data_4M0U
# 
_entry.id   4M0U 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.281 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   4M0U         
RCSB  RCSB081323   
WWPDB D_1000081323 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.details 
_pdbx_database_related.content_type 
PDB 4LYG . unspecified 
PDB 4LZP . unspecified 
PDB 4LZO . unspecified 
PDB 4M0P . unspecified 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        4M0U 
_pdbx_database_status.recvd_initial_deposition_date   2013-08-02 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Chen, P.' 1 
'Teng, M.' 2 
'Li, X.'   3 
# 
_citation.id                        primary 
_citation.title                     
;Crystal and EM Structures of Human Phosphoribosyl Pyrophosphate Synthase I (PRS1) Provide Novel Insights into the Disease-Associated Mutations
;
_citation.journal_abbrev            'Plos One' 
_citation.journal_volume            10 
_citation.page_first                e0120304 
_citation.page_last                 e0120304 
_citation.year                      2015 
_citation.journal_id_ASTM           ? 
_citation.country                   US 
_citation.journal_id_ISSN           1932-6203 
_citation.journal_id_CSD            ? 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   25781187 
_citation.pdbx_database_id_DOI      10.1371/journal.pone.0120304 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Chen, P.'  1  
primary 'Liu, Z.'   2  
primary 'Wang, X.'  3  
primary 'Peng, J.'  4  
primary 'Sun, Q.'   5  
primary 'Li, J.'    6  
primary 'Wang, M.'  7  
primary 'Niu, L.'   8  
primary 'Zhang, Z.' 9  
primary 'Cai, G.'   10 
primary 'Teng, M.'  11 
primary 'Li, X.'    12 
# 
_cell.entry_id           4M0U 
_cell.length_a           169.880 
_cell.length_b           169.880 
_cell.length_c           61.764 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        120.00 
_cell.Z_PDB              18 
_cell.pdbx_unique_axis   ? 
_cell.length_a_esd       ? 
_cell.length_b_esd       ? 
_cell.length_c_esd       ? 
_cell.angle_alpha_esd    ? 
_cell.angle_beta_esd     ? 
_cell.angle_gamma_esd    ? 
# 
_symmetry.entry_id                         4M0U 
_symmetry.space_group_name_H-M             'H 3' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                146 
_symmetry.space_group_name_Hall            ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Ribose-phosphate pyrophosphokinase 1' 35919.359 2  2.7.6.1 Q133P ? ? 
2 non-polymer syn 'SULFATE ION'                          96.063    4  ?       ?     ? ? 
3 water       nat water                                  18.015    15 ?       ?     ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'PPRibP, Phosphoribosyl pyrophosphate synthase I, PRS-I' 
# 
_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       
;MPNIKIFSGSSHQDLSQKIADRLGLELGKVVTKKFSNQETCVEIGESVRGEDVYIVQSGCGEINDNLMELLIMINACKIA
SASRVTAVIPCFPYARQDKKDKSRAPISAKLVANMLSVAGADHIITMDLHASPIQGFFDIPVDNLYAEPAVLKWIRENIS
EWRNCTIVSPDAGGAKRVTSIADRLNVDFALIHKERKKANEVDRMVLVGDVKDRVAILVDDMADTCGTICHAADKLLSAG
ATRVYAILTHGIFSGPAISRINNACFEAVVVTNTIPQEDKMKHCSKIQVIDISMILAEAIRRTHNGESVSYLFSHVPLLE
HHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MPNIKIFSGSSHQDLSQKIADRLGLELGKVVTKKFSNQETCVEIGESVRGEDVYIVQSGCGEINDNLMELLIMINACKIA
SASRVTAVIPCFPYARQDKKDKSRAPISAKLVANMLSVAGADHIITMDLHASPIQGFFDIPVDNLYAEPAVLKWIRENIS
EWRNCTIVSPDAGGAKRVTSIADRLNVDFALIHKERKKANEVDRMVLVGDVKDRVAILVDDMADTCGTICHAADKLLSAG
ATRVYAILTHGIFSGPAISRINNACFEAVVVTNTIPQEDKMKHCSKIQVIDISMILAEAIRRTHNGESVSYLFSHVPLLE
HHHHHH
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   PRO n 
1 3   ASN n 
1 4   ILE n 
1 5   LYS n 
1 6   ILE n 
1 7   PHE n 
1 8   SER n 
1 9   GLY n 
1 10  SER n 
1 11  SER n 
1 12  HIS n 
1 13  GLN n 
1 14  ASP n 
1 15  LEU n 
1 16  SER n 
1 17  GLN n 
1 18  LYS n 
1 19  ILE n 
1 20  ALA n 
1 21  ASP n 
1 22  ARG n 
1 23  LEU n 
1 24  GLY n 
1 25  LEU n 
1 26  GLU n 
1 27  LEU n 
1 28  GLY n 
1 29  LYS n 
1 30  VAL n 
1 31  VAL n 
1 32  THR n 
1 33  LYS n 
1 34  LYS n 
1 35  PHE n 
1 36  SER n 
1 37  ASN n 
1 38  GLN n 
1 39  GLU n 
1 40  THR n 
1 41  CYS n 
1 42  VAL n 
1 43  GLU n 
1 44  ILE n 
1 45  GLY n 
1 46  GLU n 
1 47  SER n 
1 48  VAL n 
1 49  ARG n 
1 50  GLY n 
1 51  GLU n 
1 52  ASP n 
1 53  VAL n 
1 54  TYR n 
1 55  ILE n 
1 56  VAL n 
1 57  GLN n 
1 58  SER n 
1 59  GLY n 
1 60  CYS n 
1 61  GLY n 
1 62  GLU n 
1 63  ILE n 
1 64  ASN n 
1 65  ASP n 
1 66  ASN n 
1 67  LEU n 
1 68  MET n 
1 69  GLU n 
1 70  LEU n 
1 71  LEU n 
1 72  ILE n 
1 73  MET n 
1 74  ILE n 
1 75  ASN n 
1 76  ALA n 
1 77  CYS n 
1 78  LYS n 
1 79  ILE n 
1 80  ALA n 
1 81  SER n 
1 82  ALA n 
1 83  SER n 
1 84  ARG n 
1 85  VAL n 
1 86  THR n 
1 87  ALA n 
1 88  VAL n 
1 89  ILE n 
1 90  PRO n 
1 91  CYS n 
1 92  PHE n 
1 93  PRO n 
1 94  TYR n 
1 95  ALA n 
1 96  ARG n 
1 97  GLN n 
1 98  ASP n 
1 99  LYS n 
1 100 LYS n 
1 101 ASP n 
1 102 LYS n 
1 103 SER n 
1 104 ARG n 
1 105 ALA n 
1 106 PRO n 
1 107 ILE n 
1 108 SER n 
1 109 ALA n 
1 110 LYS n 
1 111 LEU n 
1 112 VAL n 
1 113 ALA n 
1 114 ASN n 
1 115 MET n 
1 116 LEU n 
1 117 SER n 
1 118 VAL n 
1 119 ALA n 
1 120 GLY n 
1 121 ALA n 
1 122 ASP n 
1 123 HIS n 
1 124 ILE n 
1 125 ILE n 
1 126 THR n 
1 127 MET n 
1 128 ASP n 
1 129 LEU n 
1 130 HIS n 
1 131 ALA n 
1 132 SER n 
1 133 PRO n 
1 134 ILE n 
1 135 GLN n 
1 136 GLY n 
1 137 PHE n 
1 138 PHE n 
1 139 ASP n 
1 140 ILE n 
1 141 PRO n 
1 142 VAL n 
1 143 ASP n 
1 144 ASN n 
1 145 LEU n 
1 146 TYR n 
1 147 ALA n 
1 148 GLU n 
1 149 PRO n 
1 150 ALA n 
1 151 VAL n 
1 152 LEU n 
1 153 LYS n 
1 154 TRP n 
1 155 ILE n 
1 156 ARG n 
1 157 GLU n 
1 158 ASN n 
1 159 ILE n 
1 160 SER n 
1 161 GLU n 
1 162 TRP n 
1 163 ARG n 
1 164 ASN n 
1 165 CYS n 
1 166 THR n 
1 167 ILE n 
1 168 VAL n 
1 169 SER n 
1 170 PRO n 
1 171 ASP n 
1 172 ALA n 
1 173 GLY n 
1 174 GLY n 
1 175 ALA n 
1 176 LYS n 
1 177 ARG n 
1 178 VAL n 
1 179 THR n 
1 180 SER n 
1 181 ILE n 
1 182 ALA n 
1 183 ASP n 
1 184 ARG n 
1 185 LEU n 
1 186 ASN n 
1 187 VAL n 
1 188 ASP n 
1 189 PHE n 
1 190 ALA n 
1 191 LEU n 
1 192 ILE n 
1 193 HIS n 
1 194 LYS n 
1 195 GLU n 
1 196 ARG n 
1 197 LYS n 
1 198 LYS n 
1 199 ALA n 
1 200 ASN n 
1 201 GLU n 
1 202 VAL n 
1 203 ASP n 
1 204 ARG n 
1 205 MET n 
1 206 VAL n 
1 207 LEU n 
1 208 VAL n 
1 209 GLY n 
1 210 ASP n 
1 211 VAL n 
1 212 LYS n 
1 213 ASP n 
1 214 ARG n 
1 215 VAL n 
1 216 ALA n 
1 217 ILE n 
1 218 LEU n 
1 219 VAL n 
1 220 ASP n 
1 221 ASP n 
1 222 MET n 
1 223 ALA n 
1 224 ASP n 
1 225 THR n 
1 226 CYS n 
1 227 GLY n 
1 228 THR n 
1 229 ILE n 
1 230 CYS n 
1 231 HIS n 
1 232 ALA n 
1 233 ALA n 
1 234 ASP n 
1 235 LYS n 
1 236 LEU n 
1 237 LEU n 
1 238 SER n 
1 239 ALA n 
1 240 GLY n 
1 241 ALA n 
1 242 THR n 
1 243 ARG n 
1 244 VAL n 
1 245 TYR n 
1 246 ALA n 
1 247 ILE n 
1 248 LEU n 
1 249 THR n 
1 250 HIS n 
1 251 GLY n 
1 252 ILE n 
1 253 PHE n 
1 254 SER n 
1 255 GLY n 
1 256 PRO n 
1 257 ALA n 
1 258 ILE n 
1 259 SER n 
1 260 ARG n 
1 261 ILE n 
1 262 ASN n 
1 263 ASN n 
1 264 ALA n 
1 265 CYS n 
1 266 PHE n 
1 267 GLU n 
1 268 ALA n 
1 269 VAL n 
1 270 VAL n 
1 271 VAL n 
1 272 THR n 
1 273 ASN n 
1 274 THR n 
1 275 ILE n 
1 276 PRO n 
1 277 GLN n 
1 278 GLU n 
1 279 ASP n 
1 280 LYS n 
1 281 MET n 
1 282 LYS n 
1 283 HIS n 
1 284 CYS n 
1 285 SER n 
1 286 LYS n 
1 287 ILE n 
1 288 GLN n 
1 289 VAL n 
1 290 ILE n 
1 291 ASP n 
1 292 ILE n 
1 293 SER n 
1 294 MET n 
1 295 ILE n 
1 296 LEU n 
1 297 ALA n 
1 298 GLU n 
1 299 ALA n 
1 300 ILE n 
1 301 ARG n 
1 302 ARG n 
1 303 THR n 
1 304 HIS n 
1 305 ASN n 
1 306 GLY n 
1 307 GLU n 
1 308 SER n 
1 309 VAL n 
1 310 SER n 
1 311 TYR n 
1 312 LEU n 
1 313 PHE n 
1 314 SER n 
1 315 HIS n 
1 316 VAL n 
1 317 PRO n 
1 318 LEU n 
1 319 LEU n 
1 320 GLU n 
1 321 HIS n 
1 322 HIS n 
1 323 HIS n 
1 324 HIS n 
1 325 HIS n 
1 326 HIS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      ? 
_entity_src_gen.pdbx_beg_seq_num                   ? 
_entity_src_gen.pdbx_end_seq_num                   ? 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 PRPS1 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    PRPS1_HUMAN 
_struct_ref.pdbx_db_accession          P60891 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MPNIKIFSGSSHQDLSQKIADRLGLELGKVVTKKFSNQETCVEIGESVRGEDVYIVQSGCGEINDNLMELLIMINACKIA
SASRVTAVIPCFPYARQDKKDKSRAPISAKLVANMLSVAGADHIITMDLHASQIQGFFDIPVDNLYAEPAVLKWIRENIS
EWRNCTIVSPDAGGAKRVTSIADRLNVDFALIHKERKKANEVDRMVLVGDVKDRVAILVDDMADTCGTICHAADKLLSAG
ATRVYAILTHGIFSGPAISRINNACFEAVVVTNTIPQEDKMKHCSKIQVIDISMILAEAIRRTHNGESVSYLFSHVPL
;
_struct_ref.pdbx_align_begin           1 
_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 4M0U A 1 ? 318 ? P60891 1 ? 318 ? 1 318 
2 1 4M0U B 1 ? 318 ? P60891 1 ? 318 ? 1 318 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 4M0U PRO A 133 ? UNP P60891 GLN 133 'ENGINEERED MUTATION' 133 1  
1 4M0U LEU A 319 ? UNP P60891 ?   ?   'EXPRESSION TAG'      319 2  
1 4M0U GLU A 320 ? UNP P60891 ?   ?   'EXPRESSION TAG'      320 3  
1 4M0U HIS A 321 ? UNP P60891 ?   ?   'EXPRESSION TAG'      321 4  
1 4M0U HIS A 322 ? UNP P60891 ?   ?   'EXPRESSION TAG'      322 5  
1 4M0U HIS A 323 ? UNP P60891 ?   ?   'EXPRESSION TAG'      323 6  
1 4M0U HIS A 324 ? UNP P60891 ?   ?   'EXPRESSION TAG'      324 7  
1 4M0U HIS A 325 ? UNP P60891 ?   ?   'EXPRESSION TAG'      325 8  
1 4M0U HIS A 326 ? UNP P60891 ?   ?   'EXPRESSION TAG'      326 9  
2 4M0U PRO B 133 ? UNP P60891 GLN 133 'ENGINEERED MUTATION' 133 10 
2 4M0U LEU B 319 ? UNP P60891 ?   ?   'EXPRESSION TAG'      319 11 
2 4M0U GLU B 320 ? UNP P60891 ?   ?   'EXPRESSION TAG'      320 12 
2 4M0U HIS B 321 ? UNP P60891 ?   ?   'EXPRESSION TAG'      321 13 
2 4M0U HIS B 322 ? UNP P60891 ?   ?   'EXPRESSION TAG'      322 14 
2 4M0U HIS B 323 ? UNP P60891 ?   ?   'EXPRESSION TAG'      323 15 
2 4M0U HIS B 324 ? UNP P60891 ?   ?   'EXPRESSION TAG'      324 16 
2 4M0U HIS B 325 ? UNP P60891 ?   ?   'EXPRESSION TAG'      325 17 
2 4M0U HIS B 326 ? UNP P60891 ?   ?   'EXPRESSION TAG'      326 18 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE        ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER           ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE   ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ? 'C3 H7 N O3'     105.093 
SO4 non-polymer         . 'SULFATE ION'   ? 'O4 S -2'        96.063  
THR 'L-peptide linking' y THREONINE       ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE        ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ? 'C5 H11 N O2'    117.146 
# 
_exptl.entry_id          4M0U 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.39 
_exptl_crystal.density_percent_sol   48.48 
_exptl_crystal.description           ? 
_exptl_crystal.F_000                 ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION' 
_exptl_crystal_grow.temp            295 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              4.1 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.pdbx_details    'pH 4.1, VAPOR DIFFUSION, temperature 295K' 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               CCD 
_diffrn_detector.type                   'ADSC QUANTUM 315r' 
_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   . 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'SSRF BEAMLINE BL17U' 
_diffrn_source.pdbx_synchrotron_site       SSRF 
_diffrn_source.pdbx_synchrotron_beamline   BL17U 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_wavelength_list        ? 
# 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.entry_id                     4M0U 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             34.05 
_reflns.d_resolution_high            2.74 
_reflns.number_obs                   16179 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         ? 
_reflns.pdbx_Rmerge_I_obs            ? 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        ? 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              ? 
_reflns.R_free_details               ? 
_reflns.limit_h_max                  ? 
_reflns.limit_h_min                  ? 
_reflns.limit_k_max                  ? 
_reflns.limit_k_min                  ? 
_reflns.limit_l_max                  ? 
_reflns.limit_l_min                  ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.pdbx_chi_squared             ? 
_reflns.pdbx_scaling_rejects         ? 
# 
_reflns_shell.pdbx_diffrn_id         1 
_reflns_shell.pdbx_ordinal           1 
_reflns_shell.d_res_high             2.74 
_reflns_shell.d_res_low              ? 
_reflns_shell.percent_possible_all   ? 
_reflns_shell.Rmerge_I_obs           ? 
_reflns_shell.pdbx_Rsym_value        ? 
_reflns_shell.meanI_over_sigI_obs    ? 
_reflns_shell.pdbx_redundancy        ? 
_reflns_shell.percent_possible_obs   ? 
_reflns_shell.number_unique_all      ? 
_reflns_shell.number_measured_all    ? 
_reflns_shell.number_measured_obs    ? 
_reflns_shell.number_unique_obs      ? 
_reflns_shell.pdbx_chi_squared       ? 
# 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.entry_id                                 4M0U 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     15356 
_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                             34.05 
_refine.ls_d_res_high                            2.74 
_refine.ls_percent_reflns_obs                    92.72 
_refine.ls_R_factor_obs                          0.25539 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.25313 
_refine.ls_R_factor_R_free                       0.29772 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.1 
_refine.ls_number_reflns_R_free                  823 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.879 
_refine.correlation_coeff_Fo_to_Fc_free          0.854 
_refine.B_iso_mean                               49.923 
_refine.aniso_B[1][1]                            2.22 
_refine.aniso_B[2][2]                            2.22 
_refine.aniso_B[3][3]                            -3.33 
_refine.aniso_B[1][2]                            1.11 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][3]                            0.00 
_refine.solvent_model_details                    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                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.pdbx_starting_model                      4F8E 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_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                       ? 
_refine.pdbx_overall_ESU_R_Free                  0.472 
_refine.overall_SU_ML                            ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             ? 
_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.ls_redundancy_reflns_obs                 ? 
_refine.B_iso_min                                ? 
_refine.B_iso_max                                ? 
_refine.overall_SU_R_free                        ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        4666 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         20 
_refine_hist.number_atoms_solvent             15 
_refine_hist.number_atoms_total               4701 
_refine_hist.d_res_high                       2.74 
_refine_hist.d_res_low                        34.05 
# 
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             0.010  0.022  ? 4759 'X-RAY DIFFRACTION' ? 
r_bond_other_d               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.159  1.962  ? 6440 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       5.351  5.000  ? 607  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       36.313 24.388 ? 196  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       17.380 15.000 ? 852  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       16.529 15.000 ? 31   'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.076  0.200  ? 762  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.005  0.021  ? 3468 'X-RAY DIFFRACTION' ? 
r_gen_planes_other           ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbd_refined                ?      ?      ? ?    '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        ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_other          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_refined          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_other            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_refined       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_other         ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_refined     ?      ?      ? ?    '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                  0.406  1.500  ? 3036 'X-RAY DIFFRACTION' ? 
r_mcbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcangle_it                 0.767  2.000  ? 4914 'X-RAY DIFFRACTION' ? 
r_mcangle_other              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scbond_it                  1.045  3.000  ? 1723 'X-RAY DIFFRACTION' ? 
r_scbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scangle_it                 1.738  4.500  ? 1526 '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                       2.741 
_refine_ls_shell.d_res_low                        2.812 
_refine_ls_shell.number_reflns_R_work             1050 
_refine_ls_shell.R_factor_R_work                  0.292 
_refine_ls_shell.percent_reflns_obs               85.56 
_refine_ls_shell.R_factor_R_free                  0.350 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             46 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.number_reflns_obs                ? 
# 
_struct.entry_id                  4M0U 
_struct.title                     'crystal structure of human PRS1 Q133P mutant' 
_struct.pdbx_descriptor           'Ribose-phosphate pyrophosphokinase 1 (E.C.2.7.6.1)' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        4M0U 
_struct_keywords.pdbx_keywords   TRANSFERASE 
_struct_keywords.text            'PRS1, PRPP synthesis enzyme, ATP R5P, TRANSFERASE' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 2 ? 
E N N 2 ? 
F N N 2 ? 
G N N 3 ? 
H N N 3 ? 
# 
_struct_biol.id        1 
_struct_biol.details   ? 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  1  ASP A 14  ? LEU A 23  ? ASP A 14  LEU A 23  1 ? 10 
HELX_P HELX_P2  2  GLU A 62  ? ILE A 79  ? GLU A 62  ILE A 79  1 ? 18 
HELX_P HELX_P3  3  ILE A 107 ? GLY A 120 ? ILE A 107 GLY A 120 1 ? 14 
HELX_P HELX_P4  4  ALA A 131 ? PHE A 138 ? ALA A 131 PHE A 138 5 ? 8  
HELX_P HELX_P5  5  ALA A 147 ? ILE A 159 ? ALA A 147 ILE A 159 1 ? 13 
HELX_P HELX_P6  6  GLU A 161 ? ASN A 164 ? GLU A 161 ASN A 164 5 ? 4  
HELX_P HELX_P7  7  GLY A 174 ? LEU A 185 ? GLY A 174 LEU A 185 1 ? 12 
HELX_P HELX_P8  8  CYS A 226 ? ALA A 239 ? CYS A 226 ALA A 239 1 ? 14 
HELX_P HELX_P9  9  PRO A 256 ? ASN A 263 ? PRO A 256 ASN A 263 1 ? 8  
HELX_P HELX_P10 10 GLN A 277 ? LYS A 282 ? GLN A 277 LYS A 282 1 ? 6  
HELX_P HELX_P11 11 ILE A 292 ? GLY A 306 ? ILE A 292 GLY A 306 1 ? 15 
HELX_P HELX_P12 12 ASP B 14  ? LEU B 23  ? ASP B 14  LEU B 23  1 ? 10 
HELX_P HELX_P13 13 GLU B 62  ? ILE B 79  ? GLU B 62  ILE B 79  1 ? 18 
HELX_P HELX_P14 14 ILE B 107 ? GLY B 120 ? ILE B 107 GLY B 120 1 ? 14 
HELX_P HELX_P15 15 ALA B 131 ? PHE B 138 ? ALA B 131 PHE B 138 5 ? 8  
HELX_P HELX_P16 16 ALA B 147 ? ILE B 159 ? ALA B 147 ILE B 159 1 ? 13 
HELX_P HELX_P17 17 SER B 160 ? ASN B 164 ? SER B 160 ASN B 164 5 ? 5  
HELX_P HELX_P18 18 GLY B 174 ? LEU B 185 ? GLY B 174 LEU B 185 1 ? 12 
HELX_P HELX_P19 19 CYS B 226 ? ALA B 239 ? CYS B 226 ALA B 239 1 ? 14 
HELX_P HELX_P20 20 PRO B 256 ? ALA B 264 ? PRO B 256 ALA B 264 1 ? 9  
HELX_P HELX_P21 21 GLN B 277 ? HIS B 283 ? GLN B 277 HIS B 283 1 ? 7  
HELX_P HELX_P22 22 ILE B 292 ? GLY B 306 ? ILE B 292 GLY B 306 1 ? 15 
HELX_P HELX_P23 23 VAL B 309 ? SER B 314 ? VAL B 309 SER B 314 5 ? 6  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A ? 5 ? 
B ? 2 ? 
C ? 7 ? 
D ? 5 ? 
E ? 2 ? 
F ? 7 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
A 1 2 ? parallel      
A 2 3 ? parallel      
A 3 4 ? parallel      
A 4 5 ? parallel      
B 1 2 ? anti-parallel 
C 1 2 ? anti-parallel 
C 2 3 ? parallel      
C 3 4 ? parallel      
C 4 5 ? parallel      
C 5 6 ? parallel      
C 6 7 ? parallel      
D 1 2 ? parallel      
D 2 3 ? parallel      
D 3 4 ? parallel      
D 4 5 ? parallel      
E 1 2 ? anti-parallel 
F 1 2 ? anti-parallel 
F 2 3 ? parallel      
F 3 4 ? parallel      
F 4 5 ? parallel      
F 5 6 ? parallel      
F 6 7 ? parallel      
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
A 1 ILE A 4   ? GLY A 9   ? ILE A 4   GLY A 9   
A 2 ASP A 52  ? GLN A 57  ? ASP A 52  GLN A 57  
A 3 ARG A 84  ? VAL A 88  ? ARG A 84  VAL A 88  
A 4 HIS A 123 ? MET A 127 ? HIS A 123 MET A 127 
A 5 VAL A 142 ? LEU A 145 ? VAL A 142 LEU A 145 
B 1 VAL A 30  ? LYS A 34  ? VAL A 30  LYS A 34  
B 2 THR A 40  ? ILE A 44  ? THR A 40  ILE A 44  
C 1 MET A 205 ? VAL A 208 ? MET A 205 VAL A 208 
C 2 ASP A 188 ? LYS A 194 ? ASP A 188 LYS A 194 
C 3 THR A 166 ? SER A 169 ? THR A 166 SER A 169 
C 4 ALA A 216 ? ALA A 223 ? ALA A 216 ALA A 223 
C 5 VAL A 244 ? GLY A 251 ? VAL A 244 GLY A 251 
C 6 ALA A 268 ? THR A 272 ? ALA A 268 THR A 272 
C 7 ILE A 287 ? ILE A 290 ? ILE A 287 ILE A 290 
D 1 ILE B 4   ? SER B 8   ? ILE B 4   SER B 8   
D 2 ASP B 52  ? VAL B 56  ? ASP B 52  VAL B 56  
D 3 ARG B 84  ? ILE B 89  ? ARG B 84  ILE B 89  
D 4 HIS B 123 ? MET B 127 ? HIS B 123 MET B 127 
D 5 VAL B 142 ? LEU B 145 ? VAL B 142 LEU B 145 
E 1 VAL B 30  ? PHE B 35  ? VAL B 30  PHE B 35  
E 2 GLU B 39  ? ILE B 44  ? GLU B 39  ILE B 44  
F 1 MET B 205 ? VAL B 208 ? MET B 205 VAL B 208 
F 2 ASP B 188 ? LYS B 194 ? ASP B 188 LYS B 194 
F 3 THR B 166 ? SER B 169 ? THR B 166 SER B 169 
F 4 ALA B 216 ? ALA B 223 ? ALA B 216 ALA B 223 
F 5 VAL B 244 ? GLY B 251 ? VAL B 244 GLY B 251 
F 6 PHE B 266 ? THR B 272 ? PHE B 266 THR B 272 
F 7 ILE B 287 ? ILE B 290 ? ILE B 287 ILE B 290 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
A 1 2 N PHE A 7   ? N PHE A 7   O TYR A 54  ? O TYR A 54  
A 2 3 N ILE A 55  ? N ILE A 55  O VAL A 88  ? O VAL A 88  
A 3 4 N ALA A 87  ? N ALA A 87  O ILE A 125 ? O ILE A 125 
A 4 5 N ILE A 124 ? N ILE A 124 O ASP A 143 ? O ASP A 143 
B 1 2 N LYS A 33  ? N LYS A 33  O CYS A 41  ? O CYS A 41  
C 1 2 O VAL A 206 ? O VAL A 206 N HIS A 193 ? N HIS A 193 
C 2 3 O ILE A 192 ? O ILE A 192 N SER A 169 ? N SER A 169 
C 3 4 N THR A 166 ? N THR A 166 O ILE A 217 ? O ILE A 217 
C 4 5 N LEU A 218 ? N LEU A 218 O ILE A 247 ? O ILE A 247 
C 5 6 N LEU A 248 ? N LEU A 248 O VAL A 270 ? O VAL A 270 
C 6 7 N VAL A 271 ? N VAL A 271 O ILE A 290 ? O ILE A 290 
D 1 2 N LYS B 5   ? N LYS B 5   O TYR B 54  ? O TYR B 54  
D 2 3 N ILE B 55  ? N ILE B 55  O VAL B 88  ? O VAL B 88  
D 3 4 N ILE B 89  ? N ILE B 89  O ILE B 125 ? O ILE B 125 
D 4 5 N THR B 126 ? N THR B 126 O LEU B 145 ? O LEU B 145 
E 1 2 N PHE B 35  ? N PHE B 35  O GLU B 39  ? O GLU B 39  
F 1 2 O VAL B 206 ? O VAL B 206 N HIS B 193 ? N HIS B 193 
F 2 3 O ALA B 190 ? O ALA B 190 N ILE B 167 ? N ILE B 167 
F 3 4 N VAL B 168 ? N VAL B 168 O ILE B 217 ? O ILE B 217 
F 4 5 N LEU B 218 ? N LEU B 218 O ILE B 247 ? O ILE B 247 
F 5 6 N LEU B 248 ? N LEU B 248 O VAL B 270 ? O VAL B 270 
F 6 7 N VAL B 271 ? N VAL B 271 O ILE B 290 ? O ILE B 290 
# 
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 ? ? ? ? 6 'BINDING SITE FOR RESIDUE SO4 A 1001' 
AC2 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE SO4 A 1002' 
AC3 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE SO4 B 401'  
AC4 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE SO4 B 402'  
# 
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 6 SER A 47  ? SER A 47  . ? 2_555 ? 
2  AC1 6 ARG A 49  ? ARG A 49  . ? 2_555 ? 
3  AC1 6 SER A 308 ? SER A 308 . ? 1_555 ? 
4  AC1 6 VAL A 309 ? VAL A 309 . ? 1_555 ? 
5  AC1 6 SER A 310 ? SER A 310 . ? 1_555 ? 
6  AC1 6 ARG B 104 ? ARG B 104 . ? 2_555 ? 
7  AC2 5 ASP A 224 ? ASP A 224 . ? 1_555 ? 
8  AC2 5 THR A 225 ? THR A 225 . ? 1_555 ? 
9  AC2 5 CYS A 226 ? CYS A 226 . ? 1_555 ? 
10 AC2 5 GLY A 227 ? GLY A 227 . ? 1_555 ? 
11 AC2 5 THR A 228 ? THR A 228 . ? 1_555 ? 
12 AC3 6 ARG A 104 ? ARG A 104 . ? 3_555 ? 
13 AC3 6 SER B 47  ? SER B 47  . ? 3_555 ? 
14 AC3 6 ARG B 49  ? ARG B 49  . ? 3_555 ? 
15 AC3 6 SER B 308 ? SER B 308 . ? 1_555 ? 
16 AC3 6 VAL B 309 ? VAL B 309 . ? 1_555 ? 
17 AC3 6 SER B 310 ? SER B 310 . ? 1_555 ? 
18 AC4 6 ALA B 223 ? ALA B 223 . ? 1_555 ? 
19 AC4 6 ASP B 224 ? ASP B 224 . ? 1_555 ? 
20 AC4 6 THR B 225 ? THR B 225 . ? 1_555 ? 
21 AC4 6 CYS B 226 ? CYS B 226 . ? 1_555 ? 
22 AC4 6 GLY B 227 ? GLY B 227 . ? 1_555 ? 
23 AC4 6 THR B 228 ? THR B 228 . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          4M0U 
_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                    4M0U 
_atom_sites.fract_transf_matrix[1][1]   0.005887 
_atom_sites.fract_transf_matrix[1][2]   0.003399 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.006797 
_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]   0.016191 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . ASN A 1 3   ? 8.899   8.286   29.387  1.00  38.16  ? 3    ASN A N   1 
ATOM   2    C CA  . ASN A 1 3   ? 8.260   7.769   28.135  1.00  38.80  ? 3    ASN A CA  1 
ATOM   3    C C   . ASN A 1 3   ? 8.325   8.754   26.973  1.00  38.32  ? 3    ASN A C   1 
ATOM   4    O O   . ASN A 1 3   ? 8.541   8.351   25.836  1.00  38.36  ? 3    ASN A O   1 
ATOM   5    C CB  . ASN A 1 3   ? 6.807   7.302   28.365  1.00  38.95  ? 3    ASN A CB  1 
ATOM   6    C CG  . ASN A 1 3   ? 6.296   6.392   27.238  1.00  40.92  ? 3    ASN A CG  1 
ATOM   7    O OD1 . ASN A 1 3   ? 7.087   5.785   26.514  1.00  43.97  ? 3    ASN A OD1 1 
ATOM   8    N ND2 . ASN A 1 3   ? 4.975   6.297   27.084  1.00  42.67  ? 3    ASN A ND2 1 
ATOM   9    N N   . ILE A 1 4   ? 8.140   10.037  27.269  1.00  38.25  ? 4    ILE A N   1 
ATOM   10   C CA  . ILE A 1 4   ? 8.167   11.096  26.261  1.00  38.25  ? 4    ILE A CA  1 
ATOM   11   C C   . ILE A 1 4   ? 9.590   11.594  25.953  1.00  38.40  ? 4    ILE A C   1 
ATOM   12   O O   . ILE A 1 4   ? 10.389  11.819  26.866  1.00  38.07  ? 4    ILE A O   1 
ATOM   13   C CB  . ILE A 1 4   ? 7.240   12.267  26.663  1.00  38.38  ? 4    ILE A CB  1 
ATOM   14   C CG1 . ILE A 1 4   ? 7.209   13.356  25.583  1.00  38.69  ? 4    ILE A CG1 1 
ATOM   15   C CG2 . ILE A 1 4   ? 7.630   12.832  28.041  1.00  39.14  ? 4    ILE A CG2 1 
ATOM   16   C CD1 . ILE A 1 4   ? 6.038   14.308  25.734  1.00  40.49  ? 4    ILE A CD1 1 
ATOM   17   N N   . LYS A 1 5   ? 9.881   11.762  24.655  1.00  38.51  ? 5    LYS A N   1 
ATOM   18   C CA  . LYS A 1 5   ? 11.175  12.250  24.172  1.00  38.48  ? 5    LYS A CA  1 
ATOM   19   C C   . LYS A 1 5   ? 11.079  13.317  23.070  1.00  38.35  ? 5    LYS A C   1 
ATOM   20   O O   . LYS A 1 5   ? 10.409  13.128  22.056  1.00  38.14  ? 5    LYS A O   1 
ATOM   21   C CB  . LYS A 1 5   ? 12.066  11.082  23.731  1.00  38.59  ? 5    LYS A CB  1 
ATOM   22   C CG  . LYS A 1 5   ? 13.019  10.605  24.838  1.00  40.35  ? 5    LYS A CG  1 
ATOM   23   C CD  . LYS A 1 5   ? 14.273  11.490  24.876  1.00  43.02  ? 5    LYS A CD  1 
ATOM   24   C CE  . LYS A 1 5   ? 15.036  11.394  26.188  1.00  42.68  ? 5    LYS A CE  1 
ATOM   25   N NZ  . LYS A 1 5   ? 16.269  12.278  26.157  1.00  44.22  ? 5    LYS A NZ  1 
ATOM   26   N N   . ILE A 1 6   ? 11.802  14.405  23.224  1.00  38.55  ? 6    ILE A N   1 
ATOM   27   C CA  . ILE A 1 6   ? 11.742  15.510  22.297  1.00  38.45  ? 6    ILE A CA  1 
ATOM   28   C C   . ILE A 1 6   ? 13.045  15.788  21.626  1.00  38.35  ? 6    ILE A C   1 
ATOM   29   O O   . ILE A 1 6   ? 14.003  16.011  22.282  1.00  38.18  ? 6    ILE A O   1 
ATOM   30   C CB  . ILE A 1 6   ? 11.421  16.780  23.039  1.00  38.35  ? 6    ILE A CB  1 
ATOM   31   C CG1 . ILE A 1 6   ? 10.282  16.553  23.980  1.00  38.39  ? 6    ILE A CG1 1 
ATOM   32   C CG2 . ILE A 1 6   ? 10.982  17.840  22.094  1.00  38.13  ? 6    ILE A CG2 1 
ATOM   33   C CD1 . ILE A 1 6   ? 9.273   17.645  23.924  1.00  39.89  ? 6    ILE A CD1 1 
ATOM   34   N N   . PHE A 1 7   ? 13.067  15.804  20.307  1.00  38.88  ? 7    PHE A N   1 
ATOM   35   C CA  . PHE A 1 7   ? 14.250  16.195  19.591  1.00  39.07  ? 7    PHE A CA  1 
ATOM   36   C C   . PHE A 1 7   ? 14.011  17.422  18.767  1.00  39.84  ? 7    PHE A C   1 
ATOM   37   O O   . PHE A 1 7   ? 12.918  17.733  18.457  1.00  39.76  ? 7    PHE A O   1 
ATOM   38   C CB  . PHE A 1 7   ? 14.685  15.087  18.696  1.00  38.54  ? 7    PHE A CB  1 
ATOM   39   C CG  . PHE A 1 7   ? 15.021  13.847  19.409  1.00  36.90  ? 7    PHE A CG  1 
ATOM   40   C CD1 . PHE A 1 7   ? 14.059  13.126  19.990  1.00  36.23  ? 7    PHE A CD1 1 
ATOM   41   C CD2 . PHE A 1 7   ? 16.289  13.400  19.465  1.00  34.80  ? 7    PHE A CD2 1 
ATOM   42   C CE1 . PHE A 1 7   ? 14.348  11.975  20.640  1.00  35.78  ? 7    PHE A CE1 1 
ATOM   43   C CE2 . PHE A 1 7   ? 16.598  12.252  20.103  1.00  33.47  ? 7    PHE A CE2 1 
ATOM   44   C CZ  . PHE A 1 7   ? 15.623  11.535  20.700  1.00  34.75  ? 7    PHE A CZ  1 
ATOM   45   N N   . SER A 1 8   ? 15.056  18.160  18.499  1.00  41.20  ? 8    SER A N   1 
ATOM   46   C CA  . SER A 1 8   ? 14.933  19.325  17.687  1.00  42.53  ? 8    SER A CA  1 
ATOM   47   C C   . SER A 1 8   ? 15.432  18.917  16.377  1.00  43.85  ? 8    SER A C   1 
ATOM   48   O O   . SER A 1 8   ? 16.277  18.086  16.294  1.00  43.95  ? 8    SER A O   1 
ATOM   49   C CB  . SER A 1 8   ? 15.804  20.432  18.190  1.00  42.36  ? 8    SER A CB  1 
ATOM   50   O OG  . SER A 1 8   ? 15.825  21.480  17.279  1.00  41.48  ? 8    SER A OG  1 
ATOM   51   N N   . GLY A 1 9   ? 14.898  19.499  15.330  1.00  45.50  ? 9    GLY A N   1 
ATOM   52   C CA  . GLY A 1 9   ? 15.275  19.086  14.011  1.00  46.87  ? 9    GLY A CA  1 
ATOM   53   C C   . GLY A 1 9   ? 16.199  19.965  13.211  1.00  48.16  ? 9    GLY A C   1 
ATOM   54   O O   . GLY A 1 9   ? 16.056  19.996  12.005  1.00  48.46  ? 9    GLY A O   1 
ATOM   55   N N   . SER A 1 10  ? 17.154  20.653  13.809  1.00  49.16  ? 10   SER A N   1 
ATOM   56   C CA  . SER A 1 10  ? 17.933  21.531  12.987  1.00  50.49  ? 10   SER A CA  1 
ATOM   57   C C   . SER A 1 10  ? 19.130  22.091  13.700  1.00  51.22  ? 10   SER A C   1 
ATOM   58   O O   . SER A 1 10  ? 19.544  21.563  14.708  1.00  52.09  ? 10   SER A O   1 
ATOM   59   C CB  . SER A 1 10  ? 17.043  22.680  12.514  1.00  50.65  ? 10   SER A CB  1 
ATOM   60   N N   . SER A 1 11  ? 19.680  23.162  13.149  1.00  51.59  ? 11   SER A N   1 
ATOM   61   C CA  . SER A 1 11  ? 20.585  24.017  13.851  1.00  51.70  ? 11   SER A CA  1 
ATOM   62   C C   . SER A 1 11  ? 19.751  24.810  14.824  1.00  51.77  ? 11   SER A C   1 
ATOM   63   O O   . SER A 1 11  ? 20.198  25.188  15.881  1.00  51.72  ? 11   SER A O   1 
ATOM   64   C CB  . SER A 1 11  ? 21.254  24.956  12.868  1.00  51.83  ? 11   SER A CB  1 
ATOM   65   O OG  . SER A 1 11  ? 21.246  26.290  13.317  1.00  52.18  ? 11   SER A OG  1 
ATOM   66   N N   . HIS A 1 12  ? 18.509  25.040  14.460  0.79  51.80  ? 12   HIS A N   1 
ATOM   67   C CA  . HIS A 1 12  ? 17.608  25.836  15.253  0.79  52.19  ? 12   HIS A CA  1 
ATOM   68   C C   . HIS A 1 12  ? 17.107  25.235  16.526  0.79  52.14  ? 12   HIS A C   1 
ATOM   69   O O   . HIS A 1 12  ? 16.130  24.496  16.502  0.79  52.29  ? 12   HIS A O   1 
ATOM   70   C CB  . HIS A 1 12  ? 16.375  26.131  14.430  0.79  52.29  ? 12   HIS A CB  1 
ATOM   71   C CG  . HIS A 1 12  ? 15.124  26.237  15.253  0.79  53.44  ? 12   HIS A CG  1 
ATOM   72   N ND1 . HIS A 1 12  ? 14.265  25.228  15.394  0.79  54.53  ? 12   HIS A ND1 1 
ATOM   73   C CD2 . HIS A 1 12  ? 14.615  27.288  15.990  0.79  54.31  ? 12   HIS A CD2 1 
ATOM   74   C CE1 . HIS A 1 12  ? 13.270  25.606  16.191  0.79  55.48  ? 12   HIS A CE1 1 
ATOM   75   N NE2 . HIS A 1 12  ? 13.480  26.873  16.543  0.79  55.56  ? 12   HIS A NE2 1 
ATOM   76   N N   . GLN A 1 13  ? 17.690  25.547  17.668  1.00  52.20  ? 13   GLN A N   1 
ATOM   77   C CA  . GLN A 1 13  ? 17.038  25.091  18.894  1.00  52.32  ? 13   GLN A CA  1 
ATOM   78   C C   . GLN A 1 13  ? 16.402  26.024  19.919  1.00  51.81  ? 13   GLN A C   1 
ATOM   79   O O   . GLN A 1 13  ? 16.615  25.857  21.122  1.00  51.90  ? 13   GLN A O   1 
ATOM   80   C CB  . GLN A 1 13  ? 18.324  24.703  19.624  1.00  52.49  ? 13   GLN A CB  1 
ATOM   81   C CG  . GLN A 1 13  ? 18.914  23.375  19.167  1.00  54.01  ? 13   GLN A CG  1 
ATOM   82   C CD  . GLN A 1 13  ? 19.649  22.656  20.294  1.00  57.20  ? 13   GLN A CD  1 
ATOM   83   O OE1 . GLN A 1 13  ? 20.434  21.736  20.047  1.00  58.55  ? 13   GLN A OE1 1 
ATOM   84   N NE2 . GLN A 1 13  ? 19.394  23.072  21.542  1.00  57.54  ? 13   GLN A NE2 1 
ATOM   85   N N   . ASP A 1 14  ? 15.616  26.987  19.453  1.00  51.27  ? 14   ASP A N   1 
ATOM   86   C CA  . ASP A 1 14  ? 15.118  28.032  20.337  1.00  51.03  ? 14   ASP A CA  1 
ATOM   87   C C   . ASP A 1 14  ? 13.631  27.805  20.602  1.00  50.50  ? 14   ASP A C   1 
ATOM   88   O O   . ASP A 1 14  ? 13.122  28.211  21.657  1.00  50.53  ? 14   ASP A O   1 
ATOM   89   C CB  . ASP A 1 14  ? 15.156  29.477  19.835  1.00  51.27  ? 14   ASP A CB  1 
ATOM   90   C CG  . ASP A 1 14  ? 14.869  30.478  20.940  1.00  52.51  ? 14   ASP A CG  1 
ATOM   91   O OD1 . ASP A 1 14  ? 14.292  31.553  20.651  1.00  54.47  ? 14   ASP A OD1 1 
ATOM   92   O OD2 . ASP A 1 14  ? 15.211  30.187  22.111  1.00  54.16  ? 14   ASP A OD2 1 
ATOM   93   N N   . LEU A 1 15  ? 12.943  27.154  19.662  1.00  49.79  ? 15   LEU A N   1 
ATOM   94   C CA  . LEU A 1 15  ? 11.521  26.848  19.821  1.00  49.30  ? 15   LEU A CA  1 
ATOM   95   C C   . LEU A 1 15  ? 11.523  25.507  20.536  1.00  49.03  ? 15   LEU A C   1 
ATOM   96   O O   . LEU A 1 15  ? 10.778  25.302  21.491  1.00  49.19  ? 15   LEU A O   1 
ATOM   97   C CB  . LEU A 1 15  ? 10.812  26.688  18.476  1.00  49.32  ? 15   LEU A CB  1 
ATOM   98   C CG  . LEU A 1 15  ? 9.319   26.970  18.265  1.00  49.39  ? 15   LEU A CG  1 
ATOM   99   C CD1 . LEU A 1 15  ? 8.828   25.988  17.209  1.00  50.02  ? 15   LEU A CD1 1 
ATOM   100  C CD2 . LEU A 1 15  ? 8.457   26.879  19.534  1.00  49.15  ? 15   LEU A CD2 1 
ATOM   101  N N   . SER A 1 16  ? 12.379  24.610  20.059  1.00  48.62  ? 16   SER A N   1 
ATOM   102  C CA  . SER A 1 16  ? 12.508  23.260  20.576  1.00  48.24  ? 16   SER A CA  1 
ATOM   103  C C   . SER A 1 16  ? 12.891  23.218  22.048  1.00  48.04  ? 16   SER A C   1 
ATOM   104  O O   . SER A 1 16  ? 12.316  22.445  22.811  1.00  48.27  ? 16   SER A O   1 
ATOM   105  C CB  . SER A 1 16  ? 13.552  22.501  19.762  1.00  48.35  ? 16   SER A CB  1 
ATOM   106  O OG  . SER A 1 16  ? 13.155  22.421  18.406  1.00  48.96  ? 16   SER A OG  1 
ATOM   107  N N   . GLN A 1 17  ? 13.869  24.034  22.441  1.00  47.63  ? 17   GLN A N   1 
ATOM   108  C CA  . GLN A 1 17  ? 14.310  24.106  23.837  1.00  46.98  ? 17   GLN A CA  1 
ATOM   109  C C   . GLN A 1 17  ? 13.220  24.727  24.725  1.00  46.23  ? 17   GLN A C   1 
ATOM   110  O O   . GLN A 1 17  ? 13.058  24.333  25.875  1.00  46.24  ? 17   GLN A O   1 
ATOM   111  C CB  . GLN A 1 17  ? 15.635  24.883  23.956  1.00  47.08  ? 17   GLN A CB  1 
ATOM   112  C CG  . GLN A 1 17  ? 16.272  24.877  25.349  1.00  48.07  ? 17   GLN A CG  1 
ATOM   113  C CD  . GLN A 1 17  ? 16.742  23.496  25.796  1.00  49.75  ? 17   GLN A CD  1 
ATOM   114  O OE1 . GLN A 1 17  ? 17.705  22.940  25.252  1.00  49.27  ? 17   GLN A OE1 1 
ATOM   115  N NE2 . GLN A 1 17  ? 16.072  22.945  26.807  1.00  50.63  ? 17   GLN A NE2 1 
ATOM   116  N N   . LYS A 1 18  ? 12.477  25.690  24.187  1.00  45.17  ? 18   LYS A N   1 
ATOM   117  C CA  . LYS A 1 18  ? 11.380  26.306  24.923  1.00  44.52  ? 18   LYS A CA  1 
ATOM   118  C C   . LYS A 1 18  ? 10.282  25.289  25.257  1.00  43.94  ? 18   LYS A C   1 
ATOM   119  O O   . LYS A 1 18  ? 9.732   25.296  26.364  1.00  43.94  ? 18   LYS A O   1 
ATOM   120  C CB  . LYS A 1 18  ? 10.797  27.484  24.139  1.00  44.79  ? 18   LYS A CB  1 
ATOM   121  C CG  . LYS A 1 18  ? 11.585  28.785  24.273  1.00  44.86  ? 18   LYS A CG  1 
ATOM   122  C CD  . LYS A 1 18  ? 10.857  29.931  23.595  1.00  44.99  ? 18   LYS A CD  1 
ATOM   123  C CE  . LYS A 1 18  ? 11.477  31.269  23.938  1.00  46.38  ? 18   LYS A CE  1 
ATOM   124  N NZ  . LYS A 1 18  ? 12.863  31.474  23.366  1.00  47.40  ? 18   LYS A NZ  1 
ATOM   125  N N   . ILE A 1 19  ? 9.984   24.418  24.293  1.00  42.94  ? 19   ILE A N   1 
ATOM   126  C CA  . ILE A 1 19  ? 9.018   23.336  24.459  1.00  42.10  ? 19   ILE A CA  1 
ATOM   127  C C   . ILE A 1 19  ? 9.470   22.337  25.535  1.00  42.01  ? 19   ILE A C   1 
ATOM   128  O O   . ILE A 1 19  ? 8.704   22.004  26.453  1.00  41.74  ? 19   ILE A O   1 
ATOM   129  C CB  . ILE A 1 19  ? 8.743   22.624  23.095  1.00  41.99  ? 19   ILE A CB  1 
ATOM   130  C CG1 . ILE A 1 19  ? 8.004   23.582  22.138  1.00  41.41  ? 19   ILE A CG1 1 
ATOM   131  C CG2 . ILE A 1 19  ? 7.916   21.337  23.289  1.00  41.81  ? 19   ILE A CG2 1 
ATOM   132  C CD1 . ILE A 1 19  ? 8.154   23.262  20.681  1.00  40.45  ? 19   ILE A CD1 1 
ATOM   133  N N   . ALA A 1 20  ? 10.716  21.878  25.427  1.00  41.65  ? 20   ALA A N   1 
ATOM   134  C CA  . ALA A 1 20  ? 11.261  20.912  26.375  1.00  41.73  ? 20   ALA A CA  1 
ATOM   135  C C   . ALA A 1 20  ? 11.315  21.441  27.820  1.00  41.87  ? 20   ALA A C   1 
ATOM   136  O O   . ALA A 1 20  ? 11.064  20.690  28.770  1.00  41.56  ? 20   ALA A O   1 
ATOM   137  C CB  . ALA A 1 20  ? 12.621  20.424  25.921  1.00  41.63  ? 20   ALA A CB  1 
ATOM   138  N N   . ASP A 1 21  ? 11.627  22.726  27.981  1.00  42.14  ? 21   ASP A N   1 
ATOM   139  C CA  . ASP A 1 21  ? 11.635  23.344  29.306  1.00  42.72  ? 21   ASP A CA  1 
ATOM   140  C C   . ASP A 1 21  ? 10.230  23.283  29.925  1.00  42.78  ? 21   ASP A C   1 
ATOM   141  O O   . ASP A 1 21  ? 10.063  22.853  31.067  1.00  42.65  ? 21   ASP A O   1 
ATOM   142  C CB  . ASP A 1 21  ? 12.141  24.794  29.239  1.00  42.96  ? 21   ASP A CB  1 
ATOM   143  C CG  . ASP A 1 21  ? 13.565  24.911  28.682  1.00  43.67  ? 21   ASP A CG  1 
ATOM   144  O OD1 . ASP A 1 21  ? 14.336  23.919  28.687  1.00  43.94  ? 21   ASP A OD1 1 
ATOM   145  O OD2 . ASP A 1 21  ? 13.917  26.024  28.234  1.00  45.04  ? 21   ASP A OD2 1 
ATOM   146  N N   . ARG A 1 22  ? 9.226   23.673  29.140  1.00  42.88  ? 22   ARG A N   1 
ATOM   147  C CA  . ARG A 1 22  ? 7.826   23.717  29.588  1.00  43.00  ? 22   ARG A CA  1 
ATOM   148  C C   . ARG A 1 22  ? 7.242   22.378  29.994  1.00  42.79  ? 22   ARG A C   1 
ATOM   149  O O   . ARG A 1 22  ? 6.234   22.338  30.699  1.00  43.21  ? 22   ARG A O   1 
ATOM   150  C CB  . ARG A 1 22  ? 6.928   24.323  28.509  1.00  42.91  ? 22   ARG A CB  1 
ATOM   151  C CG  . ARG A 1 22  ? 7.124   25.802  28.298  1.00  43.69  ? 22   ARG A CG  1 
ATOM   152  C CD  . ARG A 1 22  ? 6.047   26.329  27.400  1.00  46.52  ? 22   ARG A CD  1 
ATOM   153  N NE  . ARG A 1 22  ? 6.232   27.739  27.073  1.00  48.54  ? 22   ARG A NE  1 
ATOM   154  C CZ  . ARG A 1 22  ? 5.797   28.752  27.822  1.00  49.54  ? 22   ARG A CZ  1 
ATOM   155  N NH1 . ARG A 1 22  ? 5.139   28.524  28.960  1.00  48.51  ? 22   ARG A NH1 1 
ATOM   156  N NH2 . ARG A 1 22  ? 6.016   29.996  27.417  1.00  49.86  ? 22   ARG A NH2 1 
ATOM   157  N N   . LEU A 1 23  ? 7.840   21.293  29.514  1.00  42.58  ? 23   LEU A N   1 
ATOM   158  C CA  . LEU A 1 23  ? 7.409   19.948  29.888  1.00  42.11  ? 23   LEU A CA  1 
ATOM   159  C C   . LEU A 1 23  ? 8.402   19.339  30.880  1.00  41.95  ? 23   LEU A C   1 
ATOM   160  O O   . LEU A 1 23  ? 8.254   18.186  31.289  1.00  41.89  ? 23   LEU A O   1 
ATOM   161  C CB  . LEU A 1 23  ? 7.274   19.060  28.643  1.00  42.36  ? 23   LEU A CB  1 
ATOM   162  C CG  . LEU A 1 23  ? 6.390   19.537  27.479  1.00  41.85  ? 23   LEU A CG  1 
ATOM   163  C CD1 . LEU A 1 23  ? 6.773   18.840  26.188  1.00  41.48  ? 23   LEU A CD1 1 
ATOM   164  C CD2 . LEU A 1 23  ? 4.924   19.310  27.783  1.00  41.43  ? 23   LEU A CD2 1 
ATOM   165  N N   . GLY A 1 24  ? 9.414   20.123  31.257  1.00  41.56  ? 24   GLY A N   1 
ATOM   166  C CA  . GLY A 1 24  ? 10.429  19.687  32.211  1.00  41.16  ? 24   GLY A CA  1 
ATOM   167  C C   . GLY A 1 24  ? 11.391  18.650  31.653  1.00  41.16  ? 24   GLY A C   1 
ATOM   168  O O   . GLY A 1 24  ? 11.819  17.737  32.375  1.00  40.87  ? 24   GLY A O   1 
ATOM   169  N N   . LEU A 1 25  ? 11.747  18.795  30.376  1.00  41.00  ? 25   LEU A N   1 
ATOM   170  C CA  . LEU A 1 25  ? 12.610  17.819  29.708  1.00  41.16  ? 25   LEU A CA  1 
ATOM   171  C C   . LEU A 1 25  ? 13.874  18.434  29.134  1.00  41.26  ? 25   LEU A C   1 
ATOM   172  O O   . LEU A 1 25  ? 13.972  19.658  28.998  1.00  41.67  ? 25   LEU A O   1 
ATOM   173  C CB  . LEU A 1 25  ? 11.845  17.081  28.599  1.00  40.81  ? 25   LEU A CB  1 
ATOM   174  C CG  . LEU A 1 25  ? 10.558  16.340  28.976  1.00  41.23  ? 25   LEU A CG  1 
ATOM   175  C CD1 . LEU A 1 25  ? 10.032  15.617  27.741  1.00  41.05  ? 25   LEU A CD1 1 
ATOM   176  C CD2 . LEU A 1 25  ? 10.742  15.360  30.161  1.00  40.13  ? 25   LEU A CD2 1 
ATOM   177  N N   . GLU A 1 26  ? 14.844  17.577  28.825  0.77  41.22  ? 26   GLU A N   1 
ATOM   178  C CA  . GLU A 1 26  ? 15.987  17.957  28.002  0.77  41.63  ? 26   GLU A CA  1 
ATOM   179  C C   . GLU A 1 26  ? 15.776  17.435  26.583  0.77  41.42  ? 26   GLU A C   1 
ATOM   180  O O   . GLU A 1 26  ? 15.268  16.323  26.391  0.77  41.62  ? 26   GLU A O   1 
ATOM   181  C CB  . GLU A 1 26  ? 17.289  17.386  28.568  0.77  41.81  ? 26   GLU A CB  1 
ATOM   182  C CG  . GLU A 1 26  ? 17.886  18.147  29.750  0.77  42.51  ? 26   GLU A CG  1 
ATOM   183  C CD  . GLU A 1 26  ? 19.141  17.471  30.282  0.77  44.39  ? 26   GLU A CD  1 
ATOM   184  O OE1 . GLU A 1 26  ? 19.811  16.750  29.498  0.77  44.85  ? 26   GLU A OE1 1 
ATOM   185  O OE2 . GLU A 1 26  ? 19.453  17.657  31.483  0.77  44.01  ? 26   GLU A OE2 1 
ATOM   186  N N   . LEU A 1 27  ? 16.151  18.239  25.590  1.00  41.28  ? 27   LEU A N   1 
ATOM   187  C CA  . LEU A 1 27  ? 16.112  17.789  24.193  1.00  40.89  ? 27   LEU A CA  1 
ATOM   188  C C   . LEU A 1 27  ? 16.956  16.532  24.065  1.00  40.97  ? 27   LEU A C   1 
ATOM   189  O O   . LEU A 1 27  ? 17.996  16.412  24.713  1.00  41.18  ? 27   LEU A O   1 
ATOM   190  C CB  . LEU A 1 27  ? 16.627  18.870  23.230  1.00  40.26  ? 27   LEU A CB  1 
ATOM   191  C CG  . LEU A 1 27  ? 15.828  20.166  23.081  1.00  39.36  ? 27   LEU A CG  1 
ATOM   192  C CD1 . LEU A 1 27  ? 16.636  21.197  22.293  1.00  38.89  ? 27   LEU A CD1 1 
ATOM   193  C CD2 . LEU A 1 27  ? 14.473  19.932  22.441  1.00  37.65  ? 27   LEU A CD2 1 
ATOM   194  N N   . GLY A 1 28  ? 16.494  15.583  23.259  1.00  41.02  ? 28   GLY A N   1 
ATOM   195  C CA  . GLY A 1 28  ? 17.234  14.343  23.034  1.00  41.39  ? 28   GLY A CA  1 
ATOM   196  C C   . GLY A 1 28  ? 18.615  14.578  22.447  1.00  41.54  ? 28   GLY A C   1 
ATOM   197  O O   . GLY A 1 28  ? 18.804  15.506  21.669  1.00  41.29  ? 28   GLY A O   1 
ATOM   198  N N   . LYS A 1 29  ? 19.574  13.742  22.834  0.10  42.29  ? 29   LYS A N   1 
ATOM   199  C CA  . LYS A 1 29  ? 20.931  13.823  22.306  0.10  43.02  ? 29   LYS A CA  1 
ATOM   200  C C   . LYS A 1 29  ? 20.967  13.303  20.874  0.10  43.61  ? 29   LYS A C   1 
ATOM   201  O O   . LYS A 1 29  ? 20.747  12.115  20.633  0.10  43.63  ? 29   LYS A O   1 
ATOM   202  C CB  . LYS A 1 29  ? 21.898  13.024  23.182  0.10  42.98  ? 29   LYS A CB  1 
ATOM   203  C CG  . LYS A 1 29  ? 21.949  13.482  24.631  0.10  43.06  ? 29   LYS A CG  1 
ATOM   204  C CD  . LYS A 1 29  ? 22.877  12.604  25.456  0.10  43.16  ? 29   LYS A CD  1 
ATOM   205  C CE  . LYS A 1 29  ? 22.429  11.152  25.437  0.10  43.23  ? 29   LYS A CE  1 
ATOM   206  N NZ  . LYS A 1 29  ? 21.055  10.989  25.987  0.10  43.32  ? 29   LYS A NZ  1 
ATOM   207  N N   . VAL A 1 30  ? 21.227  14.202  19.930  1.00  44.27  ? 30   VAL A N   1 
ATOM   208  C CA  . VAL A 1 30  ? 21.331  13.838  18.516  1.00  45.40  ? 30   VAL A CA  1 
ATOM   209  C C   . VAL A 1 30  ? 22.512  14.504  17.804  1.00  46.06  ? 30   VAL A C   1 
ATOM   210  O O   . VAL A 1 30  ? 22.674  15.712  17.869  1.00  46.17  ? 30   VAL A O   1 
ATOM   211  C CB  . VAL A 1 30  ? 19.976  14.081  17.734  1.00  45.73  ? 30   VAL A CB  1 
ATOM   212  C CG1 . VAL A 1 30  ? 19.439  15.519  17.917  1.00  45.33  ? 30   VAL A CG1 1 
ATOM   213  C CG2 . VAL A 1 30  ? 20.121  13.715  16.235  1.00  45.14  ? 30   VAL A CG2 1 
ATOM   214  N N   . VAL A 1 31  ? 23.326  13.701  17.124  1.00  47.46  ? 31   VAL A N   1 
ATOM   215  C CA  . VAL A 1 31  ? 24.443  14.203  16.318  1.00  48.92  ? 31   VAL A CA  1 
ATOM   216  C C   . VAL A 1 31  ? 23.988  14.393  14.877  1.00  49.67  ? 31   VAL A C   1 
ATOM   217  O O   . VAL A 1 31  ? 23.822  13.410  14.155  1.00  49.58  ? 31   VAL A O   1 
ATOM   218  C CB  . VAL A 1 31  ? 25.625  13.195  16.272  1.00  49.32  ? 31   VAL A CB  1 
ATOM   219  C CG1 . VAL A 1 31  ? 26.820  13.797  15.501  1.00  49.82  ? 31   VAL A CG1 1 
ATOM   220  C CG2 . VAL A 1 31  ? 26.041  12.722  17.684  1.00  49.19  ? 31   VAL A CG2 1 
ATOM   221  N N   . THR A 1 32  ? 23.790  15.650  14.470  1.00  50.76  ? 32   THR A N   1 
ATOM   222  C CA  . THR A 1 32  ? 23.436  15.977  13.088  1.00  52.08  ? 32   THR A CA  1 
ATOM   223  C C   . THR A 1 32  ? 24.601  16.658  12.366  1.00  52.59  ? 32   THR A C   1 
ATOM   224  O O   . THR A 1 32  ? 25.154  17.638  12.868  1.00  53.36  ? 32   THR A O   1 
ATOM   225  C CB  . THR A 1 32  ? 22.210  16.898  13.000  1.00  52.15  ? 32   THR A CB  1 
ATOM   226  O OG1 . THR A 1 32  ? 22.559  18.210  13.463  1.00  53.13  ? 32   THR A OG1 1 
ATOM   227  C CG2 . THR A 1 32  ? 21.047  16.346  13.820  1.00  53.10  ? 32   THR A CG2 1 
ATOM   228  N N   . LYS A 1 33  ? 24.966  16.149  11.194  0.010 52.95  ? 33   LYS A N   1 
ATOM   229  C CA  . LYS A 1 33  ? 26.078  16.719  10.434  0.010 53.25  ? 33   LYS A CA  1 
ATOM   230  C C   . LYS A 1 33  ? 25.784  16.777  8.940   0.010 53.56  ? 33   LYS A C   1 
ATOM   231  O O   . LYS A 1 33  ? 24.996  15.981  8.423   0.010 53.57  ? 33   LYS A O   1 
ATOM   232  C CB  . LYS A 1 33  ? 27.365  15.932  10.692  0.010 53.21  ? 33   LYS A CB  1 
ATOM   233  C CG  . LYS A 1 33  ? 27.271  14.458  10.340  0.010 53.16  ? 33   LYS A CG  1 
ATOM   234  C CD  . LYS A 1 33  ? 28.575  13.739  10.638  0.010 53.09  ? 33   LYS A CD  1 
ATOM   235  C CE  . LYS A 1 33  ? 28.330  12.283  10.996  0.010 53.07  ? 33   LYS A CE  1 
ATOM   236  N NZ  . LYS A 1 33  ? 28.211  12.086  12.467  0.010 53.07  ? 33   LYS A NZ  1 
ATOM   237  N N   . LYS A 1 34  ? 26.423  17.724  8.256   1.00  54.03  ? 34   LYS A N   1 
ATOM   238  C CA  . LYS A 1 34  ? 26.263  17.882  6.818   1.00  54.48  ? 34   LYS A CA  1 
ATOM   239  C C   . LYS A 1 34  ? 27.591  17.648  6.118   1.00  54.88  ? 34   LYS A C   1 
ATOM   240  O O   . LYS A 1 34  ? 28.551  18.394  6.326   1.00  55.11  ? 34   LYS A O   1 
ATOM   241  C CB  . LYS A 1 34  ? 25.744  19.276  6.470   1.00  54.63  ? 34   LYS A CB  1 
ATOM   242  C CG  . LYS A 1 34  ? 24.315  19.590  6.910   1.00  54.66  ? 34   LYS A CG  1 
ATOM   243  C CD  . LYS A 1 34  ? 23.590  20.459  5.863   1.00  54.14  ? 34   LYS A CD  1 
ATOM   244  C CE  . LYS A 1 34  ? 24.385  21.696  5.453   1.00  54.23  ? 34   LYS A CE  1 
ATOM   245  N NZ  . LYS A 1 34  ? 23.742  22.407  4.290   1.00  54.98  ? 34   LYS A NZ  1 
ATOM   246  N N   . PHE A 1 35  ? 27.646  16.600  5.300   1.00  55.34  ? 35   PHE A N   1 
ATOM   247  C CA  . PHE A 1 35  ? 28.833  16.298  4.498   1.00  55.79  ? 35   PHE A CA  1 
ATOM   248  C C   . PHE A 1 35  ? 29.133  17.424  3.509   1.00  55.86  ? 35   PHE A C   1 
ATOM   249  O O   . PHE A 1 35  ? 28.230  18.151  3.078   1.00  55.91  ? 35   PHE A O   1 
ATOM   250  C CB  . PHE A 1 35  ? 28.667  14.976  3.738   1.00  55.93  ? 35   PHE A CB  1 
ATOM   251  C CG  . PHE A 1 35  ? 28.536  13.761  4.625   1.00  57.02  ? 35   PHE A CG  1 
ATOM   252  C CD1 . PHE A 1 35  ? 27.559  12.803  4.364   1.00  57.53  ? 35   PHE A CD1 1 
ATOM   253  C CD2 . PHE A 1 35  ? 29.389  13.569  5.715   1.00  57.92  ? 35   PHE A CD2 1 
ATOM   254  C CE1 . PHE A 1 35  ? 27.428  11.670  5.167   1.00  57.57  ? 35   PHE A CE1 1 
ATOM   255  C CE2 . PHE A 1 35  ? 29.266  12.441  6.526   1.00  58.39  ? 35   PHE A CE2 1 
ATOM   256  C CZ  . PHE A 1 35  ? 28.282  11.489  6.247   1.00  58.39  ? 35   PHE A CZ  1 
ATOM   257  N N   . SER A 1 36  ? 30.410  17.556  3.155   0.010 55.98  ? 36   SER A N   1 
ATOM   258  C CA  . SER A 1 36  ? 30.885  18.619  2.266   0.010 56.13  ? 36   SER A CA  1 
ATOM   259  C C   . SER A 1 36  ? 30.115  18.665  0.947   0.010 56.30  ? 36   SER A C   1 
ATOM   260  O O   . SER A 1 36  ? 30.081  19.693  0.271   0.010 56.31  ? 36   SER A O   1 
ATOM   261  C CB  . SER A 1 36  ? 32.385  18.466  2.006   0.010 56.09  ? 36   SER A CB  1 
ATOM   262  O OG  . SER A 1 36  ? 32.907  19.604  1.344   0.010 56.08  ? 36   SER A OG  1 
ATOM   263  N N   . ASN A 1 37  ? 29.496  17.543  0.592   0.84  56.64  ? 37   ASN A N   1 
ATOM   264  C CA  . ASN A 1 37  ? 28.592  17.488  -0.555  0.84  56.86  ? 37   ASN A CA  1 
ATOM   265  C C   . ASN A 1 37  ? 27.114  17.645  -0.150  0.84  56.94  ? 37   ASN A C   1 
ATOM   266  O O   . ASN A 1 37  ? 26.229  16.985  -0.705  0.84  57.03  ? 37   ASN A O   1 
ATOM   267  C CB  . ASN A 1 37  ? 28.831  16.214  -1.387  0.84  56.96  ? 37   ASN A CB  1 
ATOM   268  C CG  . ASN A 1 37  ? 28.736  14.929  -0.563  0.84  57.48  ? 37   ASN A CG  1 
ATOM   269  O OD1 . ASN A 1 37  ? 28.911  14.938  0.655   0.84  58.94  ? 37   ASN A OD1 1 
ATOM   270  N ND2 . ASN A 1 37  ? 28.465  13.816  -1.238  0.84  57.81  ? 37   ASN A ND2 1 
ATOM   271  N N   . GLN A 1 38  ? 26.872  18.527  0.825   1.00  56.99  ? 38   GLN A N   1 
ATOM   272  C CA  . GLN A 1 38  ? 25.523  18.922  1.287   1.00  57.11  ? 38   GLN A CA  1 
ATOM   273  C C   . GLN A 1 38  ? 24.612  17.786  1.836   1.00  56.90  ? 38   GLN A C   1 
ATOM   274  O O   . GLN A 1 38  ? 23.453  18.040  2.245   1.00  57.17  ? 38   GLN A O   1 
ATOM   275  C CB  . GLN A 1 38  ? 24.801  19.767  0.215   1.00  57.26  ? 38   GLN A CB  1 
ATOM   276  C CG  . GLN A 1 38  ? 25.723  20.705  -0.622  1.00  58.84  ? 38   GLN A CG  1 
ATOM   277  C CD  . GLN A 1 38  ? 26.174  22.010  0.102   1.00  60.97  ? 38   GLN A CD  1 
ATOM   278  O OE1 . GLN A 1 38  ? 26.215  22.092  1.342   1.00  61.15  ? 38   GLN A OE1 1 
ATOM   279  N NE2 . GLN A 1 38  ? 26.522  23.026  -0.692  1.00  59.99  ? 38   GLN A NE2 1 
ATOM   280  N N   . GLU A 1 39  ? 25.149  16.554  1.878   1.00  56.34  ? 39   GLU A N   1 
ATOM   281  C CA  . GLU A 1 39  ? 24.422  15.383  2.405   1.00  55.68  ? 39   GLU A CA  1 
ATOM   282  C C   . GLU A 1 39  ? 24.221  15.408  3.925   1.00  55.31  ? 39   GLU A C   1 
ATOM   283  O O   . GLU A 1 39  ? 25.188  15.546  4.681   1.00  55.19  ? 39   GLU A O   1 
ATOM   284  C CB  . GLU A 1 39  ? 25.174  14.103  2.050   1.00  55.72  ? 39   GLU A CB  1 
ATOM   285  C CG  . GLU A 1 39  ? 24.621  13.330  0.885   1.00  56.07  ? 39   GLU A CG  1 
ATOM   286  C CD  . GLU A 1 39  ? 24.929  11.842  0.985   1.00  57.06  ? 39   GLU A CD  1 
ATOM   287  O OE1 . GLU A 1 39  ? 24.504  11.194  1.966   1.00  56.90  ? 39   GLU A OE1 1 
ATOM   288  O OE2 . GLU A 1 39  ? 25.596  11.309  0.077   1.00  58.43  ? 39   GLU A OE2 1 
ATOM   289  N N   . THR A 1 40  ? 22.978  15.222  4.368   1.00  54.77  ? 40   THR A N   1 
ATOM   290  C CA  . THR A 1 40  ? 22.644  15.254  5.797   1.00  54.25  ? 40   THR A CA  1 
ATOM   291  C C   . THR A 1 40  ? 22.937  13.923  6.493   1.00  54.14  ? 40   THR A C   1 
ATOM   292  O O   . THR A 1 40  ? 22.520  12.847  6.031   1.00  54.01  ? 40   THR A O   1 
ATOM   293  C CB  . THR A 1 40  ? 21.158  15.617  6.035   1.00  54.30  ? 40   THR A CB  1 
ATOM   294  O OG1 . THR A 1 40  ? 20.808  16.777  5.269   1.00  54.54  ? 40   THR A OG1 1 
ATOM   295  C CG2 . THR A 1 40  ? 20.887  15.893  7.513   1.00  54.31  ? 40   THR A CG2 1 
ATOM   296  N N   . CYS A 1 41  ? 23.652  14.016  7.613   0.62  53.77  ? 41   CYS A N   1 
ATOM   297  C CA  . CYS A 1 41  ? 23.943  12.874  8.470   0.62  53.43  ? 41   CYS A CA  1 
ATOM   298  C C   . CYS A 1 41  ? 23.348  13.121  9.858   0.62  52.94  ? 41   CYS A C   1 
ATOM   299  O O   . CYS A 1 41  ? 23.650  14.130  10.500  0.62  52.98  ? 41   CYS A O   1 
ATOM   300  C CB  . CYS A 1 41  ? 25.455  12.642  8.541   0.62  53.46  ? 41   CYS A CB  1 
ATOM   301  S SG  . CYS A 1 41  ? 26.037  11.722  9.989   0.62  55.27  ? 41   CYS A SG  1 
ATOM   302  N N   . VAL A 1 42  ? 22.492  12.200  10.300  1.00  52.40  ? 42   VAL A N   1 
ATOM   303  C CA  . VAL A 1 42  ? 21.814  12.288  11.601  1.00  51.79  ? 42   VAL A CA  1 
ATOM   304  C C   . VAL A 1 42  ? 22.028  11.006  12.396  1.00  51.44  ? 42   VAL A C   1 
ATOM   305  O O   . VAL A 1 42  ? 21.956  9.904   11.847  1.00  51.52  ? 42   VAL A O   1 
ATOM   306  C CB  . VAL A 1 42  ? 20.291  12.561  11.439  1.00  51.82  ? 42   VAL A CB  1 
ATOM   307  C CG1 . VAL A 1 42  ? 19.496  12.067  12.646  1.00  51.86  ? 42   VAL A CG1 1 
ATOM   308  C CG2 . VAL A 1 42  ? 20.030  14.037  11.210  1.00  51.96  ? 42   VAL A CG2 1 
ATOM   309  N N   . GLU A 1 43  ? 22.296  11.153  13.689  0.81  50.96  ? 43   GLU A N   1 
ATOM   310  C CA  . GLU A 1 43  ? 22.498  9.998   14.553  0.81  50.63  ? 43   GLU A CA  1 
ATOM   311  C C   . GLU A 1 43  ? 21.813  10.204  15.897  0.81  50.00  ? 43   GLU A C   1 
ATOM   312  O O   . GLU A 1 43  ? 22.140  11.131  16.641  0.81  49.98  ? 43   GLU A O   1 
ATOM   313  C CB  . GLU A 1 43  ? 23.987  9.734   14.760  0.81  50.77  ? 43   GLU A CB  1 
ATOM   314  C CG  . GLU A 1 43  ? 24.387  8.273   14.642  0.81  51.90  ? 43   GLU A CG  1 
ATOM   315  C CD  . GLU A 1 43  ? 25.086  7.971   13.323  0.81  54.06  ? 43   GLU A CD  1 
ATOM   316  O OE1 . GLU A 1 43  ? 26.195  7.375   13.357  0.81  53.75  ? 43   GLU A OE1 1 
ATOM   317  O OE2 . GLU A 1 43  ? 24.533  8.343   12.257  0.81  54.89  ? 43   GLU A OE2 1 
ATOM   318  N N   . ILE A 1 44  ? 20.858  9.333   16.204  1.00  49.26  ? 44   ILE A N   1 
ATOM   319  C CA  . ILE A 1 44  ? 20.155  9.396   17.479  1.00  48.51  ? 44   ILE A CA  1 
ATOM   320  C C   . ILE A 1 44  ? 21.071  8.841   18.567  1.00  48.14  ? 44   ILE A C   1 
ATOM   321  O O   . ILE A 1 44  ? 21.254  7.623   18.700  1.00  47.99  ? 44   ILE A O   1 
ATOM   322  C CB  . ILE A 1 44  ? 18.796  8.655   17.442  1.00  48.48  ? 44   ILE A CB  1 
ATOM   323  C CG1 . ILE A 1 44  ? 17.907  9.184   16.297  1.00  48.78  ? 44   ILE A CG1 1 
ATOM   324  C CG2 . ILE A 1 44  ? 18.085  8.766   18.788  1.00  48.21  ? 44   ILE A CG2 1 
ATOM   325  C CD1 . ILE A 1 44  ? 17.257  10.556  16.562  1.00  48.00  ? 44   ILE A CD1 1 
ATOM   326  N N   . GLY A 1 45  ? 21.646  9.756   19.343  1.00  47.51  ? 45   GLY A N   1 
ATOM   327  C CA  . GLY A 1 45  ? 22.621  9.409   20.365  1.00  46.54  ? 45   GLY A CA  1 
ATOM   328  C C   . GLY A 1 45  ? 22.039  8.856   21.646  1.00  45.82  ? 45   GLY A C   1 
ATOM   329  O O   . GLY A 1 45  ? 22.610  9.048   22.717  1.00  46.26  ? 45   GLY A O   1 
ATOM   330  N N   . GLU A 1 46  ? 20.905  8.167   21.538  0.75  44.94  ? 46   GLU A N   1 
ATOM   331  C CA  . GLU A 1 46  ? 20.283  7.463   22.669  0.75  43.84  ? 46   GLU A CA  1 
ATOM   332  C C   . GLU A 1 46  ? 19.199  6.504   22.209  0.75  43.09  ? 46   GLU A C   1 
ATOM   333  O O   . GLU A 1 46  ? 18.750  6.565   21.062  0.75  42.88  ? 46   GLU A O   1 
ATOM   334  C CB  . GLU A 1 46  ? 19.705  8.438   23.699  0.75  44.11  ? 46   GLU A CB  1 
ATOM   335  C CG  . GLU A 1 46  ? 18.831  9.554   23.133  0.75  43.70  ? 46   GLU A CG  1 
ATOM   336  C CD  . GLU A 1 46  ? 18.495  10.584  24.190  0.75  43.54  ? 46   GLU A CD  1 
ATOM   337  O OE1 . GLU A 1 46  ? 17.845  10.209  25.191  0.75  43.87  ? 46   GLU A OE1 1 
ATOM   338  O OE2 . GLU A 1 46  ? 18.898  11.759  24.034  0.75  43.04  ? 46   GLU A OE2 1 
ATOM   339  N N   . SER A 1 47  ? 18.778  5.623   23.112  1.00  42.11  ? 47   SER A N   1 
ATOM   340  C CA  . SER A 1 47  ? 17.703  4.682   22.816  1.00  41.07  ? 47   SER A CA  1 
ATOM   341  C C   . SER A 1 47  ? 16.344  5.382   22.842  1.00  40.25  ? 47   SER A C   1 
ATOM   342  O O   . SER A 1 47  ? 15.962  5.969   23.854  1.00  40.39  ? 47   SER A O   1 
ATOM   343  C CB  . SER A 1 47  ? 17.716  3.505   23.788  1.00  41.08  ? 47   SER A CB  1 
ATOM   344  O OG  . SER A 1 47  ? 17.103  2.366   23.201  1.00  41.34  ? 47   SER A OG  1 
ATOM   345  N N   . VAL A 1 48  ? 15.640  5.336   21.713  1.00  39.24  ? 48   VAL A N   1 
ATOM   346  C CA  . VAL A 1 48  ? 14.252  5.792   21.627  1.00  38.47  ? 48   VAL A CA  1 
ATOM   347  C C   . VAL A 1 48  ? 13.245  4.635   21.609  1.00  38.01  ? 48   VAL A C   1 
ATOM   348  O O   . VAL A 1 48  ? 12.068  4.833   21.300  1.00  37.88  ? 48   VAL A O   1 
ATOM   349  C CB  . VAL A 1 48  ? 13.996  6.682   20.384  1.00  38.65  ? 48   VAL A CB  1 
ATOM   350  C CG1 . VAL A 1 48  ? 14.774  7.984   20.485  1.00  38.30  ? 48   VAL A CG1 1 
ATOM   351  C CG2 . VAL A 1 48  ? 14.301  5.918   19.071  1.00  38.38  ? 48   VAL A CG2 1 
ATOM   352  N N   . ARG A 1 49  ? 13.711  3.434   21.937  1.00  37.57  ? 49   ARG A N   1 
ATOM   353  C CA  . ARG A 1 49  ? 12.880  2.230   21.909  1.00  37.31  ? 49   ARG A CA  1 
ATOM   354  C C   . ARG A 1 49  ? 11.754  2.315   22.935  1.00  37.77  ? 49   ARG A C   1 
ATOM   355  O O   . ARG A 1 49  ? 11.981  2.718   24.076  1.00  37.77  ? 49   ARG A O   1 
ATOM   356  C CB  . ARG A 1 49  ? 13.742  1.012   22.204  1.00  37.07  ? 49   ARG A CB  1 
ATOM   357  C CG  . ARG A 1 49  ? 13.096  -0.297  21.881  1.00  35.38  ? 49   ARG A CG  1 
ATOM   358  C CD  . ARG A 1 49  ? 14.026  -1.435  22.211  1.00  32.59  ? 49   ARG A CD  1 
ATOM   359  N NE  . ARG A 1 49  ? 15.222  -1.462  21.374  1.00  30.58  ? 49   ARG A NE  1 
ATOM   360  C CZ  . ARG A 1 49  ? 15.343  -2.146  20.239  1.00  28.89  ? 49   ARG A CZ  1 
ATOM   361  N NH1 . ARG A 1 49  ? 14.326  -2.855  19.761  1.00  29.50  ? 49   ARG A NH1 1 
ATOM   362  N NH2 . ARG A 1 49  ? 16.487  -2.104  19.578  1.00  26.93  ? 49   ARG A NH2 1 
ATOM   363  N N   . GLY A 1 50  ? 10.540  1.950   22.522  1.00  37.80  ? 50   GLY A N   1 
ATOM   364  C CA  . GLY A 1 50  ? 9.372   2.001   23.397  1.00  37.60  ? 50   GLY A CA  1 
ATOM   365  C C   . GLY A 1 50  ? 8.960   3.396   23.858  1.00  37.90  ? 50   GLY A C   1 
ATOM   366  O O   . GLY A 1 50  ? 8.066   3.541   24.713  1.00  37.59  ? 50   GLY A O   1 
ATOM   367  N N   . GLU A 1 51  ? 9.586   4.422   23.279  1.00  38.22  ? 51   GLU A N   1 
ATOM   368  C CA  . GLU A 1 51  ? 9.353   5.812   23.687  1.00  38.74  ? 51   GLU A CA  1 
ATOM   369  C C   . GLU A 1 51  ? 8.425   6.571   22.750  1.00  38.37  ? 51   GLU A C   1 
ATOM   370  O O   . GLU A 1 51  ? 8.354   6.250   21.562  1.00  38.70  ? 51   GLU A O   1 
ATOM   371  C CB  . GLU A 1 51  ? 10.687  6.553   23.847  1.00  39.10  ? 51   GLU A CB  1 
ATOM   372  C CG  . GLU A 1 51  ? 11.563  5.967   24.958  1.00  40.83  ? 51   GLU A CG  1 
ATOM   373  C CD  . GLU A 1 51  ? 12.726  6.853   25.337  1.00  43.75  ? 51   GLU A CD  1 
ATOM   374  O OE1 . GLU A 1 51  ? 13.448  7.321   24.435  1.00  44.76  ? 51   GLU A OE1 1 
ATOM   375  O OE2 . GLU A 1 51  ? 12.925  7.084   26.552  1.00  46.35  ? 51   GLU A OE2 1 
ATOM   376  N N   . ASP A 1 52  ? 7.716   7.564   23.300  1.00  38.12  ? 52   ASP A N   1 
ATOM   377  C CA  . ASP A 1 52  ? 6.793   8.437   22.546  1.00  38.06  ? 52   ASP A CA  1 
ATOM   378  C C   . ASP A 1 52  ? 7.557   9.682   22.043  1.00  37.51  ? 52   ASP A C   1 
ATOM   379  O O   . ASP A 1 52  ? 7.764   10.651  22.786  1.00  37.59  ? 52   ASP A O   1 
ATOM   380  C CB  . ASP A 1 52  ? 5.584   8.819   23.425  1.00  37.97  ? 52   ASP A CB  1 
ATOM   381  C CG  . ASP A 1 52  ? 4.426   9.426   22.625  1.00  40.03  ? 52   ASP A CG  1 
ATOM   382  O OD1 . ASP A 1 52  ? 4.129   8.942   21.508  1.00  41.43  ? 52   ASP A OD1 1 
ATOM   383  O OD2 . ASP A 1 52  ? 3.784   10.384  23.123  1.00  41.69  ? 52   ASP A OD2 1 
ATOM   384  N N   . VAL A 1 53  ? 7.986   9.631   20.786  1.00  36.79  ? 53   VAL A N   1 
ATOM   385  C CA  . VAL A 1 53  ? 8.970   10.582  20.246  1.00  36.59  ? 53   VAL A CA  1 
ATOM   386  C C   . VAL A 1 53  ? 8.321   11.764  19.511  1.00  36.23  ? 53   VAL A C   1 
ATOM   387  O O   . VAL A 1 53  ? 7.378   11.586  18.758  1.00  36.35  ? 53   VAL A O   1 
ATOM   388  C CB  . VAL A 1 53  ? 10.006  9.865   19.325  1.00  36.38  ? 53   VAL A CB  1 
ATOM   389  C CG1 . VAL A 1 53  ? 11.106  10.802  18.903  1.00  36.25  ? 53   VAL A CG1 1 
ATOM   390  C CG2 . VAL A 1 53  ? 10.613  8.684   20.044  1.00  36.37  ? 53   VAL A CG2 1 
ATOM   391  N N   . TYR A 1 54  ? 8.840   12.963  19.751  1.00  35.95  ? 54   TYR A N   1 
ATOM   392  C CA  . TYR A 1 54  ? 8.354   14.186  19.111  1.00  35.71  ? 54   TYR A CA  1 
ATOM   393  C C   . TYR A 1 54  ? 9.517   14.929  18.464  1.00  35.75  ? 54   TYR A C   1 
ATOM   394  O O   . TYR A 1 54  ? 10.539  15.168  19.096  1.00  35.52  ? 54   TYR A O   1 
ATOM   395  C CB  . TYR A 1 54  ? 7.632   15.086  20.137  1.00  35.49  ? 54   TYR A CB  1 
ATOM   396  C CG  . TYR A 1 54  ? 6.367   14.458  20.670  1.00  33.89  ? 54   TYR A CG  1 
ATOM   397  C CD1 . TYR A 1 54  ? 6.410   13.509  21.692  1.00  32.95  ? 54   TYR A CD1 1 
ATOM   398  C CD2 . TYR A 1 54  ? 5.127   14.800  20.138  1.00  32.19  ? 54   TYR A CD2 1 
ATOM   399  C CE1 . TYR A 1 54  ? 5.246   12.921  22.165  1.00  33.59  ? 54   TYR A CE1 1 
ATOM   400  C CE2 . TYR A 1 54  ? 3.969   14.224  20.602  1.00  32.30  ? 54   TYR A CE2 1 
ATOM   401  C CZ  . TYR A 1 54  ? 4.032   13.286  21.606  1.00  33.45  ? 54   TYR A CZ  1 
ATOM   402  O OH  . TYR A 1 54  ? 2.875   12.715  22.043  1.00  35.78  ? 54   TYR A OH  1 
ATOM   403  N N   . ILE A 1 55  ? 9.362   15.267  17.190  1.00  36.34  ? 55   ILE A N   1 
ATOM   404  C CA  . ILE A 1 55  ? 10.393  16.020  16.476  1.00  36.83  ? 55   ILE A CA  1 
ATOM   405  C C   . ILE A 1 55  ? 9.850   17.371  16.011  1.00  37.40  ? 55   ILE A C   1 
ATOM   406  O O   . ILE A 1 55  ? 8.840   17.442  15.302  1.00  37.75  ? 55   ILE A O   1 
ATOM   407  C CB  . ILE A 1 55  ? 10.997  15.207  15.316  1.00  36.79  ? 55   ILE A CB  1 
ATOM   408  C CG1 . ILE A 1 55  ? 11.641  13.918  15.855  1.00  36.72  ? 55   ILE A CG1 1 
ATOM   409  C CG2 . ILE A 1 55  ? 12.046  16.029  14.589  1.00  36.43  ? 55   ILE A CG2 1 
ATOM   410  C CD1 . ILE A 1 55  ? 11.865  12.844  14.818  1.00  36.23  ? 55   ILE A CD1 1 
ATOM   411  N N   . VAL A 1 56  ? 10.511  18.433  16.459  1.00  37.81  ? 56   VAL A N   1 
ATOM   412  C CA  . VAL A 1 56  ? 10.133  19.803  16.138  1.00  38.55  ? 56   VAL A CA  1 
ATOM   413  C C   . VAL A 1 56  ? 11.068  20.300  15.043  1.00  39.36  ? 56   VAL A C   1 
ATOM   414  O O   . VAL A 1 56  ? 12.288  20.282  15.224  1.00  39.81  ? 56   VAL A O   1 
ATOM   415  C CB  . VAL A 1 56  ? 10.233  20.710  17.403  1.00  38.72  ? 56   VAL A CB  1 
ATOM   416  C CG1 . VAL A 1 56  ? 9.730   22.132  17.113  1.00  37.43  ? 56   VAL A CG1 1 
ATOM   417  C CG2 . VAL A 1 56  ? 9.472   20.062  18.606  1.00  37.80  ? 56   VAL A CG2 1 
ATOM   418  N N   . GLN A 1 57  ? 10.510  20.730  13.911  1.00  40.44  ? 57   GLN A N   1 
ATOM   419  C CA  . GLN A 1 57  ? 11.323  21.081  12.729  1.00  41.46  ? 57   GLN A CA  1 
ATOM   420  C C   . GLN A 1 57  ? 12.140  22.374  12.916  1.00  41.61  ? 57   GLN A C   1 
ATOM   421  O O   . GLN A 1 57  ? 11.771  23.234  13.741  1.00  41.64  ? 57   GLN A O   1 
ATOM   422  C CB  . GLN A 1 57  ? 10.467  21.107  11.450  1.00  41.77  ? 57   GLN A CB  1 
ATOM   423  C CG  . GLN A 1 57  ? 10.125  22.484  10.868  1.00  44.44  ? 57   GLN A CG  1 
ATOM   424  C CD  . GLN A 1 57  ? 9.050   23.254  11.664  1.00  47.07  ? 57   GLN A CD  1 
ATOM   425  O OE1 . GLN A 1 57  ? 8.008   23.664  11.098  1.00  45.37  ? 57   GLN A OE1 1 
ATOM   426  N NE2 . GLN A 1 57  ? 9.302   23.462  12.972  1.00  45.21  ? 57   GLN A NE2 1 
ATOM   427  N N   . SER A 1 58  ? 13.216  22.504  12.124  0.52  41.37  ? 58   SER A N   1 
ATOM   428  C CA  . SER A 1 58  ? 14.325  23.447  12.381  0.52  41.17  ? 58   SER A CA  1 
ATOM   429  C C   . SER A 1 58  ? 14.180  24.900  11.908  0.52  41.06  ? 58   SER A C   1 
ATOM   430  O O   . SER A 1 58  ? 14.301  25.886  12.808  0.52  41.49  ? 58   SER A O   1 
ATOM   431  C CB  . SER A 1 58  ? 15.635  22.897  11.818  0.52  41.21  ? 58   SER A CB  1 
ATOM   432  N N   . GLY A 1 59  ? 14.237  25.123  10.577  0.010 40.81  ? 59   GLY A N   1 
ATOM   433  C CA  . GLY A 1 59  ? 14.045  26.507  10.124  0.010 40.44  ? 59   GLY A CA  1 
ATOM   434  C C   . GLY A 1 59  ? 15.273  27.348  9.799   0.010 40.21  ? 59   GLY A C   1 
ATOM   435  O O   . GLY A 1 59  ? 15.126  28.509  9.399   0.010 40.19  ? 59   GLY A O   1 
ATOM   436  N N   . CYS A 1 60  ? 16.481  26.812  9.969   0.07  40.00  ? 60   CYS A N   1 
ATOM   437  C CA  . CYS A 1 60  ? 17.565  27.441  9.242   0.07  39.81  ? 60   CYS A CA  1 
ATOM   438  C C   . CYS A 1 60  ? 16.817  27.681  7.944   0.07  39.74  ? 60   CYS A C   1 
ATOM   439  O O   . CYS A 1 60  ? 16.080  26.805  7.490   0.07  39.75  ? 60   CYS A O   1 
ATOM   440  C CB  . CYS A 1 60  ? 18.726  26.478  9.029   0.07  39.80  ? 60   CYS A CB  1 
ATOM   441  S SG  . CYS A 1 60  ? 20.150  27.212  8.187   0.07  39.50  ? 60   CYS A SG  1 
ATOM   442  N N   . GLY A 1 61  ? 16.974  28.862  7.353   0.010 39.66  ? 61   GLY A N   1 
ATOM   443  C CA  . GLY A 1 61  ? 16.067  29.299  6.284   0.010 39.61  ? 61   GLY A CA  1 
ATOM   444  C C   . GLY A 1 61  ? 15.749  28.314  5.171   0.010 39.59  ? 61   GLY A C   1 
ATOM   445  O O   . GLY A 1 61  ? 14.789  28.502  4.424   0.010 39.57  ? 61   GLY A O   1 
ATOM   446  N N   . GLU A 1 62  ? 16.549  27.260  5.059   0.75  39.65  ? 62   GLU A N   1 
ATOM   447  C CA  . GLU A 1 62  ? 16.459  26.330  3.931   0.75  39.67  ? 62   GLU A CA  1 
ATOM   448  C C   . GLU A 1 62  ? 15.391  25.245  4.133   0.75  39.59  ? 62   GLU A C   1 
ATOM   449  O O   . GLU A 1 62  ? 15.485  24.428  5.044   0.75  39.50  ? 62   GLU A O   1 
ATOM   450  C CB  . GLU A 1 62  ? 17.825  25.698  3.661   0.75  39.59  ? 62   GLU A CB  1 
ATOM   451  C CG  . GLU A 1 62  ? 18.263  25.741  2.195   0.75  40.41  ? 62   GLU A CG  1 
ATOM   452  C CD  . GLU A 1 62  ? 17.523  24.754  1.289   0.75  40.14  ? 62   GLU A CD  1 
ATOM   453  O OE1 . GLU A 1 62  ? 16.857  23.821  1.795   0.75  40.15  ? 62   GLU A OE1 1 
ATOM   454  O OE2 . GLU A 1 62  ? 17.620  24.917  0.055   0.75  38.78  ? 62   GLU A OE2 1 
ATOM   455  N N   . ILE A 1 63  ? 14.388  25.238  3.256   1.00  39.84  ? 63   ILE A N   1 
ATOM   456  C CA  . ILE A 1 63  ? 13.199  24.395  3.416   1.00  39.39  ? 63   ILE A CA  1 
ATOM   457  C C   . ILE A 1 63  ? 13.379  22.935  2.946   1.00  39.51  ? 63   ILE A C   1 
ATOM   458  O O   . ILE A 1 63  ? 12.698  22.045  3.447   1.00  39.70  ? 63   ILE A O   1 
ATOM   459  C CB  . ILE A 1 63  ? 11.949  25.051  2.756   1.00  39.39  ? 63   ILE A CB  1 
ATOM   460  C CG1 . ILE A 1 63  ? 10.669  24.326  3.186   1.00  39.08  ? 63   ILE A CG1 1 
ATOM   461  C CG2 . ILE A 1 63  ? 12.089  25.105  1.225   1.00  38.82  ? 63   ILE A CG2 1 
ATOM   462  C CD1 . ILE A 1 63  ? 9.368   24.940  2.630   1.00  39.93  ? 63   ILE A CD1 1 
ATOM   463  N N   . ASN A 1 64  ? 14.283  22.689  1.999   1.00  39.20  ? 64   ASN A N   1 
ATOM   464  C CA  . ASN A 1 64  ? 14.569  21.321  1.576   1.00  39.09  ? 64   ASN A CA  1 
ATOM   465  C C   . ASN A 1 64  ? 15.458  20.562  2.566   1.00  39.27  ? 64   ASN A C   1 
ATOM   466  O O   . ASN A 1 64  ? 15.208  19.387  2.868   1.00  39.13  ? 64   ASN A O   1 
ATOM   467  C CB  . ASN A 1 64  ? 15.177  21.306  0.174   1.00  39.05  ? 64   ASN A CB  1 
ATOM   468  C CG  . ASN A 1 64  ? 14.302  22.017  -0.848  1.00  38.78  ? 64   ASN A CG  1 
ATOM   469  O OD1 . ASN A 1 64  ? 13.090  21.813  -0.899  1.00  38.38  ? 64   ASN A OD1 1 
ATOM   470  N ND2 . ASN A 1 64  ? 14.916  22.851  -1.671  1.00  38.69  ? 64   ASN A ND2 1 
ATOM   471  N N   . ASP A 1 65  ? 16.481  21.247  3.075   1.00  39.54  ? 65   ASP A N   1 
ATOM   472  C CA  . ASP A 1 65  ? 17.399  20.680  4.066   1.00  40.12  ? 65   ASP A CA  1 
ATOM   473  C C   . ASP A 1 65  ? 16.669  20.357  5.370   1.00  39.99  ? 65   ASP A C   1 
ATOM   474  O O   . ASP A 1 65  ? 16.909  19.316  5.993   1.00  39.98  ? 65   ASP A O   1 
ATOM   475  C CB  . ASP A 1 65  ? 18.550  21.656  4.340   1.00  40.46  ? 65   ASP A CB  1 
ATOM   476  C CG  . ASP A 1 65  ? 19.409  21.924  3.101   1.00  42.07  ? 65   ASP A CG  1 
ATOM   477  O OD1 . ASP A 1 65  ? 19.469  21.051  2.202   1.00  42.80  ? 65   ASP A OD1 1 
ATOM   478  O OD2 . ASP A 1 65  ? 20.038  23.006  3.029   1.00  43.56  ? 65   ASP A OD2 1 
ATOM   479  N N   . ASN A 1 66  ? 15.786  21.269  5.772   0.96  39.60  ? 66   ASN A N   1 
ATOM   480  C CA  . ASN A 1 66  ? 14.936  21.076  6.931   0.96  39.32  ? 66   ASN A CA  1 
ATOM   481  C C   . ASN A 1 66  ? 13.955  19.934  6.728   0.96  39.11  ? 66   ASN A C   1 
ATOM   482  O O   . ASN A 1 66  ? 13.685  19.184  7.656   0.96  39.54  ? 66   ASN A O   1 
ATOM   483  C CB  . ASN A 1 66  ? 14.168  22.359  7.264   0.96  39.41  ? 66   ASN A CB  1 
ATOM   484  C CG  . ASN A 1 66  ? 15.044  23.426  7.870   0.96  39.33  ? 66   ASN A CG  1 
ATOM   485  O OD1 . ASN A 1 66  ? 16.104  23.145  8.434   0.96  40.39  ? 66   ASN A OD1 1 
ATOM   486  N ND2 . ASN A 1 66  ? 14.597  24.668  7.763   0.96  40.15  ? 66   ASN A ND2 1 
ATOM   487  N N   . LEU A 1 67  ? 13.411  19.813  5.520   1.00  38.79  ? 67   LEU A N   1 
ATOM   488  C CA  . LEU A 1 67  ? 12.504  18.716  5.195   1.00  38.29  ? 67   LEU A CA  1 
ATOM   489  C C   . LEU A 1 67  ? 13.240  17.374  5.260   1.00  38.12  ? 67   LEU A C   1 
ATOM   490  O O   . LEU A 1 67  ? 12.768  16.417  5.880   1.00  37.82  ? 67   LEU A O   1 
ATOM   491  C CB  . LEU A 1 67  ? 11.871  18.921  3.815   1.00  38.03  ? 67   LEU A CB  1 
ATOM   492  C CG  . LEU A 1 67  ? 10.724  17.986  3.387   1.00  38.73  ? 67   LEU A CG  1 
ATOM   493  C CD1 . LEU A 1 67  ? 9.550   18.014  4.371   1.00  39.84  ? 67   LEU A CD1 1 
ATOM   494  C CD2 . LEU A 1 67  ? 10.227  18.358  1.993   1.00  38.38  ? 67   LEU A CD2 1 
ATOM   495  N N   . MET A 1 68  ? 14.411  17.319  4.633   0.83  37.84  ? 68   MET A N   1 
ATOM   496  C CA  . MET A 1 68  ? 15.163  16.081  4.559   0.83  37.48  ? 68   MET A CA  1 
ATOM   497  C C   . MET A 1 68  ? 15.640  15.580  5.911   0.83  37.20  ? 68   MET A C   1 
ATOM   498  O O   . MET A 1 68  ? 15.555  14.387  6.192   0.83  37.27  ? 68   MET A O   1 
ATOM   499  C CB  . MET A 1 68  ? 16.312  16.197  3.563   0.83  37.55  ? 68   MET A CB  1 
ATOM   500  C CG  . MET A 1 68  ? 15.872  16.019  2.109   0.83  38.18  ? 68   MET A CG  1 
ATOM   501  S SD  . MET A 1 68  ? 14.905  14.515  1.818   0.83  40.05  ? 68   MET A SD  1 
ATOM   502  C CE  . MET A 1 68  ? 15.973  13.257  2.567   0.83  37.93  ? 68   MET A CE  1 
ATOM   503  N N   . GLU A 1 69  ? 16.124  16.461  6.769   1.00  37.01  ? 69   GLU A N   1 
ATOM   504  C CA  . GLU A 1 69  ? 16.492  16.114  8.132   1.00  36.42  ? 69   GLU A CA  1 
ATOM   505  C C   . GLU A 1 69  ? 15.306  15.760  8.982   1.00  35.34  ? 69   GLU A C   1 
ATOM   506  O O   . GLU A 1 69  ? 15.380  14.884  9.754   1.00  35.30  ? 69   GLU A O   1 
ATOM   507  C CB  . GLU A 1 69  ? 17.218  17.274  8.757   1.00  37.07  ? 69   GLU A CB  1 
ATOM   508  C CG  . GLU A 1 69  ? 18.165  16.917  9.889   1.00  39.39  ? 69   GLU A CG  1 
ATOM   509  C CD  . GLU A 1 69  ? 18.558  18.111  10.704  1.00  42.77  ? 69   GLU A CD  1 
ATOM   510  O OE1 . GLU A 1 69  ? 17.704  18.939  10.947  1.00  45.06  ? 69   GLU A OE1 1 
ATOM   511  O OE2 . GLU A 1 69  ? 19.706  18.233  11.098  1.00  44.26  ? 69   GLU A OE2 1 
ATOM   512  N N   . LEU A 1 70  ? 14.196  16.437  8.810   1.00  34.47  ? 70   LEU A N   1 
ATOM   513  C CA  . LEU A 1 70  ? 12.941  16.042  9.458   1.00  34.08  ? 70   LEU A CA  1 
ATOM   514  C C   . LEU A 1 70  ? 12.567  14.593  9.135   1.00  34.01  ? 70   LEU A C   1 
ATOM   515  O O   . LEU A 1 70  ? 12.255  13.808  10.035  1.00  34.17  ? 70   LEU A O   1 
ATOM   516  C CB  . LEU A 1 70  ? 11.799  16.985  9.046   1.00  34.00  ? 70   LEU A CB  1 
ATOM   517  C CG  . LEU A 1 70  ? 10.410  16.851  9.697   1.00  34.57  ? 70   LEU A CG  1 
ATOM   518  C CD1 . LEU A 1 70  ? 10.475  16.999  11.226  1.00  36.69  ? 70   LEU A CD1 1 
ATOM   519  C CD2 . LEU A 1 70  ? 9.421   17.865  9.136   1.00  33.13  ? 70   LEU A CD2 1 
ATOM   520  N N   . LEU A 1 71  ? 12.609  14.253  7.847   1.00  33.66  ? 71   LEU A N   1 
ATOM   521  C CA  . LEU A 1 71  ? 12.250  12.936  7.361   1.00  33.48  ? 71   LEU A CA  1 
ATOM   522  C C   . LEU A 1 71  ? 13.268  11.890  7.765   1.00  33.77  ? 71   LEU A C   1 
ATOM   523  O O   . LEU A 1 71  ? 12.907  10.740  8.075   1.00  33.49  ? 71   LEU A O   1 
ATOM   524  C CB  . LEU A 1 71  ? 12.145  12.946  5.837   1.00  33.65  ? 71   LEU A CB  1 
ATOM   525  C CG  . LEU A 1 71  ? 11.047  13.786  5.188   1.00  33.39  ? 71   LEU A CG  1 
ATOM   526  C CD1 . LEU A 1 71  ? 11.344  13.935  3.698   1.00  33.24  ? 71   LEU A CD1 1 
ATOM   527  C CD2 . LEU A 1 71  ? 9.668   13.184  5.440   1.00  29.49  ? 71   LEU A CD2 1 
ATOM   528  N N   . ILE A 1 72  ? 14.543  12.278  7.721   1.00  33.90  ? 72   ILE A N   1 
ATOM   529  C CA  . ILE A 1 72  ? 15.634  11.384  8.116   1.00  34.47  ? 72   ILE A CA  1 
ATOM   530  C C   . ILE A 1 72  ? 15.523  11.033  9.605   1.00  34.42  ? 72   ILE A C   1 
ATOM   531  O O   . ILE A 1 72  ? 15.687  9.878   9.979   1.00  34.94  ? 72   ILE A O   1 
ATOM   532  C CB  . ILE A 1 72  ? 17.039  11.974  7.772   1.00  34.68  ? 72   ILE A CB  1 
ATOM   533  C CG1 . ILE A 1 72  ? 17.330  11.888  6.268   1.00  34.34  ? 72   ILE A CG1 1 
ATOM   534  C CG2 . ILE A 1 72  ? 18.140  11.239  8.513   1.00  34.78  ? 72   ILE A CG2 1 
ATOM   535  C CD1 . ILE A 1 72  ? 18.465  12.824  5.807   1.00  33.33  ? 72   ILE A CD1 1 
ATOM   536  N N   . MET A 1 73  ? 15.210  12.024  10.435  1.00  34.28  ? 73   MET A N   1 
ATOM   537  C CA  . MET A 1 73  ? 14.990  11.796  11.862  1.00  34.57  ? 73   MET A CA  1 
ATOM   538  C C   . MET A 1 73  ? 13.780  10.916  12.170  1.00  34.56  ? 73   MET A C   1 
ATOM   539  O O   . MET A 1 73  ? 13.879  10.034  13.027  1.00  35.01  ? 73   MET A O   1 
ATOM   540  C CB  . MET A 1 73  ? 14.897  13.116  12.619  1.00  34.57  ? 73   MET A CB  1 
ATOM   541  C CG  . MET A 1 73  ? 16.218  13.874  12.670  1.00  35.95  ? 73   MET A CG  1 
ATOM   542  S SD  . MET A 1 73  ? 16.319  15.097  13.977  1.00  38.32  ? 73   MET A SD  1 
ATOM   543  C CE  . MET A 1 73  ? 16.078  14.056  15.433  1.00  39.54  ? 73   MET A CE  1 
ATOM   544  N N   . ILE A 1 74  ? 12.658  11.140  11.478  1.00  34.01  ? 74   ILE A N   1 
ATOM   545  C CA  . ILE A 1 74  ? 11.462  10.314  11.669  1.00  33.69  ? 74   ILE A CA  1 
ATOM   546  C C   . ILE A 1 74  ? 11.753  8.864   11.301  1.00  33.59  ? 74   ILE A C   1 
ATOM   547  O O   . ILE A 1 74  ? 11.334  7.941   11.996  1.00  33.71  ? 74   ILE A O   1 
ATOM   548  C CB  . ILE A 1 74  ? 10.250  10.848  10.854  1.00  34.06  ? 74   ILE A CB  1 
ATOM   549  C CG1 . ILE A 1 74  ? 9.704   12.136  11.477  1.00  33.85  ? 74   ILE A CG1 1 
ATOM   550  C CG2 . ILE A 1 74  ? 9.138   9.802   10.774  1.00  33.84  ? 74   ILE A CG2 1 
ATOM   551  C CD1 . ILE A 1 74  ? 8.788   12.887  10.575  1.00  34.87  ? 74   ILE A CD1 1 
ATOM   552  N N   . ASN A 1 75  ? 12.504  8.673   10.221  1.00  33.58  ? 75   ASN A N   1 
ATOM   553  C CA  . ASN A 1 75  ? 12.897  7.341   9.771   1.00  33.15  ? 75   ASN A CA  1 
ATOM   554  C C   . ASN A 1 75  ? 13.896  6.697   10.734  1.00  33.41  ? 75   ASN A C   1 
ATOM   555  O O   . ASN A 1 75  ? 13.767  5.504   11.084  1.00  32.83  ? 75   ASN A O   1 
ATOM   556  C CB  . ASN A 1 75  ? 13.465  7.412   8.356   1.00  32.99  ? 75   ASN A CB  1 
ATOM   557  C CG  . ASN A 1 75  ? 13.724  6.058   7.763   1.00  32.43  ? 75   ASN A CG  1 
ATOM   558  O OD1 . ASN A 1 75  ? 14.858  5.725   7.432   1.00  35.88  ? 75   ASN A OD1 1 
ATOM   559  N ND2 . ASN A 1 75  ? 12.686  5.261   7.635   1.00  30.64  ? 75   ASN A ND2 1 
ATOM   560  N N   . ALA A 1 76  ? 14.870  7.496   11.187  1.00  33.47  ? 76   ALA A N   1 
ATOM   561  C CA  . ALA A 1 76  ? 15.881  7.011   12.126  1.00  33.62  ? 76   ALA A CA  1 
ATOM   562  C C   . ALA A 1 76  ? 15.215  6.471   13.392  1.00  33.82  ? 76   ALA A C   1 
ATOM   563  O O   . ALA A 1 76  ? 15.578  5.393   13.885  1.00  33.81  ? 76   ALA A O   1 
ATOM   564  C CB  . ALA A 1 76  ? 16.844  8.098   12.456  1.00  33.55  ? 76   ALA A CB  1 
ATOM   565  N N   . CYS A 1 77  ? 14.221  7.212   13.880  1.00  33.89  ? 77   CYS A N   1 
ATOM   566  C CA  . CYS A 1 77  ? 13.433  6.820   15.046  1.00  34.02  ? 77   CYS A CA  1 
ATOM   567  C C   . CYS A 1 77  ? 12.503  5.634   14.793  1.00  34.46  ? 77   CYS A C   1 
ATOM   568  O O   . CYS A 1 77  ? 12.449  4.733   15.615  1.00  34.25  ? 77   CYS A O   1 
ATOM   569  C CB  . CYS A 1 77  ? 12.645  8.018   15.600  1.00  34.25  ? 77   CYS A CB  1 
ATOM   570  S SG  . CYS A 1 77  ? 13.670  9.381   16.266  1.00  32.38  ? 77   CYS A SG  1 
ATOM   571  N N   . LYS A 1 78  ? 11.798  5.610   13.653  1.00  35.37  ? 78   LYS A N   1 
ATOM   572  C CA  . LYS A 1 78  ? 10.895  4.488   13.342  1.00  35.59  ? 78   LYS A CA  1 
ATOM   573  C C   . LYS A 1 78  ? 11.599  3.122   13.291  1.00  35.54  ? 78   LYS A C   1 
ATOM   574  O O   . LYS A 1 78  ? 11.153  2.178   13.939  1.00  35.95  ? 78   LYS A O   1 
ATOM   575  C CB  . LYS A 1 78  ? 10.114  4.731   12.048  1.00  35.84  ? 78   LYS A CB  1 
ATOM   576  C CG  . LYS A 1 78  ? 8.746   4.024   12.004  1.00  37.46  ? 78   LYS A CG  1 
ATOM   577  C CD  . LYS A 1 78  ? 7.746   4.684   12.990  1.00  40.41  ? 78   LYS A CD  1 
ATOM   578  C CE  . LYS A 1 78  ? 6.385   4.017   12.963  1.00  40.98  ? 78   LYS A CE  1 
ATOM   579  N NZ  . LYS A 1 78  ? 5.681   4.291   11.676  1.00  42.57  ? 78   LYS A NZ  1 
ATOM   580  N N   . ILE A 1 79  ? 12.698  3.017   12.547  1.00  35.19  ? 79   ILE A N   1 
ATOM   581  C CA  . ILE A 1 79  ? 13.424  1.739   12.451  1.00  34.96  ? 79   ILE A CA  1 
ATOM   582  C C   . ILE A 1 79  ? 14.264  1.421   13.701  1.00  34.98  ? 79   ILE A C   1 
ATOM   583  O O   . ILE A 1 79  ? 14.918  0.376   13.784  1.00  35.44  ? 79   ILE A O   1 
ATOM   584  C CB  . ILE A 1 79  ? 14.294  1.619   11.146  1.00  35.01  ? 79   ILE A CB  1 
ATOM   585  C CG1 . ILE A 1 79  ? 15.415  2.671   11.124  1.00  35.32  ? 79   ILE A CG1 1 
ATOM   586  C CG2 . ILE A 1 79  ? 13.418  1.677   9.892   1.00  33.91  ? 79   ILE A CG2 1 
ATOM   587  C CD1 . ILE A 1 79  ? 16.544  2.350   10.183  1.00  34.18  ? 79   ILE A CD1 1 
ATOM   588  N N   . ALA A 1 80  ? 14.253  2.335   14.665  1.00  34.87  ? 80   ALA A N   1 
ATOM   589  C CA  . ALA A 1 80  ? 14.842  2.095   15.978  1.00  34.20  ? 80   ALA A CA  1 
ATOM   590  C C   . ALA A 1 80  ? 13.731  1.810   16.999  1.00  34.38  ? 80   ALA A C   1 
ATOM   591  O O   . ALA A 1 80  ? 13.883  2.086   18.192  1.00  34.67  ? 80   ALA A O   1 
ATOM   592  C CB  . ALA A 1 80  ? 15.677  3.276   16.406  1.00  33.77  ? 80   ALA A CB  1 
ATOM   593  N N   . SER A 1 81  ? 12.616  1.258   16.514  1.00  33.93  ? 81   SER A N   1 
ATOM   594  C CA  . SER A 1 81  ? 11.518  0.780   17.351  1.00  33.68  ? 81   SER A CA  1 
ATOM   595  C C   . SER A 1 81  ? 10.894  1.809   18.313  1.00  34.02  ? 81   SER A C   1 
ATOM   596  O O   . SER A 1 81  ? 10.380  1.450   19.399  1.00  34.15  ? 81   SER A O   1 
ATOM   597  C CB  . SER A 1 81  ? 11.924  -0.485  18.095  1.00  33.29  ? 81   SER A CB  1 
ATOM   598  O OG  . SER A 1 81  ? 12.252  -1.500  17.175  1.00  33.51  ? 81   SER A OG  1 
ATOM   599  N N   . ALA A 1 82  ? 10.915  3.080   17.910  1.00  33.64  ? 82   ALA A N   1 
ATOM   600  C CA  . ALA A 1 82  ? 10.101  4.082   18.582  1.00  34.06  ? 82   ALA A CA  1 
ATOM   601  C C   . ALA A 1 82  ? 8.645   3.630   18.592  1.00  34.28  ? 82   ALA A C   1 
ATOM   602  O O   . ALA A 1 82  ? 8.139   3.127   17.586  1.00  34.23  ? 82   ALA A O   1 
ATOM   603  C CB  . ALA A 1 82  ? 10.225  5.436   17.903  1.00  33.83  ? 82   ALA A CB  1 
ATOM   604  N N   . SER A 1 83  ? 7.986   3.811   19.738  1.00  34.69  ? 83   SER A N   1 
ATOM   605  C CA  . SER A 1 83  ? 6.586   3.436   19.905  1.00  34.54  ? 83   SER A CA  1 
ATOM   606  C C   . SER A 1 83  ? 5.645   4.277   19.054  1.00  34.29  ? 83   SER A C   1 
ATOM   607  O O   . SER A 1 83  ? 4.640   3.760   18.559  1.00  34.60  ? 83   SER A O   1 
ATOM   608  C CB  . SER A 1 83  ? 6.186   3.513   21.374  1.00  34.57  ? 83   SER A CB  1 
ATOM   609  O OG  . SER A 1 83  ? 4.774   3.570   21.492  1.00  36.43  ? 83   SER A OG  1 
ATOM   610  N N   . ARG A 1 84  ? 5.966   5.564   18.888  1.00  34.08  ? 84   ARG A N   1 
ATOM   611  C CA  . ARG A 1 84  ? 5.144   6.495   18.094  1.00  33.80  ? 84   ARG A CA  1 
ATOM   612  C C   . ARG A 1 84  ? 5.980   7.698   17.720  1.00  33.67  ? 84   ARG A C   1 
ATOM   613  O O   . ARG A 1 84  ? 6.640   8.282   18.575  1.00  34.09  ? 84   ARG A O   1 
ATOM   614  C CB  . ARG A 1 84  ? 3.916   6.951   18.890  1.00  33.95  ? 84   ARG A CB  1 
ATOM   615  C CG  . ARG A 1 84  ? 2.866   7.760   18.100  1.00  35.31  ? 84   ARG A CG  1 
ATOM   616  C CD  . ARG A 1 84  ? 1.566   7.945   18.926  1.00  37.08  ? 84   ARG A CD  1 
ATOM   617  N NE  . ARG A 1 84  ? 1.794   8.772   20.124  1.00  40.26  ? 84   ARG A NE  1 
ATOM   618  C CZ  . ARG A 1 84  ? 0.875   9.109   21.032  1.00  41.21  ? 84   ARG A CZ  1 
ATOM   619  N NH1 . ARG A 1 84  ? -0.385  8.691   20.944  1.00  41.91  ? 84   ARG A NH1 1 
ATOM   620  N NH2 . ARG A 1 84  ? 1.231   9.871   22.051  1.00  42.13  ? 84   ARG A NH2 1 
ATOM   621  N N   . VAL A 1 85  ? 5.979   8.067   16.441  1.00  33.43  ? 85   VAL A N   1 
ATOM   622  C CA  . VAL A 1 85  ? 6.678   9.288   16.012  1.00  32.53  ? 85   VAL A CA  1 
ATOM   623  C C   . VAL A 1 85  ? 5.681   10.359  15.566  1.00  32.26  ? 85   VAL A C   1 
ATOM   624  O O   . VAL A 1 85  ? 4.825   10.087  14.736  1.00  32.54  ? 85   VAL A O   1 
ATOM   625  C CB  . VAL A 1 85  ? 7.729   8.995   14.888  1.00  32.58  ? 85   VAL A CB  1 
ATOM   626  C CG1 . VAL A 1 85  ? 8.529   10.235  14.544  1.00  31.43  ? 85   VAL A CG1 1 
ATOM   627  C CG2 . VAL A 1 85  ? 8.685   7.902   15.316  1.00  31.68  ? 85   VAL A CG2 1 
ATOM   628  N N   . THR A 1 86  ? 5.791   11.560  16.131  1.00  32.17  ? 86   THR A N   1 
ATOM   629  C CA  . THR A 1 86  ? 4.997   12.727  15.702  1.00  32.30  ? 86   THR A CA  1 
ATOM   630  C C   . THR A 1 86  ? 5.927   13.756  15.057  1.00  32.35  ? 86   THR A C   1 
ATOM   631  O O   . THR A 1 86  ? 7.025   13.983  15.552  1.00  32.52  ? 86   THR A O   1 
ATOM   632  C CB  . THR A 1 86  ? 4.233   13.409  16.897  1.00  32.15  ? 86   THR A CB  1 
ATOM   633  O OG1 . THR A 1 86  ? 3.328   12.487  17.506  1.00  32.60  ? 86   THR A OG1 1 
ATOM   634  C CG2 . THR A 1 86  ? 3.423   14.621  16.452  1.00  32.02  ? 86   THR A CG2 1 
ATOM   635  N N   . ALA A 1 87  ? 5.494   14.358  13.951  1.00  32.51  ? 87   ALA A N   1 
ATOM   636  C CA  . ALA A 1 87  ? 6.167   15.535  13.413  1.00  32.99  ? 87   ALA A CA  1 
ATOM   637  C C   . ALA A 1 87  ? 5.468   16.785  13.938  1.00  33.49  ? 87   ALA A C   1 
ATOM   638  O O   . ALA A 1 87  ? 4.267   16.981  13.722  1.00  33.39  ? 87   ALA A O   1 
ATOM   639  C CB  . ALA A 1 87  ? 6.189   15.524  11.892  1.00  32.97  ? 87   ALA A CB  1 
ATOM   640  N N   . VAL A 1 88  ? 6.222   17.598  14.669  1.00  34.03  ? 88   VAL A N   1 
ATOM   641  C CA  . VAL A 1 88  ? 5.723   18.856  15.183  1.00  34.93  ? 88   VAL A CA  1 
ATOM   642  C C   . VAL A 1 88  ? 6.248   19.927  14.242  1.00  35.72  ? 88   VAL A C   1 
ATOM   643  O O   . VAL A 1 88  ? 7.385   20.376  14.376  1.00  36.12  ? 88   VAL A O   1 
ATOM   644  C CB  . VAL A 1 88  ? 6.180   19.100  16.672  1.00  35.27  ? 88   VAL A CB  1 
ATOM   645  C CG1 . VAL A 1 88  ? 5.588   20.399  17.250  1.00  33.49  ? 88   VAL A CG1 1 
ATOM   646  C CG2 . VAL A 1 88  ? 5.818   17.888  17.558  1.00  34.56  ? 88   VAL A CG2 1 
ATOM   647  N N   . ILE A 1 89  ? 5.408   20.313  13.285  1.00  36.46  ? 89   ILE A N   1 
ATOM   648  C CA  . ILE A 1 89  ? 5.800   21.201  12.197  1.00  37.66  ? 89   ILE A CA  1 
ATOM   649  C C   . ILE A 1 89  ? 4.844   22.391  12.166  1.00  38.27  ? 89   ILE A C   1 
ATOM   650  O O   . ILE A 1 89  ? 3.922   22.437  11.336  1.00  38.36  ? 89   ILE A O   1 
ATOM   651  C CB  . ILE A 1 89  ? 5.750   20.516  10.799  1.00  37.31  ? 89   ILE A CB  1 
ATOM   652  C CG1 . ILE A 1 89  ? 5.496   19.020  10.903  1.00  37.85  ? 89   ILE A CG1 1 
ATOM   653  C CG2 . ILE A 1 89  ? 7.005   20.775  10.037  1.00  38.53  ? 89   ILE A CG2 1 
ATOM   654  C CD1 . ILE A 1 89  ? 4.739   18.461  9.730   1.00  39.35  ? 89   ILE A CD1 1 
ATOM   655  N N   . PRO A 1 90  ? 5.075   23.377  13.049  1.00  38.91  ? 90   PRO A N   1 
ATOM   656  C CA  . PRO A 1 90  ? 4.198   24.549  13.127  1.00  39.28  ? 90   PRO A CA  1 
ATOM   657  C C   . PRO A 1 90  ? 3.937   25.185  11.758  1.00  39.53  ? 90   PRO A C   1 
ATOM   658  O O   . PRO A 1 90  ? 2.806   25.566  11.471  1.00  39.20  ? 90   PRO A O   1 
ATOM   659  C CB  . PRO A 1 90  ? 4.978   25.519  14.020  1.00  39.28  ? 90   PRO A CB  1 
ATOM   660  C CG  . PRO A 1 90  ? 5.956   24.667  14.772  1.00  39.14  ? 90   PRO A CG  1 
ATOM   661  C CD  . PRO A 1 90  ? 6.290   23.531  13.878  1.00  38.93  ? 90   PRO A CD  1 
ATOM   662  N N   . CYS A 1 91  ? 4.978   25.274  10.930  1.00  40.29  ? 91   CYS A N   1 
ATOM   663  C CA  . CYS A 1 91  ? 4.887   25.835  9.575   1.00  41.11  ? 91   CYS A CA  1 
ATOM   664  C C   . CYS A 1 91  ? 5.056   24.737  8.505   1.00  41.04  ? 91   CYS A C   1 
ATOM   665  O O   . CYS A 1 91  ? 6.179   24.390  8.098   1.00  40.84  ? 91   CYS A O   1 
ATOM   666  C CB  . CYS A 1 91  ? 5.927   26.952  9.406   1.00  41.14  ? 91   CYS A CB  1 
ATOM   667  S SG  . CYS A 1 91  ? 5.980   27.734  7.781   1.00  45.17  ? 91   CYS A SG  1 
ATOM   668  N N   . PHE A 1 92  ? 3.923   24.196  8.056   1.00  41.42  ? 92   PHE A N   1 
ATOM   669  C CA  . PHE A 1 92  ? 3.897   23.075  7.110   1.00  41.76  ? 92   PHE A CA  1 
ATOM   670  C C   . PHE A 1 92  ? 4.599   23.439  5.802   1.00  42.16  ? 92   PHE A C   1 
ATOM   671  O O   . PHE A 1 92  ? 4.190   24.388  5.127   1.00  42.12  ? 92   PHE A O   1 
ATOM   672  C CB  . PHE A 1 92  ? 2.453   22.654  6.841   1.00  41.67  ? 92   PHE A CB  1 
ATOM   673  C CG  . PHE A 1 92  ? 2.318   21.305  6.194   1.00  41.80  ? 92   PHE A CG  1 
ATOM   674  C CD1 . PHE A 1 92  ? 2.326   20.144  6.961   1.00  41.28  ? 92   PHE A CD1 1 
ATOM   675  C CD2 . PHE A 1 92  ? 2.164   21.192  4.807   1.00  41.93  ? 92   PHE A CD2 1 
ATOM   676  C CE1 . PHE A 1 92  ? 2.197   18.893  6.346   1.00  41.53  ? 92   PHE A CE1 1 
ATOM   677  C CE2 . PHE A 1 92  ? 2.029   19.943  4.193   1.00  39.97  ? 92   PHE A CE2 1 
ATOM   678  C CZ  . PHE A 1 92  ? 2.039   18.801  4.957   1.00  39.86  ? 92   PHE A CZ  1 
ATOM   679  N N   . PRO A 1 93  ? 5.675   22.697  5.457   1.00  42.61  ? 93   PRO A N   1 
ATOM   680  C CA  . PRO A 1 93  ? 6.472   23.013  4.267   1.00  42.69  ? 93   PRO A CA  1 
ATOM   681  C C   . PRO A 1 93  ? 5.679   22.801  2.992   1.00  43.30  ? 93   PRO A C   1 
ATOM   682  O O   . PRO A 1 93  ? 4.883   21.862  2.920   1.00  43.66  ? 93   PRO A O   1 
ATOM   683  C CB  . PRO A 1 93  ? 7.653   22.034  4.337   1.00  42.58  ? 93   PRO A CB  1 
ATOM   684  C CG  . PRO A 1 93  ? 7.311   21.021  5.374   1.00  42.54  ? 93   PRO A CG  1 
ATOM   685  C CD  . PRO A 1 93  ? 6.228   21.570  6.241   1.00  42.70  ? 93   PRO A CD  1 
ATOM   686  N N   . TYR A 1 94  ? 5.886   23.691  2.013   1.00  43.71  ? 94   TYR A N   1 
ATOM   687  C CA  . TYR A 1 94  ? 5.256   23.630  0.685   1.00  43.76  ? 94   TYR A CA  1 
ATOM   688  C C   . TYR A 1 94  ? 3.747   23.803  0.730   1.00  44.37  ? 94   TYR A C   1 
ATOM   689  O O   . TYR A 1 94  ? 3.044   23.480  -0.233  1.00  44.67  ? 94   TYR A O   1 
ATOM   690  C CB  . TYR A 1 94  ? 5.643   22.347  -0.063  1.00  43.69  ? 94   TYR A CB  1 
ATOM   691  C CG  . TYR A 1 94  ? 7.060   22.371  -0.604  1.00  43.13  ? 94   TYR A CG  1 
ATOM   692  C CD1 . TYR A 1 94  ? 8.156   22.134  0.232   1.00  41.59  ? 94   TYR A CD1 1 
ATOM   693  C CD2 . TYR A 1 94  ? 7.302   22.633  -1.950  1.00  41.71  ? 94   TYR A CD2 1 
ATOM   694  C CE1 . TYR A 1 94  ? 9.447   22.152  -0.261  1.00  41.24  ? 94   TYR A CE1 1 
ATOM   695  C CE2 . TYR A 1 94  ? 8.583   22.662  -2.446  1.00  41.45  ? 94   TYR A CE2 1 
ATOM   696  C CZ  . TYR A 1 94  ? 9.654   22.422  -1.600  1.00  41.47  ? 94   TYR A CZ  1 
ATOM   697  O OH  . TYR A 1 94  ? 10.936  22.442  -2.097  1.00  40.95  ? 94   TYR A OH  1 
ATOM   698  N N   . ALA A 1 95  ? 3.263   24.351  1.838   1.00  44.99  ? 95   ALA A N   1 
ATOM   699  C CA  . ALA A 1 95  ? 1.835   24.497  2.082   1.00  45.81  ? 95   ALA A CA  1 
ATOM   700  C C   . ALA A 1 95  ? 1.063   25.260  1.003   1.00  46.43  ? 95   ALA A C   1 
ATOM   701  O O   . ALA A 1 95  ? -0.129  25.006  0.821   1.00  46.96  ? 95   ALA A O   1 
ATOM   702  C CB  . ALA A 1 95  ? 1.598   25.116  3.437   1.00  45.67  ? 95   ALA A CB  1 
ATOM   703  N N   . ARG A 1 96  ? 1.730   26.184  0.305   0.57  46.99  ? 96   ARG A N   1 
ATOM   704  C CA  . ARG A 1 96  ? 1.113   26.950  -0.794  0.57  47.58  ? 96   ARG A CA  1 
ATOM   705  C C   . ARG A 1 96  ? 0.617   26.049  -1.928  0.57  47.63  ? 96   ARG A C   1 
ATOM   706  O O   . ARG A 1 96  ? -0.458  26.282  -2.485  0.57  47.52  ? 96   ARG A O   1 
ATOM   707  C CB  . ARG A 1 96  ? 2.097   27.974  -1.369  0.57  47.81  ? 96   ARG A CB  1 
ATOM   708  C CG  . ARG A 1 96  ? 2.305   29.226  -0.533  0.57  49.02  ? 96   ARG A CG  1 
ATOM   709  C CD  . ARG A 1 96  ? 3.584   29.943  -0.970  0.57  51.24  ? 96   ARG A CD  1 
ATOM   710  N NE  . ARG A 1 96  ? 3.674   31.306  -0.449  0.57  52.51  ? 96   ARG A NE  1 
ATOM   711  C CZ  . ARG A 1 96  ? 4.815   31.953  -0.212  0.57  53.56  ? 96   ARG A CZ  1 
ATOM   712  N NH1 . ARG A 1 96  ? 5.984   31.360  -0.431  0.57  53.52  ? 96   ARG A NH1 1 
ATOM   713  N NH2 . ARG A 1 96  ? 4.790   33.193  0.268   0.57  53.75  ? 96   ARG A NH2 1 
ATOM   714  N N   . GLN A 1 97  ? 1.411   25.027  -2.253  0.91  47.90  ? 97   GLN A N   1 
ATOM   715  C CA  . GLN A 1 97  ? 1.120   24.095  -3.345  0.91  48.11  ? 97   GLN A CA  1 
ATOM   716  C C   . GLN A 1 97  ? 0.145   22.979  -2.947  0.91  48.13  ? 97   GLN A C   1 
ATOM   717  O O   . GLN A 1 97  ? 0.518   21.799  -2.901  0.91  48.15  ? 97   GLN A O   1 
ATOM   718  C CB  . GLN A 1 97  ? 2.428   23.521  -3.900  0.91  48.18  ? 97   GLN A CB  1 
ATOM   719  C CG  . GLN A 1 97  ? 3.099   24.405  -4.953  0.91  49.13  ? 97   GLN A CG  1 
ATOM   720  C CD  . GLN A 1 97  ? 4.607   24.208  -5.023  0.91  50.63  ? 97   GLN A CD  1 
ATOM   721  O OE1 . GLN A 1 97  ? 5.107   23.398  -5.814  0.91  52.01  ? 97   GLN A OE1 1 
ATOM   722  N NE2 . GLN A 1 97  ? 5.342   24.952  -4.193  0.91  50.56  ? 97   GLN A NE2 1 
ATOM   723  N N   . ASP A 1 98  ? -1.100  23.371  -2.664  1.00  48.07  ? 98   ASP A N   1 
ATOM   724  C CA  . ASP A 1 98  ? -2.163  22.436  -2.284  1.00  48.30  ? 98   ASP A CA  1 
ATOM   725  C C   . ASP A 1 98  ? -3.176  22.193  -3.421  1.00  48.35  ? 98   ASP A C   1 
ATOM   726  O O   . ASP A 1 98  ? -4.131  21.421  -3.266  1.00  48.56  ? 98   ASP A O   1 
ATOM   727  C CB  . ASP A 1 98  ? -2.868  22.892  -0.989  1.00  48.29  ? 98   ASP A CB  1 
ATOM   728  C CG  . ASP A 1 98  ? -3.851  24.057  -1.204  1.00  49.34  ? 98   ASP A CG  1 
ATOM   729  O OD1 . ASP A 1 98  ? -3.722  24.822  -2.187  1.00  50.41  ? 98   ASP A OD1 1 
ATOM   730  O OD2 . ASP A 1 98  ? -4.767  24.217  -0.369  1.00  49.70  ? 98   ASP A OD2 1 
ATOM   731  N N   . LYS A 1 99  ? -2.960  22.873  -4.548  1.00  48.36  ? 99   LYS A N   1 
ATOM   732  C CA  . LYS A 1 99  ? -3.729  22.662  -5.784  1.00  48.39  ? 99   LYS A CA  1 
ATOM   733  C C   . LYS A 1 99  ? -2.919  23.026  -7.033  1.00  48.01  ? 99   LYS A C   1 
ATOM   734  O O   . LYS A 1 99  ? -1.884  23.680  -6.943  1.00  47.72  ? 99   LYS A O   1 
ATOM   735  C CB  . LYS A 1 99  ? -5.053  23.436  -5.763  1.00  48.72  ? 99   LYS A CB  1 
ATOM   736  C CG  . LYS A 1 99  ? -4.921  24.928  -5.469  1.00  50.07  ? 99   LYS A CG  1 
ATOM   737  C CD  . LYS A 1 99  ? -6.238  25.476  -4.916  1.00  51.95  ? 99   LYS A CD  1 
ATOM   738  C CE  . LYS A 1 99  ? -6.156  26.974  -4.672  1.00  51.91  ? 99   LYS A CE  1 
ATOM   739  N NZ  . LYS A 1 99  ? -5.153  27.319  -3.638  1.00  51.80  ? 99   LYS A NZ  1 
ATOM   740  N N   . LYS A 1 100 ? -3.403  22.596  -8.196  0.98  48.00  ? 100  LYS A N   1 
ATOM   741  C CA  . LYS A 1 100 ? -2.697  22.816  -9.469  0.98  47.78  ? 100  LYS A CA  1 
ATOM   742  C C   . LYS A 1 100 ? -2.775  24.270  -9.947  0.98  47.64  ? 100  LYS A C   1 
ATOM   743  O O   . LYS A 1 100 ? -1.815  24.791  -10.515 0.98  48.04  ? 100  LYS A O   1 
ATOM   744  C CB  . LYS A 1 100 ? -3.227  21.877  -10.557 0.98  47.60  ? 100  LYS A CB  1 
ATOM   745  C CG  . LYS A 1 100 ? -3.011  20.396  -10.293 0.98  46.97  ? 100  LYS A CG  1 
ATOM   746  C CD  . LYS A 1 100 ? -3.470  19.584  -11.485 0.98  46.94  ? 100  LYS A CD  1 
ATOM   747  C CE  . LYS A 1 100 ? -3.925  18.201  -11.072 0.98  48.58  ? 100  LYS A CE  1 
ATOM   748  N NZ  . LYS A 1 100 ? -4.086  17.299  -12.266 0.98  49.21  ? 100  LYS A NZ  1 
ATOM   749  N N   . ASP A 1 101 ? -3.928  24.901  -9.704  0.58  47.41  ? 101  ASP A N   1 
ATOM   750  C CA  . ASP A 1 101 ? -4.217  26.304  -10.059 0.58  47.08  ? 101  ASP A CA  1 
ATOM   751  C C   . ASP A 1 101 ? -4.219  26.535  -11.578 0.58  46.87  ? 101  ASP A C   1 
ATOM   752  O O   . ASP A 1 101 ? -3.493  27.389  -12.097 0.58  47.00  ? 101  ASP A O   1 
ATOM   753  C CB  . ASP A 1 101 ? -3.269  27.271  -9.333  0.58  47.09  ? 101  ASP A CB  1 
ATOM   754  C CG  . ASP A 1 101 ? -3.925  28.607  -9.006  0.58  47.88  ? 101  ASP A CG  1 
ATOM   755  O OD1 . ASP A 1 101 ? -4.982  28.622  -8.321  0.58  48.02  ? 101  ASP A OD1 1 
ATOM   756  O OD2 . ASP A 1 101 ? -3.367  29.653  -9.420  0.58  49.29  ? 101  ASP A OD2 1 
ATOM   757  N N   . LYS A 1 102 ? -5.035  25.784  -12.302 0.010 46.40  ? 102  LYS A N   1 
ATOM   758  C CA  . LYS A 1 102 ? -5.123  25.889  -13.759 0.010 46.01  ? 102  LYS A CA  1 
ATOM   759  C C   . LYS A 1 102 ? -3.752  25.765  -14.426 0.010 45.78  ? 102  LYS A C   1 
ATOM   760  O O   . LYS A 1 102 ? -3.422  26.523  -15.340 0.010 45.76  ? 102  LYS A O   1 
ATOM   761  C CB  . LYS A 1 102 ? -5.793  27.203  -14.165 0.010 45.98  ? 102  LYS A CB  1 
ATOM   762  C CG  . LYS A 1 102 ? -7.237  27.329  -13.707 0.010 45.90  ? 102  LYS A CG  1 
ATOM   763  C CD  . LYS A 1 102 ? -7.857  28.632  -14.185 0.010 45.81  ? 102  LYS A CD  1 
ATOM   764  C CE  . LYS A 1 102 ? -7.678  29.738  -13.159 0.010 45.77  ? 102  LYS A CE  1 
ATOM   765  N NZ  . LYS A 1 102 ? -8.864  30.637  -13.099 0.010 45.75  ? 102  LYS A NZ  1 
ATOM   766  N N   . SER A 1 103 ? -2.976  24.774  -13.942 1.00  45.62  ? 103  SER A N   1 
ATOM   767  C CA  . SER A 1 103 ? -1.617  24.512  -14.409 1.00  45.18  ? 103  SER A CA  1 
ATOM   768  C C   . SER A 1 103 ? -1.322  23.004  -14.411 1.00  44.74  ? 103  SER A C   1 
ATOM   769  O O   . SER A 1 103 ? -2.086  22.192  -13.850 1.00  44.16  ? 103  SER A O   1 
ATOM   770  C CB  . SER A 1 103 ? -0.603  25.207  -13.490 1.00  45.07  ? 103  SER A CB  1 
ATOM   771  O OG  . SER A 1 103 ? -0.777  26.612  -13.510 1.00  46.31  ? 103  SER A OG  1 
ATOM   772  N N   . ARG A 1 104 ? -0.220  22.643  -15.067 1.00  44.12  ? 104  ARG A N   1 
ATOM   773  C CA  . ARG A 1 104 ? 0.395   21.336  -14.898 1.00  43.51  ? 104  ARG A CA  1 
ATOM   774  C C   . ARG A 1 104 ? 1.383   21.427  -13.724 1.00  43.38  ? 104  ARG A C   1 
ATOM   775  O O   . ARG A 1 104 ? 2.570   21.117  -13.850 1.00  43.24  ? 104  ARG A O   1 
ATOM   776  C CB  . ARG A 1 104 ? 1.084   20.882  -16.190 1.00  43.04  ? 104  ARG A CB  1 
ATOM   777  C CG  . ARG A 1 104 ? 0.133   20.265  -17.209 1.00  43.22  ? 104  ARG A CG  1 
ATOM   778  C CD  . ARG A 1 104 ? 0.812   19.966  -18.550 1.00  42.41  ? 104  ARG A CD  1 
ATOM   779  N NE  . ARG A 1 104 ? 1.083   21.183  -19.321 1.00  42.14  ? 104  ARG A NE  1 
ATOM   780  C CZ  . ARG A 1 104 ? 0.362   21.609  -20.353 1.00  41.78  ? 104  ARG A CZ  1 
ATOM   781  N NH1 . ARG A 1 104 ? -0.684  20.919  -20.784 1.00  42.04  ? 104  ARG A NH1 1 
ATOM   782  N NH2 . ARG A 1 104 ? 0.699   22.729  -20.965 1.00  43.10  ? 104  ARG A NH2 1 
ATOM   783  N N   . ALA A 1 105 ? 0.872   21.859  -12.577 1.00  43.26  ? 105  ALA A N   1 
ATOM   784  C CA  . ALA A 1 105 ? 1.698   22.045  -11.383 1.00  43.47  ? 105  ALA A CA  1 
ATOM   785  C C   . ALA A 1 105 ? 1.532   20.879  -10.400 1.00  43.22  ? 105  ALA A C   1 
ATOM   786  O O   . ALA A 1 105 ? 0.464   20.273  -10.342 1.00  43.50  ? 105  ALA A O   1 
ATOM   787  C CB  . ALA A 1 105 ? 1.365   23.385  -10.688 1.00  43.35  ? 105  ALA A CB  1 
ATOM   788  N N   . PRO A 1 106 ? 2.594   20.563  -9.634  1.00  42.75  ? 106  PRO A N   1 
ATOM   789  C CA  . PRO A 1 106 ? 2.506   19.569  -8.577  1.00  42.73  ? 106  PRO A CA  1 
ATOM   790  C C   . PRO A 1 106 ? 1.587   20.025  -7.457  1.00  42.59  ? 106  PRO A C   1 
ATOM   791  O O   . PRO A 1 106 ? 1.413   21.232  -7.232  1.00  42.77  ? 106  PRO A O   1 
ATOM   792  C CB  . PRO A 1 106 ? 3.943   19.514  -8.032  1.00  42.81  ? 106  PRO A CB  1 
ATOM   793  C CG  . PRO A 1 106 ? 4.515   20.864  -8.391  1.00  42.48  ? 106  PRO A CG  1 
ATOM   794  C CD  . PRO A 1 106 ? 3.961   21.105  -9.742  1.00  42.69  ? 106  PRO A CD  1 
ATOM   795  N N   . ILE A 1 107 ? 1.003   19.056  -6.764  1.00  42.07  ? 107  ILE A N   1 
ATOM   796  C CA  . ILE A 1 107 ? 0.355   19.316  -5.487  1.00  41.29  ? 107  ILE A CA  1 
ATOM   797  C C   . ILE A 1 107 ? 1.400   18.952  -4.417  1.00  40.75  ? 107  ILE A C   1 
ATOM   798  O O   . ILE A 1 107 ? 1.333   17.889  -3.787  1.00  40.56  ? 107  ILE A O   1 
ATOM   799  C CB  . ILE A 1 107 ? -0.949  18.492  -5.344  1.00  41.29  ? 107  ILE A CB  1 
ATOM   800  C CG1 . ILE A 1 107 ? -1.727  18.487  -6.668  1.00  41.80  ? 107  ILE A CG1 1 
ATOM   801  C CG2 . ILE A 1 107 ? -1.823  19.070  -4.235  1.00  41.34  ? 107  ILE A CG2 1 
ATOM   802  C CD1 . ILE A 1 107 ? -2.588  17.237  -6.893  1.00  42.39  ? 107  ILE A CD1 1 
ATOM   803  N N   . SER A 1 108 ? 2.386   19.837  -4.249  1.00  39.91  ? 108  SER A N   1 
ATOM   804  C CA  . SER A 1 108 ? 3.569   19.563  -3.418  1.00  38.89  ? 108  SER A CA  1 
ATOM   805  C C   . SER A 1 108 ? 3.230   19.348  -1.944  1.00  38.25  ? 108  SER A C   1 
ATOM   806  O O   . SER A 1 108 ? 3.943   18.622  -1.242  1.00  38.28  ? 108  SER A O   1 
ATOM   807  C CB  . SER A 1 108 ? 4.594   20.687  -3.542  1.00  39.11  ? 108  SER A CB  1 
ATOM   808  O OG  . SER A 1 108 ? 4.826   21.033  -4.915  1.00  39.31  ? 108  SER A OG  1 
ATOM   809  N N   . ALA A 1 109 ? 2.150   19.973  -1.475  1.00  37.09  ? 109  ALA A N   1 
ATOM   810  C CA  . ALA A 1 109 ? 1.662   19.721  -0.120  1.00  36.13  ? 109  ALA A CA  1 
ATOM   811  C C   . ALA A 1 109 ? 1.270   18.241  0.070   1.00  35.51  ? 109  ALA A C   1 
ATOM   812  O O   . ALA A 1 109 ? 1.474   17.667  1.145   1.00  35.04  ? 109  ALA A O   1 
ATOM   813  C CB  . ALA A 1 109 ? 0.501   20.630  0.209   1.00  36.10  ? 109  ALA A CB  1 
ATOM   814  N N   . LYS A 1 110 ? 0.724   17.631  -0.982  1.00  34.73  ? 110  LYS A N   1 
ATOM   815  C CA  . LYS A 1 110 ? 0.343   16.217  -0.949  1.00  34.28  ? 110  LYS A CA  1 
ATOM   816  C C   . LYS A 1 110 ? 1.560   15.302  -1.058  1.00  34.10  ? 110  LYS A C   1 
ATOM   817  O O   . LYS A 1 110 ? 1.621   14.244  -0.412  1.00  34.60  ? 110  LYS A O   1 
ATOM   818  C CB  . LYS A 1 110 ? -0.677  15.890  -2.046  1.00  33.98  ? 110  LYS A CB  1 
ATOM   819  C CG  . LYS A 1 110 ? -1.051  14.411  -2.157  1.00  33.50  ? 110  LYS A CG  1 
ATOM   820  C CD  . LYS A 1 110 ? -1.408  13.803  -0.804  1.00  33.95  ? 110  LYS A CD  1 
ATOM   821  C CE  . LYS A 1 110 ? -1.759  12.358  -0.944  1.00  33.60  ? 110  LYS A CE  1 
ATOM   822  N NZ  . LYS A 1 110 ? -3.221  12.242  -1.134  1.00  35.73  ? 110  LYS A NZ  1 
ATOM   823  N N   . LEU A 1 111 ? 2.529   15.718  -1.862  1.00  33.46  ? 111  LEU A N   1 
ATOM   824  C CA  . LEU A 1 111 ? 3.812   15.043  -1.935  1.00  33.01  ? 111  LEU A CA  1 
ATOM   825  C C   . LEU A 1 111 ? 4.439   14.991  -0.548  1.00  32.78  ? 111  LEU A C   1 
ATOM   826  O O   . LEU A 1 111 ? 4.725   13.903  -0.028  1.00  32.90  ? 111  LEU A O   1 
ATOM   827  C CB  . LEU A 1 111 ? 4.736   15.796  -2.880  1.00  33.37  ? 111  LEU A CB  1 
ATOM   828  C CG  . LEU A 1 111 ? 5.719   15.079  -3.801  1.00  33.28  ? 111  LEU A CG  1 
ATOM   829  C CD1 . LEU A 1 111 ? 6.749   16.104  -4.296  1.00  34.26  ? 111  LEU A CD1 1 
ATOM   830  C CD2 . LEU A 1 111 ? 6.391   13.901  -3.130  1.00  32.66  ? 111  LEU A CD2 1 
ATOM   831  N N   . VAL A 1 112 ? 4.616   16.164  0.063   1.00  32.26  ? 112  VAL A N   1 
ATOM   832  C CA  . VAL A 1 112 ? 5.216   16.261  1.399   1.00  31.70  ? 112  VAL A CA  1 
ATOM   833  C C   . VAL A 1 112 ? 4.481   15.429  2.455   1.00  31.35  ? 112  VAL A C   1 
ATOM   834  O O   . VAL A 1 112 ? 5.126   14.813  3.311   1.00  31.66  ? 112  VAL A O   1 
ATOM   835  C CB  . VAL A 1 112 ? 5.369   17.738  1.859   1.00  31.88  ? 112  VAL A CB  1 
ATOM   836  C CG1 . VAL A 1 112 ? 5.890   17.827  3.307   1.00  31.60  ? 112  VAL A CG1 1 
ATOM   837  C CG2 . VAL A 1 112 ? 6.303   18.482  0.919   1.00  31.62  ? 112  VAL A CG2 1 
ATOM   838  N N   . ALA A 1 113 ? 3.149   15.415  2.405   1.00  30.69  ? 113  ALA A N   1 
ATOM   839  C CA  . ALA A 1 113 ? 2.356   14.523  3.266   1.00  29.83  ? 113  ALA A CA  1 
ATOM   840  C C   . ALA A 1 113 ? 2.686   13.046  2.987   1.00  29.43  ? 113  ALA A C   1 
ATOM   841  O O   . ALA A 1 113 ? 2.895   12.276  3.940   1.00  28.91  ? 113  ALA A O   1 
ATOM   842  C CB  . ALA A 1 113 ? 0.856   14.783  3.102   1.00  29.91  ? 113  ALA A CB  1 
ATOM   843  N N   . ASN A 1 114 ? 2.739   12.659  1.698   1.00  28.79  ? 114  ASN A N   1 
ATOM   844  C CA  . ASN A 1 114 ? 3.117   11.280  1.319   1.00  28.04  ? 114  ASN A CA  1 
ATOM   845  C C   . ASN A 1 114 ? 4.510   10.956  1.842   1.00  28.06  ? 114  ASN A C   1 
ATOM   846  O O   . ASN A 1 114 ? 4.757   9.855   2.352   1.00  28.06  ? 114  ASN A O   1 
ATOM   847  C CB  . ASN A 1 114 ? 3.069   11.054  -0.201  1.00  27.96  ? 114  ASN A CB  1 
ATOM   848  C CG  . ASN A 1 114 ? 1.657   10.899  -0.747  1.00  26.36  ? 114  ASN A CG  1 
ATOM   849  O OD1 . ASN A 1 114 ? 0.741   10.535  -0.033  1.00  26.43  ? 114  ASN A OD1 1 
ATOM   850  N ND2 . ASN A 1 114 ? 1.492   11.167  -2.035  1.00  25.04  ? 114  ASN A ND2 1 
ATOM   851  N N   . MET A 1 115 ? 5.403   11.938  1.738   1.00  28.23  ? 115  MET A N   1 
ATOM   852  C CA  . MET A 1 115 ? 6.799   11.815  2.200   1.00  28.31  ? 115  MET A CA  1 
ATOM   853  C C   . MET A 1 115 ? 6.911   11.692  3.702   1.00  27.84  ? 115  MET A C   1 
ATOM   854  O O   . MET A 1 115 ? 7.711   10.895  4.199   1.00  27.51  ? 115  MET A O   1 
ATOM   855  C CB  . MET A 1 115 ? 7.652   12.989  1.695   1.00  28.75  ? 115  MET A CB  1 
ATOM   856  C CG  . MET A 1 115 ? 7.727   13.048  0.157   1.00  30.27  ? 115  MET A CG  1 
ATOM   857  S SD  . MET A 1 115 ? 8.998   14.130  -0.494  1.00  37.03  ? 115  MET A SD  1 
ATOM   858  C CE  . MET A 1 115 ? 8.487   15.736  0.138   1.00  34.23  ? 115  MET A CE  1 
ATOM   859  N N   . LEU A 1 116 ? 6.110   12.473  4.429   1.00  28.06  ? 116  LEU A N   1 
ATOM   860  C CA  . LEU A 1 116 ? 6.097   12.386  5.887   1.00  28.36  ? 116  LEU A CA  1 
ATOM   861  C C   . LEU A 1 116 ? 5.547   11.049  6.319   1.00  29.12  ? 116  LEU A C   1 
ATOM   862  O O   . LEU A 1 116 ? 6.109   10.403  7.212   1.00  29.54  ? 116  LEU A O   1 
ATOM   863  C CB  . LEU A 1 116 ? 5.300   13.518  6.518   1.00  28.02  ? 116  LEU A CB  1 
ATOM   864  C CG  . LEU A 1 116 ? 5.963   14.890  6.624   1.00  27.91  ? 116  LEU A CG  1 
ATOM   865  C CD1 . LEU A 1 116 ? 4.860   15.929  6.900   1.00  28.34  ? 116  LEU A CD1 1 
ATOM   866  C CD2 . LEU A 1 116 ? 7.077   14.928  7.703   1.00  27.17  ? 116  LEU A CD2 1 
ATOM   867  N N   . SER A 1 117 ? 4.471   10.617  5.658   1.00  29.78  ? 117  SER A N   1 
ATOM   868  C CA  . SER A 1 117 ? 3.867   9.320   5.951   1.00  30.33  ? 117  SER A CA  1 
ATOM   869  C C   . SER A 1 117 ? 4.834   8.187   5.668   1.00  30.33  ? 117  SER A C   1 
ATOM   870  O O   . SER A 1 117 ? 5.218   7.488   6.592   1.00  31.03  ? 117  SER A O   1 
ATOM   871  C CB  . SER A 1 117 ? 2.554   9.132   5.191   1.00  30.50  ? 117  SER A CB  1 
ATOM   872  O OG  . SER A 1 117 ? 1.583   10.043  5.676   1.00  31.61  ? 117  SER A OG  1 
ATOM   873  N N   . VAL A 1 118 ? 5.244   8.022   4.415   1.00  30.25  ? 118  VAL A N   1 
ATOM   874  C CA  . VAL A 1 118 ? 6.179   6.947   4.053   1.00  30.82  ? 118  VAL A CA  1 
ATOM   875  C C   . VAL A 1 118 ? 7.458   6.925   4.890   1.00  30.82  ? 118  VAL A C   1 
ATOM   876  O O   . VAL A 1 118 ? 8.011   5.863   5.123   1.00  31.60  ? 118  VAL A O   1 
ATOM   877  C CB  . VAL A 1 118 ? 6.525   6.934   2.529   1.00  31.07  ? 118  VAL A CB  1 
ATOM   878  C CG1 . VAL A 1 118 ? 7.611   7.945   2.199   1.00  30.88  ? 118  VAL A CG1 1 
ATOM   879  C CG2 . VAL A 1 118 ? 6.940   5.535   2.093   1.00  31.79  ? 118  VAL A CG2 1 
ATOM   880  N N   . ALA A 1 119 ? 7.911   8.077   5.378   1.00  30.95  ? 119  ALA A N   1 
ATOM   881  C CA  . ALA A 1 119 ? 9.113   8.106   6.227   1.00  30.82  ? 119  ALA A CA  1 
ATOM   882  C C   . ALA A 1 119 ? 8.915   7.406   7.567   1.00  30.60  ? 119  ALA A C   1 
ATOM   883  O O   . ALA A 1 119 ? 9.876   6.897   8.145   1.00  30.96  ? 119  ALA A O   1 
ATOM   884  C CB  . ALA A 1 119 ? 9.595   9.533   6.446   1.00  30.98  ? 119  ALA A CB  1 
ATOM   885  N N   . GLY A 1 120 ? 7.676   7.406   8.065   1.00  30.26  ? 120  GLY A N   1 
ATOM   886  C CA  . GLY A 1 120 ? 7.338   6.710   9.295   1.00  30.09  ? 120  GLY A CA  1 
ATOM   887  C C   . GLY A 1 120 ? 6.397   7.416   10.256  1.00  30.43  ? 120  GLY A C   1 
ATOM   888  O O   . GLY A 1 120 ? 5.893   6.794   11.206  1.00  30.69  ? 120  GLY A O   1 
ATOM   889  N N   . ALA A 1 121 ? 6.160   8.706   10.028  1.00  30.25  ? 121  ALA A N   1 
ATOM   890  C CA  . ALA A 1 121 ? 5.315   9.528   10.902  1.00  30.41  ? 121  ALA A CA  1 
ATOM   891  C C   . ALA A 1 121 ? 3.982   8.846   11.195  1.00  30.30  ? 121  ALA A C   1 
ATOM   892  O O   . ALA A 1 121 ? 3.383   8.277   10.304  1.00  30.39  ? 121  ALA A O   1 
ATOM   893  C CB  . ALA A 1 121 ? 5.060   10.903  10.245  1.00  30.23  ? 121  ALA A CB  1 
ATOM   894  N N   . ASP A 1 122 ? 3.523   8.908   12.441  1.00  30.66  ? 122  ASP A N   1 
ATOM   895  C CA  . ASP A 1 122 ? 2.219   8.363   12.800  1.00  31.21  ? 122  ASP A CA  1 
ATOM   896  C C   . ASP A 1 122 ? 1.210   9.449   13.161  1.00  31.76  ? 122  ASP A C   1 
ATOM   897  O O   . ASP A 1 122 ? 0.015   9.167   13.361  1.00  32.45  ? 122  ASP A O   1 
ATOM   898  C CB  . ASP A 1 122 ? 2.313   7.396   13.979  1.00  31.18  ? 122  ASP A CB  1 
ATOM   899  C CG  . ASP A 1 122 ? 3.408   6.367   13.823  1.00  31.36  ? 122  ASP A CG  1 
ATOM   900  O OD1 . ASP A 1 122 ? 4.345   6.452   14.633  1.00  32.54  ? 122  ASP A OD1 1 
ATOM   901  O OD2 . ASP A 1 122 ? 3.346   5.478   12.938  1.00  31.59  ? 122  ASP A OD2 1 
ATOM   902  N N   . HIS A 1 123 ? 1.682   10.685  13.241  1.00  32.10  ? 123  HIS A N   1 
ATOM   903  C CA  . HIS A 1 123 ? 0.880   11.772  13.787  1.00  32.73  ? 123  HIS A CA  1 
ATOM   904  C C   . HIS A 1 123 ? 1.557   13.075  13.430  1.00  32.62  ? 123  HIS A C   1 
ATOM   905  O O   . HIS A 1 123 ? 2.797   13.138  13.367  1.00  32.49  ? 123  HIS A O   1 
ATOM   906  C CB  . HIS A 1 123 ? 0.766   11.612  15.318  1.00  33.10  ? 123  HIS A CB  1 
ATOM   907  C CG  . HIS A 1 123 ? -0.161  12.587  15.967  1.00  35.00  ? 123  HIS A CG  1 
ATOM   908  N ND1 . HIS A 1 123 ? 0.282   13.577  16.818  1.00  38.02  ? 123  HIS A ND1 1 
ATOM   909  C CD2 . HIS A 1 123 ? -1.507  12.725  15.896  1.00  37.14  ? 123  HIS A CD2 1 
ATOM   910  C CE1 . HIS A 1 123 ? -0.751  14.290  17.237  1.00  38.54  ? 123  HIS A CE1 1 
ATOM   911  N NE2 . HIS A 1 123 ? -1.848  13.796  16.689  1.00  39.01  ? 123  HIS A NE2 1 
ATOM   912  N N   . ILE A 1 124 ? 0.747   14.104  13.174  1.00  32.80  ? 124  ILE A N   1 
ATOM   913  C CA  . ILE A 1 124 ? 1.250   15.431  12.787  1.00  32.86  ? 124  ILE A CA  1 
ATOM   914  C C   . ILE A 1 124 ? 0.661   16.496  13.697  1.00  33.56  ? 124  ILE A C   1 
ATOM   915  O O   . ILE A 1 124 ? -0.563  16.552  13.889  1.00  33.80  ? 124  ILE A O   1 
ATOM   916  C CB  . ILE A 1 124 ? 0.912   15.764  11.293  1.00  32.79  ? 124  ILE A CB  1 
ATOM   917  C CG1 . ILE A 1 124 ? 1.404   14.652  10.344  1.00  32.35  ? 124  ILE A CG1 1 
ATOM   918  C CG2 . ILE A 1 124 ? 1.496   17.120  10.852  1.00  32.64  ? 124  ILE A CG2 1 
ATOM   919  C CD1 . ILE A 1 124 ? 2.937   14.451  10.284  1.00  30.07  ? 124  ILE A CD1 1 
ATOM   920  N N   . ILE A 1 125 ? 1.533   17.318  14.283  1.00  34.19  ? 125  ILE A N   1 
ATOM   921  C CA  . ILE A 1 125 ? 1.104   18.525  14.995  1.00  34.64  ? 125  ILE A CA  1 
ATOM   922  C C   . ILE A 1 125 ? 1.578   19.709  14.181  1.00  35.51  ? 125  ILE A C   1 
ATOM   923  O O   . ILE A 1 125 ? 2.764   19.821  13.863  1.00  35.94  ? 125  ILE A O   1 
ATOM   924  C CB  . ILE A 1 125 ? 1.683   18.613  16.425  1.00  34.25  ? 125  ILE A CB  1 
ATOM   925  C CG1 . ILE A 1 125 ? 0.932   17.681  17.379  1.00  33.72  ? 125  ILE A CG1 1 
ATOM   926  C CG2 . ILE A 1 125 ? 1.629   20.047  16.942  1.00  34.56  ? 125  ILE A CG2 1 
ATOM   927  C CD1 . ILE A 1 125 ? 1.707   17.328  18.650  1.00  31.76  ? 125  ILE A CD1 1 
ATOM   928  N N   . THR A 1 126 ? 0.645   20.582  13.829  1.00  36.66  ? 126  THR A N   1 
ATOM   929  C CA  . THR A 1 126 ? 0.949   21.747  13.009  1.00  38.27  ? 126  THR A CA  1 
ATOM   930  C C   . THR A 1 126 ? 0.116   22.923  13.476  1.00  39.62  ? 126  THR A C   1 
ATOM   931  O O   . THR A 1 126 ? -0.843  22.740  14.219  1.00  40.18  ? 126  THR A O   1 
ATOM   932  C CB  . THR A 1 126 ? 0.726   21.458  11.482  1.00  38.09  ? 126  THR A CB  1 
ATOM   933  O OG1 . THR A 1 126 ? 1.355   22.477  10.693  1.00  37.87  ? 126  THR A OG1 1 
ATOM   934  C CG2 . THR A 1 126 ? -0.758  21.366  11.119  1.00  37.44  ? 126  THR A CG2 1 
ATOM   935  N N   . MET A 1 127 ? 0.477   24.127  13.043  1.00  41.43  ? 127  MET A N   1 
ATOM   936  C CA  . MET A 1 127 ? -0.264  25.328  13.438  1.00  43.10  ? 127  MET A CA  1 
ATOM   937  C C   . MET A 1 127 ? -0.707  26.165  12.240  1.00  43.81  ? 127  MET A C   1 
ATOM   938  O O   . MET A 1 127 ? 0.065   26.395  11.313  1.00  44.11  ? 127  MET A O   1 
ATOM   939  C CB  . MET A 1 127 ? 0.572   26.176  14.399  1.00  43.09  ? 127  MET A CB  1 
ATOM   940  C CG  . MET A 1 127 ? -0.156  27.407  14.899  1.00  44.40  ? 127  MET A CG  1 
ATOM   941  S SD  . MET A 1 127 ? 0.760   28.274  16.172  1.00  48.11  ? 127  MET A SD  1 
ATOM   942  C CE  . MET A 1 127 ? 0.600   27.140  17.563  1.00  45.43  ? 127  MET A CE  1 
ATOM   943  N N   . ASP A 1 128 ? -1.953  26.624  12.278  0.87  45.29  ? 128  ASP A N   1 
ATOM   944  C CA  . ASP A 1 128 ? -2.533  27.462  11.225  0.87  46.85  ? 128  ASP A CA  1 
ATOM   945  C C   . ASP A 1 128 ? -2.034  27.154  9.816   0.87  47.25  ? 128  ASP A C   1 
ATOM   946  O O   . ASP A 1 128 ? -1.291  27.953  9.205   0.87  47.68  ? 128  ASP A O   1 
ATOM   947  C CB  . ASP A 1 128 ? -2.356  28.947  11.536  0.87  47.44  ? 128  ASP A CB  1 
ATOM   948  C CG  . ASP A 1 128 ? -3.558  29.536  12.239  0.87  50.33  ? 128  ASP A CG  1 
ATOM   949  O OD1 . ASP A 1 128 ? -3.534  30.766  12.506  0.87  52.31  ? 128  ASP A OD1 1 
ATOM   950  O OD2 . ASP A 1 128 ? -4.518  28.769  12.523  0.87  53.10  ? 128  ASP A OD2 1 
ATOM   951  N N   . LEU A 1 129 ? -2.437  25.982  9.321   1.00  47.33  ? 129  LEU A N   1 
ATOM   952  C CA  . LEU A 1 129 ? -2.183  25.614  7.946   1.00  47.72  ? 129  LEU A CA  1 
ATOM   953  C C   . LEU A 1 129 ? -2.649  26.728  7.023   1.00  48.14  ? 129  LEU A C   1 
ATOM   954  O O   . LEU A 1 129 ? -3.635  27.411  7.331   1.00  48.16  ? 129  LEU A O   1 
ATOM   955  C CB  . LEU A 1 129 ? -2.942  24.332  7.608   1.00  48.04  ? 129  LEU A CB  1 
ATOM   956  C CG  . LEU A 1 129 ? -2.317  22.985  7.969   1.00  48.20  ? 129  LEU A CG  1 
ATOM   957  C CD1 . LEU A 1 129 ? -3.359  21.902  7.898   1.00  48.43  ? 129  LEU A CD1 1 
ATOM   958  C CD2 . LEU A 1 129 ? -1.176  22.674  7.015   1.00  49.64  ? 129  LEU A CD2 1 
ATOM   959  N N   . HIS A 1 130 ? -1.937  26.912  5.906   0.010 48.38  ? 130  HIS A N   1 
ATOM   960  C CA  . HIS A 1 130 ? -2.330  27.867  4.864   0.010 48.54  ? 130  HIS A CA  1 
ATOM   961  C C   . HIS A 1 130 ? -3.804  27.642  4.557   0.010 48.90  ? 130  HIS A C   1 
ATOM   962  O O   . HIS A 1 130 ? -4.631  28.537  4.758   0.010 49.04  ? 130  HIS A O   1 
ATOM   963  C CB  . HIS A 1 130 ? -1.461  27.682  3.611   0.010 48.51  ? 130  HIS A CB  1 
ATOM   964  C CG  . HIS A 1 130 ? -1.888  28.512  2.436   0.010 48.36  ? 130  HIS A CG  1 
ATOM   965  N ND1 . HIS A 1 130 ? -1.474  29.815  2.252   0.010 48.07  ? 130  HIS A ND1 1 
ATOM   966  C CD2 . HIS A 1 130 ? -2.675  28.215  1.374   0.010 47.74  ? 130  HIS A CD2 1 
ATOM   967  C CE1 . HIS A 1 130 ? -1.996  30.288  1.134   0.010 47.78  ? 130  HIS A CE1 1 
ATOM   968  N NE2 . HIS A 1 130 ? -2.731  29.339  0.584   0.010 47.80  ? 130  HIS A NE2 1 
ATOM   969  N N   . ALA A 1 131 ? -4.113  26.428  4.102   1.00  49.35  ? 131  ALA A N   1 
ATOM   970  C CA  . ALA A 1 131 ? -5.482  25.975  3.884   1.00  49.55  ? 131  ALA A CA  1 
ATOM   971  C C   . ALA A 1 131 ? -5.722  24.706  4.703   1.00  49.84  ? 131  ALA A C   1 
ATOM   972  O O   . ALA A 1 131 ? -4.804  23.907  4.918   1.00  50.40  ? 131  ALA A O   1 
ATOM   973  C CB  . ALA A 1 131 ? -5.710  25.719  2.408   1.00  49.45  ? 131  ALA A CB  1 
ATOM   974  N N   . SER A 1 132 ? -6.958  24.510  5.141   0.010 49.95  ? 132  SER A N   1 
ATOM   975  C CA  . SER A 1 132 ? -7.274  23.449  6.098   0.010 49.95  ? 132  SER A CA  1 
ATOM   976  C C   . SER A 1 132 ? -7.363  22.009  5.529   0.010 49.56  ? 132  SER A C   1 
ATOM   977  O O   . SER A 1 132 ? -7.180  21.032  6.289   0.010 50.03  ? 132  SER A O   1 
ATOM   978  C CB  . SER A 1 132 ? -8.542  23.828  6.871   0.010 50.16  ? 132  SER A CB  1 
ATOM   979  O OG  . SER A 1 132 ? -8.593  23.154  8.121   0.010 51.99  ? 132  SER A OG  1 
ATOM   980  N N   . PRO A 1 133 ? -7.633  21.865  4.205   0.81  48.99  ? 133  PRO A N   1 
ATOM   981  C CA  . PRO A 1 133 ? -7.760  20.528  3.602   1.00  48.45  ? 133  PRO A CA  1 
ATOM   982  C C   . PRO A 1 133 ? -6.436  19.750  3.548   0.72  48.15  ? 133  PRO A C   1 
ATOM   983  O O   . PRO A 1 133 ? -6.401  18.626  3.034   0.63  48.11  ? 133  PRO A O   1 
ATOM   984  C CB  . PRO A 1 133 ? -8.230  20.834  2.179   1.00  48.46  ? 133  PRO A CB  1 
ATOM   985  C CG  . PRO A 1 133 ? -8.748  22.229  2.227   1.00  48.90  ? 133  PRO A CG  1 
ATOM   986  C CD  . PRO A 1 133 ? -7.873  22.911  3.195   1.00  48.86  ? 133  PRO A CD  1 
ATOM   987  N N   . ILE A 1 134 ? -5.362  20.342  4.072   1.00  47.47  ? 134  ILE A N   1 
ATOM   988  C CA  . ILE A 1 134 ? -4.059  19.691  4.065   1.00  46.75  ? 134  ILE A CA  1 
ATOM   989  C C   . ILE A 1 134 ? -4.075  18.613  5.136   1.00  46.08  ? 134  ILE A C   1 
ATOM   990  O O   . ILE A 1 134 ? -3.233  17.694  5.134   1.00  46.45  ? 134  ILE A O   1 
ATOM   991  C CB  . ILE A 1 134 ? -2.897  20.718  4.234   1.00  46.96  ? 134  ILE A CB  1 
ATOM   992  C CG1 . ILE A 1 134 ? -2.929  21.719  3.069   1.00  47.62  ? 134  ILE A CG1 1 
ATOM   993  C CG2 . ILE A 1 134 ? -1.543  20.023  4.288   1.00  46.46  ? 134  ILE A CG2 1 
ATOM   994  C CD1 . ILE A 1 134 ? -2.000  22.912  3.215   1.00  49.57  ? 134  ILE A CD1 1 
ATOM   995  N N   . GLN A 1 135 ? -5.051  18.714  6.037   1.00  44.79  ? 135  GLN A N   1 
ATOM   996  C CA  . GLN A 1 135 ? -5.309  17.631  6.988   1.00  43.73  ? 135  GLN A CA  1 
ATOM   997  C C   . GLN A 1 135 ? -5.768  16.419  6.208   1.00  42.50  ? 135  GLN A C   1 
ATOM   998  O O   . GLN A 1 135 ? -5.421  15.294  6.534   1.00  42.88  ? 135  GLN A O   1 
ATOM   999  C CB  . GLN A 1 135 ? -6.375  18.028  8.002   1.00  44.07  ? 135  GLN A CB  1 
ATOM   1000 C CG  . GLN A 1 135 ? -5.993  19.192  8.913   1.00  45.33  ? 135  GLN A CG  1 
ATOM   1001 C CD  . GLN A 1 135 ? -6.899  19.271  10.130  1.00  48.26  ? 135  GLN A CD  1 
ATOM   1002 O OE1 . GLN A 1 135 ? -6.432  19.241  11.271  1.00  48.68  ? 135  GLN A OE1 1 
ATOM   1003 N NE2 . GLN A 1 135 ? -8.209  19.340  9.891   1.00  49.33  ? 135  GLN A NE2 1 
ATOM   1004 N N   . GLY A 1 136 ? -6.528  16.673  5.144   1.00  41.37  ? 136  GLY A N   1 
ATOM   1005 C CA  . GLY A 1 136 ? -7.027  15.624  4.269   1.00  39.80  ? 136  GLY A CA  1 
ATOM   1006 C C   . GLY A 1 136 ? -6.008  15.020  3.318   1.00  38.81  ? 136  GLY A C   1 
ATOM   1007 O O   . GLY A 1 136 ? -6.352  14.106  2.586   1.00  38.61  ? 136  GLY A O   1 
ATOM   1008 N N   . PHE A 1 137 ? -4.773  15.530  3.318   1.00  37.85  ? 137  PHE A N   1 
ATOM   1009 C CA  . PHE A 1 137 ? -3.697  14.967  2.499   1.00  37.10  ? 137  PHE A CA  1 
ATOM   1010 C C   . PHE A 1 137 ? -3.022  13.788  3.201   1.00  36.31  ? 137  PHE A C   1 
ATOM   1011 O O   . PHE A 1 137 ? -2.284  13.023  2.598   1.00  36.06  ? 137  PHE A O   1 
ATOM   1012 C CB  . PHE A 1 137 ? -2.651  16.036  2.140   1.00  37.31  ? 137  PHE A CB  1 
ATOM   1013 C CG  . PHE A 1 137 ? -3.162  17.130  1.234   1.00  37.73  ? 137  PHE A CG  1 
ATOM   1014 C CD1 . PHE A 1 137 ? -2.456  18.319  1.106   1.00  39.03  ? 137  PHE A CD1 1 
ATOM   1015 C CD2 . PHE A 1 137 ? -4.347  16.984  0.518   1.00  37.70  ? 137  PHE A CD2 1 
ATOM   1016 C CE1 . PHE A 1 137 ? -2.918  19.337  0.274   1.00  38.96  ? 137  PHE A CE1 1 
ATOM   1017 C CE2 . PHE A 1 137 ? -4.813  17.993  -0.307  1.00  37.82  ? 137  PHE A CE2 1 
ATOM   1018 C CZ  . PHE A 1 137 ? -4.098  19.166  -0.438  1.00  38.45  ? 137  PHE A CZ  1 
ATOM   1019 N N   . PHE A 1 138 ? -3.284  13.658  4.494   1.00  35.93  ? 138  PHE A N   1 
ATOM   1020 C CA  . PHE A 1 138 ? -2.708  12.591  5.308   1.00  35.01  ? 138  PHE A CA  1 
ATOM   1021 C C   . PHE A 1 138 ? -3.758  11.527  5.566   1.00  34.95  ? 138  PHE A C   1 
ATOM   1022 O O   . PHE A 1 138 ? -4.947  11.808  5.529   1.00  34.89  ? 138  PHE A O   1 
ATOM   1023 C CB  . PHE A 1 138 ? -2.252  13.143  6.655   1.00  33.96  ? 138  PHE A CB  1 
ATOM   1024 C CG  . PHE A 1 138 ? -1.056  14.034  6.588   1.00  32.14  ? 138  PHE A CG  1 
ATOM   1025 C CD1 . PHE A 1 138 ? -1.205  15.406  6.431   1.00  32.57  ? 138  PHE A CD1 1 
ATOM   1026 C CD2 . PHE A 1 138 ? 0.218   13.513  6.736   1.00  30.88  ? 138  PHE A CD2 1 
ATOM   1027 C CE1 . PHE A 1 138 ? -0.105  16.242  6.402   1.00  31.54  ? 138  PHE A CE1 1 
ATOM   1028 C CE2 . PHE A 1 138 ? 1.323   14.329  6.707   1.00  31.03  ? 138  PHE A CE2 1 
ATOM   1029 C CZ  . PHE A 1 138 ? 1.165   15.699  6.537   1.00  32.06  ? 138  PHE A CZ  1 
ATOM   1030 N N   . ASP A 1 139 ? -3.302  10.310  5.828   1.00  35.36  ? 139  ASP A N   1 
ATOM   1031 C CA  . ASP A 1 139 ? -4.167  9.259   6.348   1.00  36.04  ? 139  ASP A CA  1 
ATOM   1032 C C   . ASP A 1 139 ? -4.001  9.096   7.853   1.00  36.06  ? 139  ASP A C   1 
ATOM   1033 O O   . ASP A 1 139 ? -4.891  8.556   8.513   1.00  36.94  ? 139  ASP A O   1 
ATOM   1034 C CB  . ASP A 1 139 ? -3.948  7.930   5.611   1.00  35.87  ? 139  ASP A CB  1 
ATOM   1035 C CG  . ASP A 1 139 ? -4.732  7.860   4.314   1.00  37.19  ? 139  ASP A CG  1 
ATOM   1036 O OD1 . ASP A 1 139 ? -5.976  8.004   4.377   1.00  36.77  ? 139  ASP A OD1 1 
ATOM   1037 O OD2 . ASP A 1 139 ? -4.106  7.687   3.233   1.00  39.34  ? 139  ASP A OD2 1 
ATOM   1038 N N   . ILE A 1 140 ? -2.876  9.578   8.387   1.00  35.69  ? 140  ILE A N   1 
ATOM   1039 C CA  . ILE A 1 140 ? -2.612  9.599   9.828   1.00  35.16  ? 140  ILE A CA  1 
ATOM   1040 C C   . ILE A 1 140 ? -3.328  10.773  10.503  1.00  35.41  ? 140  ILE A C   1 
ATOM   1041 O O   . ILE A 1 140 ? -3.685  11.744  9.837   1.00  35.55  ? 140  ILE A O   1 
ATOM   1042 C CB  . ILE A 1 140 ? -1.084  9.685   10.126  1.00  35.65  ? 140  ILE A CB  1 
ATOM   1043 C CG1 . ILE A 1 140 ? -0.465  10.950  9.446   1.00  34.76  ? 140  ILE A CG1 1 
ATOM   1044 C CG2 . ILE A 1 140 ? -0.377  8.332   9.758   1.00  34.12  ? 140  ILE A CG2 1 
ATOM   1045 C CD1 . ILE A 1 140 ? 1.025   11.130  9.663   1.00  33.58  ? 140  ILE A CD1 1 
ATOM   1046 N N   . PRO A 1 141 ? -3.546  10.698  11.833  1.00  35.57  ? 141  PRO A N   1 
ATOM   1047 C CA  . PRO A 1 141 ? -4.131  11.839  12.542  1.00  35.48  ? 141  PRO A CA  1 
ATOM   1048 C C   . PRO A 1 141 ? -3.267  13.101  12.455  1.00  35.53  ? 141  PRO A C   1 
ATOM   1049 O O   . PRO A 1 141 ? -2.045  13.023  12.542  1.00  35.41  ? 141  PRO A O   1 
ATOM   1050 C CB  . PRO A 1 141 ? -4.200  11.349  13.986  1.00  35.23  ? 141  PRO A CB  1 
ATOM   1051 C CG  . PRO A 1 141 ? -4.213  9.892   13.886  1.00  35.09  ? 141  PRO A CG  1 
ATOM   1052 C CD  . PRO A 1 141 ? -3.348  9.553   12.738  1.00  35.53  ? 141  PRO A CD  1 
ATOM   1053 N N   . VAL A 1 142 ? -3.929  14.240  12.254  1.00  36.12  ? 142  VAL A N   1 
ATOM   1054 C CA  . VAL A 1 142 ? -3.304  15.561  12.183  1.00  36.36  ? 142  VAL A CA  1 
ATOM   1055 C C   . VAL A 1 142 ? -4.008  16.432  13.202  1.00  37.18  ? 142  VAL A C   1 
ATOM   1056 O O   . VAL A 1 142 ? -5.217  16.605  13.137  1.00  37.76  ? 142  VAL A O   1 
ATOM   1057 C CB  . VAL A 1 142 ? -3.484  16.223  10.781  1.00  36.25  ? 142  VAL A CB  1 
ATOM   1058 C CG1 . VAL A 1 142 ? -2.891  17.630  10.759  1.00  36.02  ? 142  VAL A CG1 1 
ATOM   1059 C CG2 . VAL A 1 142 ? -2.854  15.379  9.678   1.00  35.60  ? 142  VAL A CG2 1 
ATOM   1060 N N   . ASP A 1 143 ? -3.262  16.974  14.154  1.00  38.19  ? 143  ASP A N   1 
ATOM   1061 C CA  . ASP A 1 143 ? -3.827  17.934  15.093  1.00  38.89  ? 143  ASP A CA  1 
ATOM   1062 C C   . ASP A 1 143 ? -3.367  19.328  14.701  1.00  39.80  ? 143  ASP A C   1 
ATOM   1063 O O   . ASP A 1 143 ? -2.242  19.722  14.989  1.00  40.36  ? 143  ASP A O   1 
ATOM   1064 C CB  . ASP A 1 143 ? -3.435  17.599  16.544  1.00  38.83  ? 143  ASP A CB  1 
ATOM   1065 C CG  . ASP A 1 143 ? -4.222  16.414  17.118  1.00  38.58  ? 143  ASP A CG  1 
ATOM   1066 O OD1 . ASP A 1 143 ? -5.410  16.244  16.764  1.00  40.13  ? 143  ASP A OD1 1 
ATOM   1067 O OD2 . ASP A 1 143 ? -3.656  15.649  17.928  1.00  36.33  ? 143  ASP A OD2 1 
ATOM   1068 N N   . ASN A 1 144 ? -4.232  20.068  14.018  1.00  41.06  ? 144  ASN A N   1 
ATOM   1069 C CA  . ASN A 1 144 ? -3.893  21.432  13.623  1.00  42.37  ? 144  ASN A CA  1 
ATOM   1070 C C   . ASN A 1 144 ? -4.346  22.481  14.627  1.00  43.01  ? 144  ASN A C   1 
ATOM   1071 O O   . ASN A 1 144 ? -5.545  22.670  14.857  1.00  43.31  ? 144  ASN A O   1 
ATOM   1072 C CB  . ASN A 1 144 ? -4.415  21.777  12.222  1.00  42.55  ? 144  ASN A CB  1 
ATOM   1073 C CG  . ASN A 1 144 ? -3.861  23.103  11.716  1.00  43.56  ? 144  ASN A CG  1 
ATOM   1074 O OD1 . ASN A 1 144 ? -2.963  23.690  12.337  1.00  45.61  ? 144  ASN A OD1 1 
ATOM   1075 N ND2 . ASN A 1 144 ? -4.388  23.584  10.596  1.00  42.57  ? 144  ASN A ND2 1 
ATOM   1076 N N   . LEU A 1 145 ? -3.369  23.165  15.212  1.00  43.98  ? 145  LEU A N   1 
ATOM   1077 C CA  . LEU A 1 145 ? -3.619  24.192  16.226  1.00  44.74  ? 145  LEU A CA  1 
ATOM   1078 C C   . LEU A 1 145 ? -3.927  25.536  15.569  1.00  45.49  ? 145  LEU A C   1 
ATOM   1079 O O   . LEU A 1 145 ? -3.665  25.726  14.374  1.00  46.01  ? 145  LEU A O   1 
ATOM   1080 C CB  . LEU A 1 145 ? -2.419  24.311  17.164  1.00  44.43  ? 145  LEU A CB  1 
ATOM   1081 C CG  . LEU A 1 145 ? -1.906  22.982  17.728  1.00  44.36  ? 145  LEU A CG  1 
ATOM   1082 C CD1 . LEU A 1 145 ? -0.546  23.200  18.390  1.00  44.72  ? 145  LEU A CD1 1 
ATOM   1083 C CD2 . LEU A 1 145 ? -2.922  22.405  18.735  1.00  43.21  ? 145  LEU A CD2 1 
ATOM   1084 N N   . TYR A 1 146 ? -4.494  26.456  16.343  1.00  46.07  ? 146  TYR A N   1 
ATOM   1085 C CA  . TYR A 1 146 ? -4.946  27.730  15.803  1.00  46.82  ? 146  TYR A CA  1 
ATOM   1086 C C   . TYR A 1 146 ? -4.245  28.883  16.493  1.00  47.27  ? 146  TYR A C   1 
ATOM   1087 O O   . TYR A 1 146 ? -4.114  28.905  17.722  1.00  47.30  ? 146  TYR A O   1 
ATOM   1088 C CB  . TYR A 1 146 ? -6.474  27.855  15.908  1.00  46.93  ? 146  TYR A CB  1 
ATOM   1089 C CG  . TYR A 1 146 ? -7.199  26.761  15.153  1.00  48.02  ? 146  TYR A CG  1 
ATOM   1090 C CD1 . TYR A 1 146 ? -7.506  25.551  15.770  1.00  49.61  ? 146  TYR A CD1 1 
ATOM   1091 C CD2 . TYR A 1 146 ? -7.550  26.924  13.810  1.00  50.42  ? 146  TYR A CD2 1 
ATOM   1092 C CE1 . TYR A 1 146 ? -8.153  24.526  15.074  1.00  51.53  ? 146  TYR A CE1 1 
ATOM   1093 C CE2 . TYR A 1 146 ? -8.201  25.898  13.094  1.00  51.32  ? 146  TYR A CE2 1 
ATOM   1094 C CZ  . TYR A 1 146 ? -8.493  24.703  13.736  1.00  51.86  ? 146  TYR A CZ  1 
ATOM   1095 O OH  . TYR A 1 146 ? -9.132  23.686  13.062  1.00  52.21  ? 146  TYR A OH  1 
ATOM   1096 N N   . ALA A 1 147 ? -3.770  29.834  15.692  1.00  47.74  ? 147  ALA A N   1 
ATOM   1097 C CA  . ALA A 1 147 ? -3.169  31.048  16.237  1.00  47.97  ? 147  ALA A CA  1 
ATOM   1098 C C   . ALA A 1 147 ? -4.258  32.050  16.573  1.00  48.10  ? 147  ALA A C   1 
ATOM   1099 O O   . ALA A 1 147 ? -4.019  33.018  17.294  1.00  48.30  ? 147  ALA A O   1 
ATOM   1100 C CB  . ALA A 1 147 ? -2.190  31.643  15.254  1.00  48.14  ? 147  ALA A CB  1 
ATOM   1101 N N   . GLU A 1 148 ? -5.455  31.789  16.051  1.00  48.40  ? 148  GLU A N   1 
ATOM   1102 C CA  . GLU A 1 148 ? -6.634  32.641  16.218  1.00  49.04  ? 148  GLU A CA  1 
ATOM   1103 C C   . GLU A 1 148 ? -6.805  33.201  17.641  1.00  49.35  ? 148  GLU A C   1 
ATOM   1104 O O   . GLU A 1 148 ? -6.921  34.425  17.804  1.00  49.33  ? 148  GLU A O   1 
ATOM   1105 C CB  . GLU A 1 148 ? -7.901  31.906  15.746  1.00  49.22  ? 148  GLU A CB  1 
ATOM   1106 C CG  . GLU A 1 148 ? -9.198  32.718  15.835  1.00  51.08  ? 148  GLU A CG  1 
ATOM   1107 C CD  . GLU A 1 148 ? -10.248 32.311  14.789  1.00  54.18  ? 148  GLU A CD  1 
ATOM   1108 O OE1 . GLU A 1 148 ? -10.457 31.089  14.564  1.00  54.73  ? 148  GLU A OE1 1 
ATOM   1109 O OE2 . GLU A 1 148 ? -10.874 33.227  14.196  1.00  54.23  ? 148  GLU A OE2 1 
ATOM   1110 N N   . PRO A 1 149 ? -6.813  32.322  18.672  1.00  49.38  ? 149  PRO A N   1 
ATOM   1111 C CA  . PRO A 1 149 ? -6.899  32.848  20.029  1.00  49.47  ? 149  PRO A CA  1 
ATOM   1112 C C   . PRO A 1 149 ? -5.725  33.742  20.418  1.00  49.67  ? 149  PRO A C   1 
ATOM   1113 O O   . PRO A 1 149 ? -5.905  34.680  21.193  1.00  49.77  ? 149  PRO A O   1 
ATOM   1114 C CB  . PRO A 1 149 ? -6.907  31.582  20.891  1.00  49.55  ? 149  PRO A CB  1 
ATOM   1115 C CG  . PRO A 1 149 ? -7.466  30.543  20.013  1.00  49.34  ? 149  PRO A CG  1 
ATOM   1116 C CD  . PRO A 1 149 ? -6.900  30.849  18.666  1.00  49.22  ? 149  PRO A CD  1 
ATOM   1117 N N   . ALA A 1 150 ? -4.541  33.463  19.880  1.00  49.94  ? 150  ALA A N   1 
ATOM   1118 C CA  . ALA A 1 150 ? -3.341  34.219  20.243  1.00  50.28  ? 150  ALA A CA  1 
ATOM   1119 C C   . ALA A 1 150 ? -3.268  35.546  19.488  1.00  50.47  ? 150  ALA A C   1 
ATOM   1120 O O   . ALA A 1 150 ? -2.710  36.531  19.996  1.00  50.48  ? 150  ALA A O   1 
ATOM   1121 C CB  . ALA A 1 150 ? -2.092  33.384  19.990  1.00  50.33  ? 150  ALA A CB  1 
ATOM   1122 N N   . VAL A 1 151 ? -3.830  35.553  18.277  1.00  50.48  ? 151  VAL A N   1 
ATOM   1123 C CA  . VAL A 1 151 ? -3.911  36.753  17.437  1.00  50.46  ? 151  VAL A CA  1 
ATOM   1124 C C   . VAL A 1 151 ? -4.939  37.743  17.992  1.00  50.85  ? 151  VAL A C   1 
ATOM   1125 O O   . VAL A 1 151 ? -4.675  38.947  18.058  1.00  50.85  ? 151  VAL A O   1 
ATOM   1126 C CB  . VAL A 1 151 ? -4.261  36.399  15.965  1.00  50.46  ? 151  VAL A CB  1 
ATOM   1127 C CG1 . VAL A 1 151 ? -4.484  37.651  15.135  1.00  50.04  ? 151  VAL A CG1 1 
ATOM   1128 C CG2 . VAL A 1 151 ? -3.175  35.533  15.331  1.00  50.08  ? 151  VAL A CG2 1 
ATOM   1129 N N   . LEU A 1 152 ? -6.100  37.216  18.389  1.00  51.32  ? 152  LEU A N   1 
ATOM   1130 C CA  . LEU A 1 152 ? -7.191  37.996  18.979  1.00  51.58  ? 152  LEU A CA  1 
ATOM   1131 C C   . LEU A 1 152 ? -6.783  38.672  20.277  1.00  52.26  ? 152  LEU A C   1 
ATOM   1132 O O   . LEU A 1 152 ? -7.156  39.826  20.537  1.00  52.55  ? 152  LEU A O   1 
ATOM   1133 C CB  . LEU A 1 152 ? -8.402  37.097  19.235  1.00  51.33  ? 152  LEU A CB  1 
ATOM   1134 C CG  . LEU A 1 152 ? -9.674  37.250  18.388  1.00  51.17  ? 152  LEU A CG  1 
ATOM   1135 C CD1 . LEU A 1 152 ? -9.393  37.367  16.882  1.00  50.81  ? 152  LEU A CD1 1 
ATOM   1136 C CD2 . LEU A 1 152 ? -10.636 36.110  18.662  1.00  50.75  ? 152  LEU A CD2 1 
ATOM   1137 N N   . LYS A 1 153 ? -6.016  37.945  21.084  0.89  52.78  ? 153  LYS A N   1 
ATOM   1138 C CA  . LYS A 1 153 ? -5.562  38.430  22.378  0.89  53.42  ? 153  LYS A CA  1 
ATOM   1139 C C   . LYS A 1 153 ? -4.599  39.608  22.203  0.89  53.78  ? 153  LYS A C   1 
ATOM   1140 O O   . LYS A 1 153 ? -4.596  40.539  23.009  0.89  54.16  ? 153  LYS A O   1 
ATOM   1141 C CB  . LYS A 1 153 ? -4.896  37.287  23.153  0.89  53.35  ? 153  LYS A CB  1 
ATOM   1142 C CG  . LYS A 1 153 ? -4.931  37.436  24.653  0.89  54.07  ? 153  LYS A CG  1 
ATOM   1143 C CD  . LYS A 1 153 ? -4.386  36.181  25.334  0.89  55.04  ? 153  LYS A CD  1 
ATOM   1144 C CE  . LYS A 1 153 ? -4.167  36.394  26.835  0.89  54.89  ? 153  LYS A CE  1 
ATOM   1145 N NZ  . LYS A 1 153 ? -3.026  37.323  27.108  0.89  54.52  ? 153  LYS A NZ  1 
ATOM   1146 N N   . TRP A 1 154 ? -3.802  39.571  21.140  1.00  54.16  ? 154  TRP A N   1 
ATOM   1147 C CA  . TRP A 1 154 ? -2.854  40.640  20.852  1.00  54.65  ? 154  TRP A CA  1 
ATOM   1148 C C   . TRP A 1 154 ? -3.556  41.916  20.388  1.00  55.27  ? 154  TRP A C   1 
ATOM   1149 O O   . TRP A 1 154 ? -3.243  43.008  20.864  1.00  55.51  ? 154  TRP A O   1 
ATOM   1150 C CB  . TRP A 1 154 ? -1.837  40.189  19.803  1.00  54.59  ? 154  TRP A CB  1 
ATOM   1151 C CG  . TRP A 1 154 ? -0.615  41.038  19.782  1.00  53.89  ? 154  TRP A CG  1 
ATOM   1152 C CD1 . TRP A 1 154 ? 0.533   40.834  20.494  1.00  53.93  ? 154  TRP A CD1 1 
ATOM   1153 C CD2 . TRP A 1 154 ? -0.412  42.234  19.025  1.00  53.52  ? 154  TRP A CD2 1 
ATOM   1154 N NE1 . TRP A 1 154 ? 1.440   41.828  20.227  1.00  53.81  ? 154  TRP A NE1 1 
ATOM   1155 C CE2 . TRP A 1 154 ? 0.888   42.701  19.325  1.00  54.03  ? 154  TRP A CE2 1 
ATOM   1156 C CE3 . TRP A 1 154 ? -1.198  42.958  18.115  1.00  53.69  ? 154  TRP A CE3 1 
ATOM   1157 C CZ2 . TRP A 1 154 ? 1.422   43.864  18.749  1.00  53.84  ? 154  TRP A CZ2 1 
ATOM   1158 C CZ3 . TRP A 1 154 ? -0.668  44.120  17.544  1.00  53.23  ? 154  TRP A CZ3 1 
ATOM   1159 C CH2 . TRP A 1 154 ? 0.631   44.557  17.865  1.00  53.13  ? 154  TRP A CH2 1 
ATOM   1160 N N   . ILE A 1 155 ? -4.495  41.768  19.452  1.00  55.94  ? 155  ILE A N   1 
ATOM   1161 C CA  . ILE A 1 155 ? -5.279  42.894  18.930  1.00  56.50  ? 155  ILE A CA  1 
ATOM   1162 C C   . ILE A 1 155 ? -6.024  43.627  20.040  1.00  57.01  ? 155  ILE A C   1 
ATOM   1163 O O   . ILE A 1 155 ? -6.064  44.862  20.052  1.00  57.36  ? 155  ILE A O   1 
ATOM   1164 C CB  . ILE A 1 155 ? -6.278  42.433  17.833  1.00  56.46  ? 155  ILE A CB  1 
ATOM   1165 C CG1 . ILE A 1 155 ? -5.516  41.903  16.612  1.00  55.87  ? 155  ILE A CG1 1 
ATOM   1166 C CG2 . ILE A 1 155 ? -7.235  43.571  17.437  1.00  56.09  ? 155  ILE A CG2 1 
ATOM   1167 C CD1 . ILE A 1 155 ? -6.326  40.970  15.739  1.00  55.44  ? 155  ILE A CD1 1 
ATOM   1168 N N   . ARG A 1 156 ? -6.601  42.863  20.968  1.00  57.47  ? 156  ARG A N   1 
ATOM   1169 C CA  . ARG A 1 156 ? -7.319  43.439  22.103  1.00  58.00  ? 156  ARG A CA  1 
ATOM   1170 C C   . ARG A 1 156 ? -6.394  44.168  23.082  1.00  58.31  ? 156  ARG A C   1 
ATOM   1171 O O   . ARG A 1 156 ? -6.780  45.185  23.662  1.00  58.35  ? 156  ARG A O   1 
ATOM   1172 C CB  . ARG A 1 156 ? -8.104  42.358  22.848  1.00  58.08  ? 156  ARG A CB  1 
ATOM   1173 C CG  . ARG A 1 156 ? -9.419  41.960  22.207  1.00  58.09  ? 156  ARG A CG  1 
ATOM   1174 C CD  . ARG A 1 156 ? -10.132 40.956  23.093  1.00  59.29  ? 156  ARG A CD  1 
ATOM   1175 N NE  . ARG A 1 156 ? -11.275 40.331  22.427  1.00  60.13  ? 156  ARG A NE  1 
ATOM   1176 C CZ  . ARG A 1 156 ? -11.249 39.137  21.837  1.00  59.96  ? 156  ARG A CZ  1 
ATOM   1177 N NH1 . ARG A 1 156 ? -10.134 38.417  21.818  1.00  59.87  ? 156  ARG A NH1 1 
ATOM   1178 N NH2 . ARG A 1 156 ? -12.348 38.660  21.266  1.00  59.92  ? 156  ARG A NH2 1 
ATOM   1179 N N   . GLU A 1 157 ? -5.181  43.647  23.256  1.00  58.68  ? 157  GLU A N   1 
ATOM   1180 C CA  . GLU A 1 157 ? -4.266  44.154  24.279  1.00  59.15  ? 157  GLU A CA  1 
ATOM   1181 C C   . GLU A 1 157 ? -3.227  45.150  23.761  1.00  59.14  ? 157  GLU A C   1 
ATOM   1182 O O   . GLU A 1 157 ? -2.518  45.771  24.566  1.00  59.24  ? 157  GLU A O   1 
ATOM   1183 C CB  . GLU A 1 157 ? -3.576  42.991  25.006  1.00  59.40  ? 157  GLU A CB  1 
ATOM   1184 C CG  . GLU A 1 157 ? -4.525  42.156  25.868  1.00  60.27  ? 157  GLU A CG  1 
ATOM   1185 C CD  . GLU A 1 157 ? -3.804  41.128  26.722  1.00  61.47  ? 157  GLU A CD  1 
ATOM   1186 O OE1 . GLU A 1 157 ? -4.309  39.983  26.835  1.00  61.60  ? 157  GLU A OE1 1 
ATOM   1187 O OE2 . GLU A 1 157 ? -2.737  41.472  27.282  1.00  62.23  ? 157  GLU A OE2 1 
ATOM   1188 N N   . ASN A 1 158 ? -3.151  45.328  22.441  1.00  59.16  ? 158  ASN A N   1 
ATOM   1189 C CA  . ASN A 1 158 ? -2.158  46.237  21.859  1.00  59.19  ? 158  ASN A CA  1 
ATOM   1190 C C   . ASN A 1 158 ? -2.722  47.383  21.020  1.00  59.29  ? 158  ASN A C   1 
ATOM   1191 O O   . ASN A 1 158 ? -2.271  48.523  21.144  1.00  59.28  ? 158  ASN A O   1 
ATOM   1192 C CB  . ASN A 1 158 ? -1.080  45.462  21.095  1.00  59.09  ? 158  ASN A CB  1 
ATOM   1193 C CG  . ASN A 1 158 ? -0.112  44.761  22.023  1.00  58.97  ? 158  ASN A CG  1 
ATOM   1194 O OD1 . ASN A 1 158 ? -0.513  43.968  22.874  1.00  58.45  ? 158  ASN A OD1 1 
ATOM   1195 N ND2 . ASN A 1 158 ? 1.170   45.057  21.871  1.00  60.00  ? 158  ASN A ND2 1 
ATOM   1196 N N   . ILE A 1 159 ? -3.696  47.074  20.170  1.00  59.51  ? 159  ILE A N   1 
ATOM   1197 C CA  . ILE A 1 159 ? -4.412  48.096  19.414  1.00  59.75  ? 159  ILE A CA  1 
ATOM   1198 C C   . ILE A 1 159 ? -5.484  48.712  20.305  1.00  60.02  ? 159  ILE A C   1 
ATOM   1199 O O   . ILE A 1 159 ? -6.402  48.023  20.770  1.00  59.92  ? 159  ILE A O   1 
ATOM   1200 C CB  . ILE A 1 159 ? -5.021  47.531  18.107  1.00  59.84  ? 159  ILE A CB  1 
ATOM   1201 C CG1 . ILE A 1 159 ? -3.901  47.212  17.116  1.00  59.98  ? 159  ILE A CG1 1 
ATOM   1202 C CG2 . ILE A 1 159 ? -5.983  48.537  17.470  1.00  59.76  ? 159  ILE A CG2 1 
ATOM   1203 C CD1 . ILE A 1 159 ? -4.139  45.985  16.282  1.00  60.14  ? 159  ILE A CD1 1 
ATOM   1204 N N   . SER A 1 160 ? -5.342  50.013  20.557  1.00  60.35  ? 160  SER A N   1 
ATOM   1205 C CA  . SER A 1 160 ? -6.249  50.723  21.451  1.00  60.62  ? 160  SER A CA  1 
ATOM   1206 C C   . SER A 1 160 ? -7.629  50.877  20.826  1.00  60.72  ? 160  SER A C   1 
ATOM   1207 O O   . SER A 1 160 ? -8.636  50.533  21.451  1.00  60.95  ? 160  SER A O   1 
ATOM   1208 C CB  . SER A 1 160 ? -5.671  52.082  21.863  1.00  60.57  ? 160  SER A CB  1 
ATOM   1209 O OG  . SER A 1 160 ? -5.308  52.867  20.739  1.00  60.79  ? 160  SER A OG  1 
ATOM   1210 N N   . GLU A 1 161 ? -7.661  51.348  19.580  1.00  60.87  ? 161  GLU A N   1 
ATOM   1211 C CA  . GLU A 1 161 ? -8.913  51.669  18.886  1.00  61.22  ? 161  GLU A CA  1 
ATOM   1212 C C   . GLU A 1 161 ? -9.457  50.480  18.091  1.00  61.09  ? 161  GLU A C   1 
ATOM   1213 O O   . GLU A 1 161 ? -9.899  50.639  16.949  1.00  61.12  ? 161  GLU A O   1 
ATOM   1214 C CB  . GLU A 1 161 ? -8.707  52.862  17.940  1.00  61.50  ? 161  GLU A CB  1 
ATOM   1215 C CG  . GLU A 1 161 ? -7.697  53.920  18.412  1.00  62.76  ? 161  GLU A CG  1 
ATOM   1216 C CD  . GLU A 1 161 ? -6.279  53.675  17.888  1.00  63.89  ? 161  GLU A CD  1 
ATOM   1217 O OE1 . GLU A 1 161 ? -5.849  52.498  17.815  1.00  63.85  ? 161  GLU A OE1 1 
ATOM   1218 O OE2 . GLU A 1 161 ? -5.589  54.672  17.562  1.00  63.80  ? 161  GLU A OE2 1 
ATOM   1219 N N   . TRP A 1 162 ? -9.426  49.293  18.695  1.00  60.90  ? 162  TRP A N   1 
ATOM   1220 C CA  . TRP A 1 162 ? -9.758  48.060  17.981  1.00  60.46  ? 162  TRP A CA  1 
ATOM   1221 C C   . TRP A 1 162 ? -11.263 47.850  17.803  1.00  60.63  ? 162  TRP A C   1 
ATOM   1222 O O   . TRP A 1 162 ? -11.698 47.373  16.751  1.00  61.02  ? 162  TRP A O   1 
ATOM   1223 C CB  . TRP A 1 162 ? -9.099  46.834  18.638  1.00  60.26  ? 162  TRP A CB  1 
ATOM   1224 C CG  . TRP A 1 162 ? -9.650  46.441  19.994  1.00  59.58  ? 162  TRP A CG  1 
ATOM   1225 C CD1 . TRP A 1 162 ? -9.202  46.859  21.214  1.00  59.21  ? 162  TRP A CD1 1 
ATOM   1226 C CD2 . TRP A 1 162 ? -10.734 45.539  20.256  1.00  58.79  ? 162  TRP A CD2 1 
ATOM   1227 N NE1 . TRP A 1 162 ? -9.944  46.285  22.218  1.00  59.02  ? 162  TRP A NE1 1 
ATOM   1228 C CE2 . TRP A 1 162 ? -10.893 45.471  21.659  1.00  58.86  ? 162  TRP A CE2 1 
ATOM   1229 C CE3 . TRP A 1 162 ? -11.592 44.788  19.441  1.00  58.52  ? 162  TRP A CE3 1 
ATOM   1230 C CZ2 . TRP A 1 162 ? -11.874 44.675  22.269  1.00  58.45  ? 162  TRP A CZ2 1 
ATOM   1231 C CZ3 . TRP A 1 162 ? -12.572 43.999  20.048  1.00  58.66  ? 162  TRP A CZ3 1 
ATOM   1232 C CH2 . TRP A 1 162 ? -12.701 43.950  21.450  1.00  58.66  ? 162  TRP A CH2 1 
ATOM   1233 N N   . ARG A 1 163 ? -12.050 48.214  18.819  1.00  60.30  ? 163  ARG A N   1 
ATOM   1234 C CA  . ARG A 1 163 ? -13.489 47.919  18.846  1.00  60.04  ? 163  ARG A CA  1 
ATOM   1235 C C   . ARG A 1 163 ? -14.250 48.429  17.619  1.00  59.97  ? 163  ARG A C   1 
ATOM   1236 O O   . ARG A 1 163 ? -15.390 48.012  17.355  1.00  59.85  ? 163  ARG A O   1 
ATOM   1237 C CB  . ARG A 1 163 ? -14.123 48.426  20.145  1.00  60.06  ? 163  ARG A CB  1 
ATOM   1238 C CG  . ARG A 1 163 ? -13.928 47.467  21.312  1.00  60.08  ? 163  ARG A CG  1 
ATOM   1239 C CD  . ARG A 1 163 ? -14.441 48.026  22.621  1.00  60.11  ? 163  ARG A CD  1 
ATOM   1240 N NE  . ARG A 1 163 ? -14.040 47.201  23.762  1.00  60.47  ? 163  ARG A NE  1 
ATOM   1241 C CZ  . ARG A 1 163 ? -14.732 46.162  24.229  1.00  60.61  ? 163  ARG A CZ  1 
ATOM   1242 N NH1 . ARG A 1 163 ? -15.873 45.799  23.657  1.00  60.82  ? 163  ARG A NH1 1 
ATOM   1243 N NH2 . ARG A 1 163 ? -14.286 45.479  25.274  1.00  60.98  ? 163  ARG A NH2 1 
ATOM   1244 N N   . ASN A 1 164 ? -13.597 49.314  16.868  1.00  59.71  ? 164  ASN A N   1 
ATOM   1245 C CA  . ASN A 1 164 ? -14.144 49.843  15.634  1.00  59.55  ? 164  ASN A CA  1 
ATOM   1246 C C   . ASN A 1 164 ? -13.090 49.847  14.519  1.00  59.58  ? 164  ASN A C   1 
ATOM   1247 O O   . ASN A 1 164 ? -12.995 50.811  13.748  1.00  59.66  ? 164  ASN A O   1 
ATOM   1248 C CB  . ASN A 1 164 ? -14.727 51.249  15.864  1.00  59.59  ? 164  ASN A CB  1 
ATOM   1249 C CG  . ASN A 1 164 ? -15.846 51.270  16.921  1.00  59.65  ? 164  ASN A CG  1 
ATOM   1250 O OD1 . ASN A 1 164 ? -15.815 52.076  17.848  1.00  59.90  ? 164  ASN A OD1 1 
ATOM   1251 N ND2 . ASN A 1 164 ? -16.834 50.386  16.777  1.00  59.42  ? 164  ASN A ND2 1 
ATOM   1252 N N   . CYS A 1 165 ? -12.310 48.762  14.438  1.00  59.24  ? 165  CYS A N   1 
ATOM   1253 C CA  . CYS A 1 165 ? -11.268 48.606  13.409  1.00  59.17  ? 165  CYS A CA  1 
ATOM   1254 C C   . CYS A 1 165 ? -11.713 47.712  12.230  1.00  58.94  ? 165  CYS A C   1 
ATOM   1255 O O   . CYS A 1 165 ? -12.860 47.235  12.197  1.00  58.83  ? 165  CYS A O   1 
ATOM   1256 C CB  . CYS A 1 165 ? -9.982  48.055  14.029  1.00  59.23  ? 165  CYS A CB  1 
ATOM   1257 S SG  . CYS A 1 165 ? -10.023 46.266  14.318  1.00  60.32  ? 165  CYS A SG  1 
ATOM   1258 N N   . THR A 1 166 ? -10.802 47.485  11.277  1.00  58.26  ? 166  THR A N   1 
ATOM   1259 C CA  . THR A 1 166 ? -11.096 46.670  10.094  1.00  57.83  ? 166  THR A CA  1 
ATOM   1260 C C   . THR A 1 166 ? -9.970  45.680  9.756   1.00  57.50  ? 166  THR A C   1 
ATOM   1261 O O   . THR A 1 166 ? -8.827  46.081  9.498   1.00  57.58  ? 166  THR A O   1 
ATOM   1262 C CB  . THR A 1 166 ? -11.415 47.556  8.851   1.00  58.11  ? 166  THR A CB  1 
ATOM   1263 O OG1 . THR A 1 166 ? -12.551 48.392  9.122   1.00  58.03  ? 166  THR A OG1 1 
ATOM   1264 C CG2 . THR A 1 166 ? -11.701 46.696  7.618   1.00  57.92  ? 166  THR A CG2 1 
ATOM   1265 N N   . ILE A 1 167 ? -10.314 44.392  9.754   1.00  56.76  ? 167  ILE A N   1 
ATOM   1266 C CA  . ILE A 1 167 ? -9.373  43.323  9.431   1.00  56.17  ? 167  ILE A CA  1 
ATOM   1267 C C   . ILE A 1 167 ? -9.385  43.104  7.921   1.00  55.87  ? 167  ILE A C   1 
ATOM   1268 O O   . ILE A 1 167 ? -10.453 42.946  7.324   1.00  55.96  ? 167  ILE A O   1 
ATOM   1269 C CB  . ILE A 1 167 ? -9.730  42.016  10.188  1.00  56.24  ? 167  ILE A CB  1 
ATOM   1270 C CG1 . ILE A 1 167 ? -9.966  42.292  11.685  1.00  56.12  ? 167  ILE A CG1 1 
ATOM   1271 C CG2 . ILE A 1 167 ? -8.676  40.927  9.964   1.00  56.26  ? 167  ILE A CG2 1 
ATOM   1272 C CD1 . ILE A 1 167 ? -8.761  42.846  12.457  1.00  55.93  ? 167  ILE A CD1 1 
ATOM   1273 N N   . VAL A 1 168 ? -8.201  43.116  7.306   1.00  55.52  ? 168  VAL A N   1 
ATOM   1274 C CA  . VAL A 1 168 ? -8.090  43.131  5.845   1.00  55.01  ? 168  VAL A CA  1 
ATOM   1275 C C   . VAL A 1 168 ? -7.283  41.956  5.323   1.00  54.92  ? 168  VAL A C   1 
ATOM   1276 O O   . VAL A 1 168 ? -6.202  41.662  5.833   1.00  55.12  ? 168  VAL A O   1 
ATOM   1277 C CB  . VAL A 1 168 ? -7.476  44.464  5.321   1.00  55.08  ? 168  VAL A CB  1 
ATOM   1278 C CG1 . VAL A 1 168 ? -7.229  44.416  3.808   1.00  54.45  ? 168  VAL A CG1 1 
ATOM   1279 C CG2 . VAL A 1 168 ? -8.375  45.641  5.664   1.00  55.26  ? 168  VAL A CG2 1 
ATOM   1280 N N   . SER A 1 169 ? -7.829  41.295  4.302   1.00  54.74  ? 169  SER A N   1 
ATOM   1281 C CA  . SER A 1 169 ? -7.145  40.229  3.579   1.00  54.26  ? 169  SER A CA  1 
ATOM   1282 C C   . SER A 1 169 ? -6.331  40.800  2.421   1.00  54.34  ? 169  SER A C   1 
ATOM   1283 O O   . SER A 1 169 ? -6.868  41.541  1.588   1.00  54.37  ? 169  SER A O   1 
ATOM   1284 C CB  . SER A 1 169 ? -8.155  39.217  3.044   1.00  54.23  ? 169  SER A CB  1 
ATOM   1285 O OG  . SER A 1 169 ? -7.511  38.244  2.245   1.00  53.55  ? 169  SER A OG  1 
ATOM   1286 N N   . PRO A 1 170 ? -5.029  40.454  2.363   1.00  54.25  ? 170  PRO A N   1 
ATOM   1287 C CA  . PRO A 1 170 ? -4.144  40.903  1.289   1.00  54.24  ? 170  PRO A CA  1 
ATOM   1288 C C   . PRO A 1 170 ? -4.434  40.260  -0.078  1.00  54.25  ? 170  PRO A C   1 
ATOM   1289 O O   . PRO A 1 170 ? -4.007  40.790  -1.109  1.00  54.33  ? 170  PRO A O   1 
ATOM   1290 C CB  . PRO A 1 170 ? -2.749  40.492  1.781   1.00  54.32  ? 170  PRO A CB  1 
ATOM   1291 C CG  . PRO A 1 170 ? -2.916  40.108  3.219   1.00  54.21  ? 170  PRO A CG  1 
ATOM   1292 C CD  . PRO A 1 170 ? -4.306  39.640  3.355   1.00  54.21  ? 170  PRO A CD  1 
ATOM   1293 N N   . ASP A 1 171 ? -5.137  39.130  -0.084  1.00  54.19  ? 171  ASP A N   1 
ATOM   1294 C CA  . ASP A 1 171 ? -5.543  38.472  -1.331  1.00  54.10  ? 171  ASP A CA  1 
ATOM   1295 C C   . ASP A 1 171 ? -7.031  38.107  -1.361  1.00  54.10  ? 171  ASP A C   1 
ATOM   1296 O O   . ASP A 1 171 ? -7.762  38.297  -0.381  1.00  53.78  ? 171  ASP A O   1 
ATOM   1297 C CB  . ASP A 1 171 ? -4.675  37.239  -1.625  1.00  54.12  ? 171  ASP A CB  1 
ATOM   1298 C CG  . ASP A 1 171 ? -4.656  36.235  -0.482  1.00  54.24  ? 171  ASP A CG  1 
ATOM   1299 O OD1 . ASP A 1 171 ? -4.051  35.158  -0.662  1.00  55.55  ? 171  ASP A OD1 1 
ATOM   1300 O OD2 . ASP A 1 171 ? -5.226  36.507  0.593   1.00  54.45  ? 171  ASP A OD2 1 
ATOM   1301 N N   . ALA A 1 172 ? -7.470  37.602  -2.510  1.00  54.09  ? 172  ALA A N   1 
ATOM   1302 C CA  . ALA A 1 172 ? -8.819  37.089  -2.680  1.00  54.13  ? 172  ALA A CA  1 
ATOM   1303 C C   . ALA A 1 172 ? -9.056  35.838  -1.827  1.00  54.16  ? 172  ALA A C   1 
ATOM   1304 O O   . ALA A 1 172 ? -10.086 35.716  -1.159  1.00  54.50  ? 172  ALA A O   1 
ATOM   1305 C CB  . ALA A 1 172 ? -9.077  36.788  -4.141  1.00  54.22  ? 172  ALA A CB  1 
ATOM   1306 N N   . GLY A 1 173 ? -8.099  34.917  -1.842  1.00  54.10  ? 173  GLY A N   1 
ATOM   1307 C CA  . GLY A 1 173 ? -8.220  33.674  -1.086  1.00  54.13  ? 173  GLY A CA  1 
ATOM   1308 C C   . GLY A 1 173 ? -7.807  33.807  0.364   1.00  54.13  ? 173  GLY A C   1 
ATOM   1309 O O   . GLY A 1 173 ? -6.986  33.029  0.855   1.00  54.68  ? 173  GLY A O   1 
ATOM   1310 N N   . GLY A 1 174 ? -8.375  34.797  1.047   1.00  53.91  ? 174  GLY A N   1 
ATOM   1311 C CA  . GLY A 1 174 ? -8.129  35.011  2.473   1.00  53.42  ? 174  GLY A CA  1 
ATOM   1312 C C   . GLY A 1 174 ? -9.383  35.521  3.158   1.00  53.26  ? 174  GLY A C   1 
ATOM   1313 O O   . GLY A 1 174 ? -9.380  35.796  4.361   1.00  53.18  ? 174  GLY A O   1 
ATOM   1314 N N   . ALA A 1 175 ? -10.458 35.636  2.377   1.00  52.99  ? 175  ALA A N   1 
ATOM   1315 C CA  . ALA A 1 175 ? -11.750 36.102  2.865   1.00  53.00  ? 175  ALA A CA  1 
ATOM   1316 C C   . ALA A 1 175 ? -12.244 35.342  4.091   1.00  53.06  ? 175  ALA A C   1 
ATOM   1317 O O   . ALA A 1 175 ? -12.666 35.958  5.067   1.00  53.06  ? 175  ALA A O   1 
ATOM   1318 C CB  . ALA A 1 175 ? -12.784 36.035  1.754   1.00  53.01  ? 175  ALA A CB  1 
ATOM   1319 N N   . LYS A 1 176 ? -12.175 34.010  4.034   1.00  53.21  ? 176  LYS A N   1 
ATOM   1320 C CA  . LYS A 1 176 ? -12.658 33.139  5.111   1.00  53.04  ? 176  LYS A CA  1 
ATOM   1321 C C   . LYS A 1 176 ? -11.981 33.458  6.438   1.00  52.90  ? 176  LYS A C   1 
ATOM   1322 O O   . LYS A 1 176 ? -12.647 33.576  7.470   1.00  52.62  ? 176  LYS A O   1 
ATOM   1323 C CB  . LYS A 1 176 ? -12.432 31.671  4.743   1.00  53.15  ? 176  LYS A CB  1 
ATOM   1324 C CG  . LYS A 1 176 ? -13.530 30.733  5.204   1.00  53.50  ? 176  LYS A CG  1 
ATOM   1325 C CD  . LYS A 1 176 ? -13.581 29.486  4.324   1.00  54.96  ? 176  LYS A CD  1 
ATOM   1326 C CE  . LYS A 1 176 ? -14.896 28.714  4.520   1.00  55.85  ? 176  LYS A CE  1 
ATOM   1327 N NZ  . LYS A 1 176 ? -16.096 29.517  4.108   1.00  56.40  ? 176  LYS A NZ  1 
ATOM   1328 N N   . ARG A 1 177 ? -10.661 33.629  6.391   0.77  53.02  ? 177  ARG A N   1 
ATOM   1329 C CA  . ARG A 1 177 ? -9.854  33.880  7.586   0.77  53.13  ? 177  ARG A CA  1 
ATOM   1330 C C   . ARG A 1 177 ? -10.113 35.239  8.249   0.77  53.10  ? 177  ARG A C   1 
ATOM   1331 O O   . ARG A 1 177 ? -10.256 35.302  9.472   0.77  53.11  ? 177  ARG A O   1 
ATOM   1332 C CB  . ARG A 1 177 ? -8.367  33.719  7.261   0.77  53.13  ? 177  ARG A CB  1 
ATOM   1333 C CG  . ARG A 1 177 ? -7.469  33.518  8.488   0.77  54.15  ? 177  ARG A CG  1 
ATOM   1334 C CD  . ARG A 1 177 ? -5.986  33.354  8.111   0.77  54.19  ? 177  ARG A CD  1 
ATOM   1335 N NE  . ARG A 1 177 ? -5.773  32.229  7.201   0.77  53.97  ? 177  ARG A NE  1 
ATOM   1336 C CZ  . ARG A 1 177 ? -5.552  32.346  5.892   0.77  53.94  ? 177  ARG A CZ  1 
ATOM   1337 N NH1 . ARG A 1 177 ? -5.496  33.547  5.327   0.77  53.37  ? 177  ARG A NH1 1 
ATOM   1338 N NH2 . ARG A 1 177 ? -5.381  31.260  5.144   0.77  54.38  ? 177  ARG A NH2 1 
ATOM   1339 N N   . VAL A 1 178 ? -10.169 36.313  7.453   1.00  53.14  ? 178  VAL A N   1 
ATOM   1340 C CA  . VAL A 1 178 ? -10.390 37.673  7.989   1.00  53.00  ? 178  VAL A CA  1 
ATOM   1341 C C   . VAL A 1 178 ? -11.814 37.939  8.492   1.00  53.07  ? 178  VAL A C   1 
ATOM   1342 O O   . VAL A 1 178 ? -11.989 38.685  9.464   1.00  53.27  ? 178  VAL A O   1 
ATOM   1343 C CB  . VAL A 1 178 ? -9.940  38.822  7.019   1.00  53.02  ? 178  VAL A CB  1 
ATOM   1344 C CG1 . VAL A 1 178 ? -8.455  38.716  6.695   1.00  52.48  ? 178  VAL A CG1 1 
ATOM   1345 C CG2 . VAL A 1 178 ? -10.799 38.887  5.751   1.00  53.34  ? 178  VAL A CG2 1 
ATOM   1346 N N   . THR A 1 179 ? -12.815 37.335  7.845   1.00  52.82  ? 179  THR A N   1 
ATOM   1347 C CA  . THR A 1 179 ? -14.202 37.446  8.304   1.00  52.78  ? 179  THR A CA  1 
ATOM   1348 C C   . THR A 1 179 ? -14.352 36.833  9.691   1.00  52.67  ? 179  THR A C   1 
ATOM   1349 O O   . THR A 1 179 ? -15.013 37.397  10.556  1.00  52.72  ? 179  THR A O   1 
ATOM   1350 C CB  . THR A 1 179 ? -15.210 36.773  7.341   1.00  52.83  ? 179  THR A CB  1 
ATOM   1351 O OG1 . THR A 1 179 ? -14.747 35.463  6.980   1.00  53.98  ? 179  THR A OG1 1 
ATOM   1352 C CG2 . THR A 1 179 ? -15.399 37.601  6.097   1.00  52.17  ? 179  THR A CG2 1 
ATOM   1353 N N   . SER A 1 180 ? -13.730 35.675  9.886   1.00  52.79  ? 180  SER A N   1 
ATOM   1354 C CA  . SER A 1 180 ? -13.741 34.972  11.165  1.00  52.82  ? 180  SER A CA  1 
ATOM   1355 C C   . SER A 1 180 ? -13.100 35.799  12.282  1.00  52.75  ? 180  SER A C   1 
ATOM   1356 O O   . SER A 1 180 ? -13.652 35.890  13.381  1.00  52.91  ? 180  SER A O   1 
ATOM   1357 C CB  . SER A 1 180 ? -13.029 33.631  11.024  1.00  52.69  ? 180  SER A CB  1 
ATOM   1358 O OG  . SER A 1 180 ? -12.655 33.125  12.291  1.00  54.24  ? 180  SER A OG  1 
ATOM   1359 N N   . ILE A 1 181 ? -11.943 36.396  11.995  1.00  52.54  ? 181  ILE A N   1 
ATOM   1360 C CA  . ILE A 1 181 ? -11.261 37.285  12.941  1.00  52.39  ? 181  ILE A CA  1 
ATOM   1361 C C   . ILE A 1 181 ? -12.113 38.531  13.236  1.00  52.48  ? 181  ILE A C   1 
ATOM   1362 O O   . ILE A 1 181 ? -12.233 38.948  14.390  1.00  52.36  ? 181  ILE A O   1 
ATOM   1363 C CB  . ILE A 1 181 ? -9.854  37.680  12.424  1.00  52.42  ? 181  ILE A CB  1 
ATOM   1364 C CG1 . ILE A 1 181 ? -8.918  36.467  12.471  1.00  52.44  ? 181  ILE A CG1 1 
ATOM   1365 C CG2 . ILE A 1 181 ? -9.267  38.835  13.242  1.00  52.66  ? 181  ILE A CG2 1 
ATOM   1366 C CD1 . ILE A 1 181 ? -7.817  36.482  11.438  1.00  52.13  ? 181  ILE A CD1 1 
ATOM   1367 N N   . ALA A 1 182 ? -12.710 39.103  12.186  1.00  52.53  ? 182  ALA A N   1 
ATOM   1368 C CA  . ALA A 1 182 ? -13.629 40.235  12.317  1.00  52.48  ? 182  ALA A CA  1 
ATOM   1369 C C   . ALA A 1 182 ? -14.861 39.893  13.156  1.00  52.74  ? 182  ALA A C   1 
ATOM   1370 O O   . ALA A 1 182 ? -15.283 40.698  13.995  1.00  53.11  ? 182  ALA A O   1 
ATOM   1371 C CB  . ALA A 1 182 ? -14.051 40.741  10.945  1.00  52.24  ? 182  ALA A CB  1 
ATOM   1372 N N   . ASP A 1 183 ? -15.429 38.706  12.934  1.00  52.79  ? 183  ASP A N   1 
ATOM   1373 C CA  . ASP A 1 183 ? -16.656 38.291  13.617  1.00  53.07  ? 183  ASP A CA  1 
ATOM   1374 C C   . ASP A 1 183 ? -16.479 38.184  15.124  1.00  53.43  ? 183  ASP A C   1 
ATOM   1375 O O   . ASP A 1 183 ? -17.333 38.647  15.881  1.00  53.86  ? 183  ASP A O   1 
ATOM   1376 C CB  . ASP A 1 183 ? -17.182 36.964  13.059  1.00  53.15  ? 183  ASP A CB  1 
ATOM   1377 C CG  . ASP A 1 183 ? -17.909 37.127  11.738  1.00  52.85  ? 183  ASP A CG  1 
ATOM   1378 O OD1 . ASP A 1 183 ? -18.593 38.151  11.548  1.00  53.94  ? 183  ASP A OD1 1 
ATOM   1379 O OD2 . ASP A 1 183 ? -17.808 36.223  10.888  1.00  52.29  ? 183  ASP A OD2 1 
ATOM   1380 N N   . ARG A 1 184 ? -15.367 37.584  15.546  0.77  53.71  ? 184  ARG A N   1 
ATOM   1381 C CA  . ARG A 1 184 ? -15.057 37.383  16.963  0.77  54.02  ? 184  ARG A CA  1 
ATOM   1382 C C   . ARG A 1 184 ? -14.837 38.697  17.727  0.77  54.27  ? 184  ARG A C   1 
ATOM   1383 O O   . ARG A 1 184 ? -15.104 38.773  18.927  0.77  54.18  ? 184  ARG A O   1 
ATOM   1384 C CB  . ARG A 1 184 ? -13.820 36.485  17.108  0.77  53.96  ? 184  ARG A CB  1 
ATOM   1385 C CG  . ARG A 1 184 ? -14.047 34.988  16.863  0.77  54.35  ? 184  ARG A CG  1 
ATOM   1386 C CD  . ARG A 1 184 ? -14.491 34.241  18.129  0.77  55.51  ? 184  ARG A CD  1 
ATOM   1387 N NE  . ARG A 1 184 ? -13.780 34.704  19.324  0.77  56.05  ? 184  ARG A NE  1 
ATOM   1388 C CZ  . ARG A 1 184 ? -13.702 34.038  20.475  0.77  55.99  ? 184  ARG A CZ  1 
ATOM   1389 N NH1 . ARG A 1 184 ? -14.277 32.846  20.608  0.77  55.49  ? 184  ARG A NH1 1 
ATOM   1390 N NH2 . ARG A 1 184 ? -13.030 34.566  21.493  0.77  55.80  ? 184  ARG A NH2 1 
ATOM   1391 N N   . LEU A 1 185 ? -14.346 39.718  17.021  1.00  54.76  ? 185  LEU A N   1 
ATOM   1392 C CA  . LEU A 1 185 ? -14.065 41.042  17.602  1.00  55.23  ? 185  LEU A CA  1 
ATOM   1393 C C   . LEU A 1 185 ? -15.205 42.041  17.372  1.00  55.30  ? 185  LEU A C   1 
ATOM   1394 O O   . LEU A 1 185 ? -15.117 43.201  17.796  1.00  55.32  ? 185  LEU A O   1 
ATOM   1395 C CB  . LEU A 1 185 ? -12.783 41.630  16.995  1.00  55.27  ? 185  LEU A CB  1 
ATOM   1396 C CG  . LEU A 1 185 ? -11.428 40.916  17.104  1.00  55.98  ? 185  LEU A CG  1 
ATOM   1397 C CD1 . LEU A 1 185 ? -10.433 41.603  16.167  1.00  56.09  ? 185  LEU A CD1 1 
ATOM   1398 C CD2 . LEU A 1 185 ? -10.894 40.896  18.537  1.00  55.78  ? 185  LEU A CD2 1 
ATOM   1399 N N   . ASN A 1 186 ? -16.260 41.590  16.691  1.00  55.30  ? 186  ASN A N   1 
ATOM   1400 C CA  . ASN A 1 186 ? -17.348 42.464  16.226  1.00  55.54  ? 186  ASN A CA  1 
ATOM   1401 C C   . ASN A 1 186 ? -16.874 43.749  15.524  1.00  55.51  ? 186  ASN A C   1 
ATOM   1402 O O   . ASN A 1 186 ? -17.422 44.835  15.744  1.00  55.54  ? 186  ASN A O   1 
ATOM   1403 C CB  . ASN A 1 186 ? -18.354 42.772  17.345  1.00  55.71  ? 186  ASN A CB  1 
ATOM   1404 C CG  . ASN A 1 186 ? -19.469 41.741  17.432  1.00  56.35  ? 186  ASN A CG  1 
ATOM   1405 O OD1 . ASN A 1 186 ? -20.655 42.097  17.457  1.00  56.99  ? 186  ASN A OD1 1 
ATOM   1406 N ND2 . ASN A 1 186 ? -19.096 40.456  17.477  1.00  56.72  ? 186  ASN A ND2 1 
ATOM   1407 N N   . VAL A 1 187 ? -15.851 43.607  14.683  1.00  55.27  ? 187  VAL A N   1 
ATOM   1408 C CA  . VAL A 1 187 ? -15.420 44.683  13.800  1.00  55.02  ? 187  VAL A CA  1 
ATOM   1409 C C   . VAL A 1 187 ? -15.763 44.344  12.349  1.00  54.91  ? 187  VAL A C   1 
ATOM   1410 O O   . VAL A 1 187 ? -16.164 43.218  12.049  1.00  55.01  ? 187  VAL A O   1 
ATOM   1411 C CB  . VAL A 1 187 ? -13.913 45.017  13.946  1.00  54.92  ? 187  VAL A CB  1 
ATOM   1412 C CG1 . VAL A 1 187 ? -13.593 45.399  15.392  1.00  54.96  ? 187  VAL A CG1 1 
ATOM   1413 C CG2 . VAL A 1 187 ? -13.035 43.864  13.453  1.00  54.90  ? 187  VAL A CG2 1 
ATOM   1414 N N   . ASP A 1 188 ? -15.620 45.333  11.471  0.91  54.69  ? 188  ASP A N   1 
ATOM   1415 C CA  . ASP A 1 188 ? -15.878 45.174  10.054  0.91  54.65  ? 188  ASP A CA  1 
ATOM   1416 C C   . ASP A 1 188 ? -14.686 44.508  9.377   0.91  54.52  ? 188  ASP A C   1 
ATOM   1417 O O   . ASP A 1 188 ? -13.597 44.435  9.954   0.91  54.78  ? 188  ASP A O   1 
ATOM   1418 C CB  . ASP A 1 188 ? -16.171 46.546  9.427   0.91  54.81  ? 188  ASP A CB  1 
ATOM   1419 C CG  . ASP A 1 188 ? -17.509 47.129  9.881   0.91  55.40  ? 188  ASP A CG  1 
ATOM   1420 O OD1 . ASP A 1 188 ? -18.023 46.722  10.952  0.91  55.45  ? 188  ASP A OD1 1 
ATOM   1421 O OD2 . ASP A 1 188 ? -18.046 48.002  9.164   0.91  56.63  ? 188  ASP A OD2 1 
ATOM   1422 N N   . PHE A 1 189 ? -14.888 44.006  8.163   1.00  54.13  ? 189  PHE A N   1 
ATOM   1423 C CA  . PHE A 1 189 ? -13.780 43.419  7.411   1.00  53.84  ? 189  PHE A CA  1 
ATOM   1424 C C   . PHE A 1 189 ? -13.697 44.033  6.019   1.00  53.87  ? 189  PHE A C   1 
ATOM   1425 O O   . PHE A 1 189 ? -14.672 44.599  5.528   1.00  53.92  ? 189  PHE A O   1 
ATOM   1426 C CB  . PHE A 1 189 ? -13.907 41.884  7.329   1.00  53.53  ? 189  PHE A CB  1 
ATOM   1427 C CG  . PHE A 1 189 ? -14.933 41.406  6.330   1.00  52.47  ? 189  PHE A CG  1 
ATOM   1428 C CD1 . PHE A 1 189 ? -14.548 41.053  5.036   1.00  51.53  ? 189  PHE A CD1 1 
ATOM   1429 C CD2 . PHE A 1 189 ? -16.277 41.311  6.682   1.00  51.74  ? 189  PHE A CD2 1 
ATOM   1430 C CE1 . PHE A 1 189 ? -15.482 40.619  4.108   1.00  51.66  ? 189  PHE A CE1 1 
ATOM   1431 C CE2 . PHE A 1 189 ? -17.232 40.875  5.760   1.00  51.93  ? 189  PHE A CE2 1 
ATOM   1432 C CZ  . PHE A 1 189 ? -16.835 40.528  4.467   1.00  52.33  ? 189  PHE A CZ  1 
ATOM   1433 N N   . ALA A 1 190 ? -12.528 43.907  5.396   1.00  53.77  ? 190  ALA A N   1 
ATOM   1434 C CA  . ALA A 1 190 ? -12.325 44.304  4.007   1.00  53.56  ? 190  ALA A CA  1 
ATOM   1435 C C   . ALA A 1 190 ? -11.377 43.322  3.326   1.00  53.63  ? 190  ALA A C   1 
ATOM   1436 O O   . ALA A 1 190 ? -10.784 42.460  3.989   1.00  53.63  ? 190  ALA A O   1 
ATOM   1437 C CB  . ALA A 1 190 ? -11.775 45.726  3.927   1.00  53.52  ? 190  ALA A CB  1 
ATOM   1438 N N   . LEU A 1 191 ? -11.229 43.459  2.008   1.00  53.57  ? 191  LEU A N   1 
ATOM   1439 C CA  . LEU A 1 191 ? -10.421 42.532  1.223   1.00  53.62  ? 191  LEU A CA  1 
ATOM   1440 C C   . LEU A 1 191 ? -9.799  43.194  -0.008  1.00  53.49  ? 191  LEU A C   1 
ATOM   1441 O O   . LEU A 1 191 ? -10.438 44.001  -0.689  1.00  53.62  ? 191  LEU A O   1 
ATOM   1442 C CB  . LEU A 1 191 ? -11.267 41.325  0.813   1.00  53.77  ? 191  LEU A CB  1 
ATOM   1443 C CG  . LEU A 1 191 ? -10.585 40.196  0.048   1.00  54.71  ? 191  LEU A CG  1 
ATOM   1444 C CD1 . LEU A 1 191 ? -11.083 38.869  0.569   1.00  55.04  ? 191  LEU A CD1 1 
ATOM   1445 C CD2 . LEU A 1 191 ? -10.837 40.333  -1.463  1.00  55.73  ? 191  LEU A CD2 1 
ATOM   1446 N N   . ILE A 1 192 ? -8.549  42.835  -0.285  1.00  53.12  ? 192  ILE A N   1 
ATOM   1447 C CA  . ILE A 1 192 ? -7.809  43.386  -1.404  1.00  52.53  ? 192  ILE A CA  1 
ATOM   1448 C C   . ILE A 1 192 ? -7.675  42.324  -2.482  1.00  52.45  ? 192  ILE A C   1 
ATOM   1449 O O   . ILE A 1 192 ? -7.538  41.136  -2.189  1.00  52.53  ? 192  ILE A O   1 
ATOM   1450 C CB  . ILE A 1 192 ? -6.403  43.894  -0.971  1.00  52.58  ? 192  ILE A CB  1 
ATOM   1451 C CG1 . ILE A 1 192 ? -6.540  45.095  -0.023  1.00  52.48  ? 192  ILE A CG1 1 
ATOM   1452 C CG2 . ILE A 1 192 ? -5.555  44.284  -2.198  1.00  52.34  ? 192  ILE A CG2 1 
ATOM   1453 C CD1 . ILE A 1 192 ? -5.204  45.634  0.512   1.00  51.34  ? 192  ILE A CD1 1 
ATOM   1454 N N   . HIS A 1 193 ? -7.732  42.763  -3.732  1.00  52.30  ? 193  HIS A N   1 
ATOM   1455 C CA  . HIS A 1 193 ? -7.506  41.887  -4.869  1.00  52.29  ? 193  HIS A CA  1 
ATOM   1456 C C   . HIS A 1 193 ? -6.682  42.602  -5.952  1.00  52.60  ? 193  HIS A C   1 
ATOM   1457 O O   . HIS A 1 193 ? -7.108  43.636  -6.495  1.00  52.42  ? 193  HIS A O   1 
ATOM   1458 C CB  . HIS A 1 193 ? -8.835  41.379  -5.442  1.00  51.81  ? 193  HIS A CB  1 
ATOM   1459 C CG  . HIS A 1 193 ? -8.707  40.795  -6.813  1.00  51.23  ? 193  HIS A CG  1 
ATOM   1460 N ND1 . HIS A 1 193 ? -8.054  39.605  -7.058  1.00  51.11  ? 193  HIS A ND1 1 
ATOM   1461 C CD2 . HIS A 1 193 ? -9.117  41.252  -8.018  1.00  51.43  ? 193  HIS A CD2 1 
ATOM   1462 C CE1 . HIS A 1 193 ? -8.079  39.348  -8.353  1.00  50.36  ? 193  HIS A CE1 1 
ATOM   1463 N NE2 . HIS A 1 193 ? -8.720  40.330  -8.960  1.00  50.70  ? 193  HIS A NE2 1 
ATOM   1464 N N   . LYS A 1 194 ? -5.511  42.047  -6.263  0.82  52.73  ? 194  LYS A N   1 
ATOM   1465 C CA  . LYS A 1 194 ? -4.664  42.604  -7.313  0.82  53.13  ? 194  LYS A CA  1 
ATOM   1466 C C   . LYS A 1 194 ? -5.199  42.207  -8.682  0.82  53.18  ? 194  LYS A C   1 
ATOM   1467 O O   . LYS A 1 194 ? -5.361  41.019  -8.985  0.82  53.03  ? 194  LYS A O   1 
ATOM   1468 C CB  . LYS A 1 194 ? -3.200  42.177  -7.151  0.82  53.45  ? 194  LYS A CB  1 
ATOM   1469 C CG  . LYS A 1 194 ? -2.204  43.116  -7.839  0.82  54.40  ? 194  LYS A CG  1 
ATOM   1470 C CD  . LYS A 1 194 ? -0.793  42.957  -7.276  0.82  56.88  ? 194  LYS A CD  1 
ATOM   1471 C CE  . LYS A 1 194 ? 0.174   44.010  -7.831  0.82  57.68  ? 194  LYS A CE  1 
ATOM   1472 N NZ  . LYS A 1 194 ? 1.439   44.085  -7.019  0.82  58.61  ? 194  LYS A NZ  1 
ATOM   1473 N N   . GLU A 1 195 ? -5.460  43.219  -9.505  0.68  53.41  ? 195  GLU A N   1 
ATOM   1474 C CA  . GLU A 1 195 ? -6.146  43.047  -10.786 0.68  53.61  ? 195  GLU A CA  1 
ATOM   1475 C C   . GLU A 1 195 ? -5.381  42.186  -11.793 0.68  53.43  ? 195  GLU A C   1 
ATOM   1476 O O   . GLU A 1 195 ? -4.187  41.930  -11.636 0.68  53.52  ? 195  GLU A O   1 
ATOM   1477 C CB  . GLU A 1 195 ? -6.466  44.417  -11.390 0.68  53.83  ? 195  GLU A CB  1 
ATOM   1478 C CG  . GLU A 1 195 ? -7.857  44.519  -12.018 0.68  55.07  ? 195  GLU A CG  1 
ATOM   1479 C CD  . GLU A 1 195 ? -8.958  44.768  -10.995 0.68  56.37  ? 195  GLU A CD  1 
ATOM   1480 O OE1 . GLU A 1 195 ? -8.989  44.070  -9.953  0.68  56.78  ? 195  GLU A OE1 1 
ATOM   1481 O OE2 . GLU A 1 195 ? -9.795  45.668  -11.241 0.68  56.90  ? 195  GLU A OE2 1 
ATOM   1482 N N   . ASP A 1 203 ? -0.055  45.493  -12.540 0.62  56.62  ? 203  ASP A N   1 
ATOM   1483 C CA  . ASP A 1 203 ? -1.337  45.081  -11.969 0.62  56.67  ? 203  ASP A CA  1 
ATOM   1484 C C   . ASP A 1 203 ? -1.826  46.089  -10.934 0.62  56.44  ? 203  ASP A C   1 
ATOM   1485 O O   . ASP A 1 203 ? -1.094  46.448  -10.013 0.62  56.36  ? 203  ASP A O   1 
ATOM   1486 C CB  . ASP A 1 203 ? -1.219  43.685  -11.343 0.62  56.71  ? 203  ASP A CB  1 
ATOM   1487 C CG  . ASP A 1 203 ? -0.882  42.616  -12.366 0.62  57.13  ? 203  ASP A CG  1 
ATOM   1488 O OD1 . ASP A 1 203 ? -1.563  42.572  -13.412 0.62  58.13  ? 203  ASP A OD1 1 
ATOM   1489 O OD2 . ASP A 1 203 ? 0.056   41.819  -12.130 0.62  57.45  ? 203  ASP A OD2 1 
ATOM   1490 N N   . ARG A 1 204 ? -3.061  46.553  -11.093 0.010 56.33  ? 204  ARG A N   1 
ATOM   1491 C CA  . ARG A 1 204 ? -3.622  47.533  -10.169 0.010 56.22  ? 204  ARG A CA  1 
ATOM   1492 C C   . ARG A 1 204 ? -4.386  46.856  -9.036  0.010 56.16  ? 204  ARG A C   1 
ATOM   1493 O O   . ARG A 1 204 ? -5.177  45.941  -9.266  0.010 56.14  ? 204  ARG A O   1 
ATOM   1494 C CB  . ARG A 1 204 ? -4.533  48.519  -10.903 0.010 56.22  ? 204  ARG A CB  1 
ATOM   1495 C CG  . ARG A 1 204 ? -5.920  47.979  -11.211 0.010 56.20  ? 204  ARG A CG  1 
ATOM   1496 C CD  . ARG A 1 204 ? -6.852  49.091  -11.667 0.010 56.19  ? 204  ARG A CD  1 
ATOM   1497 N NE  . ARG A 1 204 ? -8.237  48.639  -11.771 0.010 56.19  ? 204  ARG A NE  1 
ATOM   1498 C CZ  . ARG A 1 204 ? -9.260  49.432  -12.073 0.010 56.17  ? 204  ARG A CZ  1 
ATOM   1499 N NH1 . ARG A 1 204 ? -9.057  50.722  -12.304 0.010 56.18  ? 204  ARG A NH1 1 
ATOM   1500 N NH2 . ARG A 1 204 ? -10.488 48.935  -12.145 0.010 56.17  ? 204  ARG A NH2 1 
ATOM   1501 N N   . MET A 1 205 ? -4.142  47.315  -7.814  0.75  56.05  ? 205  MET A N   1 
ATOM   1502 C CA  . MET A 1 205 ? -4.808  46.771  -6.631  0.75  56.13  ? 205  MET A CA  1 
ATOM   1503 C C   . MET A 1 205 ? -6.210  47.347  -6.453  0.75  56.39  ? 205  MET A C   1 
ATOM   1504 O O   . MET A 1 205 ? -6.450  48.521  -6.749  0.75  56.51  ? 205  MET A O   1 
ATOM   1505 C CB  . MET A 1 205 ? -3.982  47.044  -5.370  0.75  55.82  ? 205  MET A CB  1 
ATOM   1506 C CG  . MET A 1 205 ? -2.998  45.945  -4.991  0.75  55.48  ? 205  MET A CG  1 
ATOM   1507 S SD  . MET A 1 205 ? -2.240  46.214  -3.358  0.75  55.10  ? 205  MET A SD  1 
ATOM   1508 C CE  . MET A 1 205 ? -1.517  44.602  -3.053  0.75  55.57  ? 205  MET A CE  1 
ATOM   1509 N N   . VAL A 1 206 ? -7.126  46.514  -5.961  1.00  56.54  ? 206  VAL A N   1 
ATOM   1510 C CA  . VAL A 1 206 ? -8.499  46.923  -5.679  1.00  56.83  ? 206  VAL A CA  1 
ATOM   1511 C C   . VAL A 1 206 ? -8.847  46.630  -4.213  1.00  57.12  ? 206  VAL A C   1 
ATOM   1512 O O   . VAL A 1 206 ? -8.336  45.679  -3.627  1.00  57.26  ? 206  VAL A O   1 
ATOM   1513 C CB  . VAL A 1 206 ? -9.504  46.234  -6.668  1.00  56.95  ? 206  VAL A CB  1 
ATOM   1514 C CG1 . VAL A 1 206 ? -10.966 46.326  -6.185  1.00  56.92  ? 206  VAL A CG1 1 
ATOM   1515 C CG2 . VAL A 1 206 ? -9.382  46.849  -8.059  1.00  56.90  ? 206  VAL A CG2 1 
ATOM   1516 N N   . LEU A 1 207 ? -9.711  47.457  -3.629  1.00  57.45  ? 207  LEU A N   1 
ATOM   1517 C CA  . LEU A 1 207 ? -10.160 47.272  -2.252  1.00  57.76  ? 207  LEU A CA  1 
ATOM   1518 C C   . LEU A 1 207 ? -11.678 47.185  -2.200  1.00  58.08  ? 207  LEU A C   1 
ATOM   1519 O O   . LEU A 1 207 ? -12.368 47.910  -2.921  1.00  58.43  ? 207  LEU A O   1 
ATOM   1520 C CB  . LEU A 1 207 ? -9.664  48.432  -1.378  1.00  57.63  ? 207  LEU A CB  1 
ATOM   1521 C CG  . LEU A 1 207 ? -9.850  48.405  0.146   1.00  57.78  ? 207  LEU A CG  1 
ATOM   1522 C CD1 . LEU A 1 207 ? -8.768  49.208  0.845   1.00  57.51  ? 207  LEU A CD1 1 
ATOM   1523 C CD2 . LEU A 1 207 ? -11.222 48.915  0.561   1.00  58.38  ? 207  LEU A CD2 1 
ATOM   1524 N N   . VAL A 1 208 ? -12.190 46.296  -1.349  1.00  58.36  ? 208  VAL A N   1 
ATOM   1525 C CA  . VAL A 1 208 ? -13.629 46.197  -1.085  1.00  58.65  ? 208  VAL A CA  1 
ATOM   1526 C C   . VAL A 1 208 ? -13.897 46.124  0.422   1.00  59.12  ? 208  VAL A C   1 
ATOM   1527 O O   . VAL A 1 208 ? -13.508 45.157  1.076   1.00  59.39  ? 208  VAL A O   1 
ATOM   1528 C CB  . VAL A 1 208 ? -14.311 44.996  -1.834  1.00  58.58  ? 208  VAL A CB  1 
ATOM   1529 C CG1 . VAL A 1 208 ? -14.232 45.173  -3.347  1.00  57.93  ? 208  VAL A CG1 1 
ATOM   1530 C CG2 . VAL A 1 208 ? -13.716 43.653  -1.423  1.00  58.52  ? 208  VAL A CG2 1 
ATOM   1531 N N   . GLY A 1 209 ? -14.544 47.155  0.969   1.00  59.50  ? 209  GLY A N   1 
ATOM   1532 C CA  . GLY A 1 209 ? -14.905 47.183  2.391   1.00  59.99  ? 209  GLY A CA  1 
ATOM   1533 C C   . GLY A 1 209 ? -14.468 48.453  3.104   1.00  60.56  ? 209  GLY A C   1 
ATOM   1534 O O   . GLY A 1 209 ? -13.394 48.993  2.828   1.00  60.54  ? 209  GLY A O   1 
ATOM   1535 N N   . ASP A 1 210 ? -15.305 48.918  4.032   1.00  61.05  ? 210  ASP A N   1 
ATOM   1536 C CA  . ASP A 1 210 ? -15.107 50.203  4.718   1.00  61.47  ? 210  ASP A CA  1 
ATOM   1537 C C   . ASP A 1 210 ? -13.803 50.274  5.538   1.00  61.66  ? 210  ASP A C   1 
ATOM   1538 O O   . ASP A 1 210 ? -13.631 49.556  6.529   1.00  61.73  ? 210  ASP A O   1 
ATOM   1539 C CB  . ASP A 1 210 ? -16.321 50.524  5.601   1.00  61.50  ? 210  ASP A CB  1 
ATOM   1540 C CG  . ASP A 1 210 ? -16.391 51.993  6.001   1.00  62.26  ? 210  ASP A CG  1 
ATOM   1541 O OD1 . ASP A 1 210 ? -15.726 52.832  5.345   1.00  62.60  ? 210  ASP A OD1 1 
ATOM   1542 O OD2 . ASP A 1 210 ? -17.121 52.313  6.969   1.00  62.90  ? 210  ASP A OD2 1 
ATOM   1543 N N   . VAL A 1 211 ? -12.898 51.158  5.118   1.00  61.72  ? 211  VAL A N   1 
ATOM   1544 C CA  . VAL A 1 211 ? -11.582 51.292  5.755   1.00  61.93  ? 211  VAL A CA  1 
ATOM   1545 C C   . VAL A 1 211 ? -11.214 52.723  6.162   1.00  61.97  ? 211  VAL A C   1 
ATOM   1546 O O   . VAL A 1 211 ? -10.162 52.945  6.767   1.00  61.85  ? 211  VAL A O   1 
ATOM   1547 C CB  . VAL A 1 211 ? -10.446 50.761  4.839   1.00  61.98  ? 211  VAL A CB  1 
ATOM   1548 C CG1 . VAL A 1 211 ? -10.471 49.246  4.763   1.00  61.75  ? 211  VAL A CG1 1 
ATOM   1549 C CG2 . VAL A 1 211 ? -10.515 51.405  3.443   1.00  62.22  ? 211  VAL A CG2 1 
ATOM   1550 N N   . LYS A 1 212 ? -12.075 53.679  5.819   0.70  62.14  ? 212  LYS A N   1 
ATOM   1551 C CA  . LYS A 1 212 ? -11.781 55.100  5.985   0.70  62.35  ? 212  LYS A CA  1 
ATOM   1552 C C   . LYS A 1 212 ? -11.777 55.515  7.450   0.70  62.54  ? 212  LYS A C   1 
ATOM   1553 O O   . LYS A 1 212 ? -12.711 55.205  8.196   0.70  62.61  ? 212  LYS A O   1 
ATOM   1554 C CB  . LYS A 1 212 ? -12.777 55.952  5.181   0.70  62.41  ? 212  LYS A CB  1 
ATOM   1555 C CG  . LYS A 1 212 ? -12.486 57.455  5.161   0.70  62.44  ? 212  LYS A CG  1 
ATOM   1556 C CD  . LYS A 1 212 ? -11.286 57.795  4.275   0.70  62.38  ? 212  LYS A CD  1 
ATOM   1557 C CE  . LYS A 1 212 ? -10.925 59.277  4.344   0.70  62.09  ? 212  LYS A CE  1 
ATOM   1558 N NZ  . LYS A 1 212 ? -9.755  59.580  3.450   0.70  61.17  ? 212  LYS A NZ  1 
ATOM   1559 N N   . ASP A 1 213 ? -10.704 56.207  7.842   1.00  62.83  ? 213  ASP A N   1 
ATOM   1560 C CA  . ASP A 1 213 ? -10.529 56.783  9.188   1.00  63.01  ? 213  ASP A CA  1 
ATOM   1561 C C   . ASP A 1 213 ? -10.724 55.770  10.305  1.00  63.03  ? 213  ASP A C   1 
ATOM   1562 O O   . ASP A 1 213 ? -11.347 56.069  11.325  1.00  63.01  ? 213  ASP A O   1 
ATOM   1563 C CB  . ASP A 1 213 ? -11.456 57.992  9.409   1.00  63.02  ? 213  ASP A CB  1 
ATOM   1564 C CG  . ASP A 1 213 ? -11.394 58.998  8.277   1.00  63.40  ? 213  ASP A CG  1 
ATOM   1565 O OD1 . ASP A 1 213 ? -12.472 59.379  7.782   1.00  63.83  ? 213  ASP A OD1 1 
ATOM   1566 O OD2 . ASP A 1 213 ? -10.279 59.400  7.874   1.00  64.06  ? 213  ASP A OD2 1 
ATOM   1567 N N   . ARG A 1 214 ? -10.189 54.571  10.098  0.78  63.28  ? 214  ARG A N   1 
ATOM   1568 C CA  . ARG A 1 214 ? -10.249 53.508  11.095  0.78  63.69  ? 214  ARG A CA  1 
ATOM   1569 C C   . ARG A 1 214 ? -9.002  52.625  11.036  0.78  64.10  ? 214  ARG A C   1 
ATOM   1570 O O   . ARG A 1 214 ? -8.389  52.464  9.977   0.78  64.13  ? 214  ARG A O   1 
ATOM   1571 C CB  . ARG A 1 214 ? -11.539 52.685  10.955  0.78  63.60  ? 214  ARG A CB  1 
ATOM   1572 C CG  . ARG A 1 214 ? -11.805 52.113  9.564   0.78  63.34  ? 214  ARG A CG  1 
ATOM   1573 C CD  . ARG A 1 214 ? -13.285 51.764  9.350   0.78  62.90  ? 214  ARG A CD  1 
ATOM   1574 N NE  . ARG A 1 214 ? -13.732 50.640  10.175  0.78  62.51  ? 214  ARG A NE  1 
ATOM   1575 C CZ  . ARG A 1 214 ? -14.635 50.726  11.148  0.78  62.47  ? 214  ARG A CZ  1 
ATOM   1576 N NH1 . ARG A 1 214 ? -15.210 51.886  11.430  0.78  63.30  ? 214  ARG A NH1 1 
ATOM   1577 N NH2 . ARG A 1 214 ? -14.967 49.647  11.842  0.78  62.70  ? 214  ARG A NH2 1 
ATOM   1578 N N   . VAL A 1 215 ? -8.620  52.073  12.184  1.00  64.61  ? 215  VAL A N   1 
ATOM   1579 C CA  . VAL A 1 215 ? -7.448  51.202  12.264  1.00  65.13  ? 215  VAL A CA  1 
ATOM   1580 C C   . VAL A 1 215 ? -7.585  49.988  11.335  1.00  65.38  ? 215  VAL A C   1 
ATOM   1581 O O   . VAL A 1 215 ? -8.619  49.320  11.312  1.00  65.48  ? 215  VAL A O   1 
ATOM   1582 C CB  . VAL A 1 215 ? -7.131  50.804  13.736  1.00  65.08  ? 215  VAL A CB  1 
ATOM   1583 C CG1 . VAL A 1 215 ? -6.363  49.489  13.821  1.00  65.48  ? 215  VAL A CG1 1 
ATOM   1584 C CG2 . VAL A 1 215 ? -6.348  51.924  14.416  1.00  64.96  ? 215  VAL A CG2 1 
ATOM   1585 N N   . ALA A 1 216 ? -6.539  49.736  10.555  1.00  65.94  ? 216  ALA A N   1 
ATOM   1586 C CA  . ALA A 1 216 ? -6.518  48.631  9.609   1.00  66.60  ? 216  ALA A CA  1 
ATOM   1587 C C   . ALA A 1 216 ? -5.466  47.611  10.008  1.00  67.02  ? 216  ALA A C   1 
ATOM   1588 O O   . ALA A 1 216 ? -4.330  47.974  10.305  1.00  67.36  ? 216  ALA A O   1 
ATOM   1589 C CB  . ALA A 1 216 ? -6.250  49.144  8.207   1.00  66.64  ? 216  ALA A CB  1 
ATOM   1590 N N   . ILE A 1 217 ? -5.849  46.336  10.007  1.00  67.53  ? 217  ILE A N   1 
ATOM   1591 C CA  . ILE A 1 217 ? -4.948  45.256  10.405  1.00  68.02  ? 217  ILE A CA  1 
ATOM   1592 C C   . ILE A 1 217 ? -4.888  44.159  9.340   1.00  68.30  ? 217  ILE A C   1 
ATOM   1593 O O   . ILE A 1 217 ? -5.838  43.383  9.180   1.00  68.25  ? 217  ILE A O   1 
ATOM   1594 C CB  . ILE A 1 217 ? -5.368  44.640  11.767  1.00  68.15  ? 217  ILE A CB  1 
ATOM   1595 C CG1 . ILE A 1 217 ? -5.611  45.737  12.812  1.00  68.52  ? 217  ILE A CG1 1 
ATOM   1596 C CG2 . ILE A 1 217 ? -4.311  43.671  12.267  1.00  67.94  ? 217  ILE A CG2 1 
ATOM   1597 C CD1 . ILE A 1 217 ? -6.532  45.319  13.953  1.00  69.28  ? 217  ILE A CD1 1 
ATOM   1598 N N   . LEU A 1 218 ? -3.769  44.105  8.620   1.00  68.69  ? 218  LEU A N   1 
ATOM   1599 C CA  . LEU A 1 218 ? -3.549  43.077  7.606   1.00  69.20  ? 218  LEU A CA  1 
ATOM   1600 C C   . LEU A 1 218 ? -3.174  41.762  8.259   1.00  69.46  ? 218  LEU A C   1 
ATOM   1601 O O   . LEU A 1 218 ? -2.077  41.612  8.795   1.00  69.30  ? 218  LEU A O   1 
ATOM   1602 C CB  . LEU A 1 218 ? -2.448  43.490  6.627   1.00  69.26  ? 218  LEU A CB  1 
ATOM   1603 C CG  . LEU A 1 218 ? -2.800  44.391  5.445   1.00  69.72  ? 218  LEU A CG  1 
ATOM   1604 C CD1 . LEU A 1 218 ? -1.519  44.978  4.851   1.00  70.59  ? 218  LEU A CD1 1 
ATOM   1605 C CD2 . LEU A 1 218 ? -3.584  43.628  4.384   1.00  69.37  ? 218  LEU A CD2 1 
ATOM   1606 N N   . VAL A 1 219 ? -4.098  40.812  8.215   1.00  70.09  ? 219  VAL A N   1 
ATOM   1607 C CA  . VAL A 1 219 ? -3.860  39.493  8.783   1.00  70.83  ? 219  VAL A CA  1 
ATOM   1608 C C   . VAL A 1 219 ? -3.700  38.476  7.662   1.00  71.25  ? 219  VAL A C   1 
ATOM   1609 O O   . VAL A 1 219 ? -4.543  38.386  6.770   1.00  71.31  ? 219  VAL A O   1 
ATOM   1610 C CB  . VAL A 1 219 ? -4.985  39.063  9.757   1.00  70.78  ? 219  VAL A CB  1 
ATOM   1611 C CG1 . VAL A 1 219 ? -4.580  37.807  10.513  1.00  70.88  ? 219  VAL A CG1 1 
ATOM   1612 C CG2 . VAL A 1 219 ? -5.289  40.177  10.745  1.00  70.87  ? 219  VAL A CG2 1 
ATOM   1613 N N   . ASP A 1 220 ? -2.600  37.732  7.706   1.00  71.93  ? 220  ASP A N   1 
ATOM   1614 C CA  . ASP A 1 220 ? -2.333  36.686  6.725   1.00  72.75  ? 220  ASP A CA  1 
ATOM   1615 C C   . ASP A 1 220 ? -1.589  35.494  7.348   1.00  73.24  ? 220  ASP A C   1 
ATOM   1616 O O   . ASP A 1 220 ? -1.029  35.598  8.440   1.00  73.33  ? 220  ASP A O   1 
ATOM   1617 C CB  . ASP A 1 220 ? -1.558  37.267  5.537   1.00  72.72  ? 220  ASP A CB  1 
ATOM   1618 C CG  . ASP A 1 220 ? -1.644  36.396  4.291   1.00  73.17  ? 220  ASP A CG  1 
ATOM   1619 O OD1 . ASP A 1 220 ? -2.637  35.655  4.125   1.00  73.25  ? 220  ASP A OD1 1 
ATOM   1620 O OD2 . ASP A 1 220 ? -0.711  36.461  3.464   1.00  74.00  ? 220  ASP A OD2 1 
ATOM   1621 N N   . ASP A 1 221 ? -1.602  34.362  6.649   1.00  74.04  ? 221  ASP A N   1 
ATOM   1622 C CA  . ASP A 1 221 ? -0.932  33.139  7.108   1.00  74.92  ? 221  ASP A CA  1 
ATOM   1623 C C   . ASP A 1 221 ? 0.599   33.198  6.995   1.00  75.32  ? 221  ASP A C   1 
ATOM   1624 O O   . ASP A 1 221 ? 1.310   32.743  7.901   1.00  75.40  ? 221  ASP A O   1 
ATOM   1625 C CB  . ASP A 1 221 ? -1.472  31.911  6.368   1.00  74.98  ? 221  ASP A CB  1 
ATOM   1626 C CG  . ASP A 1 221 ? -1.509  32.108  4.861   1.00  75.76  ? 221  ASP A CG  1 
ATOM   1627 O OD1 . ASP A 1 221 ? -0.618  31.571  4.172   1.00  76.94  ? 221  ASP A OD1 1 
ATOM   1628 O OD2 . ASP A 1 221 ? -2.418  32.814  4.366   1.00  75.84  ? 221  ASP A OD2 1 
ATOM   1629 N N   . MET A 1 222 ? 1.094   33.749  5.883   0.61  75.82  ? 222  MET A N   1 
ATOM   1630 C CA  . MET A 1 222 ? 2.539   33.916  5.653   0.61  76.31  ? 222  MET A CA  1 
ATOM   1631 C C   . MET A 1 222 ? 2.874   34.874  4.505   0.61  76.61  ? 222  MET A C   1 
ATOM   1632 O O   . MET A 1 222 ? 2.175   34.914  3.492   0.61  76.55  ? 222  MET A O   1 
ATOM   1633 C CB  . MET A 1 222 ? 3.240   32.560  5.434   0.61  76.32  ? 222  MET A CB  1 
ATOM   1634 C CG  . MET A 1 222 ? 2.646   31.676  4.332   0.61  76.50  ? 222  MET A CG  1 
ATOM   1635 S SD  . MET A 1 222 ? 3.437   30.052  4.182   0.61  76.91  ? 222  MET A SD  1 
ATOM   1636 C CE  . MET A 1 222 ? 2.859   29.223  5.668   0.61  77.10  ? 222  MET A CE  1 
ATOM   1637 N N   . ALA A 1 223 ? 3.952   35.639  4.685   1.00  77.13  ? 223  ALA A N   1 
ATOM   1638 C CA  . ALA A 1 223 ? 4.485   36.523  3.644   1.00  77.56  ? 223  ALA A CA  1 
ATOM   1639 C C   . ALA A 1 223 ? 5.970   36.255  3.423   1.00  77.81  ? 223  ALA A C   1 
ATOM   1640 O O   . ALA A 1 223 ? 6.758   36.262  4.374   1.00  78.10  ? 223  ALA A O   1 
ATOM   1641 C CB  . ALA A 1 223 ? 4.261   37.987  4.009   1.00  77.57  ? 223  ALA A CB  1 
ATOM   1642 N N   . ASP A 1 224 ? 6.342   36.016  2.168   1.00  78.08  ? 224  ASP A N   1 
ATOM   1643 C CA  . ASP A 1 224 ? 7.719   35.690  1.807   1.00  78.27  ? 224  ASP A CA  1 
ATOM   1644 C C   . ASP A 1 224 ? 8.505   36.937  1.404   1.00  78.37  ? 224  ASP A C   1 
ATOM   1645 O O   . ASP A 1 224 ? 9.321   37.435  2.180   1.00  78.69  ? 224  ASP A O   1 
ATOM   1646 C CB  . ASP A 1 224 ? 7.752   34.639  0.690   1.00  78.37  ? 224  ASP A CB  1 
ATOM   1647 C CG  . ASP A 1 224 ? 9.142   34.451  0.099   1.00  78.95  ? 224  ASP A CG  1 
ATOM   1648 O OD1 . ASP A 1 224 ? 10.113  34.240  0.874   1.00  79.26  ? 224  ASP A OD1 1 
ATOM   1649 O OD2 . ASP A 1 224 ? 9.261   34.523  -1.148  1.00  78.65  ? 224  ASP A OD2 1 
ATOM   1650 N N   . THR A 1 225 ? 8.260   37.435  0.193   0.10  78.37  ? 225  THR A N   1 
ATOM   1651 C CA  . THR A 1 225 ? 8.954   38.617  -0.312  0.10  78.35  ? 225  THR A CA  1 
ATOM   1652 C C   . THR A 1 225 ? 8.320   39.903  0.205   0.10  78.41  ? 225  THR A C   1 
ATOM   1653 O O   . THR A 1 225 ? 8.861   40.991  0.001   0.10  78.40  ? 225  THR A O   1 
ATOM   1654 C CB  . THR A 1 225 ? 8.963   38.657  -1.852  0.10  78.34  ? 225  THR A CB  1 
ATOM   1655 O OG1 . THR A 1 225 ? 7.626   38.505  -2.344  0.10  78.33  ? 225  THR A OG1 1 
ATOM   1656 C CG2 . THR A 1 225 ? 9.836   37.547  -2.411  0.10  78.30  ? 225  THR A CG2 1 
ATOM   1657 N N   . CYS A 1 226 ? 7.173   39.762  0.870   1.00  78.50  ? 226  CYS A N   1 
ATOM   1658 C CA  . CYS A 1 226 ? 6.372   40.892  1.370   1.00  78.72  ? 226  CYS A CA  1 
ATOM   1659 C C   . CYS A 1 226 ? 5.766   41.767  0.261   1.00  78.49  ? 226  CYS A C   1 
ATOM   1660 O O   . CYS A 1 226 ? 4.993   42.684  0.549   1.00  78.47  ? 226  CYS A O   1 
ATOM   1661 C CB  . CYS A 1 226 ? 7.162   41.751  2.381   1.00  78.81  ? 226  CYS A CB  1 
ATOM   1662 S SG  . CYS A 1 226 ? 7.061   41.216  4.128   1.00  79.82  ? 226  CYS A SG  1 
ATOM   1663 N N   . GLY A 1 227 ? 6.104   41.464  -0.996  1.00  78.26  ? 227  GLY A N   1 
ATOM   1664 C CA  . GLY A 1 227 ? 5.669   42.251  -2.153  1.00  77.99  ? 227  GLY A CA  1 
ATOM   1665 C C   . GLY A 1 227 ? 4.183   42.558  -2.173  1.00  77.74  ? 227  GLY A C   1 
ATOM   1666 O O   . GLY A 1 227 ? 3.771   43.679  -2.481  1.00  77.78  ? 227  GLY A O   1 
ATOM   1667 N N   . THR A 1 228 ? 3.381   41.556  -1.825  1.00  77.49  ? 228  THR A N   1 
ATOM   1668 C CA  . THR A 1 228 ? 1.924   41.686  -1.777  1.00  77.12  ? 228  THR A CA  1 
ATOM   1669 C C   . THR A 1 228 ? 1.458   42.520  -0.578  1.00  76.95  ? 228  THR A C   1 
ATOM   1670 O O   . THR A 1 228 ? 0.617   43.409  -0.728  1.00  76.86  ? 228  THR A O   1 
ATOM   1671 C CB  . THR A 1 228 ? 1.241   40.294  -1.755  1.00  77.10  ? 228  THR A CB  1 
ATOM   1672 O OG1 . THR A 1 228 ? 1.748   39.496  -2.832  1.00  77.01  ? 228  THR A OG1 1 
ATOM   1673 C CG2 . THR A 1 228 ? -0.268  40.421  -1.904  1.00  77.00  ? 228  THR A CG2 1 
ATOM   1674 N N   . ILE A 1 229 ? 2.018   42.233  0.597   1.00  76.75  ? 229  ILE A N   1 
ATOM   1675 C CA  . ILE A 1 229 ? 1.598   42.866  1.849   1.00  76.62  ? 229  ILE A CA  1 
ATOM   1676 C C   . ILE A 1 229 ? 2.085   44.313  1.987   1.00  76.48  ? 229  ILE A C   1 
ATOM   1677 O O   . ILE A 1 229 ? 1.436   45.129  2.651   1.00  76.62  ? 229  ILE A O   1 
ATOM   1678 C CB  . ILE A 1 229 ? 1.973   41.986  3.099   1.00  76.77  ? 229  ILE A CB  1 
ATOM   1679 C CG1 . ILE A 1 229 ? 1.289   42.497  4.373   1.00  76.76  ? 229  ILE A CG1 1 
ATOM   1680 C CG2 . ILE A 1 229 ? 3.486   41.869  3.280   1.00  76.67  ? 229  ILE A CG2 1 
ATOM   1681 C CD1 . ILE A 1 229 ? 1.172   41.458  5.474   1.00  77.02  ? 229  ILE A CD1 1 
ATOM   1682 N N   . CYS A 1 230 ? 3.212   44.630  1.352   1.00  76.27  ? 230  CYS A N   1 
ATOM   1683 C CA  . CYS A 1 230 ? 3.734   45.998  1.342   1.00  76.03  ? 230  CYS A CA  1 
ATOM   1684 C C   . CYS A 1 230 ? 2.832   46.918  0.533   1.00  75.90  ? 230  CYS A C   1 
ATOM   1685 O O   . CYS A 1 230 ? 2.402   47.962  1.026   1.00  75.96  ? 230  CYS A O   1 
ATOM   1686 C CB  . CYS A 1 230 ? 5.168   46.041  0.812   1.00  76.05  ? 230  CYS A CB  1 
ATOM   1687 S SG  . CYS A 1 230 ? 6.391   45.341  1.947   1.00  76.12  ? 230  CYS A SG  1 
ATOM   1688 N N   . HIS A 1 231 ? 2.527   46.513  -0.698  1.00  75.75  ? 231  HIS A N   1 
ATOM   1689 C CA  . HIS A 1 231 ? 1.602   47.263  -1.550  1.00  75.82  ? 231  HIS A CA  1 
ATOM   1690 C C   . HIS A 1 231 ? 0.183   47.291  -0.985  1.00  75.50  ? 231  HIS A C   1 
ATOM   1691 O O   . HIS A 1 231 ? -0.600  48.191  -1.303  1.00  75.76  ? 231  HIS A O   1 
ATOM   1692 C CB  . HIS A 1 231 ? 1.606   46.710  -2.976  1.00  76.05  ? 231  HIS A CB  1 
ATOM   1693 C CG  . HIS A 1 231 ? 2.887   46.957  -3.708  1.00  77.12  ? 231  HIS A CG  1 
ATOM   1694 N ND1 . HIS A 1 231 ? 3.296   48.219  -4.086  1.00  78.04  ? 231  HIS A ND1 1 
ATOM   1695 C CD2 . HIS A 1 231 ? 3.856   46.107  -4.123  1.00  77.78  ? 231  HIS A CD2 1 
ATOM   1696 C CE1 . HIS A 1 231 ? 4.460   48.135  -4.704  1.00  78.61  ? 231  HIS A CE1 1 
ATOM   1697 N NE2 . HIS A 1 231 ? 4.822   46.864  -4.740  1.00  78.92  ? 231  HIS A NE2 1 
ATOM   1698 N N   . ALA A 1 232 ? -0.135  46.309  -0.141  1.00  74.90  ? 232  ALA A N   1 
ATOM   1699 C CA  . ALA A 1 232 ? -1.411  46.272  0.560   1.00  74.30  ? 232  ALA A CA  1 
ATOM   1700 C C   . ALA A 1 232 ? -1.511  47.391  1.592   1.00  73.94  ? 232  ALA A C   1 
ATOM   1701 O O   . ALA A 1 232 ? -2.589  47.942  1.804   1.00  73.89  ? 232  ALA A O   1 
ATOM   1702 C CB  . ALA A 1 232 ? -1.620  44.920  1.212   1.00  74.40  ? 232  ALA A CB  1 
ATOM   1703 N N   . ALA A 1 233 ? -0.384  47.726  2.220   1.00  73.57  ? 233  ALA A N   1 
ATOM   1704 C CA  . ALA A 1 233 ? -0.328  48.825  3.186   1.00  73.21  ? 233  ALA A CA  1 
ATOM   1705 C C   . ALA A 1 233 ? -0.461  50.188  2.507   1.00  72.93  ? 233  ALA A C   1 
ATOM   1706 O O   . ALA A 1 233 ? -1.151  51.074  3.015   1.00  72.84  ? 233  ALA A O   1 
ATOM   1707 C CB  . ALA A 1 233 ? 0.955   48.755  3.997   1.00  73.34  ? 233  ALA A CB  1 
ATOM   1708 N N   . ASP A 1 234 ? 0.202   50.337  1.359   1.00  72.64  ? 234  ASP A N   1 
ATOM   1709 C CA  . ASP A 1 234 ? 0.141   51.560  0.559   1.00  72.33  ? 234  ASP A CA  1 
ATOM   1710 C C   . ASP A 1 234 ? -1.299  51.878  0.159   1.00  72.07  ? 234  ASP A C   1 
ATOM   1711 O O   . ASP A 1 234 ? -1.756  53.011  0.328   1.00  72.01  ? 234  ASP A O   1 
ATOM   1712 C CB  . ASP A 1 234 ? 1.020   51.435  -0.693  1.00  72.39  ? 234  ASP A CB  1 
ATOM   1713 C CG  . ASP A 1 234 ? 2.406   50.869  -0.396  1.00  72.79  ? 234  ASP A CG  1 
ATOM   1714 O OD1 . ASP A 1 234 ? 2.838   50.884  0.777   1.00  72.98  ? 234  ASP A OD1 1 
ATOM   1715 O OD2 . ASP A 1 234 ? 3.074   50.413  -1.351  1.00  73.40  ? 234  ASP A OD2 1 
ATOM   1716 N N   . LYS A 1 235 ? -2.002  50.865  -0.353  1.00  71.87  ? 235  LYS A N   1 
ATOM   1717 C CA  . LYS A 1 235 ? -3.392  50.998  -0.805  1.00  71.68  ? 235  LYS A CA  1 
ATOM   1718 C C   . LYS A 1 235 ? -4.303  51.444  0.335   1.00  71.39  ? 235  LYS A C   1 
ATOM   1719 O O   . LYS A 1 235 ? -5.046  52.412  0.195   1.00  71.40  ? 235  LYS A O   1 
ATOM   1720 C CB  . LYS A 1 235 ? -3.895  49.672  -1.399  1.00  71.74  ? 235  LYS A CB  1 
ATOM   1721 C CG  . LYS A 1 235 ? -4.825  49.809  -2.613  1.00  71.96  ? 235  LYS A CG  1 
ATOM   1722 C CD  . LYS A 1 235 ? -6.251  50.234  -2.255  1.00  72.81  ? 235  LYS A CD  1 
ATOM   1723 C CE  . LYS A 1 235 ? -7.046  50.568  -3.526  1.00  73.21  ? 235  LYS A CE  1 
ATOM   1724 N NZ  . LYS A 1 235 ? -8.461  51.006  -3.274  1.00  73.23  ? 235  LYS A NZ  1 
ATOM   1725 N N   . LEU A 1 236 ? -4.222  50.738  1.460   1.00  71.08  ? 236  LEU A N   1 
ATOM   1726 C CA  . LEU A 1 236 ? -5.019  51.040  2.646   1.00  70.82  ? 236  LEU A CA  1 
ATOM   1727 C C   . LEU A 1 236 ? -4.847  52.474  3.143   1.00  70.68  ? 236  LEU A C   1 
ATOM   1728 O O   . LEU A 1 236 ? -5.799  53.076  3.637   1.00  70.81  ? 236  LEU A O   1 
ATOM   1729 C CB  . LEU A 1 236 ? -4.692  50.055  3.774   1.00  70.79  ? 236  LEU A CB  1 
ATOM   1730 C CG  . LEU A 1 236 ? -5.296  48.648  3.731   1.00  70.47  ? 236  LEU A CG  1 
ATOM   1731 C CD1 . LEU A 1 236 ? -4.555  47.727  4.685   1.00  70.18  ? 236  LEU A CD1 1 
ATOM   1732 C CD2 . LEU A 1 236 ? -6.779  48.664  4.062   1.00  70.45  ? 236  LEU A CD2 1 
ATOM   1733 N N   . LEU A 1 237 ? -3.632  53.007  3.020   1.00  70.51  ? 237  LEU A N   1 
ATOM   1734 C CA  . LEU A 1 237 ? -3.344  54.390  3.410   1.00  70.44  ? 237  LEU A CA  1 
ATOM   1735 C C   . LEU A 1 237 ? -3.886  55.416  2.412   1.00  70.40  ? 237  LEU A C   1 
ATOM   1736 O O   . LEU A 1 237 ? -4.234  56.540  2.794   1.00  70.29  ? 237  LEU A O   1 
ATOM   1737 C CB  . LEU A 1 237 ? -1.843  54.608  3.633   1.00  70.28  ? 237  LEU A CB  1 
ATOM   1738 C CG  . LEU A 1 237 ? -1.217  54.289  4.998   1.00  70.17  ? 237  LEU A CG  1 
ATOM   1739 C CD1 . LEU A 1 237 ? 0.098   55.036  5.099   1.00  70.69  ? 237  LEU A CD1 1 
ATOM   1740 C CD2 . LEU A 1 237 ? -2.110  54.690  6.174   1.00  69.67  ? 237  LEU A CD2 1 
ATOM   1741 N N   . SER A 1 238 ? -3.950  55.023  1.140   1.00  70.29  ? 238  SER A N   1 
ATOM   1742 C CA  . SER A 1 238 ? -4.570  55.844  0.103   1.00  70.25  ? 238  SER A CA  1 
ATOM   1743 C C   . SER A 1 238 ? -6.085  55.873  0.306   1.00  70.26  ? 238  SER A C   1 
ATOM   1744 O O   . SER A 1 238 ? -6.741  56.885  0.049   1.00  70.39  ? 238  SER A O   1 
ATOM   1745 C CB  . SER A 1 238 ? -4.232  55.305  -1.286  1.00  70.11  ? 238  SER A CB  1 
ATOM   1746 O OG  . SER A 1 238 ? -2.835  55.127  -1.441  1.00  70.59  ? 238  SER A OG  1 
ATOM   1747 N N   . ALA A 1 239 ? -6.628  54.758  0.787   1.00  70.19  ? 239  ALA A N   1 
ATOM   1748 C CA  . ALA A 1 239 ? -8.056  54.645  1.054   1.00  70.11  ? 239  ALA A CA  1 
ATOM   1749 C C   . ALA A 1 239 ? -8.432  55.279  2.393   1.00  70.16  ? 239  ALA A C   1 
ATOM   1750 O O   . ALA A 1 239 ? -9.608  55.318  2.758   1.00  70.26  ? 239  ALA A O   1 
ATOM   1751 C CB  . ALA A 1 239 ? -8.499  53.190  0.984   1.00  70.10  ? 239  ALA A CB  1 
ATOM   1752 N N   . GLY A 1 240 ? -7.428  55.759  3.124   1.00  70.17  ? 240  GLY A N   1 
ATOM   1753 C CA  . GLY A 1 240 ? -7.650  56.670  4.243   1.00  70.38  ? 240  GLY A CA  1 
ATOM   1754 C C   . GLY A 1 240 ? -7.788  56.060  5.624   1.00  70.66  ? 240  GLY A C   1 
ATOM   1755 O O   . GLY A 1 240 ? -8.403  56.663  6.512   1.00  70.66  ? 240  GLY A O   1 
ATOM   1756 N N   . ALA A 1 241 ? -7.214  54.872  5.813   1.00  70.81  ? 241  ALA A N   1 
ATOM   1757 C CA  . ALA A 1 241 ? -7.195  54.227  7.124   1.00  70.88  ? 241  ALA A CA  1 
ATOM   1758 C C   . ALA A 1 241 ? -6.250  54.984  8.044   1.00  70.98  ? 241  ALA A C   1 
ATOM   1759 O O   . ALA A 1 241 ? -5.155  55.375  7.633   1.00  70.86  ? 241  ALA A O   1 
ATOM   1760 C CB  . ALA A 1 241 ? -6.770  52.772  7.000   1.00  70.99  ? 241  ALA A CB  1 
ATOM   1761 N N   . THR A 1 242 ? -6.684  55.193  9.284   1.00  71.26  ? 242  THR A N   1 
ATOM   1762 C CA  . THR A 1 242 ? -5.915  55.960  10.260  1.00  71.57  ? 242  THR A CA  1 
ATOM   1763 C C   . THR A 1 242 ? -4.495  55.413  10.414  1.00  71.72  ? 242  THR A C   1 
ATOM   1764 O O   . THR A 1 242 ? -3.523  56.112  10.124  1.00  71.92  ? 242  THR A O   1 
ATOM   1765 C CB  . THR A 1 242 ? -6.630  56.013  11.631  1.00  71.66  ? 242  THR A CB  1 
ATOM   1766 O OG1 . THR A 1 242 ? -7.929  56.598  11.474  1.00  71.83  ? 242  THR A OG1 1 
ATOM   1767 C CG2 . THR A 1 242 ? -5.823  56.833  12.632  1.00  71.76  ? 242  THR A CG2 1 
ATOM   1768 N N   . ARG A 1 243 ? -4.385  54.165  10.864  1.00  71.87  ? 243  ARG A N   1 
ATOM   1769 C CA  . ARG A 1 243 ? -3.090  53.489  10.991  1.00  72.06  ? 243  ARG A CA  1 
ATOM   1770 C C   . ARG A 1 243 ? -3.186  52.061  10.437  1.00  71.96  ? 243  ARG A C   1 
ATOM   1771 O O   . ARG A 1 243 ? -4.282  51.525  10.276  1.00  71.92  ? 243  ARG A O   1 
ATOM   1772 C CB  . ARG A 1 243 ? -2.602  53.493  12.453  1.00  72.06  ? 243  ARG A CB  1 
ATOM   1773 C CG  . ARG A 1 243 ? -2.388  54.891  13.042  1.00  72.78  ? 243  ARG A CG  1 
ATOM   1774 C CD  . ARG A 1 243 ? -1.760  54.881  14.437  1.00  73.37  ? 243  ARG A CD  1 
ATOM   1775 N NE  . ARG A 1 243 ? -2.646  54.314  15.455  1.00  73.90  ? 243  ARG A NE  1 
ATOM   1776 C CZ  . ARG A 1 243 ? -2.479  53.114  16.010  1.00  74.50  ? 243  ARG A CZ  1 
ATOM   1777 N NH1 . ARG A 1 243 ? -1.455  52.349  15.655  1.00  74.47  ? 243  ARG A NH1 1 
ATOM   1778 N NH2 . ARG A 1 243 ? -3.335  52.675  16.927  1.00  74.61  ? 243  ARG A NH2 1 
ATOM   1779 N N   . VAL A 1 244 ? -2.042  51.452  10.141  1.00  71.98  ? 244  VAL A N   1 
ATOM   1780 C CA  . VAL A 1 244 ? -2.023  50.117  9.541   1.00  72.14  ? 244  VAL A CA  1 
ATOM   1781 C C   . VAL A 1 244 ? -1.094  49.129  10.271  1.00  72.27  ? 244  VAL A C   1 
ATOM   1782 O O   . VAL A 1 244 ? -0.015  49.500  10.744  1.00  72.48  ? 244  VAL A O   1 
ATOM   1783 C CB  . VAL A 1 244 ? -1.719  50.187  8.011   1.00  72.08  ? 244  VAL A CB  1 
ATOM   1784 C CG1 . VAL A 1 244 ? -0.272  50.591  7.749   1.00  72.38  ? 244  VAL A CG1 1 
ATOM   1785 C CG2 . VAL A 1 244 ? -2.063  48.873  7.316   1.00  72.06  ? 244  VAL A CG2 1 
ATOM   1786 N N   . TYR A 1 245 ? -1.539  47.877  10.363  0.90  72.32  ? 245  TYR A N   1 
ATOM   1787 C CA  . TYR A 1 245 ? -0.796  46.813  11.039  0.90  72.37  ? 245  TYR A CA  1 
ATOM   1788 C C   . TYR A 1 245 ? -0.551  45.622  10.105  0.90  72.39  ? 245  TYR A C   1 
ATOM   1789 O O   . TYR A 1 245 ? -1.094  45.573  9.000   0.90  72.33  ? 245  TYR A O   1 
ATOM   1790 C CB  . TYR A 1 245 ? -1.555  46.360  12.290  0.90  72.37  ? 245  TYR A CB  1 
ATOM   1791 C CG  . TYR A 1 245 ? -1.450  47.307  13.468  0.90  72.28  ? 245  TYR A CG  1 
ATOM   1792 C CD1 . TYR A 1 245 ? -2.242  48.455  13.543  0.90  72.37  ? 245  TYR A CD1 1 
ATOM   1793 C CD2 . TYR A 1 245 ? -0.571  47.046  14.518  0.90  71.96  ? 245  TYR A CD2 1 
ATOM   1794 C CE1 . TYR A 1 245 ? -2.150  49.322  14.628  0.90  71.95  ? 245  TYR A CE1 1 
ATOM   1795 C CE2 . TYR A 1 245 ? -0.473  47.906  15.603  0.90  71.60  ? 245  TYR A CE2 1 
ATOM   1796 C CZ  . TYR A 1 245 ? -1.262  49.039  15.650  0.90  71.76  ? 245  TYR A CZ  1 
ATOM   1797 O OH  . TYR A 1 245 ? -1.160  49.887  16.725  0.90  72.83  ? 245  TYR A OH  1 
ATOM   1798 N N   . ALA A 1 246 ? 0.270   44.671  10.549  1.00  72.50  ? 246  ALA A N   1 
ATOM   1799 C CA  . ALA A 1 246 ? 0.571   43.467  9.767   1.00  72.77  ? 246  ALA A CA  1 
ATOM   1800 C C   . ALA A 1 246 ? 0.727   42.212  10.630  1.00  72.92  ? 246  ALA A C   1 
ATOM   1801 O O   . ALA A 1 246 ? 1.766   42.006  11.261  1.00  72.93  ? 246  ALA A O   1 
ATOM   1802 C CB  . ALA A 1 246 ? 1.815   43.681  8.909   1.00  72.70  ? 246  ALA A CB  1 
ATOM   1803 N N   . ILE A 1 247 ? -0.308  41.375  10.644  1.00  73.21  ? 247  ILE A N   1 
ATOM   1804 C CA  . ILE A 1 247 ? -0.262  40.104  11.371  1.00  73.61  ? 247  ILE A CA  1 
ATOM   1805 C C   . ILE A 1 247 ? 0.023   38.929  10.434  1.00  73.90  ? 247  ILE A C   1 
ATOM   1806 O O   . ILE A 1 247 ? -0.765  38.613  9.539   1.00  73.77  ? 247  ILE A O   1 
ATOM   1807 C CB  . ILE A 1 247 ? -1.544  39.839  12.184  1.00  73.49  ? 247  ILE A CB  1 
ATOM   1808 C CG1 . ILE A 1 247 ? -1.803  40.996  13.153  1.00  73.40  ? 247  ILE A CG1 1 
ATOM   1809 C CG2 . ILE A 1 247 ? -1.429  38.503  12.931  1.00  73.66  ? 247  ILE A CG2 1 
ATOM   1810 C CD1 . ILE A 1 247 ? -3.127  40.922  13.870  1.00  73.35  ? 247  ILE A CD1 1 
ATOM   1811 N N   . LEU A 1 248 ? 1.162   38.288  10.664  1.00  74.40  ? 248  LEU A N   1 
ATOM   1812 C CA  . LEU A 1 248 ? 1.633   37.193  9.832   1.00  74.98  ? 248  LEU A CA  1 
ATOM   1813 C C   . LEU A 1 248 ? 2.108   36.050  10.717  1.00  75.43  ? 248  LEU A C   1 
ATOM   1814 O O   . LEU A 1 248 ? 3.231   36.084  11.226  1.00  75.52  ? 248  LEU A O   1 
ATOM   1815 C CB  . LEU A 1 248 ? 2.787   37.670  8.949   1.00  74.86  ? 248  LEU A CB  1 
ATOM   1816 C CG  . LEU A 1 248 ? 2.452   38.646  7.824   1.00  75.09  ? 248  LEU A CG  1 
ATOM   1817 C CD1 . LEU A 1 248 ? 3.666   39.491  7.502   1.00  75.30  ? 248  LEU A CD1 1 
ATOM   1818 C CD2 . LEU A 1 248 ? 1.946   37.906  6.584   1.00  75.58  ? 248  LEU A CD2 1 
ATOM   1819 N N   . THR A 1 249 ? 1.255   35.045  10.906  1.00  75.91  ? 249  THR A N   1 
ATOM   1820 C CA  . THR A 1 249 ? 1.592   33.912  11.771  1.00  76.62  ? 249  THR A CA  1 
ATOM   1821 C C   . THR A 1 249 ? 2.977   33.336  11.448  1.00  77.18  ? 249  THR A C   1 
ATOM   1822 O O   . THR A 1 249 ? 3.876   33.348  12.294  1.00  77.27  ? 249  THR A O   1 
ATOM   1823 C CB  . THR A 1 249 ? 0.492   32.808  11.777  1.00  76.57  ? 249  THR A CB  1 
ATOM   1824 O OG1 . THR A 1 249 ? 1.099   31.506  11.830  1.00  76.07  ? 249  THR A OG1 1 
ATOM   1825 C CG2 . THR A 1 249 ? -0.392  32.909  10.543  1.00  76.82  ? 249  THR A CG2 1 
ATOM   1826 N N   . HIS A 1 250 ? 3.150   32.859  10.221  1.00  77.76  ? 250  HIS A N   1 
ATOM   1827 C CA  . HIS A 1 250 ? 4.430   32.319  9.795   1.00  78.25  ? 250  HIS A CA  1 
ATOM   1828 C C   . HIS A 1 250 ? 5.224   33.406  9.084   1.00  78.55  ? 250  HIS A C   1 
ATOM   1829 O O   . HIS A 1 250 ? 4.848   33.851  7.995   1.00  78.74  ? 250  HIS A O   1 
ATOM   1830 C CB  . HIS A 1 250 ? 4.213   31.098  8.905   1.00  78.43  ? 250  HIS A CB  1 
ATOM   1831 C CG  . HIS A 1 250 ? 3.280   30.089  9.498   1.00  78.89  ? 250  HIS A CG  1 
ATOM   1832 N ND1 . HIS A 1 250 ? 3.647   29.256  10.533  1.00  79.06  ? 250  HIS A ND1 1 
ATOM   1833 C CD2 . HIS A 1 250 ? 1.989   29.791  9.215   1.00  79.40  ? 250  HIS A CD2 1 
ATOM   1834 C CE1 . HIS A 1 250 ? 2.625   28.484  10.857  1.00  79.34  ? 250  HIS A CE1 1 
ATOM   1835 N NE2 . HIS A 1 250 ? 1.607   28.786  10.071  1.00  79.37  ? 250  HIS A NE2 1 
ATOM   1836 N N   . GLY A 1 251 ? 6.304   33.848  9.724   1.00  78.79  ? 251  GLY A N   1 
ATOM   1837 C CA  . GLY A 1 251 ? 7.141   34.924  9.198   1.00  79.08  ? 251  GLY A CA  1 
ATOM   1838 C C   . GLY A 1 251 ? 8.403   34.418  8.525   1.00  79.46  ? 251  GLY A C   1 
ATOM   1839 O O   . GLY A 1 251 ? 9.424   34.193  9.186   1.00  79.48  ? 251  GLY A O   1 
ATOM   1840 N N   . ILE A 1 252 ? 8.330   34.247  7.206   1.00  79.70  ? 252  ILE A N   1 
ATOM   1841 C CA  . ILE A 1 252 ? 9.450   33.735  6.413   1.00  79.95  ? 252  ILE A CA  1 
ATOM   1842 C C   . ILE A 1 252 ? 10.493  34.833  6.169   1.00  80.14  ? 252  ILE A C   1 
ATOM   1843 O O   . ILE A 1 252 ? 11.687  34.624  6.398   1.00  80.13  ? 252  ILE A O   1 
ATOM   1844 C CB  . ILE A 1 252 ? 8.965   33.124  5.073   1.00  80.08  ? 252  ILE A CB  1 
ATOM   1845 C CG1 . ILE A 1 252 ? 7.585   32.467  5.252   1.00  80.09  ? 252  ILE A CG1 1 
ATOM   1846 C CG2 . ILE A 1 252 ? 9.994   32.117  4.545   1.00  79.88  ? 252  ILE A CG2 1 
ATOM   1847 C CD1 . ILE A 1 252 ? 6.745   32.416  3.991   1.00  79.79  ? 252  ILE A CD1 1 
ATOM   1848 N N   . PHE A 1 253 ? 10.026  35.990  5.695   0.010 80.41  ? 253  PHE A N   1 
ATOM   1849 C CA  . PHE A 1 253 ? 10.810  37.238  5.616   0.010 80.69  ? 253  PHE A CA  1 
ATOM   1850 C C   . PHE A 1 253 ? 12.218  37.147  5.017   0.010 80.94  ? 253  PHE A C   1 
ATOM   1851 O O   . PHE A 1 253 ? 13.195  37.527  5.669   0.010 80.96  ? 253  PHE A O   1 
ATOM   1852 C CB  . PHE A 1 253 ? 10.900  37.897  6.996   0.010 80.66  ? 253  PHE A CB  1 
ATOM   1853 C CG  . PHE A 1 253 ? 9.576   38.318  7.556   0.010 80.62  ? 253  PHE A CG  1 
ATOM   1854 C CD1 . PHE A 1 253 ? 9.274   38.096  8.887   0.010 80.58  ? 253  PHE A CD1 1 
ATOM   1855 C CD2 . PHE A 1 253 ? 8.630   38.930  6.751   0.010 80.58  ? 253  PHE A CD2 1 
ATOM   1856 C CE1 . PHE A 1 253 ? 8.059   38.483  9.407   0.010 80.56  ? 253  PHE A CE1 1 
ATOM   1857 C CE2 . PHE A 1 253 ? 7.410   39.316  7.267   0.010 80.56  ? 253  PHE A CE2 1 
ATOM   1858 C CZ  . PHE A 1 253 ? 7.125   39.092  8.597   0.010 80.55  ? 253  PHE A CZ  1 
ATOM   1859 N N   . SER A 1 254 ? 12.316  36.664  3.782   1.00  81.30  ? 254  SER A N   1 
ATOM   1860 C CA  . SER A 1 254 ? 13.608  36.540  3.098   1.00  81.62  ? 254  SER A CA  1 
ATOM   1861 C C   . SER A 1 254 ? 13.791  37.596  2.010   1.00  81.80  ? 254  SER A C   1 
ATOM   1862 O O   . SER A 1 254 ? 12.826  38.238  1.588   1.00  81.96  ? 254  SER A O   1 
ATOM   1863 C CB  . SER A 1 254 ? 13.752  35.144  2.488   1.00  81.61  ? 254  SER A CB  1 
ATOM   1864 O OG  . SER A 1 254 ? 12.736  34.911  1.527   1.00  82.03  ? 254  SER A OG  1 
ATOM   1865 N N   . GLY A 1 255 ? 15.034  37.765  1.562   0.010 81.97  ? 255  GLY A N   1 
ATOM   1866 C CA  . GLY A 1 255 ? 15.358  38.654  0.448   0.010 82.19  ? 255  GLY A CA  1 
ATOM   1867 C C   . GLY A 1 255 ? 14.988  40.077  0.824   0.010 82.38  ? 255  GLY A C   1 
ATOM   1868 O O   . GLY A 1 255 ? 15.308  40.529  1.925   0.010 82.36  ? 255  GLY A O   1 
ATOM   1869 N N   . PRO A 1 256 ? 14.308  40.795  -0.092  1.00  82.56  ? 256  PRO A N   1 
ATOM   1870 C CA  . PRO A 1 256 ? 13.946  42.191  0.148   1.00  82.78  ? 256  PRO A CA  1 
ATOM   1871 C C   . PRO A 1 256 ? 12.944  42.507  1.262   1.00  82.95  ? 256  PRO A C   1 
ATOM   1872 O O   . PRO A 1 256 ? 12.809  43.670  1.650   1.00  82.92  ? 256  PRO A O   1 
ATOM   1873 C CB  . PRO A 1 256 ? 13.374  42.605  -1.219  1.00  82.78  ? 256  PRO A CB  1 
ATOM   1874 C CG  . PRO A 1 256 ? 13.270  41.334  -2.043  1.00  82.63  ? 256  PRO A CG  1 
ATOM   1875 C CD  . PRO A 1 256 ? 13.399  40.190  -1.102  1.00  82.57  ? 256  PRO A CD  1 
ATOM   1876 N N   . ALA A 1 257 ? 12.268  41.479  1.774   1.00  83.18  ? 257  ALA A N   1 
ATOM   1877 C CA  . ALA A 1 257 ? 11.180  41.647  2.743   1.00  83.43  ? 257  ALA A CA  1 
ATOM   1878 C C   . ALA A 1 257 ? 11.537  42.554  3.923   1.00  83.57  ? 257  ALA A C   1 
ATOM   1879 O O   . ALA A 1 257 ? 10.856  43.552  4.168   1.00  83.75  ? 257  ALA A O   1 
ATOM   1880 C CB  . ALA A 1 257 ? 10.691  40.286  3.239   1.00  83.42  ? 257  ALA A CB  1 
ATOM   1881 N N   . ILE A 1 258 ? 12.612  42.209  4.631   1.00  83.62  ? 258  ILE A N   1 
ATOM   1882 C CA  . ILE A 1 258 ? 13.038  42.913  5.846   1.00  83.71  ? 258  ILE A CA  1 
ATOM   1883 C C   . ILE A 1 258 ? 13.093  44.436  5.689   1.00  83.74  ? 258  ILE A C   1 
ATOM   1884 O O   . ILE A 1 258 ? 12.525  45.171  6.506   1.00  83.91  ? 258  ILE A O   1 
ATOM   1885 C CB  . ILE A 1 258 ? 14.411  42.372  6.350   1.00  83.78  ? 258  ILE A CB  1 
ATOM   1886 C CG1 . ILE A 1 258 ? 14.323  40.868  6.666   1.00  83.59  ? 258  ILE A CG1 1 
ATOM   1887 C CG2 . ILE A 1 258 ? 14.942  43.193  7.545   1.00  84.11  ? 258  ILE A CG2 1 
ATOM   1888 C CD1 . ILE A 1 258 ? 13.287  40.489  7.730   1.00  83.48  ? 258  ILE A CD1 1 
ATOM   1889 N N   . SER A 1 259 ? 13.773  44.893  4.638   1.00  83.70  ? 259  SER A N   1 
ATOM   1890 C CA  . SER A 1 259 ? 13.916  46.320  4.342   1.00  83.63  ? 259  SER A CA  1 
ATOM   1891 C C   . SER A 1 259 ? 12.604  46.937  3.865   1.00  83.66  ? 259  SER A C   1 
ATOM   1892 O O   . SER A 1 259 ? 12.327  48.111  4.135   1.00  83.72  ? 259  SER A O   1 
ATOM   1893 C CB  . SER A 1 259 ? 15.010  46.541  3.293   1.00  83.64  ? 259  SER A CB  1 
ATOM   1894 O OG  . SER A 1 259 ? 14.656  45.956  2.049   1.00  83.12  ? 259  SER A OG  1 
ATOM   1895 N N   . ARG A 1 260 ? 11.810  46.133  3.156   1.00  83.60  ? 260  ARG A N   1 
ATOM   1896 C CA  . ARG A 1 260 ? 10.504  46.546  2.635   1.00  83.52  ? 260  ARG A CA  1 
ATOM   1897 C C   . ARG A 1 260 ? 9.517   46.877  3.755   1.00  83.48  ? 260  ARG A C   1 
ATOM   1898 O O   . ARG A 1 260 ? 8.627   47.714  3.580   1.00  83.36  ? 260  ARG A O   1 
ATOM   1899 C CB  . ARG A 1 260 ? 9.924   45.450  1.740   1.00  83.49  ? 260  ARG A CB  1 
ATOM   1900 C CG  . ARG A 1 260 ? 10.448  45.447  0.317   1.00  83.79  ? 260  ARG A CG  1 
ATOM   1901 C CD  . ARG A 1 260 ? 10.093  44.151  -0.395  1.00  83.94  ? 260  ARG A CD  1 
ATOM   1902 N NE  . ARG A 1 260 ? 10.226  44.275  -1.845  1.00  84.24  ? 260  ARG A NE  1 
ATOM   1903 C CZ  . ARG A 1 260 ? 10.133  43.262  -2.704  1.00  84.89  ? 260  ARG A CZ  1 
ATOM   1904 N NH1 . ARG A 1 260 ? 9.916   42.028  -2.267  1.00  85.02  ? 260  ARG A NH1 1 
ATOM   1905 N NH2 . ARG A 1 260 ? 10.263  43.480  -4.009  1.00  84.99  ? 260  ARG A NH2 1 
ATOM   1906 N N   . ILE A 1 261 ? 9.688   46.216  4.898   1.00  83.37  ? 261  ILE A N   1 
ATOM   1907 C CA  . ILE A 1 261 ? 8.821   46.408  6.060   1.00  83.32  ? 261  ILE A CA  1 
ATOM   1908 C C   . ILE A 1 261 ? 9.122   47.721  6.790   1.00  83.28  ? 261  ILE A C   1 
ATOM   1909 O O   . ILE A 1 261 ? 8.207   48.375  7.300   1.00  83.30  ? 261  ILE A O   1 
ATOM   1910 C CB  . ILE A 1 261 ? 8.913   45.207  7.036   1.00  83.27  ? 261  ILE A CB  1 
ATOM   1911 C CG1 . ILE A 1 261 ? 8.454   43.919  6.340   1.00  83.20  ? 261  ILE A CG1 1 
ATOM   1912 C CG2 . ILE A 1 261 ? 8.069   45.449  8.276   1.00  83.31  ? 261  ILE A CG2 1 
ATOM   1913 C CD1 . ILE A 1 261 ? 8.942   42.644  7.004   1.00  82.96  ? 261  ILE A CD1 1 
ATOM   1914 N N   . ASN A 1 262 ? 10.397  48.107  6.830   1.00  83.23  ? 262  ASN A N   1 
ATOM   1915 C CA  . ASN A 1 262 ? 10.810  49.344  7.508   1.00  83.09  ? 262  ASN A CA  1 
ATOM   1916 C C   . ASN A 1 262 ? 10.490  50.602  6.710   1.00  82.88  ? 262  ASN A C   1 
ATOM   1917 O O   . ASN A 1 262 ? 10.051  51.602  7.281   1.00  82.98  ? 262  ASN A O   1 
ATOM   1918 C CB  . ASN A 1 262 ? 12.291  49.299  7.886   1.00  83.15  ? 262  ASN A CB  1 
ATOM   1919 C CG  . ASN A 1 262 ? 12.564  48.367  9.053   1.00  83.31  ? 262  ASN A CG  1 
ATOM   1920 O OD1 . ASN A 1 262 ? 12.098  48.597  10.173  1.00  83.09  ? 262  ASN A OD1 1 
ATOM   1921 N ND2 . ASN A 1 262 ? 13.329  47.311  8.797   1.00  83.63  ? 262  ASN A ND2 1 
ATOM   1922 N N   . ASN A 1 263 ? 10.715  50.545  5.397   1.00  82.60  ? 263  ASN A N   1 
ATOM   1923 C CA  . ASN A 1 263 ? 10.249  51.581  4.474   1.00  82.23  ? 263  ASN A CA  1 
ATOM   1924 C C   . ASN A 1 263 ? 8.725   51.601  4.372   1.00  81.97  ? 263  ASN A C   1 
ATOM   1925 O O   . ASN A 1 263 ? 8.138   52.573  3.886   1.00  81.99  ? 263  ASN A O   1 
ATOM   1926 C CB  . ASN A 1 263 ? 10.872  51.394  3.087   1.00  82.38  ? 263  ASN A CB  1 
ATOM   1927 C CG  . ASN A 1 263 ? 11.881  52.475  2.747   1.00  82.42  ? 263  ASN A CG  1 
ATOM   1928 O OD1 . ASN A 1 263 ? 11.524  53.642  2.577   1.00  82.84  ? 263  ASN A OD1 1 
ATOM   1929 N ND2 . ASN A 1 263 ? 13.149  52.088  2.632   1.00  82.47  ? 263  ASN A ND2 1 
ATOM   1930 N N   . ALA A 1 264 ? 8.096   50.518  4.827   1.00  81.57  ? 264  ALA A N   1 
ATOM   1931 C CA  . ALA A 1 264 ? 6.645   50.458  4.946   1.00  81.11  ? 264  ALA A CA  1 
ATOM   1932 C C   . ALA A 1 264 ? 6.193   51.222  6.184   1.00  80.75  ? 264  ALA A C   1 
ATOM   1933 O O   . ALA A 1 264 ? 6.993   51.510  7.081   1.00  80.50  ? 264  ALA A O   1 
ATOM   1934 C CB  . ALA A 1 264 ? 6.155   49.013  4.982   1.00  81.22  ? 264  ALA A CB  1 
ATOM   1935 N N   . CYS A 1 265 ? 4.900   51.521  6.223   1.00  80.43  ? 265  CYS A N   1 
ATOM   1936 C CA  . CYS A 1 265 ? 4.334   52.495  7.155   1.00  80.25  ? 265  CYS A CA  1 
ATOM   1937 C C   . CYS A 1 265 ? 3.796   51.897  8.456   1.00  79.83  ? 265  CYS A C   1 
ATOM   1938 O O   . CYS A 1 265 ? 3.381   52.638  9.358   1.00  79.85  ? 265  CYS A O   1 
ATOM   1939 C CB  . CYS A 1 265 ? 3.243   53.297  6.438   1.00  80.21  ? 265  CYS A CB  1 
ATOM   1940 S SG  . CYS A 1 265 ? 2.538   52.423  5.004   1.00  81.27  ? 265  CYS A SG  1 
ATOM   1941 N N   . PHE A 1 266 ? 3.831   50.565  8.550   1.00  79.21  ? 266  PHE A N   1 
ATOM   1942 C CA  . PHE A 1 266 ? 3.267   49.825  9.685   1.00  78.58  ? 266  PHE A CA  1 
ATOM   1943 C C   . PHE A 1 266 ? 3.655   50.384  11.056  1.00  78.31  ? 266  PHE A C   1 
ATOM   1944 O O   . PHE A 1 266 ? 4.811   50.750  11.283  1.00  78.34  ? 266  PHE A O   1 
ATOM   1945 C CB  . PHE A 1 266 ? 3.673   48.347  9.619   1.00  78.52  ? 266  PHE A CB  1 
ATOM   1946 C CG  . PHE A 1 266 ? 3.189   47.624  8.388   1.00  77.91  ? 266  PHE A CG  1 
ATOM   1947 C CD1 . PHE A 1 266 ? 4.097   47.155  7.445   1.00  76.98  ? 266  PHE A CD1 1 
ATOM   1948 C CD2 . PHE A 1 266 ? 1.831   47.397  8.181   1.00  77.29  ? 266  PHE A CD2 1 
ATOM   1949 C CE1 . PHE A 1 266 ? 3.663   46.480  6.312   1.00  76.78  ? 266  PHE A CE1 1 
ATOM   1950 C CE2 . PHE A 1 266 ? 1.388   46.726  7.043   1.00  77.05  ? 266  PHE A CE2 1 
ATOM   1951 C CZ  . PHE A 1 266 ? 2.306   46.263  6.112   1.00  76.62  ? 266  PHE A CZ  1 
ATOM   1952 N N   . GLU A 1 267 ? 2.675   50.454  11.956  1.00  77.88  ? 267  GLU A N   1 
ATOM   1953 C CA  . GLU A 1 267 ? 2.924   50.805  13.352  1.00  77.74  ? 267  GLU A CA  1 
ATOM   1954 C C   . GLU A 1 267 ? 3.531   49.601  14.078  1.00  77.44  ? 267  GLU A C   1 
ATOM   1955 O O   . GLU A 1 267 ? 4.377   49.753  14.964  1.00  77.60  ? 267  GLU A O   1 
ATOM   1956 C CB  . GLU A 1 267 ? 1.624   51.260  14.036  1.00  77.79  ? 267  GLU A CB  1 
ATOM   1957 C CG  . GLU A 1 267 ? 1.760   51.628  15.525  1.00  78.18  ? 267  GLU A CG  1 
ATOM   1958 C CD  . GLU A 1 267 ? 2.370   53.009  15.777  1.00  78.84  ? 267  GLU A CD  1 
ATOM   1959 O OE1 . GLU A 1 267 ? 2.662   53.746  14.799  1.00  78.23  ? 267  GLU A OE1 1 
ATOM   1960 O OE2 . GLU A 1 267 ? 2.550   53.356  16.971  1.00  78.92  ? 267  GLU A OE2 1 
ATOM   1961 N N   . ALA A 1 268 ? 3.082   48.409  13.693  1.00  76.95  ? 268  ALA A N   1 
ATOM   1962 C CA  . ALA A 1 268 ? 3.611   47.161  14.224  1.00  76.40  ? 268  ALA A CA  1 
ATOM   1963 C C   . ALA A 1 268 ? 3.426   46.022  13.223  1.00  75.97  ? 268  ALA A C   1 
ATOM   1964 O O   . ALA A 1 268 ? 2.474   46.019  12.436  1.00  75.83  ? 268  ALA A O   1 
ATOM   1965 C CB  . ALA A 1 268 ? 2.947   46.822  15.557  1.00  76.47  ? 268  ALA A CB  1 
ATOM   1966 N N   . VAL A 1 269 ? 4.356   45.070  13.252  1.00  75.49  ? 269  VAL A N   1 
ATOM   1967 C CA  . VAL A 1 269 ? 4.280   43.861  12.433  1.00  75.03  ? 269  VAL A CA  1 
ATOM   1968 C C   . VAL A 1 269 ? 4.414   42.639  13.338  1.00  74.74  ? 269  VAL A C   1 
ATOM   1969 O O   . VAL A 1 269 ? 5.516   42.270  13.744  1.00  74.81  ? 269  VAL A O   1 
ATOM   1970 C CB  . VAL A 1 269 ? 5.361   43.839  11.323  1.00  75.05  ? 269  VAL A CB  1 
ATOM   1971 C CG1 . VAL A 1 269 ? 5.383   42.486  10.597  1.00  75.28  ? 269  VAL A CG1 1 
ATOM   1972 C CG2 . VAL A 1 269 ? 5.127   44.967  10.328  1.00  74.95  ? 269  VAL A CG2 1 
ATOM   1973 N N   . VAL A 1 270 ? 3.281   42.028  13.661  1.00  74.40  ? 270  VAL A N   1 
ATOM   1974 C CA  . VAL A 1 270 ? 3.251   40.887  14.574  1.00  74.06  ? 270  VAL A CA  1 
ATOM   1975 C C   . VAL A 1 270 ? 3.551   39.594  13.833  1.00  73.82  ? 270  VAL A C   1 
ATOM   1976 O O   . VAL A 1 270 ? 3.211   39.444  12.655  1.00  73.82  ? 270  VAL A O   1 
ATOM   1977 C CB  . VAL A 1 270 ? 1.886   40.752  15.290  1.00  74.04  ? 270  VAL A CB  1 
ATOM   1978 C CG1 . VAL A 1 270 ? 2.059   40.104  16.655  1.00  73.96  ? 270  VAL A CG1 1 
ATOM   1979 C CG2 . VAL A 1 270 ? 1.239   42.107  15.449  1.00  74.37  ? 270  VAL A CG2 1 
ATOM   1980 N N   . VAL A 1 271 ? 4.208   38.676  14.533  1.00  73.52  ? 271  VAL A N   1 
ATOM   1981 C CA  . VAL A 1 271 ? 4.465   37.329  14.027  1.00  73.38  ? 271  VAL A CA  1 
ATOM   1982 C C   . VAL A 1 271 ? 4.343   36.319  15.158  1.00  73.24  ? 271  VAL A C   1 
ATOM   1983 O O   . VAL A 1 271 ? 4.089   36.685  16.309  1.00  73.11  ? 271  VAL A O   1 
ATOM   1984 C CB  . VAL A 1 271 ? 5.872   37.187  13.375  1.00  73.27  ? 271  VAL A CB  1 
ATOM   1985 C CG1 . VAL A 1 271 ? 5.891   37.762  11.974  1.00  73.24  ? 271  VAL A CG1 1 
ATOM   1986 C CG2 . VAL A 1 271 ? 6.942   37.832  14.237  1.00  73.51  ? 271  VAL A CG2 1 
ATOM   1987 N N   . THR A 1 272 ? 4.508   35.048  14.813  1.00  73.25  ? 272  THR A N   1 
ATOM   1988 C CA  . THR A 1 272 ? 4.673   33.992  15.800  1.00  73.39  ? 272  THR A CA  1 
ATOM   1989 C C   . THR A 1 272 ? 6.030   33.354  15.554  1.00  73.53  ? 272  THR A C   1 
ATOM   1990 O O   . THR A 1 272 ? 6.492   33.296  14.410  1.00  73.44  ? 272  THR A O   1 
ATOM   1991 C CB  . THR A 1 272 ? 3.579   32.916  15.694  1.00  73.39  ? 272  THR A CB  1 
ATOM   1992 O OG1 . THR A 1 272 ? 3.577   32.370  14.368  1.00  72.67  ? 272  THR A OG1 1 
ATOM   1993 C CG2 . THR A 1 272 ? 2.202   33.498  16.018  1.00  73.12  ? 272  THR A CG2 1 
ATOM   1994 N N   . ASN A 1 273 ? 6.667   32.876  16.622  1.00  73.73  ? 273  ASN A N   1 
ATOM   1995 C CA  . ASN A 1 273 ? 8.009   32.305  16.509  1.00  73.87  ? 273  ASN A CA  1 
ATOM   1996 C C   . ASN A 1 273 ? 8.022   30.866  15.973  1.00  73.96  ? 273  ASN A C   1 
ATOM   1997 O O   . ASN A 1 273 ? 8.765   30.005  16.454  1.00  74.09  ? 273  ASN A O   1 
ATOM   1998 C CB  . ASN A 1 273 ? 8.826   32.483  17.806  1.00  73.84  ? 273  ASN A CB  1 
ATOM   1999 C CG  . ASN A 1 273 ? 8.244   31.735  18.993  1.00  74.11  ? 273  ASN A CG  1 
ATOM   2000 O OD1 . ASN A 1 273 ? 8.979   31.100  19.750  1.00  74.36  ? 273  ASN A OD1 1 
ATOM   2001 N ND2 . ASN A 1 273 ? 6.932   31.819  19.176  1.00  74.86  ? 273  ASN A ND2 1 
ATOM   2002 N N   . THR A 1 274 ? 7.190   30.628  14.958  1.00  74.03  ? 274  THR A N   1 
ATOM   2003 C CA  . THR A 1 274 ? 7.242   29.410  14.153  1.00  74.05  ? 274  THR A CA  1 
ATOM   2004 C C   . THR A 1 274 ? 8.510   29.434  13.300  1.00  74.13  ? 274  THR A C   1 
ATOM   2005 O O   . THR A 1 274 ? 9.058   28.381  12.946  1.00  74.23  ? 274  THR A O   1 
ATOM   2006 C CB  . THR A 1 274 ? 6.009   29.283  13.223  1.00  74.10  ? 274  THR A CB  1 
ATOM   2007 O OG1 . THR A 1 274 ? 5.941   30.425  12.360  1.00  74.28  ? 274  THR A OG1 1 
ATOM   2008 C CG2 . THR A 1 274 ? 4.717   29.186  14.029  1.00  73.97  ? 274  THR A CG2 1 
ATOM   2009 N N   . ILE A 1 275 ? 8.947   30.650  12.963  1.00  74.03  ? 275  ILE A N   1 
ATOM   2010 C CA  . ILE A 1 275 ? 10.215  30.905  12.283  1.00  73.87  ? 275  ILE A CA  1 
ATOM   2011 C C   . ILE A 1 275 ? 10.930  32.017  13.061  1.00  73.68  ? 275  ILE A C   1 
ATOM   2012 O O   . ILE A 1 275 ? 10.411  33.135  13.150  1.00  73.72  ? 275  ILE A O   1 
ATOM   2013 C CB  . ILE A 1 275 ? 10.005  31.328  10.790  1.00  74.05  ? 275  ILE A CB  1 
ATOM   2014 C CG1 . ILE A 1 275 ? 9.174   30.281  10.030  1.00  73.74  ? 275  ILE A CG1 1 
ATOM   2015 C CG2 . ILE A 1 275 ? 11.359  31.581  10.092  1.00  74.19  ? 275  ILE A CG2 1 
ATOM   2016 C CD1 . ILE A 1 275 ? 8.594   30.771  8.715   1.00  73.69  ? 275  ILE A CD1 1 
ATOM   2017 N N   . PRO A 1 276 ? 12.118  31.712  13.632  1.00  73.61  ? 276  PRO A N   1 
ATOM   2018 C CA  . PRO A 1 276 ? 12.899  32.606  14.526  1.00  73.43  ? 276  PRO A CA  1 
ATOM   2019 C C   . PRO A 1 276 ? 13.210  34.012  13.984  1.00  73.20  ? 276  PRO A C   1 
ATOM   2020 O O   . PRO A 1 276 ? 13.934  34.157  12.988  1.00  73.17  ? 276  PRO A O   1 
ATOM   2021 C CB  . PRO A 1 276 ? 14.213  31.838  14.734  1.00  73.37  ? 276  PRO A CB  1 
ATOM   2022 C CG  . PRO A 1 276 ? 13.863  30.430  14.515  1.00  73.22  ? 276  PRO A CG  1 
ATOM   2023 C CD  . PRO A 1 276 ? 12.778  30.400  13.474  1.00  73.54  ? 276  PRO A CD  1 
ATOM   2024 N N   . GLN A 1 277 ? 12.683  35.028  14.671  0.010 72.98  ? 277  GLN A N   1 
ATOM   2025 C CA  . GLN A 1 277 ? 12.854  36.424  14.264  0.010 72.75  ? 277  GLN A CA  1 
ATOM   2026 C C   . GLN A 1 277 ? 14.001  37.112  14.990  0.010 72.61  ? 277  GLN A C   1 
ATOM   2027 O O   . GLN A 1 277 ? 14.314  38.270  14.718  0.010 72.59  ? 277  GLN A O   1 
ATOM   2028 C CB  . GLN A 1 277 ? 11.561  37.194  14.510  0.010 72.76  ? 277  GLN A CB  1 
ATOM   2029 C CG  . GLN A 1 277 ? 10.340  36.510  13.938  0.010 72.73  ? 277  GLN A CG  1 
ATOM   2030 C CD  . GLN A 1 277 ? 10.444  36.309  12.441  0.010 72.71  ? 277  GLN A CD  1 
ATOM   2031 O OE1 . GLN A 1 277 ? 11.434  36.696  11.820  0.010 72.72  ? 277  GLN A OE1 1 
ATOM   2032 N NE2 . GLN A 1 277 ? 9.420   35.704  11.852  0.010 72.70  ? 277  GLN A NE2 1 
ATOM   2033 N N   . GLU A 1 278 ? 14.623  36.398  15.917  0.010 72.43  ? 278  GLU A N   1 
ATOM   2034 C CA  . GLU A 1 278 ? 15.701  36.982  16.683  0.010 72.26  ? 278  GLU A CA  1 
ATOM   2035 C C   . GLU A 1 278 ? 16.665  37.782  15.779  0.010 72.16  ? 278  GLU A C   1 
ATOM   2036 O O   . GLU A 1 278 ? 16.839  38.991  16.024  0.010 72.14  ? 278  GLU A O   1 
ATOM   2037 C CB  . GLU A 1 278 ? 16.418  35.910  17.523  0.010 72.26  ? 278  GLU A CB  1 
ATOM   2038 C CG  . GLU A 1 278 ? 15.542  35.346  18.653  0.010 72.23  ? 278  GLU A CG  1 
ATOM   2039 C CD  . GLU A 1 278 ? 14.198  34.841  18.142  0.010 72.21  ? 278  GLU A CD  1 
ATOM   2040 O OE1 . GLU A 1 278 ? 13.351  34.439  18.967  0.010 72.20  ? 278  GLU A OE1 1 
ATOM   2041 O OE2 . GLU A 1 278 ? 13.992  34.849  16.909  0.010 72.20  ? 278  GLU A OE2 1 
ATOM   2042 N N   . ASP A 1 279 ? 17.274  37.183  14.765  0.010 72.03  ? 279  ASP A N   1 
ATOM   2043 C CA  . ASP A 1 279 ? 18.262  37.968  14.032  0.010 71.92  ? 279  ASP A CA  1 
ATOM   2044 C C   . ASP A 1 279 ? 17.658  39.180  13.276  0.010 71.87  ? 279  ASP A C   1 
ATOM   2045 O O   . ASP A 1 279 ? 18.335  40.231  13.082  0.010 71.85  ? 279  ASP A O   1 
ATOM   2046 C CB  . ASP A 1 279 ? 19.179  37.053  13.089  0.010 71.92  ? 279  ASP A CB  1 
ATOM   2047 C CG  . ASP A 1 279 ? 20.331  37.915  12.532  0.010 71.90  ? 279  ASP A CG  1 
ATOM   2048 O OD1 . ASP A 1 279 ? 20.933  37.506  11.504  0.010 71.88  ? 279  ASP A OD1 1 
ATOM   2049 O OD2 . ASP A 1 279 ? 20.630  38.994  13.109  0.010 71.89  ? 279  ASP A OD2 1 
ATOM   2050 N N   . LYS A 1 280 ? 16.365  39.034  12.908  0.010 71.81  ? 280  LYS A N   1 
ATOM   2051 C CA  . LYS A 1 280 ? 15.654  40.116  12.168  0.010 71.77  ? 280  LYS A CA  1 
ATOM   2052 C C   . LYS A 1 280 ? 14.927  41.184  13.010  0.010 71.77  ? 280  LYS A C   1 
ATOM   2053 O O   . LYS A 1 280 ? 14.710  42.298  12.524  0.010 71.76  ? 280  LYS A O   1 
ATOM   2054 C CB  . LYS A 1 280 ? 14.645  39.509  11.190  0.010 71.75  ? 280  LYS A CB  1 
ATOM   2055 C CG  . LYS A 1 280 ? 15.185  38.369  10.342  0.010 71.72  ? 280  LYS A CG  1 
ATOM   2056 C CD  . LYS A 1 280 ? 16.151  38.862  9.274   0.010 71.68  ? 280  LYS A CD  1 
ATOM   2057 C CE  . LYS A 1 280 ? 16.311  37.830  8.164   0.010 71.66  ? 280  LYS A CE  1 
ATOM   2058 N NZ  . LYS A 1 280 ? 16.996  38.392  6.956   0.010 71.65  ? 280  LYS A NZ  1 
ATOM   2059 N N   . MET A 1 281 ? 14.515  40.844  14.228  1.00  71.81  ? 281  MET A N   1 
ATOM   2060 C CA  . MET A 1 281 ? 13.952  41.850  15.142  1.00  71.78  ? 281  MET A CA  1 
ATOM   2061 C C   . MET A 1 281 ? 14.985  42.966  15.321  1.00  71.31  ? 281  MET A C   1 
ATOM   2062 O O   . MET A 1 281 ? 14.642  44.133  15.521  1.00  71.44  ? 281  MET A O   1 
ATOM   2063 C CB  . MET A 1 281 ? 13.579  41.183  16.475  1.00  72.05  ? 281  MET A CB  1 
ATOM   2064 C CG  . MET A 1 281 ? 13.571  42.083  17.714  1.00  73.19  ? 281  MET A CG  1 
ATOM   2065 S SD  . MET A 1 281 ? 15.228  42.444  18.354  1.00  76.45  ? 281  MET A SD  1 
ATOM   2066 C CE  . MET A 1 281 ? 15.799  40.811  18.853  1.00  75.59  ? 281  MET A CE  1 
ATOM   2067 N N   . LYS A 1 282 ? 16.257  42.586  15.227  0.010 70.69  ? 282  LYS A N   1 
ATOM   2068 C CA  . LYS A 1 282 ? 17.357  43.529  15.356  0.010 70.04  ? 282  LYS A CA  1 
ATOM   2069 C C   . LYS A 1 282 ? 17.412  44.502  14.170  0.010 69.60  ? 282  LYS A C   1 
ATOM   2070 O O   . LYS A 1 282 ? 17.901  45.641  14.301  0.010 69.55  ? 282  LYS A O   1 
ATOM   2071 C CB  . LYS A 1 282 ? 18.683  42.784  15.542  0.010 70.07  ? 282  LYS A CB  1 
ATOM   2072 C CG  . LYS A 1 282 ? 18.732  41.981  16.838  0.010 70.01  ? 282  LYS A CG  1 
ATOM   2073 C CD  . LYS A 1 282 ? 20.038  41.222  17.002  0.010 69.97  ? 282  LYS A CD  1 
ATOM   2074 C CE  . LYS A 1 282 ? 20.052  40.436  18.305  0.010 69.95  ? 282  LYS A CE  1 
ATOM   2075 N NZ  . LYS A 1 282 ? 21.314  39.667  18.481  0.010 69.93  ? 282  LYS A NZ  1 
ATOM   2076 N N   . HIS A 1 283 ? 16.881  44.056  13.026  0.010 69.03  ? 283  HIS A N   1 
ATOM   2077 C CA  . HIS A 1 283 ? 16.908  44.869  11.813  0.010 68.48  ? 283  HIS A CA  1 
ATOM   2078 C C   . HIS A 1 283 ? 15.542  45.480  11.501  0.010 68.11  ? 283  HIS A C   1 
ATOM   2079 O O   . HIS A 1 283 ? 15.284  45.919  10.380  0.010 68.06  ? 283  HIS A O   1 
ATOM   2080 C CB  . HIS A 1 283 ? 17.376  44.019  10.638  0.010 68.49  ? 283  HIS A CB  1 
ATOM   2081 C CG  . HIS A 1 283 ? 18.426  44.676  9.803   0.010 68.42  ? 283  HIS A CG  1 
ATOM   2082 N ND1 . HIS A 1 283 ? 18.146  45.698  8.922   0.010 68.38  ? 283  HIS A ND1 1 
ATOM   2083 C CD2 . HIS A 1 283 ? 19.759  44.457  9.716   0.010 68.38  ? 283  HIS A CD2 1 
ATOM   2084 C CE1 . HIS A 1 283 ? 19.262  46.080  8.327   0.010 68.36  ? 283  HIS A CE1 1 
ATOM   2085 N NE2 . HIS A 1 283 ? 20.256  45.342  8.790   0.010 68.36  ? 283  HIS A NE2 1 
ATOM   2086 N N   . CYS A 1 284 ? 14.674  45.500  12.507  0.010 67.64  ? 284  CYS A N   1 
ATOM   2087 C CA  . CYS A 1 284 ? 13.335  46.058  12.378  0.010 67.21  ? 284  CYS A CA  1 
ATOM   2088 C C   . CYS A 1 284 ? 12.702  46.116  13.765  0.010 66.91  ? 284  CYS A C   1 
ATOM   2089 O O   . CYS A 1 284 ? 12.566  45.086  14.439  0.010 66.88  ? 284  CYS A O   1 
ATOM   2090 C CB  . CYS A 1 284 ? 12.491  45.201  11.435  0.010 67.21  ? 284  CYS A CB  1 
ATOM   2091 S SG  . CYS A 1 284 ? 10.863  45.879  11.044  0.010 67.19  ? 284  CYS A SG  1 
ATOM   2092 N N   . SER A 1 285 ? 12.302  47.318  14.179  1.00  66.60  ? 285  SER A N   1 
ATOM   2093 C CA  . SER A 1 285 ? 11.888  47.552  15.564  1.00  66.15  ? 285  SER A CA  1 
ATOM   2094 C C   . SER A 1 285 ? 10.388  47.354  15.792  1.00  65.72  ? 285  SER A C   1 
ATOM   2095 O O   . SER A 1 285 ? 9.967   46.928  16.880  1.00  65.65  ? 285  SER A O   1 
ATOM   2096 C CB  . SER A 1 285 ? 12.304  48.957  16.004  1.00  66.21  ? 285  SER A CB  1 
ATOM   2097 O OG  . SER A 1 285 ? 12.616  48.983  17.389  1.00  66.67  ? 285  SER A OG  1 
ATOM   2098 N N   . LYS A 1 286 ? 9.598   47.644  14.757  1.00  65.03  ? 286  LYS A N   1 
ATOM   2099 C CA  . LYS A 1 286 ? 8.135   47.508  14.803  1.00  64.25  ? 286  LYS A CA  1 
ATOM   2100 C C   . LYS A 1 286 ? 7.628   46.056  14.927  1.00  63.64  ? 286  LYS A C   1 
ATOM   2101 O O   . LYS A 1 286 ? 6.429   45.845  15.137  1.00  63.59  ? 286  LYS A O   1 
ATOM   2102 C CB  . LYS A 1 286 ? 7.489   48.199  13.585  1.00  64.13  ? 286  LYS A CB  1 
ATOM   2103 C CG  . LYS A 1 286 ? 7.807   47.534  12.242  1.00  64.09  ? 286  LYS A CG  1 
ATOM   2104 C CD  . LYS A 1 286 ? 7.151   48.242  11.051  1.00  64.28  ? 286  LYS A CD  1 
ATOM   2105 C CE  . LYS A 1 286 ? 7.971   49.430  10.529  1.00  63.27  ? 286  LYS A CE  1 
ATOM   2106 N NZ  . LYS A 1 286 ? 7.764   50.684  11.311  1.00  62.76  ? 286  LYS A NZ  1 
ATOM   2107 N N   . ILE A 1 287 ? 8.524   45.075  14.793  1.00  62.90  ? 287  ILE A N   1 
ATOM   2108 C CA  . ILE A 1 287 ? 8.155   43.653  14.910  1.00  62.39  ? 287  ILE A CA  1 
ATOM   2109 C C   . ILE A 1 287 ? 7.905   43.215  16.364  1.00  61.91  ? 287  ILE A C   1 
ATOM   2110 O O   . ILE A 1 287 ? 8.643   43.585  17.280  1.00  61.86  ? 287  ILE A O   1 
ATOM   2111 C CB  . ILE A 1 287 ? 9.220   42.702  14.271  1.00  62.54  ? 287  ILE A CB  1 
ATOM   2112 C CG1 . ILE A 1 287 ? 9.572   43.138  12.845  1.00  62.67  ? 287  ILE A CG1 1 
ATOM   2113 C CG2 . ILE A 1 287 ? 8.729   41.235  14.272  1.00  62.60  ? 287  ILE A CG2 1 
ATOM   2114 C CD1 . ILE A 1 287 ? 10.677  42.306  12.188  1.00  63.27  ? 287  ILE A CD1 1 
ATOM   2115 N N   . GLN A 1 288 ? 6.859   42.419  16.559  1.00  61.29  ? 288  GLN A N   1 
ATOM   2116 C CA  . GLN A 1 288 ? 6.603   41.769  17.846  1.00  60.83  ? 288  GLN A CA  1 
ATOM   2117 C C   . GLN A 1 288 ? 6.270   40.287  17.653  1.00  60.08  ? 288  GLN A C   1 
ATOM   2118 O O   . GLN A 1 288 ? 5.586   39.918  16.696  1.00  60.19  ? 288  GLN A O   1 
ATOM   2119 C CB  . GLN A 1 288 ? 5.497   42.501  18.615  1.00  60.92  ? 288  GLN A CB  1 
ATOM   2120 C CG  . GLN A 1 288 ? 6.022   43.688  19.423  1.00  61.64  ? 288  GLN A CG  1 
ATOM   2121 C CD  . GLN A 1 288 ? 4.921   44.554  20.010  1.00  62.44  ? 288  GLN A CD  1 
ATOM   2122 O OE1 . GLN A 1 288 ? 4.659   44.512  21.217  1.00  62.07  ? 288  GLN A OE1 1 
ATOM   2123 N NE2 . GLN A 1 288 ? 4.277   45.355  19.158  1.00  61.74  ? 288  GLN A NE2 1 
ATOM   2124 N N   . VAL A 1 289 ? 6.772   39.442  18.551  1.00  59.16  ? 289  VAL A N   1 
ATOM   2125 C CA  . VAL A 1 289 ? 6.564   37.991  18.447  1.00  58.41  ? 289  VAL A CA  1 
ATOM   2126 C C   . VAL A 1 289 ? 5.556   37.452  19.465  1.00  57.89  ? 289  VAL A C   1 
ATOM   2127 O O   . VAL A 1 289 ? 5.609   37.788  20.655  1.00  57.87  ? 289  VAL A O   1 
ATOM   2128 C CB  . VAL A 1 289 ? 7.887   37.184  18.567  1.00  58.27  ? 289  VAL A CB  1 
ATOM   2129 C CG1 . VAL A 1 289 ? 8.741   37.376  17.345  1.00  58.87  ? 289  VAL A CG1 1 
ATOM   2130 C CG2 . VAL A 1 289 ? 8.664   37.576  19.814  1.00  58.57  ? 289  VAL A CG2 1 
ATOM   2131 N N   . ILE A 1 290 ? 4.635   36.620  18.983  1.00  57.13  ? 290  ILE A N   1 
ATOM   2132 C CA  . ILE A 1 290 ? 3.753   35.861  19.859  1.00  56.39  ? 290  ILE A CA  1 
ATOM   2133 C C   . ILE A 1 290 ? 4.427   34.516  20.115  1.00  55.99  ? 290  ILE A C   1 
ATOM   2134 O O   . ILE A 1 290 ? 4.842   33.816  19.170  1.00  55.83  ? 290  ILE A O   1 
ATOM   2135 C CB  . ILE A 1 290 ? 2.352   35.633  19.246  1.00  56.49  ? 290  ILE A CB  1 
ATOM   2136 C CG1 . ILE A 1 290 ? 1.680   36.967  18.889  1.00  56.60  ? 290  ILE A CG1 1 
ATOM   2137 C CG2 . ILE A 1 290 ? 1.475   34.822  20.207  1.00  56.56  ? 290  ILE A CG2 1 
ATOM   2138 C CD1 . ILE A 1 290 ? 0.511   36.831  17.904  1.00  56.14  ? 290  ILE A CD1 1 
ATOM   2139 N N   . ASP A 1 291 ? 4.568   34.181  21.396  1.00  55.38  ? 291  ASP A N   1 
ATOM   2140 C CA  . ASP A 1 291 ? 5.161   32.920  21.797  1.00  54.65  ? 291  ASP A CA  1 
ATOM   2141 C C   . ASP A 1 291 ? 4.141   31.806  21.592  1.00  54.09  ? 291  ASP A C   1 
ATOM   2142 O O   . ASP A 1 291 ? 3.061   31.827  22.182  1.00  54.24  ? 291  ASP A O   1 
ATOM   2143 C CB  . ASP A 1 291 ? 5.599   32.989  23.261  1.00  54.75  ? 291  ASP A CB  1 
ATOM   2144 C CG  . ASP A 1 291 ? 6.553   31.871  23.644  1.00  55.47  ? 291  ASP A CG  1 
ATOM   2145 O OD1 . ASP A 1 291 ? 6.744   30.929  22.841  1.00  56.00  ? 291  ASP A OD1 1 
ATOM   2146 O OD2 . ASP A 1 291 ? 7.120   31.940  24.764  1.00  56.75  ? 291  ASP A OD2 1 
ATOM   2147 N N   . ILE A 1 292 ? 4.481   30.843  20.740  1.00  53.16  ? 292  ILE A N   1 
ATOM   2148 C CA  . ILE A 1 292 ? 3.593   29.705  20.482  1.00  52.40  ? 292  ILE A CA  1 
ATOM   2149 C C   . ILE A 1 292 ? 4.092   28.384  21.083  1.00  51.93  ? 292  ILE A C   1 
ATOM   2150 O O   . ILE A 1 292 ? 3.585   27.305  20.754  1.00  51.61  ? 292  ILE A O   1 
ATOM   2151 C CB  . ILE A 1 292 ? 3.253   29.545  18.972  1.00  52.31  ? 292  ILE A CB  1 
ATOM   2152 C CG1 . ILE A 1 292 ? 4.502   29.664  18.090  1.00  52.33  ? 292  ILE A CG1 1 
ATOM   2153 C CG2 . ILE A 1 292 ? 2.214   30.569  18.562  1.00  52.07  ? 292  ILE A CG2 1 
ATOM   2154 C CD1 . ILE A 1 292 ? 5.162   28.347  17.724  1.00  51.52  ? 292  ILE A CD1 1 
ATOM   2155 N N   . SER A 1 293 ? 5.066   28.488  21.984  1.00  51.34  ? 293  SER A N   1 
ATOM   2156 C CA  . SER A 1 293 ? 5.662   27.320  22.607  1.00  51.03  ? 293  SER A CA  1 
ATOM   2157 C C   . SER A 1 293 ? 4.731   26.632  23.614  1.00  50.74  ? 293  SER A C   1 
ATOM   2158 O O   . SER A 1 293 ? 4.643   25.409  23.618  1.00  51.12  ? 293  SER A O   1 
ATOM   2159 C CB  . SER A 1 293 ? 7.017   27.664  23.233  1.00  51.00  ? 293  SER A CB  1 
ATOM   2160 O OG  . SER A 1 293 ? 6.923   28.799  24.072  1.00  51.21  ? 293  SER A OG  1 
ATOM   2161 N N   . MET A 1 294 ? 4.039   27.405  24.450  0.67  50.22  ? 294  MET A N   1 
ATOM   2162 C CA  . MET A 1 294 ? 3.091   26.834  25.412  0.67  49.88  ? 294  MET A CA  1 
ATOM   2163 C C   . MET A 1 294 ? 1.974   26.066  24.690  0.67  49.18  ? 294  MET A C   1 
ATOM   2164 O O   . MET A 1 294 ? 1.610   24.965  25.103  0.67  48.97  ? 294  MET A O   1 
ATOM   2165 C CB  . MET A 1 294 ? 2.532   27.918  26.360  0.67  50.16  ? 294  MET A CB  1 
ATOM   2166 C CG  . MET A 1 294 ? 1.390   27.470  27.291  0.67  51.01  ? 294  MET A CG  1 
ATOM   2167 S SD  . MET A 1 294 ? 1.808   26.162  28.474  0.67  54.57  ? 294  MET A SD  1 
ATOM   2168 C CE  . MET A 1 294 ? 2.166   27.111  29.964  0.67  53.50  ? 294  MET A CE  1 
ATOM   2169 N N   . ILE A 1 295 ? 1.464   26.636  23.598  1.00  48.48  ? 295  ILE A N   1 
ATOM   2170 C CA  . ILE A 1 295 ? 0.453   25.971  22.765  1.00  47.78  ? 295  ILE A CA  1 
ATOM   2171 C C   . ILE A 1 295 ? 0.981   24.654  22.164  1.00  47.07  ? 295  ILE A C   1 
ATOM   2172 O O   . ILE A 1 295 ? 0.269   23.643  22.128  1.00  46.60  ? 295  ILE A O   1 
ATOM   2173 C CB  . ILE A 1 295 ? -0.072  26.885  21.629  1.00  47.77  ? 295  ILE A CB  1 
ATOM   2174 C CG1 . ILE A 1 295 ? -0.466  28.260  22.176  1.00  48.32  ? 295  ILE A CG1 1 
ATOM   2175 C CG2 . ILE A 1 295 ? -1.272  26.237  20.948  1.00  48.02  ? 295  ILE A CG2 1 
ATOM   2176 C CD1 . ILE A 1 295 ? -0.688  29.336  21.118  1.00  48.78  ? 295  ILE A CD1 1 
ATOM   2177 N N   . LEU A 1 296 ? 2.230   24.671  21.706  1.00  46.34  ? 296  LEU A N   1 
ATOM   2178 C CA  . LEU A 1 296 ? 2.877   23.464  21.201  1.00  45.82  ? 296  LEU A CA  1 
ATOM   2179 C C   . LEU A 1 296 ? 3.227   22.460  22.307  1.00  45.75  ? 296  LEU A C   1 
ATOM   2180 O O   . LEU A 1 296 ? 3.119   21.252  22.106  1.00  45.27  ? 296  LEU A O   1 
ATOM   2181 C CB  . LEU A 1 296 ? 4.118   23.812  20.373  1.00  45.68  ? 296  LEU A CB  1 
ATOM   2182 C CG  . LEU A 1 296 ? 3.940   24.521  19.018  1.00  44.85  ? 296  LEU A CG  1 
ATOM   2183 C CD1 . LEU A 1 296 ? 5.302   24.800  18.391  1.00  43.79  ? 296  LEU A CD1 1 
ATOM   2184 C CD2 . LEU A 1 296 ? 3.063   23.724  18.059  1.00  44.43  ? 296  LEU A CD2 1 
ATOM   2185 N N   . ALA A 1 297 ? 3.636   22.964  23.469  1.00  45.81  ? 297  ALA A N   1 
ATOM   2186 C CA  . ALA A 1 297 ? 3.989   22.111  24.597  1.00  45.95  ? 297  ALA A CA  1 
ATOM   2187 C C   . ALA A 1 297 ? 2.744   21.482  25.212  1.00  46.05  ? 297  ALA A C   1 
ATOM   2188 O O   . ALA A 1 297 ? 2.739   20.296  25.568  1.00  46.04  ? 297  ALA A O   1 
ATOM   2189 C CB  . ALA A 1 297 ? 4.767   22.897  25.639  1.00  46.00  ? 297  ALA A CB  1 
ATOM   2190 N N   . GLU A 1 298 ? 1.687   22.280  25.318  1.00  46.06  ? 298  GLU A N   1 
ATOM   2191 C CA  . GLU A 1 298 ? 0.413   21.810  25.840  1.00  46.12  ? 298  GLU A CA  1 
ATOM   2192 C C   . GLU A 1 298 ? -0.216  20.782  24.904  1.00  45.66  ? 298  GLU A C   1 
ATOM   2193 O O   . GLU A 1 298 ? -0.846  19.833  25.370  1.00  45.26  ? 298  GLU A O   1 
ATOM   2194 C CB  . GLU A 1 298 ? -0.534  22.989  26.092  1.00  46.41  ? 298  GLU A CB  1 
ATOM   2195 C CG  . GLU A 1 298 ? -1.703  22.686  27.015  1.00  48.46  ? 298  GLU A CG  1 
ATOM   2196 C CD  . GLU A 1 298 ? -1.290  21.922  28.265  1.00  51.49  ? 298  GLU A CD  1 
ATOM   2197 O OE1 . GLU A 1 298 ? -0.639  22.529  29.153  1.00  52.42  ? 298  GLU A OE1 1 
ATOM   2198 O OE2 . GLU A 1 298 ? -1.627  20.710  28.357  1.00  51.72  ? 298  GLU A OE2 1 
ATOM   2199 N N   . ALA A 1 299 ? -0.027  20.970  23.593  1.00  45.35  ? 299  ALA A N   1 
ATOM   2200 C CA  . ALA A 1 299 ? -0.527  20.031  22.580  1.00  45.25  ? 299  ALA A CA  1 
ATOM   2201 C C   . ALA A 1 299 ? 0.268   18.725  22.513  1.00  45.15  ? 299  ALA A C   1 
ATOM   2202 O O   . ALA A 1 299 ? -0.244  17.715  22.047  1.00  45.26  ? 299  ALA A O   1 
ATOM   2203 C CB  . ALA A 1 299 ? -0.583  20.691  21.193  1.00  45.39  ? 299  ALA A CB  1 
ATOM   2204 N N   . ILE A 1 300 ? 1.517   18.755  22.963  1.00  45.16  ? 300  ILE A N   1 
ATOM   2205 C CA  . ILE A 1 300 ? 2.344   17.549  23.054  1.00  45.16  ? 300  ILE A CA  1 
ATOM   2206 C C   . ILE A 1 300 ? 1.996   16.705  24.292  1.00  45.71  ? 300  ILE A C   1 
ATOM   2207 O O   . ILE A 1 300 ? 1.881   15.479  24.192  1.00  45.35  ? 300  ILE A O   1 
ATOM   2208 C CB  . ILE A 1 300 ? 3.860   17.900  22.999  1.00  44.96  ? 300  ILE A CB  1 
ATOM   2209 C CG1 . ILE A 1 300 ? 4.281   18.154  21.553  1.00  43.72  ? 300  ILE A CG1 1 
ATOM   2210 C CG2 . ILE A 1 300 ? 4.720   16.796  23.601  1.00  44.49  ? 300  ILE A CG2 1 
ATOM   2211 C CD1 . ILE A 1 300 ? 5.581   18.902  21.400  1.00  41.23  ? 300  ILE A CD1 1 
ATOM   2212 N N   . ARG A 1 301 ? 1.820   17.364  25.440  1.00  46.54  ? 301  ARG A N   1 
ATOM   2213 C CA  . ARG A 1 301 ? 1.485   16.680  26.693  1.00  47.60  ? 301  ARG A CA  1 
ATOM   2214 C C   . ARG A 1 301 ? 0.134   15.990  26.589  1.00  47.92  ? 301  ARG A C   1 
ATOM   2215 O O   . ARG A 1 301 ? -0.015  14.835  26.997  1.00  47.99  ? 301  ARG A O   1 
ATOM   2216 C CB  . ARG A 1 301 ? 1.479   17.654  27.879  1.00  47.80  ? 301  ARG A CB  1 
ATOM   2217 C CG  . ARG A 1 301 ? 1.480   16.948  29.234  1.00  49.80  ? 301  ARG A CG  1 
ATOM   2218 C CD  . ARG A 1 301 ? 1.190   17.877  30.420  1.00  52.33  ? 301  ARG A CD  1 
ATOM   2219 N NE  . ARG A 1 301 ? -0.246  18.001  30.684  1.00  53.72  ? 301  ARG A NE  1 
ATOM   2220 C CZ  . ARG A 1 301 ? -0.895  19.154  30.841  1.00  55.17  ? 301  ARG A CZ  1 
ATOM   2221 N NH1 . ARG A 1 301 ? -0.248  20.318  30.772  1.00  54.93  ? 301  ARG A NH1 1 
ATOM   2222 N NH2 . ARG A 1 301 ? -2.208  19.142  31.073  1.00  55.61  ? 301  ARG A NH2 1 
ATOM   2223 N N   . ARG A 1 302 ? -0.836  16.704  26.019  0.84  48.46  ? 302  ARG A N   1 
ATOM   2224 C CA  . ARG A 1 302 ? -2.205  16.209  25.876  0.84  48.97  ? 302  ARG A CA  1 
ATOM   2225 C C   . ARG A 1 302 ? -2.324  15.108  24.830  0.84  48.91  ? 302  ARG A C   1 
ATOM   2226 O O   . ARG A 1 302 ? -3.176  14.230  24.943  0.84  48.93  ? 302  ARG A O   1 
ATOM   2227 C CB  . ARG A 1 302 ? -3.168  17.366  25.589  0.84  49.06  ? 302  ARG A CB  1 
ATOM   2228 C CG  . ARG A 1 302 ? -3.309  18.327  26.776  0.84  50.39  ? 302  ARG A CG  1 
ATOM   2229 C CD  . ARG A 1 302 ? -4.270  19.475  26.486  0.84  52.88  ? 302  ARG A CD  1 
ATOM   2230 N NE  . ARG A 1 302 ? -4.246  20.506  27.527  0.84  53.61  ? 302  ARG A NE  1 
ATOM   2231 C CZ  . ARG A 1 302 ? -4.953  20.476  28.656  0.84  54.08  ? 302  ARG A CZ  1 
ATOM   2232 N NH1 . ARG A 1 302 ? -5.756  19.453  28.935  0.84  53.72  ? 302  ARG A NH1 1 
ATOM   2233 N NH2 . ARG A 1 302 ? -4.847  21.478  29.521  0.84  54.41  ? 302  ARG A NH2 1 
ATOM   2234 N N   . THR A 1 303 ? -1.464  15.157  23.818  1.00  49.27  ? 303  THR A N   1 
ATOM   2235 C CA  . THR A 1 303 ? -1.375  14.082  22.829  1.00  49.68  ? 303  THR A CA  1 
ATOM   2236 C C   . THR A 1 303 ? -0.769  12.820  23.446  1.00  49.91  ? 303  THR A C   1 
ATOM   2237 O O   . THR A 1 303 ? -1.238  11.715  23.190  1.00  50.16  ? 303  THR A O   1 
ATOM   2238 C CB  . THR A 1 303 ? -0.567  14.532  21.610  1.00  49.60  ? 303  THR A CB  1 
ATOM   2239 O OG1 . THR A 1 303 ? -1.333  15.501  20.894  1.00  48.97  ? 303  THR A OG1 1 
ATOM   2240 C CG2 . THR A 1 303 ? -0.234  13.360  20.689  1.00  50.25  ? 303  THR A CG2 1 
ATOM   2241 N N   . HIS A 1 304 ? 0.263   13.003  24.266  1.00  50.19  ? 304  HIS A N   1 
ATOM   2242 C CA  . HIS A 1 304 ? 0.922   11.901  24.945  1.00  50.82  ? 304  HIS A CA  1 
ATOM   2243 C C   . HIS A 1 304 ? 0.068   11.268  26.058  1.00  51.21  ? 304  HIS A C   1 
ATOM   2244 O O   . HIS A 1 304 ? 0.182   10.067  26.319  1.00  51.46  ? 304  HIS A O   1 
ATOM   2245 C CB  . HIS A 1 304 ? 2.266   12.360  25.511  1.00  50.90  ? 304  HIS A CB  1 
ATOM   2246 C CG  . HIS A 1 304 ? 2.935   11.335  26.372  1.00  50.95  ? 304  HIS A CG  1 
ATOM   2247 N ND1 . HIS A 1 304 ? 3.474   10.171  25.865  1.00  50.38  ? 304  HIS A ND1 1 
ATOM   2248 C CD2 . HIS A 1 304 ? 3.130   11.288  27.710  1.00  50.67  ? 304  HIS A CD2 1 
ATOM   2249 C CE1 . HIS A 1 304 ? 3.987   9.460   26.852  1.00  49.37  ? 304  HIS A CE1 1 
ATOM   2250 N NE2 . HIS A 1 304 ? 3.791   10.115  27.981  1.00  50.46  ? 304  HIS A NE2 1 
ATOM   2251 N N   . ASN A 1 305 ? -0.778  12.069  26.704  1.00  51.38  ? 305  ASN A N   1 
ATOM   2252 C CA  . ASN A 1 305 ? -1.611  11.581  27.805  1.00  51.72  ? 305  ASN A CA  1 
ATOM   2253 C C   . ASN A 1 305 ? -2.985  11.112  27.361  1.00  52.14  ? 305  ASN A C   1 
ATOM   2254 O O   . ASN A 1 305 ? -3.748  10.585  28.166  1.00  52.65  ? 305  ASN A O   1 
ATOM   2255 C CB  . ASN A 1 305 ? -1.804  12.655  28.883  1.00  51.58  ? 305  ASN A CB  1 
ATOM   2256 C CG  . ASN A 1 305 ? -0.503  13.192  29.435  1.00  51.18  ? 305  ASN A CG  1 
ATOM   2257 O OD1 . ASN A 1 305 ? 0.564   12.595  29.281  1.00  51.97  ? 305  ASN A OD1 1 
ATOM   2258 N ND2 . ASN A 1 305 ? -0.591  14.340  30.090  1.00  50.13  ? 305  ASN A ND2 1 
ATOM   2259 N N   . GLY A 1 306 ? -3.308  11.318  26.090  1.00  52.69  ? 306  GLY A N   1 
ATOM   2260 C CA  . GLY A 1 306 ? -4.645  11.014  25.576  1.00  53.23  ? 306  GLY A CA  1 
ATOM   2261 C C   . GLY A 1 306 ? -5.716  12.002  26.021  1.00  53.68  ? 306  GLY A C   1 
ATOM   2262 O O   . GLY A 1 306 ? -6.903  11.659  26.065  1.00  53.69  ? 306  GLY A O   1 
ATOM   2263 N N   . GLU A 1 307 ? -5.302  13.229  26.344  1.00  54.01  ? 307  GLU A N   1 
ATOM   2264 C CA  . GLU A 1 307 ? -6.234  14.289  26.738  1.00  54.64  ? 307  GLU A CA  1 
ATOM   2265 C C   . GLU A 1 307 ? -6.655  15.143  25.547  1.00  54.90  ? 307  GLU A C   1 
ATOM   2266 O O   . GLU A 1 307 ? -5.959  15.204  24.522  1.00  55.18  ? 307  GLU A O   1 
ATOM   2267 C CB  . GLU A 1 307 ? -5.643  15.167  27.860  1.00  54.86  ? 307  GLU A CB  1 
ATOM   2268 C CG  . GLU A 1 307 ? -6.318  16.561  28.061  1.00  56.37  ? 307  GLU A CG  1 
ATOM   2269 C CD  . GLU A 1 307 ? -7.729  16.530  28.703  1.00  57.24  ? 307  GLU A CD  1 
ATOM   2270 O OE1 . GLU A 1 307 ? -8.130  15.497  29.270  1.00  56.78  ? 307  GLU A OE1 1 
ATOM   2271 O OE2 . GLU A 1 307 ? -8.447  17.553  28.642  1.00  58.32  ? 307  GLU A OE2 1 
ATOM   2272 N N   . SER A 1 308 ? -7.795  15.812  25.705  1.00  55.17  ? 308  SER A N   1 
ATOM   2273 C CA  . SER A 1 308 ? -8.370  16.659  24.675  1.00  55.28  ? 308  SER A CA  1 
ATOM   2274 C C   . SER A 1 308 ? -7.461  17.815  24.281  1.00  55.66  ? 308  SER A C   1 
ATOM   2275 O O   . SER A 1 308 ? -7.008  18.588  25.134  1.00  55.90  ? 308  SER A O   1 
ATOM   2276 C CB  . SER A 1 308 ? -9.731  17.197  25.122  1.00  55.30  ? 308  SER A CB  1 
ATOM   2277 O OG  . SER A 1 308 ? -10.297 18.016  24.110  1.00  54.99  ? 308  SER A OG  1 
ATOM   2278 N N   . VAL A 1 309 ? -7.203  17.914  22.978  1.00  55.92  ? 309  VAL A N   1 
ATOM   2279 C CA  . VAL A 1 309 ? -6.496  19.054  22.387  1.00  56.19  ? 309  VAL A CA  1 
ATOM   2280 C C   . VAL A 1 309 ? -7.508  20.044  21.775  1.00  56.52  ? 309  VAL A C   1 
ATOM   2281 O O   . VAL A 1 309 ? -7.155  21.180  21.433  1.00  56.35  ? 309  VAL A O   1 
ATOM   2282 C CB  . VAL A 1 309 ? -5.472  18.607  21.300  1.00  56.05  ? 309  VAL A CB  1 
ATOM   2283 C CG1 . VAL A 1 309 ? -4.594  19.766  20.891  1.00  56.28  ? 309  VAL A CG1 1 
ATOM   2284 C CG2 . VAL A 1 309 ? -4.596  17.456  21.793  1.00  56.37  ? 309  VAL A CG2 1 
ATOM   2285 N N   . SER A 1 310 ? -8.766  19.612  21.649  0.53  56.96  ? 310  SER A N   1 
ATOM   2286 C CA  . SER A 1 310 ? -9.819  20.437  21.040  0.53  57.36  ? 310  SER A CA  1 
ATOM   2287 C C   . SER A 1 310 ? -10.050 21.751  21.792  0.53  57.72  ? 310  SER A C   1 
ATOM   2288 O O   . SER A 1 310 ? -10.452 22.754  21.194  0.53  57.84  ? 310  SER A O   1 
ATOM   2289 C CB  . SER A 1 310 ? -11.132 19.657  20.901  0.53  57.34  ? 310  SER A CB  1 
ATOM   2290 O OG  . SER A 1 310 ? -11.843 19.602  22.126  0.53  57.32  ? 310  SER A OG  1 
ATOM   2291 N N   . TYR A 1 311 ? -9.790  21.739  23.099  0.66  58.23  ? 311  TYR A N   1 
ATOM   2292 C CA  . TYR A 1 311 ? -9.831  22.970  23.894  0.66  58.84  ? 311  TYR A CA  1 
ATOM   2293 C C   . TYR A 1 311 ? -8.871  24.041  23.357  0.66  59.15  ? 311  TYR A C   1 
ATOM   2294 O O   . TYR A 1 311 ? -9.237  25.213  23.273  0.66  59.26  ? 311  TYR A O   1 
ATOM   2295 C CB  . TYR A 1 311 ? -9.543  22.690  25.376  0.66  58.79  ? 311  TYR A CB  1 
ATOM   2296 C CG  . TYR A 1 311 ? -9.328  23.948  26.193  0.66  58.84  ? 311  TYR A CG  1 
ATOM   2297 C CD1 . TYR A 1 311 ? -10.408 24.735  26.595  0.66  59.14  ? 311  TYR A CD1 1 
ATOM   2298 C CD2 . TYR A 1 311 ? -8.043  24.356  26.556  0.66  59.04  ? 311  TYR A CD2 1 
ATOM   2299 C CE1 . TYR A 1 311 ? -10.216 25.897  27.343  0.66  59.31  ? 311  TYR A CE1 1 
ATOM   2300 C CE2 . TYR A 1 311 ? -7.837  25.513  27.303  0.66  59.07  ? 311  TYR A CE2 1 
ATOM   2301 C CZ  . TYR A 1 311 ? -8.928  26.279  27.693  0.66  59.32  ? 311  TYR A CZ  1 
ATOM   2302 O OH  . TYR A 1 311 ? -8.723  27.422  28.432  0.66  58.98  ? 311  TYR A OH  1 
ATOM   2303 N N   . LEU A 1 312 ? -7.649  23.632  23.011  1.00  59.66  ? 312  LEU A N   1 
ATOM   2304 C CA  . LEU A 1 312 ? -6.658  24.538  22.425  1.00  60.14  ? 312  LEU A CA  1 
ATOM   2305 C C   . LEU A 1 312 ? -7.134  25.056  21.069  1.00  60.41  ? 312  LEU A C   1 
ATOM   2306 O O   . LEU A 1 312 ? -7.184  26.298  20.842  1.00  60.84  ? 312  LEU A O   1 
ATOM   2307 C CB  . LEU A 1 312 ? -5.298  23.843  22.272  1.00  60.12  ? 312  LEU A CB  1 
ATOM   2308 C CG  . LEU A 1 312 ? -4.473  23.558  23.534  1.00  60.87  ? 312  LEU A CG  1 
ATOM   2309 C CD1 . LEU A 1 312 ? -3.466  22.437  23.269  1.00  60.90  ? 312  LEU A CD1 1 
ATOM   2310 C CD2 . LEU A 1 312 ? -3.764  24.817  24.041  1.00  60.97  ? 312  LEU A CD2 1 
ATOM   2311 N N   . ASN B 1 3   ? 6.467   10.150  -28.484 0.84  38.52  ? 3    ASN B N   1 
ATOM   2312 C CA  . ASN B 1 3   ? 6.182   9.346   -27.249 0.84  38.51  ? 3    ASN B CA  1 
ATOM   2313 C C   . ASN B 1 3   ? 7.165   9.654   -26.113 0.84  38.08  ? 3    ASN B C   1 
ATOM   2314 O O   . ASN B 1 3   ? 6.753   9.850   -24.967 0.84  37.70  ? 3    ASN B O   1 
ATOM   2315 C CB  . ASN B 1 3   ? 6.205   7.851   -27.578 0.84  38.67  ? 3    ASN B CB  1 
ATOM   2316 C CG  . ASN B 1 3   ? 5.259   7.031   -26.714 0.84  40.15  ? 3    ASN B CG  1 
ATOM   2317 O OD1 . ASN B 1 3   ? 4.544   6.176   -27.229 0.84  41.87  ? 3    ASN B OD1 1 
ATOM   2318 N ND2 . ASN B 1 3   ? 5.248   7.282   -25.401 0.84  42.26  ? 3    ASN B ND2 1 
ATOM   2319 N N   . ILE B 1 4   ? 8.457   9.691   -26.444 1.00  37.90  ? 4    ILE B N   1 
ATOM   2320 C CA  . ILE B 1 4   ? 9.520   9.930   -25.469 1.00  37.91  ? 4    ILE B CA  1 
ATOM   2321 C C   . ILE B 1 4   ? 9.562   11.410  -25.111 1.00  37.78  ? 4    ILE B C   1 
ATOM   2322 O O   . ILE B 1 4   ? 9.294   12.260  -25.955 1.00  38.02  ? 4    ILE B O   1 
ATOM   2323 C CB  . ILE B 1 4   ? 10.896  9.442   -26.010 1.00  37.80  ? 4    ILE B CB  1 
ATOM   2324 C CG1 . ILE B 1 4   ? 11.813  8.938   -24.883 1.00  38.43  ? 4    ILE B CG1 1 
ATOM   2325 C CG2 . ILE B 1 4   ? 11.552  10.497  -26.875 1.00  38.04  ? 4    ILE B CG2 1 
ATOM   2326 C CD1 . ILE B 1 4   ? 12.654  10.015  -24.165 1.00  38.22  ? 4    ILE B CD1 1 
ATOM   2327 N N   . LYS B 1 5   ? 9.882   11.713  -23.855 0.50  37.57  ? 5    LYS B N   1 
ATOM   2328 C CA  . LYS B 1 5   ? 9.960   13.096  -23.398 0.50  37.34  ? 5    LYS B CA  1 
ATOM   2329 C C   . LYS B 1 5   ? 10.969  13.225  -22.259 0.50  37.22  ? 5    LYS B C   1 
ATOM   2330 O O   . LYS B 1 5   ? 10.756  12.702  -21.160 0.50  37.04  ? 5    LYS B O   1 
ATOM   2331 C CB  . LYS B 1 5   ? 8.575   13.581  -22.952 0.50  37.49  ? 5    LYS B CB  1 
ATOM   2332 C CG  . LYS B 1 5   ? 8.360   15.097  -22.974 0.50  38.13  ? 5    LYS B CG  1 
ATOM   2333 C CD  . LYS B 1 5   ? 7.792   15.588  -24.314 0.50  39.25  ? 5    LYS B CD  1 
ATOM   2334 C CE  . LYS B 1 5   ? 8.856   16.230  -25.207 0.50  39.94  ? 5    LYS B CE  1 
ATOM   2335 N NZ  . LYS B 1 5   ? 9.229   17.614  -24.792 0.50  39.13  ? 5    LYS B NZ  1 
ATOM   2336 N N   . ILE B 1 6   ? 12.066  13.926  -22.529 1.00  37.13  ? 6    ILE B N   1 
ATOM   2337 C CA  . ILE B 1 6   ? 13.127  14.132  -21.535 1.00  36.86  ? 6    ILE B CA  1 
ATOM   2338 C C   . ILE B 1 6   ? 13.000  15.495  -20.873 1.00  36.72  ? 6    ILE B C   1 
ATOM   2339 O O   . ILE B 1 6   ? 12.711  16.489  -21.526 1.00  36.83  ? 6    ILE B O   1 
ATOM   2340 C CB  . ILE B 1 6   ? 14.524  14.042  -22.175 1.00  36.99  ? 6    ILE B CB  1 
ATOM   2341 C CG1 . ILE B 1 6   ? 14.587  12.861  -23.142 1.00  36.82  ? 6    ILE B CG1 1 
ATOM   2342 C CG2 . ILE B 1 6   ? 15.625  13.958  -21.097 1.00  36.52  ? 6    ILE B CG2 1 
ATOM   2343 C CD1 . ILE B 1 6   ? 15.737  12.913  -24.077 1.00  37.55  ? 6    ILE B CD1 1 
ATOM   2344 N N   . PHE B 1 7   ? 13.227  15.528  -19.568 1.00  37.10  ? 7    PHE B N   1 
ATOM   2345 C CA  . PHE B 1 7   ? 13.282  16.770  -18.807 1.00  37.27  ? 7    PHE B CA  1 
ATOM   2346 C C   . PHE B 1 7   ? 14.541  16.800  -17.951 1.00  38.04  ? 7    PHE B C   1 
ATOM   2347 O O   . PHE B 1 7   ? 15.146  15.759  -17.671 1.00  38.02  ? 7    PHE B O   1 
ATOM   2348 C CB  . PHE B 1 7   ? 12.062  16.898  -17.898 1.00  36.94  ? 7    PHE B CB  1 
ATOM   2349 C CG  . PHE B 1 7   ? 10.782  17.230  -18.614 1.00  35.36  ? 7    PHE B CG  1 
ATOM   2350 C CD1 . PHE B 1 7   ? 9.983   16.223  -19.136 1.00  35.00  ? 7    PHE B CD1 1 
ATOM   2351 C CD2 . PHE B 1 7   ? 10.357  18.541  -18.720 1.00  33.07  ? 7    PHE B CD2 1 
ATOM   2352 C CE1 . PHE B 1 7   ? 8.781   16.524  -19.771 1.00  35.35  ? 7    PHE B CE1 1 
ATOM   2353 C CE2 . PHE B 1 7   ? 9.173   18.853  -19.358 1.00  34.59  ? 7    PHE B CE2 1 
ATOM   2354 C CZ  . PHE B 1 7   ? 8.375   17.843  -19.882 1.00  35.35  ? 7    PHE B CZ  1 
ATOM   2355 N N   . SER B 1 8   ? 14.913  18.004  -17.532 1.00  39.16  ? 8    SER B N   1 
ATOM   2356 C CA  . SER B 1 8   ? 16.071  18.243  -16.680 1.00  40.35  ? 8    SER B CA  1 
ATOM   2357 C C   . SER B 1 8   ? 15.636  18.858  -15.357 1.00  40.93  ? 8    SER B C   1 
ATOM   2358 O O   . SER B 1 8   ? 14.518  19.393  -15.271 1.00  41.15  ? 8    SER B O   1 
ATOM   2359 C CB  . SER B 1 8   ? 17.014  19.217  -17.381 1.00  40.44  ? 8    SER B CB  1 
ATOM   2360 O OG  . SER B 1 8   ? 18.262  19.281  -16.710 1.00  42.04  ? 8    SER B OG  1 
ATOM   2361 N N   . GLY B 1 9   ? 16.524  18.798  -14.354 1.00  41.66  ? 9    GLY B N   1 
ATOM   2362 C CA  . GLY B 1 9   ? 16.354  19.493  -13.060 1.00  42.23  ? 9    GLY B CA  1 
ATOM   2363 C C   . GLY B 1 9   ? 17.123  20.816  -12.942 1.00  42.85  ? 9    GLY B C   1 
ATOM   2364 O O   . GLY B 1 9   ? 18.196  20.989  -13.532 1.00  43.66  ? 9    GLY B O   1 
ATOM   2365 N N   . SER B 1 10  ? 16.566  21.760  -12.184 0.010 42.77  ? 10   SER B N   1 
ATOM   2366 C CA  . SER B 1 10  ? 17.186  23.073  -11.939 0.010 42.71  ? 10   SER B CA  1 
ATOM   2367 C C   . SER B 1 10  ? 17.688  23.751  -13.214 0.010 42.73  ? 10   SER B C   1 
ATOM   2368 O O   . SER B 1 10  ? 16.966  23.838  -14.206 0.010 42.71  ? 10   SER B O   1 
ATOM   2369 C CB  . SER B 1 10  ? 18.322  22.967  -10.914 0.010 42.69  ? 10   SER B CB  1 
ATOM   2370 O OG  . SER B 1 10  ? 19.487  22.406  -11.496 0.010 42.67  ? 10   SER B OG  1 
ATOM   2371 N N   . SER B 1 11  ? 18.931  24.224  -13.180 0.10  42.79  ? 11   SER B N   1 
ATOM   2372 C CA  . SER B 1 11  ? 19.515  24.907  -14.329 0.10  42.97  ? 11   SER B CA  1 
ATOM   2373 C C   . SER B 1 11  ? 20.798  24.233  -14.807 0.10  43.13  ? 11   SER B C   1 
ATOM   2374 O O   . SER B 1 11  ? 21.476  24.741  -15.701 0.10  43.11  ? 11   SER B O   1 
ATOM   2375 C CB  . SER B 1 11  ? 19.784  26.378  -14.005 0.10  42.96  ? 11   SER B CB  1 
ATOM   2376 O OG  . SER B 1 11  ? 20.267  27.070  -15.144 0.10  42.84  ? 11   SER B OG  1 
ATOM   2377 N N   . HIS B 1 12  ? 21.127  23.091  -14.209 0.84  43.41  ? 12   HIS B N   1 
ATOM   2378 C CA  . HIS B 1 12  ? 22.307  22.332  -14.607 0.84  43.76  ? 12   HIS B CA  1 
ATOM   2379 C C   . HIS B 1 12  ? 21.957  21.359  -15.742 0.84  43.87  ? 12   HIS B C   1 
ATOM   2380 O O   . HIS B 1 12  ? 21.928  20.130  -15.557 0.84  43.79  ? 12   HIS B O   1 
ATOM   2381 C CB  . HIS B 1 12  ? 22.907  21.618  -13.393 0.84  43.91  ? 12   HIS B CB  1 
ATOM   2382 C CG  . HIS B 1 12  ? 23.587  22.538  -12.426 0.84  45.32  ? 12   HIS B CG  1 
ATOM   2383 N ND1 . HIS B 1 12  ? 24.885  22.341  -12.000 0.84  46.39  ? 12   HIS B ND1 1 
ATOM   2384 C CD2 . HIS B 1 12  ? 23.159  23.672  -11.816 0.84  45.93  ? 12   HIS B CD2 1 
ATOM   2385 C CE1 . HIS B 1 12  ? 25.221  23.306  -11.159 0.84  46.71  ? 12   HIS B CE1 1 
ATOM   2386 N NE2 . HIS B 1 12  ? 24.194  24.130  -11.036 0.84  46.29  ? 12   HIS B NE2 1 
ATOM   2387 N N   . GLN B 1 13  ? 21.712  21.934  -16.921 1.00  43.95  ? 13   GLN B N   1 
ATOM   2388 C CA  . GLN B 1 13  ? 21.133  21.216  -18.051 1.00  44.00  ? 13   GLN B CA  1 
ATOM   2389 C C   . GLN B 1 13  ? 22.161  20.829  -19.114 1.00  43.80  ? 13   GLN B C   1 
ATOM   2390 O O   . GLN B 1 13  ? 21.943  21.055  -20.313 1.00  44.37  ? 13   GLN B O   1 
ATOM   2391 C CB  . GLN B 1 13  ? 20.010  22.047  -18.700 1.00  44.13  ? 13   GLN B CB  1 
ATOM   2392 C CG  . GLN B 1 13  ? 18.979  22.627  -17.742 1.00  45.51  ? 13   GLN B CG  1 
ATOM   2393 C CD  . GLN B 1 13  ? 17.636  22.921  -18.420 1.00  48.40  ? 13   GLN B CD  1 
ATOM   2394 O OE1 . GLN B 1 13  ? 17.118  22.108  -19.192 1.00  50.20  ? 13   GLN B OE1 1 
ATOM   2395 N NE2 . GLN B 1 13  ? 17.048  24.068  -18.097 1.00  49.19  ? 13   GLN B NE2 1 
ATOM   2396 N N   . ASP B 1 14  ? 23.269  20.228  -18.699 0.87  43.35  ? 14   ASP B N   1 
ATOM   2397 C CA  . ASP B 1 14  ? 24.290  19.844  -19.667 0.87  43.09  ? 14   ASP B CA  1 
ATOM   2398 C C   . ASP B 1 14  ? 24.224  18.385  -20.064 0.87  42.46  ? 14   ASP B C   1 
ATOM   2399 O O   . ASP B 1 14  ? 24.323  18.066  -21.246 0.87  43.11  ? 14   ASP B O   1 
ATOM   2400 C CB  . ASP B 1 14  ? 25.694  20.193  -19.177 0.87  43.44  ? 14   ASP B CB  1 
ATOM   2401 C CG  . ASP B 1 14  ? 26.665  20.411  -20.327 0.87  45.18  ? 14   ASP B CG  1 
ATOM   2402 O OD1 . ASP B 1 14  ? 26.650  21.522  -20.908 0.87  47.27  ? 14   ASP B OD1 1 
ATOM   2403 O OD2 . ASP B 1 14  ? 27.441  19.482  -20.657 0.87  46.48  ? 14   ASP B OD2 1 
ATOM   2404 N N   . LEU B 1 15  ? 24.085  17.503  -19.077 1.00  41.79  ? 15   LEU B N   1 
ATOM   2405 C CA  . LEU B 1 15  ? 23.973  16.068  -19.323 1.00  41.09  ? 15   LEU B CA  1 
ATOM   2406 C C   . LEU B 1 15  ? 22.628  15.770  -19.993 1.00  40.76  ? 15   LEU B C   1 
ATOM   2407 O O   . LEU B 1 15  ? 22.554  14.959  -20.925 1.00  40.50  ? 15   LEU B O   1 
ATOM   2408 C CB  . LEU B 1 15  ? 24.099  15.295  -18.012 1.00  40.97  ? 15   LEU B CB  1 
ATOM   2409 C CG  . LEU B 1 15  ? 24.974  14.043  -17.875 1.00  41.03  ? 15   LEU B CG  1 
ATOM   2410 C CD1 . LEU B 1 15  ? 24.373  13.145  -16.780 1.00  40.35  ? 15   LEU B CD1 1 
ATOM   2411 C CD2 . LEU B 1 15  ? 25.173  13.264  -19.176 1.00  40.83  ? 15   LEU B CD2 1 
ATOM   2412 N N   . SER B 1 16  ? 21.585  16.444  -19.508 1.00  40.44  ? 16   SER B N   1 
ATOM   2413 C CA  . SER B 1 16  ? 20.239  16.403  -20.082 1.00  40.48  ? 16   SER B CA  1 
ATOM   2414 C C   . SER B 1 16  ? 20.244  16.789  -21.548 1.00  40.51  ? 16   SER B C   1 
ATOM   2415 O O   . SER B 1 16  ? 19.617  16.130  -22.374 1.00  41.00  ? 16   SER B O   1 
ATOM   2416 C CB  . SER B 1 16  ? 19.328  17.379  -19.344 1.00  40.77  ? 16   SER B CB  1 
ATOM   2417 O OG  . SER B 1 16  ? 18.922  16.874  -18.083 1.00  41.57  ? 16   SER B OG  1 
ATOM   2418 N N   . GLN B 1 17  ? 20.953  17.864  -21.874 1.00  40.56  ? 17   GLN B N   1 
ATOM   2419 C CA  . GLN B 1 17  ? 21.057  18.314  -23.258 1.00  40.40  ? 17   GLN B CA  1 
ATOM   2420 C C   . GLN B 1 17  ? 21.875  17.325  -24.065 1.00  39.87  ? 17   GLN B C   1 
ATOM   2421 O O   . GLN B 1 17  ? 21.489  16.973  -25.184 1.00  39.83  ? 17   GLN B O   1 
ATOM   2422 C CB  . GLN B 1 17  ? 21.674  19.711  -23.339 1.00  40.70  ? 17   GLN B CB  1 
ATOM   2423 C CG  . GLN B 1 17  ? 21.820  20.250  -24.754 1.00  41.67  ? 17   GLN B CG  1 
ATOM   2424 C CD  . GLN B 1 17  ? 20.503  20.725  -25.343 1.00  43.06  ? 17   GLN B CD  1 
ATOM   2425 O OE1 . GLN B 1 17  ? 19.660  21.286  -24.640 1.00  43.54  ? 17   GLN B OE1 1 
ATOM   2426 N NE2 . GLN B 1 17  ? 20.322  20.504  -26.645 1.00  43.83  ? 17   GLN B NE2 1 
ATOM   2427 N N   . LYS B 1 18  ? 22.998  16.884  -23.500 1.00  39.21  ? 18   LYS B N   1 
ATOM   2428 C CA  . LYS B 1 18  ? 23.827  15.875  -24.162 1.00  39.40  ? 18   LYS B CA  1 
ATOM   2429 C C   . LYS B 1 18  ? 23.035  14.596  -24.464 1.00  39.12  ? 18   LYS B C   1 
ATOM   2430 O O   . LYS B 1 18  ? 23.106  14.080  -25.572 1.00  39.00  ? 18   LYS B O   1 
ATOM   2431 C CB  . LYS B 1 18  ? 25.081  15.552  -23.345 1.00  39.63  ? 18   LYS B CB  1 
ATOM   2432 C CG  . LYS B 1 18  ? 26.286  16.431  -23.640 1.00  40.74  ? 18   LYS B CG  1 
ATOM   2433 C CD  . LYS B 1 18  ? 27.562  15.775  -23.113 1.00  43.11  ? 18   LYS B CD  1 
ATOM   2434 C CE  . LYS B 1 18  ? 28.799  16.643  -23.319 1.00  43.83  ? 18   LYS B CE  1 
ATOM   2435 N NZ  . LYS B 1 18  ? 30.051  15.950  -22.840 1.00  44.62  ? 18   LYS B NZ  1 
ATOM   2436 N N   . ILE B 1 19  ? 22.265  14.110  -23.484 1.00  38.92  ? 19   ILE B N   1 
ATOM   2437 C CA  . ILE B 1 19  ? 21.395  12.949  -23.682 1.00  38.53  ? 19   ILE B CA  1 
ATOM   2438 C C   . ILE B 1 19  ? 20.300  13.265  -24.713 1.00  38.25  ? 19   ILE B C   1 
ATOM   2439 O O   . ILE B 1 19  ? 20.076  12.488  -25.640 1.00  38.07  ? 19   ILE B O   1 
ATOM   2440 C CB  . ILE B 1 19  ? 20.780  12.429  -22.330 1.00  38.87  ? 19   ILE B CB  1 
ATOM   2441 C CG1 . ILE B 1 19  ? 21.885  11.985  -21.364 1.00  38.31  ? 19   ILE B CG1 1 
ATOM   2442 C CG2 . ILE B 1 19  ? 19.827  11.240  -22.580 1.00  38.60  ? 19   ILE B CG2 1 
ATOM   2443 C CD1 . ILE B 1 19  ? 21.452  11.868  -19.922 1.00  37.01  ? 19   ILE B CD1 1 
ATOM   2444 N N   . ALA B 1 20  ? 19.636  14.413  -24.550 1.00  37.95  ? 20   ALA B N   1 
ATOM   2445 C CA  . ALA B 1 20  ? 18.645  14.896  -25.528 1.00  37.71  ? 20   ALA B CA  1 
ATOM   2446 C C   . ALA B 1 20  ? 19.188  14.998  -26.975 1.00  37.44  ? 20   ALA B C   1 
ATOM   2447 O O   . ALA B 1 20  ? 18.495  14.629  -27.926 1.00  37.00  ? 20   ALA B O   1 
ATOM   2448 C CB  . ALA B 1 20  ? 18.071  16.231  -25.083 1.00  37.70  ? 20   ALA B CB  1 
ATOM   2449 N N   . ASP B 1 21  ? 20.414  15.507  -27.118 0.95  37.33  ? 21   ASP B N   1 
ATOM   2450 C CA  . ASP B 1 21  ? 21.077  15.636  -28.423 0.95  37.37  ? 21   ASP B CA  1 
ATOM   2451 C C   . ASP B 1 21  ? 21.205  14.277  -29.104 0.95  37.24  ? 21   ASP B C   1 
ATOM   2452 O O   . ASP B 1 21  ? 20.813  14.117  -30.261 0.95  36.69  ? 21   ASP B O   1 
ATOM   2453 C CB  . ASP B 1 21  ? 22.475  16.261  -28.275 0.95  37.53  ? 21   ASP B CB  1 
ATOM   2454 C CG  . ASP B 1 21  ? 22.444  17.774  -28.084 0.95  37.43  ? 21   ASP B CG  1 
ATOM   2455 O OD1 . ASP B 1 21  ? 21.396  18.408  -28.330 0.95  39.22  ? 21   ASP B OD1 1 
ATOM   2456 O OD2 . ASP B 1 21  ? 23.493  18.338  -27.707 0.95  36.09  ? 21   ASP B OD2 1 
ATOM   2457 N N   . ARG B 1 22  ? 21.733  13.299  -28.364 1.00  37.25  ? 22   ARG B N   1 
ATOM   2458 C CA  . ARG B 1 22  ? 22.025  11.964  -28.905 1.00  37.34  ? 22   ARG B CA  1 
ATOM   2459 C C   . ARG B 1 22  ? 20.777  11.188  -29.329 1.00  37.17  ? 22   ARG B C   1 
ATOM   2460 O O   . ARG B 1 22  ? 20.860  10.227  -30.096 1.00  36.97  ? 22   ARG B O   1 
ATOM   2461 C CB  . ARG B 1 22  ? 22.872  11.155  -27.920 1.00  37.23  ? 22   ARG B CB  1 
ATOM   2462 C CG  . ARG B 1 22  ? 24.190  11.848  -27.553 1.00  38.77  ? 22   ARG B CG  1 
ATOM   2463 C CD  . ARG B 1 22  ? 25.194  10.889  -26.908 1.00  40.97  ? 22   ARG B CD  1 
ATOM   2464 N NE  . ARG B 1 22  ? 25.974  10.143  -27.908 1.00  42.91  ? 22   ARG B NE  1 
ATOM   2465 C CZ  . ARG B 1 22  ? 27.293  10.219  -28.044 1.00  43.92  ? 22   ARG B CZ  1 
ATOM   2466 N NH1 . ARG B 1 22  ? 28.009  11.004  -27.236 1.00  44.02  ? 22   ARG B NH1 1 
ATOM   2467 N NH2 . ARG B 1 22  ? 27.899  9.491   -28.980 1.00  44.60  ? 22   ARG B NH2 1 
ATOM   2468 N N   . LEU B 1 23  ? 19.619  11.622  -28.838 1.00  37.26  ? 23   LEU B N   1 
ATOM   2469 C CA  . LEU B 1 23  ? 18.337  11.011  -29.208 1.00  37.00  ? 23   LEU B CA  1 
ATOM   2470 C C   . LEU B 1 23  ? 17.564  11.884  -30.203 1.00  36.91  ? 23   LEU B C   1 
ATOM   2471 O O   . LEU B 1 23  ? 16.433  11.575  -30.567 1.00  37.04  ? 23   LEU B O   1 
ATOM   2472 C CB  . LEU B 1 23  ? 17.495  10.725  -27.958 1.00  36.84  ? 23   LEU B CB  1 
ATOM   2473 C CG  . LEU B 1 23  ? 18.071  9.748   -26.906 1.00  36.84  ? 23   LEU B CG  1 
ATOM   2474 C CD1 . LEU B 1 23  ? 17.357  9.973   -25.554 1.00  36.46  ? 23   LEU B CD1 1 
ATOM   2475 C CD2 . LEU B 1 23  ? 17.942  8.264   -27.344 1.00  36.80  ? 23   LEU B CD2 1 
ATOM   2476 N N   . GLY B 1 24  ? 18.186  12.974  -30.644 1.00  36.88  ? 24   GLY B N   1 
ATOM   2477 C CA  . GLY B 1 24  ? 17.563  13.894  -31.599 1.00  36.84  ? 24   GLY B CA  1 
ATOM   2478 C C   . GLY B 1 24  ? 16.296  14.537  -31.069 1.00  36.99  ? 24   GLY B C   1 
ATOM   2479 O O   . GLY B 1 24  ? 15.264  14.577  -31.758 1.00  37.12  ? 24   GLY B O   1 
ATOM   2480 N N   . LEU B 1 25  ? 16.377  15.049  -29.840 1.00  36.80  ? 25   LEU B N   1 
ATOM   2481 C CA  . LEU B 1 25  ? 15.231  15.654  -29.164 1.00  36.64  ? 25   LEU B CA  1 
ATOM   2482 C C   . LEU B 1 25  ? 15.614  16.963  -28.506 1.00  36.76  ? 25   LEU B C   1 
ATOM   2483 O O   . LEU B 1 25  ? 16.787  17.193  -28.204 1.00  37.15  ? 25   LEU B O   1 
ATOM   2484 C CB  . LEU B 1 25  ? 14.682  14.716  -28.073 1.00  36.37  ? 25   LEU B CB  1 
ATOM   2485 C CG  . LEU B 1 25  ? 14.051  13.377  -28.456 1.00  36.58  ? 25   LEU B CG  1 
ATOM   2486 C CD1 . LEU B 1 25  ? 14.027  12.470  -27.234 1.00  35.79  ? 25   LEU B CD1 1 
ATOM   2487 C CD2 . LEU B 1 25  ? 12.655  13.543  -29.035 1.00  36.35  ? 25   LEU B CD2 1 
ATOM   2488 N N   . GLU B 1 26  ? 14.617  17.809  -28.269 0.89  36.81  ? 26   GLU B N   1 
ATOM   2489 C CA  . GLU B 1 26  ? 14.785  18.961  -27.397 0.89  37.44  ? 26   GLU B CA  1 
ATOM   2490 C C   . GLU B 1 26  ? 14.374  18.588  -25.976 0.89  37.16  ? 26   GLU B C   1 
ATOM   2491 O O   . GLU B 1 26  ? 13.608  17.647  -25.774 0.89  37.12  ? 26   GLU B O   1 
ATOM   2492 C CB  . GLU B 1 26  ? 13.940  20.139  -27.877 0.89  37.67  ? 26   GLU B CB  1 
ATOM   2493 C CG  . GLU B 1 26  ? 14.421  20.797  -29.143 0.89  39.53  ? 26   GLU B CG  1 
ATOM   2494 C CD  . GLU B 1 26  ? 13.770  22.144  -29.349 0.89  44.14  ? 26   GLU B CD  1 
ATOM   2495 O OE1 . GLU B 1 26  ? 12.782  22.440  -28.616 0.89  45.58  ? 26   GLU B OE1 1 
ATOM   2496 O OE2 . GLU B 1 26  ? 14.246  22.902  -30.237 0.89  46.09  ? 26   GLU B OE2 1 
ATOM   2497 N N   . LEU B 1 27  ? 14.890  19.317  -24.990 1.00  37.13  ? 27   LEU B N   1 
ATOM   2498 C CA  . LEU B 1 27  ? 14.426  19.140  -23.620 1.00  37.25  ? 27   LEU B CA  1 
ATOM   2499 C C   . LEU B 1 27  ? 13.066  19.798  -23.504 1.00  37.50  ? 27   LEU B C   1 
ATOM   2500 O O   . LEU B 1 27  ? 12.824  20.833  -24.145 1.00  37.48  ? 27   LEU B O   1 
ATOM   2501 C CB  . LEU B 1 27  ? 15.399  19.750  -22.611 1.00  36.99  ? 27   LEU B CB  1 
ATOM   2502 C CG  . LEU B 1 27  ? 16.709  19.000  -22.384 1.00  36.96  ? 27   LEU B CG  1 
ATOM   2503 C CD1 . LEU B 1 27  ? 17.628  19.885  -21.565 1.00  37.15  ? 27   LEU B CD1 1 
ATOM   2504 C CD2 . LEU B 1 27  ? 16.482  17.655  -21.690 1.00  35.52  ? 27   LEU B CD2 1 
ATOM   2505 N N   . GLY B 1 28  ? 12.185  19.175  -22.716 1.00  37.43  ? 28   GLY B N   1 
ATOM   2506 C CA  . GLY B 1 28  ? 10.842  19.686  -22.476 1.00  37.85  ? 28   GLY B CA  1 
ATOM   2507 C C   . GLY B 1 28  ? 10.860  20.947  -21.634 1.00  38.44  ? 28   GLY B C   1 
ATOM   2508 O O   . GLY B 1 28  ? 11.723  21.113  -20.743 1.00  38.78  ? 28   GLY B O   1 
ATOM   2509 N N   . LYS B 1 29  ? 9.918   21.848  -21.934 0.30  39.15  ? 29   LYS B N   1 
ATOM   2510 C CA  . LYS B 1 29  ? 9.862   23.135  -21.250 0.30  40.22  ? 29   LYS B CA  1 
ATOM   2511 C C   . LYS B 1 29  ? 9.427   22.990  -19.779 0.30  40.72  ? 29   LYS B C   1 
ATOM   2512 O O   . LYS B 1 29  ? 8.377   22.379  -19.466 0.30  40.79  ? 29   LYS B O   1 
ATOM   2513 C CB  . LYS B 1 29  ? 8.955   24.115  -22.017 0.30  40.18  ? 29   LYS B CB  1 
ATOM   2514 C CG  . LYS B 1 29  ? 9.081   24.007  -23.553 0.30  41.82  ? 29   LYS B CG  1 
ATOM   2515 C CD  . LYS B 1 29  ? 8.727   25.317  -24.277 0.30  44.36  ? 29   LYS B CD  1 
ATOM   2516 C CE  . LYS B 1 29  ? 7.943   25.075  -25.592 0.30  45.39  ? 29   LYS B CE  1 
ATOM   2517 N NZ  . LYS B 1 29  ? 8.766   24.490  -26.715 0.30  47.48  ? 29   LYS B NZ  1 
ATOM   2518 N N   . VAL B 1 30  ? 10.275  23.518  -18.888 1.00  41.46  ? 30   VAL B N   1 
ATOM   2519 C CA  . VAL B 1 30  ? 9.956   23.582  -17.465 1.00  42.38  ? 30   VAL B CA  1 
ATOM   2520 C C   . VAL B 1 30  ? 10.058  25.027  -16.975 1.00  43.15  ? 30   VAL B C   1 
ATOM   2521 O O   . VAL B 1 30  ? 11.071  25.692  -17.191 1.00  43.29  ? 30   VAL B O   1 
ATOM   2522 C CB  . VAL B 1 30  ? 10.895  22.699  -16.598 1.00  42.24  ? 30   VAL B CB  1 
ATOM   2523 C CG1 . VAL B 1 30  ? 10.171  22.231  -15.353 1.00  41.23  ? 30   VAL B CG1 1 
ATOM   2524 C CG2 . VAL B 1 30  ? 11.411  21.509  -17.382 1.00  41.98  ? 30   VAL B CG2 1 
ATOM   2525 N N   . VAL B 1 31  ? 9.000   25.504  -16.323 1.00  44.16  ? 31   VAL B N   1 
ATOM   2526 C CA  . VAL B 1 31  ? 9.007   26.815  -15.678 1.00  45.11  ? 31   VAL B CA  1 
ATOM   2527 C C   . VAL B 1 31  ? 9.317   26.587  -14.206 1.00  45.69  ? 31   VAL B C   1 
ATOM   2528 O O   . VAL B 1 31  ? 8.452   26.153  -13.440 1.00  46.06  ? 31   VAL B O   1 
ATOM   2529 C CB  . VAL B 1 31  ? 7.656   27.554  -15.848 1.00  45.36  ? 31   VAL B CB  1 
ATOM   2530 C CG1 . VAL B 1 31  ? 7.664   28.888  -15.074 1.00  45.73  ? 31   VAL B CG1 1 
ATOM   2531 C CG2 . VAL B 1 31  ? 7.353   27.803  -17.368 1.00  46.01  ? 31   VAL B CG2 1 
ATOM   2532 N N   . THR B 1 32  ? 10.561  26.866  -13.819 0.81  46.20  ? 32   THR B N   1 
ATOM   2533 C CA  . THR B 1 32  ? 11.032  26.548  -12.478 0.81  46.72  ? 32   THR B CA  1 
ATOM   2534 C C   . THR B 1 32  ? 11.937  27.599  -11.843 0.81  47.05  ? 32   THR B C   1 
ATOM   2535 O O   . THR B 1 32  ? 13.146  27.643  -12.112 0.81  47.54  ? 32   THR B O   1 
ATOM   2536 C CB  . THR B 1 32  ? 11.740  25.160  -12.431 0.81  46.78  ? 32   THR B CB  1 
ATOM   2537 O OG1 . THR B 1 32  ? 12.441  25.015  -11.183 0.81  47.06  ? 32   THR B OG1 1 
ATOM   2538 C CG2 . THR B 1 32  ? 12.718  25.011  -13.580 0.81  47.19  ? 32   THR B CG2 1 
ATOM   2539 N N   . LYS B 1 33  ? 11.345  28.439  -10.998 0.21  47.08  ? 33   LYS B N   1 
ATOM   2540 C CA  . LYS B 1 33  ? 12.106  29.343  -10.143 0.21  47.20  ? 33   LYS B CA  1 
ATOM   2541 C C   . LYS B 1 33  ? 11.905  28.926  -8.690  0.21  47.31  ? 33   LYS B C   1 
ATOM   2542 O O   . LYS B 1 33  ? 11.008  28.141  -8.382  0.21  47.26  ? 33   LYS B O   1 
ATOM   2543 C CB  . LYS B 1 33  ? 11.682  30.798  -10.360 0.21  47.21  ? 33   LYS B CB  1 
ATOM   2544 C CG  . LYS B 1 33  ? 10.264  31.120  -9.911  0.21  47.18  ? 33   LYS B CG  1 
ATOM   2545 C CD  . LYS B 1 33  ? 9.832   32.490  -10.412 0.21  47.27  ? 33   LYS B CD  1 
ATOM   2546 C CE  . LYS B 1 33  ? 8.365   32.756  -10.100 0.21  47.44  ? 33   LYS B CE  1 
ATOM   2547 N NZ  . LYS B 1 33  ? 7.926   34.094  -10.587 0.21  46.96  ? 33   LYS B NZ  1 
ATOM   2548 N N   . LYS B 1 34  ? 12.748  29.442  -7.802  1.00  47.57  ? 34   LYS B N   1 
ATOM   2549 C CA  . LYS B 1 34  ? 12.667  29.101  -6.389  1.00  47.81  ? 34   LYS B CA  1 
ATOM   2550 C C   . LYS B 1 34  ? 12.061  30.253  -5.613  1.00  47.66  ? 34   LYS B C   1 
ATOM   2551 O O   . LYS B 1 34  ? 12.489  31.409  -5.774  1.00  47.77  ? 34   LYS B O   1 
ATOM   2552 C CB  . LYS B 1 34  ? 14.048  28.756  -5.814  1.00  47.80  ? 34   LYS B CB  1 
ATOM   2553 C CG  . LYS B 1 34  ? 14.616  27.416  -6.286  1.00  49.32  ? 34   LYS B CG  1 
ATOM   2554 C CD  . LYS B 1 34  ? 15.342  26.667  -5.148  1.00  51.16  ? 34   LYS B CD  1 
ATOM   2555 C CE  . LYS B 1 34  ? 16.626  27.380  -4.691  1.00  51.69  ? 34   LYS B CE  1 
ATOM   2556 N NZ  . LYS B 1 34  ? 17.279  26.681  -3.541  1.00  51.82  ? 34   LYS B NZ  1 
ATOM   2557 N N   . PHE B 1 35  ? 11.025  29.931  -4.786  0.010 47.47  ? 35   PHE B N   1 
ATOM   2558 C CA  . PHE B 1 35  ? 10.451  30.912  -3.882  0.010 47.28  ? 35   PHE B CA  1 
ATOM   2559 C C   . PHE B 1 35  ? 11.561  31.404  -2.955  0.010 47.19  ? 35   PHE B C   1 
ATOM   2560 O O   . PHE B 1 35  ? 12.334  30.603  -2.402  0.010 47.17  ? 35   PHE B O   1 
ATOM   2561 C CB  . PHE B 1 35  ? 9.278   30.312  -3.098  0.010 47.27  ? 35   PHE B CB  1 
ATOM   2562 C CG  . PHE B 1 35  ? 8.028   30.138  -3.922  0.010 47.21  ? 35   PHE B CG  1 
ATOM   2563 C CD1 . PHE B 1 35  ? 7.510   28.878  -4.169  0.010 47.17  ? 35   PHE B CD1 1 
ATOM   2564 C CD2 . PHE B 1 35  ? 7.382   31.240  -4.462  0.010 47.17  ? 35   PHE B CD2 1 
ATOM   2565 C CE1 . PHE B 1 35  ? 6.366   28.719  -4.931  0.010 47.14  ? 35   PHE B CE1 1 
ATOM   2566 C CE2 . PHE B 1 35  ? 6.239   31.087  -5.225  0.010 47.14  ? 35   PHE B CE2 1 
ATOM   2567 C CZ  . PHE B 1 35  ? 5.730   29.825  -5.459  0.010 47.13  ? 35   PHE B CZ  1 
ATOM   2568 N N   . SER B 1 36  ? 11.698  32.736  -2.834  0.010 47.09  ? 36   SER B N   1 
ATOM   2569 C CA  . SER B 1 36  ? 12.747  33.313  -2.008  0.010 47.01  ? 36   SER B CA  1 
ATOM   2570 C C   . SER B 1 36  ? 12.793  32.551  -0.692  0.010 46.97  ? 36   SER B C   1 
ATOM   2571 O O   . SER B 1 36  ? 13.790  32.586  0.030   0.010 46.96  ? 36   SER B O   1 
ATOM   2572 C CB  . SER B 1 36  ? 12.491  34.801  -1.769  0.010 47.01  ? 36   SER B CB  1 
ATOM   2573 O OG  . SER B 1 36  ? 13.529  35.383  -1.001  0.010 47.00  ? 36   SER B OG  1 
ATOM   2574 N N   . ASN B 1 37  ? 11.699  31.857  -0.397  0.010 46.94  ? 37   ASN B N   1 
ATOM   2575 C CA  . ASN B 1 37  ? 11.593  31.044  0.806   0.010 46.91  ? 37   ASN B CA  1 
ATOM   2576 C C   . ASN B 1 37  ? 12.396  29.754  0.696   0.010 46.91  ? 37   ASN B C   1 
ATOM   2577 O O   . ASN B 1 37  ? 12.486  28.986  1.653   0.010 46.91  ? 37   ASN B O   1 
ATOM   2578 C CB  . ASN B 1 37  ? 10.128  30.704  1.081   0.010 46.90  ? 37   ASN B CB  1 
ATOM   2579 C CG  . ASN B 1 37  ? 9.556   29.738  0.061   0.010 46.88  ? 37   ASN B CG  1 
ATOM   2580 O OD1 . ASN B 1 37  ? 10.216  29.390  -0.919  0.010 46.86  ? 37   ASN B OD1 1 
ATOM   2581 N ND2 . ASN B 1 37  ? 8.324   29.300  0.287   0.010 46.87  ? 37   ASN B ND2 1 
ATOM   2582 N N   . GLN B 1 38  ? 12.973  29.514  -0.476  0.010 46.93  ? 38   GLN B N   1 
ATOM   2583 C CA  . GLN B 1 38  ? 13.759  28.308  -0.698  0.010 46.96  ? 38   GLN B CA  1 
ATOM   2584 C C   . GLN B 1 38  ? 12.848  27.155  -1.124  0.010 47.02  ? 38   GLN B C   1 
ATOM   2585 O O   . GLN B 1 38  ? 13.268  25.953  -1.125  0.010 47.00  ? 38   GLN B O   1 
ATOM   2586 C CB  . GLN B 1 38  ? 14.446  27.867  0.593   0.010 46.95  ? 38   GLN B CB  1 
ATOM   2587 C CG  . GLN B 1 38  ? 14.764  28.996  1.546   0.010 46.92  ? 38   GLN B CG  1 
ATOM   2588 C CD  . GLN B 1 38  ? 15.593  30.077  0.898   0.010 46.90  ? 38   GLN B CD  1 
ATOM   2589 O OE1 . GLN B 1 38  ? 15.945  31.070  1.535   0.010 46.89  ? 38   GLN B OE1 1 
ATOM   2590 N NE2 . GLN B 1 38  ? 15.915  29.893  -0.377  0.010 46.92  ? 38   GLN B NE2 1 
ATOM   2591 N N   . GLU B 1 39  ? 11.602  27.522  -1.477  0.88  47.04  ? 39   GLU B N   1 
ATOM   2592 C CA  . GLU B 1 39  ? 10.660  26.516  -1.980  0.88  47.36  ? 39   GLU B CA  1 
ATOM   2593 C C   . GLU B 1 39  ? 10.863  26.467  -3.474  0.88  47.46  ? 39   GLU B C   1 
ATOM   2594 O O   . GLU B 1 39  ? 11.214  27.476  -4.080  0.88  47.54  ? 39   GLU B O   1 
ATOM   2595 C CB  . GLU B 1 39  ? 9.213   26.925  -1.729  0.88  47.36  ? 39   GLU B CB  1 
ATOM   2596 C CG  . GLU B 1 39  ? 8.700   26.639  -0.353  0.88  47.56  ? 39   GLU B CG  1 
ATOM   2597 C CD  . GLU B 1 39  ? 7.191   26.635  -0.290  0.88  48.11  ? 39   GLU B CD  1 
ATOM   2598 O OE1 . GLU B 1 39  ? 6.528   26.553  -1.361  0.88  47.47  ? 39   GLU B OE1 1 
ATOM   2599 O OE2 . GLU B 1 39  ? 6.665   26.708  0.846   0.88  49.50  ? 39   GLU B OE2 1 
ATOM   2600 N N   . THR B 1 40  ? 10.686  25.299  -4.048  1.00  47.58  ? 40   THR B N   1 
ATOM   2601 C CA  . THR B 1 40  ? 10.829  25.181  -5.457  1.00  47.67  ? 40   THR B CA  1 
ATOM   2602 C C   . THR B 1 40  ? 9.489   25.117  -6.068  1.00  47.71  ? 40   THR B C   1 
ATOM   2603 O O   . THR B 1 40  ? 8.640   24.435  -5.602  1.00  47.10  ? 40   THR B O   1 
ATOM   2604 C CB  . THR B 1 40  ? 11.601  23.963  -5.840  1.00  47.89  ? 40   THR B CB  1 
ATOM   2605 O OG1 . THR B 1 40  ? 12.238  23.452  -4.690  1.00  47.88  ? 40   THR B OG1 1 
ATOM   2606 C CG2 . THR B 1 40  ? 12.649  24.325  -6.816  1.00  47.87  ? 40   THR B CG2 1 
ATOM   2607 N N   . CYS B 1 41  ? 9.329   25.852  -7.142  1.00  47.75  ? 41   CYS B N   1 
ATOM   2608 C CA  . CYS B 1 41  ? 8.134   25.827  -7.907  1.00  47.92  ? 41   CYS B CA  1 
ATOM   2609 C C   . CYS B 1 41  ? 8.427   25.352  -9.283  1.00  47.36  ? 41   CYS B C   1 
ATOM   2610 O O   . CYS B 1 41  ? 9.204   25.950  -9.967  1.00  47.61  ? 41   CYS B O   1 
ATOM   2611 C CB  . CYS B 1 41  ? 7.627   27.219  -8.007  1.00  48.45  ? 41   CYS B CB  1 
ATOM   2612 S SG  . CYS B 1 41  ? 6.228   27.506  -7.008  1.00  52.43  ? 41   CYS B SG  1 
ATOM   2613 N N   . VAL B 1 42  ? 7.753   24.296  -9.688  1.00  46.56  ? 42   VAL B N   1 
ATOM   2614 C CA  . VAL B 1 42  ? 7.904   23.738  -11.007 1.00  45.95  ? 42   VAL B CA  1 
ATOM   2615 C C   . VAL B 1 42  ? 6.612   23.803  -11.822 1.00  45.37  ? 42   VAL B C   1 
ATOM   2616 O O   . VAL B 1 42  ? 5.545   23.644  -11.294 1.00  45.32  ? 42   VAL B O   1 
ATOM   2617 C CB  . VAL B 1 42  ? 8.370   22.320  -10.907 1.00  45.85  ? 42   VAL B CB  1 
ATOM   2618 C CG1 . VAL B 1 42  ? 8.047   21.580  -12.111 1.00  45.60  ? 42   VAL B CG1 1 
ATOM   2619 C CG2 . VAL B 1 42  ? 9.805   22.266  -10.653 1.00  46.65  ? 42   VAL B CG2 1 
ATOM   2620 N N   . GLU B 1 43  ? 6.719   24.092  -13.116 0.010 44.54  ? 43   GLU B N   1 
ATOM   2621 C CA  . GLU B 1 43  ? 5.581   23.986  -14.006 0.010 43.76  ? 43   GLU B CA  1 
ATOM   2622 C C   . GLU B 1 43  ? 6.099   23.177  -15.191 0.010 43.26  ? 43   GLU B C   1 
ATOM   2623 O O   . GLU B 1 43  ? 7.271   23.323  -15.596 0.010 43.17  ? 43   GLU B O   1 
ATOM   2624 C CB  . GLU B 1 43  ? 5.088   25.402  -14.422 0.010 43.78  ? 43   GLU B CB  1 
ATOM   2625 C CG  . GLU B 1 43  ? 3.683   25.405  -15.049 0.010 43.69  ? 43   GLU B CG  1 
ATOM   2626 C CD  . GLU B 1 43  ? 3.075   26.800  -15.109 0.010 43.64  ? 43   GLU B CD  1 
ATOM   2627 O OE1 . GLU B 1 43  ? 1.993   26.952  -15.717 0.010 43.61  ? 43   GLU B OE1 1 
ATOM   2628 O OE2 . GLU B 1 43  ? 3.676   27.741  -14.548 0.010 43.62  ? 43   GLU B OE2 1 
ATOM   2629 N N   . ILE B 1 44  ? 5.236   22.290  -15.700 1.00  42.55  ? 44   ILE B N   1 
ATOM   2630 C CA  . ILE B 1 44  ? 5.567   21.508  -16.890 1.00  42.24  ? 44   ILE B CA  1 
ATOM   2631 C C   . ILE B 1 44  ? 4.924   22.237  -18.060 1.00  41.90  ? 44   ILE B C   1 
ATOM   2632 O O   . ILE B 1 44  ? 3.702   22.238  -18.224 1.00  41.57  ? 44   ILE B O   1 
ATOM   2633 C CB  . ILE B 1 44  ? 5.034   20.048  -16.809 1.00  42.41  ? 44   ILE B CB  1 
ATOM   2634 C CG1 . ILE B 1 44  ? 5.571   19.322  -15.561 1.00  43.00  ? 44   ILE B CG1 1 
ATOM   2635 C CG2 . ILE B 1 44  ? 5.371   19.268  -18.083 1.00  42.31  ? 44   ILE B CG2 1 
ATOM   2636 C CD1 . ILE B 1 44  ? 7.072   18.968  -15.605 1.00  42.78  ? 44   ILE B CD1 1 
ATOM   2637 N N   . GLY B 1 45  ? 5.755   22.878  -18.869 1.00  41.71  ? 45   GLY B N   1 
ATOM   2638 C CA  . GLY B 1 45  ? 5.262   23.782  -19.901 1.00  41.57  ? 45   GLY B CA  1 
ATOM   2639 C C   . GLY B 1 45  ? 4.725   23.096  -21.138 1.00  41.36  ? 45   GLY B C   1 
ATOM   2640 O O   . GLY B 1 45  ? 4.782   23.659  -22.226 1.00  42.03  ? 45   GLY B O   1 
ATOM   2641 N N   . GLU B 1 46  ? 4.203   21.884  -20.972 1.00  40.77  ? 46   GLU B N   1 
ATOM   2642 C CA  . GLU B 1 46  ? 3.626   21.114  -22.063 1.00  40.03  ? 46   GLU B CA  1 
ATOM   2643 C C   . GLU B 1 46  ? 2.950   19.852  -21.559 1.00  39.26  ? 46   GLU B C   1 
ATOM   2644 O O   . GLU B 1 46  ? 3.307   19.328  -20.496 1.00  38.98  ? 46   GLU B O   1 
ATOM   2645 C CB  . GLU B 1 46  ? 4.685   20.737  -23.097 1.00  40.49  ? 46   GLU B CB  1 
ATOM   2646 C CG  . GLU B 1 46  ? 5.962   20.144  -22.532 1.00  42.60  ? 46   GLU B CG  1 
ATOM   2647 C CD  . GLU B 1 46  ? 7.051   20.065  -23.582 1.00  45.86  ? 46   GLU B CD  1 
ATOM   2648 O OE1 . GLU B 1 46  ? 6.957   19.199  -24.482 1.00  47.13  ? 46   GLU B OE1 1 
ATOM   2649 O OE2 . GLU B 1 46  ? 7.998   20.882  -23.517 1.00  47.78  ? 46   GLU B OE2 1 
ATOM   2650 N N   . SER B 1 47  ? 1.979   19.371  -22.339 1.00  37.94  ? 47   SER B N   1 
ATOM   2651 C CA  . SER B 1 47  ? 1.309   18.114  -22.073 1.00  36.64  ? 47   SER B CA  1 
ATOM   2652 C C   . SER B 1 47  ? 2.322   16.979  -21.998 1.00  36.00  ? 47   SER B C   1 
ATOM   2653 O O   . SER B 1 47  ? 3.321   16.979  -22.716 1.00  36.25  ? 47   SER B O   1 
ATOM   2654 C CB  . SER B 1 47  ? 0.290   17.833  -23.165 1.00  36.71  ? 47   SER B CB  1 
ATOM   2655 O OG  . SER B 1 47  ? -0.541  16.723  -22.835 1.00  37.64  ? 47   SER B OG  1 
ATOM   2656 N N   . VAL B 1 48  ? 2.079   16.035  -21.095 1.00  35.11  ? 48   VAL B N   1 
ATOM   2657 C CA  . VAL B 1 48  ? 2.848   14.790  -21.031 1.00  34.02  ? 48   VAL B CA  1 
ATOM   2658 C C   . VAL B 1 48  ? 1.893   13.602  -21.078 1.00  33.47  ? 48   VAL B C   1 
ATOM   2659 O O   . VAL B 1 48  ? 2.279   12.474  -20.817 1.00  33.18  ? 48   VAL B O   1 
ATOM   2660 C CB  . VAL B 1 48  ? 3.763   14.711  -19.773 1.00  33.97  ? 48   VAL B CB  1 
ATOM   2661 C CG1 . VAL B 1 48  ? 4.797   15.819  -19.800 1.00  34.03  ? 48   VAL B CG1 1 
ATOM   2662 C CG2 . VAL B 1 48  ? 2.949   14.754  -18.466 1.00  33.84  ? 48   VAL B CG2 1 
ATOM   2663 N N   . ARG B 1 49  ? 0.647   13.878  -21.447 1.00  33.24  ? 49   ARG B N   1 
ATOM   2664 C CA  . ARG B 1 49  ? -0.438  12.898  -21.405 1.00  32.95  ? 49   ARG B CA  1 
ATOM   2665 C C   . ARG B 1 49  ? -0.143  11.648  -22.238 1.00  32.61  ? 49   ARG B C   1 
ATOM   2666 O O   . ARG B 1 49  ? 0.022   11.727  -23.438 1.00  32.69  ? 49   ARG B O   1 
ATOM   2667 C CB  . ARG B 1 49  ? -1.747  13.557  -21.846 1.00  32.54  ? 49   ARG B CB  1 
ATOM   2668 C CG  . ARG B 1 49  ? -2.977  12.776  -21.465 1.00  32.26  ? 49   ARG B CG  1 
ATOM   2669 C CD  . ARG B 1 49  ? -4.249  13.534  -21.754 1.00  31.41  ? 49   ARG B CD  1 
ATOM   2670 N NE  . ARG B 1 49  ? -4.431  14.641  -20.825 1.00  32.54  ? 49   ARG B NE  1 
ATOM   2671 C CZ  . ARG B 1 49  ? -5.021  14.543  -19.635 1.00  34.26  ? 49   ARG B CZ  1 
ATOM   2672 N NH1 . ARG B 1 49  ? -5.503  13.373  -19.211 1.00  36.03  ? 49   ARG B NH1 1 
ATOM   2673 N NH2 . ARG B 1 49  ? -5.128  15.617  -18.862 1.00  32.91  ? 49   ARG B NH2 1 
ATOM   2674 N N   . GLY B 1 50  ? -0.058  10.499  -21.580 1.00  32.66  ? 50   GLY B N   1 
ATOM   2675 C CA  . GLY B 1 50  ? 0.214   9.229   -22.261 1.00  32.99  ? 50   GLY B CA  1 
ATOM   2676 C C   . GLY B 1 50  ? 1.599   9.152   -22.885 1.00  33.23  ? 50   GLY B C   1 
ATOM   2677 O O   . GLY B 1 50  ? 1.812   8.447   -23.878 1.00  33.39  ? 50   GLY B O   1 
ATOM   2678 N N   . GLU B 1 51  ? 2.544   9.885   -22.301 0.85  33.08  ? 51   GLU B N   1 
ATOM   2679 C CA  . GLU B 1 51  ? 3.889   9.963   -22.847 0.85  32.96  ? 51   GLU B CA  1 
ATOM   2680 C C   . GLU B 1 51  ? 4.856   9.263   -21.920 0.85  32.60  ? 51   GLU B C   1 
ATOM   2681 O O   . GLU B 1 51  ? 4.632   9.203   -20.712 0.85  31.67  ? 51   GLU B O   1 
ATOM   2682 C CB  . GLU B 1 51  ? 4.305   11.419  -23.033 0.85  32.91  ? 51   GLU B CB  1 
ATOM   2683 C CG  . GLU B 1 51  ? 3.385   12.174  -23.961 0.85  34.06  ? 51   GLU B CG  1 
ATOM   2684 C CD  . GLU B 1 51  ? 4.091   12.745  -25.151 0.85  35.36  ? 51   GLU B CD  1 
ATOM   2685 O OE1 . GLU B 1 51  ? 4.530   11.965  -26.041 0.85  35.07  ? 51   GLU B OE1 1 
ATOM   2686 O OE2 . GLU B 1 51  ? 4.205   13.997  -25.185 0.85  37.08  ? 51   GLU B OE2 1 
ATOM   2687 N N   . ASP B 1 52  ? 5.921   8.732   -22.516 1.00  32.63  ? 52   ASP B N   1 
ATOM   2688 C CA  . ASP B 1 52  ? 6.977   8.025   -21.807 1.00  32.78  ? 52   ASP B CA  1 
ATOM   2689 C C   . ASP B 1 52  ? 8.004   9.071   -21.361 1.00  32.29  ? 52   ASP B C   1 
ATOM   2690 O O   . ASP B 1 52  ? 8.876   9.481   -22.146 1.00  32.65  ? 52   ASP B O   1 
ATOM   2691 C CB  . ASP B 1 52  ? 7.600   6.995   -22.750 1.00  33.14  ? 52   ASP B CB  1 
ATOM   2692 C CG  . ASP B 1 52  ? 8.476   5.990   -22.037 1.00  35.49  ? 52   ASP B CG  1 
ATOM   2693 O OD1 . ASP B 1 52  ? 8.337   5.821   -20.809 1.00  36.48  ? 52   ASP B OD1 1 
ATOM   2694 O OD2 . ASP B 1 52  ? 9.303   5.342   -22.725 1.00  38.78  ? 52   ASP B OD2 1 
ATOM   2695 N N   . VAL B 1 53  ? 7.874   9.515   -20.112 1.00  31.31  ? 53   VAL B N   1 
ATOM   2696 C CA  . VAL B 1 53  ? 8.656   10.633  -19.573 1.00  30.79  ? 53   VAL B CA  1 
ATOM   2697 C C   . VAL B 1 53  ? 9.979   10.185  -18.901 1.00  30.45  ? 53   VAL B C   1 
ATOM   2698 O O   . VAL B 1 53  ? 10.029  9.165   -18.212 1.00  30.65  ? 53   VAL B O   1 
ATOM   2699 C CB  . VAL B 1 53  ? 7.796   11.505  -18.577 1.00  30.73  ? 53   VAL B CB  1 
ATOM   2700 C CG1 . VAL B 1 53  ? 8.574   12.713  -18.054 1.00  29.35  ? 53   VAL B CG1 1 
ATOM   2701 C CG2 . VAL B 1 53  ? 6.500   11.980  -19.227 1.00  30.68  ? 53   VAL B CG2 1 
ATOM   2702 N N   . TYR B 1 54  ? 11.039  10.961  -19.115 1.00  29.82  ? 54   TYR B N   1 
ATOM   2703 C CA  . TYR B 1 54  ? 12.335  10.738  -18.463 1.00  29.14  ? 54   TYR B CA  1 
ATOM   2704 C C   . TYR B 1 54  ? 12.851  11.996  -17.790 1.00  29.31  ? 54   TYR B C   1 
ATOM   2705 O O   . TYR B 1 54  ? 13.058  13.024  -18.432 1.00  28.91  ? 54   TYR B O   1 
ATOM   2706 C CB  . TYR B 1 54  ? 13.373  10.218  -19.479 1.00  28.71  ? 54   TYR B CB  1 
ATOM   2707 C CG  . TYR B 1 54  ? 13.010  8.866   -20.011 1.00  25.12  ? 54   TYR B CG  1 
ATOM   2708 C CD1 . TYR B 1 54  ? 12.072  8.725   -21.031 1.00  23.48  ? 54   TYR B CD1 1 
ATOM   2709 C CD2 . TYR B 1 54  ? 13.570  7.719   -19.460 1.00  22.54  ? 54   TYR B CD2 1 
ATOM   2710 C CE1 . TYR B 1 54  ? 11.720  7.457   -21.510 1.00  22.70  ? 54   TYR B CE1 1 
ATOM   2711 C CE2 . TYR B 1 54  ? 13.227  6.454   -19.916 1.00  20.78  ? 54   TYR B CE2 1 
ATOM   2712 C CZ  . TYR B 1 54  ? 12.302  6.337   -20.938 1.00  21.83  ? 54   TYR B CZ  1 
ATOM   2713 O OH  . TYR B 1 54  ? 11.957  5.108   -21.386 1.00  21.61  ? 54   TYR B OH  1 
ATOM   2714 N N   . ILE B 1 55  ? 13.068  11.919  -16.482 1.00  30.50  ? 55   ILE B N   1 
ATOM   2715 C CA  . ILE B 1 55  ? 13.591  13.087  -15.755 1.00  31.19  ? 55   ILE B CA  1 
ATOM   2716 C C   . ILE B 1 55  ? 15.003  12.860  -15.235 1.00  31.92  ? 55   ILE B C   1 
ATOM   2717 O O   . ILE B 1 55  ? 15.243  11.937  -14.464 1.00  31.89  ? 55   ILE B O   1 
ATOM   2718 C CB  . ILE B 1 55  ? 12.618  13.578  -14.656 1.00  31.07  ? 55   ILE B CB  1 
ATOM   2719 C CG1 . ILE B 1 55  ? 11.217  13.758  -15.260 1.00  30.06  ? 55   ILE B CG1 1 
ATOM   2720 C CG2 . ILE B 1 55  ? 13.118  14.897  -14.032 1.00  29.89  ? 55   ILE B CG2 1 
ATOM   2721 C CD1 . ILE B 1 55  ? 10.109  13.850  -14.267 1.00  32.55  ? 55   ILE B CD1 1 
ATOM   2722 N N   . VAL B 1 56  ? 15.921  13.704  -15.704 1.00  33.22  ? 56   VAL B N   1 
ATOM   2723 C CA  . VAL B 1 56  ? 17.357  13.599  -15.406 1.00  34.72  ? 56   VAL B CA  1 
ATOM   2724 C C   . VAL B 1 56  ? 17.707  14.472  -14.205 1.00  36.07  ? 56   VAL B C   1 
ATOM   2725 O O   . VAL B 1 56  ? 17.449  15.679  -14.219 1.00  36.34  ? 56   VAL B O   1 
ATOM   2726 C CB  . VAL B 1 56  ? 18.221  14.022  -16.628 1.00  34.47  ? 56   VAL B CB  1 
ATOM   2727 C CG1 . VAL B 1 56  ? 19.682  14.147  -16.248 1.00  33.69  ? 56   VAL B CG1 1 
ATOM   2728 C CG2 . VAL B 1 56  ? 18.025  13.054  -17.809 1.00  33.93  ? 56   VAL B CG2 1 
ATOM   2729 N N   . GLN B 1 57  ? 18.281  13.856  -13.173 0.69  37.57  ? 57   GLN B N   1 
ATOM   2730 C CA  . GLN B 1 57  ? 18.647  14.576  -11.960 0.69  38.89  ? 57   GLN B CA  1 
ATOM   2731 C C   . GLN B 1 57  ? 19.874  15.433  -12.223 0.69  39.79  ? 57   GLN B C   1 
ATOM   2732 O O   . GLN B 1 57  ? 20.887  14.966  -12.770 0.69  39.64  ? 57   GLN B O   1 
ATOM   2733 C CB  . GLN B 1 57  ? 18.854  13.610  -10.779 0.69  39.32  ? 57   GLN B CB  1 
ATOM   2734 C CG  . GLN B 1 57  ? 20.298  13.163  -10.509 0.69  40.13  ? 57   GLN B CG  1 
ATOM   2735 C CD  . GLN B 1 57  ? 20.928  13.908  -9.340  0.69  41.07  ? 57   GLN B CD  1 
ATOM   2736 O OE1 . GLN B 1 57  ? 21.732  14.831  -9.531  0.69  41.35  ? 57   GLN B OE1 1 
ATOM   2737 N NE2 . GLN B 1 57  ? 20.556  13.522  -8.122  0.69  40.09  ? 57   GLN B NE2 1 
ATOM   2738 N N   . SER B 1 58  ? 19.749  16.698  -11.829 1.00  41.09  ? 58   SER B N   1 
ATOM   2739 C CA  . SER B 1 58  ? 20.733  17.758  -12.104 1.00  42.08  ? 58   SER B CA  1 
ATOM   2740 C C   . SER B 1 58  ? 21.930  17.764  -11.142 1.00  42.05  ? 58   SER B C   1 
ATOM   2741 O O   . SER B 1 58  ? 21.745  17.649  -9.934  1.00  42.26  ? 58   SER B O   1 
ATOM   2742 C CB  . SER B 1 58  ? 20.010  19.102  -12.043 1.00  42.05  ? 58   SER B CB  1 
ATOM   2743 O OG  . SER B 1 58  ? 20.767  20.066  -11.332 1.00  43.91  ? 58   SER B OG  1 
ATOM   2744 N N   . GLY B 1 59  ? 23.137  17.918  -11.683 0.010 42.23  ? 59   GLY B N   1 
ATOM   2745 C CA  . GLY B 1 59  ? 24.360  17.953  -10.876 0.010 42.42  ? 59   GLY B CA  1 
ATOM   2746 C C   . GLY B 1 59  ? 24.738  19.353  -10.425 0.010 42.62  ? 59   GLY B C   1 
ATOM   2747 O O   . GLY B 1 59  ? 25.914  19.717  -10.417 0.010 42.60  ? 59   GLY B O   1 
ATOM   2748 N N   . CYS B 1 60  ? 23.735  20.137  -10.041 0.010 42.89  ? 60   CYS B N   1 
ATOM   2749 C CA  . CYS B 1 60  ? 23.948  21.521  -9.627  0.010 43.23  ? 60   CYS B CA  1 
ATOM   2750 C C   . CYS B 1 60  ? 24.866  21.629  -8.412  0.010 43.55  ? 60   CYS B C   1 
ATOM   2751 O O   . CYS B 1 60  ? 25.815  22.415  -8.417  0.010 43.57  ? 60   CYS B O   1 
ATOM   2752 C CB  . CYS B 1 60  ? 22.611  22.211  -9.345  0.010 43.17  ? 60   CYS B CB  1 
ATOM   2753 S SG  . CYS B 1 60  ? 22.757  23.936  -8.822  0.010 43.19  ? 60   CYS B SG  1 
ATOM   2754 N N   . GLY B 1 61  ? 24.575  20.846  -7.374  1.00  44.13  ? 61   GLY B N   1 
ATOM   2755 C CA  . GLY B 1 61  ? 25.435  20.815  -6.193  1.00  44.49  ? 61   GLY B CA  1 
ATOM   2756 C C   . GLY B 1 61  ? 24.794  20.841  -4.819  1.00  44.33  ? 61   GLY B C   1 
ATOM   2757 O O   . GLY B 1 61  ? 25.488  20.596  -3.836  1.00  45.32  ? 61   GLY B O   1 
ATOM   2758 N N   . GLU B 1 62  ? 23.499  21.154  -4.737  0.95  43.95  ? 62   GLU B N   1 
ATOM   2759 C CA  . GLU B 1 62  ? 22.757  21.103  -3.465  0.95  43.24  ? 62   GLU B CA  1 
ATOM   2760 C C   . GLU B 1 62  ? 21.842  19.891  -3.532  0.95  42.85  ? 62   GLU B C   1 
ATOM   2761 O O   . GLU B 1 62  ? 20.800  19.923  -4.200  0.95  42.87  ? 62   GLU B O   1 
ATOM   2762 C CB  . GLU B 1 62  ? 21.934  22.375  -3.237  0.95  43.16  ? 62   GLU B CB  1 
ATOM   2763 C CG  . GLU B 1 62  ? 21.805  22.830  -1.765  0.95  43.79  ? 62   GLU B CG  1 
ATOM   2764 C CD  . GLU B 1 62  ? 21.028  21.875  -0.852  0.95  43.87  ? 62   GLU B CD  1 
ATOM   2765 O OE1 . GLU B 1 62  ? 20.089  21.197  -1.314  0.95  43.77  ? 62   GLU B OE1 1 
ATOM   2766 O OE2 . GLU B 1 62  ? 21.357  21.823  0.353   0.95  44.00  ? 62   GLU B OE2 1 
ATOM   2767 N N   . ILE B 1 63  ? 22.236  18.828  -2.840  1.00  42.58  ? 63   ILE B N   1 
ATOM   2768 C CA  . ILE B 1 63  ? 21.588  17.512  -2.942  1.00  42.01  ? 63   ILE B CA  1 
ATOM   2769 C C   . ILE B 1 63  ? 20.127  17.478  -2.459  1.00  41.81  ? 63   ILE B C   1 
ATOM   2770 O O   . ILE B 1 63  ? 19.302  16.790  -3.057  1.00  42.27  ? 63   ILE B O   1 
ATOM   2771 C CB  . ILE B 1 63  ? 22.442  16.411  -2.242  1.00  42.13  ? 63   ILE B CB  1 
ATOM   2772 C CG1 . ILE B 1 63  ? 21.925  15.011  -2.574  1.00  42.23  ? 63   ILE B CG1 1 
ATOM   2773 C CG2 . ILE B 1 63  ? 22.543  16.649  -0.716  1.00  42.31  ? 63   ILE B CG2 1 
ATOM   2774 C CD1 . ILE B 1 63  ? 22.876  13.893  -2.157  1.00  42.48  ? 63   ILE B CD1 1 
ATOM   2775 N N   . ASN B 1 64  ? 19.795  18.205  -1.395  1.00  41.11  ? 64   ASN B N   1 
ATOM   2776 C CA  . ASN B 1 64  ? 18.406  18.190  -0.916  1.00  40.63  ? 64   ASN B CA  1 
ATOM   2777 C C   . ASN B 1 64  ? 17.471  19.006  -1.807  1.00  40.16  ? 64   ASN B C   1 
ATOM   2778 O O   . ASN B 1 64  ? 16.309  18.639  -2.002  1.00  39.96  ? 64   ASN B O   1 
ATOM   2779 C CB  . ASN B 1 64  ? 18.297  18.621  0.554   1.00  40.55  ? 64   ASN B CB  1 
ATOM   2780 C CG  . ASN B 1 64  ? 19.213  17.824  1.463   1.00  40.22  ? 64   ASN B CG  1 
ATOM   2781 O OD1 . ASN B 1 64  ? 20.061  18.385  2.148   1.00  39.95  ? 64   ASN B OD1 1 
ATOM   2782 N ND2 . ASN B 1 64  ? 19.059  16.508  1.458   1.00  40.91  ? 64   ASN B ND2 1 
ATOM   2783 N N   . ASP B 1 65  ? 17.990  20.102  -2.350  1.00  39.78  ? 65   ASP B N   1 
ATOM   2784 C CA  . ASP B 1 65  ? 17.271  20.884  -3.356  1.00  39.63  ? 65   ASP B CA  1 
ATOM   2785 C C   . ASP B 1 65  ? 17.036  20.062  -4.624  1.00  39.38  ? 65   ASP B C   1 
ATOM   2786 O O   . ASP B 1 65  ? 15.914  20.000  -5.148  1.00  39.07  ? 65   ASP B O   1 
ATOM   2787 C CB  . ASP B 1 65  ? 18.051  22.148  -3.696  1.00  39.53  ? 65   ASP B CB  1 
ATOM   2788 C CG  . ASP B 1 65  ? 18.016  23.165  -2.587  1.00  39.83  ? 65   ASP B CG  1 
ATOM   2789 O OD1 . ASP B 1 65  ? 17.524  22.840  -1.481  1.00  41.05  ? 65   ASP B OD1 1 
ATOM   2790 O OD2 . ASP B 1 65  ? 18.481  24.295  -2.836  1.00  39.73  ? 65   ASP B OD2 1 
ATOM   2791 N N   . ASN B 1 66  ? 18.102  19.418  -5.093  1.00  38.96  ? 66   ASN B N   1 
ATOM   2792 C CA  . ASN B 1 66  ? 18.038  18.582  -6.278  1.00  38.75  ? 66   ASN B CA  1 
ATOM   2793 C C   . ASN B 1 66  ? 17.081  17.429  -6.130  1.00  38.42  ? 66   ASN B C   1 
ATOM   2794 O O   . ASN B 1 66  ? 16.304  17.143  -7.038  1.00  38.84  ? 66   ASN B O   1 
ATOM   2795 C CB  . ASN B 1 66  ? 19.422  18.046  -6.625  1.00  39.05  ? 66   ASN B CB  1 
ATOM   2796 C CG  . ASN B 1 66  ? 20.211  19.000  -7.481  1.00  39.55  ? 66   ASN B CG  1 
ATOM   2797 O OD1 . ASN B 1 66  ? 19.653  19.784  -8.256  1.00  39.64  ? 66   ASN B OD1 1 
ATOM   2798 N ND2 . ASN B 1 66  ? 21.526  18.926  -7.358  1.00  41.42  ? 66   ASN B ND2 1 
ATOM   2799 N N   . LEU B 1 67  ? 17.146  16.753  -4.989  1.00  38.03  ? 67   LEU B N   1 
ATOM   2800 C CA  . LEU B 1 67  ? 16.252  15.641  -4.730  1.00  37.75  ? 67   LEU B CA  1 
ATOM   2801 C C   . LEU B 1 67  ? 14.803  16.105  -4.684  1.00  37.69  ? 67   LEU B C   1 
ATOM   2802 O O   . LEU B 1 67  ? 13.936  15.462  -5.267  1.00  38.08  ? 67   LEU B O   1 
ATOM   2803 C CB  . LEU B 1 67  ? 16.624  14.930  -3.435  1.00  37.88  ? 67   LEU B CB  1 
ATOM   2804 C CG  . LEU B 1 67  ? 15.816  13.676  -3.095  1.00  38.01  ? 67   LEU B CG  1 
ATOM   2805 C CD1 . LEU B 1 67  ? 16.146  12.547  -4.066  1.00  38.83  ? 67   LEU B CD1 1 
ATOM   2806 C CD2 . LEU B 1 67  ? 16.103  13.259  -1.667  1.00  37.92  ? 67   LEU B CD2 1 
ATOM   2807 N N   . MET B 1 68  ? 14.546  17.220  -3.996  0.91  37.38  ? 68   MET B N   1 
ATOM   2808 C CA  . MET B 1 68  ? 13.197  17.767  -3.906  0.91  36.94  ? 68   MET B CA  1 
ATOM   2809 C C   . MET B 1 68  ? 12.631  18.133  -5.267  0.91  36.61  ? 68   MET B C   1 
ATOM   2810 O O   . MET B 1 68  ? 11.471  17.821  -5.572  0.91  36.74  ? 68   MET B O   1 
ATOM   2811 C CB  . MET B 1 68  ? 13.134  18.966  -2.954  0.91  37.09  ? 68   MET B CB  1 
ATOM   2812 C CG  . MET B 1 68  ? 12.788  18.589  -1.508  0.91  38.08  ? 68   MET B CG  1 
ATOM   2813 S SD  . MET B 1 68  ? 11.359  17.465  -1.400  0.91  40.46  ? 68   MET B SD  1 
ATOM   2814 C CE  . MET B 1 68  ? 10.029  18.481  -2.065  0.91  37.71  ? 68   MET B CE  1 
ATOM   2815 N N   . GLU B 1 69  ? 13.452  18.772  -6.096  1.00  36.25  ? 69   GLU B N   1 
ATOM   2816 C CA  . GLU B 1 69  ? 13.016  19.150  -7.434  1.00  35.95  ? 69   GLU B CA  1 
ATOM   2817 C C   . GLU B 1 69  ? 12.726  17.928  -8.294  1.00  34.96  ? 69   GLU B C   1 
ATOM   2818 O O   . GLU B 1 69  ? 11.757  17.907  -9.045  1.00  35.32  ? 69   GLU B O   1 
ATOM   2819 C CB  . GLU B 1 69  ? 14.037  20.042  -8.131  1.00  36.28  ? 69   GLU B CB  1 
ATOM   2820 C CG  . GLU B 1 69  ? 13.360  21.050  -9.058  1.00  39.72  ? 69   GLU B CG  1 
ATOM   2821 C CD  . GLU B 1 69  ? 14.252  21.515  -10.179 1.00  43.73  ? 69   GLU B CD  1 
ATOM   2822 O OE1 . GLU B 1 69  ? 15.210  20.790  -10.513 1.00  46.18  ? 69   GLU B OE1 1 
ATOM   2823 O OE2 . GLU B 1 69  ? 13.992  22.596  -10.743 1.00  45.17  ? 69   GLU B OE2 1 
ATOM   2824 N N   . LEU B 1 70  ? 13.563  16.905  -8.175  1.00  33.80  ? 70   LEU B N   1 
ATOM   2825 C CA  . LEU B 1 70  ? 13.339  15.643  -8.865  1.00  32.53  ? 70   LEU B CA  1 
ATOM   2826 C C   . LEU B 1 70  ? 12.030  14.982  -8.411  1.00  32.28  ? 70   LEU B C   1 
ATOM   2827 O O   . LEU B 1 70  ? 11.310  14.397  -9.216  1.00  32.18  ? 70   LEU B O   1 
ATOM   2828 C CB  . LEU B 1 70  ? 14.540  14.722  -8.628  1.00  32.38  ? 70   LEU B CB  1 
ATOM   2829 C CG  . LEU B 1 70  ? 14.573  13.262  -9.079  1.00  31.29  ? 70   LEU B CG  1 
ATOM   2830 C CD1 . LEU B 1 70  ? 14.302  13.137  -10.589 1.00  31.72  ? 70   LEU B CD1 1 
ATOM   2831 C CD2 . LEU B 1 70  ? 15.917  12.686  -8.737  1.00  28.36  ? 70   LEU B CD2 1 
ATOM   2832 N N   . LEU B 1 71  ? 11.719  15.092  -7.121  1.00  31.92  ? 71   LEU B N   1 
ATOM   2833 C CA  . LEU B 1 71  ? 10.486  14.535  -6.587  1.00  31.69  ? 71   LEU B CA  1 
ATOM   2834 C C   . LEU B 1 71  ? 9.251   15.294  -7.056  1.00  32.02  ? 71   LEU B C   1 
ATOM   2835 O O   . LEU B 1 71  ? 8.219   14.691  -7.371  1.00  31.73  ? 71   LEU B O   1 
ATOM   2836 C CB  . LEU B 1 71  ? 10.531  14.504  -5.071  1.00  31.32  ? 71   LEU B CB  1 
ATOM   2837 C CG  . LEU B 1 71  ? 11.450  13.446  -4.461  1.00  31.13  ? 71   LEU B CG  1 
ATOM   2838 C CD1 . LEU B 1 71  ? 11.388  13.554  -2.933  1.00  30.67  ? 71   LEU B CD1 1 
ATOM   2839 C CD2 . LEU B 1 71  ? 11.091  12.045  -4.930  1.00  28.90  ? 71   LEU B CD2 1 
ATOM   2840 N N   . ILE B 1 72  ? 9.380   16.621  -7.105  1.00  32.52  ? 72   ILE B N   1 
ATOM   2841 C CA  . ILE B 1 72  ? 8.291   17.528  -7.484  1.00  32.49  ? 72   ILE B CA  1 
ATOM   2842 C C   . ILE B 1 72  ? 7.920   17.349  -8.953  1.00  32.50  ? 72   ILE B C   1 
ATOM   2843 O O   . ILE B 1 72  ? 6.740   17.253  -9.290  1.00  32.62  ? 72   ILE B O   1 
ATOM   2844 C CB  . ILE B 1 72  ? 8.652   18.999  -7.128  1.00  32.64  ? 72   ILE B CB  1 
ATOM   2845 C CG1 . ILE B 1 72  ? 8.450   19.243  -5.630  1.00  32.16  ? 72   ILE B CG1 1 
ATOM   2846 C CG2 . ILE B 1 72  ? 7.814   19.988  -7.908  1.00  32.68  ? 72   ILE B CG2 1 
ATOM   2847 C CD1 . ILE B 1 72  ? 9.214   20.428  -5.087  1.00  32.64  ? 72   ILE B CD1 1 
ATOM   2848 N N   . MET B 1 73  ? 8.934   17.272  -9.809  1.00  32.63  ? 73   MET B N   1 
ATOM   2849 C CA  . MET B 1 73  ? 8.747   16.994  -11.238 1.00  32.99  ? 73   MET B CA  1 
ATOM   2850 C C   . MET B 1 73  ? 8.141   15.619  -11.537 1.00  32.60  ? 73   MET B C   1 
ATOM   2851 O O   . MET B 1 73  ? 7.345   15.495  -12.462 1.00  32.62  ? 73   MET B O   1 
ATOM   2852 C CB  . MET B 1 73  ? 10.071  17.120  -11.988 1.00  33.30  ? 73   MET B CB  1 
ATOM   2853 C CG  . MET B 1 73  ? 10.665  18.515  -11.970 1.00  35.69  ? 73   MET B CG  1 
ATOM   2854 S SD  . MET B 1 73  ? 12.036  18.732  -13.130 1.00  39.83  ? 73   MET B SD  1 
ATOM   2855 C CE  . MET B 1 73  ? 11.156  18.456  -14.673 1.00  38.35  ? 73   MET B CE  1 
ATOM   2856 N N   . ILE B 1 74  ? 8.539   14.592  -10.777 1.00  32.34  ? 74   ILE B N   1 
ATOM   2857 C CA  . ILE B 1 74  ? 7.954   13.244  -10.907 1.00  31.90  ? 74   ILE B CA  1 
ATOM   2858 C C   . ILE B 1 74  ? 6.468   13.284  -10.585 1.00  31.56  ? 74   ILE B C   1 
ATOM   2859 O O   . ILE B 1 74  ? 5.666   12.636  -11.253 1.00  31.75  ? 74   ILE B O   1 
ATOM   2860 C CB  . ILE B 1 74  ? 8.642   12.203  -9.980  1.00  32.12  ? 74   ILE B CB  1 
ATOM   2861 C CG1 . ILE B 1 74  ? 9.993   11.774  -10.544 1.00  31.93  ? 74   ILE B CG1 1 
ATOM   2862 C CG2 . ILE B 1 74  ? 7.767   10.964  -9.787  1.00  32.22  ? 74   ILE B CG2 1 
ATOM   2863 C CD1 . ILE B 1 74  ? 10.789  10.886  -9.622  1.00  29.81  ? 74   ILE B CD1 1 
ATOM   2864 N N   . ASN B 1 75  ? 6.108   14.065  -9.571  1.00  31.21  ? 75   ASN B N   1 
ATOM   2865 C CA  . ASN B 1 75  ? 4.711   14.189  -9.170  1.00  30.88  ? 75   ASN B CA  1 
ATOM   2866 C C   . ASN B 1 75  ? 3.864   14.928  -10.190 1.00  30.64  ? 75   ASN B C   1 
ATOM   2867 O O   . ASN B 1 75  ? 2.754   14.479  -10.517 1.00  30.35  ? 75   ASN B O   1 
ATOM   2868 C CB  . ASN B 1 75  ? 4.583   14.880  -7.825  1.00  30.70  ? 75   ASN B CB  1 
ATOM   2869 C CG  . ASN B 1 75  ? 3.273   14.571  -7.157  1.00  32.21  ? 75   ASN B CG  1 
ATOM   2870 O OD1 . ASN B 1 75  ? 2.893   13.400  -7.002  1.00  33.02  ? 75   ASN B OD1 1 
ATOM   2871 N ND2 . ASN B 1 75  ? 2.562   15.613  -6.756  1.00  35.76  ? 75   ASN B ND2 1 
ATOM   2872 N N   . ALA B 1 76  ? 4.400   16.057  -10.679 1.00  30.21  ? 76   ALA B N   1 
ATOM   2873 C CA  . ALA B 1 76  ? 3.738   16.895  -11.666 1.00  29.59  ? 76   ALA B CA  1 
ATOM   2874 C C   . ALA B 1 76  ? 3.369   16.089  -12.916 1.00  29.91  ? 76   ALA B C   1 
ATOM   2875 O O   . ALA B 1 76  ? 2.228   16.161  -13.404 1.00  30.37  ? 76   ALA B O   1 
ATOM   2876 C CB  . ALA B 1 76  ? 4.621   18.041  -12.031 1.00  29.66  ? 76   ALA B CB  1 
ATOM   2877 N N   . CYS B 1 77  ? 4.326   15.306  -13.410 1.00  29.33  ? 77   CYS B N   1 
ATOM   2878 C CA  . CYS B 1 77  ? 4.111   14.463  -14.572 1.00  29.10  ? 77   CYS B CA  1 
ATOM   2879 C C   . CYS B 1 77  ? 3.112   13.349  -14.303 1.00  29.21  ? 77   CYS B C   1 
ATOM   2880 O O   . CYS B 1 77  ? 2.298   13.061  -15.153 1.00  29.45  ? 77   CYS B O   1 
ATOM   2881 C CB  . CYS B 1 77  ? 5.435   13.860  -15.058 1.00  29.16  ? 77   CYS B CB  1 
ATOM   2882 S SG  . CYS B 1 77  ? 6.675   15.065  -15.465 1.00  28.70  ? 77   CYS B SG  1 
ATOM   2883 N N   . LYS B 1 78  ? 3.196   12.703  -13.142 1.00  29.76  ? 78   LYS B N   1 
ATOM   2884 C CA  . LYS B 1 78  ? 2.251   11.640  -12.778 1.00  30.04  ? 78   LYS B CA  1 
ATOM   2885 C C   . LYS B 1 78  ? 0.794   12.115  -12.672 1.00  30.30  ? 78   LYS B C   1 
ATOM   2886 O O   . LYS B 1 78  ? -0.120  11.439  -13.160 1.00  30.92  ? 78   LYS B O   1 
ATOM   2887 C CB  . LYS B 1 78  ? 2.667   10.938  -11.483 1.00  30.37  ? 78   LYS B CB  1 
ATOM   2888 C CG  . LYS B 1 78  ? 3.273   9.559   -11.663 1.00  30.21  ? 78   LYS B CG  1 
ATOM   2889 C CD  . LYS B 1 78  ? 2.179   8.492   -11.803 1.00  31.37  ? 78   LYS B CD  1 
ATOM   2890 C CE  . LYS B 1 78  ? 2.737   7.137   -12.266 1.00  31.53  ? 78   LYS B CE  1 
ATOM   2891 N NZ  . LYS B 1 78  ? 3.542   7.269   -13.537 1.00  32.07  ? 78   LYS B NZ  1 
ATOM   2892 N N   . ILE B 1 79  ? 0.563   13.274  -12.064 1.00  29.90  ? 79   ILE B N   1 
ATOM   2893 C CA  . ILE B 1 79  ? -0.811  13.793  -11.976 1.00  29.57  ? 79   ILE B CA  1 
ATOM   2894 C C   . ILE B 1 79  ? -1.231  14.559  -13.236 1.00  29.72  ? 79   ILE B C   1 
ATOM   2895 O O   . ILE B 1 79  ? -2.374  15.068  -13.317 1.00  30.26  ? 79   ILE B O   1 
ATOM   2896 C CB  . ILE B 1 79  ? -1.051  14.663  -10.712 1.00  29.46  ? 79   ILE B CB  1 
ATOM   2897 C CG1 . ILE B 1 79  ? -0.158  15.920  -10.762 1.00  29.76  ? 79   ILE B CG1 1 
ATOM   2898 C CG2 . ILE B 1 79  ? -0.896  13.809  -9.410  1.00  28.66  ? 79   ILE B CG2 1 
ATOM   2899 C CD1 . ILE B 1 79  ? -0.117  16.714  -9.482  1.00  30.43  ? 79   ILE B CD1 1 
ATOM   2900 N N   . ALA B 1 80  ? -0.309  14.664  -14.197 1.00  29.15  ? 80   ALA B N   1 
ATOM   2901 C CA  . ALA B 1 80  ? -0.643  15.142  -15.540 1.00  28.40  ? 80   ALA B CA  1 
ATOM   2902 C C   . ALA B 1 80  ? -0.782  13.966  -16.514 1.00  28.29  ? 80   ALA B C   1 
ATOM   2903 O O   . ALA B 1 80  ? -0.652  14.154  -17.728 1.00  28.19  ? 80   ALA B O   1 
ATOM   2904 C CB  . ALA B 1 80  ? 0.403   16.145  -16.035 1.00  28.28  ? 80   ALA B CB  1 
ATOM   2905 N N   . SER B 1 81  ? -1.031  12.762  -15.971 1.00  28.33  ? 81   SER B N   1 
ATOM   2906 C CA  . SER B 1 81  ? -1.445  11.566  -16.760 1.00  28.57  ? 81   SER B CA  1 
ATOM   2907 C C   . SER B 1 81  ? -0.396  11.074  -17.746 1.00  28.76  ? 81   SER B C   1 
ATOM   2908 O O   . SER B 1 81  ? -0.735  10.563  -18.813 1.00  29.05  ? 81   SER B O   1 
ATOM   2909 C CB  . SER B 1 81  ? -2.738  11.813  -17.535 1.00  28.22  ? 81   SER B CB  1 
ATOM   2910 O OG  . SER B 1 81  ? -3.794  12.141  -16.636 1.00  29.47  ? 81   SER B OG  1 
ATOM   2911 N N   . ALA B 1 82  ? 0.875   11.272  -17.417 1.00  28.72  ? 82   ALA B N   1 
ATOM   2912 C CA  . ALA B 1 82  ? 1.933   10.604  -18.139 1.00  28.64  ? 82   ALA B CA  1 
ATOM   2913 C C   . ALA B 1 82  ? 1.683   9.103   -18.059 1.00  28.99  ? 82   ALA B C   1 
ATOM   2914 O O   . ALA B 1 82  ? 1.169   8.593   -17.068 1.00  29.25  ? 82   ALA B O   1 
ATOM   2915 C CB  . ALA B 1 82  ? 3.304   10.956  -17.558 1.00  28.02  ? 82   ALA B CB  1 
ATOM   2916 N N   . SER B 1 83  ? 2.024   8.405   -19.127 1.00  29.69  ? 83   SER B N   1 
ATOM   2917 C CA  . SER B 1 83  ? 1.978   6.960   -19.152 1.00  30.17  ? 83   SER B CA  1 
ATOM   2918 C C   . SER B 1 83  ? 2.980   6.349   -18.205 1.00  29.86  ? 83   SER B C   1 
ATOM   2919 O O   . SER B 1 83  ? 2.675   5.362   -17.555 1.00  30.77  ? 83   SER B O   1 
ATOM   2920 C CB  . SER B 1 83  ? 2.259   6.458   -20.563 1.00  30.82  ? 83   SER B CB  1 
ATOM   2921 O OG  . SER B 1 83  ? 2.514   5.066   -20.544 1.00  33.48  ? 83   SER B OG  1 
ATOM   2922 N N   . ARG B 1 84  ? 4.183   6.920   -18.146 1.00  29.93  ? 84   ARG B N   1 
ATOM   2923 C CA  . ARG B 1 84  ? 5.289   6.385   -17.326 1.00  29.67  ? 84   ARG B CA  1 
ATOM   2924 C C   . ARG B 1 84  ? 6.303   7.476   -17.020 1.00  29.44  ? 84   ARG B C   1 
ATOM   2925 O O   . ARG B 1 84  ? 6.624   8.272   -17.890 1.00  29.06  ? 84   ARG B O   1 
ATOM   2926 C CB  . ARG B 1 84  ? 5.979   5.198   -18.020 1.00  29.63  ? 84   ARG B CB  1 
ATOM   2927 C CG  . ARG B 1 84  ? 6.950   4.404   -17.128 1.00  30.59  ? 84   ARG B CG  1 
ATOM   2928 C CD  . ARG B 1 84  ? 7.457   3.115   -17.782 1.00  30.74  ? 84   ARG B CD  1 
ATOM   2929 N NE  . ARG B 1 84  ? 8.165   3.436   -19.018 1.00  35.08  ? 84   ARG B NE  1 
ATOM   2930 C CZ  . ARG B 1 84  ? 8.644   2.553   -19.893 1.00  35.02  ? 84   ARG B CZ  1 
ATOM   2931 N NH1 . ARG B 1 84  ? 8.508   1.241   -19.687 1.00  34.18  ? 84   ARG B NH1 1 
ATOM   2932 N NH2 . ARG B 1 84  ? 9.257   3.005   -20.984 1.00  32.47  ? 84   ARG B NH2 1 
ATOM   2933 N N   . VAL B 1 85  ? 6.785   7.523   -15.774 1.00  29.90  ? 85   VAL B N   1 
ATOM   2934 C CA  . VAL B 1 85  ? 7.852   8.453   -15.388 1.00  29.67  ? 85   VAL B CA  1 
ATOM   2935 C C   . VAL B 1 85  ? 9.040   7.639   -14.905 1.00  29.80  ? 85   VAL B C   1 
ATOM   2936 O O   . VAL B 1 85  ? 8.917   6.830   -13.993 1.00  29.91  ? 85   VAL B O   1 
ATOM   2937 C CB  . VAL B 1 85  ? 7.390   9.470   -14.300 1.00  29.89  ? 85   VAL B CB  1 
ATOM   2938 C CG1 . VAL B 1 85  ? 8.565   10.328  -13.798 1.00  29.52  ? 85   VAL B CG1 1 
ATOM   2939 C CG2 . VAL B 1 85  ? 6.275   10.359  -14.827 1.00  28.98  ? 85   VAL B CG2 1 
ATOM   2940 N N   . THR B 1 86  ? 10.176  7.844   -15.560 1.00  30.33  ? 86   THR B N   1 
ATOM   2941 C CA  . THR B 1 86  ? 11.423  7.171   -15.232 1.00  30.78  ? 86   THR B CA  1 
ATOM   2942 C C   . THR B 1 86  ? 12.335  8.252   -14.706 1.00  31.24  ? 86   THR B C   1 
ATOM   2943 O O   . THR B 1 86  ? 12.526  9.271   -15.373 1.00  31.57  ? 86   THR B O   1 
ATOM   2944 C CB  . THR B 1 86  ? 12.070  6.558   -16.489 1.00  30.67  ? 86   THR B CB  1 
ATOM   2945 O OG1 . THR B 1 86  ? 11.240  5.510   -17.009 1.00  32.32  ? 86   THR B OG1 1 
ATOM   2946 C CG2 . THR B 1 86  ? 13.451  6.017   -16.197 1.00  29.92  ? 86   THR B CG2 1 
ATOM   2947 N N   . ALA B 1 87  ? 12.878  8.046   -13.505 1.00  31.65  ? 87   ALA B N   1 
ATOM   2948 C CA  . ALA B 1 87  ? 13.835  8.980   -12.943 1.00  32.06  ? 87   ALA B CA  1 
ATOM   2949 C C   . ALA B 1 87  ? 15.210  8.507   -13.326 1.00  32.40  ? 87   ALA B C   1 
ATOM   2950 O O   . ALA B 1 87  ? 15.633  7.436   -12.916 1.00  33.11  ? 87   ALA B O   1 
ATOM   2951 C CB  . ALA B 1 87  ? 13.699  9.069   -11.439 1.00  32.20  ? 87   ALA B CB  1 
ATOM   2952 N N   . VAL B 1 88  ? 15.888  9.289   -14.157 1.00  32.83  ? 88   VAL B N   1 
ATOM   2953 C CA  . VAL B 1 88  ? 17.250  8.992   -14.569 1.00  33.21  ? 88   VAL B CA  1 
ATOM   2954 C C   . VAL B 1 88  ? 18.189  9.705   -13.596 1.00  33.76  ? 88   VAL B C   1 
ATOM   2955 O O   . VAL B 1 88  ? 18.345  10.931  -13.665 1.00  33.87  ? 88   VAL B O   1 
ATOM   2956 C CB  . VAL B 1 88  ? 17.496  9.446   -16.036 1.00  33.20  ? 88   VAL B CB  1 
ATOM   2957 C CG1 . VAL B 1 88  ? 18.939  9.196   -16.474 1.00  32.92  ? 88   VAL B CG1 1 
ATOM   2958 C CG2 . VAL B 1 88  ? 16.527  8.733   -16.992 1.00  33.48  ? 88   VAL B CG2 1 
ATOM   2959 N N   . ILE B 1 89  ? 18.783  8.933   -12.683 1.00  34.17  ? 89   ILE B N   1 
ATOM   2960 C CA  . ILE B 1 89  ? 19.621  9.469   -11.608 1.00  35.01  ? 89   ILE B CA  1 
ATOM   2961 C C   . ILE B 1 89  ? 21.042  8.911   -11.687 1.00  35.39  ? 89   ILE B C   1 
ATOM   2962 O O   . ILE B 1 89  ? 21.395  7.971   -10.960 1.00  34.97  ? 89   ILE B O   1 
ATOM   2963 C CB  . ILE B 1 89  ? 19.070  9.134   -10.198 1.00  35.13  ? 89   ILE B CB  1 
ATOM   2964 C CG1 . ILE B 1 89  ? 17.565  9.338   -10.113 1.00  35.36  ? 89   ILE B CG1 1 
ATOM   2965 C CG2 . ILE B 1 89  ? 19.787  9.965   -9.149  1.00  36.07  ? 89   ILE B CG2 1 
ATOM   2966 C CD1 . ILE B 1 89  ? 16.968  8.926   -8.789  1.00  35.79  ? 89   ILE B CD1 1 
ATOM   2967 N N   . PRO B 1 90  ? 21.872  9.498   -12.557 1.00  36.22  ? 90   PRO B N   1 
ATOM   2968 C CA  . PRO B 1 90  ? 23.227  8.976   -12.752 1.00  36.79  ? 90   PRO B CA  1 
ATOM   2969 C C   . PRO B 1 90  ? 23.931  8.761   -11.414 1.00  37.38  ? 90   PRO B C   1 
ATOM   2970 O O   . PRO B 1 90  ? 24.391  7.648   -11.119 1.00  37.37  ? 90   PRO B O   1 
ATOM   2971 C CB  . PRO B 1 90  ? 23.908  10.082  -13.559 1.00  36.82  ? 90   PRO B CB  1 
ATOM   2972 C CG  . PRO B 1 90  ? 22.772  10.757  -14.296 1.00  36.34  ? 90   PRO B CG  1 
ATOM   2973 C CD  . PRO B 1 90  ? 21.644  10.742  -13.319 1.00  36.29  ? 90   PRO B CD  1 
ATOM   2974 N N   . CYS B 1 91  ? 23.977  9.815   -10.602 1.00  37.92  ? 91   CYS B N   1 
ATOM   2975 C CA  . CYS B 1 91  ? 24.591  9.749   -9.291  1.00  38.68  ? 91   CYS B CA  1 
ATOM   2976 C C   . CYS B 1 91  ? 23.510  9.719   -8.197  1.00  39.34  ? 91   CYS B C   1 
ATOM   2977 O O   . CYS B 1 91  ? 22.932  10.750  -7.822  1.00  39.72  ? 91   CYS B O   1 
ATOM   2978 C CB  . CYS B 1 91  ? 25.544  10.917  -9.096  1.00  38.52  ? 91   CYS B CB  1 
ATOM   2979 S SG  . CYS B 1 91  ? 26.418  10.831  -7.543  1.00  41.86  ? 91   CYS B SG  1 
ATOM   2980 N N   . PHE B 1 92  ? 23.252  8.523   -7.681  1.00  39.75  ? 92   PHE B N   1 
ATOM   2981 C CA  . PHE B 1 92  ? 22.148  8.306   -6.781  1.00  40.63  ? 92   PHE B CA  1 
ATOM   2982 C C   . PHE B 1 92  ? 22.429  8.905   -5.415  1.00  41.43  ? 92   PHE B C   1 
ATOM   2983 O O   . PHE B 1 92  ? 23.375  8.483   -4.741  1.00  41.76  ? 92   PHE B O   1 
ATOM   2984 C CB  . PHE B 1 92  ? 21.860  6.811   -6.648  1.00  40.85  ? 92   PHE B CB  1 
ATOM   2985 C CG  . PHE B 1 92  ? 20.498  6.496   -6.087  1.00  40.83  ? 92   PHE B CG  1 
ATOM   2986 C CD1 . PHE B 1 92  ? 19.472  6.051   -6.925  1.00  40.41  ? 92   PHE B CD1 1 
ATOM   2987 C CD2 . PHE B 1 92  ? 20.240  6.632   -4.724  1.00  40.45  ? 92   PHE B CD2 1 
ATOM   2988 C CE1 . PHE B 1 92  ? 18.211  5.751   -6.421  1.00  39.37  ? 92   PHE B CE1 1 
ATOM   2989 C CE2 . PHE B 1 92  ? 18.971  6.328   -4.204  1.00  40.72  ? 92   PHE B CE2 1 
ATOM   2990 C CZ  . PHE B 1 92  ? 17.956  5.891   -5.058  1.00  39.67  ? 92   PHE B CZ  1 
ATOM   2991 N N   . PRO B 1 93  ? 21.589  9.874   -4.991  1.00  42.01  ? 93   PRO B N   1 
ATOM   2992 C CA  . PRO B 1 93  ? 21.765  10.613  -3.744  1.00  42.38  ? 93   PRO B CA  1 
ATOM   2993 C C   . PRO B 1 93  ? 21.659  9.735   -2.506  1.00  43.16  ? 93   PRO B C   1 
ATOM   2994 O O   . PRO B 1 93  ? 20.871  8.785   -2.490  1.00  43.63  ? 93   PRO B O   1 
ATOM   2995 C CB  . PRO B 1 93  ? 20.607  11.615  -3.768  1.00  42.52  ? 93   PRO B CB  1 
ATOM   2996 C CG  . PRO B 1 93  ? 19.596  11.011  -4.686  1.00  42.21  ? 93   PRO B CG  1 
ATOM   2997 C CD  . PRO B 1 93  ? 20.378  10.308  -5.718  1.00  41.95  ? 93   PRO B CD  1 
ATOM   2998 N N   . TYR B 1 94  ? 22.446  10.068  -1.483  1.00  43.76  ? 94   TYR B N   1 
ATOM   2999 C CA  . TYR B 1 94  ? 22.413  9.404   -0.179  1.00  44.39  ? 94   TYR B CA  1 
ATOM   3000 C C   . TYR B 1 94  ? 22.750  7.915   -0.255  1.00  45.01  ? 94   TYR B C   1 
ATOM   3001 O O   . TYR B 1 94  ? 22.476  7.154   0.692   1.00  45.20  ? 94   TYR B O   1 
ATOM   3002 C CB  . TYR B 1 94  ? 21.055  9.614   0.514   1.00  44.64  ? 94   TYR B CB  1 
ATOM   3003 C CG  . TYR B 1 94  ? 20.851  10.981  1.150   1.00  45.00  ? 94   TYR B CG  1 
ATOM   3004 C CD1 . TYR B 1 94  ? 20.226  12.011  0.454   1.00  45.22  ? 94   TYR B CD1 1 
ATOM   3005 C CD2 . TYR B 1 94  ? 21.261  11.232  2.459   1.00  45.40  ? 94   TYR B CD2 1 
ATOM   3006 C CE1 . TYR B 1 94  ? 20.028  13.263  1.040   1.00  44.91  ? 94   TYR B CE1 1 
ATOM   3007 C CE2 . TYR B 1 94  ? 21.075  12.472  3.049   1.00  44.99  ? 94   TYR B CE2 1 
ATOM   3008 C CZ  . TYR B 1 94  ? 20.459  13.484  2.336   1.00  45.20  ? 94   TYR B CZ  1 
ATOM   3009 O OH  . TYR B 1 94  ? 20.272  14.722  2.916   1.00  45.13  ? 94   TYR B OH  1 
ATOM   3010 N N   . ALA B 1 95  ? 23.356  7.506   -1.372  1.00  45.63  ? 95   ALA B N   1 
ATOM   3011 C CA  . ALA B 1 95  ? 23.755  6.113   -1.598  1.00  46.47  ? 95   ALA B CA  1 
ATOM   3012 C C   . ALA B 1 95  ? 24.702  5.535   -0.526  1.00  47.37  ? 95   ALA B C   1 
ATOM   3013 O O   . ALA B 1 95  ? 24.617  4.338   -0.206  1.00  47.50  ? 95   ALA B O   1 
ATOM   3014 C CB  . ALA B 1 95  ? 24.353  5.958   -2.971  1.00  46.48  ? 95   ALA B CB  1 
ATOM   3015 N N   . ARG B 1 96  ? 25.577  6.380   0.031   0.92  48.05  ? 96   ARG B N   1 
ATOM   3016 C CA  . ARG B 1 96  ? 26.499  5.966   1.108   0.92  48.96  ? 96   ARG B CA  1 
ATOM   3017 C C   . ARG B 1 96  ? 25.796  5.621   2.436   0.92  49.15  ? 96   ARG B C   1 
ATOM   3018 O O   . ARG B 1 96  ? 26.426  5.106   3.367   0.92  49.28  ? 96   ARG B O   1 
ATOM   3019 C CB  . ARG B 1 96  ? 27.580  7.032   1.347   0.92  49.02  ? 96   ARG B CB  1 
ATOM   3020 C CG  . ARG B 1 96  ? 28.571  7.196   0.197   0.92  50.30  ? 96   ARG B CG  1 
ATOM   3021 C CD  . ARG B 1 96  ? 29.543  8.346   0.440   0.92  52.69  ? 96   ARG B CD  1 
ATOM   3022 N NE  . ARG B 1 96  ? 28.870  9.640   0.602   0.92  54.07  ? 96   ARG B NE  1 
ATOM   3023 C CZ  . ARG B 1 96  ? 29.478  10.761  0.977   0.92  55.55  ? 96   ARG B CZ  1 
ATOM   3024 N NH1 . ARG B 1 96  ? 30.782  10.768  1.233   0.92  56.50  ? 96   ARG B NH1 1 
ATOM   3025 N NH2 . ARG B 1 96  ? 28.781  11.883  1.096   0.92  56.74  ? 96   ARG B NH2 1 
ATOM   3026 N N   . GLN B 1 97  ? 24.499  5.911   2.520   0.87  49.28  ? 97   GLN B N   1 
ATOM   3027 C CA  . GLN B 1 97  ? 23.720  5.607   3.724   0.87  49.65  ? 97   GLN B CA  1 
ATOM   3028 C C   . GLN B 1 97  ? 22.718  4.491   3.434   0.87  49.47  ? 97   GLN B C   1 
ATOM   3029 O O   . GLN B 1 97  ? 21.515  4.729   3.306   0.87  49.32  ? 97   GLN B O   1 
ATOM   3030 C CB  . GLN B 1 97  ? 23.042  6.875   4.274   0.87  49.71  ? 97   GLN B CB  1 
ATOM   3031 C CG  . GLN B 1 97  ? 24.016  7.826   4.978   0.87  50.94  ? 97   GLN B CG  1 
ATOM   3032 C CD  . GLN B 1 97  ? 23.569  9.279   4.966   0.87  52.95  ? 97   GLN B CD  1 
ATOM   3033 O OE1 . GLN B 1 97  ? 22.459  9.611   5.400   0.87  54.39  ? 97   GLN B OE1 1 
ATOM   3034 N NE2 . GLN B 1 97  ? 24.444  10.163  4.484   0.87  52.85  ? 97   GLN B NE2 1 
ATOM   3035 N N   . ASP B 1 98  ? 23.240  3.270   3.329   0.59  49.56  ? 98   ASP B N   1 
ATOM   3036 C CA  . ASP B 1 98  ? 22.464  2.113   2.888   0.59  49.80  ? 98   ASP B CA  1 
ATOM   3037 C C   . ASP B 1 98  ? 22.363  1.014   3.950   0.59  49.98  ? 98   ASP B C   1 
ATOM   3038 O O   . ASP B 1 98  ? 21.690  0.003   3.741   0.59  50.15  ? 98   ASP B O   1 
ATOM   3039 C CB  . ASP B 1 98  ? 23.045  1.549   1.585   0.59  49.94  ? 98   ASP B CB  1 
ATOM   3040 C CG  . ASP B 1 98  ? 24.506  1.127   1.722   0.59  50.58  ? 98   ASP B CG  1 
ATOM   3041 O OD1 . ASP B 1 98  ? 25.364  1.998   1.982   0.59  50.78  ? 98   ASP B OD1 1 
ATOM   3042 O OD2 . ASP B 1 98  ? 24.801  -0.079  1.560   0.59  51.47  ? 98   ASP B OD2 1 
ATOM   3043 N N   . LYS B 1 99  ? 23.029  1.226   5.085   0.62  50.14  ? 99   LYS B N   1 
ATOM   3044 C CA  . LYS B 1 99  ? 22.998  0.310   6.230   0.62  50.03  ? 99   LYS B CA  1 
ATOM   3045 C C   . LYS B 1 99  ? 23.241  1.083   7.527   0.62  50.38  ? 99   LYS B C   1 
ATOM   3046 O O   . LYS B 1 99  ? 24.009  2.048   7.535   0.62  50.50  ? 99   LYS B O   1 
ATOM   3047 C CB  . LYS B 1 99  ? 24.030  -0.814  6.069   0.62  49.86  ? 99   LYS B CB  1 
ATOM   3048 C CG  . LYS B 1 99  ? 25.411  -0.375  5.598   0.62  49.25  ? 99   LYS B CG  1 
ATOM   3049 C CD  . LYS B 1 99  ? 26.219  -1.571  5.088   0.62  48.36  ? 99   LYS B CD  1 
ATOM   3050 C CE  . LYS B 1 99  ? 27.536  -1.135  4.447   0.62  48.19  ? 99   LYS B CE  1 
ATOM   3051 N NZ  . LYS B 1 99  ? 28.311  -2.283  3.886   0.62  47.45  ? 99   LYS B NZ  1 
ATOM   3052 N N   . LYS B 1 100 ? 22.583  0.665   8.611   1.00  50.71  ? 100  LYS B N   1 
ATOM   3053 C CA  . LYS B 1 100 ? 22.647  1.382   9.897   1.00  51.06  ? 100  LYS B CA  1 
ATOM   3054 C C   . LYS B 1 100 ? 24.087  1.471   10.432  1.00  51.49  ? 100  LYS B C   1 
ATOM   3055 O O   . LYS B 1 100 ? 24.455  2.467   11.060  1.00  51.99  ? 100  LYS B O   1 
ATOM   3056 C CB  . LYS B 1 100 ? 21.748  0.709   10.947  1.00  51.28  ? 100  LYS B CB  1 
ATOM   3057 C CG  . LYS B 1 100 ? 20.244  0.981   10.874  1.00  50.55  ? 100  LYS B CG  1 
ATOM   3058 C CD  . LYS B 1 100 ? 19.479  -0.172  11.531  1.00  50.70  ? 100  LYS B CD  1 
ATOM   3059 C CE  . LYS B 1 100 ? 18.426  0.311   12.568  1.00  51.74  ? 100  LYS B CE  1 
ATOM   3060 N NZ  . LYS B 1 100 ? 17.571  -0.804  13.114  1.00  49.87  ? 100  LYS B NZ  1 
ATOM   3061 N N   . ASP B 1 101 ? 24.881  0.425   10.176  0.010 51.53  ? 101  ASP B N   1 
ATOM   3062 C CA  . ASP B 1 101 ? 26.317  0.352   10.521  0.010 51.61  ? 101  ASP B CA  1 
ATOM   3063 C C   . ASP B 1 101 ? 26.637  0.408   12.017  0.010 51.74  ? 101  ASP B C   1 
ATOM   3064 O O   . ASP B 1 101 ? 27.506  1.177   12.442  0.010 51.74  ? 101  ASP B O   1 
ATOM   3065 C CB  . ASP B 1 101 ? 27.129  1.404   9.752   0.010 51.57  ? 101  ASP B CB  1 
ATOM   3066 C CG  . ASP B 1 101 ? 27.085  1.188   8.253   0.010 51.53  ? 101  ASP B CG  1 
ATOM   3067 O OD1 . ASP B 1 101 ? 26.423  0.226   7.811   0.010 51.52  ? 101  ASP B OD1 1 
ATOM   3068 O OD2 . ASP B 1 101 ? 27.712  1.979   7.516   0.010 51.52  ? 101  ASP B OD2 1 
ATOM   3069 N N   . LYS B 1 102 ? 25.937  -0.427  12.790  1.00  52.05  ? 102  LYS B N   1 
ATOM   3070 C CA  . LYS B 1 102 ? 26.135  -0.542  14.246  1.00  52.18  ? 102  LYS B CA  1 
ATOM   3071 C C   . LYS B 1 102 ? 26.008  0.838   14.887  1.00  51.74  ? 102  LYS B C   1 
ATOM   3072 O O   . LYS B 1 102 ? 26.566  1.111   15.976  1.00  52.45  ? 102  LYS B O   1 
ATOM   3073 C CB  . LYS B 1 102 ? 27.524  -1.135  14.562  1.00  52.49  ? 102  LYS B CB  1 
ATOM   3074 C CG  . LYS B 1 102 ? 27.555  -2.008  15.848  1.00  53.31  ? 102  LYS B CG  1 
ATOM   3075 C CD  . LYS B 1 102 ? 28.954  -1.975  16.482  1.00  54.89  ? 102  LYS B CD  1 
ATOM   3076 C CE  . LYS B 1 102 ? 30.027  -2.506  15.500  1.00  55.78  ? 102  LYS B CE  1 
ATOM   3077 N NZ  . LYS B 1 102 ? 31.255  -1.638  15.506  1.00  56.34  ? 102  LYS B NZ  1 
ATOM   3078 N N   . SER B 1 103 ? 25.307  1.712   14.164  0.010 50.89  ? 103  SER B N   1 
ATOM   3079 C CA  . SER B 1 103 ? 24.968  3.018   14.687  0.010 50.00  ? 103  SER B CA  1 
ATOM   3080 C C   . SER B 1 103 ? 23.460  2.981   14.745  0.010 49.42  ? 103  SER B C   1 
ATOM   3081 O O   . SER B 1 103 ? 22.842  2.014   14.290  0.010 49.36  ? 103  SER B O   1 
ATOM   3082 C CB  . SER B 1 103 ? 25.452  4.124   13.745  0.010 50.03  ? 103  SER B CB  1 
ATOM   3083 O OG  . SER B 1 103 ? 25.044  5.403   14.201  0.010 49.96  ? 103  SER B OG  1 
ATOM   3084 N N   . ARG B 1 104 ? 22.869  4.022   15.317  1.00  48.74  ? 104  ARG B N   1 
ATOM   3085 C CA  . ARG B 1 104 ? 21.422  4.196   15.311  1.00  47.87  ? 104  ARG B CA  1 
ATOM   3086 C C   . ARG B 1 104 ? 21.049  5.190   14.200  1.00  47.49  ? 104  ARG B C   1 
ATOM   3087 O O   . ARG B 1 104 ? 20.330  6.167   14.430  1.00  47.19  ? 104  ARG B O   1 
ATOM   3088 C CB  . ARG B 1 104 ? 20.967  4.697   16.677  1.00  47.81  ? 104  ARG B CB  1 
ATOM   3089 C CG  . ARG B 1 104 ? 19.598  4.217   17.131  1.00  47.74  ? 104  ARG B CG  1 
ATOM   3090 C CD  . ARG B 1 104 ? 19.627  3.799   18.606  1.00  47.68  ? 104  ARG B CD  1 
ATOM   3091 N NE  . ARG B 1 104 ? 20.543  4.626   19.394  1.00  48.45  ? 104  ARG B NE  1 
ATOM   3092 C CZ  . ARG B 1 104 ? 21.118  4.261   20.537  1.00  49.20  ? 104  ARG B CZ  1 
ATOM   3093 N NH1 . ARG B 1 104 ? 20.893  3.067   21.072  1.00  51.54  ? 104  ARG B NH1 1 
ATOM   3094 N NH2 . ARG B 1 104 ? 21.930  5.096   21.154  1.00  49.32  ? 104  ARG B NH2 1 
ATOM   3095 N N   . ALA B 1 105 ? 21.555  4.926   12.995  1.00  46.93  ? 105  ALA B N   1 
ATOM   3096 C CA  . ALA B 1 105 ? 21.396  5.823   11.851  1.00  46.58  ? 105  ALA B CA  1 
ATOM   3097 C C   . ALA B 1 105 ? 20.249  5.424   10.922  1.00  46.25  ? 105  ALA B C   1 
ATOM   3098 O O   . ALA B 1 105 ? 19.833  4.266   10.898  1.00  46.19  ? 105  ALA B O   1 
ATOM   3099 C CB  . ALA B 1 105 ? 22.701  5.903   11.051  1.00  46.78  ? 105  ALA B CB  1 
ATOM   3100 N N   . PRO B 1 106 ? 19.732  6.391   10.145  0.85  45.94  ? 106  PRO B N   1 
ATOM   3101 C CA  . PRO B 1 106 ? 18.773  6.032   9.107   0.85  45.59  ? 106  PRO B CA  1 
ATOM   3102 C C   . PRO B 1 106 ? 19.460  5.336   7.937   0.85  45.12  ? 106  PRO B C   1 
ATOM   3103 O O   . PRO B 1 106 ? 20.627  5.600   7.643   0.85  45.09  ? 106  PRO B O   1 
ATOM   3104 C CB  . PRO B 1 106 ? 18.262  7.393   8.634   0.85  45.65  ? 106  PRO B CB  1 
ATOM   3105 C CG  . PRO B 1 106 ? 19.452  8.304   8.864   0.85  45.57  ? 106  PRO B CG  1 
ATOM   3106 C CD  . PRO B 1 106 ? 19.994  7.844   10.173  0.85  45.66  ? 106  PRO B CD  1 
ATOM   3107 N N   . ILE B 1 107 ? 18.733  4.451   7.276   1.00  44.60  ? 107  ILE B N   1 
ATOM   3108 C CA  . ILE B 1 107 ? 19.168  3.920   5.992   1.00  43.86  ? 107  ILE B CA  1 
ATOM   3109 C C   . ILE B 1 107 ? 18.601  4.840   4.894   1.00  43.14  ? 107  ILE B C   1 
ATOM   3110 O O   . ILE B 1 107 ? 17.536  4.578   4.318   1.00  43.05  ? 107  ILE B O   1 
ATOM   3111 C CB  . ILE B 1 107 ? 18.758  2.427   5.863   1.00  44.18  ? 107  ILE B CB  1 
ATOM   3112 C CG1 . ILE B 1 107 ? 19.397  1.637   7.024   1.00  44.54  ? 107  ILE B CG1 1 
ATOM   3113 C CG2 . ILE B 1 107 ? 19.129  1.862   4.480   1.00  43.44  ? 107  ILE B CG2 1 
ATOM   3114 C CD1 . ILE B 1 107 ? 19.098  0.148   7.054   1.00  45.76  ? 107  ILE B CD1 1 
ATOM   3115 N N   . SER B 1 108 ? 19.309  5.945   4.650   1.00  42.31  ? 108  SER B N   1 
ATOM   3116 C CA  . SER B 1 108 ? 18.828  7.028   3.777   1.00  41.33  ? 108  SER B CA  1 
ATOM   3117 C C   . SER B 1 108 ? 18.564  6.602   2.339   1.00  40.85  ? 108  SER B C   1 
ATOM   3118 O O   . SER B 1 108 ? 17.682  7.165   1.687   1.00  41.18  ? 108  SER B O   1 
ATOM   3119 C CB  . SER B 1 108 ? 19.801  8.205   3.783   1.00  41.57  ? 108  SER B CB  1 
ATOM   3120 O OG  . SER B 1 108 ? 19.658  8.983   4.961   1.00  40.60  ? 108  SER B OG  1 
ATOM   3121 N N   . ALA B 1 109 ? 19.332  5.623   1.856   1.00  39.84  ? 109  ALA B N   1 
ATOM   3122 C CA  . ALA B 1 109 ? 19.141  5.055   0.527   1.00  38.78  ? 109  ALA B CA  1 
ATOM   3123 C C   . ALA B 1 109 ? 17.714  4.535   0.364   1.00  38.04  ? 109  ALA B C   1 
ATOM   3124 O O   . ALA B 1 109 ? 17.019  4.891   -0.590  1.00  38.03  ? 109  ALA B O   1 
ATOM   3125 C CB  . ALA B 1 109 ? 20.164  3.956   0.258   1.00  38.60  ? 109  ALA B CB  1 
ATOM   3126 N N   . LYS B 1 110 ? 17.272  3.731   1.325   1.00  37.33  ? 110  LYS B N   1 
ATOM   3127 C CA  . LYS B 1 110 ? 15.898  3.214   1.344   1.00  36.73  ? 110  LYS B CA  1 
ATOM   3128 C C   . LYS B 1 110 ? 14.858  4.345   1.426   1.00  36.28  ? 110  LYS B C   1 
ATOM   3129 O O   . LYS B 1 110 ? 13.804  4.279   0.775   1.00  36.27  ? 110  LYS B O   1 
ATOM   3130 C CB  . LYS B 1 110 ? 15.703  2.214   2.499   1.00  36.36  ? 110  LYS B CB  1 
ATOM   3131 C CG  . LYS B 1 110 ? 14.284  1.655   2.613   1.00  35.97  ? 110  LYS B CG  1 
ATOM   3132 C CD  . LYS B 1 110 ? 13.953  0.648   1.500   1.00  34.83  ? 110  LYS B CD  1 
ATOM   3133 C CE  . LYS B 1 110 ? 12.479  0.267   1.486   1.00  35.91  ? 110  LYS B CE  1 
ATOM   3134 N NZ  . LYS B 1 110 ? 12.005  -0.245  2.840   1.00  36.97  ? 110  LYS B NZ  1 
ATOM   3135 N N   . LEU B 1 111 ? 15.158  5.377   2.215   1.00  35.38  ? 111  LEU B N   1 
ATOM   3136 C CA  . LEU B 1 111 ? 14.255  6.521   2.337   1.00  34.70  ? 111  LEU B CA  1 
ATOM   3137 C C   . LEU B 1 111 ? 14.090  7.228   0.995   1.00  34.34  ? 111  LEU B C   1 
ATOM   3138 O O   . LEU B 1 111 ? 12.975  7.460   0.550   1.00  34.53  ? 111  LEU B O   1 
ATOM   3139 C CB  . LEU B 1 111 ? 14.732  7.492   3.426   1.00  34.96  ? 111  LEU B CB  1 
ATOM   3140 C CG  . LEU B 1 111 ? 13.858  8.696   3.833   1.00  34.56  ? 111  LEU B CG  1 
ATOM   3141 C CD1 . LEU B 1 111 ? 12.414  8.313   4.203   1.00  32.80  ? 111  LEU B CD1 1 
ATOM   3142 C CD2 . LEU B 1 111 ? 14.534  9.489   4.976   1.00  33.11  ? 111  LEU B CD2 1 
ATOM   3143 N N   . VAL B 1 112 ? 15.203  7.549   0.339   1.00  33.97  ? 112  VAL B N   1 
ATOM   3144 C CA  . VAL B 1 112 ? 15.175  8.119   -1.013  1.00  32.94  ? 112  VAL B CA  1 
ATOM   3145 C C   . VAL B 1 112 ? 14.442  7.177   -1.990  1.00  32.64  ? 112  VAL B C   1 
ATOM   3146 O O   . VAL B 1 112 ? 13.694  7.631   -2.871  1.00  32.53  ? 112  VAL B O   1 
ATOM   3147 C CB  . VAL B 1 112 ? 16.596  8.456   -1.479  1.00  32.92  ? 112  VAL B CB  1 
ATOM   3148 C CG1 . VAL B 1 112 ? 16.632  8.880   -2.959  1.00  32.76  ? 112  VAL B CG1 1 
ATOM   3149 C CG2 . VAL B 1 112 ? 17.164  9.546   -0.585  1.00  33.03  ? 112  VAL B CG2 1 
ATOM   3150 N N   . ALA B 1 113 ? 14.635  5.873   -1.814  1.00  31.77  ? 113  ALA B N   1 
ATOM   3151 C CA  . ALA B 1 113 ? 13.924  4.892   -2.621  1.00  31.34  ? 113  ALA B CA  1 
ATOM   3152 C C   . ALA B 1 113 ? 12.403  4.952   -2.369  1.00  31.41  ? 113  ALA B C   1 
ATOM   3153 O O   . ALA B 1 113 ? 11.597  4.850   -3.320  1.00  31.48  ? 113  ALA B O   1 
ATOM   3154 C CB  . ALA B 1 113 ? 14.463  3.492   -2.366  1.00  31.18  ? 113  ALA B CB  1 
ATOM   3155 N N   . ASN B 1 114 ? 12.007  5.109   -1.100  1.00  30.68  ? 114  ASN B N   1 
ATOM   3156 C CA  . ASN B 1 114 ? 10.589  5.205   -0.763  1.00  29.86  ? 114  ASN B CA  1 
ATOM   3157 C C   . ASN B 1 114 ? 10.011  6.523   -1.270  1.00  29.54  ? 114  ASN B C   1 
ATOM   3158 O O   . ASN B 1 114 ? 8.864   6.591   -1.720  1.00  30.33  ? 114  ASN B O   1 
ATOM   3159 C CB  . ASN B 1 114 ? 10.362  5.103   0.750   1.00  29.82  ? 114  ASN B CB  1 
ATOM   3160 C CG  . ASN B 1 114 ? 10.498  3.668   1.302   1.00  29.63  ? 114  ASN B CG  1 
ATOM   3161 O OD1 . ASN B 1 114 ? 10.443  2.667   0.570   1.00  28.15  ? 114  ASN B OD1 1 
ATOM   3162 N ND2 . ASN B 1 114 ? 10.640  3.584   2.628   1.00  29.63  ? 114  ASN B ND2 1 
ATOM   3163 N N   . MET B 1 115 ? 10.800  7.582   -1.187  1.00  28.98  ? 115  MET B N   1 
ATOM   3164 C CA  . MET B 1 115 ? 10.332  8.907   -1.599  1.00  28.54  ? 115  MET B CA  1 
ATOM   3165 C C   . MET B 1 115 ? 10.127  8.972   -3.111  1.00  27.73  ? 115  MET B C   1 
ATOM   3166 O O   . MET B 1 115 ? 9.087   9.429   -3.577  1.00  27.24  ? 115  MET B O   1 
ATOM   3167 C CB  . MET B 1 115 ? 11.279  10.000  -1.103  1.00  28.62  ? 115  MET B CB  1 
ATOM   3168 C CG  . MET B 1 115 ? 11.353  10.104  0.425   1.00  29.52  ? 115  MET B CG  1 
ATOM   3169 S SD  . MET B 1 115 ? 12.328  11.515  1.017   1.00  32.69  ? 115  MET B SD  1 
ATOM   3170 C CE  . MET B 1 115 ? 13.981  11.043  0.649   1.00  32.16  ? 115  MET B CE  1 
ATOM   3171 N N   . LEU B 1 116 ? 11.104  8.471   -3.861  1.00  27.50  ? 116  LEU B N   1 
ATOM   3172 C CA  . LEU B 1 116 ? 10.977  8.342   -5.312  1.00  27.65  ? 116  LEU B CA  1 
ATOM   3173 C C   . LEU B 1 116 ? 9.732   7.530   -5.710  1.00  28.13  ? 116  LEU B C   1 
ATOM   3174 O O   . LEU B 1 116 ? 8.975   7.924   -6.614  1.00  27.93  ? 116  LEU B O   1 
ATOM   3175 C CB  . LEU B 1 116 ? 12.264  7.761   -5.920  1.00  27.31  ? 116  LEU B CB  1 
ATOM   3176 C CG  . LEU B 1 116 ? 13.497  8.685   -5.907  1.00  26.32  ? 116  LEU B CG  1 
ATOM   3177 C CD1 . LEU B 1 116 ? 14.771  7.918   -6.215  1.00  23.60  ? 116  LEU B CD1 1 
ATOM   3178 C CD2 . LEU B 1 116 ? 13.302  9.840   -6.893  1.00  23.81  ? 116  LEU B CD2 1 
ATOM   3179 N N   . SER B 1 117 ? 9.512   6.420   -5.003  1.00  28.45  ? 117  SER B N   1 
ATOM   3180 C CA  . SER B 1 117 ? 8.368   5.542   -5.242  1.00  29.29  ? 117  SER B CA  1 
ATOM   3181 C C   . SER B 1 117 ? 7.003   6.221   -5.037  1.00  29.40  ? 117  SER B C   1 
ATOM   3182 O O   . SER B 1 117 ? 6.137   6.181   -5.935  1.00  29.40  ? 117  SER B O   1 
ATOM   3183 C CB  . SER B 1 117 ? 8.463   4.301   -4.358  1.00  29.60  ? 117  SER B CB  1 
ATOM   3184 O OG  . SER B 1 117 ? 9.744   3.694   -4.483  1.00  32.74  ? 117  SER B OG  1 
ATOM   3185 N N   . VAL B 1 118 ? 6.796   6.835   -3.870  1.00  29.17  ? 118  VAL B N   1 
ATOM   3186 C CA  . VAL B 1 118 ? 5.507   7.499   -3.601  1.00  29.44  ? 118  VAL B CA  1 
ATOM   3187 C C   . VAL B 1 118 ? 5.299   8.787   -4.397  1.00  29.39  ? 118  VAL B C   1 
ATOM   3188 O O   . VAL B 1 118 ? 4.156   9.174   -4.667  1.00  30.19  ? 118  VAL B O   1 
ATOM   3189 C CB  . VAL B 1 118 ? 5.226   7.744   -2.076  1.00  29.67  ? 118  VAL B CB  1 
ATOM   3190 C CG1 . VAL B 1 118 ? 5.424   6.426   -1.284  1.00  30.47  ? 118  VAL B CG1 1 
ATOM   3191 C CG2 . VAL B 1 118 ? 6.131   8.856   -1.496  1.00  30.17  ? 118  VAL B CG2 1 
ATOM   3192 N N   . ALA B 1 119 ? 6.385   9.448   -4.782  1.00  29.06  ? 119  ALA B N   1 
ATOM   3193 C CA  . ALA B 1 119 ? 6.264   10.633  -5.627  1.00  29.02  ? 119  ALA B CA  1 
ATOM   3194 C C   . ALA B 1 119 ? 5.661   10.282  -6.976  1.00  28.62  ? 119  ALA B C   1 
ATOM   3195 O O   . ALA B 1 119 ? 5.144   11.160  -7.654  1.00  29.15  ? 119  ALA B O   1 
ATOM   3196 C CB  . ALA B 1 119 ? 7.614   11.341  -5.797  1.00  29.12  ? 119  ALA B CB  1 
ATOM   3197 N N   . GLY B 1 120 ? 5.738   9.000   -7.349  1.00  28.36  ? 120  GLY B N   1 
ATOM   3198 C CA  . GLY B 1 120 ? 5.136   8.481   -8.582  1.00  27.79  ? 120  GLY B CA  1 
ATOM   3199 C C   . GLY B 1 120 ? 6.053   7.816   -9.602  1.00  27.41  ? 120  GLY B C   1 
ATOM   3200 O O   . GLY B 1 120 ? 5.608   7.456   -10.681 1.00  27.31  ? 120  GLY B O   1 
ATOM   3201 N N   . ALA B 1 121 ? 7.328   7.639   -9.260  1.00  27.49  ? 121  ALA B N   1 
ATOM   3202 C CA  . ALA B 1 121 ? 8.305   6.974   -10.138 1.00  27.28  ? 121  ALA B CA  1 
ATOM   3203 C C   . ALA B 1 121 ? 7.930   5.522   -10.497 1.00  27.10  ? 121  ALA B C   1 
ATOM   3204 O O   . ALA B 1 121 ? 7.586   4.741   -9.622  1.00  27.04  ? 121  ALA B O   1 
ATOM   3205 C CB  . ALA B 1 121 ? 9.682   7.019   -9.493  1.00  26.96  ? 121  ALA B CB  1 
ATOM   3206 N N   . ASP B 1 122 ? 8.008   5.179   -11.782 1.00  26.98  ? 122  ASP B N   1 
ATOM   3207 C CA  . ASP B 1 122 ? 7.715   3.832   -12.275 1.00  27.27  ? 122  ASP B CA  1 
ATOM   3208 C C   . ASP B 1 122 ? 8.962   3.042   -12.599 1.00  28.13  ? 122  ASP B C   1 
ATOM   3209 O O   . ASP B 1 122 ? 8.912   1.808   -12.796 1.00  28.54  ? 122  ASP B O   1 
ATOM   3210 C CB  . ASP B 1 122 ? 6.906   3.875   -13.570 1.00  27.00  ? 122  ASP B CB  1 
ATOM   3211 C CG  . ASP B 1 122 ? 5.603   4.622   -13.433 1.00  27.18  ? 122  ASP B CG  1 
ATOM   3212 O OD1 . ASP B 1 122 ? 4.819   4.360   -12.485 1.00  26.12  ? 122  ASP B OD1 1 
ATOM   3213 O OD2 . ASP B 1 122 ? 5.358   5.479   -14.306 1.00  27.15  ? 122  ASP B OD2 1 
ATOM   3214 N N   . HIS B 1 123 ? 10.086  3.740   -12.704 1.00  29.13  ? 123  HIS B N   1 
ATOM   3215 C CA  . HIS B 1 123 ? 11.293  3.093   -13.165 1.00  29.82  ? 123  HIS B CA  1 
ATOM   3216 C C   . HIS B 1 123 ? 12.481  3.927   -12.759 1.00  29.93  ? 123  HIS B C   1 
ATOM   3217 O O   . HIS B 1 123 ? 12.350  5.146   -12.539 1.00  29.81  ? 123  HIS B O   1 
ATOM   3218 C CB  . HIS B 1 123 ? 11.226  2.905   -14.691 1.00  30.37  ? 123  HIS B CB  1 
ATOM   3219 C CG  . HIS B 1 123 ? 12.418  2.216   -15.273 1.00  32.44  ? 123  HIS B CG  1 
ATOM   3220 N ND1 . HIS B 1 123 ? 12.971  1.082   -14.712 1.00  35.19  ? 123  HIS B ND1 1 
ATOM   3221 C CD2 . HIS B 1 123 ? 13.153  2.489   -16.376 1.00  33.47  ? 123  HIS B CD2 1 
ATOM   3222 C CE1 . HIS B 1 123 ? 14.002  0.693   -15.439 1.00  36.04  ? 123  HIS B CE1 1 
ATOM   3223 N NE2 . HIS B 1 123 ? 14.133  1.527   -16.457 1.00  36.02  ? 123  HIS B NE2 1 
ATOM   3224 N N   . ILE B 1 124 ? 13.628  3.259   -12.637 1.00  30.44  ? 124  ILE B N   1 
ATOM   3225 C CA  . ILE B 1 124 ? 14.884  3.914   -12.275 1.00  31.04  ? 124  ILE B CA  1 
ATOM   3226 C C   . ILE B 1 124 ? 15.994  3.552   -13.273 1.00  31.91  ? 124  ILE B C   1 
ATOM   3227 O O   . ILE B 1 124 ? 16.174  2.381   -13.655 1.00  31.90  ? 124  ILE B O   1 
ATOM   3228 C CB  . ILE B 1 124 ? 15.308  3.575   -10.823 1.00  30.66  ? 124  ILE B CB  1 
ATOM   3229 C CG1 . ILE B 1 124 ? 14.163  3.839   -9.822  1.00  30.02  ? 124  ILE B CG1 1 
ATOM   3230 C CG2 . ILE B 1 124 ? 16.582  4.324   -10.423 1.00  31.45  ? 124  ILE B CG2 1 
ATOM   3231 C CD1 . ILE B 1 124 ? 13.763  5.329   -9.632  1.00  26.81  ? 124  ILE B CD1 1 
ATOM   3232 N N   . ILE B 1 125 ? 16.697  4.579   -13.742 1.00  32.73  ? 125  ILE B N   1 
ATOM   3233 C CA  . ILE B 1 125 ? 17.946  4.361   -14.471 1.00  33.44  ? 125  ILE B CA  1 
ATOM   3234 C C   . ILE B 1 125 ? 19.011  5.058   -13.644 1.00  34.10  ? 125  ILE B C   1 
ATOM   3235 O O   . ILE B 1 125 ? 18.873  6.229   -13.300 1.00  34.44  ? 125  ILE B O   1 
ATOM   3236 C CB  . ILE B 1 125 ? 17.895  4.877   -15.949 1.00  33.27  ? 125  ILE B CB  1 
ATOM   3237 C CG1 . ILE B 1 125 ? 16.887  4.049   -16.765 1.00  32.80  ? 125  ILE B CG1 1 
ATOM   3238 C CG2 . ILE B 1 125 ? 19.266  4.784   -16.594 1.00  32.53  ? 125  ILE B CG2 1 
ATOM   3239 C CD1 . ILE B 1 125 ? 16.515  4.604   -18.124 1.00  30.76  ? 125  ILE B CD1 1 
ATOM   3240 N N   . THR B 1 126 ? 20.047  4.314   -13.290 1.00  35.13  ? 126  THR B N   1 
ATOM   3241 C CA  . THR B 1 126 ? 21.124  4.822   -12.451 1.00  36.21  ? 126  THR B CA  1 
ATOM   3242 C C   . THR B 1 126 ? 22.461  4.233   -12.922 1.00  37.31  ? 126  THR B C   1 
ATOM   3243 O O   . THR B 1 126 ? 22.491  3.353   -13.788 1.00  37.77  ? 126  THR B O   1 
ATOM   3244 C CB  . THR B 1 126 ? 20.841  4.505   -10.955 1.00  35.95  ? 126  THR B CB  1 
ATOM   3245 O OG1 . THR B 1 126 ? 21.615  5.362   -10.105 1.00  36.39  ? 126  THR B OG1 1 
ATOM   3246 C CG2 . THR B 1 126 ? 21.129  3.042   -10.632 1.00  35.82  ? 126  THR B CG2 1 
ATOM   3247 N N   . MET B 1 127 ? 23.566  4.712   -12.365 1.00  38.90  ? 127  MET B N   1 
ATOM   3248 C CA  . MET B 1 127 ? 24.873  4.172   -12.727 1.00  40.73  ? 127  MET B CA  1 
ATOM   3249 C C   . MET B 1 127 ? 25.795  3.891   -11.537 1.00  41.70  ? 127  MET B C   1 
ATOM   3250 O O   . MET B 1 127 ? 25.947  4.721   -10.646 1.00  42.03  ? 127  MET B O   1 
ATOM   3251 C CB  . MET B 1 127 ? 25.576  5.085   -13.724 1.00  40.98  ? 127  MET B CB  1 
ATOM   3252 C CG  . MET B 1 127 ? 26.671  4.390   -14.499 1.00  42.32  ? 127  MET B CG  1 
ATOM   3253 S SD  . MET B 1 127 ? 27.408  5.507   -15.684 1.00  46.54  ? 127  MET B SD  1 
ATOM   3254 C CE  . MET B 1 127 ? 26.033  5.735   -16.808 1.00  43.60  ? 127  MET B CE  1 
ATOM   3255 N N   . ASP B 1 128 ? 26.419  2.714   -11.569 1.00  42.98  ? 128  ASP B N   1 
ATOM   3256 C CA  . ASP B 1 128 ? 27.323  2.196   -10.527 1.00  44.54  ? 128  ASP B CA  1 
ATOM   3257 C C   . ASP B 1 128 ? 27.017  2.533   -9.044  1.00  45.11  ? 128  ASP B C   1 
ATOM   3258 O O   . ASP B 1 128 ? 27.873  3.121   -8.337  1.00  45.77  ? 128  ASP B O   1 
ATOM   3259 C CB  . ASP B 1 128 ? 28.781  2.524   -10.858 1.00  44.84  ? 128  ASP B CB  1 
ATOM   3260 C CG  . ASP B 1 128 ? 29.264  1.816   -12.110 1.00  47.03  ? 128  ASP B CG  1 
ATOM   3261 O OD1 . ASP B 1 128 ? 30.217  0.990   -12.024 1.00  47.74  ? 128  ASP B OD1 1 
ATOM   3262 O OD2 . ASP B 1 128 ? 28.679  2.092   -13.186 1.00  48.14  ? 128  ASP B OD2 1 
ATOM   3263 N N   . LEU B 1 129 ? 25.826  2.142   -8.570  1.00  45.44  ? 129  LEU B N   1 
ATOM   3264 C CA  . LEU B 1 129 ? 25.470  2.330   -7.154  1.00  46.06  ? 129  LEU B CA  1 
ATOM   3265 C C   . LEU B 1 129 ? 26.619  1.970   -6.206  1.00  46.28  ? 129  LEU B C   1 
ATOM   3266 O O   . LEU B 1 129 ? 27.178  0.867   -6.294  1.00  46.69  ? 129  LEU B O   1 
ATOM   3267 C CB  . LEU B 1 129 ? 24.227  1.505   -6.782  1.00  46.30  ? 129  LEU B CB  1 
ATOM   3268 C CG  . LEU B 1 129 ? 22.872  1.922   -7.356  1.00  46.34  ? 129  LEU B CG  1 
ATOM   3269 C CD1 . LEU B 1 129 ? 21.866  0.798   -7.266  1.00  47.55  ? 129  LEU B CD1 1 
ATOM   3270 C CD2 . LEU B 1 129 ? 22.364  3.136   -6.622  1.00  47.01  ? 129  LEU B CD2 1 
ATOM   3271 N N   . HIS B 1 130 ? 26.968  2.908   -5.320  0.10  46.37  ? 130  HIS B N   1 
ATOM   3272 C CA  . HIS B 1 130 ? 28.025  2.722   -4.314  0.10  46.51  ? 130  HIS B CA  1 
ATOM   3273 C C   . HIS B 1 130 ? 27.995  1.303   -3.754  0.10  46.80  ? 130  HIS B C   1 
ATOM   3274 O O   . HIS B 1 130 ? 29.006  0.598   -3.763  0.10  46.74  ? 130  HIS B O   1 
ATOM   3275 C CB  . HIS B 1 130 ? 27.879  3.750   -3.186  0.10  46.41  ? 130  HIS B CB  1 
ATOM   3276 C CG  . HIS B 1 130 ? 28.581  3.366   -1.921  0.10  46.17  ? 130  HIS B CG  1 
ATOM   3277 N ND1 . HIS B 1 130 ? 29.928  3.582   -1.721  0.10  46.01  ? 130  HIS B ND1 1 
ATOM   3278 C CD2 . HIS B 1 130 ? 28.122  2.782   -0.789  0.10  45.92  ? 130  HIS B CD2 1 
ATOM   3279 C CE1 . HIS B 1 130 ? 30.268  3.146   -0.520  0.10  45.81  ? 130  HIS B CE1 1 
ATOM   3280 N NE2 . HIS B 1 130 ? 29.191  2.656   0.065   0.10  45.80  ? 130  HIS B NE2 1 
ATOM   3281 N N   . ALA B 1 131 ? 26.823  0.904   -3.269  1.00  47.35  ? 131  ALA B N   1 
ATOM   3282 C CA  . ALA B 1 131 ? 26.503  -0.501  -3.042  1.00  47.86  ? 131  ALA B CA  1 
ATOM   3283 C C   . ALA B 1 131 ? 25.365  -0.853  -3.991  1.00  48.20  ? 131  ALA B C   1 
ATOM   3284 O O   . ALA B 1 131 ? 24.324  -0.199  -3.988  1.00  48.57  ? 131  ALA B O   1 
ATOM   3285 C CB  . ALA B 1 131 ? 26.097  -0.744  -1.599  1.00  47.65  ? 131  ALA B CB  1 
ATOM   3286 N N   . SER B 1 132 ? 25.575  -1.873  -4.818  1.00  48.31  ? 132  SER B N   1 
ATOM   3287 C CA  . SER B 1 132 ? 24.570  -2.308  -5.802  1.00  48.27  ? 132  SER B CA  1 
ATOM   3288 C C   . SER B 1 132 ? 23.196  -2.718  -5.227  1.00  48.06  ? 132  SER B C   1 
ATOM   3289 O O   . SER B 1 132 ? 22.151  -2.592  -5.946  1.00  48.27  ? 132  SER B O   1 
ATOM   3290 C CB  . SER B 1 132 ? 25.120  -3.470  -6.641  1.00  48.38  ? 132  SER B CB  1 
ATOM   3291 O OG  . SER B 1 132 ? 26.311  -3.111  -7.330  1.00  49.80  ? 132  SER B OG  1 
ATOM   3292 N N   . PRO B 1 133 ? 23.196  -3.211  -3.930  1.00  47.35  ? 133  PRO B N   1 
ATOM   3293 C CA  . PRO B 1 133 ? 22.006  -3.813  -3.320  1.00  46.98  ? 133  PRO B CA  1 
ATOM   3294 C C   . PRO B 1 133 ? 20.888  -2.817  -3.144  1.00  46.54  ? 133  PRO B C   1 
ATOM   3295 O O   . PRO B 1 133 ? 19.871  -3.108  -2.476  1.00  46.89  ? 133  PRO B O   1 
ATOM   3296 C CB  . PRO B 1 133 ? 22.517  -4.255  -1.954  1.00  47.25  ? 133  PRO B CB  1 
ATOM   3297 C CG  . PRO B 1 133 ? 23.882  -4.694  -2.236  1.00  47.29  ? 133  PRO B CG  1 
ATOM   3298 C CD  . PRO B 1 133 ? 24.424  -3.728  -3.242  1.00  47.32  ? 133  PRO B CD  1 
ATOM   3299 N N   . ILE B 1 134 ? 21.080  -1.641  -3.731  1.00  45.53  ? 134  ILE B N   1 
ATOM   3300 C CA  . ILE B 1 134 ? 20.087  -0.597  -3.631  1.00  44.54  ? 134  ILE B CA  1 
ATOM   3301 C C   . ILE B 1 134 ? 18.910  -0.875  -4.569  1.00  43.45  ? 134  ILE B C   1 
ATOM   3302 O O   . ILE B 1 134 ? 17.803  -0.392  -4.326  1.00  43.21  ? 134  ILE B O   1 
ATOM   3303 C CB  . ILE B 1 134 ? 20.729  0.810   -3.818  1.00  45.03  ? 134  ILE B CB  1 
ATOM   3304 C CG1 . ILE B 1 134 ? 21.312  1.306   -2.484  1.00  44.39  ? 134  ILE B CG1 1 
ATOM   3305 C CG2 . ILE B 1 134 ? 19.715  1.845   -4.317  1.00  44.94  ? 134  ILE B CG2 1 
ATOM   3306 C CD1 . ILE B 1 134 ? 22.725  0.879   -2.204  1.00  44.63  ? 134  ILE B CD1 1 
ATOM   3307 N N   . GLN B 1 135 ? 19.132  -1.684  -5.608  1.00  42.32  ? 135  GLN B N   1 
ATOM   3308 C CA  . GLN B 1 135 ? 18.016  -2.139  -6.458  1.00  41.25  ? 135  GLN B CA  1 
ATOM   3309 C C   . GLN B 1 135 ? 16.994  -2.857  -5.578  1.00  40.33  ? 135  GLN B C   1 
ATOM   3310 O O   . GLN B 1 135 ? 15.786  -2.776  -5.821  1.00  40.19  ? 135  GLN B O   1 
ATOM   3311 C CB  . GLN B 1 135 ? 18.455  -3.064  -7.601  1.00  41.50  ? 135  GLN B CB  1 
ATOM   3312 C CG  . GLN B 1 135 ? 19.947  -2.993  -8.051  1.00  42.96  ? 135  GLN B CG  1 
ATOM   3313 C CD  . GLN B 1 135 ? 20.715  -4.309  -7.797  1.00  43.51  ? 135  GLN B CD  1 
ATOM   3314 O OE1 . GLN B 1 135 ? 20.138  -5.333  -7.410  1.00  44.14  ? 135  GLN B OE1 1 
ATOM   3315 N NE2 . GLN B 1 135 ? 22.011  -4.279  -8.034  1.00  43.67  ? 135  GLN B NE2 1 
ATOM   3316 N N   . GLY B 1 136 ? 17.489  -3.533  -4.535  1.00  39.06  ? 136  GLY B N   1 
ATOM   3317 C CA  . GLY B 1 136 ? 16.639  -4.177  -3.536  1.00  37.42  ? 136  GLY B CA  1 
ATOM   3318 C C   . GLY B 1 136 ? 15.818  -3.241  -2.660  1.00  36.59  ? 136  GLY B C   1 
ATOM   3319 O O   . GLY B 1 136 ? 14.927  -3.688  -1.944  1.00  36.51  ? 136  GLY B O   1 
ATOM   3320 N N   . PHE B 1 137 ? 16.101  -1.940  -2.712  1.00  35.84  ? 137  PHE B N   1 
ATOM   3321 C CA  . PHE B 1 137 ? 15.370  -0.955  -1.903  1.00  34.52  ? 137  PHE B CA  1 
ATOM   3322 C C   . PHE B 1 137 ? 14.117  -0.448  -2.604  1.00  34.01  ? 137  PHE B C   1 
ATOM   3323 O O   . PHE B 1 137 ? 13.365  0.349   -2.054  1.00  33.66  ? 137  PHE B O   1 
ATOM   3324 C CB  . PHE B 1 137 ? 16.269  0.229   -1.537  1.00  34.72  ? 137  PHE B CB  1 
ATOM   3325 C CG  . PHE B 1 137 ? 17.367  -0.098  -0.545  1.00  34.38  ? 137  PHE B CG  1 
ATOM   3326 C CD1 . PHE B 1 137 ? 18.406  0.794   -0.328  1.00  34.88  ? 137  PHE B CD1 1 
ATOM   3327 C CD2 . PHE B 1 137 ? 17.371  -1.281  0.165   1.00  34.11  ? 137  PHE B CD2 1 
ATOM   3328 C CE1 . PHE B 1 137 ? 19.416  0.511   0.588   1.00  34.28  ? 137  PHE B CE1 1 
ATOM   3329 C CE2 . PHE B 1 137 ? 18.391  -1.566  1.072   1.00  34.10  ? 137  PHE B CE2 1 
ATOM   3330 C CZ  . PHE B 1 137 ? 19.407  -0.671  1.285   1.00  32.59  ? 137  PHE B CZ  1 
ATOM   3331 N N   . PHE B 1 138 ? 13.899  -0.921  -3.825  1.00  33.93  ? 138  PHE B N   1 
ATOM   3332 C CA  . PHE B 1 138 ? 12.767  -0.518  -4.649  1.00  32.90  ? 138  PHE B CA  1 
ATOM   3333 C C   . PHE B 1 138 ? 11.912  -1.736  -4.894  1.00  32.91  ? 138  PHE B C   1 
ATOM   3334 O O   . PHE B 1 138 ? 12.382  -2.868  -4.704  1.00  32.59  ? 138  PHE B O   1 
ATOM   3335 C CB  . PHE B 1 138 ? 13.265  0.006   -5.998  1.00  32.57  ? 138  PHE B CB  1 
ATOM   3336 C CG  . PHE B 1 138 ? 13.832  1.388   -5.953  1.00  30.93  ? 138  PHE B CG  1 
ATOM   3337 C CD1 . PHE B 1 138 ? 15.205  1.585   -5.931  1.00  30.96  ? 138  PHE B CD1 1 
ATOM   3338 C CD2 . PHE B 1 138 ? 12.996  2.494   -5.981  1.00  30.37  ? 138  PHE B CD2 1 
ATOM   3339 C CE1 . PHE B 1 138 ? 15.744  2.863   -5.922  1.00  30.69  ? 138  PHE B CE1 1 
ATOM   3340 C CE2 . PHE B 1 138 ? 13.522  3.775   -5.970  1.00  31.46  ? 138  PHE B CE2 1 
ATOM   3341 C CZ  . PHE B 1 138 ? 14.905  3.962   -5.948  1.00  30.40  ? 138  PHE B CZ  1 
ATOM   3342 N N   . ASP B 1 139 ? 10.666  -1.498  -5.314  0.90  33.22  ? 139  ASP B N   1 
ATOM   3343 C CA  . ASP B 1 139 ? 9.783   -2.549  -5.825  0.90  33.80  ? 139  ASP B CA  1 
ATOM   3344 C C   . ASP B 1 139 ? 9.554   -2.389  -7.327  0.90  34.07  ? 139  ASP B C   1 
ATOM   3345 O O   . ASP B 1 139 ? 9.249   -3.355  -8.032  0.90  34.60  ? 139  ASP B O   1 
ATOM   3346 C CB  . ASP B 1 139 ? 8.453   -2.555  -5.074  0.90  33.82  ? 139  ASP B CB  1 
ATOM   3347 C CG  . ASP B 1 139 ? 8.500   -3.401  -3.820  0.90  34.75  ? 139  ASP B CG  1 
ATOM   3348 O OD1 . ASP B 1 139 ? 9.207   -4.435  -3.828  0.90  35.43  ? 139  ASP B OD1 1 
ATOM   3349 O OD2 . ASP B 1 139 ? 7.832   -3.050  -2.820  0.90  36.82  ? 139  ASP B OD2 1 
ATOM   3350 N N   . ILE B 1 140 ? 9.695   -1.155  -7.802  1.00  34.10  ? 140  ILE B N   1 
ATOM   3351 C CA  . ILE B 1 140 ? 9.684   -0.853  -9.228  1.00  34.08  ? 140  ILE B CA  1 
ATOM   3352 C C   . ILE B 1 140 ? 11.029  -1.302  -9.795  1.00  34.40  ? 140  ILE B C   1 
ATOM   3353 O O   . ILE B 1 140 ? 12.000  -1.402  -9.034  1.00  34.81  ? 140  ILE B O   1 
ATOM   3354 C CB  . ILE B 1 140 ? 9.452   0.669   -9.490  1.00  33.88  ? 140  ILE B CB  1 
ATOM   3355 C CG1 . ILE B 1 140 ? 10.648  1.500   -8.988  1.00  33.92  ? 140  ILE B CG1 1 
ATOM   3356 C CG2 . ILE B 1 140 ? 8.108   1.132   -8.858  1.00  32.67  ? 140  ILE B CG2 1 
ATOM   3357 C CD1 . ILE B 1 140 ? 10.524  3.005   -9.302  1.00  33.18  ? 140  ILE B CD1 1 
ATOM   3358 N N   . PRO B 1 141 ? 11.093  -1.604  -11.113 1.00  34.40  ? 141  PRO B N   1 
ATOM   3359 C CA  . PRO B 1 141 ? 12.352  -2.048  -11.706 1.00  34.21  ? 141  PRO B CA  1 
ATOM   3360 C C   . PRO B 1 141 ? 13.423  -0.967  -11.726 1.00  34.36  ? 141  PRO B C   1 
ATOM   3361 O O   . PRO B 1 141 ? 13.125  0.208   -11.911 1.00  34.05  ? 141  PRO B O   1 
ATOM   3362 C CB  . PRO B 1 141 ? 11.954  -2.413  -13.142 1.00  34.57  ? 141  PRO B CB  1 
ATOM   3363 C CG  . PRO B 1 141 ? 10.682  -1.687  -13.401 1.00  33.27  ? 141  PRO B CG  1 
ATOM   3364 C CD  . PRO B 1 141 ? 9.989   -1.636  -12.096 1.00  34.42  ? 141  PRO B CD  1 
ATOM   3365 N N   . VAL B 1 142 ? 14.669  -1.390  -11.533 1.00  35.02  ? 142  VAL B N   1 
ATOM   3366 C CA  . VAL B 1 142 ? 15.836  -0.506  -11.564 1.00  35.14  ? 142  VAL B CA  1 
ATOM   3367 C C   . VAL B 1 142 ? 16.823  -1.032  -12.601 1.00  35.50  ? 142  VAL B C   1 
ATOM   3368 O O   . VAL B 1 142 ? 17.099  -2.225  -12.632 1.00  35.95  ? 142  VAL B O   1 
ATOM   3369 C CB  . VAL B 1 142 ? 16.553  -0.486  -10.194 1.00  35.02  ? 142  VAL B CB  1 
ATOM   3370 C CG1 . VAL B 1 142 ? 17.919  0.184   -10.308 1.00  35.23  ? 142  VAL B CG1 1 
ATOM   3371 C CG2 . VAL B 1 142 ? 15.694  0.184   -9.121  1.00  34.33  ? 142  VAL B CG2 1 
ATOM   3372 N N   . ASP B 1 143 ? 17.342  -0.155  -13.454 1.00  35.96  ? 143  ASP B N   1 
ATOM   3373 C CA  . ASP B 1 143 ? 18.474  -0.507  -14.307 1.00  36.02  ? 143  ASP B CA  1 
ATOM   3374 C C   . ASP B 1 143 ? 19.756  0.151   -13.797 1.00  36.65  ? 143  ASP B C   1 
ATOM   3375 O O   . ASP B 1 143 ? 19.921  1.373   -13.880 1.00  36.59  ? 143  ASP B O   1 
ATOM   3376 C CB  . ASP B 1 143 ? 18.186  -0.163  -15.769 1.00  35.92  ? 143  ASP B CB  1 
ATOM   3377 C CG  . ASP B 1 143 ? 17.029  -0.987  -16.352 1.00  35.59  ? 143  ASP B CG  1 
ATOM   3378 O OD1 . ASP B 1 143 ? 16.942  -2.199  -16.060 1.00  35.03  ? 143  ASP B OD1 1 
ATOM   3379 O OD2 . ASP B 1 143 ? 16.207  -0.431  -17.118 1.00  33.93  ? 143  ASP B OD2 1 
ATOM   3380 N N   . ASN B 1 144 ? 20.636  -0.673  -13.221 1.00  37.40  ? 144  ASN B N   1 
ATOM   3381 C CA  . ASN B 1 144 ? 21.910  -0.188  -12.709 1.00  38.13  ? 144  ASN B CA  1 
ATOM   3382 C C   . ASN B 1 144 ? 22.988  -0.362  -13.764 1.00  38.16  ? 144  ASN B C   1 
ATOM   3383 O O   . ASN B 1 144 ? 23.449  -1.472  -14.027 1.00  38.23  ? 144  ASN B O   1 
ATOM   3384 C CB  . ASN B 1 144 ? 22.296  -0.879  -11.401 1.00  38.47  ? 144  ASN B CB  1 
ATOM   3385 C CG  . ASN B 1 144 ? 23.628  -0.385  -10.850 1.00  40.57  ? 144  ASN B CG  1 
ATOM   3386 O OD1 . ASN B 1 144 ? 23.900  0.825   -10.802 1.00  41.64  ? 144  ASN B OD1 1 
ATOM   3387 N ND2 . ASN B 1 144 ? 24.475  -1.325  -10.445 1.00  42.72  ? 144  ASN B ND2 1 
ATOM   3388 N N   . LEU B 1 145 ? 23.371  0.750   -14.380 1.00  38.32  ? 145  LEU B N   1 
ATOM   3389 C CA  . LEU B 1 145 ? 24.325  0.730   -15.478 1.00  38.23  ? 145  LEU B CA  1 
ATOM   3390 C C   . LEU B 1 145 ? 25.732  0.670   -14.959 1.00  38.27  ? 145  LEU B C   1 
ATOM   3391 O O   . LEU B 1 145 ? 26.038  1.248   -13.922 1.00  38.93  ? 145  LEU B O   1 
ATOM   3392 C CB  . LEU B 1 145 ? 24.166  1.977   -16.342 1.00  38.08  ? 145  LEU B CB  1 
ATOM   3393 C CG  . LEU B 1 145 ? 22.860  2.086   -17.115 1.00  37.44  ? 145  LEU B CG  1 
ATOM   3394 C CD1 . LEU B 1 145 ? 22.691  3.516   -17.598 1.00  37.82  ? 145  LEU B CD1 1 
ATOM   3395 C CD2 . LEU B 1 145 ? 22.857  1.078   -18.275 1.00  36.03  ? 145  LEU B CD2 1 
ATOM   3396 N N   . TYR B 1 146 ? 26.592  -0.020  -15.693 0.71  38.34  ? 146  TYR B N   1 
ATOM   3397 C CA  . TYR B 1 146 ? 27.989  -0.099  -15.334 0.71  38.38  ? 146  TYR B CA  1 
ATOM   3398 C C   . TYR B 1 146 ? 28.809  0.884   -16.151 0.71  38.52  ? 146  TYR B C   1 
ATOM   3399 O O   . TYR B 1 146 ? 28.649  0.991   -17.367 0.71  38.44  ? 146  TYR B O   1 
ATOM   3400 C CB  . TYR B 1 146 ? 28.502  -1.525  -15.498 0.71  38.48  ? 146  TYR B CB  1 
ATOM   3401 C CG  . TYR B 1 146 ? 27.968  -2.465  -14.446 0.71  39.18  ? 146  TYR B CG  1 
ATOM   3402 C CD1 . TYR B 1 146 ? 26.785  -3.176  -14.657 0.71  39.96  ? 146  TYR B CD1 1 
ATOM   3403 C CD2 . TYR B 1 146 ? 28.640  -2.642  -13.232 0.71  40.37  ? 146  TYR B CD2 1 
ATOM   3404 C CE1 . TYR B 1 146 ? 26.279  -4.039  -13.690 0.71  40.34  ? 146  TYR B CE1 1 
ATOM   3405 C CE2 . TYR B 1 146 ? 28.146  -3.507  -12.258 0.71  41.34  ? 146  TYR B CE2 1 
ATOM   3406 C CZ  . TYR B 1 146 ? 26.966  -4.204  -12.502 0.71  40.75  ? 146  TYR B CZ  1 
ATOM   3407 O OH  . TYR B 1 146 ? 26.476  -5.060  -11.558 0.71  41.22  ? 146  TYR B OH  1 
ATOM   3408 N N   . ALA B 1 147 ? 29.668  1.623   -15.455 1.00  38.77  ? 147  ALA B N   1 
ATOM   3409 C CA  . ALA B 1 147 ? 30.631  2.502   -16.097 1.00  39.09  ? 147  ALA B CA  1 
ATOM   3410 C C   . ALA B 1 147 ? 31.904  1.715   -16.380 1.00  39.04  ? 147  ALA B C   1 
ATOM   3411 O O   . ALA B 1 147 ? 32.777  2.167   -17.122 1.00  39.08  ? 147  ALA B O   1 
ATOM   3412 C CB  . ALA B 1 147 ? 30.922  3.696   -15.210 1.00  39.58  ? 147  ALA B CB  1 
ATOM   3413 N N   . GLU B 1 148 ? 31.980  0.529   -15.780 1.00  39.06  ? 148  GLU B N   1 
ATOM   3414 C CA  . GLU B 1 148 ? 33.054  -0.434  -15.997 1.00  39.31  ? 148  GLU B CA  1 
ATOM   3415 C C   . GLU B 1 148 ? 33.513  -0.566  -17.456 1.00  39.49  ? 148  GLU B C   1 
ATOM   3416 O O   . GLU B 1 148 ? 34.700  -0.404  -17.731 1.00  39.75  ? 148  GLU B O   1 
ATOM   3417 C CB  . GLU B 1 148 ? 32.658  -1.806  -15.431 1.00  39.21  ? 148  GLU B CB  1 
ATOM   3418 C CG  . GLU B 1 148 ? 33.665  -2.923  -15.725 1.00  39.60  ? 148  GLU B CG  1 
ATOM   3419 C CD  . GLU B 1 148 ? 33.614  -4.057  -14.710 1.00  40.16  ? 148  GLU B CD  1 
ATOM   3420 O OE1 . GLU B 1 148 ? 33.088  -3.852  -13.599 1.00  41.71  ? 148  GLU B OE1 1 
ATOM   3421 O OE2 . GLU B 1 148 ? 34.117  -5.157  -15.010 1.00  39.53  ? 148  GLU B OE2 1 
ATOM   3422 N N   . PRO B 1 149 ? 32.589  -0.867  -18.393 1.00  39.71  ? 149  PRO B N   1 
ATOM   3423 C CA  . PRO B 1 149 ? 33.051  -0.988  -19.779 1.00  39.88  ? 149  PRO B CA  1 
ATOM   3424 C C   . PRO B 1 149 ? 33.793  0.267   -20.249 1.00  40.34  ? 149  PRO B C   1 
ATOM   3425 O O   . PRO B 1 149 ? 34.905  0.169   -20.762 1.00  40.43  ? 149  PRO B O   1 
ATOM   3426 C CB  . PRO B 1 149 ? 31.755  -1.187  -20.565 1.00  39.91  ? 149  PRO B CB  1 
ATOM   3427 C CG  . PRO B 1 149 ? 30.812  -1.807  -19.576 1.00  39.82  ? 149  PRO B CG  1 
ATOM   3428 C CD  . PRO B 1 149 ? 31.151  -1.184  -18.261 1.00  39.83  ? 149  PRO B CD  1 
ATOM   3429 N N   . ALA B 1 150 ? 33.195  1.436   -20.030 1.00  40.93  ? 150  ALA B N   1 
ATOM   3430 C CA  . ALA B 1 150 ? 33.776  2.719   -20.419 1.00  41.48  ? 150  ALA B CA  1 
ATOM   3431 C C   . ALA B 1 150 ? 35.132  2.975   -19.749 1.00  42.29  ? 150  ALA B C   1 
ATOM   3432 O O   . ALA B 1 150 ? 36.020  3.625   -20.327 1.00  42.55  ? 150  ALA B O   1 
ATOM   3433 C CB  . ALA B 1 150 ? 32.813  3.839   -20.093 1.00  41.20  ? 150  ALA B CB  1 
ATOM   3434 N N   . VAL B 1 151 ? 35.276  2.465   -18.528 1.00  42.74  ? 151  VAL B N   1 
ATOM   3435 C CA  . VAL B 1 151 ? 36.506  2.575   -17.767 1.00  43.12  ? 151  VAL B CA  1 
ATOM   3436 C C   . VAL B 1 151 ? 37.578  1.693   -18.402 1.00  43.77  ? 151  VAL B C   1 
ATOM   3437 O O   . VAL B 1 151 ? 38.683  2.159   -18.681 1.00  43.94  ? 151  VAL B O   1 
ATOM   3438 C CB  . VAL B 1 151 ? 36.268  2.190   -16.279 1.00  43.09  ? 151  VAL B CB  1 
ATOM   3439 C CG1 . VAL B 1 151 ? 37.594  2.064   -15.506 1.00  42.91  ? 151  VAL B CG1 1 
ATOM   3440 C CG2 . VAL B 1 151 ? 35.367  3.234   -15.612 1.00  43.06  ? 151  VAL B CG2 1 
ATOM   3441 N N   . LEU B 1 152 ? 37.239  0.424   -18.641 1.00  44.43  ? 152  LEU B N   1 
ATOM   3442 C CA  . LEU B 1 152 ? 38.156  -0.536  -19.265 1.00  45.04  ? 152  LEU B CA  1 
ATOM   3443 C C   . LEU B 1 152 ? 38.681  -0.052  -20.623 1.00  45.40  ? 152  LEU B C   1 
ATOM   3444 O O   . LEU B 1 152 ? 39.855  -0.247  -20.947 1.00  45.81  ? 152  LEU B O   1 
ATOM   3445 C CB  . LEU B 1 152 ? 37.476  -1.894  -19.419 1.00  45.09  ? 152  LEU B CB  1 
ATOM   3446 C CG  . LEU B 1 152 ? 37.191  -2.706  -18.150 1.00  45.61  ? 152  LEU B CG  1 
ATOM   3447 C CD1 . LEU B 1 152 ? 36.087  -3.704  -18.422 1.00  46.43  ? 152  LEU B CD1 1 
ATOM   3448 C CD2 . LEU B 1 152 ? 38.435  -3.433  -17.673 1.00  45.06  ? 152  LEU B CD2 1 
ATOM   3449 N N   . LYS B 1 153 ? 37.801  0.581   -21.397 1.00  45.53  ? 153  LYS B N   1 
ATOM   3450 C CA  . LYS B 1 153 ? 38.138  1.155   -22.688 1.00  45.43  ? 153  LYS B CA  1 
ATOM   3451 C C   . LYS B 1 153 ? 39.097  2.328   -22.490 1.00  45.89  ? 153  LYS B C   1 
ATOM   3452 O O   . LYS B 1 153 ? 39.989  2.555   -23.309 1.00  46.31  ? 153  LYS B O   1 
ATOM   3453 C CB  . LYS B 1 153 ? 36.857  1.621   -23.381 1.00  45.53  ? 153  LYS B CB  1 
ATOM   3454 C CG  . LYS B 1 153 ? 37.015  2.191   -24.787 1.00  45.39  ? 153  LYS B CG  1 
ATOM   3455 C CD  . LYS B 1 153 ? 35.645  2.339   -25.446 1.00  45.55  ? 153  LYS B CD  1 
ATOM   3456 C CE  . LYS B 1 153 ? 35.722  3.066   -26.780 1.00  46.43  ? 153  LYS B CE  1 
ATOM   3457 N NZ  . LYS B 1 153 ? 35.993  4.530   -26.612 1.00  45.80  ? 153  LYS B NZ  1 
ATOM   3458 N N   . TRP B 1 154 ? 38.921  3.072   -21.401 1.00  45.95  ? 154  TRP B N   1 
ATOM   3459 C CA  . TRP B 1 154 ? 39.783  4.223   -21.120 1.00  45.70  ? 154  TRP B CA  1 
ATOM   3460 C C   . TRP B 1 154 ? 41.192  3.759   -20.728 1.00  45.68  ? 154  TRP B C   1 
ATOM   3461 O O   . TRP B 1 154 ? 42.188  4.359   -21.136 1.00  45.41  ? 154  TRP B O   1 
ATOM   3462 C CB  . TRP B 1 154 ? 39.174  5.126   -20.033 1.00  45.39  ? 154  TRP B CB  1 
ATOM   3463 C CG  . TRP B 1 154 ? 39.850  6.454   -19.935 1.00  45.44  ? 154  TRP B CG  1 
ATOM   3464 C CD1 . TRP B 1 154 ? 39.448  7.625   -20.516 1.00  44.63  ? 154  TRP B CD1 1 
ATOM   3465 C CD2 . TRP B 1 154 ? 41.066  6.750   -19.233 1.00  46.28  ? 154  TRP B CD2 1 
ATOM   3466 N NE1 . TRP B 1 154 ? 40.331  8.630   -20.212 1.00  44.61  ? 154  TRP B NE1 1 
ATOM   3467 C CE2 . TRP B 1 154 ? 41.336  8.121   -19.429 1.00  45.88  ? 154  TRP B CE2 1 
ATOM   3468 C CE3 . TRP B 1 154 ? 41.953  5.988   -18.451 1.00  47.04  ? 154  TRP B CE3 1 
ATOM   3469 C CZ2 . TRP B 1 154 ? 42.464  8.748   -18.882 1.00  46.66  ? 154  TRP B CZ2 1 
ATOM   3470 C CZ3 . TRP B 1 154 ? 43.072  6.614   -17.903 1.00  46.70  ? 154  TRP B CZ3 1 
ATOM   3471 C CH2 . TRP B 1 154 ? 43.317  7.979   -18.125 1.00  46.89  ? 154  TRP B CH2 1 
ATOM   3472 N N   . ILE B 1 155 ? 41.267  2.686   -19.944 1.00  45.81  ? 155  ILE B N   1 
ATOM   3473 C CA  . ILE B 1 155 ? 42.552  2.160   -19.473 1.00  45.96  ? 155  ILE B CA  1 
ATOM   3474 C C   . ILE B 1 155 ? 43.357  1.562   -20.631 1.00  46.07  ? 155  ILE B C   1 
ATOM   3475 O O   . ILE B 1 155 ? 44.557  1.829   -20.768 1.00  46.20  ? 155  ILE B O   1 
ATOM   3476 C CB  . ILE B 1 155 ? 42.365  1.123   -18.334 1.00  46.10  ? 155  ILE B CB  1 
ATOM   3477 C CG1 . ILE B 1 155 ? 41.774  1.796   -17.088 1.00  46.14  ? 155  ILE B CG1 1 
ATOM   3478 C CG2 . ILE B 1 155 ? 43.680  0.433   -17.990 1.00  46.01  ? 155  ILE B CG2 1 
ATOM   3479 C CD1 . ILE B 1 155 ? 41.526  0.847   -15.925 1.00  45.98  ? 155  ILE B CD1 1 
ATOM   3480 N N   . ARG B 1 156 ? 42.679  0.779   -21.469 1.00  46.05  ? 156  ARG B N   1 
ATOM   3481 C CA  . ARG B 1 156 ? 43.302  0.129   -22.614 1.00  46.03  ? 156  ARG B CA  1 
ATOM   3482 C C   . ARG B 1 156 ? 43.993  1.089   -23.589 1.00  46.15  ? 156  ARG B C   1 
ATOM   3483 O O   . ARG B 1 156 ? 45.002  0.722   -24.203 1.00  46.19  ? 156  ARG B O   1 
ATOM   3484 C CB  . ARG B 1 156 ? 42.282  -0.749  -23.352 1.00  46.25  ? 156  ARG B CB  1 
ATOM   3485 C CG  . ARG B 1 156 ? 42.053  -2.114  -22.708 1.00  46.56  ? 156  ARG B CG  1 
ATOM   3486 C CD  . ARG B 1 156 ? 41.510  -3.145  -23.716 1.00  47.32  ? 156  ARG B CD  1 
ATOM   3487 N NE  . ARG B 1 156 ? 41.275  -4.431  -23.058 1.00  48.64  ? 156  ARG B NE  1 
ATOM   3488 C CZ  . ARG B 1 156 ? 40.127  -4.786  -22.477 1.00  49.34  ? 156  ARG B CZ  1 
ATOM   3489 N NH1 . ARG B 1 156 ? 39.083  -3.957  -22.486 1.00  48.47  ? 156  ARG B NH1 1 
ATOM   3490 N NH2 . ARG B 1 156 ? 40.015  -5.973  -21.881 1.00  48.70  ? 156  ARG B NH2 1 
ATOM   3491 N N   . GLU B 1 157 ? 43.466  2.308   -23.719 0.83  46.23  ? 157  GLU B N   1 
ATOM   3492 C CA  . GLU B 1 157 ? 43.966  3.261   -24.722 0.83  46.60  ? 157  GLU B CA  1 
ATOM   3493 C C   . GLU B 1 157 ? 44.781  4.430   -24.156 0.83  46.53  ? 157  GLU B C   1 
ATOM   3494 O O   . GLU B 1 157 ? 45.588  5.025   -24.870 0.83  46.57  ? 157  GLU B O   1 
ATOM   3495 C CB  . GLU B 1 157 ? 42.815  3.774   -25.593 0.83  46.78  ? 157  GLU B CB  1 
ATOM   3496 C CG  . GLU B 1 157 ? 41.792  4.636   -24.868 0.83  48.51  ? 157  GLU B CG  1 
ATOM   3497 C CD  . GLU B 1 157 ? 40.443  4.680   -25.573 0.83  50.93  ? 157  GLU B CD  1 
ATOM   3498 O OE1 . GLU B 1 157 ? 39.540  5.391   -25.078 0.83  52.34  ? 157  GLU B OE1 1 
ATOM   3499 O OE2 . GLU B 1 157 ? 40.279  4.002   -26.614 0.83  50.94  ? 157  GLU B OE2 1 
ATOM   3500 N N   . ASN B 1 158 ? 44.569  4.749   -22.880 1.00  46.57  ? 158  ASN B N   1 
ATOM   3501 C CA  . ASN B 1 158 ? 45.253  5.862   -22.225 1.00  46.58  ? 158  ASN B CA  1 
ATOM   3502 C C   . ASN B 1 158 ? 46.413  5.436   -21.335 1.00  46.24  ? 158  ASN B C   1 
ATOM   3503 O O   . ASN B 1 158 ? 47.244  6.261   -20.956 1.00  46.66  ? 158  ASN B O   1 
ATOM   3504 C CB  . ASN B 1 158 ? 44.257  6.705   -21.419 1.00  46.83  ? 158  ASN B CB  1 
ATOM   3505 C CG  . ASN B 1 158 ? 43.286  7.457   -22.305 1.00  47.22  ? 158  ASN B CG  1 
ATOM   3506 O OD1 . ASN B 1 158 ? 43.629  8.482   -22.894 1.00  48.08  ? 158  ASN B OD1 1 
ATOM   3507 N ND2 . ASN B 1 158 ? 42.064  6.952   -22.403 1.00  46.91  ? 158  ASN B ND2 1 
ATOM   3508 N N   . ILE B 1 159 ? 46.460  4.157   -20.994 1.00  45.93  ? 159  ILE B N   1 
ATOM   3509 C CA  . ILE B 1 159 ? 47.561  3.619   -20.199 1.00  45.86  ? 159  ILE B CA  1 
ATOM   3510 C C   . ILE B 1 159 ? 48.243  2.511   -20.991 1.00  45.77  ? 159  ILE B C   1 
ATOM   3511 O O   . ILE B 1 159 ? 47.645  1.468   -21.260 1.00  45.67  ? 159  ILE B O   1 
ATOM   3512 C CB  . ILE B 1 159 ? 47.081  3.111   -18.825 1.00  45.74  ? 159  ILE B CB  1 
ATOM   3513 C CG1 . ILE B 1 159 ? 46.476  4.271   -18.033 1.00  45.86  ? 159  ILE B CG1 1 
ATOM   3514 C CG2 . ILE B 1 159 ? 48.236  2.506   -18.051 1.00  45.87  ? 159  ILE B CG2 1 
ATOM   3515 C CD1 . ILE B 1 159 ? 45.242  3.902   -17.243 1.00  46.32  ? 159  ILE B CD1 1 
ATOM   3516 N N   . SER B 1 160 ? 49.488  2.773   -21.383 1.00  45.74  ? 160  SER B N   1 
ATOM   3517 C CA  . SER B 1 160 ? 50.291  1.849   -22.188 1.00  45.53  ? 160  SER B CA  1 
ATOM   3518 C C   . SER B 1 160 ? 50.656  0.577   -21.425 1.00  45.30  ? 160  SER B C   1 
ATOM   3519 O O   . SER B 1 160 ? 50.645  -0.518  -21.998 1.00  44.97  ? 160  SER B O   1 
ATOM   3520 C CB  . SER B 1 160 ? 51.569  2.552   -22.668 1.00  45.58  ? 160  SER B CB  1 
ATOM   3521 O OG  . SER B 1 160 ? 51.265  3.637   -23.533 1.00  46.19  ? 160  SER B OG  1 
ATOM   3522 N N   . GLU B 1 161 ? 50.955  0.734   -20.131 1.00  45.29  ? 161  GLU B N   1 
ATOM   3523 C CA  . GLU B 1 161 ? 51.353  -0.381  -19.276 1.00  45.32  ? 161  GLU B CA  1 
ATOM   3524 C C   . GLU B 1 161 ? 50.173  -1.194  -18.713 1.00  45.07  ? 161  GLU B C   1 
ATOM   3525 O O   . GLU B 1 161 ? 50.354  -1.955  -17.755 1.00  45.42  ? 161  GLU B O   1 
ATOM   3526 C CB  . GLU B 1 161 ? 52.247  0.109   -18.128 1.00  45.47  ? 161  GLU B CB  1 
ATOM   3527 C CG  . GLU B 1 161 ? 53.540  0.823   -18.552 1.00  46.91  ? 161  GLU B CG  1 
ATOM   3528 C CD  . GLU B 1 161 ? 53.411  2.349   -18.560 1.00  50.23  ? 161  GLU B CD  1 
ATOM   3529 O OE1 . GLU B 1 161 ? 52.296  2.876   -18.838 1.00  50.74  ? 161  GLU B OE1 1 
ATOM   3530 O OE2 . GLU B 1 161 ? 54.435  3.026   -18.285 1.00  50.39  ? 161  GLU B OE2 1 
ATOM   3531 N N   . TRP B 1 162 ? 48.988  -1.066  -19.319 1.00  44.39  ? 162  TRP B N   1 
ATOM   3532 C CA  . TRP B 1 162 ? 47.771  -1.678  -18.764 1.00  44.08  ? 162  TRP B CA  1 
ATOM   3533 C C   . TRP B 1 162 ? 47.807  -3.198  -18.659 1.00  44.16  ? 162  TRP B C   1 
ATOM   3534 O O   . TRP B 1 162 ? 47.159  -3.783  -17.791 1.00  43.82  ? 162  TRP B O   1 
ATOM   3535 C CB  . TRP B 1 162 ? 46.491  -1.203  -19.479 1.00  43.74  ? 162  TRP B CB  1 
ATOM   3536 C CG  . TRP B 1 162 ? 46.245  -1.732  -20.860 1.00  42.69  ? 162  TRP B CG  1 
ATOM   3537 C CD1 . TRP B 1 162 ? 46.477  -1.075  -22.038 1.00  41.86  ? 162  TRP B CD1 1 
ATOM   3538 C CD2 . TRP B 1 162 ? 45.679  -3.003  -21.218 1.00  42.64  ? 162  TRP B CD2 1 
ATOM   3539 N NE1 . TRP B 1 162 ? 46.110  -1.856  -23.102 1.00  41.85  ? 162  TRP B NE1 1 
ATOM   3540 C CE2 . TRP B 1 162 ? 45.621  -3.048  -22.632 1.00  42.74  ? 162  TRP B CE2 1 
ATOM   3541 C CE3 . TRP B 1 162 ? 45.232  -4.116  -20.487 1.00  42.55  ? 162  TRP B CE3 1 
ATOM   3542 C CZ2 . TRP B 1 162 ? 45.126  -4.161  -23.329 1.00  42.83  ? 162  TRP B CZ2 1 
ATOM   3543 C CZ3 . TRP B 1 162 ? 44.740  -5.223  -21.180 1.00  41.49  ? 162  TRP B CZ3 1 
ATOM   3544 C CH2 . TRP B 1 162 ? 44.690  -5.235  -22.586 1.00  42.44  ? 162  TRP B CH2 1 
ATOM   3545 N N   . ARG B 1 163 ? 48.564  -3.830  -19.549 1.00  44.46  ? 163  ARG B N   1 
ATOM   3546 C CA  . ARG B 1 163 ? 48.713  -5.284  -19.538 1.00  44.37  ? 163  ARG B CA  1 
ATOM   3547 C C   . ARG B 1 163 ? 49.445  -5.787  -18.291 1.00  44.22  ? 163  ARG B C   1 
ATOM   3548 O O   . ARG B 1 163 ? 49.269  -6.934  -17.898 1.00  43.98  ? 163  ARG B O   1 
ATOM   3549 C CB  . ARG B 1 163 ? 49.397  -5.757  -20.825 1.00  44.62  ? 163  ARG B CB  1 
ATOM   3550 C CG  . ARG B 1 163 ? 48.481  -5.678  -22.047 1.00  44.73  ? 163  ARG B CG  1 
ATOM   3551 C CD  . ARG B 1 163 ? 49.097  -6.347  -23.270 1.00  45.15  ? 163  ARG B CD  1 
ATOM   3552 N NE  . ARG B 1 163 ? 48.203  -6.285  -24.426 1.00  45.58  ? 163  ARG B NE  1 
ATOM   3553 C CZ  . ARG B 1 163 ? 48.084  -5.241  -25.249 1.00  46.10  ? 163  ARG B CZ  1 
ATOM   3554 N NH1 . ARG B 1 163 ? 48.814  -4.139  -25.068 1.00  45.60  ? 163  ARG B NH1 1 
ATOM   3555 N NH2 . ARG B 1 163 ? 47.228  -5.302  -26.268 1.00  45.89  ? 163  ARG B NH2 1 
ATOM   3556 N N   . ASN B 1 164 ? 50.236  -4.911  -17.665 1.00  44.46  ? 164  ASN B N   1 
ATOM   3557 C CA  . ASN B 1 164 ? 50.983  -5.243  -16.444 1.00  44.67  ? 164  ASN B CA  1 
ATOM   3558 C C   . ASN B 1 164 ? 50.681  -4.380  -15.227 1.00  44.77  ? 164  ASN B C   1 
ATOM   3559 O O   . ASN B 1 164 ? 51.481  -4.336  -14.295 1.00  44.74  ? 164  ASN B O   1 
ATOM   3560 C CB  . ASN B 1 164 ? 52.488  -5.211  -16.704 1.00  44.76  ? 164  ASN B CB  1 
ATOM   3561 C CG  . ASN B 1 164 ? 52.979  -6.448  -17.411 1.00  44.91  ? 164  ASN B CG  1 
ATOM   3562 O OD1 . ASN B 1 164 ? 53.614  -7.317  -16.801 1.00  45.16  ? 164  ASN B OD1 1 
ATOM   3563 N ND2 . ASN B 1 164 ? 52.678  -6.547  -18.705 1.00  43.56  ? 164  ASN B ND2 1 
ATOM   3564 N N   . CYS B 1 165 ? 49.528  -3.715  -15.219 1.00  44.92  ? 165  CYS B N   1 
ATOM   3565 C CA  . CYS B 1 165 ? 49.194  -2.814  -14.118 1.00  44.77  ? 165  CYS B CA  1 
ATOM   3566 C C   . CYS B 1 165 ? 48.569  -3.547  -12.934 1.00  45.08  ? 165  CYS B C   1 
ATOM   3567 O O   . CYS B 1 165 ? 48.469  -4.781  -12.933 1.00  45.39  ? 165  CYS B O   1 
ATOM   3568 C CB  . CYS B 1 165 ? 48.279  -1.687  -14.600 1.00  44.80  ? 165  CYS B CB  1 
ATOM   3569 S SG  . CYS B 1 165 ? 46.554  -2.149  -14.827 1.00  43.98  ? 165  CYS B SG  1 
ATOM   3570 N N   . THR B 1 166 ? 48.169  -2.776  -11.922 1.00  45.13  ? 166  THR B N   1 
ATOM   3571 C CA  . THR B 1 166 ? 47.494  -3.304  -10.743 1.00  44.72  ? 166  THR B CA  1 
ATOM   3572 C C   . THR B 1 166 ? 46.294  -2.423  -10.407 1.00  44.64  ? 166  THR B C   1 
ATOM   3573 O O   . THR B 1 166 ? 46.434  -1.212  -10.223 1.00  44.27  ? 166  THR B O   1 
ATOM   3574 C CB  . THR B 1 166 ? 48.450  -3.369  -9.540  1.00  44.81  ? 166  THR B CB  1 
ATOM   3575 O OG1 . THR B 1 166 ? 49.572  -4.184  -9.876  1.00  44.59  ? 166  THR B OG1 1 
ATOM   3576 C CG2 . THR B 1 166 ? 47.752  -3.953  -8.303  1.00  45.08  ? 166  THR B CG2 1 
ATOM   3577 N N   . ILE B 1 167 ? 45.120  -3.050  -10.338 1.00  44.70  ? 167  ILE B N   1 
ATOM   3578 C CA  . ILE B 1 167 ? 43.862  -2.375  -10.010 1.00  44.51  ? 167  ILE B CA  1 
ATOM   3579 C C   . ILE B 1 167 ? 43.687  -2.355  -8.495  1.00  44.71  ? 167  ILE B C   1 
ATOM   3580 O O   . ILE B 1 167 ? 43.702  -3.400  -7.839  1.00  44.76  ? 167  ILE B O   1 
ATOM   3581 C CB  . ILE B 1 167 ? 42.658  -3.056  -10.721 1.00  44.42  ? 167  ILE B CB  1 
ATOM   3582 C CG1 . ILE B 1 167 ? 42.838  -3.034  -12.251 1.00  43.47  ? 167  ILE B CG1 1 
ATOM   3583 C CG2 . ILE B 1 167 ? 41.323  -2.423  -10.318 1.00  44.96  ? 167  ILE B CG2 1 
ATOM   3584 C CD1 . ILE B 1 167 ? 43.217  -1.682  -12.855 1.00  40.45  ? 167  ILE B CD1 1 
ATOM   3585 N N   . VAL B 1 168 ? 43.546  -1.154  -7.941  1.00  44.81  ? 168  VAL B N   1 
ATOM   3586 C CA  . VAL B 1 168 ? 43.605  -0.973  -6.493  1.00  44.91  ? 168  VAL B CA  1 
ATOM   3587 C C   . VAL B 1 168 ? 42.272  -0.479  -5.948  1.00  45.27  ? 168  VAL B C   1 
ATOM   3588 O O   . VAL B 1 168 ? 41.646  0.432   -6.508  1.00  45.41  ? 168  VAL B O   1 
ATOM   3589 C CB  . VAL B 1 168 ? 44.746  0.012   -6.079  1.00  44.75  ? 168  VAL B CB  1 
ATOM   3590 C CG1 . VAL B 1 168 ? 44.921  0.048   -4.558  1.00  45.10  ? 168  VAL B CG1 1 
ATOM   3591 C CG2 . VAL B 1 168 ? 46.053  -0.368  -6.734  1.00  44.38  ? 168  VAL B CG2 1 
ATOM   3592 N N   . SER B 1 169 ? 41.838  -1.095  -4.858  1.00  45.67  ? 169  SER B N   1 
ATOM   3593 C CA  . SER B 1 169 ? 40.677  -0.623  -4.130  1.00  46.17  ? 169  SER B CA  1 
ATOM   3594 C C   . SER B 1 169 ? 41.191  0.257   -3.005  1.00  46.84  ? 169  SER B C   1 
ATOM   3595 O O   . SER B 1 169 ? 42.083  -0.160  -2.260  1.00  46.74  ? 169  SER B O   1 
ATOM   3596 C CB  . SER B 1 169 ? 39.874  -1.799  -3.570  1.00  46.04  ? 169  SER B CB  1 
ATOM   3597 O OG  . SER B 1 169 ? 38.770  -1.345  -2.806  1.00  45.55  ? 169  SER B OG  1 
ATOM   3598 N N   . PRO B 1 170 ? 40.650  1.483   -2.886  1.00  47.53  ? 170  PRO B N   1 
ATOM   3599 C CA  . PRO B 1 170 ? 41.092  2.399   -1.842  1.00  47.94  ? 170  PRO B CA  1 
ATOM   3600 C C   . PRO B 1 170 ? 40.557  1.994   -0.468  1.00  48.71  ? 170  PRO B C   1 
ATOM   3601 O O   . PRO B 1 170 ? 41.165  2.327   0.550   1.00  48.89  ? 170  PRO B O   1 
ATOM   3602 C CB  . PRO B 1 170 ? 40.522  3.760   -2.280  1.00  48.05  ? 170  PRO B CB  1 
ATOM   3603 C CG  . PRO B 1 170 ? 39.958  3.557   -3.675  1.00  47.91  ? 170  PRO B CG  1 
ATOM   3604 C CD  . PRO B 1 170 ? 39.619  2.094   -3.745  1.00  47.94  ? 170  PRO B CD  1 
ATOM   3605 N N   . ASP B 1 171 ? 39.429  1.285   -0.442  1.00  49.55  ? 171  ASP B N   1 
ATOM   3606 C CA  . ASP B 1 171 ? 38.886  0.708   0.794   1.00  50.03  ? 171  ASP B CA  1 
ATOM   3607 C C   . ASP B 1 171 ? 38.671  -0.806  0.666   1.00  50.28  ? 171  ASP B C   1 
ATOM   3608 O O   . ASP B 1 171 ? 39.098  -1.417  -0.322  1.00  50.32  ? 171  ASP B O   1 
ATOM   3609 C CB  . ASP B 1 171 ? 37.591  1.429   1.211   1.00  50.25  ? 171  ASP B CB  1 
ATOM   3610 C CG  . ASP B 1 171 ? 36.515  1.422   0.122   1.00  51.27  ? 171  ASP B CG  1 
ATOM   3611 O OD1 . ASP B 1 171 ? 36.552  0.571   -0.797  1.00  51.49  ? 171  ASP B OD1 1 
ATOM   3612 O OD2 . ASP B 1 171 ? 35.603  2.278   0.198   1.00  52.96  ? 171  ASP B OD2 1 
ATOM   3613 N N   . ALA B 1 172 ? 38.016  -1.404  1.662   1.00  50.68  ? 172  ALA B N   1 
ATOM   3614 C CA  . ALA B 1 172 ? 37.735  -2.842  1.671   1.00  50.80  ? 172  ALA B CA  1 
ATOM   3615 C C   . ALA B 1 172 ? 36.348  -3.177  1.104   1.00  51.19  ? 172  ALA B C   1 
ATOM   3616 O O   . ALA B 1 172 ? 36.039  -4.343  0.854   1.00  51.50  ? 172  ALA B O   1 
ATOM   3617 C CB  . ALA B 1 172 ? 37.891  -3.400  3.077   1.00  50.97  ? 172  ALA B CB  1 
ATOM   3618 N N   . GLY B 1 173 ? 35.519  -2.155  0.895   1.00  51.44  ? 173  GLY B N   1 
ATOM   3619 C CA  . GLY B 1 173 ? 34.184  -2.342  0.318   1.00  51.37  ? 173  GLY B CA  1 
ATOM   3620 C C   . GLY B 1 173 ? 34.168  -2.285  -1.202  1.00  51.69  ? 173  GLY B C   1 
ATOM   3621 O O   . GLY B 1 173 ? 33.099  -2.381  -1.822  1.00  51.71  ? 173  GLY B O   1 
ATOM   3622 N N   . GLY B 1 174 ? 35.354  -2.133  -1.802  1.00  51.70  ? 174  GLY B N   1 
ATOM   3623 C CA  . GLY B 1 174 ? 35.507  -2.015  -3.260  1.00  51.38  ? 174  GLY B CA  1 
ATOM   3624 C C   . GLY B 1 174 ? 36.270  -3.178  -3.878  1.00  51.37  ? 174  GLY B C   1 
ATOM   3625 O O   . GLY B 1 174 ? 36.707  -3.108  -5.033  1.00  51.21  ? 174  GLY B O   1 
ATOM   3626 N N   . ALA B 1 175 ? 36.425  -4.250  -3.105  1.00  51.25  ? 175  ALA B N   1 
ATOM   3627 C CA  . ALA B 1 175 ? 37.099  -5.457  -3.566  1.00  51.31  ? 175  ALA B CA  1 
ATOM   3628 C C   . ALA B 1 175 ? 36.332  -6.175  -4.674  1.00  51.52  ? 175  ALA B C   1 
ATOM   3629 O O   . ALA B 1 175 ? 36.937  -6.636  -5.641  1.00  51.92  ? 175  ALA B O   1 
ATOM   3630 C CB  . ALA B 1 175 ? 37.351  -6.402  -2.397  1.00  51.50  ? 175  ALA B CB  1 
ATOM   3631 N N   . LYS B 1 176 ? 35.009  -6.279  -4.537  0.010 51.59  ? 176  LYS B N   1 
ATOM   3632 C CA  . LYS B 1 176 ? 34.176  -6.931  -5.555  0.010 51.63  ? 176  LYS B CA  1 
ATOM   3633 C C   . LYS B 1 176 ? 34.137  -6.143  -6.862  0.010 51.70  ? 176  LYS B C   1 
ATOM   3634 O O   . LYS B 1 176 ? 33.682  -6.643  -7.891  0.010 51.69  ? 176  LYS B O   1 
ATOM   3635 C CB  . LYS B 1 176 ? 32.755  -7.163  -5.037  0.010 51.61  ? 176  LYS B CB  1 
ATOM   3636 C CG  . LYS B 1 176 ? 32.473  -8.597  -4.617  0.010 51.59  ? 176  LYS B CG  1 
ATOM   3637 C CD  . LYS B 1 176 ? 31.009  -8.785  -4.254  0.010 51.55  ? 176  LYS B CD  1 
ATOM   3638 C CE  . LYS B 1 176 ? 30.583  -10.240 -4.393  0.010 51.52  ? 176  LYS B CE  1 
ATOM   3639 N NZ  . LYS B 1 176 ? 31.438  -11.161 -3.596  0.010 51.51  ? 176  LYS B NZ  1 
ATOM   3640 N N   . ARG B 1 177 ? 34.622  -4.908  -6.808  0.99  51.78  ? 177  ARG B N   1 
ATOM   3641 C CA  . ARG B 1 177 ? 34.660  -4.035  -7.972  0.99  51.98  ? 177  ARG B CA  1 
ATOM   3642 C C   . ARG B 1 177 ? 36.030  -4.065  -8.653  0.99  51.68  ? 177  ARG B C   1 
ATOM   3643 O O   . ARG B 1 177 ? 36.111  -4.088  -9.882  0.99  51.52  ? 177  ARG B O   1 
ATOM   3644 C CB  . ARG B 1 177 ? 34.294  -2.593  -7.586  0.99  52.11  ? 177  ARG B CB  1 
ATOM   3645 C CG  . ARG B 1 177 ? 33.873  -1.720  -8.787  0.99  53.71  ? 177  ARG B CG  1 
ATOM   3646 C CD  . ARG B 1 177 ? 33.647  -0.244  -8.416  0.99  55.75  ? 177  ARG B CD  1 
ATOM   3647 N NE  . ARG B 1 177 ? 32.631  -0.050  -7.375  0.99  57.46  ? 177  ARG B NE  1 
ATOM   3648 C CZ  . ARG B 1 177 ? 31.315  -0.044  -7.594  0.99  58.42  ? 177  ARG B CZ  1 
ATOM   3649 N NH1 . ARG B 1 177 ? 30.826  -0.241  -8.830  0.99  58.31  ? 177  ARG B NH1 1 
ATOM   3650 N NH2 . ARG B 1 177 ? 30.485  0.158   -6.569  0.99  57.78  ? 177  ARG B NH2 1 
ATOM   3651 N N   . VAL B 1 178 ? 37.103  -4.057  -7.861  1.00  51.48  ? 178  VAL B N   1 
ATOM   3652 C CA  . VAL B 1 178 ? 38.454  -4.057  -8.434  1.00  51.37  ? 178  VAL B CA  1 
ATOM   3653 C C   . VAL B 1 178 ? 38.863  -5.412  -9.005  1.00  51.20  ? 178  VAL B C   1 
ATOM   3654 O O   . VAL B 1 178 ? 39.531  -5.465  -10.035 1.00  50.92  ? 178  VAL B O   1 
ATOM   3655 C CB  . VAL B 1 178 ? 39.559  -3.489  -7.480  1.00  51.29  ? 178  VAL B CB  1 
ATOM   3656 C CG1 . VAL B 1 178 ? 39.262  -2.054  -7.125  1.00  51.50  ? 178  VAL B CG1 1 
ATOM   3657 C CG2 . VAL B 1 178 ? 39.733  -4.328  -6.227  1.00  51.90  ? 178  VAL B CG2 1 
ATOM   3658 N N   . THR B 1 179 ? 38.454  -6.492  -8.339  1.00  51.13  ? 179  THR B N   1 
ATOM   3659 C CA  . THR B 1 179 ? 38.752  -7.850  -8.799  1.00  51.39  ? 179  THR B CA  1 
ATOM   3660 C C   . THR B 1 179 ? 38.152  -8.155  -10.177 1.00  51.42  ? 179  THR B C   1 
ATOM   3661 O O   . THR B 1 179 ? 38.846  -8.669  -11.056 1.00  51.34  ? 179  THR B O   1 
ATOM   3662 C CB  . THR B 1 179 ? 38.296  -8.920  -7.790  1.00  51.44  ? 179  THR B CB  1 
ATOM   3663 O OG1 . THR B 1 179 ? 36.922  -8.704  -7.440  1.00  52.37  ? 179  THR B OG1 1 
ATOM   3664 C CG2 . THR B 1 179 ? 39.156  -8.883  -6.527  1.00  51.94  ? 179  THR B CG2 1 
ATOM   3665 N N   . SER B 1 180 ? 36.876  -7.821  -10.365 1.00  51.60  ? 180  SER B N   1 
ATOM   3666 C CA  . SER B 1 180 ? 36.198  -8.047  -11.645 1.00  51.95  ? 180  SER B CA  1 
ATOM   3667 C C   . SER B 1 180 ? 36.824  -7.255  -12.783 1.00  51.78  ? 180  SER B C   1 
ATOM   3668 O O   . SER B 1 180 ? 36.866  -7.729  -13.917 1.00  52.38  ? 180  SER B O   1 
ATOM   3669 C CB  . SER B 1 180 ? 34.704  -7.732  -11.551 1.00  52.08  ? 180  SER B CB  1 
ATOM   3670 O OG  . SER B 1 180 ? 34.441  -6.343  -11.846 1.00  53.41  ? 180  SER B OG  1 
ATOM   3671 N N   . ILE B 1 181 ? 37.307  -6.052  -12.481 1.00  51.56  ? 181  ILE B N   1 
ATOM   3672 C CA  . ILE B 1 181 ? 37.980  -5.227  -13.487 1.00  51.21  ? 181  ILE B CA  1 
ATOM   3673 C C   . ILE B 1 181 ? 39.351  -5.801  -13.827 1.00  51.28  ? 181  ILE B C   1 
ATOM   3674 O O   . ILE B 1 181 ? 39.716  -5.878  -14.998 1.00  51.59  ? 181  ILE B O   1 
ATOM   3675 C CB  . ILE B 1 181 ? 38.098  -3.754  -13.050 1.00  51.20  ? 181  ILE B CB  1 
ATOM   3676 C CG1 . ILE B 1 181 ? 36.708  -3.107  -12.946 1.00  50.51  ? 181  ILE B CG1 1 
ATOM   3677 C CG2 . ILE B 1 181 ? 38.991  -2.972  -14.018 1.00  51.57  ? 181  ILE B CG2 1 
ATOM   3678 C CD1 . ILE B 1 181 ? 36.743  -1.670  -12.464 1.00  49.93  ? 181  ILE B CD1 1 
ATOM   3679 N N   . ALA B 1 182 ? 40.095  -6.220  -12.801 1.00  51.36  ? 182  ALA B N   1 
ATOM   3680 C CA  . ALA B 1 182 ? 41.418  -6.822  -12.979 1.00  51.18  ? 182  ALA B CA  1 
ATOM   3681 C C   . ALA B 1 182 ? 41.345  -8.089  -13.824 1.00  51.31  ? 182  ALA B C   1 
ATOM   3682 O O   . ALA B 1 182 ? 42.254  -8.375  -14.608 1.00  51.17  ? 182  ALA B O   1 
ATOM   3683 C CB  . ALA B 1 182 ? 42.049  -7.127  -11.637 1.00  51.08  ? 182  ALA B CB  1 
ATOM   3684 N N   . ASP B 1 183 ? 40.251  -8.832  -13.663 1.00  51.33  ? 183  ASP B N   1 
ATOM   3685 C CA  . ASP B 1 183 ? 40.059  -10.107 -14.346 1.00  51.19  ? 183  ASP B CA  1 
ATOM   3686 C C   . ASP B 1 183 ? 39.747  -9.929  -15.824 1.00  51.22  ? 183  ASP B C   1 
ATOM   3687 O O   . ASP B 1 183 ? 40.228  -10.695 -16.657 1.00  51.18  ? 183  ASP B O   1 
ATOM   3688 C CB  . ASP B 1 183 ? 38.966  -10.925 -13.662 1.00  51.13  ? 183  ASP B CB  1 
ATOM   3689 C CG  . ASP B 1 183 ? 39.338  -11.338 -12.240 1.00  51.56  ? 183  ASP B CG  1 
ATOM   3690 O OD1 . ASP B 1 183 ? 40.437  -10.973 -11.758 1.00  51.48  ? 183  ASP B OD1 1 
ATOM   3691 O OD2 . ASP B 1 183 ? 38.517  -12.030 -11.599 1.00  51.95  ? 183  ASP B OD2 1 
ATOM   3692 N N   . ARG B 1 184 ? 38.951  -8.915  -16.153 0.97  51.41  ? 184  ARG B N   1 
ATOM   3693 C CA  . ARG B 1 184 ? 38.613  -8.641  -17.549 0.97  51.51  ? 184  ARG B CA  1 
ATOM   3694 C C   . ARG B 1 184 ? 39.812  -8.147  -18.341 0.97  51.39  ? 184  ARG B C   1 
ATOM   3695 O O   . ARG B 1 184 ? 39.925  -8.428  -19.530 0.97  51.77  ? 184  ARG B O   1 
ATOM   3696 C CB  . ARG B 1 184 ? 37.452  -7.662  -17.654 0.97  51.84  ? 184  ARG B CB  1 
ATOM   3697 C CG  . ARG B 1 184 ? 36.098  -8.312  -17.419 0.97  53.06  ? 184  ARG B CG  1 
ATOM   3698 C CD  . ARG B 1 184 ? 34.964  -7.308  -17.624 0.97  54.45  ? 184  ARG B CD  1 
ATOM   3699 N NE  . ARG B 1 184 ? 33.679  -7.814  -17.133 0.97  55.14  ? 184  ARG B NE  1 
ATOM   3700 C CZ  . ARG B 1 184 ? 33.389  -8.028  -15.849 0.97  55.36  ? 184  ARG B CZ  1 
ATOM   3701 N NH1 . ARG B 1 184 ? 34.299  -7.808  -14.903 0.97  56.85  ? 184  ARG B NH1 1 
ATOM   3702 N NH2 . ARG B 1 184 ? 32.189  -8.471  -15.507 0.97  54.78  ? 184  ARG B NH2 1 
ATOM   3703 N N   . LEU B 1 185 ? 40.701  -7.409  -17.681 1.00  51.28  ? 185  LEU B N   1 
ATOM   3704 C CA  . LEU B 1 185 ? 42.001  -7.048  -18.258 1.00  51.10  ? 185  LEU B CA  1 
ATOM   3705 C C   . LEU B 1 185 ? 43.062  -8.137  -18.046 1.00  51.09  ? 185  LEU B C   1 
ATOM   3706 O O   . LEU B 1 185 ? 44.154  -8.058  -18.619 1.00  51.30  ? 185  LEU B O   1 
ATOM   3707 C CB  . LEU B 1 185 ? 42.518  -5.728  -17.672 1.00  51.12  ? 185  LEU B CB  1 
ATOM   3708 C CG  . LEU B 1 185 ? 41.832  -4.389  -17.974 1.00  50.97  ? 185  LEU B CG  1 
ATOM   3709 C CD1 . LEU B 1 185 ? 42.561  -3.251  -17.268 1.00  50.12  ? 185  LEU B CD1 1 
ATOM   3710 C CD2 . LEU B 1 185 ? 41.738  -4.112  -19.472 1.00  50.36  ? 185  LEU B CD2 1 
ATOM   3711 N N   . ASN B 1 186 ? 42.741  -9.129  -17.213 1.00  50.75  ? 186  ASN B N   1 
ATOM   3712 C CA  . ASN B 1 186 ? 43.653  -10.224 -16.868 1.00  50.62  ? 186  ASN B CA  1 
ATOM   3713 C C   . ASN B 1 186 ? 44.950  -9.756  -16.187 1.00  50.48  ? 186  ASN B C   1 
ATOM   3714 O O   . ASN B 1 186 ? 46.053  -10.073 -16.626 1.00  50.53  ? 186  ASN B O   1 
ATOM   3715 C CB  . ASN B 1 186 ? 43.940  -11.105 -18.094 1.00  50.69  ? 186  ASN B CB  1 
ATOM   3716 C CG  . ASN B 1 186 ? 44.541  -12.448 -17.722 1.00  51.28  ? 186  ASN B CG  1 
ATOM   3717 O OD1 . ASN B 1 186 ? 45.474  -12.912 -18.373 1.00  51.22  ? 186  ASN B OD1 1 
ATOM   3718 N ND2 . ASN B 1 186 ? 44.023  -13.072 -16.659 1.00  52.12  ? 186  ASN B ND2 1 
ATOM   3719 N N   . VAL B 1 187 ? 44.796  -9.003  -15.099 1.00  50.37  ? 187  VAL B N   1 
ATOM   3720 C CA  . VAL B 1 187 ? 45.920  -8.375  -14.399 1.00  49.87  ? 187  VAL B CA  1 
ATOM   3721 C C   . VAL B 1 187 ? 45.766  -8.515  -12.883 1.00  49.89  ? 187  VAL B C   1 
ATOM   3722 O O   . VAL B 1 187 ? 44.788  -9.095  -12.404 1.00  50.14  ? 187  VAL B O   1 
ATOM   3723 C CB  . VAL B 1 187 ? 46.097  -6.867  -14.794 1.00  49.90  ? 187  VAL B CB  1 
ATOM   3724 C CG1 . VAL B 1 187 ? 46.249  -6.711  -16.300 1.00  49.48  ? 187  VAL B CG1 1 
ATOM   3725 C CG2 . VAL B 1 187 ? 44.939  -6.009  -14.293 1.00  49.29  ? 187  VAL B CG2 1 
ATOM   3726 N N   . ASP B 1 188 ? 46.727  -7.979  -12.132 1.00  49.65  ? 188  ASP B N   1 
ATOM   3727 C CA  . ASP B 1 188 ? 46.715  -8.070  -10.669 1.00  49.63  ? 188  ASP B CA  1 
ATOM   3728 C C   . ASP B 1 188 ? 45.784  -7.053  -10.010 1.00  49.41  ? 188  ASP B C   1 
ATOM   3729 O O   . ASP B 1 188 ? 45.465  -6.018  -10.604 1.00  49.58  ? 188  ASP B O   1 
ATOM   3730 C CB  . ASP B 1 188 ? 48.132  -7.905  -10.116 1.00  49.52  ? 188  ASP B CB  1 
ATOM   3731 C CG  . ASP B 1 188 ? 49.075  -8.973  -10.612 1.00  50.30  ? 188  ASP B CG  1 
ATOM   3732 O OD1 . ASP B 1 188 ? 48.605  -9.951  -11.240 1.00  50.06  ? 188  ASP B OD1 1 
ATOM   3733 O OD2 . ASP B 1 188 ? 50.295  -8.831  -10.373 1.00  52.39  ? 188  ASP B OD2 1 
ATOM   3734 N N   . PHE B 1 189 ? 45.354  -7.358  -8.787  1.00  49.14  ? 189  PHE B N   1 
ATOM   3735 C CA  . PHE B 1 189 ? 44.575  -6.421  -7.973  1.00  49.26  ? 189  PHE B CA  1 
ATOM   3736 C C   . PHE B 1 189 ? 45.237  -6.183  -6.624  1.00  49.12  ? 189  PHE B C   1 
ATOM   3737 O O   . PHE B 1 189 ? 45.904  -7.072  -6.085  1.00  49.36  ? 189  PHE B O   1 
ATOM   3738 C CB  . PHE B 1 189 ? 43.132  -6.914  -7.764  1.00  49.31  ? 189  PHE B CB  1 
ATOM   3739 C CG  . PHE B 1 189 ? 42.966  -7.874  -6.597  1.00  49.61  ? 189  PHE B CG  1 
ATOM   3740 C CD1 . PHE B 1 189 ? 42.559  -7.413  -5.349  1.00  49.00  ? 189  PHE B CD1 1 
ATOM   3741 C CD2 . PHE B 1 189 ? 43.205  -9.242  -6.757  1.00  49.41  ? 189  PHE B CD2 1 
ATOM   3742 C CE1 . PHE B 1 189 ? 42.405  -8.288  -4.286  1.00  48.63  ? 189  PHE B CE1 1 
ATOM   3743 C CE2 . PHE B 1 189 ? 43.054  -10.128 -5.694  1.00  48.22  ? 189  PHE B CE2 1 
ATOM   3744 C CZ  . PHE B 1 189 ? 42.651  -9.653  -4.461  1.00  48.73  ? 189  PHE B CZ  1 
ATOM   3745 N N   . ALA B 1 190 ? 45.038  -4.987  -6.078  1.00  48.96  ? 190  ALA B N   1 
ATOM   3746 C CA  . ALA B 1 190 ? 45.527  -4.662  -4.738  1.00  48.62  ? 190  ALA B CA  1 
ATOM   3747 C C   . ALA B 1 190 ? 44.395  -4.134  -3.860  1.00  48.54  ? 190  ALA B C   1 
ATOM   3748 O O   . ALA B 1 190 ? 43.283  -3.892  -4.326  1.00  48.43  ? 190  ALA B O   1 
ATOM   3749 C CB  . ALA B 1 190 ? 46.675  -3.669  -4.806  1.00  48.50  ? 190  ALA B CB  1 
ATOM   3750 N N   . LEU B 1 191 ? 44.679  -3.966  -2.578  1.00  48.63  ? 191  LEU B N   1 
ATOM   3751 C CA  . LEU B 1 191 ? 43.652  -3.561  -1.638  1.00  48.73  ? 191  LEU B CA  1 
ATOM   3752 C C   . LEU B 1 191 ? 44.242  -2.777  -0.467  1.00  48.62  ? 191  LEU B C   1 
ATOM   3753 O O   . LEU B 1 191 ? 45.050  -3.297  0.301   1.00  48.50  ? 191  LEU B O   1 
ATOM   3754 C CB  . LEU B 1 191 ? 42.886  -4.797  -1.146  1.00  48.83  ? 191  LEU B CB  1 
ATOM   3755 C CG  . LEU B 1 191 ? 41.550  -4.645  -0.423  1.00  48.66  ? 191  LEU B CG  1 
ATOM   3756 C CD1 . LEU B 1 191 ? 40.744  -5.916  -0.606  1.00  48.86  ? 191  LEU B CD1 1 
ATOM   3757 C CD2 . LEU B 1 191 ? 41.743  -4.330  1.052   1.00  48.69  ? 191  LEU B CD2 1 
ATOM   3758 N N   . ILE B 1 192 ? 43.815  -1.523  -0.348  1.00  48.67  ? 192  ILE B N   1 
ATOM   3759 C CA  . ILE B 1 192 ? 44.207  -0.643  0.747   1.00  48.91  ? 192  ILE B CA  1 
ATOM   3760 C C   . ILE B 1 192 ? 43.145  -0.642  1.842   1.00  48.96  ? 192  ILE B C   1 
ATOM   3761 O O   . ILE B 1 192 ? 41.953  -0.489  1.557   1.00  49.25  ? 192  ILE B O   1 
ATOM   3762 C CB  . ILE B 1 192 ? 44.427  0.796   0.243   1.00  48.83  ? 192  ILE B CB  1 
ATOM   3763 C CG1 . ILE B 1 192 ? 45.798  0.911   -0.429  1.00  48.76  ? 192  ILE B CG1 1 
ATOM   3764 C CG2 . ILE B 1 192 ? 44.306  1.813   1.391   1.00  49.33  ? 192  ILE B CG2 1 
ATOM   3765 C CD1 . ILE B 1 192 ? 45.931  2.071   -1.386  1.00  48.77  ? 192  ILE B CD1 1 
ATOM   3766 N N   . HIS B 1 193 ? 43.573  -0.811  3.088   1.00  48.96  ? 193  HIS B N   1 
ATOM   3767 C CA  . HIS B 1 193 ? 42.657  -0.729  4.224   1.00  49.29  ? 193  HIS B CA  1 
ATOM   3768 C C   . HIS B 1 193 ? 43.167  0.229   5.301   1.00  49.45  ? 193  HIS B C   1 
ATOM   3769 O O   . HIS B 1 193 ? 44.209  -0.016  5.920   1.00  49.00  ? 193  HIS B O   1 
ATOM   3770 C CB  . HIS B 1 193 ? 42.387  -2.123  4.810   1.00  49.33  ? 193  HIS B CB  1 
ATOM   3771 C CG  . HIS B 1 193 ? 41.737  -2.097  6.158   1.00  49.39  ? 193  HIS B CG  1 
ATOM   3772 N ND1 . HIS B 1 193 ? 40.484  -1.562  6.370   1.00  49.44  ? 193  HIS B ND1 1 
ATOM   3773 C CD2 . HIS B 1 193 ? 42.164  -2.542  7.365   1.00  49.71  ? 193  HIS B CD2 1 
ATOM   3774 C CE1 . HIS B 1 193 ? 40.168  -1.672  7.648   1.00  49.06  ? 193  HIS B CE1 1 
ATOM   3775 N NE2 . HIS B 1 193 ? 41.170  -2.263  8.274   1.00  49.74  ? 193  HIS B NE2 1 
ATOM   3776 N N   . LYS B 1 194 ? 42.428  1.318   5.509   0.88  49.79  ? 194  LYS B N   1 
ATOM   3777 C CA  . LYS B 1 194 ? 42.758  2.294   6.547   0.88  50.32  ? 194  LYS B CA  1 
ATOM   3778 C C   . LYS B 1 194 ? 42.194  1.806   7.866   0.88  50.59  ? 194  LYS B C   1 
ATOM   3779 O O   . LYS B 1 194 ? 40.979  1.712   8.027   0.88  50.67  ? 194  LYS B O   1 
ATOM   3780 C CB  . LYS B 1 194 ? 42.194  3.682   6.203   0.88  50.34  ? 194  LYS B CB  1 
ATOM   3781 C CG  . LYS B 1 194 ? 42.765  4.835   7.031   0.88  50.33  ? 194  LYS B CG  1 
ATOM   3782 C CD  . LYS B 1 194 ? 42.810  6.147   6.227   0.88  51.18  ? 194  LYS B CD  1 
ATOM   3783 C CE  . LYS B 1 194 ? 43.911  7.091   6.754   0.88  51.89  ? 194  LYS B CE  1 
ATOM   3784 N NZ  . LYS B 1 194 ? 44.157  8.312   5.920   0.88  50.63  ? 194  LYS B NZ  1 
ATOM   3785 N N   . GLU B 1 195 ? 43.074  1.485   8.809   1.00  51.13  ? 195  GLU B N   1 
ATOM   3786 C CA  . GLU B 1 195 ? 42.615  1.013   10.116  1.00  51.89  ? 195  GLU B CA  1 
ATOM   3787 C C   . GLU B 1 195 ? 42.040  2.093   11.035  1.00  51.85  ? 195  GLU B C   1 
ATOM   3788 O O   . GLU B 1 195 ? 40.915  1.935   11.513  1.00  52.34  ? 195  GLU B O   1 
ATOM   3789 C CB  . GLU B 1 195 ? 43.648  0.121   10.830  1.00  51.97  ? 195  GLU B CB  1 
ATOM   3790 C CG  . GLU B 1 195 ? 45.107  0.479   10.611  1.00  53.46  ? 195  GLU B CG  1 
ATOM   3791 C CD  . GLU B 1 195 ? 45.975  -0.767  10.410  1.00  56.06  ? 195  GLU B CD  1 
ATOM   3792 O OE1 . GLU B 1 195 ? 47.096  -0.850  10.997  1.00  55.76  ? 195  GLU B OE1 1 
ATOM   3793 O OE2 . GLU B 1 195 ? 45.536  -1.676  9.658   1.00  56.96  ? 195  GLU B OE2 1 
ATOM   3794 N N   . ARG B 1 196 ? 42.787  3.177   11.261  0.010 51.69  ? 196  ARG B N   1 
ATOM   3795 C CA  . ARG B 1 196 ? 42.364  4.277   12.152  0.010 51.50  ? 196  ARG B CA  1 
ATOM   3796 C C   . ARG B 1 196 ? 42.590  3.953   13.628  0.010 51.47  ? 196  ARG B C   1 
ATOM   3797 O O   . ARG B 1 196 ? 42.126  2.928   14.128  0.010 51.44  ? 196  ARG B O   1 
ATOM   3798 C CB  . ARG B 1 196 ? 40.896  4.671   11.909  0.010 51.46  ? 196  ARG B CB  1 
ATOM   3799 C CG  . ARG B 1 196 ? 40.073  4.854   13.184  0.010 51.34  ? 196  ARG B CG  1 
ATOM   3800 C CD  . ARG B 1 196 ? 38.641  4.351   12.996  0.010 51.16  ? 196  ARG B CD  1 
ATOM   3801 N NE  . ARG B 1 196 ? 37.684  5.414   12.691  0.010 51.04  ? 196  ARG B NE  1 
ATOM   3802 C CZ  . ARG B 1 196 ? 37.743  6.645   13.188  0.010 50.98  ? 196  ARG B CZ  1 
ATOM   3803 N NH1 . ARG B 1 196 ? 38.713  6.978   14.028  0.010 50.95  ? 196  ARG B NH1 1 
ATOM   3804 N NH2 . ARG B 1 196 ? 36.826  7.542   12.852  0.010 50.95  ? 196  ARG B NH2 1 
ATOM   3805 N N   . ARG B 1 204 ? 46.124  4.473   10.034  0.74  51.44  ? 204  ARG B N   1 
ATOM   3806 C CA  . ARG B 1 204 ? 47.113  4.026   9.055   0.74  51.49  ? 204  ARG B CA  1 
ATOM   3807 C C   . ARG B 1 204 ? 46.495  3.169   7.950   0.74  51.31  ? 204  ARG B C   1 
ATOM   3808 O O   . ARG B 1 204 ? 45.570  2.391   8.191   0.74  51.49  ? 204  ARG B O   1 
ATOM   3809 C CB  . ARG B 1 204 ? 48.227  3.227   9.738   0.74  51.56  ? 204  ARG B CB  1 
ATOM   3810 C CG  . ARG B 1 204 ? 49.208  4.037   10.598  0.74  53.07  ? 204  ARG B CG  1 
ATOM   3811 C CD  . ARG B 1 204 ? 50.011  5.105   9.828   0.74  54.25  ? 204  ARG B CD  1 
ATOM   3812 N NE  . ARG B 1 204 ? 50.337  4.722   8.454   0.74  56.65  ? 204  ARG B NE  1 
ATOM   3813 C CZ  . ARG B 1 204 ? 51.212  3.777   8.106   0.74  57.49  ? 204  ARG B CZ  1 
ATOM   3814 N NH1 . ARG B 1 204 ? 51.867  3.085   9.034   0.74  57.31  ? 204  ARG B NH1 1 
ATOM   3815 N NH2 . ARG B 1 204 ? 51.421  3.512   6.818   0.74  56.99  ? 204  ARG B NH2 1 
ATOM   3816 N N   . MET B 1 205 ? 47.028  3.302   6.739   1.00  51.00  ? 205  MET B N   1 
ATOM   3817 C CA  . MET B 1 205 ? 46.613  2.479   5.609   1.00  50.84  ? 205  MET B CA  1 
ATOM   3818 C C   . MET B 1 205 ? 47.507  1.252   5.460   1.00  50.70  ? 205  MET B C   1 
ATOM   3819 O O   . MET B 1 205 ? 48.729  1.352   5.530   1.00  50.84  ? 205  MET B O   1 
ATOM   3820 C CB  . MET B 1 205 ? 46.684  3.281   4.312   1.00  50.94  ? 205  MET B CB  1 
ATOM   3821 C CG  . MET B 1 205 ? 45.596  4.311   4.131   1.00  51.31  ? 205  MET B CG  1 
ATOM   3822 S SD  . MET B 1 205 ? 45.761  5.119   2.532   1.00  51.25  ? 205  MET B SD  1 
ATOM   3823 C CE  . MET B 1 205 ? 44.156  5.912   2.421   1.00  52.05  ? 205  MET B CE  1 
ATOM   3824 N N   . VAL B 1 206 ? 46.894  0.094   5.246   1.00  50.41  ? 206  VAL B N   1 
ATOM   3825 C CA  . VAL B 1 206 ? 47.650  -1.119  4.957   1.00  50.03  ? 206  VAL B CA  1 
ATOM   3826 C C   . VAL B 1 206 ? 47.281  -1.665  3.585   1.00  49.75  ? 206  VAL B C   1 
ATOM   3827 O O   . VAL B 1 206 ? 46.106  -1.725  3.212   1.00  49.62  ? 206  VAL B O   1 
ATOM   3828 C CB  . VAL B 1 206 ? 47.477  -2.202  6.034   1.00  50.11  ? 206  VAL B CB  1 
ATOM   3829 C CG1 . VAL B 1 206 ? 48.131  -1.757  7.338   1.00  50.78  ? 206  VAL B CG1 1 
ATOM   3830 C CG2 . VAL B 1 206 ? 46.013  -2.507  6.264   1.00  50.96  ? 206  VAL B CG2 1 
ATOM   3831 N N   . LEU B 1 207 ? 48.306  -2.038  2.828   1.00  49.49  ? 207  LEU B N   1 
ATOM   3832 C CA  . LEU B 1 207 ? 48.124  -2.517  1.477   1.00  48.85  ? 207  LEU B CA  1 
ATOM   3833 C C   . LEU B 1 207 ? 48.465  -3.997  1.393   1.00  48.85  ? 207  LEU B C   1 
ATOM   3834 O O   . LEU B 1 207 ? 49.455  -4.451  1.966   1.00  49.00  ? 207  LEU B O   1 
ATOM   3835 C CB  . LEU B 1 207 ? 48.968  -1.690  0.513   1.00  48.81  ? 207  LEU B CB  1 
ATOM   3836 C CG  . LEU B 1 207 ? 48.983  -2.008  -0.992  1.00  48.66  ? 207  LEU B CG  1 
ATOM   3837 C CD1 . LEU B 1 207 ? 47.601  -1.918  -1.637  1.00  47.74  ? 207  LEU B CD1 1 
ATOM   3838 C CD2 . LEU B 1 207 ? 49.950  -1.068  -1.684  1.00  47.80  ? 207  LEU B CD2 1 
ATOM   3839 N N   . VAL B 1 208 ? 47.608  -4.740  0.699   1.00  48.83  ? 208  VAL B N   1 
ATOM   3840 C CA  . VAL B 1 208 ? 47.785  -6.168  0.462   1.00  48.70  ? 208  VAL B CA  1 
ATOM   3841 C C   . VAL B 1 208 ? 47.671  -6.459  -1.041  1.00  48.80  ? 208  VAL B C   1 
ATOM   3842 O O   . VAL B 1 208 ? 46.673  -6.105  -1.692  1.00  48.87  ? 208  VAL B O   1 
ATOM   3843 C CB  . VAL B 1 208 ? 46.779  -7.021  1.281   1.00  48.95  ? 208  VAL B CB  1 
ATOM   3844 C CG1 . VAL B 1 208 ? 47.142  -6.993  2.766   1.00  49.32  ? 208  VAL B CG1 1 
ATOM   3845 C CG2 . VAL B 1 208 ? 45.328  -6.545  1.076   1.00  48.69  ? 208  VAL B CG2 1 
ATOM   3846 N N   . GLY B 1 209 ? 48.705  -7.087  -1.589  1.00  48.63  ? 209  GLY B N   1 
ATOM   3847 C CA  . GLY B 1 209 ? 48.812  -7.305  -3.025  1.00  48.29  ? 209  GLY B CA  1 
ATOM   3848 C C   . GLY B 1 209 ? 50.041  -6.617  -3.575  1.00  48.33  ? 209  GLY B C   1 
ATOM   3849 O O   . GLY B 1 209 ? 50.478  -5.606  -3.032  1.00  48.49  ? 209  GLY B O   1 
ATOM   3850 N N   . ASP B 1 210 ? 50.589  -7.160  -4.659  0.68  48.56  ? 210  ASP B N   1 
ATOM   3851 C CA  . ASP B 1 210 ? 51.829  -6.663  -5.251  0.68  48.90  ? 210  ASP B CA  1 
ATOM   3852 C C   . ASP B 1 210 ? 51.569  -5.470  -6.163  0.68  48.94  ? 210  ASP B C   1 
ATOM   3853 O O   . ASP B 1 210 ? 50.714  -5.535  -7.051  0.68  49.02  ? 210  ASP B O   1 
ATOM   3854 C CB  . ASP B 1 210 ? 52.539  -7.788  -6.024  0.68  49.05  ? 210  ASP B CB  1 
ATOM   3855 C CG  . ASP B 1 210 ? 54.021  -7.500  -6.257  0.68  49.59  ? 210  ASP B CG  1 
ATOM   3856 O OD1 . ASP B 1 210 ? 54.359  -6.917  -7.314  0.68  48.24  ? 210  ASP B OD1 1 
ATOM   3857 O OD2 . ASP B 1 210 ? 54.846  -7.879  -5.389  0.68  50.34  ? 210  ASP B OD2 1 
ATOM   3858 N N   . VAL B 1 211 ? 52.295  -4.376  -5.925  1.00  48.96  ? 211  VAL B N   1 
ATOM   3859 C CA  . VAL B 1 211 ? 52.250  -3.194  -6.803  1.00  49.00  ? 211  VAL B CA  1 
ATOM   3860 C C   . VAL B 1 211 ? 53.637  -2.716  -7.238  1.00  49.04  ? 211  VAL B C   1 
ATOM   3861 O O   . VAL B 1 211 ? 53.755  -1.657  -7.849  1.00  49.17  ? 211  VAL B O   1 
ATOM   3862 C CB  . VAL B 1 211 ? 51.473  -1.992  -6.176  1.00  49.05  ? 211  VAL B CB  1 
ATOM   3863 C CG1 . VAL B 1 211 ? 49.977  -2.263  -6.134  1.00  49.10  ? 211  VAL B CG1 1 
ATOM   3864 C CG2 . VAL B 1 211 ? 52.007  -1.632  -4.789  1.00  49.46  ? 211  VAL B CG2 1 
ATOM   3865 N N   . LYS B 1 212 ? 54.670  -3.500  -6.928  0.87  49.18  ? 212  LYS B N   1 
ATOM   3866 C CA  . LYS B 1 212 ? 56.055  -3.134  -7.216  0.87  49.31  ? 212  LYS B CA  1 
ATOM   3867 C C   . LYS B 1 212 ? 56.302  -3.025  -8.715  0.87  49.47  ? 212  LYS B C   1 
ATOM   3868 O O   . LYS B 1 212 ? 55.934  -3.918  -9.478  0.87  49.17  ? 212  LYS B O   1 
ATOM   3869 C CB  . LYS B 1 212 ? 57.022  -4.142  -6.590  0.87  49.47  ? 212  LYS B CB  1 
ATOM   3870 C CG  . LYS B 1 212 ? 58.463  -3.649  -6.484  0.87  50.29  ? 212  LYS B CG  1 
ATOM   3871 C CD  . LYS B 1 212 ? 59.325  -4.640  -5.705  0.87  52.07  ? 212  LYS B CD  1 
ATOM   3872 C CE  . LYS B 1 212 ? 60.788  -4.185  -5.612  0.87  52.91  ? 212  LYS B CE  1 
ATOM   3873 N NZ  . LYS B 1 212 ? 60.968  -2.925  -4.829  0.87  52.74  ? 212  LYS B NZ  1 
ATOM   3874 N N   . ASP B 1 213 ? 56.914  -1.908  -9.119  1.00  49.83  ? 213  ASP B N   1 
ATOM   3875 C CA  . ASP B 1 213 ? 57.236  -1.610  -10.520 1.00  49.88  ? 213  ASP B CA  1 
ATOM   3876 C C   . ASP B 1 213 ? 56.079  -1.822  -11.480 1.00  49.78  ? 213  ASP B C   1 
ATOM   3877 O O   . ASP B 1 213 ? 56.274  -2.224  -12.632 1.00  50.13  ? 213  ASP B O   1 
ATOM   3878 C CB  . ASP B 1 213 ? 58.476  -2.384  -10.978 1.00  50.08  ? 213  ASP B CB  1 
ATOM   3879 C CG  . ASP B 1 213 ? 59.744  -1.879  -10.330 1.00  50.85  ? 213  ASP B CG  1 
ATOM   3880 O OD1 . ASP B 1 213 ? 60.657  -2.711  -10.132 1.00  53.14  ? 213  ASP B OD1 1 
ATOM   3881 O OD2 . ASP B 1 213 ? 59.826  -0.663  -10.009 1.00  50.22  ? 213  ASP B OD2 1 
ATOM   3882 N N   . ARG B 1 214 ? 54.873  -1.559  -10.990 1.00  49.59  ? 214  ARG B N   1 
ATOM   3883 C CA  . ARG B 1 214 ? 53.671  -1.594  -11.810 1.00  49.15  ? 214  ARG B CA  1 
ATOM   3884 C C   . ARG B 1 214 ? 52.944  -0.261  -11.698 1.00  48.69  ? 214  ARG B C   1 
ATOM   3885 O O   . ARG B 1 214 ? 52.945  0.375   -10.630 1.00  48.52  ? 214  ARG B O   1 
ATOM   3886 C CB  . ARG B 1 214 ? 52.747  -2.723  -11.353 1.00  49.35  ? 214  ARG B CB  1 
ATOM   3887 C CG  . ARG B 1 214 ? 53.278  -4.114  -11.641 1.00  50.75  ? 214  ARG B CG  1 
ATOM   3888 C CD  . ARG B 1 214 ? 52.404  -5.197  -11.034 1.00  52.62  ? 214  ARG B CD  1 
ATOM   3889 N NE  . ARG B 1 214 ? 52.771  -6.517  -11.549 1.00  55.41  ? 214  ARG B NE  1 
ATOM   3890 C CZ  . ARG B 1 214 ? 52.073  -7.200  -12.457 1.00  56.85  ? 214  ARG B CZ  1 
ATOM   3891 N NH1 . ARG B 1 214 ? 50.940  -6.702  -12.958 1.00  56.50  ? 214  ARG B NH1 1 
ATOM   3892 N NH2 . ARG B 1 214 ? 52.503  -8.394  -12.858 1.00  57.78  ? 214  ARG B NH2 1 
ATOM   3893 N N   . VAL B 1 215 ? 52.347  0.169   -12.806 1.00  47.89  ? 215  VAL B N   1 
ATOM   3894 C CA  . VAL B 1 215 ? 51.360  1.244   -12.777 1.00  47.28  ? 215  VAL B CA  1 
ATOM   3895 C C   . VAL B 1 215 ? 50.217  0.790   -11.867 1.00  47.04  ? 215  VAL B C   1 
ATOM   3896 O O   . VAL B 1 215 ? 49.746  -0.342  -11.980 1.00  46.97  ? 215  VAL B O   1 
ATOM   3897 C CB  . VAL B 1 215 ? 50.835  1.568   -14.202 1.00  47.20  ? 215  VAL B CB  1 
ATOM   3898 C CG1 . VAL B 1 215 ? 49.584  2.434   -14.158 1.00  47.14  ? 215  VAL B CG1 1 
ATOM   3899 C CG2 . VAL B 1 215 ? 51.916  2.236   -15.036 1.00  47.00  ? 215  VAL B CG2 1 
ATOM   3900 N N   . ALA B 1 216 ? 49.811  1.653   -10.942 1.00  46.84  ? 216  ALA B N   1 
ATOM   3901 C CA  . ALA B 1 216 ? 48.684  1.356   -10.069 1.00  46.96  ? 216  ALA B CA  1 
ATOM   3902 C C   . ALA B 1 216 ? 47.487  2.234   -10.413 1.00  47.09  ? 216  ALA B C   1 
ATOM   3903 O O   . ALA B 1 216 ? 47.620  3.444   -10.607 1.00  47.38  ? 216  ALA B O   1 
ATOM   3904 C CB  . ALA B 1 216 ? 49.069  1.515   -8.608  1.00  47.18  ? 216  ALA B CB  1 
ATOM   3905 N N   . ILE B 1 217 ? 46.317  1.610   -10.495 1.00  46.97  ? 217  ILE B N   1 
ATOM   3906 C CA  . ILE B 1 217 ? 45.099  2.303   -10.867 1.00  47.06  ? 217  ILE B CA  1 
ATOM   3907 C C   . ILE B 1 217 ? 44.075  2.188   -9.754  1.00  47.53  ? 217  ILE B C   1 
ATOM   3908 O O   . ILE B 1 217 ? 43.473  1.130   -9.549  1.00  47.51  ? 217  ILE B O   1 
ATOM   3909 C CB  . ILE B 1 217 ? 44.514  1.761   -12.195 1.00  47.00  ? 217  ILE B CB  1 
ATOM   3910 C CG1 . ILE B 1 217 ? 45.510  1.972   -13.341 1.00  46.60  ? 217  ILE B CG1 1 
ATOM   3911 C CG2 . ILE B 1 217 ? 43.167  2.414   -12.502 1.00  46.98  ? 217  ILE B CG2 1 
ATOM   3912 C CD1 . ILE B 1 217 ? 45.191  1.213   -14.597 1.00  45.55  ? 217  ILE B CD1 1 
ATOM   3913 N N   . LEU B 1 218 ? 43.903  3.284   -9.023  1.00  48.29  ? 218  LEU B N   1 
ATOM   3914 C CA  . LEU B 1 218 ? 42.858  3.393   -8.015  1.00  48.93  ? 218  LEU B CA  1 
ATOM   3915 C C   . LEU B 1 218 ? 41.480  3.505   -8.660  1.00  49.64  ? 218  LEU B C   1 
ATOM   3916 O O   . LEU B 1 218 ? 41.229  4.377   -9.495  1.00  49.64  ? 218  LEU B O   1 
ATOM   3917 C CB  . LEU B 1 218 ? 43.132  4.575   -7.081  1.00  48.86  ? 218  LEU B CB  1 
ATOM   3918 C CG  . LEU B 1 218 ? 44.111  4.283   -5.934  1.00  48.30  ? 218  LEU B CG  1 
ATOM   3919 C CD1 . LEU B 1 218 ? 44.776  5.539   -5.398  1.00  48.04  ? 218  LEU B CD1 1 
ATOM   3920 C CD2 . LEU B 1 218 ? 43.416  3.532   -4.810  1.00  48.26  ? 218  LEU B CD2 1 
ATOM   3921 N N   . VAL B 1 219 ? 40.607  2.584   -8.273  1.00  50.77  ? 219  VAL B N   1 
ATOM   3922 C CA  . VAL B 1 219 ? 39.254  2.485   -8.809  1.00  51.71  ? 219  VAL B CA  1 
ATOM   3923 C C   . VAL B 1 219 ? 38.274  2.723   -7.670  1.00  52.34  ? 219  VAL B C   1 
ATOM   3924 O O   . VAL B 1 219 ? 38.387  2.101   -6.612  1.00  52.61  ? 219  VAL B O   1 
ATOM   3925 C CB  . VAL B 1 219 ? 39.035  1.087   -9.438  1.00  51.73  ? 219  VAL B CB  1 
ATOM   3926 C CG1 . VAL B 1 219 ? 37.547  0.707   -9.482  1.00  52.51  ? 219  VAL B CG1 1 
ATOM   3927 C CG2 . VAL B 1 219 ? 39.669  1.033   -10.830 1.00  51.54  ? 219  VAL B CG2 1 
ATOM   3928 N N   . ASP B 1 220 ? 37.322  3.628   -7.873  1.00  53.28  ? 220  ASP B N   1 
ATOM   3929 C CA  . ASP B 1 220 ? 36.296  3.873   -6.857  1.00  54.27  ? 220  ASP B CA  1 
ATOM   3930 C C   . ASP B 1 220 ? 34.940  4.231   -7.466  1.00  54.72  ? 220  ASP B C   1 
ATOM   3931 O O   . ASP B 1 220 ? 34.830  4.455   -8.679  1.00  54.81  ? 220  ASP B O   1 
ATOM   3932 C CB  . ASP B 1 220 ? 36.758  4.951   -5.871  1.00  54.39  ? 220  ASP B CB  1 
ATOM   3933 C CG  . ASP B 1 220 ? 36.420  4.606   -4.428  1.00  55.77  ? 220  ASP B CG  1 
ATOM   3934 O OD1 . ASP B 1 220 ? 35.879  3.505   -4.192  1.00  57.33  ? 220  ASP B OD1 1 
ATOM   3935 O OD2 . ASP B 1 220 ? 36.701  5.428   -3.524  1.00  56.78  ? 220  ASP B OD2 1 
ATOM   3936 N N   . ASP B 1 221 ? 33.911  4.249   -6.619  0.83  55.38  ? 221  ASP B N   1 
ATOM   3937 C CA  . ASP B 1 221 ? 32.561  4.621   -7.036  0.83  56.13  ? 221  ASP B CA  1 
ATOM   3938 C C   . ASP B 1 221 ? 32.408  6.141   -7.064  0.83  56.78  ? 221  ASP B C   1 
ATOM   3939 O O   . ASP B 1 221 ? 31.749  6.700   -7.948  0.83  56.58  ? 221  ASP B O   1 
ATOM   3940 C CB  . ASP B 1 221 ? 31.506  3.976   -6.124  0.83  56.08  ? 221  ASP B CB  1 
ATOM   3941 C CG  . ASP B 1 221 ? 31.692  4.322   -4.646  0.83  56.28  ? 221  ASP B CG  1 
ATOM   3942 O OD1 . ASP B 1 221 ? 32.757  4.862   -4.263  0.83  56.96  ? 221  ASP B OD1 1 
ATOM   3943 O OD2 . ASP B 1 221 ? 30.760  4.040   -3.861  0.83  56.18  ? 221  ASP B OD2 1 
ATOM   3944 N N   . MET B 1 222 ? 33.034  6.799   -6.088  1.00  57.67  ? 222  MET B N   1 
ATOM   3945 C CA  . MET B 1 222 ? 33.020  8.257   -5.985  1.00  58.52  ? 222  MET B CA  1 
ATOM   3946 C C   . MET B 1 222 ? 34.259  8.791   -5.254  1.00  58.59  ? 222  MET B C   1 
ATOM   3947 O O   . MET B 1 222 ? 34.988  8.031   -4.610  1.00  58.59  ? 222  MET B O   1 
ATOM   3948 C CB  . MET B 1 222 ? 31.725  8.753   -5.314  1.00  58.66  ? 222  MET B CB  1 
ATOM   3949 C CG  . MET B 1 222 ? 31.586  8.418   -3.828  1.00  60.19  ? 222  MET B CG  1 
ATOM   3950 S SD  . MET B 1 222 ? 30.038  9.043   -3.113  1.00  64.45  ? 222  MET B SD  1 
ATOM   3951 C CE  . MET B 1 222 ? 28.846  7.772   -3.601  1.00  63.14  ? 222  MET B CE  1 
ATOM   3952 N N   . ALA B 1 223 ? 34.488  10.097  -5.386  1.00  58.91  ? 223  ALA B N   1 
ATOM   3953 C CA  . ALA B 1 223 ? 35.480  10.826  -4.596  1.00  58.90  ? 223  ALA B CA  1 
ATOM   3954 C C   . ALA B 1 223 ? 34.851  12.121  -4.085  1.00  59.20  ? 223  ALA B C   1 
ATOM   3955 O O   . ALA B 1 223 ? 34.247  12.867  -4.871  1.00  58.80  ? 223  ALA B O   1 
ATOM   3956 C CB  . ALA B 1 223 ? 36.697  11.131  -5.431  1.00  58.94  ? 223  ALA B CB  1 
ATOM   3957 N N   . ASP B 1 224 ? 35.004  12.393  -2.781  1.00  59.65  ? 224  ASP B N   1 
ATOM   3958 C CA  . ASP B 1 224 ? 34.290  13.517  -2.136  1.00  59.97  ? 224  ASP B CA  1 
ATOM   3959 C C   . ASP B 1 224 ? 35.118  14.655  -1.505  1.00  60.18  ? 224  ASP B C   1 
ATOM   3960 O O   . ASP B 1 224 ? 34.820  15.841  -1.744  1.00  60.88  ? 224  ASP B O   1 
ATOM   3961 C CB  . ASP B 1 224 ? 33.264  13.018  -1.121  1.00  59.97  ? 224  ASP B CB  1 
ATOM   3962 C CG  . ASP B 1 224 ? 32.455  14.156  -0.514  1.00  60.48  ? 224  ASP B CG  1 
ATOM   3963 O OD1 . ASP B 1 224 ? 32.049  15.082  -1.269  1.00  61.22  ? 224  ASP B OD1 1 
ATOM   3964 O OD2 . ASP B 1 224 ? 32.234  14.128  0.722   1.00  60.60  ? 224  ASP B OD2 1 
ATOM   3965 N N   . THR B 1 225 ? 36.103  14.317  -0.673  1.00  59.97  ? 225  THR B N   1 
ATOM   3966 C CA  . THR B 1 225 ? 37.075  15.310  -0.189  1.00  59.52  ? 225  THR B CA  1 
ATOM   3967 C C   . THR B 1 225 ? 38.471  14.843  -0.605  1.00  59.51  ? 225  THR B C   1 
ATOM   3968 O O   . THR B 1 225 ? 39.470  15.562  -0.443  1.00  59.47  ? 225  THR B O   1 
ATOM   3969 C CB  . THR B 1 225 ? 37.004  15.537  1.344   1.00  59.46  ? 225  THR B CB  1 
ATOM   3970 O OG1 . THR B 1 225 ? 37.347  14.336  2.049   1.00  59.18  ? 225  THR B OG1 1 
ATOM   3971 C CG2 . THR B 1 225 ? 35.621  16.006  1.764   1.00  59.81  ? 225  THR B CG2 1 
ATOM   3972 N N   . CYS B 1 226 ? 38.508  13.622  -1.148  1.00  59.20  ? 226  CYS B N   1 
ATOM   3973 C CA  . CYS B 1 226 ? 39.708  12.992  -1.707  1.00  59.00  ? 226  CYS B CA  1 
ATOM   3974 C C   . CYS B 1 226 ? 40.803  12.687  -0.679  1.00  58.83  ? 226  CYS B C   1 
ATOM   3975 O O   . CYS B 1 226 ? 41.924  12.306  -1.055  1.00  58.76  ? 226  CYS B O   1 
ATOM   3976 C CB  . CYS B 1 226 ? 40.260  13.795  -2.897  1.00  59.21  ? 226  CYS B CB  1 
ATOM   3977 S SG  . CYS B 1 226 ? 39.222  13.715  -4.382  1.00  59.35  ? 226  CYS B SG  1 
ATOM   3978 N N   . GLY B 1 227 ? 40.466  12.833  0.606   1.00  58.31  ? 227  GLY B N   1 
ATOM   3979 C CA  . GLY B 1 227 ? 41.359  12.458  1.695   1.00  57.76  ? 227  GLY B CA  1 
ATOM   3980 C C   . GLY B 1 227 ? 41.924  11.063  1.509   1.00  57.49  ? 227  GLY B C   1 
ATOM   3981 O O   . GLY B 1 227 ? 43.141  10.887  1.472   1.00  57.41  ? 227  GLY B O   1 
ATOM   3982 N N   . THR B 1 228 ? 41.034  10.081  1.359   1.00  57.27  ? 228  THR B N   1 
ATOM   3983 C CA  . THR B 1 228 ? 41.415  8.675   1.180   1.00  56.88  ? 228  THR B CA  1 
ATOM   3984 C C   . THR B 1 228 ? 42.261  8.440   -0.087  1.00  56.64  ? 228  THR B C   1 
ATOM   3985 O O   . THR B 1 228 ? 43.349  7.850   -0.013  1.00  56.46  ? 228  THR B O   1 
ATOM   3986 C CB  . THR B 1 228 ? 40.165  7.750   1.176   1.00  56.92  ? 228  THR B CB  1 
ATOM   3987 O OG1 . THR B 1 228 ? 39.372  8.006   2.344   1.00  57.08  ? 228  THR B OG1 1 
ATOM   3988 C CG2 . THR B 1 228 ? 40.563  6.275   1.145   1.00  56.96  ? 228  THR B CG2 1 
ATOM   3989 N N   . ILE B 1 229 ? 41.774  8.913   -1.236  1.00  56.13  ? 229  ILE B N   1 
ATOM   3990 C CA  . ILE B 1 229 ? 42.444  8.648   -2.526  1.00  55.70  ? 229  ILE B CA  1 
ATOM   3991 C C   . ILE B 1 229 ? 43.864  9.236   -2.662  1.00  55.31  ? 229  ILE B C   1 
ATOM   3992 O O   . ILE B 1 229 ? 44.663  8.747   -3.466  1.00  55.04  ? 229  ILE B O   1 
ATOM   3993 C CB  . ILE B 1 229 ? 41.582  9.072   -3.754  1.00  55.76  ? 229  ILE B CB  1 
ATOM   3994 C CG1 . ILE B 1 229 ? 41.558  10.591  -3.927  1.00  55.73  ? 229  ILE B CG1 1 
ATOM   3995 C CG2 . ILE B 1 229 ? 40.166  8.499   -3.668  1.00  56.51  ? 229  ILE B CG2 1 
ATOM   3996 C CD1 . ILE B 1 229 ? 41.303  11.012  -5.354  1.00  56.17  ? 229  ILE B CD1 1 
ATOM   3997 N N   . CYS B 1 230 ? 44.163  10.281  -1.884  1.00  54.88  ? 230  CYS B N   1 
ATOM   3998 C CA  . CYS B 1 230 ? 45.473  10.935  -1.908  1.00  54.36  ? 230  CYS B CA  1 
ATOM   3999 C C   . CYS B 1 230 ? 46.471  10.211  -1.010  1.00  53.92  ? 230  CYS B C   1 
ATOM   4000 O O   . CYS B 1 230 ? 47.644  10.046  -1.376  1.00  53.64  ? 230  CYS B O   1 
ATOM   4001 C CB  . CYS B 1 230 ? 45.355  12.403  -1.493  1.00  54.35  ? 230  CYS B CB  1 
ATOM   4002 S SG  . CYS B 1 230 ? 44.393  13.436  -2.636  1.00  55.92  ? 230  CYS B SG  1 
ATOM   4003 N N   . HIS B 1 231 ? 46.002  9.787   0.165   0.90  53.25  ? 231  HIS B N   1 
ATOM   4004 C CA  . HIS B 1 231 ? 46.820  9.006   1.095   0.90  52.68  ? 231  HIS B CA  1 
ATOM   4005 C C   . HIS B 1 231 ? 47.074  7.610   0.519   0.90  52.18  ? 231  HIS B C   1 
ATOM   4006 O O   . HIS B 1 231 ? 48.015  6.920   0.921   0.90  52.07  ? 231  HIS B O   1 
ATOM   4007 C CB  . HIS B 1 231 ? 46.137  8.894   2.463   0.90  52.62  ? 231  HIS B CB  1 
ATOM   4008 C CG  . HIS B 1 231 ? 46.081  10.182  3.228   0.90  53.29  ? 231  HIS B CG  1 
ATOM   4009 N ND1 . HIS B 1 231 ? 45.408  11.295  2.770   0.90  53.41  ? 231  HIS B ND1 1 
ATOM   4010 C CD2 . HIS B 1 231 ? 46.596  10.525  4.434   0.90  53.50  ? 231  HIS B CD2 1 
ATOM   4011 C CE1 . HIS B 1 231 ? 45.517  12.269  3.657   0.90  53.30  ? 231  HIS B CE1 1 
ATOM   4012 N NE2 . HIS B 1 231 ? 46.234  11.829  4.674   0.90  52.86  ? 231  HIS B NE2 1 
ATOM   4013 N N   . ALA B 1 232 ? 46.218  7.205   -0.421  1.00  51.29  ? 232  ALA B N   1 
ATOM   4014 C CA  . ALA B 1 232 ? 46.362  5.927   -1.108  1.00  50.67  ? 232  ALA B CA  1 
ATOM   4015 C C   . ALA B 1 232 ? 47.385  6.024   -2.237  1.00  50.13  ? 232  ALA B C   1 
ATOM   4016 O O   . ALA B 1 232 ? 48.060  5.044   -2.560  1.00  49.56  ? 232  ALA B O   1 
ATOM   4017 C CB  . ALA B 1 232 ? 45.007  5.446   -1.638  1.00  50.60  ? 232  ALA B CB  1 
ATOM   4018 N N   . ALA B 1 233 ? 47.488  7.211   -2.832  1.00  49.91  ? 233  ALA B N   1 
ATOM   4019 C CA  . ALA B 1 233 ? 48.494  7.495   -3.862  1.00  49.90  ? 233  ALA B CA  1 
ATOM   4020 C C   . ALA B 1 233 ? 49.906  7.482   -3.276  1.00  49.79  ? 233  ALA B C   1 
ATOM   4021 O O   . ALA B 1 233 ? 50.808  6.874   -3.857  1.00  50.31  ? 233  ALA B O   1 
ATOM   4022 C CB  . ALA B 1 233 ? 48.212  8.832   -4.550  1.00  49.77  ? 233  ALA B CB  1 
ATOM   4023 N N   . ASP B 1 234 ? 50.089  8.143   -2.133  1.00  49.43  ? 234  ASP B N   1 
ATOM   4024 C CA  . ASP B 1 234 ? 51.371  8.113   -1.426  1.00  49.32  ? 234  ASP B CA  1 
ATOM   4025 C C   . ASP B 1 234 ? 51.720  6.677   -1.067  1.00  48.96  ? 234  ASP B C   1 
ATOM   4026 O O   . ASP B 1 234 ? 52.835  6.214   -1.340  1.00  49.11  ? 234  ASP B O   1 
ATOM   4027 C CB  . ASP B 1 234 ? 51.357  8.983   -0.154  1.00  49.42  ? 234  ASP B CB  1 
ATOM   4028 C CG  . ASP B 1 234 ? 50.994  10.440  -0.424  1.00  49.12  ? 234  ASP B CG  1 
ATOM   4029 O OD1 . ASP B 1 234 ? 51.330  10.968  -1.510  1.00  49.31  ? 234  ASP B OD1 1 
ATOM   4030 O OD2 . ASP B 1 234 ? 50.366  11.059  0.465   1.00  48.76  ? 234  ASP B OD2 1 
ATOM   4031 N N   . LYS B 1 235 ? 50.753  5.981   -0.473  1.00  48.45  ? 235  LYS B N   1 
ATOM   4032 C CA  . LYS B 1 235 ? 50.916  4.592   -0.045  1.00  48.22  ? 235  LYS B CA  1 
ATOM   4033 C C   . LYS B 1 235 ? 51.393  3.703   -1.193  1.00  48.33  ? 235  LYS B C   1 
ATOM   4034 O O   . LYS B 1 235 ? 52.365  2.954   -1.040  1.00  48.64  ? 235  LYS B O   1 
ATOM   4035 C CB  . LYS B 1 235 ? 49.603  4.060   0.548   1.00  48.02  ? 235  LYS B CB  1 
ATOM   4036 C CG  . LYS B 1 235 ? 49.667  2.657   1.112   1.00  47.80  ? 235  LYS B CG  1 
ATOM   4037 C CD  . LYS B 1 235 ? 50.081  2.649   2.573   1.00  48.23  ? 235  LYS B CD  1 
ATOM   4038 C CE  . LYS B 1 235 ? 50.678  1.295   2.950   1.00  49.00  ? 235  LYS B CE  1 
ATOM   4039 N NZ  . LYS B 1 235 ? 51.395  1.340   4.261   1.00  48.28  ? 235  LYS B NZ  1 
ATOM   4040 N N   . LEU B 1 236 ? 50.724  3.800   -2.340  1.00  48.16  ? 236  LEU B N   1 
ATOM   4041 C CA  . LEU B 1 236 ? 51.073  2.984   -3.497  1.00  48.22  ? 236  LEU B CA  1 
ATOM   4042 C C   . LEU B 1 236 ? 52.489  3.269   -3.995  1.00  48.45  ? 236  LEU B C   1 
ATOM   4043 O O   . LEU B 1 236 ? 53.278  2.333   -4.175  1.00  48.72  ? 236  LEU B O   1 
ATOM   4044 C CB  . LEU B 1 236 ? 50.032  3.131   -4.620  1.00  48.34  ? 236  LEU B CB  1 
ATOM   4045 C CG  . LEU B 1 236 ? 48.688  2.414   -4.374  1.00  48.24  ? 236  LEU B CG  1 
ATOM   4046 C CD1 . LEU B 1 236 ? 47.581  2.964   -5.257  1.00  47.27  ? 236  LEU B CD1 1 
ATOM   4047 C CD2 . LEU B 1 236 ? 48.813  0.904   -4.542  1.00  47.69  ? 236  LEU B CD2 1 
ATOM   4048 N N   . LEU B 1 237 ? 52.821  4.548   -4.194  1.00  48.45  ? 237  LEU B N   1 
ATOM   4049 C CA  . LEU B 1 237 ? 54.186  4.940   -4.572  1.00  48.19  ? 237  LEU B CA  1 
ATOM   4050 C C   . LEU B 1 237 ? 55.215  4.540   -3.498  1.00  48.24  ? 237  LEU B C   1 
ATOM   4051 O O   . LEU B 1 237 ? 56.346  4.182   -3.823  1.00  48.20  ? 237  LEU B O   1 
ATOM   4052 C CB  . LEU B 1 237 ? 54.277  6.438   -4.898  1.00  48.10  ? 237  LEU B CB  1 
ATOM   4053 C CG  . LEU B 1 237 ? 53.645  7.005   -6.187  1.00  48.04  ? 237  LEU B CG  1 
ATOM   4054 C CD1 . LEU B 1 237 ? 53.970  8.468   -6.331  1.00  47.77  ? 237  LEU B CD1 1 
ATOM   4055 C CD2 . LEU B 1 237 ? 54.041  6.291   -7.473  1.00  47.81  ? 237  LEU B CD2 1 
ATOM   4056 N N   . SER B 1 238 ? 54.816  4.583   -2.226  1.00  48.17  ? 238  SER B N   1 
ATOM   4057 C CA  . SER B 1 238 ? 55.648  4.050   -1.143  1.00  48.31  ? 238  SER B CA  1 
ATOM   4058 C C   . SER B 1 238 ? 55.962  2.560   -1.352  1.00  48.13  ? 238  SER B C   1 
ATOM   4059 O O   . SER B 1 238 ? 57.101  2.126   -1.146  1.00  47.72  ? 238  SER B O   1 
ATOM   4060 C CB  . SER B 1 238 ? 54.983  4.252   0.230   1.00  48.57  ? 238  SER B CB  1 
ATOM   4061 O OG  . SER B 1 238 ? 55.288  5.527   0.805   1.00  49.55  ? 238  SER B OG  1 
ATOM   4062 N N   . ALA B 1 239 ? 54.951  1.792   -1.776  1.00  47.96  ? 239  ALA B N   1 
ATOM   4063 C CA  . ALA B 1 239 ? 55.061  0.328   -1.883  1.00  47.82  ? 239  ALA B CA  1 
ATOM   4064 C C   . ALA B 1 239 ? 55.746  -0.164  -3.168  1.00  47.73  ? 239  ALA B C   1 
ATOM   4065 O O   . ALA B 1 239 ? 55.903  -1.370  -3.377  1.00  47.78  ? 239  ALA B O   1 
ATOM   4066 C CB  . ALA B 1 239 ? 53.693  -0.317  -1.725  1.00  47.49  ? 239  ALA B CB  1 
ATOM   4067 N N   . GLY B 1 240 ? 56.136  0.770   -4.030  1.00  47.59  ? 240  GLY B N   1 
ATOM   4068 C CA  . GLY B 1 240 ? 56.899  0.446   -5.233  1.00  47.62  ? 240  GLY B CA  1 
ATOM   4069 C C   . GLY B 1 240 ? 56.136  0.633   -6.539  1.00  47.74  ? 240  GLY B C   1 
ATOM   4070 O O   . GLY B 1 240 ? 56.584  0.196   -7.604  1.00  47.76  ? 240  GLY B O   1 
ATOM   4071 N N   . ALA B 1 241 ? 54.974  1.269   -6.465  1.00  47.58  ? 241  ALA B N   1 
ATOM   4072 C CA  . ALA B 1 241 ? 54.203  1.563   -7.664  1.00  47.64  ? 241  ALA B CA  1 
ATOM   4073 C C   . ALA B 1 241 ? 54.915  2.606   -8.528  1.00  47.64  ? 241  ALA B C   1 
ATOM   4074 O O   . ALA B 1 241 ? 55.413  3.613   -8.022  1.00  47.59  ? 241  ALA B O   1 
ATOM   4075 C CB  . ALA B 1 241 ? 52.777  2.020   -7.305  1.00  47.43  ? 241  ALA B CB  1 
ATOM   4076 N N   . THR B 1 242 ? 54.961  2.347   -9.833  1.00  47.68  ? 242  THR B N   1 
ATOM   4077 C CA  . THR B 1 242 ? 55.641  3.224   -10.781 1.00  47.51  ? 242  THR B CA  1 
ATOM   4078 C C   . THR B 1 242 ? 54.925  4.568   -10.829 1.00  47.56  ? 242  THR B C   1 
ATOM   4079 O O   . THR B 1 242 ? 55.525  5.604   -10.548 1.00  47.79  ? 242  THR B O   1 
ATOM   4080 C CB  . THR B 1 242 ? 55.746  2.562   -12.176 1.00  47.46  ? 242  THR B CB  1 
ATOM   4081 O OG1 . THR B 1 242 ? 56.641  1.442   -12.093 1.00  47.79  ? 242  THR B OG1 1 
ATOM   4082 C CG2 . THR B 1 242 ? 56.249  3.542   -13.226 1.00  46.88  ? 242  THR B CG2 1 
ATOM   4083 N N   . ARG B 1 243 ? 53.667  4.559   -11.240 1.00  47.58  ? 243  ARG B N   1 
ATOM   4084 C CA  . ARG B 1 243 ? 52.790  5.737   -11.224 1.00  47.62  ? 243  ARG B CA  1 
ATOM   4085 C C   . ARG B 1 243 ? 51.363  5.411   -10.826 1.00  47.26  ? 243  ARG B C   1 
ATOM   4086 O O   . ARG B 1 243 ? 50.944  4.320   -10.989 1.00  47.28  ? 243  ARG B O   1 
ATOM   4087 C CB  . ARG B 1 243 ? 52.774  6.538   -12.534 1.00  47.79  ? 243  ARG B CB  1 
ATOM   4088 C CG  . ARG B 1 243 ? 53.295  5.894   -13.763 1.00  49.20  ? 243  ARG B CG  1 
ATOM   4089 C CD  . ARG B 1 243 ? 53.219  6.830   -14.936 1.00  50.85  ? 243  ARG B CD  1 
ATOM   4090 N NE  . ARG B 1 243 ? 53.153  6.140   -16.213 1.00  52.76  ? 243  ARG B NE  1 
ATOM   4091 C CZ  . ARG B 1 243 ? 52.045  5.992   -16.913 1.00  54.32  ? 243  ARG B CZ  1 
ATOM   4092 N NH1 . ARG B 1 243 ? 50.918  6.456   -16.439 1.00  54.03  ? 243  ARG B NH1 1 
ATOM   4093 N NH2 . ARG B 1 243 ? 52.038  5.338   -18.060 1.00  55.06  ? 243  ARG B NH2 1 
ATOM   4094 N N   . VAL B 1 244 ? 50.627  6.378   -10.301 1.00  46.93  ? 244  VAL B N   1 
ATOM   4095 C CA  . VAL B 1 244 ? 49.296  6.136   -9.766  1.00  46.51  ? 244  VAL B CA  1 
ATOM   4096 C C   . VAL B 1 244 ? 48.220  6.884   -10.555 1.00  46.48  ? 244  VAL B C   1 
ATOM   4097 O O   . VAL B 1 244 ? 48.310  8.087   -10.800 1.00  46.42  ? 244  VAL B O   1 
ATOM   4098 C CB  . VAL B 1 244 ? 49.224  6.475   -8.260  1.00  46.39  ? 244  VAL B CB  1 
ATOM   4099 C CG1 . VAL B 1 244 ? 47.906  6.001   -7.652  1.00  46.42  ? 244  VAL B CG1 1 
ATOM   4100 C CG2 . VAL B 1 244 ? 50.396  5.850   -7.515  1.00  46.34  ? 244  VAL B CG2 1 
ATOM   4101 N N   . TYR B 1 245 ? 47.208  6.138   -10.977 1.00  46.41  ? 245  TYR B N   1 
ATOM   4102 C CA  . TYR B 1 245 ? 46.014  6.730   -11.555 1.00  46.48  ? 245  TYR B CA  1 
ATOM   4103 C C   . TYR B 1 245 ? 44.838  6.556   -10.602 1.00  46.11  ? 245  TYR B C   1 
ATOM   4104 O O   . TYR B 1 245 ? 44.777  5.584   -9.852  1.00  45.82  ? 245  TYR B O   1 
ATOM   4105 C CB  . TYR B 1 245 ? 45.705  6.096   -12.908 1.00  46.64  ? 245  TYR B CB  1 
ATOM   4106 C CG  . TYR B 1 245 ? 46.644  6.538   -14.015 1.00  47.60  ? 245  TYR B CG  1 
ATOM   4107 C CD1 . TYR B 1 245 ? 47.811  5.827   -14.299 1.00  47.52  ? 245  TYR B CD1 1 
ATOM   4108 C CD2 . TYR B 1 245 ? 46.359  7.666   -14.782 1.00  47.87  ? 245  TYR B CD2 1 
ATOM   4109 C CE1 . TYR B 1 245 ? 48.661  6.232   -15.314 1.00  47.74  ? 245  TYR B CE1 1 
ATOM   4110 C CE2 . TYR B 1 245 ? 47.203  8.076   -15.793 1.00  47.52  ? 245  TYR B CE2 1 
ATOM   4111 C CZ  . TYR B 1 245 ? 48.348  7.361   -16.057 1.00  47.92  ? 245  TYR B CZ  1 
ATOM   4112 O OH  . TYR B 1 245 ? 49.173  7.782   -17.079 1.00  49.15  ? 245  TYR B OH  1 
ATOM   4113 N N   . ALA B 1 246 ? 43.928  7.524   -10.611 1.00  45.89  ? 246  ALA B N   1 
ATOM   4114 C CA  . ALA B 1 246 ? 42.670  7.401   -9.888  1.00  45.86  ? 246  ALA B CA  1 
ATOM   4115 C C   . ALA B 1 246 ? 41.522  7.461   -10.876 1.00  45.81  ? 246  ALA B C   1 
ATOM   4116 O O   . ALA B 1 246 ? 41.443  8.377   -11.691 1.00  45.67  ? 246  ALA B O   1 
ATOM   4117 C CB  . ALA B 1 246 ? 42.537  8.497   -8.858  1.00  45.86  ? 246  ALA B CB  1 
ATOM   4118 N N   . ILE B 1 247 ? 40.645  6.471   -10.825 1.00  46.22  ? 247  ILE B N   1 
ATOM   4119 C CA  . ILE B 1 247 ? 39.460  6.485   -11.678 1.00  47.05  ? 247  ILE B CA  1 
ATOM   4120 C C   . ILE B 1 247 ? 38.190  6.397   -10.839 1.00  47.38  ? 247  ILE B C   1 
ATOM   4121 O O   . ILE B 1 247 ? 38.016  5.483   -10.049 1.00  47.35  ? 247  ILE B O   1 
ATOM   4122 C CB  . ILE B 1 247 ? 39.506  5.407   -12.802 1.00  47.05  ? 247  ILE B CB  1 
ATOM   4123 C CG1 . ILE B 1 247 ? 40.870  5.434   -13.508 1.00  46.90  ? 247  ILE B CG1 1 
ATOM   4124 C CG2 . ILE B 1 247 ? 38.406  5.662   -13.819 1.00  47.43  ? 247  ILE B CG2 1 
ATOM   4125 C CD1 . ILE B 1 247 ? 41.077  4.358   -14.538 1.00  46.62  ? 247  ILE B CD1 1 
ATOM   4126 N N   . LEU B 1 248 ? 37.327  7.391   -10.997 1.00  48.44  ? 248  LEU B N   1 
ATOM   4127 C CA  . LEU B 1 248 ? 36.072  7.467   -10.252 1.00  49.33  ? 248  LEU B CA  1 
ATOM   4128 C C   . LEU B 1 248 ? 34.925  7.509   -11.257 1.00  49.98  ? 248  LEU B C   1 
ATOM   4129 O O   . LEU B 1 248 ? 35.079  8.057   -12.350 1.00  50.19  ? 248  LEU B O   1 
ATOM   4130 C CB  . LEU B 1 248 ? 36.040  8.717   -9.368  1.00  49.17  ? 248  LEU B CB  1 
ATOM   4131 C CG  . LEU B 1 248 ? 37.232  9.130   -8.468  1.00  50.05  ? 248  LEU B CG  1 
ATOM   4132 C CD1 . LEU B 1 248 ? 37.848  7.941   -7.701  1.00  49.77  ? 248  LEU B CD1 1 
ATOM   4133 C CD2 . LEU B 1 248 ? 38.338  9.871   -9.247  1.00  49.82  ? 248  LEU B CD2 1 
ATOM   4134 N N   . THR B 1 249 ? 33.789  6.907   -10.913 1.00  50.64  ? 249  THR B N   1 
ATOM   4135 C CA  . THR B 1 249 ? 32.601  7.060   -11.741 1.00  51.51  ? 249  THR B CA  1 
ATOM   4136 C C   . THR B 1 249 ? 31.961  8.419   -11.432 1.00  51.65  ? 249  THR B C   1 
ATOM   4137 O O   . THR B 1 249 ? 31.832  9.259   -12.319 1.00  51.82  ? 249  THR B O   1 
ATOM   4138 C CB  . THR B 1 249 ? 31.608  5.892   -11.578 1.00  51.74  ? 249  THR B CB  1 
ATOM   4139 O OG1 . THR B 1 249 ? 31.031  5.922   -10.270 1.00  53.26  ? 249  THR B OG1 1 
ATOM   4140 C CG2 . THR B 1 249 ? 32.316  4.547   -11.773 1.00  52.54  ? 249  THR B CG2 1 
ATOM   4141 N N   . HIS B 1 250 ? 31.618  8.651   -10.165 0.40  51.98  ? 250  HIS B N   1 
ATOM   4142 C CA  . HIS B 1 250 ? 31.031  9.924   -9.741  0.40  52.30  ? 250  HIS B CA  1 
ATOM   4143 C C   . HIS B 1 250 ? 32.073  10.837  -9.092  0.40  52.83  ? 250  HIS B C   1 
ATOM   4144 O O   . HIS B 1 250 ? 32.657  10.494  -8.062  0.40  52.63  ? 250  HIS B O   1 
ATOM   4145 C CB  . HIS B 1 250 ? 29.858  9.683   -8.789  0.40  52.06  ? 250  HIS B CB  1 
ATOM   4146 C CG  . HIS B 1 250 ? 28.931  8.596   -9.240  0.40  51.67  ? 250  HIS B CG  1 
ATOM   4147 N ND1 . HIS B 1 250 ? 28.183  8.687   -10.393 0.40  51.31  ? 250  HIS B ND1 1 
ATOM   4148 C CD2 . HIS B 1 250 ? 28.632  7.394   -8.692  0.40  51.09  ? 250  HIS B CD2 1 
ATOM   4149 C CE1 . HIS B 1 250 ? 27.464  7.588   -10.537 0.40  51.05  ? 250  HIS B CE1 1 
ATOM   4150 N NE2 . HIS B 1 250 ? 27.718  6.788   -9.518  0.40  50.76  ? 250  HIS B NE2 1 
ATOM   4151 N N   . GLY B 1 251 ? 32.299  11.999  -9.701  1.00  53.64  ? 251  GLY B N   1 
ATOM   4152 C CA  . GLY B 1 251 ? 33.300  12.946  -9.215  1.00  54.50  ? 251  GLY B CA  1 
ATOM   4153 C C   . GLY B 1 251 ? 32.616  14.138  -8.585  1.00  55.30  ? 251  GLY B C   1 
ATOM   4154 O O   . GLY B 1 251 ? 32.129  15.032  -9.281  1.00  55.71  ? 251  GLY B O   1 
ATOM   4155 N N   . ILE B 1 252 ? 32.584  14.160  -7.256  1.00  56.00  ? 252  ILE B N   1 
ATOM   4156 C CA  . ILE B 1 252 ? 31.899  15.229  -6.534  1.00  56.70  ? 252  ILE B CA  1 
ATOM   4157 C C   . ILE B 1 252 ? 32.879  16.372  -6.266  1.00  57.26  ? 252  ILE B C   1 
ATOM   4158 O O   . ILE B 1 252 ? 32.546  17.539  -6.479  1.00  57.39  ? 252  ILE B O   1 
ATOM   4159 C CB  . ILE B 1 252 ? 31.259  14.779  -5.204  1.00  56.68  ? 252  ILE B CB  1 
ATOM   4160 C CG1 . ILE B 1 252 ? 30.698  13.357  -5.300  1.00  56.67  ? 252  ILE B CG1 1 
ATOM   4161 C CG2 . ILE B 1 252 ? 30.176  15.771  -4.789  1.00  57.05  ? 252  ILE B CG2 1 
ATOM   4162 C CD1 . ILE B 1 252 ? 30.348  12.746  -3.937  1.00  57.88  ? 252  ILE B CD1 1 
ATOM   4163 N N   . PHE B 1 253 ? 34.075  16.023  -5.788  1.00  57.94  ? 253  PHE B N   1 
ATOM   4164 C CA  . PHE B 1 253 ? 35.147  16.988  -5.498  1.00  58.43  ? 253  PHE B CA  1 
ATOM   4165 C C   . PHE B 1 253 ? 34.659  18.254  -4.785  1.00  58.93  ? 253  PHE B C   1 
ATOM   4166 O O   . PHE B 1 253 ? 34.697  19.358  -5.343  1.00  58.88  ? 253  PHE B O   1 
ATOM   4167 C CB  . PHE B 1 253 ? 35.926  17.353  -6.768  1.00  58.39  ? 253  PHE B CB  1 
ATOM   4168 C CG  . PHE B 1 253 ? 36.382  16.167  -7.565  1.00  58.40  ? 253  PHE B CG  1 
ATOM   4169 C CD1 . PHE B 1 253 ? 36.135  16.099  -8.930  1.00  58.01  ? 253  PHE B CD1 1 
ATOM   4170 C CD2 . PHE B 1 253 ? 37.054  15.112  -6.949  1.00  58.46  ? 253  PHE B CD2 1 
ATOM   4171 C CE1 . PHE B 1 253 ? 36.558  15.008  -9.668  1.00  58.14  ? 253  PHE B CE1 1 
ATOM   4172 C CE2 . PHE B 1 253 ? 37.477  14.014  -7.678  1.00  57.92  ? 253  PHE B CE2 1 
ATOM   4173 C CZ  . PHE B 1 253 ? 37.230  13.961  -9.038  1.00  58.36  ? 253  PHE B CZ  1 
ATOM   4174 N N   . SER B 1 254 ? 34.188  18.072  -3.555  1.00  59.47  ? 254  SER B N   1 
ATOM   4175 C CA  . SER B 1 254 ? 33.819  19.184  -2.683  1.00  60.04  ? 254  SER B CA  1 
ATOM   4176 C C   . SER B 1 254 ? 34.968  19.463  -1.719  1.00  60.49  ? 254  SER B C   1 
ATOM   4177 O O   . SER B 1 254 ? 35.919  18.680  -1.637  1.00  60.67  ? 254  SER B O   1 
ATOM   4178 C CB  . SER B 1 254 ? 32.543  18.853  -1.903  1.00  60.00  ? 254  SER B CB  1 
ATOM   4179 O OG  . SER B 1 254 ? 32.679  17.628  -1.200  1.00  59.67  ? 254  SER B OG  1 
ATOM   4180 N N   . GLY B 1 255 ? 34.878  20.575  -0.991  1.00  60.91  ? 255  GLY B N   1 
ATOM   4181 C CA  . GLY B 1 255 ? 35.876  20.918  0.020   1.00  61.29  ? 255  GLY B CA  1 
ATOM   4182 C C   . GLY B 1 255 ? 37.276  21.046  -0.550  1.00  61.54  ? 255  GLY B C   1 
ATOM   4183 O O   . GLY B 1 255 ? 37.455  21.647  -1.615  1.00  61.52  ? 255  GLY B O   1 
ATOM   4184 N N   . PRO B 1 256 ? 38.274  20.448  0.133   1.00  61.82  ? 256  PRO B N   1 
ATOM   4185 C CA  . PRO B 1 256 ? 39.686  20.634  -0.218  1.00  62.05  ? 256  PRO B CA  1 
ATOM   4186 C C   . PRO B 1 256 ? 40.183  19.686  -1.318  1.00  62.32  ? 256  PRO B C   1 
ATOM   4187 O O   . PRO B 1 256 ? 41.391  19.614  -1.568  1.00  62.45  ? 256  PRO B O   1 
ATOM   4188 C CB  . PRO B 1 256 ? 40.400  20.332  1.101   1.00  61.91  ? 256  PRO B CB  1 
ATOM   4189 C CG  . PRO B 1 256 ? 39.528  19.291  1.757   1.00  61.95  ? 256  PRO B CG  1 
ATOM   4190 C CD  . PRO B 1 256 ? 38.112  19.489  1.245   1.00  61.72  ? 256  PRO B CD  1 
ATOM   4191 N N   . ALA B 1 257 ? 39.259  18.986  -1.973  1.00  62.62  ? 257  ALA B N   1 
ATOM   4192 C CA  . ALA B 1 257 ? 39.600  17.969  -2.967  1.00  62.91  ? 257  ALA B CA  1 
ATOM   4193 C C   . ALA B 1 257 ? 40.499  18.487  -4.096  1.00  63.19  ? 257  ALA B C   1 
ATOM   4194 O O   . ALA B 1 257 ? 41.464  17.823  -4.477  1.00  63.31  ? 257  ALA B O   1 
ATOM   4195 C CB  . ALA B 1 257 ? 38.344  17.330  -3.530  1.00  62.81  ? 257  ALA B CB  1 
ATOM   4196 N N   . ILE B 1 258 ? 40.190  19.669  -4.624  1.00  63.45  ? 258  ILE B N   1 
ATOM   4197 C CA  . ILE B 1 258 ? 40.975  20.247  -5.724  1.00  63.78  ? 258  ILE B CA  1 
ATOM   4198 C C   . ILE B 1 258 ? 42.405  20.561  -5.276  1.00  64.06  ? 258  ILE B C   1 
ATOM   4199 O O   . ILE B 1 258 ? 43.361  20.374  -6.036  1.00  64.17  ? 258  ILE B O   1 
ATOM   4200 C CB  . ILE B 1 258 ? 40.286  21.497  -6.333  1.00  63.80  ? 258  ILE B CB  1 
ATOM   4201 C CG1 . ILE B 1 258 ? 38.839  21.177  -6.759  1.00  63.87  ? 258  ILE B CG1 1 
ATOM   4202 C CG2 . ILE B 1 258 ? 41.106  22.084  -7.493  1.00  63.80  ? 258  ILE B CG2 1 
ATOM   4203 C CD1 . ILE B 1 258 ? 38.665  19.894  -7.600  1.00  64.09  ? 258  ILE B CD1 1 
ATOM   4204 N N   . SER B 1 259 ? 42.535  21.025  -4.035  1.00  64.30  ? 259  SER B N   1 
ATOM   4205 C CA  . SER B 1 259 ? 43.832  21.193  -3.388  1.00  64.54  ? 259  SER B CA  1 
ATOM   4206 C C   . SER B 1 259 ? 44.478  19.836  -3.101  1.00  64.66  ? 259  SER B C   1 
ATOM   4207 O O   . SER B 1 259 ? 45.702  19.703  -3.157  1.00  64.75  ? 259  SER B O   1 
ATOM   4208 C CB  . SER B 1 259 ? 43.680  21.983  -2.084  1.00  64.67  ? 259  SER B CB  1 
ATOM   4209 O OG  . SER B 1 259 ? 43.146  23.279  -2.319  1.00  64.66  ? 259  SER B OG  1 
ATOM   4210 N N   . ARG B 1 260 ? 43.645  18.845  -2.784  1.00  64.81  ? 260  ARG B N   1 
ATOM   4211 C CA  . ARG B 1 260 ? 44.095  17.475  -2.550  1.00  65.05  ? 260  ARG B CA  1 
ATOM   4212 C C   . ARG B 1 260 ? 44.636  16.837  -3.820  1.00  65.04  ? 260  ARG B C   1 
ATOM   4213 O O   . ARG B 1 260 ? 45.674  16.188  -3.787  1.00  65.20  ? 260  ARG B O   1 
ATOM   4214 C CB  . ARG B 1 260 ? 42.953  16.623  -1.989  1.00  65.20  ? 260  ARG B CB  1 
ATOM   4215 C CG  . ARG B 1 260 ? 43.123  16.175  -0.546  1.00  65.84  ? 260  ARG B CG  1 
ATOM   4216 C CD  . ARG B 1 260 ? 42.606  17.188  0.454   1.00  65.88  ? 260  ARG B CD  1 
ATOM   4217 N NE  . ARG B 1 260 ? 41.962  16.520  1.585   1.00  67.45  ? 260  ARG B NE  1 
ATOM   4218 C CZ  . ARG B 1 260 ? 42.607  15.938  2.598   1.00  68.55  ? 260  ARG B CZ  1 
ATOM   4219 N NH1 . ARG B 1 260 ? 43.938  15.927  2.649   1.00  68.39  ? 260  ARG B NH1 1 
ATOM   4220 N NH2 . ARG B 1 260 ? 41.911  15.359  3.572   1.00  69.28  ? 260  ARG B NH2 1 
ATOM   4221 N N   . ILE B 1 261 ? 43.926  17.041  -4.929  1.00  65.16  ? 261  ILE B N   1 
ATOM   4222 C CA  . ILE B 1 261 ? 44.289  16.481  -6.235  1.00  65.28  ? 261  ILE B CA  1 
ATOM   4223 C C   . ILE B 1 261 ? 45.561  17.111  -6.818  1.00  65.43  ? 261  ILE B C   1 
ATOM   4224 O O   . ILE B 1 261 ? 46.469  16.392  -7.238  1.00  65.64  ? 261  ILE B O   1 
ATOM   4225 C CB  . ILE B 1 261 ? 43.106  16.603  -7.245  1.00  65.27  ? 261  ILE B CB  1 
ATOM   4226 C CG1 . ILE B 1 261 ? 41.959  15.669  -6.840  1.00  65.11  ? 261  ILE B CG1 1 
ATOM   4227 C CG2 . ILE B 1 261 ? 43.560  16.291  -8.672  1.00  65.27  ? 261  ILE B CG2 1 
ATOM   4228 C CD1 . ILE B 1 261 ? 40.593  16.120  -7.322  1.00  64.56  ? 261  ILE B CD1 1 
ATOM   4229 N N   . ASN B 1 262 ? 45.614  18.445  -6.835  1.00  65.51  ? 262  ASN B N   1 
ATOM   4230 C CA  . ASN B 1 262 ? 46.715  19.192  -7.464  1.00  65.52  ? 262  ASN B CA  1 
ATOM   4231 C C   . ASN B 1 262 ? 48.082  18.996  -6.814  1.00  65.39  ? 262  ASN B C   1 
ATOM   4232 O O   . ASN B 1 262 ? 49.104  19.092  -7.494  1.00  65.45  ? 262  ASN B O   1 
ATOM   4233 C CB  . ASN B 1 262 ? 46.385  20.692  -7.547  1.00  65.68  ? 262  ASN B CB  1 
ATOM   4234 C CG  . ASN B 1 262 ? 45.393  21.022  -8.661  1.00  65.97  ? 262  ASN B CG  1 
ATOM   4235 O OD1 . ASN B 1 262 ? 45.490  20.510  -9.783  1.00  65.31  ? 262  ASN B OD1 1 
ATOM   4236 N ND2 . ASN B 1 262 ? 44.441  21.900  -8.356  1.00  66.74  ? 262  ASN B ND2 1 
ATOM   4237 N N   . ASN B 1 263 ? 48.096  18.743  -5.506  1.00  65.31  ? 263  ASN B N   1 
ATOM   4238 C CA  . ASN B 1 263 ? 49.341  18.488  -4.783  1.00  65.18  ? 263  ASN B CA  1 
ATOM   4239 C C   . ASN B 1 263 ? 49.643  16.983  -4.697  1.00  65.01  ? 263  ASN B C   1 
ATOM   4240 O O   . ASN B 1 263 ? 50.772  16.574  -4.368  1.00  64.98  ? 263  ASN B O   1 
ATOM   4241 C CB  . ASN B 1 263 ? 49.315  19.145  -3.390  1.00  65.21  ? 263  ASN B CB  1 
ATOM   4242 C CG  . ASN B 1 263 ? 49.241  20.678  -3.453  1.00  65.54  ? 263  ASN B CG  1 
ATOM   4243 O OD1 . ASN B 1 263 ? 48.339  21.289  -2.864  1.00  64.79  ? 263  ASN B OD1 1 
ATOM   4244 N ND2 . ASN B 1 263 ? 50.189  21.300  -4.164  1.00  65.31  ? 263  ASN B ND2 1 
ATOM   4245 N N   . ALA B 1 264 ? 48.634  16.167  -5.016  1.00  64.61  ? 264  ALA B N   1 
ATOM   4246 C CA  . ALA B 1 264 ? 48.774  14.704  -4.995  1.00  64.19  ? 264  ALA B CA  1 
ATOM   4247 C C   . ALA B 1 264 ? 49.575  14.212  -6.193  1.00  63.82  ? 264  ALA B C   1 
ATOM   4248 O O   . ALA B 1 264 ? 49.634  14.890  -7.230  1.00  63.59  ? 264  ALA B O   1 
ATOM   4249 C CB  . ALA B 1 264 ? 47.413  14.025  -4.947  1.00  64.03  ? 264  ALA B CB  1 
ATOM   4250 N N   . CYS B 1 265 ? 50.174  13.030  -6.039  1.00  63.29  ? 265  CYS B N   1 
ATOM   4251 C CA  . CYS B 1 265 ? 51.112  12.488  -7.023  1.00  63.13  ? 265  CYS B CA  1 
ATOM   4252 C C   . CYS B 1 265 ? 50.440  11.621  -8.095  1.00  62.66  ? 265  CYS B C   1 
ATOM   4253 O O   . CYS B 1 265 ? 51.064  10.705  -8.657  1.00  62.86  ? 265  CYS B O   1 
ATOM   4254 C CB  . CYS B 1 265 ? 52.256  11.730  -6.329  1.00  63.27  ? 265  CYS B CB  1 
ATOM   4255 S SG  . CYS B 1 265 ? 51.824  10.822  -4.814  1.00  65.09  ? 265  CYS B SG  1 
ATOM   4256 N N   . PHE B 1 266 ? 49.171  11.918  -8.372  1.00  61.76  ? 266  PHE B N   1 
ATOM   4257 C CA  . PHE B 1 266 ? 48.440  11.275  -9.445  1.00  60.83  ? 266  PHE B CA  1 
ATOM   4258 C C   . PHE B 1 266 ? 49.013  11.718  -10.775 1.00  60.61  ? 266  PHE B C   1 
ATOM   4259 O O   . PHE B 1 266 ? 49.414  12.877  -10.928 1.00  60.69  ? 266  PHE B O   1 
ATOM   4260 C CB  . PHE B 1 266 ? 46.965  11.682  -9.417  1.00  60.88  ? 266  PHE B CB  1 
ATOM   4261 C CG  . PHE B 1 266 ? 46.211  11.196  -8.218  1.00  59.90  ? 266  PHE B CG  1 
ATOM   4262 C CD1 . PHE B 1 266 ? 45.584  12.099  -7.380  1.00  59.22  ? 266  PHE B CD1 1 
ATOM   4263 C CD2 . PHE B 1 266 ? 46.107  9.837   -7.940  1.00  59.84  ? 266  PHE B CD2 1 
ATOM   4264 C CE1 . PHE B 1 266 ? 44.873  11.665  -6.275  1.00  58.98  ? 266  PHE B CE1 1 
ATOM   4265 C CE2 . PHE B 1 266 ? 45.399  9.391   -6.835  1.00  59.25  ? 266  PHE B CE2 1 
ATOM   4266 C CZ  . PHE B 1 266 ? 44.783  10.310  -6.003  1.00  59.46  ? 266  PHE B CZ  1 
ATOM   4267 N N   . GLU B 1 267 ? 49.051  10.799  -11.737 1.00  60.03  ? 267  GLU B N   1 
ATOM   4268 C CA  . GLU B 1 267 ? 49.336  11.173  -13.111 1.00  59.56  ? 267  GLU B CA  1 
ATOM   4269 C C   . GLU B 1 267 ? 48.079  11.838  -13.657 1.00  59.19  ? 267  GLU B C   1 
ATOM   4270 O O   . GLU B 1 267 ? 48.147  12.919  -14.240 1.00  59.54  ? 267  GLU B O   1 
ATOM   4271 C CB  . GLU B 1 267 ? 49.722  9.955   -13.952 1.00  59.61  ? 267  GLU B CB  1 
ATOM   4272 C CG  . GLU B 1 267 ? 50.324  10.295  -15.320 1.00  59.86  ? 267  GLU B CG  1 
ATOM   4273 C CD  . GLU B 1 267 ? 51.830  10.088  -15.392 1.00  60.55  ? 267  GLU B CD  1 
ATOM   4274 O OE1 . GLU B 1 267 ? 52.492  10.003  -14.332 1.00  62.09  ? 267  GLU B OE1 1 
ATOM   4275 O OE2 . GLU B 1 267 ? 52.362  10.003  -16.518 1.00  59.93  ? 267  GLU B OE2 1 
ATOM   4276 N N   . ALA B 1 268 ? 46.931  11.198  -13.434 1.00  58.64  ? 268  ALA B N   1 
ATOM   4277 C CA  . ALA B 1 268 ? 45.642  11.695  -13.912 1.00  58.00  ? 268  ALA B CA  1 
ATOM   4278 C C   . ALA B 1 268 ? 44.497  11.251  -13.009 1.00  57.34  ? 268  ALA B C   1 
ATOM   4279 O O   . ALA B 1 268 ? 44.551  10.173  -12.422 1.00  57.28  ? 268  ALA B O   1 
ATOM   4280 C CB  . ALA B 1 268 ? 45.395  11.229  -15.345 1.00  58.09  ? 268  ALA B CB  1 
ATOM   4281 N N   . VAL B 1 269 ? 43.472  12.094  -12.900 1.00  56.74  ? 269  VAL B N   1 
ATOM   4282 C CA  . VAL B 1 269 ? 42.257  11.761  -12.163 1.00  56.27  ? 269  VAL B CA  1 
ATOM   4283 C C   . VAL B 1 269 ? 41.098  11.732  -13.151 1.00  56.17  ? 269  VAL B C   1 
ATOM   4284 O O   . VAL B 1 269 ? 40.741  12.751  -13.750 1.00  56.32  ? 269  VAL B O   1 
ATOM   4285 C CB  . VAL B 1 269 ? 41.966  12.760  -11.015 1.00  56.38  ? 269  VAL B CB  1 
ATOM   4286 C CG1 . VAL B 1 269 ? 40.655  12.411  -10.325 1.00  56.42  ? 269  VAL B CG1 1 
ATOM   4287 C CG2 . VAL B 1 269 ? 43.098  12.771  -9.995  1.00  55.86  ? 269  VAL B CG2 1 
ATOM   4288 N N   . VAL B 1 270 ? 40.518  10.554  -13.328 1.00  55.71  ? 270  VAL B N   1 
ATOM   4289 C CA  . VAL B 1 270 ? 39.515  10.355  -14.359 1.00  55.19  ? 270  VAL B CA  1 
ATOM   4290 C C   . VAL B 1 270 ? 38.152  10.231  -13.714 1.00  55.01  ? 270  VAL B C   1 
ATOM   4291 O O   . VAL B 1 270 ? 37.964  9.454   -12.772 1.00  54.88  ? 270  VAL B O   1 
ATOM   4292 C CB  . VAL B 1 270 ? 39.825  9.095   -15.216 1.00  55.29  ? 270  VAL B CB  1 
ATOM   4293 C CG1 . VAL B 1 270 ? 38.976  9.063   -16.482 1.00  54.97  ? 270  VAL B CG1 1 
ATOM   4294 C CG2 . VAL B 1 270 ? 41.287  9.068   -15.585 1.00  54.95  ? 270  VAL B CG2 1 
ATOM   4295 N N   . VAL B 1 271 ? 37.212  11.018  -14.219 1.00  54.94  ? 271  VAL B N   1 
ATOM   4296 C CA  . VAL B 1 271 ? 35.824  10.957  -13.781 1.00  54.96  ? 271  VAL B CA  1 
ATOM   4297 C C   . VAL B 1 271 ? 34.847  10.926  -14.956 1.00  55.34  ? 271  VAL B C   1 
ATOM   4298 O O   . VAL B 1 271 ? 35.111  11.495  -16.018 1.00  55.34  ? 271  VAL B O   1 
ATOM   4299 C CB  . VAL B 1 271 ? 35.462  12.139  -12.851 1.00  54.73  ? 271  VAL B CB  1 
ATOM   4300 C CG1 . VAL B 1 271 ? 35.968  11.885  -11.459 1.00  54.83  ? 271  VAL B CG1 1 
ATOM   4301 C CG2 . VAL B 1 271 ? 36.009  13.441  -13.387 1.00  54.39  ? 271  VAL B CG2 1 
ATOM   4302 N N   . THR B 1 272 ? 33.716  10.257  -14.760 1.00  55.70  ? 272  THR B N   1 
ATOM   4303 C CA  . THR B 1 272 ? 32.604  10.387  -15.696 1.00  56.23  ? 272  THR B CA  1 
ATOM   4304 C C   . THR B 1 272 ? 31.890  11.720  -15.456 1.00  56.50  ? 272  THR B C   1 
ATOM   4305 O O   . THR B 1 272 ? 32.123  12.383  -14.438 1.00  56.28  ? 272  THR B O   1 
ATOM   4306 C CB  . THR B 1 272 ? 31.580  9.233   -15.575 1.00  56.04  ? 272  THR B CB  1 
ATOM   4307 O OG1 . THR B 1 272 ? 30.848  9.386   -14.360 1.00  56.29  ? 272  THR B OG1 1 
ATOM   4308 C CG2 . THR B 1 272 ? 32.254  7.865   -15.601 1.00  55.85  ? 272  THR B CG2 1 
ATOM   4309 N N   . ASN B 1 273 ? 31.031  12.109  -16.398 1.00  57.24  ? 273  ASN B N   1 
ATOM   4310 C CA  . ASN B 1 273 ? 30.285  13.359  -16.276 1.00  58.21  ? 273  ASN B CA  1 
ATOM   4311 C C   . ASN B 1 273 ? 28.872  13.184  -15.701 1.00  58.50  ? 273  ASN B C   1 
ATOM   4312 O O   . ASN B 1 273 ? 27.916  13.822  -16.158 1.00  58.59  ? 273  ASN B O   1 
ATOM   4313 C CB  . ASN B 1 273 ? 30.271  14.132  -17.607 1.00  58.47  ? 273  ASN B CB  1 
ATOM   4314 C CG  . ASN B 1 273 ? 29.617  13.355  -18.734 1.00  59.41  ? 273  ASN B CG  1 
ATOM   4315 O OD1 . ASN B 1 273 ? 29.736  12.131  -18.813 1.00  61.01  ? 273  ASN B OD1 1 
ATOM   4316 N ND2 . ASN B 1 273 ? 28.928  14.069  -19.622 1.00  59.88  ? 273  ASN B ND2 1 
ATOM   4317 N N   . THR B 1 274 ? 28.754  12.314  -14.696 1.00  58.84  ? 274  THR B N   1 
ATOM   4318 C CA  . THR B 1 274 ? 27.532  12.192  -13.905 1.00  59.23  ? 274  THR B CA  1 
ATOM   4319 C C   . THR B 1 274 ? 27.366  13.454  -13.062 1.00  59.77  ? 274  THR B C   1 
ATOM   4320 O O   . THR B 1 274 ? 26.243  13.923  -12.823 1.00  59.92  ? 274  THR B O   1 
ATOM   4321 C CB  . THR B 1 274 ? 27.560  10.953  -12.974 1.00  59.35  ? 274  THR B CB  1 
ATOM   4322 O OG1 . THR B 1 274 ? 28.615  11.081  -12.010 1.00  58.85  ? 274  THR B OG1 1 
ATOM   4323 C CG2 . THR B 1 274 ? 27.750  9.665   -13.777 1.00  58.97  ? 274  THR B CG2 1 
ATOM   4324 N N   . ILE B 1 275 ? 28.500  13.974  -12.594 1.00  60.18  ? 275  ILE B N   1 
ATOM   4325 C CA  . ILE B 1 275 ? 28.568  15.279  -11.960 1.00  60.67  ? 275  ILE B CA  1 
ATOM   4326 C C   . ILE B 1 275 ? 29.461  16.130  -12.851 1.00  61.28  ? 275  ILE B C   1 
ATOM   4327 O O   . ILE B 1 275 ? 30.593  15.729  -13.151 1.00  61.53  ? 275  ILE B O   1 
ATOM   4328 C CB  . ILE B 1 275 ? 29.152  15.199  -10.524 1.00  60.72  ? 275  ILE B CB  1 
ATOM   4329 C CG1 . ILE B 1 275 ? 28.252  14.342  -9.625  1.00  60.17  ? 275  ILE B CG1 1 
ATOM   4330 C CG2 . ILE B 1 275 ? 29.345  16.608  -9.932  1.00  60.93  ? 275  ILE B CG2 1 
ATOM   4331 C CD1 . ILE B 1 275 ? 28.942  13.787  -8.413  1.00  59.36  ? 275  ILE B CD1 1 
ATOM   4332 N N   . PRO B 1 276 ? 28.948  17.291  -13.303 1.00  61.76  ? 276  PRO B N   1 
ATOM   4333 C CA  . PRO B 1 276 ? 29.676  18.203  -14.187 1.00  62.04  ? 276  PRO B CA  1 
ATOM   4334 C C   . PRO B 1 276 ? 31.073  18.561  -13.666 1.00  62.41  ? 276  PRO B C   1 
ATOM   4335 O O   . PRO B 1 276 ? 31.270  18.709  -12.455 1.00  62.13  ? 276  PRO B O   1 
ATOM   4336 C CB  . PRO B 1 276 ? 28.771  19.449  -14.243 1.00  61.97  ? 276  PRO B CB  1 
ATOM   4337 C CG  . PRO B 1 276 ? 27.738  19.260  -13.187 1.00  61.81  ? 276  PRO B CG  1 
ATOM   4338 C CD  . PRO B 1 276 ? 27.585  17.780  -13.042 1.00  61.99  ? 276  PRO B CD  1 
ATOM   4339 N N   . GLN B 1 277 ? 32.026  18.688  -14.591 1.00  62.96  ? 277  GLN B N   1 
ATOM   4340 C CA  . GLN B 1 277 ? 33.436  18.895  -14.243 1.00  63.53  ? 277  GLN B CA  1 
ATOM   4341 C C   . GLN B 1 277 ? 34.050  20.105  -14.952 1.00  64.08  ? 277  GLN B C   1 
ATOM   4342 O O   . GLN B 1 277 ? 35.259  20.350  -14.838 1.00  64.20  ? 277  GLN B O   1 
ATOM   4343 C CB  . GLN B 1 277 ? 34.262  17.638  -14.564 1.00  63.32  ? 277  GLN B CB  1 
ATOM   4344 C CG  . GLN B 1 277 ? 33.785  16.339  -13.909 1.00  63.08  ? 277  GLN B CG  1 
ATOM   4345 C CD  . GLN B 1 277 ? 34.092  16.240  -12.408 1.00  63.51  ? 277  GLN B CD  1 
ATOM   4346 O OE1 . GLN B 1 277 ? 33.602  15.333  -11.733 1.00  63.28  ? 277  GLN B OE1 1 
ATOM   4347 N NE2 . GLN B 1 277 ? 34.905  17.162  -11.888 1.00  63.33  ? 277  GLN B NE2 1 
ATOM   4348 N N   . GLU B 1 278 ? 33.208  20.859  -15.663 0.78  64.68  ? 278  GLU B N   1 
ATOM   4349 C CA  . GLU B 1 278 ? 33.650  21.957  -16.537 0.78  65.15  ? 278  GLU B CA  1 
ATOM   4350 C C   . GLU B 1 278 ? 34.444  23.012  -15.776 0.78  65.55  ? 278  GLU B C   1 
ATOM   4351 O O   . GLU B 1 278 ? 35.532  23.403  -16.203 0.78  65.68  ? 278  GLU B O   1 
ATOM   4352 C CB  . GLU B 1 278 ? 32.461  22.600  -17.271 0.78  65.10  ? 278  GLU B CB  1 
ATOM   4353 C CG  . GLU B 1 278 ? 31.570  21.626  -18.055 0.78  64.93  ? 278  GLU B CG  1 
ATOM   4354 C CD  . GLU B 1 278 ? 30.569  20.884  -17.169 0.78  64.63  ? 278  GLU B CD  1 
ATOM   4355 O OE1 . GLU B 1 278 ? 29.614  21.519  -16.674 0.78  64.57  ? 278  GLU B OE1 1 
ATOM   4356 O OE2 . GLU B 1 278 ? 30.740  19.662  -16.974 0.78  64.54  ? 278  GLU B OE2 1 
ATOM   4357 N N   . ASP B 1 279 ? 33.893  23.464  -14.652 1.00  66.08  ? 279  ASP B N   1 
ATOM   4358 C CA  . ASP B 1 279 ? 34.563  24.438  -13.789 1.00  66.74  ? 279  ASP B CA  1 
ATOM   4359 C C   . ASP B 1 279 ? 35.791  23.825  -13.100 1.00  67.11  ? 279  ASP B C   1 
ATOM   4360 O O   . ASP B 1 279 ? 36.857  24.448  -13.046 1.00  67.20  ? 279  ASP B O   1 
ATOM   4361 C CB  . ASP B 1 279 ? 33.574  24.999  -12.757 1.00  66.78  ? 279  ASP B CB  1 
ATOM   4362 C CG  . ASP B 1 279 ? 34.146  26.161  -11.948 1.00  66.96  ? 279  ASP B CG  1 
ATOM   4363 O OD1 . ASP B 1 279 ? 33.632  26.401  -10.830 1.00  67.76  ? 279  ASP B OD1 1 
ATOM   4364 O OD2 . ASP B 1 279 ? 35.093  26.834  -12.412 1.00  66.83  ? 279  ASP B OD2 1 
ATOM   4365 N N   . LYS B 1 280 ? 35.632  22.596  -12.605 1.00  67.34  ? 280  LYS B N   1 
ATOM   4366 C CA  . LYS B 1 280 ? 36.677  21.886  -11.864 1.00  67.59  ? 280  LYS B CA  1 
ATOM   4367 C C   . LYS B 1 280 ? 37.917  21.531  -12.703 1.00  67.84  ? 280  LYS B C   1 
ATOM   4368 O O   . LYS B 1 280 ? 38.959  21.153  -12.148 1.00  68.03  ? 280  LYS B O   1 
ATOM   4369 C CB  . LYS B 1 280 ? 36.097  20.625  -11.207 1.00  67.71  ? 280  LYS B CB  1 
ATOM   4370 C CG  . LYS B 1 280 ? 34.949  20.892  -10.223 1.00  67.79  ? 280  LYS B CG  1 
ATOM   4371 C CD  . LYS B 1 280 ? 35.460  21.198  -8.816  1.00  68.13  ? 280  LYS B CD  1 
ATOM   4372 C CE  . LYS B 1 280 ? 34.550  22.170  -8.063  1.00  68.19  ? 280  LYS B CE  1 
ATOM   4373 N NZ  . LYS B 1 280 ? 33.190  21.627  -7.776  1.00  67.73  ? 280  LYS B NZ  1 
ATOM   4374 N N   . MET B 1 281 ? 37.806  21.649  -14.027 1.00  67.85  ? 281  MET B N   1 
ATOM   4375 C CA  . MET B 1 281 ? 38.946  21.427  -14.915 1.00  68.06  ? 281  MET B CA  1 
ATOM   4376 C C   . MET B 1 281 ? 39.688  22.727  -15.238 1.00  68.11  ? 281  MET B C   1 
ATOM   4377 O O   . MET B 1 281 ? 40.848  22.704  -15.669 1.00  68.38  ? 281  MET B O   1 
ATOM   4378 C CB  . MET B 1 281 ? 38.511  20.705  -16.194 1.00  68.35  ? 281  MET B CB  1 
ATOM   4379 C CG  . MET B 1 281 ? 38.208  19.217  -15.990 1.00  68.77  ? 281  MET B CG  1 
ATOM   4380 S SD  . MET B 1 281 ? 37.172  18.494  -17.278 1.00  69.93  ? 281  MET B SD  1 
ATOM   4381 C CE  . MET B 1 281 ? 38.359  18.262  -18.611 1.00  69.92  ? 281  MET B CE  1 
ATOM   4382 N N   . LYS B 1 282 ? 39.019  23.857  -15.024 1.00  67.96  ? 282  LYS B N   1 
ATOM   4383 C CA  . LYS B 1 282 ? 39.672  25.165  -15.103 1.00  67.79  ? 282  LYS B CA  1 
ATOM   4384 C C   . LYS B 1 282 ? 40.697  25.281  -13.976 1.00  67.56  ? 282  LYS B C   1 
ATOM   4385 O O   . LYS B 1 282 ? 41.792  25.812  -14.172 1.00  67.78  ? 282  LYS B O   1 
ATOM   4386 C CB  . LYS B 1 282 ? 38.654  26.308  -14.972 1.00  67.91  ? 282  LYS B CB  1 
ATOM   4387 C CG  . LYS B 1 282 ? 37.482  26.281  -15.955 1.00  67.97  ? 282  LYS B CG  1 
ATOM   4388 C CD  . LYS B 1 282 ? 36.430  27.310  -15.553 1.00  68.06  ? 282  LYS B CD  1 
ATOM   4389 C CE  . LYS B 1 282 ? 35.074  27.009  -16.171 1.00  67.88  ? 282  LYS B CE  1 
ATOM   4390 N NZ  . LYS B 1 282 ? 33.963  27.516  -15.306 1.00  67.77  ? 282  LYS B NZ  1 
ATOM   4391 N N   . HIS B 1 283 ? 40.323  24.776  -12.800 1.00  67.18  ? 283  HIS B N   1 
ATOM   4392 C CA  . HIS B 1 283 ? 41.157  24.847  -11.594 1.00  66.90  ? 283  HIS B CA  1 
ATOM   4393 C C   . HIS B 1 283 ? 42.048  23.611  -11.391 1.00  66.47  ? 283  HIS B C   1 
ATOM   4394 O O   . HIS B 1 283 ? 42.931  23.608  -10.519 1.00  66.40  ? 283  HIS B O   1 
ATOM   4395 C CB  . HIS B 1 283 ? 40.276  25.051  -10.351 1.00  67.08  ? 283  HIS B CB  1 
ATOM   4396 C CG  . HIS B 1 283 ? 39.466  26.309  -10.379 1.00  67.75  ? 283  HIS B CG  1 
ATOM   4397 N ND1 . HIS B 1 283 ? 39.931  27.506  -9.875  1.00  68.09  ? 283  HIS B ND1 1 
ATOM   4398 C CD2 . HIS B 1 283 ? 38.218  26.556  -10.845 1.00  68.74  ? 283  HIS B CD2 1 
ATOM   4399 C CE1 . HIS B 1 283 ? 39.007  28.438  -10.037 1.00  68.70  ? 283  HIS B CE1 1 
ATOM   4400 N NE2 . HIS B 1 283 ? 37.958  27.888  -10.622 1.00  69.31  ? 283  HIS B NE2 1 
ATOM   4401 N N   . CYS B 1 284 ? 41.803  22.560  -12.178 1.00  65.81  ? 284  CYS B N   1 
ATOM   4402 C CA  . CYS B 1 284 ? 42.577  21.320  -12.066 1.00  65.12  ? 284  CYS B CA  1 
ATOM   4403 C C   . CYS B 1 284 ? 42.811  20.640  -13.419 1.00  64.31  ? 284  CYS B C   1 
ATOM   4404 O O   . CYS B 1 284 ? 41.886  20.079  -14.020 1.00  64.42  ? 284  CYS B O   1 
ATOM   4405 C CB  . CYS B 1 284 ? 41.919  20.353  -11.077 1.00  65.17  ? 284  CYS B CB  1 
ATOM   4406 S SG  . CYS B 1 284 ? 42.890  18.861  -10.750 1.00  66.86  ? 284  CYS B SG  1 
ATOM   4407 N N   . SER B 1 285 ? 44.059  20.693  -13.880 1.00  63.17  ? 285  SER B N   1 
ATOM   4408 C CA  . SER B 1 285 ? 44.448  20.131  -15.173 1.00  62.11  ? 285  SER B CA  1 
ATOM   4409 C C   . SER B 1 285 ? 44.345  18.608  -15.207 1.00  61.10  ? 285  SER B C   1 
ATOM   4410 O O   . SER B 1 285 ? 43.959  18.029  -16.231 1.00  61.09  ? 285  SER B O   1 
ATOM   4411 C CB  . SER B 1 285 ? 45.876  20.554  -15.532 1.00  62.33  ? 285  SER B CB  1 
ATOM   4412 O OG  . SER B 1 285 ? 46.807  20.038  -14.596 1.00  62.35  ? 285  SER B OG  1 
ATOM   4413 N N   . LYS B 1 286 ? 44.683  17.977  -14.080 1.00  59.62  ? 286  LYS B N   1 
ATOM   4414 C CA  . LYS B 1 286 ? 44.717  16.515  -13.943 1.00  58.30  ? 286  LYS B CA  1 
ATOM   4415 C C   . LYS B 1 286 ? 43.395  15.808  -14.298 1.00  57.33  ? 286  LYS B C   1 
ATOM   4416 O O   . LYS B 1 286 ? 43.390  14.629  -14.687 1.00  57.17  ? 286  LYS B O   1 
ATOM   4417 C CB  . LYS B 1 286 ? 45.125  16.129  -12.516 1.00  58.31  ? 286  LYS B CB  1 
ATOM   4418 C CG  . LYS B 1 286 ? 46.415  16.760  -12.012 1.00  58.52  ? 286  LYS B CG  1 
ATOM   4419 C CD  . LYS B 1 286 ? 47.640  15.938  -12.374 1.00  58.88  ? 286  LYS B CD  1 
ATOM   4420 C CE  . LYS B 1 286 ? 48.799  16.262  -11.442 1.00  59.45  ? 286  LYS B CE  1 
ATOM   4421 N NZ  . LYS B 1 286 ? 48.492  15.889  -10.023 1.00  59.70  ? 286  LYS B NZ  1 
ATOM   4422 N N   . ILE B 1 287 ? 42.285  16.535  -14.176 1.00  56.01  ? 287  ILE B N   1 
ATOM   4423 C CA  . ILE B 1 287 ? 40.965  15.951  -14.343 1.00  54.84  ? 287  ILE B CA  1 
ATOM   4424 C C   . ILE B 1 287 ? 40.567  15.753  -15.819 1.00  54.16  ? 287  ILE B C   1 
ATOM   4425 O O   . ILE B 1 287 ? 40.519  16.698  -16.612 1.00  54.04  ? 287  ILE B O   1 
ATOM   4426 C CB  . ILE B 1 287 ? 39.890  16.726  -13.526 1.00  54.88  ? 287  ILE B CB  1 
ATOM   4427 C CG1 . ILE B 1 287 ? 40.221  16.648  -12.019 1.00  54.87  ? 287  ILE B CG1 1 
ATOM   4428 C CG2 . ILE B 1 287 ? 38.485  16.180  -13.821 1.00  54.53  ? 287  ILE B CG2 1 
ATOM   4429 C CD1 . ILE B 1 287 ? 39.363  17.532  -11.096 1.00  53.07  ? 287  ILE B CD1 1 
ATOM   4430 N N   . GLN B 1 288 ? 40.303  14.498  -16.166 1.00  53.08  ? 288  GLN B N   1 
ATOM   4431 C CA  . GLN B 1 288 ? 39.821  14.127  -17.481 1.00  51.98  ? 288  GLN B CA  1 
ATOM   4432 C C   . GLN B 1 288 ? 38.423  13.533  -17.350 1.00  51.48  ? 288  GLN B C   1 
ATOM   4433 O O   . GLN B 1 288 ? 38.098  12.908  -16.336 1.00  51.28  ? 288  GLN B O   1 
ATOM   4434 C CB  . GLN B 1 288 ? 40.769  13.122  -18.116 1.00  51.96  ? 288  GLN B CB  1 
ATOM   4435 C CG  . GLN B 1 288 ? 42.175  13.660  -18.279 1.00  51.54  ? 288  GLN B CG  1 
ATOM   4436 C CD  . GLN B 1 288 ? 42.978  12.866  -19.261 1.00  51.24  ? 288  GLN B CD  1 
ATOM   4437 O OE1 . GLN B 1 288 ? 43.991  12.273  -18.905 1.00  52.02  ? 288  GLN B OE1 1 
ATOM   4438 N NE2 . GLN B 1 288 ? 42.530  12.845  -20.514 1.00  52.28  ? 288  GLN B NE2 1 
ATOM   4439 N N   . VAL B 1 289 ? 37.595  13.736  -18.370 1.00  50.67  ? 289  VAL B N   1 
ATOM   4440 C CA  . VAL B 1 289 ? 36.192  13.331  -18.294 1.00  49.73  ? 289  VAL B CA  1 
ATOM   4441 C C   . VAL B 1 289 ? 35.832  12.226  -19.277 1.00  49.12  ? 289  VAL B C   1 
ATOM   4442 O O   . VAL B 1 289 ? 36.059  12.348  -20.477 1.00  49.53  ? 289  VAL B O   1 
ATOM   4443 C CB  . VAL B 1 289 ? 35.237  14.538  -18.479 1.00  49.79  ? 289  VAL B CB  1 
ATOM   4444 C CG1 . VAL B 1 289 ? 33.799  14.078  -18.619 1.00  49.83  ? 289  VAL B CG1 1 
ATOM   4445 C CG2 . VAL B 1 289 ? 35.349  15.486  -17.304 1.00  49.47  ? 289  VAL B CG2 1 
ATOM   4446 N N   . ILE B 1 290 ? 35.275  11.140  -18.758 1.00  48.19  ? 290  ILE B N   1 
ATOM   4447 C CA  . ILE B 1 290 ? 34.628  10.160  -19.613 1.00  47.06  ? 290  ILE B CA  1 
ATOM   4448 C C   . ILE B 1 290 ? 33.196  10.621  -19.825 1.00  46.30  ? 290  ILE B C   1 
ATOM   4449 O O   . ILE B 1 290 ? 32.500  10.921  -18.865 1.00  45.86  ? 290  ILE B O   1 
ATOM   4450 C CB  . ILE B 1 290 ? 34.663  8.742   -19.013 1.00  47.12  ? 290  ILE B CB  1 
ATOM   4451 C CG1 . ILE B 1 290 ? 36.121  8.267   -18.871 1.00  46.53  ? 290  ILE B CG1 1 
ATOM   4452 C CG2 . ILE B 1 290 ? 33.847  7.770   -19.889 1.00  46.75  ? 290  ILE B CG2 1 
ATOM   4453 C CD1 . ILE B 1 290 ? 36.291  7.060   -17.993 1.00  47.47  ? 290  ILE B CD1 1 
ATOM   4454 N N   . ASP B 1 291 ? 32.774  10.701  -21.086 1.00  45.70  ? 291  ASP B N   1 
ATOM   4455 C CA  . ASP B 1 291 ? 31.403  11.064  -21.417 1.00  44.96  ? 291  ASP B CA  1 
ATOM   4456 C C   . ASP B 1 291 ? 30.488  9.854   -21.250 1.00  44.26  ? 291  ASP B C   1 
ATOM   4457 O O   . ASP B 1 291 ? 30.632  8.872   -21.968 1.00  44.12  ? 291  ASP B O   1 
ATOM   4458 C CB  . ASP B 1 291 ? 31.324  11.591  -22.852 1.00  45.14  ? 291  ASP B CB  1 
ATOM   4459 C CG  . ASP B 1 291 ? 30.009  12.305  -23.147 1.00  46.00  ? 291  ASP B CG  1 
ATOM   4460 O OD1 . ASP B 1 291 ? 29.167  12.458  -22.221 1.00  47.57  ? 291  ASP B OD1 1 
ATOM   4461 O OD2 . ASP B 1 291 ? 29.817  12.725  -24.311 1.00  45.52  ? 291  ASP B OD2 1 
ATOM   4462 N N   . ILE B 1 292 ? 29.557  9.921   -20.302 1.00  43.29  ? 292  ILE B N   1 
ATOM   4463 C CA  . ILE B 1 292 ? 28.612  8.818   -20.104 1.00  42.93  ? 292  ILE B CA  1 
ATOM   4464 C C   . ILE B 1 292 ? 27.257  9.013   -20.776 1.00  42.37  ? 292  ILE B C   1 
ATOM   4465 O O   . ILE B 1 292 ? 26.453  8.084   -20.823 1.00  42.36  ? 292  ILE B O   1 
ATOM   4466 C CB  . ILE B 1 292 ? 28.402  8.428   -18.605 1.00  42.98  ? 292  ILE B CB  1 
ATOM   4467 C CG1 . ILE B 1 292 ? 28.394  9.655   -17.683 1.00  43.11  ? 292  ILE B CG1 1 
ATOM   4468 C CG2 . ILE B 1 292 ? 29.454  7.424   -18.176 1.00  42.76  ? 292  ILE B CG2 1 
ATOM   4469 C CD1 . ILE B 1 292 ? 27.063  10.362  -17.565 1.00  42.50  ? 292  ILE B CD1 1 
ATOM   4470 N N   . SER B 1 293 ? 27.029  10.215  -21.301 1.00  41.96  ? 293  SER B N   1 
ATOM   4471 C CA  . SER B 1 293 ? 25.762  10.603  -21.935 1.00  41.34  ? 293  SER B CA  1 
ATOM   4472 C C   . SER B 1 293 ? 25.207  9.604   -22.958 1.00  41.32  ? 293  SER B C   1 
ATOM   4473 O O   . SER B 1 293 ? 24.004  9.419   -23.029 1.00  41.40  ? 293  SER B O   1 
ATOM   4474 C CB  . SER B 1 293 ? 25.866  12.009  -22.552 1.00  41.31  ? 293  SER B CB  1 
ATOM   4475 O OG  . SER B 1 293 ? 26.989  12.130  -23.406 1.00  39.39  ? 293  SER B OG  1 
ATOM   4476 N N   . MET B 1 294 ? 26.075  8.968   -23.736 1.00  41.42  ? 294  MET B N   1 
ATOM   4477 C CA  . MET B 1 294 ? 25.639  7.982   -24.733 1.00  41.80  ? 294  MET B CA  1 
ATOM   4478 C C   . MET B 1 294 ? 25.131  6.699   -24.103 1.00  41.47  ? 294  MET B C   1 
ATOM   4479 O O   . MET B 1 294 ? 24.193  6.082   -24.608 1.00  40.95  ? 294  MET B O   1 
ATOM   4480 C CB  . MET B 1 294 ? 26.748  7.664   -25.750 1.00  42.25  ? 294  MET B CB  1 
ATOM   4481 C CG  . MET B 1 294 ? 28.183  8.040   -25.330 1.00  44.18  ? 294  MET B CG  1 
ATOM   4482 S SD  . MET B 1 294 ? 28.726  7.380   -23.723 1.00  47.64  ? 294  MET B SD  1 
ATOM   4483 C CE  . MET B 1 294 ? 30.398  6.845   -24.160 1.00  46.99  ? 294  MET B CE  1 
ATOM   4484 N N   . ILE B 1 295 ? 25.765  6.290   -23.005 1.00  41.52  ? 295  ILE B N   1 
ATOM   4485 C CA  . ILE B 1 295 ? 25.324  5.110   -22.264 1.00  41.39  ? 295  ILE B CA  1 
ATOM   4486 C C   . ILE B 1 295 ? 23.940  5.368   -21.663 1.00  41.38  ? 295  ILE B C   1 
ATOM   4487 O O   . ILE B 1 295 ? 23.058  4.502   -21.705 1.00  41.46  ? 295  ILE B O   1 
ATOM   4488 C CB  . ILE B 1 295 ? 26.328  4.694   -21.167 1.00  41.35  ? 295  ILE B CB  1 
ATOM   4489 C CG1 . ILE B 1 295 ? 27.730  4.524   -21.768 1.00  41.50  ? 295  ILE B CG1 1 
ATOM   4490 C CG2 . ILE B 1 295 ? 25.874  3.387   -20.504 1.00  41.02  ? 295  ILE B CG2 1 
ATOM   4491 C CD1 . ILE B 1 295 ? 28.876  4.675   -20.770 1.00  41.45  ? 295  ILE B CD1 1 
ATOM   4492 N N   . LEU B 1 296 ? 23.746  6.572   -21.139 1.00  40.91  ? 296  LEU B N   1 
ATOM   4493 C CA  . LEU B 1 296 ? 22.454  6.948   -20.607 1.00  40.84  ? 296  LEU B CA  1 
ATOM   4494 C C   . LEU B 1 296 ? 21.400  7.111   -21.699 1.00  40.93  ? 296  LEU B C   1 
ATOM   4495 O O   . LEU B 1 296 ? 20.256  6.696   -21.524 1.00  40.71  ? 296  LEU B O   1 
ATOM   4496 C CB  . LEU B 1 296 ? 22.572  8.210   -19.755 1.00  40.88  ? 296  LEU B CB  1 
ATOM   4497 C CG  . LEU B 1 296 ? 23.250  8.064   -18.390 1.00  39.48  ? 296  LEU B CG  1 
ATOM   4498 C CD1 . LEU B 1 296 ? 23.468  9.430   -17.831 1.00  39.63  ? 296  LEU B CD1 1 
ATOM   4499 C CD2 . LEU B 1 296 ? 22.402  7.244   -17.438 1.00  39.17  ? 296  LEU B CD2 1 
ATOM   4500 N N   . ALA B 1 297 ? 21.803  7.705   -22.823 1.00  41.37  ? 297  ALA B N   1 
ATOM   4501 C CA  . ALA B 1 297 ? 20.927  7.884   -23.990 1.00  41.47  ? 297  ALA B CA  1 
ATOM   4502 C C   . ALA B 1 297 ? 20.503  6.545   -24.570 1.00  41.73  ? 297  ALA B C   1 
ATOM   4503 O O   . ALA B 1 297 ? 19.337  6.335   -24.893 1.00  41.73  ? 297  ALA B O   1 
ATOM   4504 C CB  . ALA B 1 297 ? 21.616  8.723   -25.046 1.00  41.09  ? 297  ALA B CB  1 
ATOM   4505 N N   . GLU B 1 298 ? 21.464  5.638   -24.683 0.94  42.42  ? 298  GLU B N   1 
ATOM   4506 C CA  . GLU B 1 298 ? 21.220  4.277   -25.141 0.94  42.97  ? 298  GLU B CA  1 
ATOM   4507 C C   . GLU B 1 298 ? 20.296  3.541   -24.182 0.94  42.72  ? 298  GLU B C   1 
ATOM   4508 O O   . GLU B 1 298 ? 19.414  2.808   -24.611 0.94  42.55  ? 298  GLU B O   1 
ATOM   4509 C CB  . GLU B 1 298 ? 22.543  3.520   -25.269 0.94  43.33  ? 298  GLU B CB  1 
ATOM   4510 C CG  . GLU B 1 298 ? 22.422  2.170   -25.959 0.94  45.75  ? 298  GLU B CG  1 
ATOM   4511 C CD  . GLU B 1 298 ? 22.451  2.271   -27.476 0.94  48.63  ? 298  GLU B CD  1 
ATOM   4512 O OE1 . GLU B 1 298 ? 22.799  3.354   -28.003 0.94  49.78  ? 298  GLU B OE1 1 
ATOM   4513 O OE2 . GLU B 1 298 ? 22.144  1.255   -28.142 0.94  49.96  ? 298  GLU B OE2 1 
ATOM   4514 N N   . ALA B 1 299 ? 20.498  3.750   -22.881 1.00  42.72  ? 299  ALA B N   1 
ATOM   4515 C CA  . ALA B 1 299 ? 19.627  3.160   -21.864 1.00  42.71  ? 299  ALA B CA  1 
ATOM   4516 C C   . ALA B 1 299 ? 18.176  3.660   -21.923 1.00  42.51  ? 299  ALA B C   1 
ATOM   4517 O O   . ALA B 1 299 ? 17.249  2.878   -21.756 1.00  42.72  ? 299  ALA B O   1 
ATOM   4518 C CB  . ALA B 1 299 ? 20.220  3.338   -20.465 1.00  42.72  ? 299  ALA B CB  1 
ATOM   4519 N N   . ILE B 1 300 ? 17.979  4.947   -22.173 1.00  42.73  ? 300  ILE B N   1 
ATOM   4520 C CA  . ILE B 1 300 ? 16.623  5.509   -22.322 1.00  43.36  ? 300  ILE B CA  1 
ATOM   4521 C C   . ILE B 1 300 ? 15.918  5.007   -23.594 1.00  44.09  ? 300  ILE B C   1 
ATOM   4522 O O   . ILE B 1 300 ? 14.768  4.556   -23.546 1.00  43.86  ? 300  ILE B O   1 
ATOM   4523 C CB  . ILE B 1 300 ? 16.617  7.062   -22.263 1.00  42.96  ? 300  ILE B CB  1 
ATOM   4524 C CG1 . ILE B 1 300 ? 16.858  7.537   -20.830 1.00  42.49  ? 300  ILE B CG1 1 
ATOM   4525 C CG2 . ILE B 1 300 ? 15.298  7.618   -22.776 1.00  42.44  ? 300  ILE B CG2 1 
ATOM   4526 C CD1 . ILE B 1 300 ? 17.454  8.930   -20.731 1.00  41.07  ? 300  ILE B CD1 1 
ATOM   4527 N N   . ARG B 1 301 ? 16.623  5.084   -24.720 1.00  45.28  ? 301  ARG B N   1 
ATOM   4528 C CA  . ARG B 1 301 ? 16.153  4.563   -26.004 1.00  46.63  ? 301  ARG B CA  1 
ATOM   4529 C C   . ARG B 1 301 ? 15.670  3.117   -25.885 1.00  47.22  ? 301  ARG B C   1 
ATOM   4530 O O   . ARG B 1 301 ? 14.547  2.791   -26.292 1.00  47.37  ? 301  ARG B O   1 
ATOM   4531 C CB  . ARG B 1 301 ? 17.282  4.650   -27.043 1.00  46.93  ? 301  ARG B CB  1 
ATOM   4532 C CG  . ARG B 1 301 ? 16.882  4.269   -28.472 1.00  48.28  ? 301  ARG B CG  1 
ATOM   4533 C CD  . ARG B 1 301 ? 18.058  4.429   -29.434 1.00  49.18  ? 301  ARG B CD  1 
ATOM   4534 N NE  . ARG B 1 301 ? 18.116  3.342   -30.417 1.00  50.73  ? 301  ARG B NE  1 
ATOM   4535 C CZ  . ARG B 1 301 ? 18.688  2.161   -30.196 1.00  51.28  ? 301  ARG B CZ  1 
ATOM   4536 N NH1 . ARG B 1 301 ? 19.261  1.904   -29.028 1.00  52.58  ? 301  ARG B NH1 1 
ATOM   4537 N NH2 . ARG B 1 301 ? 18.697  1.239   -31.144 1.00  52.01  ? 301  ARG B NH2 1 
ATOM   4538 N N   . ARG B 1 302 ? 16.527  2.263   -25.322 1.00  48.06  ? 302  ARG B N   1 
ATOM   4539 C CA  . ARG B 1 302 ? 16.220  0.841   -25.112 1.00  48.75  ? 302  ARG B CA  1 
ATOM   4540 C C   . ARG B 1 302 ? 15.020  0.626   -24.196 1.00  48.69  ? 302  ARG B C   1 
ATOM   4541 O O   . ARG B 1 302 ? 14.153  -0.185  -24.494 1.00  48.75  ? 302  ARG B O   1 
ATOM   4542 C CB  . ARG B 1 302 ? 17.445  0.098   -24.566 1.00  49.06  ? 302  ARG B CB  1 
ATOM   4543 C CG  . ARG B 1 302 ? 18.696  0.165   -25.455 1.00  50.46  ? 302  ARG B CG  1 
ATOM   4544 C CD  . ARG B 1 302 ? 18.608  -0.814  -26.591 1.00  54.23  ? 302  ARG B CD  1 
ATOM   4545 N NE  . ARG B 1 302 ? 19.759  -0.757  -27.498 1.00  56.70  ? 302  ARG B NE  1 
ATOM   4546 C CZ  . ARG B 1 302 ? 20.785  -1.606  -27.482 1.00  57.29  ? 302  ARG B CZ  1 
ATOM   4547 N NH1 . ARG B 1 302 ? 20.844  -2.589  -26.586 1.00  56.93  ? 302  ARG B NH1 1 
ATOM   4548 N NH2 . ARG B 1 302 ? 21.760  -1.460  -28.367 1.00  57.84  ? 302  ARG B NH2 1 
ATOM   4549 N N   . THR B 1 303 ? 14.968  1.365   -23.090 1.00  49.23  ? 303  THR B N   1 
ATOM   4550 C CA  . THR B 1 303 ? 13.830  1.300   -22.157 1.00  49.75  ? 303  THR B CA  1 
ATOM   4551 C C   . THR B 1 303 ? 12.512  1.649   -22.847 1.00  49.91  ? 303  THR B C   1 
ATOM   4552 O O   . THR B 1 303 ? 11.475  1.074   -22.535 1.00  49.77  ? 303  THR B O   1 
ATOM   4553 C CB  . THR B 1 303 ? 14.044  2.227   -20.938 1.00  49.66  ? 303  THR B CB  1 
ATOM   4554 O OG1 . THR B 1 303 ? 15.272  1.876   -20.293 1.00  50.31  ? 303  THR B OG1 1 
ATOM   4555 C CG2 . THR B 1 303 ? 12.907  2.105   -19.938 1.00  49.30  ? 303  THR B CG2 1 
ATOM   4556 N N   . HIS B 1 304 ? 12.569  2.588   -23.786 1.00  50.55  ? 304  HIS B N   1 
ATOM   4557 C CA  . HIS B 1 304 ? 11.397  2.996   -24.549 1.00  51.21  ? 304  HIS B CA  1 
ATOM   4558 C C   . HIS B 1 304 ? 10.956  1.937   -25.571 1.00  51.60  ? 304  HIS B C   1 
ATOM   4559 O O   . HIS B 1 304 ? 9.766   1.647   -25.686 1.00  51.45  ? 304  HIS B O   1 
ATOM   4560 C CB  . HIS B 1 304 ? 11.656  4.338   -25.230 1.00  51.16  ? 304  HIS B CB  1 
ATOM   4561 C CG  . HIS B 1 304 ? 10.470  4.881   -25.964 1.00  51.69  ? 304  HIS B CG  1 
ATOM   4562 N ND1 . HIS B 1 304 ? 9.341   5.337   -25.320 1.00  51.06  ? 304  HIS B ND1 1 
ATOM   4563 C CD2 . HIS B 1 304 ? 10.239  5.041   -27.289 1.00  51.61  ? 304  HIS B CD2 1 
ATOM   4564 C CE1 . HIS B 1 304 ? 8.466   5.755   -26.218 1.00  51.11  ? 304  HIS B CE1 1 
ATOM   4565 N NE2 . HIS B 1 304 ? 8.989   5.591   -27.419 1.00  50.82  ? 304  HIS B NE2 1 
ATOM   4566 N N   . ASN B 1 305 ? 11.916  1.354   -26.284 1.00  52.27  ? 305  ASN B N   1 
ATOM   4567 C CA  . ASN B 1 305 ? 11.635  0.369   -27.337 1.00  53.20  ? 305  ASN B CA  1 
ATOM   4568 C C   . ASN B 1 305 ? 11.527  -1.068  -26.821 1.00  53.62  ? 305  ASN B C   1 
ATOM   4569 O O   . ASN B 1 305 ? 11.200  -1.991  -27.582 1.00  53.85  ? 305  ASN B O   1 
ATOM   4570 C CB  . ASN B 1 305 ? 12.700  0.436   -28.447 1.00  53.15  ? 305  ASN B CB  1 
ATOM   4571 C CG  . ASN B 1 305 ? 12.795  1.805   -29.091 1.00  53.70  ? 305  ASN B CG  1 
ATOM   4572 O OD1 . ASN B 1 305 ? 11.779  2.434   -29.405 1.00  53.82  ? 305  ASN B OD1 1 
ATOM   4573 N ND2 . ASN B 1 305 ? 14.030  2.274   -29.296 1.00  55.01  ? 305  ASN B ND2 1 
ATOM   4574 N N   . GLY B 1 306 ? 11.813  -1.257  -25.537 1.00  54.02  ? 306  GLY B N   1 
ATOM   4575 C CA  . GLY B 1 306 ? 11.773  -2.588  -24.930 1.00  54.83  ? 306  GLY B CA  1 
ATOM   4576 C C   . GLY B 1 306 ? 12.915  -3.500  -25.348 1.00  55.22  ? 306  GLY B C   1 
ATOM   4577 O O   . GLY B 1 306 ? 12.797  -4.728  -25.288 1.00  55.06  ? 306  GLY B O   1 
ATOM   4578 N N   . GLU B 1 307 ? 14.019  -2.898  -25.777 1.00  55.85  ? 307  GLU B N   1 
ATOM   4579 C CA  . GLU B 1 307 ? 15.201  -3.650  -26.190 1.00  56.63  ? 307  GLU B CA  1 
ATOM   4580 C C   . GLU B 1 307 ? 16.139  -3.829  -25.007 1.00  56.64  ? 307  GLU B C   1 
ATOM   4581 O O   . GLU B 1 307 ? 16.053  -3.089  -24.028 1.00  56.68  ? 307  GLU B O   1 
ATOM   4582 C CB  . GLU B 1 307 ? 15.930  -2.935  -27.334 1.00  56.75  ? 307  GLU B CB  1 
ATOM   4583 C CG  . GLU B 1 307 ? 15.183  -2.888  -28.647 1.00  58.23  ? 307  GLU B CG  1 
ATOM   4584 C CD  . GLU B 1 307 ? 15.833  -1.939  -29.651 1.00  61.00  ? 307  GLU B CD  1 
ATOM   4585 O OE1 . GLU B 1 307 ? 15.083  -1.223  -30.363 1.00  61.79  ? 307  GLU B OE1 1 
ATOM   4586 O OE2 . GLU B 1 307 ? 17.087  -1.898  -29.723 1.00  61.15  ? 307  GLU B OE2 1 
ATOM   4587 N N   . SER B 1 308 ? 17.044  -4.796  -25.119 1.00  57.07  ? 308  SER B N   1 
ATOM   4588 C CA  . SER B 1 308 ? 17.952  -5.166  -24.033 1.00  57.74  ? 308  SER B CA  1 
ATOM   4589 C C   . SER B 1 308 ? 18.894  -4.050  -23.578 1.00  58.10  ? 308  SER B C   1 
ATOM   4590 O O   . SER B 1 308 ? 19.714  -3.556  -24.358 1.00  58.25  ? 308  SER B O   1 
ATOM   4591 C CB  . SER B 1 308 ? 18.755  -6.417  -24.408 1.00  57.79  ? 308  SER B CB  1 
ATOM   4592 O OG  . SER B 1 308 ? 19.637  -6.783  -23.361 1.00  58.12  ? 308  SER B OG  1 
ATOM   4593 N N   . VAL B 1 309 ? 18.745  -3.667  -22.311 1.00  58.43  ? 309  VAL B N   1 
ATOM   4594 C CA  . VAL B 1 309 ? 19.605  -2.690  -21.643 1.00  58.93  ? 309  VAL B CA  1 
ATOM   4595 C C   . VAL B 1 309 ? 20.859  -3.372  -21.075 1.00  59.37  ? 309  VAL B C   1 
ATOM   4596 O O   . VAL B 1 309 ? 21.891  -2.734  -20.878 1.00  59.46  ? 309  VAL B O   1 
ATOM   4597 C CB  . VAL B 1 309 ? 18.823  -1.953  -20.510 1.00  58.90  ? 309  VAL B CB  1 
ATOM   4598 C CG1 . VAL B 1 309 ? 19.756  -1.179  -19.580 1.00  58.30  ? 309  VAL B CG1 1 
ATOM   4599 C CG2 . VAL B 1 309 ? 17.768  -1.023  -21.106 1.00  59.10  ? 309  VAL B CG2 1 
ATOM   4600 N N   . SER B 1 310 ? 20.758  -4.673  -20.812 1.00  60.08  ? 310  SER B N   1 
ATOM   4601 C CA  . SER B 1 310 ? 21.865  -5.465  -20.257 1.00  60.67  ? 310  SER B CA  1 
ATOM   4602 C C   . SER B 1 310 ? 23.045  -5.591  -21.224 1.00  60.65  ? 310  SER B C   1 
ATOM   4603 O O   . SER B 1 310 ? 24.155  -5.954  -20.834 1.00  60.66  ? 310  SER B O   1 
ATOM   4604 C CB  . SER B 1 310 ? 21.362  -6.847  -19.844 1.00  60.76  ? 310  SER B CB  1 
ATOM   4605 O OG  . SER B 1 310 ? 20.225  -6.713  -19.000 1.00  61.86  ? 310  SER B OG  1 
ATOM   4606 N N   . TYR B 1 311 ? 22.781  -5.277  -22.486 0.89  60.87  ? 311  TYR B N   1 
ATOM   4607 C CA  . TYR B 1 311 ? 23.792  -5.215  -23.537 0.89  61.15  ? 311  TYR B CA  1 
ATOM   4608 C C   . TYR B 1 311 ? 24.853  -4.148  -23.230 0.89  61.09  ? 311  TYR B C   1 
ATOM   4609 O O   . TYR B 1 311 ? 26.009  -4.264  -23.649 0.89  61.38  ? 311  TYR B O   1 
ATOM   4610 C CB  . TYR B 1 311 ? 23.082  -4.948  -24.866 0.89  61.11  ? 311  TYR B CB  1 
ATOM   4611 C CG  . TYR B 1 311 ? 23.904  -4.350  -25.980 0.89  61.95  ? 311  TYR B CG  1 
ATOM   4612 C CD1 . TYR B 1 311 ? 24.608  -5.164  -26.869 0.89  63.29  ? 311  TYR B CD1 1 
ATOM   4613 C CD2 . TYR B 1 311 ? 23.937  -2.970  -26.182 0.89  62.30  ? 311  TYR B CD2 1 
ATOM   4614 C CE1 . TYR B 1 311 ? 25.345  -4.610  -27.920 0.89  63.58  ? 311  TYR B CE1 1 
ATOM   4615 C CE2 . TYR B 1 311 ? 24.670  -2.410  -27.219 0.89  62.56  ? 311  TYR B CE2 1 
ATOM   4616 C CZ  . TYR B 1 311 ? 25.366  -3.233  -28.083 0.89  63.07  ? 311  TYR B CZ  1 
ATOM   4617 O OH  . TYR B 1 311 ? 26.088  -2.679  -29.111 0.89  64.16  ? 311  TYR B OH  1 
ATOM   4618 N N   . LEU B 1 312 ? 24.453  -3.124  -22.482 1.00  60.73  ? 312  LEU B N   1 
ATOM   4619 C CA  . LEU B 1 312 ? 25.349  -2.042  -22.097 1.00  60.57  ? 312  LEU B CA  1 
ATOM   4620 C C   . LEU B 1 312 ? 26.308  -2.438  -20.976 1.00  60.62  ? 312  LEU B C   1 
ATOM   4621 O O   . LEU B 1 312 ? 27.286  -1.726  -20.717 1.00  60.68  ? 312  LEU B O   1 
ATOM   4622 C CB  . LEU B 1 312 ? 24.542  -0.806  -21.669 1.00  60.43  ? 312  LEU B CB  1 
ATOM   4623 C CG  . LEU B 1 312 ? 23.824  0.015   -22.744 1.00  60.06  ? 312  LEU B CG  1 
ATOM   4624 C CD1 . LEU B 1 312 ? 22.679  0.807   -22.146 1.00  59.68  ? 312  LEU B CD1 1 
ATOM   4625 C CD2 . LEU B 1 312 ? 24.799  0.936   -23.459 1.00  59.76  ? 312  LEU B CD2 1 
ATOM   4626 N N   . PHE B 1 313 ? 26.031  -3.568  -20.323 1.00  60.59  ? 313  PHE B N   1 
ATOM   4627 C CA  . PHE B 1 313 ? 26.760  -3.971  -19.111 1.00  60.59  ? 313  PHE B CA  1 
ATOM   4628 C C   . PHE B 1 313 ? 28.195  -4.457  -19.359 1.00  60.53  ? 313  PHE B C   1 
ATOM   4629 O O   . PHE B 1 313 ? 28.922  -4.759  -18.404 1.00  60.56  ? 313  PHE B O   1 
ATOM   4630 C CB  . PHE B 1 313 ? 25.979  -5.027  -18.304 1.00  60.57  ? 313  PHE B CB  1 
ATOM   4631 C CG  . PHE B 1 313 ? 24.684  -4.524  -17.698 1.00  60.82  ? 313  PHE B CG  1 
ATOM   4632 C CD1 . PHE B 1 313 ? 24.395  -3.159  -17.620 1.00  60.52  ? 313  PHE B CD1 1 
ATOM   4633 C CD2 . PHE B 1 313 ? 23.761  -5.429  -17.174 1.00  60.92  ? 313  PHE B CD2 1 
ATOM   4634 C CE1 . PHE B 1 313 ? 23.192  -2.709  -17.051 1.00  60.79  ? 313  PHE B CE1 1 
ATOM   4635 C CE2 . PHE B 1 313 ? 22.558  -4.987  -16.599 1.00  60.96  ? 313  PHE B CE2 1 
ATOM   4636 C CZ  . PHE B 1 313 ? 22.275  -3.626  -16.539 1.00  60.22  ? 313  PHE B CZ  1 
ATOM   4637 N N   . SER B 1 314 ? 28.588  -4.544  -20.631 0.84  60.48  ? 314  SER B N   1 
ATOM   4638 C CA  . SER B 1 314 ? 29.951  -4.932  -20.999 0.84  60.62  ? 314  SER B CA  1 
ATOM   4639 C C   . SER B 1 314 ? 30.418  -4.287  -22.311 0.84  60.70  ? 314  SER B C   1 
ATOM   4640 O O   . SER B 1 314 ? 31.601  -4.349  -22.653 0.84  60.76  ? 314  SER B O   1 
ATOM   4641 C CB  . SER B 1 314 ? 30.094  -6.459  -21.052 0.84  60.63  ? 314  SER B CB  1 
ATOM   4642 O OG  . SER B 1 314 ? 29.197  -7.026  -21.991 0.84  61.21  ? 314  SER B OG  1 
ATOM   4643 N N   . HIS B 1 315 ? 29.532  -3.565  -22.975 0.50  60.76  ? 315  HIS B N   1 
ATOM   4644 C CA  . HIS B 1 315 ? 29.727  -3.108  -24.338 0.50  60.84  ? 315  HIS B CA  1 
ATOM   4645 C C   . HIS B 1 315 ? 29.406  -1.609  -24.460 0.50  61.11  ? 315  HIS B C   1 
ATOM   4646 O O   . HIS B 1 315 ? 28.272  -1.232  -24.238 0.50  61.13  ? 315  HIS B O   1 
ATOM   4647 C CB  . HIS B 1 315 ? 28.783  -3.982  -25.176 0.50  60.77  ? 315  HIS B CB  1 
ATOM   4648 C CG  . HIS B 1 315 ? 28.862  -3.797  -26.658 0.50  60.67  ? 315  HIS B CG  1 
ATOM   4649 N ND1 . HIS B 1 315 ? 29.622  -2.826  -27.263 0.50  60.70  ? 315  HIS B ND1 1 
ATOM   4650 C CD2 . HIS B 1 315 ? 28.238  -4.460  -27.660 0.50  60.43  ? 315  HIS B CD2 1 
ATOM   4651 C CE1 . HIS B 1 315 ? 29.465  -2.897  -28.571 0.50  60.90  ? 315  HIS B CE1 1 
ATOM   4652 N NE2 . HIS B 1 315 ? 28.633  -3.882  -28.839 0.50  60.38  ? 315  HIS B NE2 1 
ATOM   4653 N N   . VAL B 1 316 ? 30.397  -0.763  -24.803 1.00  61.42  ? 316  VAL B N   1 
ATOM   4654 C CA  . VAL B 1 316 ? 30.229  0.685   -24.916 1.00  61.53  ? 316  VAL B CA  1 
ATOM   4655 C C   . VAL B 1 316 ? 29.576  1.012   -26.258 1.00  61.56  ? 316  VAL B C   1 
ATOM   4656 O O   . VAL B 1 316 ? 30.123  0.653   -27.310 1.00  61.96  ? 316  VAL B O   1 
ATOM   4657 C CB  . VAL B 1 316 ? 31.591  1.431   -24.822 1.00  61.77  ? 316  VAL B CB  1 
ATOM   4658 C CG1 . VAL B 1 316 ? 31.383  2.889   -24.383 1.00  61.52  ? 316  VAL B CG1 1 
ATOM   4659 C CG2 . VAL B 1 316 ? 32.550  0.709   -23.866 1.00  61.70  ? 316  VAL B CG2 1 
ATOM   4660 N N   . PRO B 1 317 ? 28.412  1.698   -26.234 1.00  61.27  ? 317  PRO B N   1 
ATOM   4661 C CA  . PRO B 1 317 ? 27.674  2.003   -27.466 1.00  61.12  ? 317  PRO B CA  1 
ATOM   4662 C C   . PRO B 1 317 ? 28.509  2.808   -28.469 1.00  61.11  ? 317  PRO B C   1 
ATOM   4663 O O   . PRO B 1 317 ? 28.721  2.350   -29.594 1.00  61.09  ? 317  PRO B O   1 
ATOM   4664 C CB  . PRO B 1 317 ? 26.473  2.822   -26.971 1.00  60.67  ? 317  PRO B CB  1 
ATOM   4665 C CG  . PRO B 1 317 ? 26.868  3.318   -25.636 1.00  60.76  ? 317  PRO B CG  1 
ATOM   4666 C CD  . PRO B 1 317 ? 27.744  2.264   -25.051 1.00  61.27  ? 317  PRO B CD  1 
HETATM 4667 S S   . SO4 C 2 .   ? -9.603  15.882  21.274  1.00  39.77  ? 1001 SO4 A S   1 
HETATM 4668 O O1  . SO4 C 2 .   ? -10.397 15.021  20.396  1.00  37.74  ? 1001 SO4 A O1  1 
HETATM 4669 O O2  . SO4 C 2 .   ? -9.031  17.017  20.525  1.00  37.58  ? 1001 SO4 A O2  1 
HETATM 4670 O O3  . SO4 C 2 .   ? -10.531 16.404  22.303  1.00  40.98  ? 1001 SO4 A O3  1 
HETATM 4671 O O4  . SO4 C 2 .   ? -8.524  15.066  21.855  1.00  38.37  ? 1001 SO4 A O4  1 
HETATM 4672 S S   . SO4 D 2 .   ? 4.595   37.750  -0.971  0.98  144.58 ? 1002 SO4 A S   1 
HETATM 4673 O O1  . SO4 D 2 .   ? 3.542   36.923  -0.374  0.98  144.44 ? 1002 SO4 A O1  1 
HETATM 4674 O O2  . SO4 D 2 .   ? 4.013   38.913  -1.636  0.98  144.55 ? 1002 SO4 A O2  1 
HETATM 4675 O O3  . SO4 D 2 .   ? 5.509   38.186  0.077   0.98  144.44 ? 1002 SO4 A O3  1 
HETATM 4676 O O4  . SO4 D 2 .   ? 5.336   36.967  -1.956  0.98  144.42 ? 1002 SO4 A O4  1 
HETATM 4677 S S   . SO4 E 2 .   ? 17.287  -6.522  -20.544 1.00  37.89  ? 401  SO4 B S   1 
HETATM 4678 O O1  . SO4 E 2 .   ? 16.198  -5.764  -21.154 1.00  37.58  ? 401  SO4 B O1  1 
HETATM 4679 O O2  . SO4 E 2 .   ? 17.779  -7.457  -21.554 1.00  38.26  ? 401  SO4 B O2  1 
HETATM 4680 O O3  . SO4 E 2 .   ? 18.348  -5.620  -20.116 1.00  37.68  ? 401  SO4 B O3  1 
HETATM 4681 O O4  . SO4 E 2 .   ? 16.822  -7.256  -19.369 1.00  36.89  ? 401  SO4 B O4  1 
HETATM 4682 S S   . SO4 F 2 .   ? 37.010  10.511  -0.025  1.00  69.36  ? 402  SO4 B S   1 
HETATM 4683 O O1  . SO4 F 2 .   ? 36.707  11.851  0.479   1.00  69.15  ? 402  SO4 B O1  1 
HETATM 4684 O O2  . SO4 F 2 .   ? 36.615  10.400  -1.434  1.00  69.30  ? 402  SO4 B O2  1 
HETATM 4685 O O3  . SO4 F 2 .   ? 38.446  10.277  0.108   1.00  69.86  ? 402  SO4 B O3  1 
HETATM 4686 O O4  . SO4 F 2 .   ? 36.278  9.528   0.772   1.00  68.70  ? 402  SO4 B O4  1 
HETATM 4687 O O   . HOH G 3 .   ? 21.007  7.920   27.210  1.00  34.26  ? 1101 HOH A O   1 
HETATM 4688 O O   . HOH G 3 .   ? -23.857 42.159  17.403  1.00  40.95  ? 1102 HOH A O   1 
HETATM 4689 O O   . HOH G 3 .   ? -6.557  14.524  9.536   1.00  42.64  ? 1103 HOH A O   1 
HETATM 4690 O O   . HOH G 3 .   ? -17.350 44.532  7.125   1.00  52.82  ? 1104 HOH A O   1 
HETATM 4691 O O   . HOH G 3 .   ? -16.038 49.004  -1.480  1.00  41.58  ? 1105 HOH A O   1 
HETATM 4692 O O   . HOH H 3 .   ? 31.426  12.884  -12.213 1.00  36.24  ? 501  HOH B O   1 
HETATM 4693 O O   . HOH H 3 .   ? 11.255  1.776   -2.014  1.00  34.14  ? 502  HOH B O   1 
HETATM 4694 O O   . HOH H 3 .   ? 18.516  29.833  1.750   1.00  52.92  ? 503  HOH B O   1 
HETATM 4695 O O   . HOH H 3 .   ? 53.519  -10.098 -17.563 1.00  37.96  ? 504  HOH B O   1 
HETATM 4696 O O   . HOH H 3 .   ? 39.162  13.751  4.908   1.00  42.99  ? 505  HOH B O   1 
HETATM 4697 O O   . HOH H 3 .   ? 4.381   4.134   -21.730 1.00  31.41  ? 506  HOH B O   1 
HETATM 4698 O O   . HOH H 3 .   ? 27.991  0.753   -21.564 1.00  48.75  ? 507  HOH B O   1 
HETATM 4699 O O   . HOH H 3 .   ? 19.088  23.544  -22.976 1.00  25.93  ? 508  HOH B O   1 
HETATM 4700 O O   . HOH H 3 .   ? 38.760  2.374   -27.699 1.00  60.60  ? 509  HOH B O   1 
HETATM 4701 O O   . HOH H 3 .   ? 30.430  11.340  -29.637 1.00  52.06  ? 510  HOH B O   1 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   PRO 2   2   ?   ?   ?   A . n 
A 1 3   ASN 3   3   3   ASN ASN A . n 
A 1 4   ILE 4   4   4   ILE ILE A . n 
A 1 5   LYS 5   5   5   LYS LYS A . n 
A 1 6   ILE 6   6   6   ILE ILE A . n 
A 1 7   PHE 7   7   7   PHE PHE A . n 
A 1 8   SER 8   8   8   SER SER A . n 
A 1 9   GLY 9   9   9   GLY GLY A . n 
A 1 10  SER 10  10  10  SER SER A . n 
A 1 11  SER 11  11  11  SER SER A . n 
A 1 12  HIS 12  12  12  HIS HIS A . n 
A 1 13  GLN 13  13  13  GLN GLN A . n 
A 1 14  ASP 14  14  14  ASP ASP A . n 
A 1 15  LEU 15  15  15  LEU LEU A . n 
A 1 16  SER 16  16  16  SER SER A . n 
A 1 17  GLN 17  17  17  GLN GLN A . n 
A 1 18  LYS 18  18  18  LYS LYS A . n 
A 1 19  ILE 19  19  19  ILE ILE A . n 
A 1 20  ALA 20  20  20  ALA ALA A . n 
A 1 21  ASP 21  21  21  ASP ASP A . n 
A 1 22  ARG 22  22  22  ARG ARG A . n 
A 1 23  LEU 23  23  23  LEU LEU A . n 
A 1 24  GLY 24  24  24  GLY GLY A . n 
A 1 25  LEU 25  25  25  LEU LEU A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  LEU 27  27  27  LEU LEU A . n 
A 1 28  GLY 28  28  28  GLY GLY A . n 
A 1 29  LYS 29  29  29  LYS LYS A . n 
A 1 30  VAL 30  30  30  VAL VAL A . n 
A 1 31  VAL 31  31  31  VAL VAL A . n 
A 1 32  THR 32  32  32  THR THR A . n 
A 1 33  LYS 33  33  33  LYS LYS A . n 
A 1 34  LYS 34  34  34  LYS LYS A . n 
A 1 35  PHE 35  35  35  PHE PHE A . n 
A 1 36  SER 36  36  36  SER SER A . n 
A 1 37  ASN 37  37  37  ASN ASN A . n 
A 1 38  GLN 38  38  38  GLN GLN A . n 
A 1 39  GLU 39  39  39  GLU GLU A . n 
A 1 40  THR 40  40  40  THR THR A . n 
A 1 41  CYS 41  41  41  CYS CYS A . n 
A 1 42  VAL 42  42  42  VAL VAL A . n 
A 1 43  GLU 43  43  43  GLU GLU A . n 
A 1 44  ILE 44  44  44  ILE ILE A . n 
A 1 45  GLY 45  45  45  GLY GLY A . n 
A 1 46  GLU 46  46  46  GLU GLU A . n 
A 1 47  SER 47  47  47  SER SER A . n 
A 1 48  VAL 48  48  48  VAL VAL A . n 
A 1 49  ARG 49  49  49  ARG ARG A . n 
A 1 50  GLY 50  50  50  GLY GLY A . n 
A 1 51  GLU 51  51  51  GLU GLU A . n 
A 1 52  ASP 52  52  52  ASP ASP A . n 
A 1 53  VAL 53  53  53  VAL VAL A . n 
A 1 54  TYR 54  54  54  TYR TYR A . n 
A 1 55  ILE 55  55  55  ILE ILE A . n 
A 1 56  VAL 56  56  56  VAL VAL A . n 
A 1 57  GLN 57  57  57  GLN GLN A . n 
A 1 58  SER 58  58  58  SER SER A . n 
A 1 59  GLY 59  59  59  GLY GLY A . n 
A 1 60  CYS 60  60  60  CYS CYS A . n 
A 1 61  GLY 61  61  61  GLY GLY A . n 
A 1 62  GLU 62  62  62  GLU GLU A . n 
A 1 63  ILE 63  63  63  ILE ILE A . n 
A 1 64  ASN 64  64  64  ASN ASN A . n 
A 1 65  ASP 65  65  65  ASP ASP A . n 
A 1 66  ASN 66  66  66  ASN ASN A . n 
A 1 67  LEU 67  67  67  LEU LEU A . n 
A 1 68  MET 68  68  68  MET MET A . n 
A 1 69  GLU 69  69  69  GLU GLU A . n 
A 1 70  LEU 70  70  70  LEU LEU A . n 
A 1 71  LEU 71  71  71  LEU LEU A . n 
A 1 72  ILE 72  72  72  ILE ILE A . n 
A 1 73  MET 73  73  73  MET MET A . n 
A 1 74  ILE 74  74  74  ILE ILE A . n 
A 1 75  ASN 75  75  75  ASN ASN A . n 
A 1 76  ALA 76  76  76  ALA ALA A . n 
A 1 77  CYS 77  77  77  CYS CYS A . n 
A 1 78  LYS 78  78  78  LYS LYS A . n 
A 1 79  ILE 79  79  79  ILE ILE A . n 
A 1 80  ALA 80  80  80  ALA ALA A . n 
A 1 81  SER 81  81  81  SER SER A . n 
A 1 82  ALA 82  82  82  ALA ALA A . n 
A 1 83  SER 83  83  83  SER SER A . n 
A 1 84  ARG 84  84  84  ARG ARG A . n 
A 1 85  VAL 85  85  85  VAL VAL A . n 
A 1 86  THR 86  86  86  THR THR A . n 
A 1 87  ALA 87  87  87  ALA ALA A . n 
A 1 88  VAL 88  88  88  VAL VAL A . n 
A 1 89  ILE 89  89  89  ILE ILE A . n 
A 1 90  PRO 90  90  90  PRO PRO A . n 
A 1 91  CYS 91  91  91  CYS CYS A . n 
A 1 92  PHE 92  92  92  PHE PHE A . n 
A 1 93  PRO 93  93  93  PRO PRO A . n 
A 1 94  TYR 94  94  94  TYR TYR A . n 
A 1 95  ALA 95  95  95  ALA ALA A . n 
A 1 96  ARG 96  96  96  ARG ARG A . n 
A 1 97  GLN 97  97  97  GLN GLN A . n 
A 1 98  ASP 98  98  98  ASP ASP A . n 
A 1 99  LYS 99  99  99  LYS LYS A . n 
A 1 100 LYS 100 100 100 LYS LYS A . n 
A 1 101 ASP 101 101 101 ASP ASP A . n 
A 1 102 LYS 102 102 102 LYS LYS A . n 
A 1 103 SER 103 103 103 SER SER A . n 
A 1 104 ARG 104 104 104 ARG ARG A . n 
A 1 105 ALA 105 105 105 ALA ALA A . n 
A 1 106 PRO 106 106 106 PRO PRO A . n 
A 1 107 ILE 107 107 107 ILE ILE A . n 
A 1 108 SER 108 108 108 SER SER A . n 
A 1 109 ALA 109 109 109 ALA ALA A . n 
A 1 110 LYS 110 110 110 LYS LYS A . n 
A 1 111 LEU 111 111 111 LEU LEU A . n 
A 1 112 VAL 112 112 112 VAL VAL A . n 
A 1 113 ALA 113 113 113 ALA ALA A . n 
A 1 114 ASN 114 114 114 ASN ASN A . n 
A 1 115 MET 115 115 115 MET MET A . n 
A 1 116 LEU 116 116 116 LEU LEU A . n 
A 1 117 SER 117 117 117 SER SER A . n 
A 1 118 VAL 118 118 118 VAL VAL A . n 
A 1 119 ALA 119 119 119 ALA ALA A . n 
A 1 120 GLY 120 120 120 GLY GLY A . n 
A 1 121 ALA 121 121 121 ALA ALA A . n 
A 1 122 ASP 122 122 122 ASP ASP A . n 
A 1 123 HIS 123 123 123 HIS HIS A . n 
A 1 124 ILE 124 124 124 ILE ILE A . n 
A 1 125 ILE 125 125 125 ILE ILE A . n 
A 1 126 THR 126 126 126 THR THR A . n 
A 1 127 MET 127 127 127 MET MET A . n 
A 1 128 ASP 128 128 128 ASP ASP A . n 
A 1 129 LEU 129 129 129 LEU LEU A . n 
A 1 130 HIS 130 130 130 HIS HIS A . n 
A 1 131 ALA 131 131 131 ALA ALA A . n 
A 1 132 SER 132 132 132 SER SER A . n 
A 1 133 PRO 133 133 133 PRO PRO A . n 
A 1 134 ILE 134 134 134 ILE ILE A . n 
A 1 135 GLN 135 135 135 GLN GLN A . n 
A 1 136 GLY 136 136 136 GLY GLY A . n 
A 1 137 PHE 137 137 137 PHE PHE A . n 
A 1 138 PHE 138 138 138 PHE PHE A . n 
A 1 139 ASP 139 139 139 ASP ASP A . n 
A 1 140 ILE 140 140 140 ILE ILE A . n 
A 1 141 PRO 141 141 141 PRO PRO A . n 
A 1 142 VAL 142 142 142 VAL VAL A . n 
A 1 143 ASP 143 143 143 ASP ASP A . n 
A 1 144 ASN 144 144 144 ASN ASN A . n 
A 1 145 LEU 145 145 145 LEU LEU A . n 
A 1 146 TYR 146 146 146 TYR TYR A . n 
A 1 147 ALA 147 147 147 ALA ALA A . n 
A 1 148 GLU 148 148 148 GLU GLU A . n 
A 1 149 PRO 149 149 149 PRO PRO A . n 
A 1 150 ALA 150 150 150 ALA ALA A . n 
A 1 151 VAL 151 151 151 VAL VAL A . n 
A 1 152 LEU 152 152 152 LEU LEU A . n 
A 1 153 LYS 153 153 153 LYS LYS A . n 
A 1 154 TRP 154 154 154 TRP TRP A . n 
A 1 155 ILE 155 155 155 ILE ILE A . n 
A 1 156 ARG 156 156 156 ARG ARG A . n 
A 1 157 GLU 157 157 157 GLU GLU A . n 
A 1 158 ASN 158 158 158 ASN ASN A . n 
A 1 159 ILE 159 159 159 ILE ILE A . n 
A 1 160 SER 160 160 160 SER SER A . n 
A 1 161 GLU 161 161 161 GLU GLU A . n 
A 1 162 TRP 162 162 162 TRP TRP A . n 
A 1 163 ARG 163 163 163 ARG ARG A . n 
A 1 164 ASN 164 164 164 ASN ASN A . n 
A 1 165 CYS 165 165 165 CYS CYS A . n 
A 1 166 THR 166 166 166 THR THR A . n 
A 1 167 ILE 167 167 167 ILE ILE A . n 
A 1 168 VAL 168 168 168 VAL VAL A . n 
A 1 169 SER 169 169 169 SER SER A . n 
A 1 170 PRO 170 170 170 PRO PRO A . n 
A 1 171 ASP 171 171 171 ASP ASP A . n 
A 1 172 ALA 172 172 172 ALA ALA A . n 
A 1 173 GLY 173 173 173 GLY GLY A . n 
A 1 174 GLY 174 174 174 GLY GLY A . n 
A 1 175 ALA 175 175 175 ALA ALA A . n 
A 1 176 LYS 176 176 176 LYS LYS A . n 
A 1 177 ARG 177 177 177 ARG ARG A . n 
A 1 178 VAL 178 178 178 VAL VAL A . n 
A 1 179 THR 179 179 179 THR THR A . n 
A 1 180 SER 180 180 180 SER SER A . n 
A 1 181 ILE 181 181 181 ILE ILE A . n 
A 1 182 ALA 182 182 182 ALA ALA A . n 
A 1 183 ASP 183 183 183 ASP ASP A . n 
A 1 184 ARG 184 184 184 ARG ARG A . n 
A 1 185 LEU 185 185 185 LEU LEU A . n 
A 1 186 ASN 186 186 186 ASN ASN A . n 
A 1 187 VAL 187 187 187 VAL VAL A . n 
A 1 188 ASP 188 188 188 ASP ASP A . n 
A 1 189 PHE 189 189 189 PHE PHE A . n 
A 1 190 ALA 190 190 190 ALA ALA A . n 
A 1 191 LEU 191 191 191 LEU LEU A . n 
A 1 192 ILE 192 192 192 ILE ILE A . n 
A 1 193 HIS 193 193 193 HIS HIS A . n 
A 1 194 LYS 194 194 194 LYS LYS A . n 
A 1 195 GLU 195 195 195 GLU GLU A . n 
A 1 196 ARG 196 196 ?   ?   ?   A . n 
A 1 197 LYS 197 197 ?   ?   ?   A . n 
A 1 198 LYS 198 198 ?   ?   ?   A . n 
A 1 199 ALA 199 199 ?   ?   ?   A . n 
A 1 200 ASN 200 200 ?   ?   ?   A . n 
A 1 201 GLU 201 201 ?   ?   ?   A . n 
A 1 202 VAL 202 202 ?   ?   ?   A . n 
A 1 203 ASP 203 203 203 ASP ASP A . n 
A 1 204 ARG 204 204 204 ARG ARG A . n 
A 1 205 MET 205 205 205 MET MET A . n 
A 1 206 VAL 206 206 206 VAL VAL A . n 
A 1 207 LEU 207 207 207 LEU LEU A . n 
A 1 208 VAL 208 208 208 VAL VAL A . n 
A 1 209 GLY 209 209 209 GLY GLY A . n 
A 1 210 ASP 210 210 210 ASP ASP A . n 
A 1 211 VAL 211 211 211 VAL VAL A . n 
A 1 212 LYS 212 212 212 LYS LYS A . n 
A 1 213 ASP 213 213 213 ASP ASP A . n 
A 1 214 ARG 214 214 214 ARG ARG A . n 
A 1 215 VAL 215 215 215 VAL VAL A . n 
A 1 216 ALA 216 216 216 ALA ALA A . n 
A 1 217 ILE 217 217 217 ILE ILE A . n 
A 1 218 LEU 218 218 218 LEU LEU A . n 
A 1 219 VAL 219 219 219 VAL VAL A . n 
A 1 220 ASP 220 220 220 ASP ASP A . n 
A 1 221 ASP 221 221 221 ASP ASP A . n 
A 1 222 MET 222 222 222 MET MET A . n 
A 1 223 ALA 223 223 223 ALA ALA A . n 
A 1 224 ASP 224 224 224 ASP ASP A . n 
A 1 225 THR 225 225 225 THR THR A . n 
A 1 226 CYS 226 226 226 CYS CYS A . n 
A 1 227 GLY 227 227 227 GLY GLY A . n 
A 1 228 THR 228 228 228 THR THR A . n 
A 1 229 ILE 229 229 229 ILE ILE A . n 
A 1 230 CYS 230 230 230 CYS CYS A . n 
A 1 231 HIS 231 231 231 HIS HIS A . n 
A 1 232 ALA 232 232 232 ALA ALA A . n 
A 1 233 ALA 233 233 233 ALA ALA A . n 
A 1 234 ASP 234 234 234 ASP ASP A . n 
A 1 235 LYS 235 235 235 LYS LYS A . n 
A 1 236 LEU 236 236 236 LEU LEU A . n 
A 1 237 LEU 237 237 237 LEU LEU A . n 
A 1 238 SER 238 238 238 SER SER A . n 
A 1 239 ALA 239 239 239 ALA ALA A . n 
A 1 240 GLY 240 240 240 GLY GLY 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 ARG 243 243 243 ARG ARG A . n 
A 1 244 VAL 244 244 244 VAL VAL A . n 
A 1 245 TYR 245 245 245 TYR TYR A . n 
A 1 246 ALA 246 246 246 ALA ALA A . n 
A 1 247 ILE 247 247 247 ILE ILE A . n 
A 1 248 LEU 248 248 248 LEU LEU A . n 
A 1 249 THR 249 249 249 THR THR A . n 
A 1 250 HIS 250 250 250 HIS HIS A . n 
A 1 251 GLY 251 251 251 GLY GLY A . n 
A 1 252 ILE 252 252 252 ILE ILE A . n 
A 1 253 PHE 253 253 253 PHE PHE A . n 
A 1 254 SER 254 254 254 SER SER A . n 
A 1 255 GLY 255 255 255 GLY GLY A . n 
A 1 256 PRO 256 256 256 PRO PRO A . n 
A 1 257 ALA 257 257 257 ALA ALA A . n 
A 1 258 ILE 258 258 258 ILE ILE A . n 
A 1 259 SER 259 259 259 SER SER A . n 
A 1 260 ARG 260 260 260 ARG ARG A . n 
A 1 261 ILE 261 261 261 ILE ILE A . n 
A 1 262 ASN 262 262 262 ASN ASN A . n 
A 1 263 ASN 263 263 263 ASN ASN A . n 
A 1 264 ALA 264 264 264 ALA ALA A . n 
A 1 265 CYS 265 265 265 CYS CYS A . n 
A 1 266 PHE 266 266 266 PHE PHE A . n 
A 1 267 GLU 267 267 267 GLU GLU A . n 
A 1 268 ALA 268 268 268 ALA ALA A . n 
A 1 269 VAL 269 269 269 VAL VAL A . n 
A 1 270 VAL 270 270 270 VAL VAL A . n 
A 1 271 VAL 271 271 271 VAL VAL A . n 
A 1 272 THR 272 272 272 THR THR A . n 
A 1 273 ASN 273 273 273 ASN ASN A . n 
A 1 274 THR 274 274 274 THR THR A . n 
A 1 275 ILE 275 275 275 ILE ILE A . n 
A 1 276 PRO 276 276 276 PRO PRO A . n 
A 1 277 GLN 277 277 277 GLN GLN A . n 
A 1 278 GLU 278 278 278 GLU GLU A . n 
A 1 279 ASP 279 279 279 ASP ASP A . n 
A 1 280 LYS 280 280 280 LYS LYS A . n 
A 1 281 MET 281 281 281 MET MET A . n 
A 1 282 LYS 282 282 282 LYS LYS A . n 
A 1 283 HIS 283 283 283 HIS HIS A . n 
A 1 284 CYS 284 284 284 CYS CYS A . n 
A 1 285 SER 285 285 285 SER SER A . n 
A 1 286 LYS 286 286 286 LYS LYS A . n 
A 1 287 ILE 287 287 287 ILE ILE A . n 
A 1 288 GLN 288 288 288 GLN GLN A . n 
A 1 289 VAL 289 289 289 VAL VAL A . n 
A 1 290 ILE 290 290 290 ILE ILE A . n 
A 1 291 ASP 291 291 291 ASP ASP A . n 
A 1 292 ILE 292 292 292 ILE ILE A . n 
A 1 293 SER 293 293 293 SER SER A . n 
A 1 294 MET 294 294 294 MET MET A . n 
A 1 295 ILE 295 295 295 ILE ILE A . n 
A 1 296 LEU 296 296 296 LEU LEU A . n 
A 1 297 ALA 297 297 297 ALA ALA A . n 
A 1 298 GLU 298 298 298 GLU GLU A . n 
A 1 299 ALA 299 299 299 ALA ALA A . n 
A 1 300 ILE 300 300 300 ILE ILE A . n 
A 1 301 ARG 301 301 301 ARG ARG A . n 
A 1 302 ARG 302 302 302 ARG ARG A . n 
A 1 303 THR 303 303 303 THR THR A . n 
A 1 304 HIS 304 304 304 HIS HIS A . n 
A 1 305 ASN 305 305 305 ASN ASN A . n 
A 1 306 GLY 306 306 306 GLY GLY A . n 
A 1 307 GLU 307 307 307 GLU GLU A . n 
A 1 308 SER 308 308 308 SER SER A . n 
A 1 309 VAL 309 309 309 VAL VAL A . n 
A 1 310 SER 310 310 310 SER SER A . n 
A 1 311 TYR 311 311 311 TYR TYR A . n 
A 1 312 LEU 312 312 312 LEU LEU A . n 
A 1 313 PHE 313 313 ?   ?   ?   A . n 
A 1 314 SER 314 314 ?   ?   ?   A . n 
A 1 315 HIS 315 315 ?   ?   ?   A . n 
A 1 316 VAL 316 316 ?   ?   ?   A . n 
A 1 317 PRO 317 317 ?   ?   ?   A . n 
A 1 318 LEU 318 318 ?   ?   ?   A . n 
A 1 319 LEU 319 319 ?   ?   ?   A . n 
A 1 320 GLU 320 320 ?   ?   ?   A . n 
A 1 321 HIS 321 321 ?   ?   ?   A . n 
A 1 322 HIS 322 322 ?   ?   ?   A . n 
A 1 323 HIS 323 323 ?   ?   ?   A . n 
A 1 324 HIS 324 324 ?   ?   ?   A . n 
A 1 325 HIS 325 325 ?   ?   ?   A . n 
A 1 326 HIS 326 326 ?   ?   ?   A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   PRO 2   2   ?   ?   ?   B . n 
B 1 3   ASN 3   3   3   ASN ASN B . n 
B 1 4   ILE 4   4   4   ILE ILE B . n 
B 1 5   LYS 5   5   5   LYS LYS B . n 
B 1 6   ILE 6   6   6   ILE ILE B . n 
B 1 7   PHE 7   7   7   PHE PHE B . n 
B 1 8   SER 8   8   8   SER SER B . n 
B 1 9   GLY 9   9   9   GLY GLY B . n 
B 1 10  SER 10  10  10  SER SER B . n 
B 1 11  SER 11  11  11  SER SER B . n 
B 1 12  HIS 12  12  12  HIS HIS B . n 
B 1 13  GLN 13  13  13  GLN GLN B . n 
B 1 14  ASP 14  14  14  ASP ASP B . n 
B 1 15  LEU 15  15  15  LEU LEU B . n 
B 1 16  SER 16  16  16  SER SER B . n 
B 1 17  GLN 17  17  17  GLN GLN B . n 
B 1 18  LYS 18  18  18  LYS LYS B . n 
B 1 19  ILE 19  19  19  ILE ILE B . n 
B 1 20  ALA 20  20  20  ALA ALA B . n 
B 1 21  ASP 21  21  21  ASP ASP B . n 
B 1 22  ARG 22  22  22  ARG ARG B . n 
B 1 23  LEU 23  23  23  LEU LEU B . n 
B 1 24  GLY 24  24  24  GLY GLY B . n 
B 1 25  LEU 25  25  25  LEU LEU B . n 
B 1 26  GLU 26  26  26  GLU GLU B . n 
B 1 27  LEU 27  27  27  LEU LEU B . n 
B 1 28  GLY 28  28  28  GLY GLY B . n 
B 1 29  LYS 29  29  29  LYS LYS B . n 
B 1 30  VAL 30  30  30  VAL VAL B . n 
B 1 31  VAL 31  31  31  VAL VAL B . n 
B 1 32  THR 32  32  32  THR THR B . n 
B 1 33  LYS 33  33  33  LYS LYS B . n 
B 1 34  LYS 34  34  34  LYS LYS B . n 
B 1 35  PHE 35  35  35  PHE PHE B . n 
B 1 36  SER 36  36  36  SER SER B . n 
B 1 37  ASN 37  37  37  ASN ASN B . n 
B 1 38  GLN 38  38  38  GLN GLN B . n 
B 1 39  GLU 39  39  39  GLU GLU B . n 
B 1 40  THR 40  40  40  THR THR B . n 
B 1 41  CYS 41  41  41  CYS CYS B . n 
B 1 42  VAL 42  42  42  VAL VAL B . n 
B 1 43  GLU 43  43  43  GLU GLU B . n 
B 1 44  ILE 44  44  44  ILE ILE B . n 
B 1 45  GLY 45  45  45  GLY GLY B . n 
B 1 46  GLU 46  46  46  GLU GLU B . n 
B 1 47  SER 47  47  47  SER SER B . n 
B 1 48  VAL 48  48  48  VAL VAL B . n 
B 1 49  ARG 49  49  49  ARG ARG B . n 
B 1 50  GLY 50  50  50  GLY GLY B . n 
B 1 51  GLU 51  51  51  GLU GLU B . n 
B 1 52  ASP 52  52  52  ASP ASP B . n 
B 1 53  VAL 53  53  53  VAL VAL B . n 
B 1 54  TYR 54  54  54  TYR TYR B . n 
B 1 55  ILE 55  55  55  ILE ILE B . n 
B 1 56  VAL 56  56  56  VAL VAL B . n 
B 1 57  GLN 57  57  57  GLN GLN B . n 
B 1 58  SER 58  58  58  SER SER B . n 
B 1 59  GLY 59  59  59  GLY GLY B . n 
B 1 60  CYS 60  60  60  CYS CYS B . n 
B 1 61  GLY 61  61  61  GLY GLY B . n 
B 1 62  GLU 62  62  62  GLU GLU B . n 
B 1 63  ILE 63  63  63  ILE ILE B . n 
B 1 64  ASN 64  64  64  ASN ASN B . n 
B 1 65  ASP 65  65  65  ASP ASP B . n 
B 1 66  ASN 66  66  66  ASN ASN B . n 
B 1 67  LEU 67  67  67  LEU LEU B . n 
B 1 68  MET 68  68  68  MET MET B . n 
B 1 69  GLU 69  69  69  GLU GLU B . n 
B 1 70  LEU 70  70  70  LEU LEU B . n 
B 1 71  LEU 71  71  71  LEU LEU B . n 
B 1 72  ILE 72  72  72  ILE ILE B . n 
B 1 73  MET 73  73  73  MET MET B . n 
B 1 74  ILE 74  74  74  ILE ILE B . n 
B 1 75  ASN 75  75  75  ASN ASN B . n 
B 1 76  ALA 76  76  76  ALA ALA B . n 
B 1 77  CYS 77  77  77  CYS CYS B . n 
B 1 78  LYS 78  78  78  LYS LYS B . n 
B 1 79  ILE 79  79  79  ILE ILE B . n 
B 1 80  ALA 80  80  80  ALA ALA B . n 
B 1 81  SER 81  81  81  SER SER B . n 
B 1 82  ALA 82  82  82  ALA ALA B . n 
B 1 83  SER 83  83  83  SER SER B . n 
B 1 84  ARG 84  84  84  ARG ARG B . n 
B 1 85  VAL 85  85  85  VAL VAL B . n 
B 1 86  THR 86  86  86  THR THR B . n 
B 1 87  ALA 87  87  87  ALA ALA B . n 
B 1 88  VAL 88  88  88  VAL VAL B . n 
B 1 89  ILE 89  89  89  ILE ILE B . n 
B 1 90  PRO 90  90  90  PRO PRO B . n 
B 1 91  CYS 91  91  91  CYS CYS B . n 
B 1 92  PHE 92  92  92  PHE PHE B . n 
B 1 93  PRO 93  93  93  PRO PRO B . n 
B 1 94  TYR 94  94  94  TYR TYR B . n 
B 1 95  ALA 95  95  95  ALA ALA B . n 
B 1 96  ARG 96  96  96  ARG ARG B . n 
B 1 97  GLN 97  97  97  GLN GLN B . n 
B 1 98  ASP 98  98  98  ASP ASP B . n 
B 1 99  LYS 99  99  99  LYS LYS B . n 
B 1 100 LYS 100 100 100 LYS LYS B . n 
B 1 101 ASP 101 101 101 ASP ASP B . n 
B 1 102 LYS 102 102 102 LYS LYS B . n 
B 1 103 SER 103 103 103 SER SER B . n 
B 1 104 ARG 104 104 104 ARG ARG B . n 
B 1 105 ALA 105 105 105 ALA ALA B . n 
B 1 106 PRO 106 106 106 PRO PRO B . n 
B 1 107 ILE 107 107 107 ILE ILE B . n 
B 1 108 SER 108 108 108 SER SER B . n 
B 1 109 ALA 109 109 109 ALA ALA B . n 
B 1 110 LYS 110 110 110 LYS LYS B . n 
B 1 111 LEU 111 111 111 LEU LEU B . n 
B 1 112 VAL 112 112 112 VAL VAL B . n 
B 1 113 ALA 113 113 113 ALA ALA B . n 
B 1 114 ASN 114 114 114 ASN ASN B . n 
B 1 115 MET 115 115 115 MET MET B . n 
B 1 116 LEU 116 116 116 LEU LEU B . n 
B 1 117 SER 117 117 117 SER SER B . n 
B 1 118 VAL 118 118 118 VAL VAL B . n 
B 1 119 ALA 119 119 119 ALA ALA B . n 
B 1 120 GLY 120 120 120 GLY GLY B . n 
B 1 121 ALA 121 121 121 ALA ALA B . n 
B 1 122 ASP 122 122 122 ASP ASP B . n 
B 1 123 HIS 123 123 123 HIS HIS B . n 
B 1 124 ILE 124 124 124 ILE ILE B . n 
B 1 125 ILE 125 125 125 ILE ILE B . n 
B 1 126 THR 126 126 126 THR THR B . n 
B 1 127 MET 127 127 127 MET MET B . n 
B 1 128 ASP 128 128 128 ASP ASP B . n 
B 1 129 LEU 129 129 129 LEU LEU B . n 
B 1 130 HIS 130 130 130 HIS HIS B . n 
B 1 131 ALA 131 131 131 ALA ALA B . n 
B 1 132 SER 132 132 132 SER SER B . n 
B 1 133 PRO 133 133 133 PRO PRO B . n 
B 1 134 ILE 134 134 134 ILE ILE B . n 
B 1 135 GLN 135 135 135 GLN GLN B . n 
B 1 136 GLY 136 136 136 GLY GLY B . n 
B 1 137 PHE 137 137 137 PHE PHE B . n 
B 1 138 PHE 138 138 138 PHE PHE B . n 
B 1 139 ASP 139 139 139 ASP ASP B . n 
B 1 140 ILE 140 140 140 ILE ILE B . n 
B 1 141 PRO 141 141 141 PRO PRO B . n 
B 1 142 VAL 142 142 142 VAL VAL B . n 
B 1 143 ASP 143 143 143 ASP ASP B . n 
B 1 144 ASN 144 144 144 ASN ASN B . n 
B 1 145 LEU 145 145 145 LEU LEU B . n 
B 1 146 TYR 146 146 146 TYR TYR B . n 
B 1 147 ALA 147 147 147 ALA ALA B . n 
B 1 148 GLU 148 148 148 GLU GLU B . n 
B 1 149 PRO 149 149 149 PRO PRO B . n 
B 1 150 ALA 150 150 150 ALA ALA B . n 
B 1 151 VAL 151 151 151 VAL VAL B . n 
B 1 152 LEU 152 152 152 LEU LEU B . n 
B 1 153 LYS 153 153 153 LYS LYS B . n 
B 1 154 TRP 154 154 154 TRP TRP B . n 
B 1 155 ILE 155 155 155 ILE ILE B . n 
B 1 156 ARG 156 156 156 ARG ARG B . n 
B 1 157 GLU 157 157 157 GLU GLU B . n 
B 1 158 ASN 158 158 158 ASN ASN B . n 
B 1 159 ILE 159 159 159 ILE ILE B . n 
B 1 160 SER 160 160 160 SER SER B . n 
B 1 161 GLU 161 161 161 GLU GLU B . n 
B 1 162 TRP 162 162 162 TRP TRP B . n 
B 1 163 ARG 163 163 163 ARG ARG B . n 
B 1 164 ASN 164 164 164 ASN ASN B . n 
B 1 165 CYS 165 165 165 CYS CYS B . n 
B 1 166 THR 166 166 166 THR THR B . n 
B 1 167 ILE 167 167 167 ILE ILE B . n 
B 1 168 VAL 168 168 168 VAL VAL B . n 
B 1 169 SER 169 169 169 SER SER B . n 
B 1 170 PRO 170 170 170 PRO PRO B . n 
B 1 171 ASP 171 171 171 ASP ASP B . n 
B 1 172 ALA 172 172 172 ALA ALA B . n 
B 1 173 GLY 173 173 173 GLY GLY B . n 
B 1 174 GLY 174 174 174 GLY GLY B . n 
B 1 175 ALA 175 175 175 ALA ALA B . n 
B 1 176 LYS 176 176 176 LYS LYS B . n 
B 1 177 ARG 177 177 177 ARG ARG B . n 
B 1 178 VAL 178 178 178 VAL VAL B . n 
B 1 179 THR 179 179 179 THR THR B . n 
B 1 180 SER 180 180 180 SER SER B . n 
B 1 181 ILE 181 181 181 ILE ILE B . n 
B 1 182 ALA 182 182 182 ALA ALA B . n 
B 1 183 ASP 183 183 183 ASP ASP B . n 
B 1 184 ARG 184 184 184 ARG ARG B . n 
B 1 185 LEU 185 185 185 LEU LEU B . n 
B 1 186 ASN 186 186 186 ASN ASN B . n 
B 1 187 VAL 187 187 187 VAL VAL B . n 
B 1 188 ASP 188 188 188 ASP ASP B . n 
B 1 189 PHE 189 189 189 PHE PHE B . n 
B 1 190 ALA 190 190 190 ALA ALA B . n 
B 1 191 LEU 191 191 191 LEU LEU B . n 
B 1 192 ILE 192 192 192 ILE ILE B . n 
B 1 193 HIS 193 193 193 HIS HIS B . n 
B 1 194 LYS 194 194 194 LYS LYS B . n 
B 1 195 GLU 195 195 195 GLU GLU B . n 
B 1 196 ARG 196 196 196 ARG ARG B . n 
B 1 197 LYS 197 197 ?   ?   ?   B . n 
B 1 198 LYS 198 198 ?   ?   ?   B . n 
B 1 199 ALA 199 199 ?   ?   ?   B . n 
B 1 200 ASN 200 200 ?   ?   ?   B . n 
B 1 201 GLU 201 201 ?   ?   ?   B . n 
B 1 202 VAL 202 202 ?   ?   ?   B . n 
B 1 203 ASP 203 203 ?   ?   ?   B . n 
B 1 204 ARG 204 204 204 ARG ARG B . n 
B 1 205 MET 205 205 205 MET MET B . n 
B 1 206 VAL 206 206 206 VAL VAL B . n 
B 1 207 LEU 207 207 207 LEU LEU B . n 
B 1 208 VAL 208 208 208 VAL VAL B . n 
B 1 209 GLY 209 209 209 GLY GLY B . n 
B 1 210 ASP 210 210 210 ASP ASP B . n 
B 1 211 VAL 211 211 211 VAL VAL B . n 
B 1 212 LYS 212 212 212 LYS LYS B . n 
B 1 213 ASP 213 213 213 ASP ASP B . n 
B 1 214 ARG 214 214 214 ARG ARG B . n 
B 1 215 VAL 215 215 215 VAL VAL B . n 
B 1 216 ALA 216 216 216 ALA ALA B . n 
B 1 217 ILE 217 217 217 ILE ILE B . n 
B 1 218 LEU 218 218 218 LEU LEU B . n 
B 1 219 VAL 219 219 219 VAL VAL B . n 
B 1 220 ASP 220 220 220 ASP ASP B . n 
B 1 221 ASP 221 221 221 ASP ASP B . n 
B 1 222 MET 222 222 222 MET MET B . n 
B 1 223 ALA 223 223 223 ALA ALA B . n 
B 1 224 ASP 224 224 224 ASP ASP B . n 
B 1 225 THR 225 225 225 THR THR B . n 
B 1 226 CYS 226 226 226 CYS CYS B . n 
B 1 227 GLY 227 227 227 GLY GLY B . n 
B 1 228 THR 228 228 228 THR THR B . n 
B 1 229 ILE 229 229 229 ILE ILE B . n 
B 1 230 CYS 230 230 230 CYS CYS B . n 
B 1 231 HIS 231 231 231 HIS HIS B . n 
B 1 232 ALA 232 232 232 ALA ALA B . n 
B 1 233 ALA 233 233 233 ALA ALA B . n 
B 1 234 ASP 234 234 234 ASP ASP B . n 
B 1 235 LYS 235 235 235 LYS LYS B . n 
B 1 236 LEU 236 236 236 LEU LEU B . n 
B 1 237 LEU 237 237 237 LEU LEU B . n 
B 1 238 SER 238 238 238 SER SER B . n 
B 1 239 ALA 239 239 239 ALA ALA B . n 
B 1 240 GLY 240 240 240 GLY GLY 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 ARG 243 243 243 ARG ARG B . n 
B 1 244 VAL 244 244 244 VAL VAL B . n 
B 1 245 TYR 245 245 245 TYR TYR B . n 
B 1 246 ALA 246 246 246 ALA ALA B . n 
B 1 247 ILE 247 247 247 ILE ILE B . n 
B 1 248 LEU 248 248 248 LEU LEU B . n 
B 1 249 THR 249 249 249 THR THR B . n 
B 1 250 HIS 250 250 250 HIS HIS B . n 
B 1 251 GLY 251 251 251 GLY GLY B . n 
B 1 252 ILE 252 252 252 ILE ILE B . n 
B 1 253 PHE 253 253 253 PHE PHE B . n 
B 1 254 SER 254 254 254 SER SER B . n 
B 1 255 GLY 255 255 255 GLY GLY B . n 
B 1 256 PRO 256 256 256 PRO PRO B . n 
B 1 257 ALA 257 257 257 ALA ALA B . n 
B 1 258 ILE 258 258 258 ILE ILE B . n 
B 1 259 SER 259 259 259 SER SER B . n 
B 1 260 ARG 260 260 260 ARG ARG B . n 
B 1 261 ILE 261 261 261 ILE ILE B . n 
B 1 262 ASN 262 262 262 ASN ASN B . n 
B 1 263 ASN 263 263 263 ASN ASN B . n 
B 1 264 ALA 264 264 264 ALA ALA B . n 
B 1 265 CYS 265 265 265 CYS CYS B . n 
B 1 266 PHE 266 266 266 PHE PHE B . n 
B 1 267 GLU 267 267 267 GLU GLU B . n 
B 1 268 ALA 268 268 268 ALA ALA B . n 
B 1 269 VAL 269 269 269 VAL VAL B . n 
B 1 270 VAL 270 270 270 VAL VAL B . n 
B 1 271 VAL 271 271 271 VAL VAL B . n 
B 1 272 THR 272 272 272 THR THR B . n 
B 1 273 ASN 273 273 273 ASN ASN B . n 
B 1 274 THR 274 274 274 THR THR B . n 
B 1 275 ILE 275 275 275 ILE ILE B . n 
B 1 276 PRO 276 276 276 PRO PRO B . n 
B 1 277 GLN 277 277 277 GLN GLN B . n 
B 1 278 GLU 278 278 278 GLU GLU B . n 
B 1 279 ASP 279 279 279 ASP ASP B . n 
B 1 280 LYS 280 280 280 LYS LYS B . n 
B 1 281 MET 281 281 281 MET MET B . n 
B 1 282 LYS 282 282 282 LYS LYS B . n 
B 1 283 HIS 283 283 283 HIS HIS B . n 
B 1 284 CYS 284 284 284 CYS CYS B . n 
B 1 285 SER 285 285 285 SER SER B . n 
B 1 286 LYS 286 286 286 LYS LYS B . n 
B 1 287 ILE 287 287 287 ILE ILE B . n 
B 1 288 GLN 288 288 288 GLN GLN B . n 
B 1 289 VAL 289 289 289 VAL VAL B . n 
B 1 290 ILE 290 290 290 ILE ILE B . n 
B 1 291 ASP 291 291 291 ASP ASP B . n 
B 1 292 ILE 292 292 292 ILE ILE B . n 
B 1 293 SER 293 293 293 SER SER B . n 
B 1 294 MET 294 294 294 MET MET B . n 
B 1 295 ILE 295 295 295 ILE ILE B . n 
B 1 296 LEU 296 296 296 LEU LEU B . n 
B 1 297 ALA 297 297 297 ALA ALA B . n 
B 1 298 GLU 298 298 298 GLU GLU B . n 
B 1 299 ALA 299 299 299 ALA ALA B . n 
B 1 300 ILE 300 300 300 ILE ILE B . n 
B 1 301 ARG 301 301 301 ARG ARG B . n 
B 1 302 ARG 302 302 302 ARG ARG B . n 
B 1 303 THR 303 303 303 THR THR B . n 
B 1 304 HIS 304 304 304 HIS HIS B . n 
B 1 305 ASN 305 305 305 ASN ASN B . n 
B 1 306 GLY 306 306 306 GLY GLY B . n 
B 1 307 GLU 307 307 307 GLU GLU B . n 
B 1 308 SER 308 308 308 SER SER B . n 
B 1 309 VAL 309 309 309 VAL VAL B . n 
B 1 310 SER 310 310 310 SER SER B . n 
B 1 311 TYR 311 311 311 TYR TYR B . n 
B 1 312 LEU 312 312 312 LEU LEU B . n 
B 1 313 PHE 313 313 313 PHE PHE B . n 
B 1 314 SER 314 314 314 SER SER B . n 
B 1 315 HIS 315 315 315 HIS HIS B . n 
B 1 316 VAL 316 316 316 VAL VAL B . n 
B 1 317 PRO 317 317 317 PRO PRO B . n 
B 1 318 LEU 318 318 ?   ?   ?   B . n 
B 1 319 LEU 319 319 ?   ?   ?   B . n 
B 1 320 GLU 320 320 ?   ?   ?   B . n 
B 1 321 HIS 321 321 ?   ?   ?   B . n 
B 1 322 HIS 322 322 ?   ?   ?   B . n 
B 1 323 HIS 323 323 ?   ?   ?   B . n 
B 1 324 HIS 324 324 ?   ?   ?   B . n 
B 1 325 HIS 325 325 ?   ?   ?   B . n 
B 1 326 HIS 326 326 ?   ?   ?   B . n 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   hexameric 
_pdbx_struct_assembly.oligomeric_count     6 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2,3 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H 
# 
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)' 27260 ? 
1 MORE         -320  ? 
1 'SSA (A^2)'  61030 ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z     1.0000000000  0.0000000000  0.0000000000 0.0000000000 0.0000000000  1.0000000000  
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 
2 'crystal symmetry operation' 2_555 -y,x-y,z  -0.5000000000 -0.8660254038 0.0000000000 0.0000000000 0.8660254038  -0.5000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 
3 'crystal symmetry operation' 3_555 -x+y,-x,z -0.5000000000 0.8660254038  0.0000000000 0.0000000000 -0.8660254038 -0.5000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2015-02-04 
2 'Structure model' 1 1 2015-03-25 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
HKL-2000 'data collection' .        ? 1 
MOLREP   phasing           .        ? 2 
REFMAC   refinement        5.5.0109 ? 3 
HKL-2000 'data reduction'  .        ? 4 
HKL-2000 'data scaling'    .        ? 5 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   CB 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   SER 
_pdbx_validate_close_contact.auth_seq_id_1    10 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   CB 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   SER 
_pdbx_validate_close_contact.auth_seq_id_2    58 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             1.59 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             N 
_pdbx_validate_rmsd_angle.auth_asym_id_1             A 
_pdbx_validate_rmsd_angle.auth_comp_id_1             GLN 
_pdbx_validate_rmsd_angle.auth_seq_id_1              13 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CA 
_pdbx_validate_rmsd_angle.auth_asym_id_2             A 
_pdbx_validate_rmsd_angle.auth_comp_id_2             GLN 
_pdbx_validate_rmsd_angle.auth_seq_id_2              13 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             CB 
_pdbx_validate_rmsd_angle.auth_asym_id_3             A 
_pdbx_validate_rmsd_angle.auth_comp_id_3             GLN 
_pdbx_validate_rmsd_angle.auth_seq_id_3              13 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                96.00 
_pdbx_validate_rmsd_angle.angle_target_value         110.60 
_pdbx_validate_rmsd_angle.angle_deviation            -14.60 
_pdbx_validate_rmsd_angle.angle_standard_deviation   1.80 
_pdbx_validate_rmsd_angle.linker_flag                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 SER A 10  ? ? -170.40 -162.45 
2  1 ASN A 37  ? ? -96.42  38.56   
3  1 GLN A 38  ? ? 59.43   1.94    
4  1 SER A 58  ? ? -84.40  -71.10  
5  1 ASP A 128 ? ? 33.64   69.21   
6  1 PRO A 133 ? ? -68.52  1.78    
7  1 GLU A 161 ? ? -91.09  43.56   
8  1 ASP A 224 ? ? -93.54  -76.22  
9  1 CYS A 226 ? ? 66.17   -4.42   
10 1 ASN A 273 ? ? -79.23  42.05   
11 1 CYS A 284 ? ? -171.17 122.28  
12 1 SER B 10  ? ? 47.85   -130.94 
13 1 GLN B 13  ? ? -102.44 49.24   
14 1 SER B 36  ? ? -44.64  -19.25  
15 1 GLN B 38  ? ? 86.02   13.20   
16 1 GLN B 97  ? ? -111.06 74.27   
17 1 ARG B 104 ? ? -99.52  51.11   
18 1 ASP B 128 ? ? 35.04   58.65   
19 1 PRO B 133 ? ? -65.18  9.32    
20 1 ASN B 273 ? ? -96.26  40.40   
21 1 SER B 314 ? ? -149.30 -4.66   
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1 1 Y 1 A SER 10 ? OG ? A SER 10 OG 
2 1 Y 1 A SER 58 ? OG ? A SER 58 OG 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET 1   ? A MET 1   
2  1 Y 1 A PRO 2   ? A PRO 2   
3  1 Y 1 A ARG 196 ? A ARG 196 
4  1 Y 1 A LYS 197 ? A LYS 197 
5  1 Y 1 A LYS 198 ? A LYS 198 
6  1 Y 1 A ALA 199 ? A ALA 199 
7  1 Y 1 A ASN 200 ? A ASN 200 
8  1 Y 1 A GLU 201 ? A GLU 201 
9  1 Y 1 A VAL 202 ? A VAL 202 
10 1 Y 1 A PHE 313 ? A PHE 313 
11 1 Y 1 A SER 314 ? A SER 314 
12 1 Y 1 A HIS 315 ? A HIS 315 
13 1 Y 1 A VAL 316 ? A VAL 316 
14 1 Y 1 A PRO 317 ? A PRO 317 
15 1 Y 1 A LEU 318 ? A LEU 318 
16 1 Y 1 A LEU 319 ? A LEU 319 
17 1 Y 1 A GLU 320 ? A GLU 320 
18 1 Y 1 A HIS 321 ? A HIS 321 
19 1 Y 1 A HIS 322 ? A HIS 322 
20 1 Y 1 A HIS 323 ? A HIS 323 
21 1 Y 1 A HIS 324 ? A HIS 324 
22 1 Y 1 A HIS 325 ? A HIS 325 
23 1 Y 1 A HIS 326 ? A HIS 326 
24 1 Y 1 B MET 1   ? B MET 1   
25 1 Y 1 B PRO 2   ? B PRO 2   
26 1 Y 1 B LYS 197 ? B LYS 197 
27 1 Y 1 B LYS 198 ? B LYS 198 
28 1 Y 1 B ALA 199 ? B ALA 199 
29 1 Y 1 B ASN 200 ? B ASN 200 
30 1 Y 1 B GLU 201 ? B GLU 201 
31 1 Y 1 B VAL 202 ? B VAL 202 
32 1 Y 1 B ASP 203 ? B ASP 203 
33 1 Y 1 B LEU 318 ? B LEU 318 
34 1 Y 1 B LEU 319 ? B LEU 319 
35 1 Y 1 B GLU 320 ? B GLU 320 
36 1 Y 1 B HIS 321 ? B HIS 321 
37 1 Y 1 B HIS 322 ? B HIS 322 
38 1 Y 1 B HIS 323 ? B HIS 323 
39 1 Y 1 B HIS 324 ? B HIS 324 
40 1 Y 1 B HIS 325 ? B HIS 325 
41 1 Y 1 B HIS 326 ? B HIS 326 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'SULFATE ION' SO4 
3 water         HOH 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 SO4 1  1001 1001 SO4 SO4 A . 
D 2 SO4 1  1002 1004 SO4 SO4 A . 
E 2 SO4 1  401  1002 SO4 SO4 B . 
F 2 SO4 1  402  1003 SO4 SO4 B . 
G 3 HOH 1  1101 7    HOH HOH A . 
G 3 HOH 2  1102 18   HOH HOH A . 
G 3 HOH 3  1103 24   HOH HOH A . 
G 3 HOH 4  1104 26   HOH HOH A . 
G 3 HOH 5  1105 1    HOH HOH A . 
H 3 HOH 1  501  1    HOH HOH B . 
H 3 HOH 2  502  2    HOH HOH B . 
H 3 HOH 3  503  4    HOH HOH B . 
H 3 HOH 4  504  6    HOH HOH B . 
H 3 HOH 5  505  8    HOH HOH B . 
H 3 HOH 6  506  9    HOH HOH B . 
H 3 HOH 7  507  13   HOH HOH B . 
H 3 HOH 8  508  20   HOH HOH B . 
H 3 HOH 9  509  23   HOH HOH B . 
H 3 HOH 10 510  1    HOH HOH B . 
# 
