329 HOH HOH C . 
UA 8 HOH 330 2330 2330 HOH HOH C . 
UA 8 HOH 331 2331 2331 HOH HOH C . 
UA 8 HOH 332 2332 2332 HOH HOH C . 
UA 8 HOH 333 2333 2333 HOH HOH C . 
UA 8 HOH 334 2334 2334 HOH HOH C . 
UA 8 HOH 335 2335 2335 HOH HOH C . 
UA 8 HOH 336 2336 2336 HOH HOH C . 
UA 8 HOH 337 2337 2337 HOH HOH C . 
UA 8 HOH 338 2338 2338 HOH HOH C . 
UA 8 HOH 339 2339 2339 HOH HOH C . 
UA 8 HOH 340 2340 2340 HOH HOH C . 
UA 8 HOH 341 2341 2341 HOH HOH C . 
UA 8 HOH 342 2342 2342 HOH HOH C . 
UA 8 HOH 343 2343 2343 HOH HOH C . 
UA 8 HOH 344 2344 2344 HOH HOH C . 
UA 8 HOH 345 2345 2345 HOH HOH C . 
UA 8 HOH 346 2346 2346 HOH HOH C . 
UA 8 HOH 347 2347 2347 HOH HOH C . 
UA 8 HOH 348 2348 2348 HOH HOH C . 
UA 8 HOH 349 2349 2349 HOH HOH C . 
UA 8 HOH 350 2350 2350 HOH HOH C . 
UA 8 HOH 351 2351 2351 HOH HOH C . 
UA 8 HOH 352 2352 2352 HOH HOH C . 
UA 8 HOH 353 2353 2353 HOH HOH C . 
UA 8 HOH 354 2354 2354 HOH HOH C . 
UA 8 HOH 355 2355 2355 HOH HOH C . 
UA 8 HOH 356 2356 2356 HOH HOH C . 
UA 8 HOH 357 2357 2357 HOH HOH C . 
UA 8 HOH 358 2358 2358 HOH HOH C . 
UA 8 HOH 359 2359 2359 HOH HOH C . 
UA 8 HOH 360 2360 2360 HOH HOH C . 
UA 8 HOH 361 2361 2361 HOH HOH C . 
UA 8 HOH 362 2362 2362 HOH HOH C . 
UA 8 HOH 363 2363 2363 HOH HOH C . 
UA 8 HOH 364 2364 2364 HOH HOH C . 
UA 8 HOH 365 2365 2365 HOH HOH C . 
UA 8 HOH 366 2366 2366 HOH HOH C . 
UA 8 HOH 367 2367 2367 HOH HOH C . 
UA 8 HOH 368 2368 2368 HOH HOH C . 
UA 8 HOH 369 2369 2369 HOH HOH C . 
UA 8 HOH 370 2370 2370 HOH HOH C . 
UA 8 HOH 371 2371 2371 HOH HOH C . 
UA 8 HOH 372 2372 2372 HOH HOH C . 
UA 8 HOH 373 2373 2373 HOH HOH C . 
UA 8 HOH 374 2374 2374 HOH HOH C . 
UA 8 HOH 375 2375 2375 HOH HOH C . 
UA 8 HOH 376 2376 2376 HOH HOH C . 
UA 8 HOH 377 2377 2377 HOH HOH C . 
UA 8 HOH 378 2378 2378 HOH HOH C . 
UA 8 HOH 379 2379 2379 HOH HOH C . 
UA 8 HOH 380 2380 2380 HOH HOH C . 
UA 8 HOH 381 2381 2381 HOH HOH C . 
VA 8 HOH 1   2001 2001 HOH HOH D . 
VA 8 HOH 2   2002 2002 HOH HOH D . 
VA 8 HOH 3   2003 2003 HOH HOH D . 
VA 8 HOH 4   2004 2004 HOH HOH D . 
VA 8 HOH 5   2005 2005 HOH HOH D . 
VA 8 HOH 6   2006 2006 HOH HOH D . 
VA 8 HOH 7   2007 2007 HOH HOH D . 
VA 8 HOH 8   2008 2008 HOH HOH D . 
VA 8 HOH 9   2009 2009 HOH HOH D . 
VA 8 HOH 10  2010 2010 HOH HOH D . 
VA 8 HOH 11  2011 2011 HOH HOH D . 
VA 8 HOH 12  2012 2012 HOH HOH D . 
VA 8 HOH 13  2013 2013 HOH HOH D . 
VA 8 HOH 14  2014 2014 HOH HOH D . 
VA 8 HOH 15  2015 2015 HOH HOH D . 
VA 8 HOH 16  2016 2016 HOH HOH D . 
VA 8 HOH 17  2017 2017 HOH HOH D . 
VA 8 HOH 18  2018 2018 HOH HOH D . 
VA 8 HOH 19  2019 2019 HOH HOH D . 
VA 8 HOH 20  2020 2020 HOH HOH D . 
VA 8 HOH 21  2021 2021 HOH HOH D . 
VA 8 HOH 22  2022 2022 HOH HOH D . 
VA 8 HOH 23  2023 2023 HOH HOH D . 
VA 8 HOH 24  2024 2024 HOH HOH D . 
VA 8 HOH 25  2025 2025 HOH HOH D . 
VA 8 HOH 26  2026 2026 HOH HOH D . 
VA 8 HOH 27  2027 2027 HOH HOH D . 
VA 8 HOH 28  2028 2028 HOH HOH D . 
VA 8 HOH 29  2029 2029 HOH HOH D . 
VA 8 HOH 30  2030 2030 HOH HOH D . 
VA 8 HOH 31  2031 2031 HOH HOH D . 
VA 8 HOH 32  2032 2032 HOH HOH D . 
VA 8 HOH 33  2033 2033 HOH HOH D . 
VA 8 HOH 34  2034 2034 HOH HOH D . 
VA 8 HOH 35  2035 2035 HOH HOH D . 
VA 8 HOH 36  2036 2036 HOH HOH D . 
VA 8 HOH 37  2037 2037 HOH HOH D . 
VA 8 HOH 38  2038 2038 HOH HOH D . 
VA 8 HOH 39  2039 2039 HOH HOH D . 
VA 8 HOH 40  2040 2040 HOH HOH D . 
VA 8 HOH 41  2041 2041 HOH HOH D . 
VA 8 HOH 42  2042 2042 HOH HOH D . 
VA 8 HOH 43  2043 2043 HOH HOH D . 
VA 8 HOH 44  2044 2044 HOH HOH D . 
VA 8 HOH 45  2045 2045 HOH HOH D . 
VA 8 HOH 46  2046 2046 HOH HOH D . 
VA 8 HOH 47  2047 2047 HOH HOH D . 
VA 8 HOH 48  2048 2048 HOH HOH D . 
VA 8 HOH 49  2049 2049 HOH HOH D . 
VA 8 HOH 50  2050 2050 HOH HOH D . 
VA 8 HOH 51  2051 2051 HOH HOH D . 
VA 8 HOH 52  2052 2052 HOH HOH D . 
VA 8 HOH 53  2053 2053 HOH HOH D . 
VA 8 HOH 54  2054 2054 HOH HOH D . 
VA 8 HOH 55  2055 2055 HOH HOH D . 
VA 8 HOH 56  2056 2056 HOH HOH D . 
VA 8 HOH 57  2057 2057 HOH HOH D . 
VA 8 HOH 58  2058 2058 HOH HOH D . 
VA 8 HOH 59  2059 2059 HOH HOH D . 
VA 8 HOH 60  2060 2060 HOH HOH D . 
VA 8 HOH 61  2061 2061 HOH HOH D . 
VA 8 HOH 62  2062 2062 HOH HOH D . 
VA 8 HOH 63  2063 2063 HOH HOH D . 
VA 8 HOH 64  2064 2064 HOH HOH D . 
VA 8 HOH 65  2065 2065 HOH HOH D . 
VA 8 HOH 66  2066 2066 HOH HOH D . 
VA 8 HOH 67  2067 2067 HOH HOH D . 
VA 8 HOH 68  2068 2068 HOH HOH D . 
VA 8 HOH 69  2069 2069 HOH HOH D . 
VA 8 HOH 70  2070 2070 HOH HOH D . 
VA 8 HOH 71  2071 2071 HOH HOH D . 
VA 8 HOH 72  2072 2072 HOH HOH D . 
VA 8 HOH 73  2073 2073 HOH HOH D . 
VA 8 HOH 74  2074 2074 HOH HOH D . 
VA 8 HOH 75  2075 2075 HOH HOH D . 
VA 8 HOH 76  2076 2076 HOH HOH D . 
VA 8 HOH 77  2077 2077 HOH HOH D . 
VA 8 HOH 78  2078 2078 HOH HOH D . 
VA 8 HOH 79  2079 2079 HOH HOH D . 
VA 8 HOH 80  2080 2080 HOH HOH D . 
VA 8 HOH 81  2081 2081 HOH HOH D . 
VA 8 HOH 82  2082 2082 HOH HOH D . 
VA 8 HOH 83  2083 2083 HOH HOH D . 
VA 8 HOH 84  2084 2084 HOH HOH D . 
VA 8 HOH 85  2085 2085 HOH HOH D . 
VA 8 HOH 86  2086 2086 HOH HOH D . 
VA 8 HOH 87  2087 2087 HOH HOH D . 
VA 8 HOH 88  2088 2088 HOH HOH D . 
VA 8 HOH 89  2089 2089 HOH HOH D . 
VA 8 HOH 90  2090 2090 HOH HOH D . 
VA 8 HOH 91  2091 2091 HOH HOH D . 
VA 8 HOH 92  2092 2092 HOH HOH D . 
VA 8 HOH 93  2093 2093 HOH HOH D . 
VA 8 HOH 94  2094 2094 HOH HOH D . 
VA 8 HOH 95  2095 2095 HOH HOH D . 
VA 8 HOH 96  2096 2096 HOH HOH D . 
VA 8 HOH 97  2097 2097 HOH HOH D . 
VA 8 HOH 98  2098 2098 HOH HOH D . 
VA 8 HOH 99  2099 2099 HOH HOH D . 
VA 8 HOH 100 2100 2100 HOH HOH D . 
VA 8 HOH 101 2101 2101 HOH HOH D . 
VA 8 HOH 102 2102 2102 HOH HOH D . 
VA 8 HOH 103 2103 2103 HOH HOH D . 
VA 8 HOH 104 2104 2104 HOH HOH D . 
VA 8 HOH 105 2105 2105 HOH HOH D . 
VA 8 HOH 106 2106 2106 HOH HOH D . 
VA 8 HOH 107 2107 2107 HOH HOH D . 
VA 8 HOH 108 2108 2108 HOH HOH D . 
VA 8 HOH 109 2109 2109 HOH HOH D . 
VA 8 HOH 110 2110 2110 HOH HOH D . 
VA 8 HOH 111 2111 2111 HOH HOH D . 
VA 8 HOH 112 2112 2112 HOH HOH D . 
VA 8 HOH 113 2113 2113 HOH HOH D . 
VA 8 HOH 114 2114 2114 HOH HOH D . 
VA 8 HOH 115 2115 2115 HOH HOH D . 
VA 8 HOH 116 2116 2116 HOH HOH D . 
VA 8 HOH 117 2117 2117 HOH HOH D . 
VA 8 HOH 118 2118 2118 HOH HOH D . 
VA 8 HOH 119 2119 2119 HOH HOH D . 
VA 8 HOH 120 2120 2120 HOH HOH D . 
VA 8 HOH 121 2121 2121 HOH HOH D . 
VA 8 HOH 122 2122 2122 HOH HOH D . 
VA 8 HOH 123 2123 2123 HOH HOH D . 
VA 8 HOH 124 2124 2124 HOH HOH D . 
VA 8 HOH 125 2125 2125 HOH HOH D . 
VA 8 HOH 126 2126 2126 HOH HOH D . 
VA 8 HOH 127 2127 2127 HOH HOH D . 
VA 8 HOH 128 2128 2128 HOH HOH D . 
VA 8 HOH 129 2129 2129 HOH HOH D . 
VA 8 HOH 130 2130 2130 HOH HOH D . 
VA 8 HOH 131 2131 2131 HOH HOH D . 
VA 8 HOH 132 2132 2132 HOH HOH D . 
VA 8 HOH 133 2133 2133 HOH HOH D . 
VA 8 HOH 134 2134 2134 HOH HOH D . 
VA 8 HOH 135 2135 2135 HOH HOH D . 
VA 8 HOH 136 2136 2136 HOH HOH D . 
VA 8 HOH 137 2137 2137 HOH HOH D . 
VA 8 HOH 138 2138 2138 HOH HOH D . 
VA 8 HOH 139 2139 2139 HOH HOH D . 
VA 8 HOH 140 2140 2140 HOH HOH D . 
VA 8 HOH 141 2141 2141 HOH HOH D . 
VA 8 HOH 142 2142 2142 HOH HOH D . 
VA 8 HOH 143 2143 2143 HOH HOH D . 
VA 8 HOH 144 2144 2144 HOH HOH D . 
VA 8 HOH 145 2145 2145 HOH HOH D . 
VA 8 HOH 146 2146 2146 HOH HOH D . 
VA 8 HOH 147 2147 2147 HOH HOH D . 
VA 8 HOH 148 2148 2148 HOH HOH D . 
VA 8 HOH 149 2149 2149 HOH HOH D . 
VA 8 HOH 150 2150 2150 HOH HOH D . 
VA 8 HOH 151 2151 2151 HOH HOH D . 
VA 8 HOH 152 2152 2152 HOH HOH D . 
VA 8 HOH 153 2153 2153 HOH HOH D . 
VA 8 HOH 154 2154 2154 HOH HOH D . 
VA 8 HOH 155 2155 2155 HOH HOH D . 
VA 8 HOH 156 2156 2156 HOH HOH D . 
VA 8 HOH 157 2157 2157 HOH HOH D . 
VA 8 HOH 158 2158 2158 HOH HOH D . 
VA 8 HOH 159 2159 2159 HOH HOH D . 
VA 8 HOH 160 2160 2160 HOH HOH D . 
VA 8 HOH 161 2161 2161 HOH HOH D . 
VA 8 HOH 162 2162 2162 HOH HOH D . 
VA 8 HOH 163 2163 2163 HOH HOH D . 
VA 8 HOH 164 2164 2164 HOH HOH D . 
VA 8 HOH 165 2165 2165 HOH HOH D . 
VA 8 HOH 166 2166 2166 HOH HOH D . 
VA 8 HOH 167 2167 2167 HOH HOH D . 
VA 8 HOH 168 2168 2168 HOH HOH D . 
VA 8 HOH 169 2169 2169 HOH HOH D . 
VA 8 HOH 170 2170 2170 HOH HOH D . 
VA 8 HOH 171 2171 2171 HOH HOH D . 
VA 8 HOH 172 2172 2172 HOH HOH D . 
VA 8 HOH 173 2173 2173 HOH HOH D . 
VA 8 HOH 174 2174 2174 HOH HOH D . 
VA 8 HOH 175 2175 2175 HOH HOH D . 
VA 8 HOH 176 2176 2176 HOH HOH D . 
VA 8 HOH 177 2177 2177 HOH HOH D . 
VA 8 HOH 178 2178 2178 HOH HOH D . 
VA 8 HOH 179 2179 2179 HOH HOH D . 
VA 8 HOH 180 2180 2180 HOH HOH D . 
VA 8 HOH 181 2181 2181 HOH HOH D . 
VA 8 HOH 182 2182 2182 HOH HOH D . 
VA 8 HOH 183 2183 2183 HOH HOH D . 
VA 8 HOH 184 2184 2184 HOH HOH D . 
VA 8 HOH 185 2185 2185 HOH HOH D . 
VA 8 HOH 186 2186 2186 HOH HOH D . 
VA 8 HOH 187 2187 2187 HOH HOH D . 
VA 8 HOH 188 2188 2188 HOH HOH D . 
VA 8 HOH 189 2189 2189 HOH HOH D . 
VA 8 HOH 190 2190 2190 HOH HOH D . 
VA 8 HOH 191 2191 2191 HOH HOH D . 
VA 8 HOH 192 2192 2192 HOH HOH D . 
VA 8 HOH 193 2193 2193 HOH HOH D . 
VA 8 HOH 194 2194 2194 HOH HOH D . 
VA 8 HOH 195 2195 2195 HOH HOH D . 
VA 8 HOH 196 2196 2196 HOH HOH D . 
VA 8 HOH 197 2197 2197 HOH HOH D . 
VA 8 HOH 198 2198 2198 HOH HOH D . 
VA 8 HOH 199 2199 2199 HOH HOH D . 
VA 8 HOH 200 2200 2200 HOH HOH D . 
VA 8 HOH 201 2201 2201 HOH HOH D . 
VA 8 HOH 202 2202 2202 HOH HOH D . 
VA 8 HOH 203 2203 2203 HOH HOH D . 
VA 8 HOH 204 2204 2204 HOH HOH D . 
VA 8 HOH 205 2205 2205 HOH HOH D . 
VA 8 HOH 206 2206 2206 HOH HOH D . 
VA 8 HOH 207 2207 2207 HOH HOH D . 
VA 8 HOH 208 2208 2208 HOH HOH D . 
VA 8 HOH 209 2209 2209 HOH HOH D . 
VA 8 HOH 210 2210 2210 HOH HOH D . 
VA 8 HOH 211 2211 2211 HOH HOH D . 
VA 8 HOH 212 2212 2212 HOH HOH D . 
VA 8 HOH 213 2213 2213 HOH HOH D . 
VA 8 HOH 214 2214 2214 HOH HOH D . 
VA 8 HOH 215 2215 2215 HOH HOH D . 
VA 8 HOH 216 2216 2216 HOH HOH D . 
VA 8 HOH 217 2217 2217 HOH HOH D . 
VA 8 HOH 218 2218 2218 HOH HOH D . 
VA 8 HOH 219 2219 2219 HOH HOH D . 
VA 8 HOH 220 2220 2220 HOH HOH D . 
VA 8 HOH 221 2221 2221 HOH HOH D . 
VA 8 HOH 222 2222 2222 HOH HOH D . 
VA 8 HOH 223 2223 2223 HOH HOH D . 
VA 8 HOH 224 2224 2224 HOH HOH D . 
VA 8 HOH 225 2225 2225 HOH HOH D . 
VA 8 HOH 226 2226 2226 HOH HOH D . 
VA 8 HOH 227 2227 2227 HOH HOH D . 
VA 8 HOH 228 2228 2228 HOH HOH D . 
VA 8 HOH 229 2229 2229 HOH HOH D . 
VA 8 HOH 230 2230 2230 HOH HOH D . 
VA 8 HOH 231 2231 2231 HOH HOH D . 
VA 8 HOH 232 2232 2232 HOH HOH D . 
VA 8 HOH 233 2233 2233 HOH HOH D . 
VA 8 HOH 234 2234 2234 HOH HOH D . 
VA 8 HOH 235 2235 2235 HOH HOH D . 
VA 8 HOH 236 2236 2236 HOH HOH D . 
VA 8 HOH 237 2237 2237 HOH HOH D . 
VA 8 HOH 238 2238 2238 HOH HOH D . 
VA 8 HOH 239 2239 2239 HOH HOH D . 
VA 8 HOH 240 2240 2240 HOH HOH D . 
VA 8 HOH 241 2241 2241 HOH HOH D . 
VA 8 HOH 242 2242 2242 HOH HOH D . 
VA 8 HOH 243 2243 2243 HOH HOH D . 
VA 8 HOH 244 2244 2244 HOH HOH D . 
VA 8 HOH 245 2245 2245 HOH HOH D . 
VA 8 HOH 246 2246 2246 HOH HOH D . 
VA 8 HOH 247 2247 2247 HOH HOH D . 
VA 8 HOH 248 2248 2248 HOH HOH D . 
VA 8 HOH 249 2249 2249 HOH HOH D . 
VA 8 HOH 250 2250 2250 HOH HOH D . 
VA 8 HOH 251 2251 2251 HOH HOH D . 
VA 8 HOH 252 2252 2252 HOH HOH D . 
VA 8 HOH 253 2253 2253 HOH HOH D . 
VA 8 HOH 254 2254 2254 HOH HOH D . 
VA 8 HOH 255 2255 2255 HOH HOH D . 
VA 8 HOH 256 2256 2256 HOH HOH D . 
VA 8 HOH 257 2257 2257 HOH HOH D . 
VA 8 HOH 258 2258 2258 HOH HOH D . 
VA 8 HOH 259 2259 2259 HOH HOH D . 
VA 8 HOH 260 2260 2260 HOH HOH D . 
VA 8 HOH 261 2261 2261 HOH HOH D . 
VA 8 HOH 262 2262 2262 HOH HOH D . 
VA 8 HOH 263 2263 2263 HOH HOH D . 
VA 8 HOH 264 2264 2264 HOH HOH D . 
VA 8 HOH 265 2265 2265 HOH HOH D . 
VA 8 HOH 266 2266 2266 HOH HOH D . 
VA 8 HOH 267 2267 2267 HOH HOH D . 
VA 8 HOH 268 2268 2268 HOH HOH D . 
VA 8 HOH 269 2269 2269 HOH HOH D . 
VA 8 HOH 270 2270 2270 HOH HOH D . 
VA 8 HOH 271 2271 2271 HOH HOH D . 
VA 8 HOH 272 2272 2272 HOH HOH D . 
VA 8 HOH 273 2273 2273 HOH HOH D . 
VA 8 HOH 274 2274 2274 HOH HOH D . 
VA 8 HOH 275 2275 2275 HOH HOH D . 
VA 8 HOH 276 2276 2276 HOH HOH D . 
VA 8 HOH 277 2277 2277 HOH HOH D . 
VA 8 HOH 278 2278 2278 HOH HOH D . 
VA 8 HOH 279 2279 2279 HOH HOH D . 
VA 8 HOH 280 2280 2280 HOH HOH D . 
VA 8 HOH 281 2281 2281 HOH HOH D . 
VA 8 HOH 282 2282 2282 HOH HOH D . 
VA 8 HOH 283 2283 2283 HOH HOH D . 
VA 8 HOH 284 2284 2284 HOH HOH D . 
VA 8 HOH 285 2285 2285 HOH HOH D . 
VA 8 HOH 286 2286 2286 HOH HOH D . 
VA 8 HOH 287 2287 2287 HOH HOH D . 
VA 8 HOH 288 2288 2288 HOH HOH D . 
VA 8 HOH 289 2289 2289 HOH HOH D . 
VA 8 HOH 290 2290 2290 HOH HOH D . 
VA 8 HOH 291 2291 2291 HOH HOH D . 
VA 8 HOH 292 2292 2292 HOH HOH D . 
VA 8 HOH 293 2293 2293 HOH HOH D . 
VA 8 HOH 294 2294 2294 HOH HOH D . 
VA 8 HOH 295 2295 2295 HOH HOH D . 
VA 8 HOH 296 2296 2296 HOH HOH D . 
VA 8 HOH 297 2297 2297 HOH HOH D . 
VA 8 HOH 298 2298 2298 HOH HOH D . 
VA 8 HOH 299 2299 2299 HOH HOH D . 
VA 8 HOH 300 2300 2300 HOH HOH D . 
VA 8 HOH 301 2301 2301 HOH HOH D . 
VA 8 HOH 302 2302 2302 HOH HOH D . 
VA 8 HOH 303 2303 2303 HOH HOH D . 
VA 8 HOH 304 2304 2304 HOH HOH D . 
VA 8 HOH 305 2305 2305 HOH HOH D . 
VA 8 HOH 306 2306 2306 HOH HOH D . 
VA 8 HOH 307 2307 2307 HOH HOH D . 
VA 8 HOH 308 2308 2308 HOH HOH D . 
VA 8 HOH 309 2309 2309 HOH HOH D . 
VA 8 HOH 310 2310 2310 HOH HOH D . 
VA 8 HOH 311 2311 2311 HOH HOH D . 
VA 8 HOH 312 2312 2312 HOH HOH D . 
VA 8 HOH 313 2313 2313 HOH HOH D . 
VA 8 HOH 314 2314 2314 HOH HOH D . 
VA 8 HOH 315 2315 2315 HOH HOH D . 
VA 8 HOH 316 2316 2316 HOH HOH D . 
VA 8 HOH 317 2317 2317 HOH HOH D . 
VA 8 HOH 318 2318 2318 HOH HOH D . 
VA 8 HOH 319 2319 2319 HOH HOH D . 
VA 8 HOH 320 2320 2320 HOH HOH D . 
VA 8 HOH 321 2321 2321 HOH HOH D . 
VA 8 HOH 322 2322 2322 HOH HOH D . 
VA 8 HOH 323 2323 2323 HOH HOH D . 
VA 8 HOH 324 2324 2324 HOH HOH D . 
VA 8 HOH 325 2325 2325 HOH HOH D . 
VA 8 HOH 326 2326 2326 HOH HOH D . 
VA 8 HOH 327 2327 2327 HOH HOH D . 
VA 8 HOH 328 2328 2328 HOH HOH D . 
VA 8 HOH 329 2329 2329 HOH HOH D . 
VA 8 HOH 330 2330 2330 HOH HOH D . 
VA 8 HOH 331 2331 2331 HOH HOH D . 
VA 8 HOH 332 2332 2332 HOH HOH D . 
VA 8 HOH 333 2333 2333 HOH HOH D . 
VA 8 HOH 334 2334 2334 HOH HOH D . 
VA 8 HOH 335 2335 2335 HOH HOH D . 
VA 8 HOH 336 2336 2336 HOH HOH D . 
VA 8 HOH 337 2337 2337 HOH HOH D . 
VA 8 HOH 338 2338 2338 HOH HOH D . 
VA 8 HOH 339 2339 2339 HOH HOH D . 
VA 8 HOH 340 2340 2340 HOH HOH D . 
VA 8 HOH 341 2341 2341 HOH HOH D . 
VA 8 HOH 342 2342 2342 HOH HOH D . 
VA 8 HOH 343 2343 2343 HOH HOH D . 
VA 8 HOH 344 2344 2344 HOH HOH D . 
VA 8 HOH 345 2345 2345 HOH HOH D . 
VA 8 HOH 346 2346 2346 HOH HOH D . 
VA 8 HOH 347 2347 2347 HOH HOH D . 
VA 8 HOH 348 2348 2348 HOH HOH D . 
VA 8 HOH 349 2349 2349 HOH HOH D . 
VA 8 HOH 350 2350 2350 HOH HOH D . 
VA 8 HOH 351 2351 2351 HOH HOH D . 
VA 8 HOH 352 2352 2352 HOH HOH D . 
VA 8 HOH 353 2353 2353 HOH HOH D . 
VA 8 HOH 354 2354 2354 HOH HOH D . 
VA 8 HOH 355 2355 2355 HOH HOH D . 
VA 8 HOH 356 2356 2356 HOH HOH D . 
VA 8 HOH 357 2357 2357 HOH HOH D . 
VA 8 HOH 358 2358 2358 HOH HOH D . 
VA 8 HOH 359 2359 2359 HOH HOH D . 
VA 8 HOH 360 2360 2360 HOH HOH D . 
VA 8 HOH 361 2361 2361 HOH HOH D . 
VA 8 HOH 362 2362 2362 HOH HOH D . 
VA 8 HOH 363 2363 2363 HOH HOH D . 
# 
loop_
_pdbx_struct_mod_residue.id 
_pdbx_struct_mod_residue.label_asym_id 
_pdbx_struct_mod_residue.label_comp_id 
_pdbx_struct_mod_residue.label_seq_id 
_pdbx_struct_mod_residue.auth_asym_id 
_pdbx_struct_mod_residue.auth_comp_id 
_pdbx_struct_mod_residue.auth_seq_id 
_pdbx_struct_mod_residue.PDB_ins_code 
_pdbx_struct_mod_residue.parent_comp_id 
_pdbx_struct_mod_residue.details 
1  A ASN 90  A ASN 90  ? ASN 'GLYCOSYLATION SITE' 
2  A ASN 109 A ASN 109 ? ASN 'GLYCOSYLATION SITE' 
3  A ASN 142 A ASN 142 ? ASN 'GLYCOSYLATION SITE' 
4  A ASN 191 A ASN 191 ? ASN 'GLYCOSYLATION SITE' 
5  A ASN 248 A ASN 248 ? ASN 'GLYCOSYLATION SITE' 
6  B ASN 109 B ASN 109 ? ASN 'GLYCOSYLATION SITE' 
7  B ASN 142 B ASN 142 ? ASN 'GLYCOSYLATION SITE' 
8  B ASN 191 B ASN 191 ? ASN 'GLYCOSYLATION SITE' 
9  B ASN 248 B ASN 248 ? ASN 'GLYCOSYLATION SITE' 
10 C ASN 109 C ASN 109 ? ASN 'GLYCOSYLATION SITE' 
11 C ASN 142 C ASN 142 ? ASN 'GLYCOSYLATION SITE' 
12 C ASN 191 C ASN 191 ? ASN 'GLYCOSYLATION SITE' 
13 C ASN 248 C ASN 248 ? ASN 'GLYCOSYLATION SITE' 
14 D ASN 109 D ASN 109 ? ASN 'GLYCOSYLATION SITE' 
15 D ASN 142 D ASN 142 ? ASN 'GLYCOSYLATION SITE' 
16 D ASN 191 D ASN 191 ? ASN 'GLYCOSYLATION SITE' 
17 D ASN 248 D ASN 248 ? ASN 'GLYCOSYLATION SITE' 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_and_software_defined_assembly PISA dimeric 2 
2 author_and_software_defined_assembly PISA dimeric 2 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,E,F,G,H,I,J,K,L,M,N,O,P,BA,CA,DA,EA,FA,GA,HA,IA,JA,KA,SA,UA 
2 1 B,D,Q,R,S,T,U,V,W,X,Y,Z,AA,LA,MA,NA,OA,PA,QA,RA,TA,VA           
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 10520 ? 
1 MORE         -37.4 ? 
1 'SSA (A^2)'  24330 ? 
2 'ABSA (A^2)' 9670  ? 
2 MORE         -43.7 ? 
2 'SSA (A^2)'  23880 ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  O27 ? N  KMP .   ? A KMP 1360 ? 1_555 CU ? O  CU . ? A CU 1361 ? 1_555 NE2 ? A  HIS 112 ? A HIS 112  ? 1_555 148.8 ? 
2  O27 ? N  KMP .   ? A KMP 1360 ? 1_555 CU ? O  CU . ? A CU 1361 ? 1_555 NE2 ? A  HIS 66  ? A HIS 66   ? 1_555 103.4 ? 
3  NE2 ? A  HIS 112 ? A HIS 112  ? 1_555 CU ? O  CU . ? A CU 1361 ? 1_555 NE2 ? A  HIS 66  ? A HIS 66   ? 1_555 94.3  ? 
4  O27 ? N  KMP .   ? A KMP 1360 ? 1_555 CU ? O  CU . ? A CU 1361 ? 1_555 OE1 ? A  GLU 73  ? A GLU 73   ? 1_555 78.2  ? 
5  NE2 ? A  HIS 112 ? A HIS 112  ? 1_555 CU ? O  CU . ? A CU 1361 ? 1_555 OE1 ? A  GLU 73  ? A GLU 73   ? 1_555 81.2  ? 
6  NE2 ? A  HIS 66  ? A HIS 66   ? 1_555 CU ? O  CU . ? A CU 1361 ? 1_555 OE1 ? A  GLU 73  ? A GLU 73   ? 1_555 172.7 ? 
7  O27 ? N  KMP .   ? A KMP 1360 ? 1_555 CU ? O  CU . ? A CU 1361 ? 1_555 NE2 ? A  HIS 68  ? A HIS 68   ? 1_555 94.4  ? 
8  NE2 ? A  HIS 112 ? A HIS 112  ? 1_555 CU ? O  CU . ? A CU 1361 ? 1_555 NE2 ? A  HIS 68  ? A HIS 68   ? 1_555 105.6 ? 
9  NE2 ? A  HIS 66  ? A HIS 66   ? 1_555 CU ? O  CU . ? A CU 1361 ? 1_555 NE2 ? A  HIS 68  ? A HIS 68   ? 1_555 105.2 ? 
10 OE1 ? A  GLU 73  ? A GLU 73   ? 1_555 CU ? O  CU . ? A CU 1361 ? 1_555 NE2 ? A  HIS 68  ? A HIS 68   ? 1_555 81.6  ? 
11 O27 ? X  KMP .   ? B KMP 1358 ? 1_555 CU ? Y  CU . ? B CU 1359 ? 1_555 NE2 ? B  HIS 112 ? B HIS 112  ? 1_555 145.9 ? 
12 O27 ? X  KMP .   ? B KMP 1358 ? 1_555 CU ? Y  CU . ? B CU 1359 ? 1_555 NE2 ? B  HIS 68  ? B HIS 68   ? 1_555 102.3 ? 
13 NE2 ? B  HIS 112 ? B HIS 112  ? 1_555 CU ? Y  CU . ? B CU 1359 ? 1_555 NE2 ? B  HIS 68  ? B HIS 68   ? 1_555 99.2  ? 
14 O27 ? X  KMP .   ? B KMP 1358 ? 1_555 CU ? Y  CU . ? B CU 1359 ? 1_555 NE2 ? B  HIS 66  ? B HIS 66   ? 1_555 104.3 ? 
15 NE2 ? B  HIS 112 ? B HIS 112  ? 1_555 CU ? Y  CU . ? B CU 1359 ? 1_555 NE2 ? B  HIS 66  ? B HIS 66   ? 1_555 93.9  ? 
16 NE2 ? B  HIS 68  ? B HIS 68   ? 1_555 CU ? Y  CU . ? B CU 1359 ? 1_555 NE2 ? B  HIS 66  ? B HIS 66   ? 1_555 107.8 ? 
17 O27 ? X  KMP .   ? B KMP 1358 ? 1_555 CU ? Y  CU . ? B CU 1359 ? 1_555 OE1 ? B  GLU 73  ? B GLU 73   ? 1_555 79.5  ? 
18 NE2 ? B  HIS 112 ? B HIS 112  ? 1_555 CU ? Y  CU . ? B CU 1359 ? 1_555 OE1 ? B  GLU 73  ? B GLU 73   ? 1_555 79.3  ? 
19 NE2 ? B  HIS 68  ? B HIS 68   ? 1_555 CU ? Y  CU . ? B CU 1359 ? 1_555 OE1 ? B  GLU 73  ? B GLU 73   ? 1_555 78.1  ? 
20 NE2 ? B  HIS 66  ? B HIS 66   ? 1_555 CU ? Y  CU . ? B CU 1359 ? 1_555 OE1 ? B  GLU 73  ? B GLU 73   ? 1_555 171.8 ? 
21 NE2 ? C  HIS 112 ? C HIS 112  ? 1_555 CU ? JA CU . ? C CU 1359 ? 1_555 NE2 ? C  HIS 68  ? C HIS 68   ? 1_555 103.8 ? 
22 NE2 ? C  HIS 112 ? C HIS 112  ? 1_555 CU ? JA CU . ? C CU 1359 ? 1_555 O27 ? IA KMP .   ? C KMP 1358 ? 1_555 147.5 ? 
23 NE2 ? C  HIS 68  ? C HIS 68   ? 1_555 CU ? JA CU . ? C CU 1359 ? 1_555 O27 ? IA KMP .   ? C KMP 1358 ? 1_555 96.7  ? 
24 NE2 ? C  HIS 112 ? C HIS 112  ? 1_555 CU ? JA CU . ? C CU 1359 ? 1_555 OE1 ? C  GLU 73  ? C GLU 73   ? 1_555 80.9  ? 
25 NE2 ? C  HIS 68  ? C HIS 68   ? 1_555 CU ? JA CU . ? C CU 1359 ? 1_555 OE1 ? C  GLU 73  ? C GLU 73   ? 1_555 74.6  ? 
26 O27 ? IA KMP .   ? C KMP 1358 ? 1_555 CU ? JA CU . ? C CU 1359 ? 1_555 OE1 ? C  GLU 73  ? C GLU 73   ? 1_555 80.7  ? 
27 NE2 ? C  HIS 112 ? C HIS 112  ? 1_555 CU ? JA CU . ? C CU 1359 ? 1_555 NE2 ? C  HIS 66  ? C HIS 66   ? 1_555 91.9  ? 
28 NE2 ? C  HIS 68  ? C HIS 68   ? 1_555 CU ? JA CU . ? C CU 1359 ? 1_555 NE2 ? C  HIS 66  ? C HIS 66   ? 1_555 99.3  ? 
29 O27 ? IA KMP .   ? C KMP 1358 ? 1_555 CU ? JA CU . ? C CU 1359 ? 1_555 NE2 ? C  HIS 66  ? C HIS 66   ? 1_555 109.4 ? 
30 OE1 ? C  GLU 73  ? C GLU 73   ? 1_555 CU ? JA CU . ? C CU 1359 ? 1_555 NE2 ? C  HIS 66  ? C HIS 66   ? 1_555 169.1 ? 
31 O27 ? QA KMP .   ? D KMP 1356 ? 1_555 CU ? RA CU . ? D CU 1357 ? 1_555 NE2 ? D  HIS 66  ? D HIS 66   ? 1_555 105.8 ? 
32 O27 ? QA KMP .   ? D KMP 1356 ? 1_555 CU ? RA CU . ? D CU 1357 ? 1_555 NE2 ? D  HIS 112 ? D HIS 112  ? 1_555 151.5 ? 
33 NE2 ? D  HIS 66  ? D HIS 66   ? 1_555 CU ? RA CU . ? D CU 1357 ? 1_555 NE2 ? D  HIS 112 ? D HIS 112  ? 1_555 94.0  ? 
34 O27 ? QA KMP .   ? D KMP 1356 ? 1_555 CU ? RA CU . ? D CU 1357 ? 1_555 OE1 ? D  GLU 73  ? D GLU 73   ? 1_555 74.3  ? 
35 NE2 ? D  HIS 66  ? D HIS 66   ? 1_555 CU ? RA CU . ? D CU 1357 ? 1_555 OE1 ? D  GLU 73  ? D GLU 73   ? 1_555 179.0 ? 
36 NE2 ? D  HIS 112 ? D HIS 112  ? 1_555 CU ? RA CU . ? D CU 1357 ? 1_555 OE1 ? D  GLU 73  ? D GLU 73   ? 1_555 85.5  ? 
37 O27 ? QA KMP .   ? D KMP 1356 ? 1_555 CU ? RA CU . ? D CU 1357 ? 1_555 NE2 ? D  HIS 68  ? D HIS 68   ? 1_555 92.4  ? 
38 NE2 ? D  HIS 66  ? D HIS 66   ? 1_555 CU ? RA CU . ? D CU 1357 ? 1_555 NE2 ? D  HIS 68  ? D HIS 68   ? 1_555 97.3  ? 
39 NE2 ? D  HIS 112 ? D HIS 112  ? 1_555 CU ? RA CU . ? D CU 1357 ? 1_555 NE2 ? D  HIS 68  ? D HIS 68   ? 1_555 105.4 ? 
40 OE1 ? D  GLU 73  ? D GLU 73   ? 1_555 CU ? RA CU . ? D CU 1357 ? 1_555 NE2 ? D  HIS 68  ? D HIS 68   ? 1_555 83.7  ? 
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2002-11-28 
2 'Structure model' 1 1 2011-07-13 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' Advisory                    
2 2 'Structure model' 'Version format compliance' 
# 
loop_
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][3] 
'X-RAY DIFFRACTION' 1 ? refined 67.5487 13.7396 71.3325 0.0284 0.0513 0.0670 -0.0132 -0.0195 0.0159  0.4621 0.7445 1.0146 0.0537  
0.0897  0.1688  0.0050  -0.0718 -0.0482 0.0956  -0.0386 -0.0449 0.0293  0.0104  0.0336  
'X-RAY DIFFRACTION' 2 ? refined 57.7631 15.6140 59.9435 0.0038 0.0372 0.0512 -0.0045 -0.0129 -0.0005 0.5528 1.0819 1.0087 0.0100  
-0.1621 0.1554  0.0077  -0.0246 -0.0041 -0.0304 -0.0094 0.0368  0.0179  -0.1131 0.0018  
'X-RAY DIFFRACTION' 3 ? refined 86.3080 25.8196 9.5432  0.0672 0.0922 0.0737 0.0025  0.0025  -0.0011 0.6622 0.4458 0.7799 0.0466  
-0.3660 -0.1261 -0.0173 -0.1377 0.0643  0.1241  0.0157  0.0600  -0.0517 0.0368  0.0016  
'X-RAY DIFFRACTION' 4 ? refined 92.4932 15.1078 0.9037  0.0373 0.0828 0.0614 0.0277  -0.0040 0.0172  0.5842 0.8641 1.2396 0.2171  
-0.0184 0.1000  -0.0326 -0.1122 -0.0160 0.1039  0.0500  0.0136  0.0650  0.1087  -0.0175 
'X-RAY DIFFRACTION' 5 ? refined 75.8670 10.6347 37.3640 0.0993 0.0466 0.0828 0.0250  0.0214  -0.0030 0.7890 0.2950 1.2057 0.0526  
-0.1641 -0.2053 -0.0214 0.0874  -0.0952 -0.1798 -0.0241 -0.0373 0.1584  0.0865  0.0455  
'X-RAY DIFFRACTION' 6 ? refined 85.6478 14.3433 48.2123 0.0246 0.0837 0.1053 0.0280  0.0084  0.0301  0.6999 1.1092 1.5145 0.0292  
-0.2666 -0.1424 0.0175  0.0140  -0.0271 -0.0661 -0.0566 -0.1503 0.0734  0.2361  0.0391  
'X-RAY DIFFRACTION' 7 ? refined 22.1229 -0.8799 25.4187 0.0684 0.0562 0.0693 -0.0056 -0.0155 -0.0173 0.3155 0.9722 1.0725 -0.0813 
-0.0664 -0.4053 0.0089  -0.0828 0.0264  0.1561  0.0129  0.0362  -0.1529 -0.0459 -0.0218 
'X-RAY DIFFRACTION' 8 ? refined 32.6522 6.0072  16.9660 0.0686 0.0538 0.0819 -0.0428 -0.0254 -0.0171 0.7416 0.9612 1.4378 -0.1582 
0.1022  -0.1473 0.0283  -0.0420 0.0496  0.0945  -0.0142 -0.0999 -0.1798 0.1212  -0.0141 
# 
loop_
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
'X-RAY DIFFRACTION' 1  1 A 3    ? ? A 154  ? ? ? ? 
'X-RAY DIFFRACTION' 2  1 A 1361 ? ? A 1361 ? ? ? ? 
'X-RAY DIFFRACTION' 3  1 A 1360 ? ? A 1360 ? ? ? ? 
'X-RAY DIFFRACTION' 4  2 A 159  ? ? A 350  ? ? ? ? 
'X-RAY DIFFRACTION' 5  3 B 3    ? ? B 154  ? ? ? ? 
'X-RAY DIFFRACTION' 6  3 B 1359 ? ? B 1359 ? ? ? ? 
'X-RAY DIFFRACTION' 7  3 B 1358 ? ? B 1358 ? ? ? ? 
'X-RAY DIFFRACTION' 8  4 B 159  ? ? B 350  ? ? ? ? 
'X-RAY DIFFRACTION' 9  5 C 3    ? ? C 153  ? ? ? ? 
'X-RAY DIFFRACTION' 10 5 C 1359 ? ? C 1359 ? ? ? ? 
'X-RAY DIFFRACTION' 11 5 C 1358 ? ? C 1358 ? ? ? ? 
'X-RAY DIFFRACTION' 12 6 C 159  ? ? C 350  ? ? ? ? 
'X-RAY DIFFRACTION' 13 7 D 4    ? ? D 154  ? ? ? ? 
'X-RAY DIFFRACTION' 14 7 D 1357 ? ? D 1357 ? ? ? ? 
'X-RAY DIFFRACTION' 15 7 D 1356 ? ? D 1356 ? ? ? ? 
'X-RAY DIFFRACTION' 16 8 D 159  ? ? D 350  ? ? ? ? 
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
REFMAC    refinement       5.1.24 ? 1 
DENZO     'data reduction' .      ? 2 
SCALEPACK 'data scaling'   .      ? 3 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   CG 
_pdbx_validate_close_contact.auth_asym_id_1   D 
_pdbx_validate_close_contact.auth_comp_id_1   ASN 
_pdbx_validate_close_contact.auth_seq_id_1    109 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   A 
_pdbx_validate_close_contact.auth_atom_id_2   C1 
_pdbx_validate_close_contact.auth_asym_id_2   D 
_pdbx_validate_close_contact.auth_comp_id_2   NAG 
_pdbx_validate_close_contact.auth_seq_id_2    1351 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.15 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 CB A ASP 31  ? ? CG A ASP 31  ? ? OD2 A ASP 31  ? ? 124.21 118.30 5.91 0.90 N 
2 1 CB A ASP 120 ? ? CG A ASP 120 ? ? OD2 A ASP 120 ? ? 124.10 118.30 5.80 0.90 N 
3 1 CB A ASP 176 ? ? CG A ASP 176 ? ? OD2 A ASP 176 ? ? 124.93 118.30 6.63 0.90 N 
4 1 CB A ASP 246 ? ? CG A ASP 246 ? ? OD2 A ASP 246 ? ? 125.23 118.30 6.93 0.90 N 
5 1 CB B ASP 9   ? ? CG B ASP 9   ? ? OD2 B ASP 9   ? ? 125.14 118.30 6.84 0.90 N 
6 1 CB B ASP 120 ? ? CG B ASP 120 ? ? OD2 B ASP 120 ? ? 125.56 118.30 7.26 0.90 N 
7 1 CB C ASP 120 ? ? CG C ASP 120 ? ? OD2 C ASP 120 ? ? 124.61 118.30 6.31 0.90 N 
8 1 CB D ASP 31  ? ? CG D ASP 31  ? ? OD2 D ASP 31  ? ? 124.25 118.30 5.95 0.90 N 
9 1 CB D ASP 120 ? ? CG D ASP 120 ? ? OD2 D ASP 120 ? ? 124.02 118.30 5.72 0.90 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ASP A 31  ? ? 49.21   -119.05 
2  1 TYR A 46  ? ? 80.06   15.40   
3  1 SER A 99  ? ? -112.34 -168.31 
4  1 ASP A 120 ? ? -110.46 66.55   
5  1 ASN A 197 ? ? -76.99  49.10   
6  1 GLN A 245 ? ? 45.51   -125.65 
7  1 ASP B 31  ? ? 57.15   -123.36 
8  1 LEU B 61  ? ? -49.90  151.97  
9  1 ASP B 120 ? ? -112.96 62.66   
10 1 ASP B 145 ? ? 34.89   69.73   
11 1 ASN B 197 ? ? -81.64  49.44   
12 1 GLN B 245 ? ? 43.98   -125.88 
13 1 THR B 262 ? ? 81.01   -18.18  
14 1 ASP C 31  ? ? 59.97   -123.17 
15 1 SER C 99  ? ? -113.72 -167.81 
16 1 ASP C 120 ? ? -109.68 64.34   
17 1 ASP C 145 ? ? 39.00   66.63   
18 1 GLN C 245 ? ? 46.70   -131.20 
19 1 ASP D 31  ? ? 47.94   -119.77 
20 1 ASP D 120 ? ? -108.49 61.45   
21 1 ASP D 145 ? ? 38.91   62.77   
22 1 GLN D 245 ? ? 45.59   -129.85 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1  1 O ? A HOH 2003 ? 7.26 .    
2  1 O ? A HOH 2010 ? 6.97 .    
3  1 O ? A HOH 2012 ? 6.34 .    
4  1 O ? A HOH 2020 ? 5.86 .    
5  1 O ? A HOH 2180 ? .    6.53 
6  1 O ? B HOH 2053 ? 6.00 .    
7  1 O ? C HOH 2006 ? 6.79 .    
8  1 O ? C HOH 2015 ? 6.97 .    
9  1 O ? C HOH 2016 ? 6.77 .    
10 1 O ? C HOH 2019 ? 6.60 .    
11 1 O ? C HOH 2035 ? 5.85 .    
12 1 O ? C HOH 2040 ? 6.43 .    
13 1 O ? C HOH 2047 ? 6.11 .    
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A ASP 1   ? A ASP 1   
2  1 Y 1 A THR 2   ? A THR 2   
3  1 Y 1 A SER 155 ? A SER 155 
4  1 Y 1 A SER 156 ? A SER 156 
5  1 Y 1 A ASP 157 ? A ASP 157 
6  1 Y 1 A SER 158 ? A SER 158 
7  1 Y 1 B ASP 1   ? B ASP 1   
8  1 Y 1 B THR 2   ? B THR 2   
9  1 Y 1 B SER 155 ? B SER 155 
10 1 Y 1 B SER 156 ? B SER 156 
11 1 Y 1 B ASP 157 ? B ASP 157 
12 1 Y 1 B SER 158 ? B SER 158 
13 1 Y 1 C ASP 1   ? C ASP 1   
14 1 Y 1 C THR 2   ? C THR 2   
15 1 Y 1 C SER 154 ? C SER 154 
16 1 Y 1 C SER 155 ? C SER 155 
17 1 Y 1 C SER 156 ? C SER 156 
18 1 Y 1 C ASP 157 ? C ASP 157 
19 1 Y 1 C SER 158 ? C SER 158 
20 1 Y 1 D ASP 1   ? D ASP 1   
21 1 Y 1 D THR 2   ? D THR 2   
22 1 Y 1 D SER 3   ? D SER 3   
23 1 Y 1 D SER 155 ? D SER 155 
24 1 Y 1 D SER 156 ? D SER 156 
25 1 Y 1 D ASP 157 ? D ASP 157 
26 1 Y 1 D SER 158 ? D SER 158 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 N-ACETYL-D-GLUCOSAMINE                                  NAG 
3 BETA-D-MANNOSE                                          BMA 
4 ALPHA-D-MANNOSE                                         MAN 
5 '3,5,7-TRIHYDROXY-2-(4-HYDROXYPHENYL)-4H-CHROMEN-4-ONE' KMP 
6 'COPPER (II) ION'                                       CU  
7 '(4S)-2-METHYL-2,4-PENTANEDIOL'                         MPD 
8 water                                                   HOH 
# 
