data_9K7O
# 
_entry.id   9K7O 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.398 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9K7O         pdb_00009k7o 10.2210/pdb9k7o/pdb 
WWPDB D_1300052935 ?            ?                   
# 
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 2024-11-06 
2 'Structure model' 1 1 2024-11-20 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Database references' 
2 2 'Structure model' 'Structure summary'   
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' audit_author        
2 2 'Structure model' citation_author     
3 2 'Structure model' pdbx_contact_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_audit_author.name'              
2 2 'Structure model' '_citation_author.name'           
3 2 'Structure model' '_pdbx_contact_author.name_first' 
4 2 'Structure model' '_pdbx_contact_author.name_last'  
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9K7O 
_pdbx_database_status.recvd_initial_deposition_date   2024-10-24 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              tonozuka@cc.tuat.ac.jp 
_pdbx_contact_author.name_first         Takashi 
_pdbx_contact_author.name_last          Tonozuka 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-5422-7548 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Shiojima, Y.' 1 0009-0004-0986-6764 
'Tonozuka, T.' 2 0000-0002-5422-7548 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
'Crystal structure of CcGH131B, a protein belonging to glycoside hydrolase family 131 from the basidiomycete Coprinopsis cinerea' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Shiojima, Y.' 1 0009-0004-0986-6764 
primary 'Tonozuka, T.' 2 0000-0002-5422-7548 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Glycoside hydrolase 131 catalytic N-terminal domain-containing protein' 35219.707 2   ? T87A/K247E ? 
;The original protein name: CC1G_15039 The original N-terminal signal peptide is removed in the expression vector. Met is artificially placed at the N-terminus, and C-terminal tag sequence is AAALEHHHHHH. In the sequence of CC1G_15039 in the databese, the 87th and the 247th residues are Thr and Lys, while these residues are Ala and Glu, respectively, in this study.
;
2 non-polymer syn 'DI(HYDROXYETHYL)ETHER'                                                  106.120   2   ? ?          ? ? 
3 water       nat water                                                                    18.015    458 ? ?          ? ? 
# 
_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       
;MGKVLWDGRAPRNYTSFHLDASVDPYLTVVKGPRAASIYTRLLGREVTPTPLWNDRLFPEVPYPAVSTEQALLVLIGNSS
VFTPGSSGRPQTGFRRTELIAQVNGSNIDLIPIIGKGRVAFHFSVLMDEWHKLDMIHEHQLVFVEPSDGSHVFTLQVGSP
FTNPTGPLPAPRADWLKILNHNLDVLFETEFTDETWHNFAVIVDWEKRTLQVWYSQNENNLVWVTPVLPNETVKRGTAGR
GDFHFGILKLPLVNVADPPEVRDDVVHYGIQPPTTHGIMYSGVFIEDLEDGLSVGNKFIQEVAAALEHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MGKVLWDGRAPRNYTSFHLDASVDPYLTVVKGPRAASIYTRLLGREVTPTPLWNDRLFPEVPYPAVSTEQALLVLIGNSS
VFTPGSSGRPQTGFRRTELIAQVNGSNIDLIPIIGKGRVAFHFSVLMDEWHKLDMIHEHQLVFVEPSDGSHVFTLQVGSP
FTNPTGPLPAPRADWLKILNHNLDVLFETEFTDETWHNFAVIVDWEKRTLQVWYSQNENNLVWVTPVLPNETVKRGTAGR
GDFHFGILKLPLVNVADPPEVRDDVVHYGIQPPTTHGIMYSGVFIEDLEDGLSVGNKFIQEVAAALEHHHHHH
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'DI(HYDROXYETHYL)ETHER' PEG 
3 water                   HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   GLY n 
1 3   LYS n 
1 4   VAL n 
1 5   LEU n 
1 6   TRP n 
1 7   ASP n 
1 8   GLY n 
1 9   ARG n 
1 10  ALA n 
1 11  PRO n 
1 12  ARG n 
1 13  ASN n 
1 14  TYR n 
1 15  THR n 
1 16  SER n 
1 17  PHE n 
1 18  HIS n 
1 19  LEU n 
1 20  ASP n 
1 21  ALA n 
1 22  SER n 
1 23  VAL n 
1 24  ASP n 
1 25  PRO n 
1 26  TYR n 
1 27  LEU n 
1 28  THR n 
1 29  VAL n 
1 30  VAL n 
1 31  LYS n 
1 32  GLY n 
1 33  PRO n 
1 34  ARG n 
1 35  ALA n 
1 36  ALA n 
1 37  SER n 
1 38  ILE n 
1 39  TYR n 
1 40  THR n 
1 41  ARG n 
1 42  LEU n 
1 43  LEU n 
1 44  GLY n 
1 45  ARG n 
1 46  GLU n 
1 47  VAL n 
1 48  THR n 
1 49  PRO n 
1 50  THR n 
1 51  PRO n 
1 52  LEU n 
1 53  TRP n 
1 54  ASN n 
1 55  ASP n 
1 56  ARG n 
1 57  LEU n 
1 58  PHE n 
1 59  PRO n 
1 60  GLU n 
1 61  VAL n 
1 62  PRO n 
1 63  TYR n 
1 64  PRO n 
1 65  ALA n 
1 66  VAL n 
1 67  SER n 
1 68  THR n 
1 69  GLU n 
1 70  GLN n 
1 71  ALA n 
1 72  LEU n 
1 73  LEU n 
1 74  VAL n 
1 75  LEU n 
1 76  ILE n 
1 77  GLY n 
1 78  ASN n 
1 79  SER n 
1 80  SER n 
1 81  VAL n 
1 82  PHE n 
1 83  THR n 
1 84  PRO n 
1 85  GLY n 
1 86  SER n 
1 87  SER n 
1 88  GLY n 
1 89  ARG n 
1 90  PRO n 
1 91  GLN n 
1 92  THR n 
1 93  GLY n 
1 94  PHE n 
1 95  ARG n 
1 96  ARG n 
1 97  THR n 
1 98  GLU n 
1 99  LEU n 
1 100 ILE n 
1 101 ALA n 
1 102 GLN n 
1 103 VAL n 
1 104 ASN n 
1 105 GLY n 
1 106 SER n 
1 107 ASN n 
1 108 ILE n 
1 109 ASP n 
1 110 LEU n 
1 111 ILE n 
1 112 PRO n 
1 113 ILE n 
1 114 ILE n 
1 115 GLY n 
1 116 LYS n 
1 117 GLY n 
1 118 ARG n 
1 119 VAL n 
1 120 ALA n 
1 121 PHE n 
1 122 HIS n 
1 123 PHE n 
1 124 SER n 
1 125 VAL n 
1 126 LEU n 
1 127 MET n 
1 128 ASP n 
1 129 GLU n 
1 130 TRP n 
1 131 HIS n 
1 132 LYS n 
1 133 LEU n 
1 134 ASP n 
1 135 MET n 
1 136 ILE n 
1 137 HIS n 
1 138 GLU n 
1 139 HIS n 
1 140 GLN n 
1 141 LEU n 
1 142 VAL n 
1 143 PHE n 
1 144 VAL n 
1 145 GLU n 
1 146 PRO n 
1 147 SER n 
1 148 ASP n 
1 149 GLY n 
1 150 SER n 
1 151 HIS n 
1 152 VAL n 
1 153 PHE n 
1 154 THR n 
1 155 LEU n 
1 156 GLN n 
1 157 VAL n 
1 158 GLY n 
1 159 SER n 
1 160 PRO n 
1 161 PHE n 
1 162 THR n 
1 163 ASN n 
1 164 PRO n 
1 165 THR n 
1 166 GLY n 
1 167 PRO n 
1 168 LEU n 
1 169 PRO n 
1 170 ALA n 
1 171 PRO n 
1 172 ARG n 
1 173 ALA n 
1 174 ASP n 
1 175 TRP n 
1 176 LEU n 
1 177 LYS n 
1 178 ILE n 
1 179 LEU n 
1 180 ASN n 
1 181 HIS n 
1 182 ASN n 
1 183 LEU n 
1 184 ASP n 
1 185 VAL n 
1 186 LEU n 
1 187 PHE n 
1 188 GLU n 
1 189 THR n 
1 190 GLU n 
1 191 PHE n 
1 192 THR n 
1 193 ASP n 
1 194 GLU n 
1 195 THR n 
1 196 TRP n 
1 197 HIS n 
1 198 ASN n 
1 199 PHE n 
1 200 ALA n 
1 201 VAL n 
1 202 ILE n 
1 203 VAL n 
1 204 ASP n 
1 205 TRP n 
1 206 GLU n 
1 207 LYS n 
1 208 ARG n 
1 209 THR n 
1 210 LEU n 
1 211 GLN n 
1 212 VAL n 
1 213 TRP n 
1 214 TYR n 
1 215 SER n 
1 216 GLN n 
1 217 ASN n 
1 218 GLU n 
1 219 ASN n 
1 220 ASN n 
1 221 LEU n 
1 222 VAL n 
1 223 TRP n 
1 224 VAL n 
1 225 THR n 
1 226 PRO n 
1 227 VAL n 
1 228 LEU n 
1 229 PRO n 
1 230 ASN n 
1 231 GLU n 
1 232 THR n 
1 233 VAL n 
1 234 LYS n 
1 235 ARG n 
1 236 GLY n 
1 237 THR n 
1 238 ALA n 
1 239 GLY n 
1 240 ARG n 
1 241 GLY n 
1 242 ASP n 
1 243 PHE n 
1 244 HIS n 
1 245 PHE n 
1 246 GLY n 
1 247 ILE n 
1 248 LEU n 
1 249 LYS n 
1 250 LEU n 
1 251 PRO n 
1 252 LEU n 
1 253 VAL n 
1 254 ASN n 
1 255 VAL n 
1 256 ALA n 
1 257 ASP n 
1 258 PRO n 
1 259 PRO n 
1 260 GLU n 
1 261 VAL n 
1 262 ARG n 
1 263 ASP n 
1 264 ASP n 
1 265 VAL n 
1 266 VAL n 
1 267 HIS n 
1 268 TYR n 
1 269 GLY n 
1 270 ILE n 
1 271 GLN n 
1 272 PRO n 
1 273 PRO n 
1 274 THR n 
1 275 THR n 
1 276 HIS n 
1 277 GLY n 
1 278 ILE n 
1 279 MET n 
1 280 TYR n 
1 281 SER n 
1 282 GLY n 
1 283 VAL n 
1 284 PHE n 
1 285 ILE n 
1 286 GLU n 
1 287 ASP n 
1 288 LEU n 
1 289 GLU n 
1 290 ASP n 
1 291 GLY n 
1 292 LEU n 
1 293 SER n 
1 294 VAL n 
1 295 GLY n 
1 296 ASN n 
1 297 LYS n 
1 298 PHE n 
1 299 ILE n 
1 300 GLN n 
1 301 GLU n 
1 302 VAL n 
1 303 ALA n 
1 304 ALA n 
1 305 ALA n 
1 306 LEU n 
1 307 GLU n 
1 308 HIS n 
1 309 HIS n 
1 310 HIS n 
1 311 HIS n 
1 312 HIS n 
1 313 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                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   313 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 CC1G_15039 
_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      'Coprinopsis cinerea (strain Okayama-7 / 130 / ATCC MYA-4618 / FGSC 9003)' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     240176 
_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          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                 ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE                ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE              ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'         ? 'C4 H7 N O4'     133.103 
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 
PEG non-polymer         . 'DI(HYDROXYETHYL)ETHER' ? 'C4 H10 O3'      106.120 
PHE 'L-peptide linking' y PHENYLALANINE           ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE                 ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE                  ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE               ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN              ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE                ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE                  ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   17  ?   ?   ?   A . n 
A 1 2   GLY 2   18  18  GLY GLY A . n 
A 1 3   LYS 3   19  19  LYS LYS A . n 
A 1 4   VAL 4   20  20  VAL VAL A . n 
A 1 5   LEU 5   21  21  LEU LEU A . n 
A 1 6   TRP 6   22  22  TRP TRP A . n 
A 1 7   ASP 7   23  23  ASP ASP A . n 
A 1 8   GLY 8   24  24  GLY GLY A . n 
A 1 9   ARG 9   25  25  ARG ARG A . n 
A 1 10  ALA 10  26  26  ALA ALA A . n 
A 1 11  PRO 11  27  27  PRO PRO A . n 
A 1 12  ARG 12  28  28  ARG ARG A . n 
A 1 13  ASN 13  29  29  ASN ASN A . n 
A 1 14  TYR 14  30  30  TYR TYR A . n 
A 1 15  THR 15  31  31  THR THR A . n 
A 1 16  SER 16  32  32  SER SER A . n 
A 1 17  PHE 17  33  33  PHE PHE A . n 
A 1 18  HIS 18  34  34  HIS HIS A . n 
A 1 19  LEU 19  35  35  LEU LEU A . n 
A 1 20  ASP 20  36  36  ASP ASP A . n 
A 1 21  ALA 21  37  37  ALA ALA A . n 
A 1 22  SER 22  38  38  SER SER A . n 
A 1 23  VAL 23  39  39  VAL VAL A . n 
A 1 24  ASP 24  40  40  ASP ASP A . n 
A 1 25  PRO 25  41  41  PRO PRO A . n 
A 1 26  TYR 26  42  42  TYR TYR A . n 
A 1 27  LEU 27  43  43  LEU LEU A . n 
A 1 28  THR 28  44  44  THR THR A . n 
A 1 29  VAL 29  45  45  VAL VAL A . n 
A 1 30  VAL 30  46  46  VAL VAL A . n 
A 1 31  LYS 31  47  47  LYS LYS A . n 
A 1 32  GLY 32  48  48  GLY GLY A . n 
A 1 33  PRO 33  49  49  PRO PRO A . n 
A 1 34  ARG 34  50  50  ARG ARG A . n 
A 1 35  ALA 35  51  51  ALA ALA A . n 
A 1 36  ALA 36  52  52  ALA ALA A . n 
A 1 37  SER 37  53  53  SER SER A . n 
A 1 38  ILE 38  54  54  ILE ILE A . n 
A 1 39  TYR 39  55  55  TYR TYR A . n 
A 1 40  THR 40  56  56  THR THR A . n 
A 1 41  ARG 41  57  57  ARG ARG A . n 
A 1 42  LEU 42  58  58  LEU LEU A . n 
A 1 43  LEU 43  59  59  LEU LEU A . n 
A 1 44  GLY 44  60  60  GLY GLY A . n 
A 1 45  ARG 45  61  61  ARG ARG A . n 
A 1 46  GLU 46  62  62  GLU GLU A . n 
A 1 47  VAL 47  63  63  VAL VAL A . n 
A 1 48  THR 48  64  64  THR THR A . n 
A 1 49  PRO 49  65  65  PRO PRO A . n 
A 1 50  THR 50  66  66  THR THR A . n 
A 1 51  PRO 51  67  67  PRO PRO A . n 
A 1 52  LEU 52  68  68  LEU LEU A . n 
A 1 53  TRP 53  69  69  TRP TRP A . n 
A 1 54  ASN 54  70  70  ASN ASN A . n 
A 1 55  ASP 55  71  71  ASP ASP A . n 
A 1 56  ARG 56  72  72  ARG ARG A . n 
A 1 57  LEU 57  73  73  LEU LEU A . n 
A 1 58  PHE 58  74  74  PHE PHE A . n 
A 1 59  PRO 59  75  75  PRO PRO A . n 
A 1 60  GLU 60  76  76  GLU GLU A . n 
A 1 61  VAL 61  77  77  VAL VAL A . n 
A 1 62  PRO 62  78  78  PRO PRO A . n 
A 1 63  TYR 63  79  79  TYR TYR A . n 
A 1 64  PRO 64  80  80  PRO PRO A . n 
A 1 65  ALA 65  81  81  ALA ALA A . n 
A 1 66  VAL 66  82  82  VAL VAL A . n 
A 1 67  SER 67  83  83  SER SER A . n 
A 1 68  THR 68  84  84  THR THR A . n 
A 1 69  GLU 69  85  85  GLU GLU A . n 
A 1 70  GLN 70  86  86  GLN GLN A . n 
A 1 71  ALA 71  87  87  ALA ALA A . n 
A 1 72  LEU 72  88  88  LEU LEU A . n 
A 1 73  LEU 73  89  89  LEU LEU A . n 
A 1 74  VAL 74  90  90  VAL VAL A . n 
A 1 75  LEU 75  91  91  LEU LEU A . n 
A 1 76  ILE 76  92  92  ILE ILE A . n 
A 1 77  GLY 77  93  93  GLY GLY A . n 
A 1 78  ASN 78  94  94  ASN ASN A . n 
A 1 79  SER 79  95  95  SER SER A . n 
A 1 80  SER 80  96  96  SER SER A . n 
A 1 81  VAL 81  97  97  VAL VAL A . n 
A 1 82  PHE 82  98  98  PHE PHE A . n 
A 1 83  THR 83  99  99  THR THR A . n 
A 1 84  PRO 84  100 100 PRO PRO A . n 
A 1 85  GLY 85  101 101 GLY GLY A . n 
A 1 86  SER 86  102 102 SER SER A . n 
A 1 87  SER 87  103 103 SER SER A . n 
A 1 88  GLY 88  104 104 GLY GLY A . n 
A 1 89  ARG 89  105 105 ARG ARG A . n 
A 1 90  PRO 90  106 106 PRO PRO A . n 
A 1 91  GLN 91  107 107 GLN GLN A . n 
A 1 92  THR 92  108 108 THR THR A . n 
A 1 93  GLY 93  109 109 GLY GLY A . n 
A 1 94  PHE 94  110 110 PHE PHE A . n 
A 1 95  ARG 95  111 111 ARG ARG A . n 
A 1 96  ARG 96  112 112 ARG ARG A . n 
A 1 97  THR 97  113 113 THR THR A . n 
A 1 98  GLU 98  114 114 GLU GLU A . n 
A 1 99  LEU 99  115 115 LEU LEU A . n 
A 1 100 ILE 100 116 116 ILE ILE A . n 
A 1 101 ALA 101 117 117 ALA ALA A . n 
A 1 102 GLN 102 118 118 GLN GLN A . n 
A 1 103 VAL 103 119 119 VAL VAL A . n 
A 1 104 ASN 104 120 120 ASN ASN A . n 
A 1 105 GLY 105 121 121 GLY GLY A . n 
A 1 106 SER 106 122 122 SER SER A . n 
A 1 107 ASN 107 123 123 ASN ASN A . n 
A 1 108 ILE 108 124 124 ILE ILE A . n 
A 1 109 ASP 109 125 125 ASP ASP A . n 
A 1 110 LEU 110 126 126 LEU LEU A . n 
A 1 111 ILE 111 127 127 ILE ILE A . n 
A 1 112 PRO 112 128 128 PRO PRO A . n 
A 1 113 ILE 113 129 129 ILE ILE A . n 
A 1 114 ILE 114 130 130 ILE ILE A . n 
A 1 115 GLY 115 131 131 GLY GLY A . n 
A 1 116 LYS 116 132 132 LYS LYS A . n 
A 1 117 GLY 117 133 133 GLY GLY A . n 
A 1 118 ARG 118 134 134 ARG ARG A . n 
A 1 119 VAL 119 135 135 VAL VAL A . n 
A 1 120 ALA 120 136 136 ALA ALA A . n 
A 1 121 PHE 121 137 137 PHE PHE A . n 
A 1 122 HIS 122 138 138 HIS HIS A . n 
A 1 123 PHE 123 139 139 PHE PHE A . n 
A 1 124 SER 124 140 140 SER SER A . n 
A 1 125 VAL 125 141 141 VAL VAL A . n 
A 1 126 LEU 126 142 142 LEU LEU A . n 
A 1 127 MET 127 143 143 MET MET A . n 
A 1 128 ASP 128 144 144 ASP ASP A . n 
A 1 129 GLU 129 145 145 GLU GLU A . n 
A 1 130 TRP 130 146 146 TRP TRP A . n 
A 1 131 HIS 131 147 147 HIS HIS A . n 
A 1 132 LYS 132 148 148 LYS LYS A . n 
A 1 133 LEU 133 149 149 LEU LEU A . n 
A 1 134 ASP 134 150 150 ASP ASP A . n 
A 1 135 MET 135 151 151 MET MET A . n 
A 1 136 ILE 136 152 152 ILE ILE A . n 
A 1 137 HIS 137 153 153 HIS HIS A . n 
A 1 138 GLU 138 154 154 GLU GLU A . n 
A 1 139 HIS 139 155 155 HIS HIS A . n 
A 1 140 GLN 140 156 156 GLN GLN A . n 
A 1 141 LEU 141 157 157 LEU LEU A . n 
A 1 142 VAL 142 158 158 VAL VAL A . n 
A 1 143 PHE 143 159 159 PHE PHE A . n 
A 1 144 VAL 144 160 160 VAL VAL A . n 
A 1 145 GLU 145 161 161 GLU GLU A . n 
A 1 146 PRO 146 162 162 PRO PRO A . n 
A 1 147 SER 147 163 163 SER SER A . n 
A 1 148 ASP 148 164 164 ASP ASP A . n 
A 1 149 GLY 149 165 165 GLY GLY A . n 
A 1 150 SER 150 166 166 SER SER A . n 
A 1 151 HIS 151 167 167 HIS HIS A . n 
A 1 152 VAL 152 168 168 VAL VAL A . n 
A 1 153 PHE 153 169 169 PHE PHE A . n 
A 1 154 THR 154 170 170 THR THR A . n 
A 1 155 LEU 155 171 171 LEU LEU A . n 
A 1 156 GLN 156 172 172 GLN GLN A . n 
A 1 157 VAL 157 173 173 VAL VAL A . n 
A 1 158 GLY 158 174 174 GLY GLY A . n 
A 1 159 SER 159 175 175 SER SER A . n 
A 1 160 PRO 160 176 176 PRO PRO A . n 
A 1 161 PHE 161 177 177 PHE PHE A . n 
A 1 162 THR 162 178 178 THR THR A . n 
A 1 163 ASN 163 179 179 ASN ASN A . n 
A 1 164 PRO 164 180 180 PRO PRO A . n 
A 1 165 THR 165 181 181 THR THR A . n 
A 1 166 GLY 166 182 182 GLY GLY A . n 
A 1 167 PRO 167 183 183 PRO PRO A . n 
A 1 168 LEU 168 184 184 LEU LEU A . n 
A 1 169 PRO 169 185 185 PRO PRO A . n 
A 1 170 ALA 170 186 186 ALA ALA A . n 
A 1 171 PRO 171 187 187 PRO PRO A . n 
A 1 172 ARG 172 188 188 ARG ARG A . n 
A 1 173 ALA 173 189 189 ALA ALA A . n 
A 1 174 ASP 174 190 190 ASP ASP A . n 
A 1 175 TRP 175 191 191 TRP TRP A . n 
A 1 176 LEU 176 192 192 LEU LEU A . n 
A 1 177 LYS 177 193 193 LYS LYS A . n 
A 1 178 ILE 178 194 194 ILE ILE A . n 
A 1 179 LEU 179 195 195 LEU LEU A . n 
A 1 180 ASN 180 196 196 ASN ASN A . n 
A 1 181 HIS 181 197 197 HIS HIS A . n 
A 1 182 ASN 182 198 198 ASN ASN A . n 
A 1 183 LEU 183 199 199 LEU LEU A . n 
A 1 184 ASP 184 200 200 ASP ASP A . n 
A 1 185 VAL 185 201 201 VAL VAL A . n 
A 1 186 LEU 186 202 202 LEU LEU A . n 
A 1 187 PHE 187 203 203 PHE PHE A . n 
A 1 188 GLU 188 204 204 GLU GLU A . n 
A 1 189 THR 189 205 205 THR THR A . n 
A 1 190 GLU 190 206 206 GLU GLU A . n 
A 1 191 PHE 191 207 207 PHE PHE A . n 
A 1 192 THR 192 208 208 THR THR A . n 
A 1 193 ASP 193 209 209 ASP ASP A . n 
A 1 194 GLU 194 210 210 GLU GLU A . n 
A 1 195 THR 195 211 211 THR THR A . n 
A 1 196 TRP 196 212 212 TRP TRP A . n 
A 1 197 HIS 197 213 213 HIS HIS A . n 
A 1 198 ASN 198 214 214 ASN ASN A . n 
A 1 199 PHE 199 215 215 PHE PHE A . n 
A 1 200 ALA 200 216 216 ALA ALA A . n 
A 1 201 VAL 201 217 217 VAL VAL A . n 
A 1 202 ILE 202 218 218 ILE ILE A . n 
A 1 203 VAL 203 219 219 VAL VAL A . n 
A 1 204 ASP 204 220 220 ASP ASP A . n 
A 1 205 TRP 205 221 221 TRP TRP A . n 
A 1 206 GLU 206 222 222 GLU GLU A . n 
A 1 207 LYS 207 223 223 LYS LYS A . n 
A 1 208 ARG 208 224 224 ARG ARG A . n 
A 1 209 THR 209 225 225 THR THR A . n 
A 1 210 LEU 210 226 226 LEU LEU A . n 
A 1 211 GLN 211 227 227 GLN GLN A . n 
A 1 212 VAL 212 228 228 VAL VAL A . n 
A 1 213 TRP 213 229 229 TRP TRP A . n 
A 1 214 TYR 214 230 230 TYR TYR A . n 
A 1 215 SER 215 231 231 SER SER A . n 
A 1 216 GLN 216 232 232 GLN GLN A . n 
A 1 217 ASN 217 233 233 ASN ASN A . n 
A 1 218 GLU 218 234 234 GLU GLU A . n 
A 1 219 ASN 219 235 235 ASN ASN A . n 
A 1 220 ASN 220 236 236 ASN ASN A . n 
A 1 221 LEU 221 237 237 LEU LEU A . n 
A 1 222 VAL 222 238 238 VAL VAL A . n 
A 1 223 TRP 223 239 239 TRP TRP A . n 
A 1 224 VAL 224 240 240 VAL VAL A . n 
A 1 225 THR 225 241 241 THR THR A . n 
A 1 226 PRO 226 242 242 PRO PRO A . n 
A 1 227 VAL 227 243 243 VAL VAL A . n 
A 1 228 LEU 228 244 244 LEU LEU A . n 
A 1 229 PRO 229 245 245 PRO PRO A . n 
A 1 230 ASN 230 246 246 ASN ASN A . n 
A 1 231 GLU 231 247 247 GLU GLU A . n 
A 1 232 THR 232 248 248 THR THR A . n 
A 1 233 VAL 233 249 249 VAL VAL A . n 
A 1 234 LYS 234 250 250 LYS LYS A . n 
A 1 235 ARG 235 251 251 ARG ARG A . n 
A 1 236 GLY 236 252 252 GLY GLY A . n 
A 1 237 THR 237 253 253 THR THR A . n 
A 1 238 ALA 238 254 254 ALA ALA A . n 
A 1 239 GLY 239 255 255 GLY GLY A . n 
A 1 240 ARG 240 256 256 ARG ARG A . n 
A 1 241 GLY 241 257 257 GLY GLY A . n 
A 1 242 ASP 242 258 258 ASP ASP A . n 
A 1 243 PHE 243 259 259 PHE PHE A . n 
A 1 244 HIS 244 260 260 HIS HIS A . n 
A 1 245 PHE 245 261 261 PHE PHE A . n 
A 1 246 GLY 246 262 262 GLY GLY A . n 
A 1 247 ILE 247 263 263 ILE ILE A . n 
A 1 248 LEU 248 264 264 LEU LEU A . n 
A 1 249 LYS 249 265 265 LYS LYS A . n 
A 1 250 LEU 250 266 266 LEU LEU A . n 
A 1 251 PRO 251 267 267 PRO PRO A . n 
A 1 252 LEU 252 268 268 LEU LEU A . n 
A 1 253 VAL 253 269 269 VAL VAL A . n 
A 1 254 ASN 254 270 270 ASN ASN A . n 
A 1 255 VAL 255 271 271 VAL VAL A . n 
A 1 256 ALA 256 272 272 ALA ALA A . n 
A 1 257 ASP 257 273 273 ASP ASP A . n 
A 1 258 PRO 258 274 274 PRO PRO A . n 
A 1 259 PRO 259 275 275 PRO PRO A . n 
A 1 260 GLU 260 276 276 GLU GLU A . n 
A 1 261 VAL 261 277 277 VAL VAL A . n 
A 1 262 ARG 262 278 278 ARG ARG A . n 
A 1 263 ASP 263 279 279 ASP ASP A . n 
A 1 264 ASP 264 280 280 ASP ASP A . n 
A 1 265 VAL 265 281 281 VAL VAL A . n 
A 1 266 VAL 266 282 282 VAL VAL A . n 
A 1 267 HIS 267 283 283 HIS HIS A . n 
A 1 268 TYR 268 284 284 TYR TYR A . n 
A 1 269 GLY 269 285 285 GLY GLY A . n 
A 1 270 ILE 270 286 286 ILE ILE A . n 
A 1 271 GLN 271 287 287 GLN GLN A . n 
A 1 272 PRO 272 288 288 PRO PRO A . n 
A 1 273 PRO 273 289 289 PRO PRO A . n 
A 1 274 THR 274 290 290 THR THR A . n 
A 1 275 THR 275 291 291 THR THR A . n 
A 1 276 HIS 276 292 292 HIS HIS A . n 
A 1 277 GLY 277 293 293 GLY GLY A . n 
A 1 278 ILE 278 294 294 ILE ILE A . n 
A 1 279 MET 279 295 295 MET MET A . n 
A 1 280 TYR 280 296 296 TYR TYR A . n 
A 1 281 SER 281 297 297 SER SER A . n 
A 1 282 GLY 282 298 298 GLY GLY A . n 
A 1 283 VAL 283 299 299 VAL VAL A . n 
A 1 284 PHE 284 300 300 PHE PHE A . n 
A 1 285 ILE 285 301 301 ILE ILE A . n 
A 1 286 GLU 286 302 302 GLU GLU A . n 
A 1 287 ASP 287 303 303 ASP ASP A . n 
A 1 288 LEU 288 304 304 LEU LEU A . n 
A 1 289 GLU 289 305 305 GLU GLU A . n 
A 1 290 ASP 290 306 306 ASP ASP A . n 
A 1 291 GLY 291 307 307 GLY GLY A . n 
A 1 292 LEU 292 308 308 LEU LEU A . n 
A 1 293 SER 293 309 309 SER SER A . n 
A 1 294 VAL 294 310 310 VAL VAL A . n 
A 1 295 GLY 295 311 311 GLY GLY A . n 
A 1 296 ASN 296 312 312 ASN ASN A . n 
A 1 297 LYS 297 313 313 LYS LYS A . n 
A 1 298 PHE 298 314 314 PHE PHE A . n 
A 1 299 ILE 299 315 315 ILE ILE A . n 
A 1 300 GLN 300 316 316 GLN GLN A . n 
A 1 301 GLU 301 317 317 GLU GLU A . n 
A 1 302 VAL 302 318 318 VAL VAL A . n 
A 1 303 ALA 303 319 319 ALA ALA A . n 
A 1 304 ALA 304 320 ?   ?   ?   A . n 
A 1 305 ALA 305 321 ?   ?   ?   A . n 
A 1 306 LEU 306 322 ?   ?   ?   A . n 
A 1 307 GLU 307 323 ?   ?   ?   A . n 
A 1 308 HIS 308 324 ?   ?   ?   A . n 
A 1 309 HIS 309 325 ?   ?   ?   A . n 
A 1 310 HIS 310 326 ?   ?   ?   A . n 
A 1 311 HIS 311 327 ?   ?   ?   A . n 
A 1 312 HIS 312 328 ?   ?   ?   A . n 
A 1 313 HIS 313 329 ?   ?   ?   A . n 
B 1 1   MET 1   17  ?   ?   ?   B . n 
B 1 2   GLY 2   18  18  GLY GLY B . n 
B 1 3   LYS 3   19  19  LYS LYS B . n 
B 1 4   VAL 4   20  20  VAL VAL B . n 
B 1 5   LEU 5   21  21  LEU LEU B . n 
B 1 6   TRP 6   22  22  TRP TRP B . n 
B 1 7   ASP 7   23  23  ASP ASP B . n 
B 1 8   GLY 8   24  24  GLY GLY B . n 
B 1 9   ARG 9   25  25  ARG ARG B . n 
B 1 10  ALA 10  26  26  ALA ALA B . n 
B 1 11  PRO 11  27  27  PRO PRO B . n 
B 1 12  ARG 12  28  28  ARG ARG B . n 
B 1 13  ASN 13  29  29  ASN ASN B . n 
B 1 14  TYR 14  30  30  TYR TYR B . n 
B 1 15  THR 15  31  31  THR THR B . n 
B 1 16  SER 16  32  32  SER SER B . n 
B 1 17  PHE 17  33  33  PHE PHE B . n 
B 1 18  HIS 18  34  34  HIS HIS B . n 
B 1 19  LEU 19  35  35  LEU LEU B . n 
B 1 20  ASP 20  36  36  ASP ASP B . n 
B 1 21  ALA 21  37  37  ALA ALA B . n 
B 1 22  SER 22  38  38  SER SER B . n 
B 1 23  VAL 23  39  39  VAL VAL B . n 
B 1 24  ASP 24  40  40  ASP ASP B . n 
B 1 25  PRO 25  41  41  PRO PRO B . n 
B 1 26  TYR 26  42  42  TYR TYR B . n 
B 1 27  LEU 27  43  43  LEU LEU B . n 
B 1 28  THR 28  44  44  THR THR B . n 
B 1 29  VAL 29  45  45  VAL VAL B . n 
B 1 30  VAL 30  46  46  VAL VAL B . n 
B 1 31  LYS 31  47  47  LYS LYS B . n 
B 1 32  GLY 32  48  48  GLY GLY B . n 
B 1 33  PRO 33  49  49  PRO PRO B . n 
B 1 34  ARG 34  50  50  ARG ARG B . n 
B 1 35  ALA 35  51  51  ALA ALA B . n 
B 1 36  ALA 36  52  52  ALA ALA B . n 
B 1 37  SER 37  53  53  SER SER B . n 
B 1 38  ILE 38  54  54  ILE ILE B . n 
B 1 39  TYR 39  55  55  TYR TYR B . n 
B 1 40  THR 40  56  56  THR THR B . n 
B 1 41  ARG 41  57  57  ARG ARG B . n 
B 1 42  LEU 42  58  58  LEU LEU B . n 
B 1 43  LEU 43  59  59  LEU LEU B . n 
B 1 44  GLY 44  60  60  GLY GLY B . n 
B 1 45  ARG 45  61  61  ARG ARG B . n 
B 1 46  GLU 46  62  62  GLU GLU B . n 
B 1 47  VAL 47  63  63  VAL VAL B . n 
B 1 48  THR 48  64  64  THR THR B . n 
B 1 49  PRO 49  65  65  PRO PRO B . n 
B 1 50  THR 50  66  66  THR THR B . n 
B 1 51  PRO 51  67  67  PRO PRO B . n 
B 1 52  LEU 52  68  68  LEU LEU B . n 
B 1 53  TRP 53  69  69  TRP TRP B . n 
B 1 54  ASN 54  70  70  ASN ASN B . n 
B 1 55  ASP 55  71  71  ASP ASP B . n 
B 1 56  ARG 56  72  72  ARG ARG B . n 
B 1 57  LEU 57  73  73  LEU LEU B . n 
B 1 58  PHE 58  74  74  PHE PHE B . n 
B 1 59  PRO 59  75  75  PRO PRO B . n 
B 1 60  GLU 60  76  76  GLU GLU B . n 
B 1 61  VAL 61  77  77  VAL VAL B . n 
B 1 62  PRO 62  78  78  PRO PRO B . n 
B 1 63  TYR 63  79  79  TYR TYR B . n 
B 1 64  PRO 64  80  80  PRO PRO B . n 
B 1 65  ALA 65  81  81  ALA ALA B . n 
B 1 66  VAL 66  82  82  VAL VAL B . n 
B 1 67  SER 67  83  83  SER SER B . n 
B 1 68  THR 68  84  84  THR THR B . n 
B 1 69  GLU 69  85  85  GLU GLU B . n 
B 1 70  GLN 70  86  86  GLN GLN B . n 
B 1 71  ALA 71  87  87  ALA ALA B . n 
B 1 72  LEU 72  88  88  LEU LEU B . n 
B 1 73  LEU 73  89  89  LEU LEU B . n 
B 1 74  VAL 74  90  90  VAL VAL B . n 
B 1 75  LEU 75  91  91  LEU LEU B . n 
B 1 76  ILE 76  92  92  ILE ILE B . n 
B 1 77  GLY 77  93  93  GLY GLY B . n 
B 1 78  ASN 78  94  94  ASN ASN B . n 
B 1 79  SER 79  95  95  SER SER B . n 
B 1 80  SER 80  96  96  SER SER B . n 
B 1 81  VAL 81  97  97  VAL VAL B . n 
B 1 82  PHE 82  98  98  PHE PHE B . n 
B 1 83  THR 83  99  99  THR THR B . n 
B 1 84  PRO 84  100 100 PRO PRO B . n 
B 1 85  GLY 85  101 101 GLY GLY B . n 
B 1 86  SER 86  102 102 SER SER B . n 
B 1 87  SER 87  103 103 SER SER B . n 
B 1 88  GLY 88  104 104 GLY GLY B . n 
B 1 89  ARG 89  105 105 ARG ARG B . n 
B 1 90  PRO 90  106 106 PRO PRO B . n 
B 1 91  GLN 91  107 107 GLN GLN B . n 
B 1 92  THR 92  108 108 THR THR B . n 
B 1 93  GLY 93  109 109 GLY GLY B . n 
B 1 94  PHE 94  110 110 PHE PHE B . n 
B 1 95  ARG 95  111 111 ARG ARG B . n 
B 1 96  ARG 96  112 112 ARG ARG B . n 
B 1 97  THR 97  113 113 THR THR B . n 
B 1 98  GLU 98  114 114 GLU GLU B . n 
B 1 99  LEU 99  115 115 LEU LEU B . n 
B 1 100 ILE 100 116 116 ILE ILE B . n 
B 1 101 ALA 101 117 117 ALA ALA B . n 
B 1 102 GLN 102 118 118 GLN GLN B . n 
B 1 103 VAL 103 119 119 VAL VAL B . n 
B 1 104 ASN 104 120 120 ASN ASN B . n 
B 1 105 GLY 105 121 121 GLY GLY B . n 
B 1 106 SER 106 122 122 SER SER B . n 
B 1 107 ASN 107 123 123 ASN ASN B . n 
B 1 108 ILE 108 124 124 ILE ILE B . n 
B 1 109 ASP 109 125 125 ASP ASP B . n 
B 1 110 LEU 110 126 126 LEU LEU B . n 
B 1 111 ILE 111 127 127 ILE ILE B . n 
B 1 112 PRO 112 128 128 PRO PRO B . n 
B 1 113 ILE 113 129 129 ILE ILE B . n 
B 1 114 ILE 114 130 130 ILE ILE B . n 
B 1 115 GLY 115 131 131 GLY GLY B . n 
B 1 116 LYS 116 132 132 LYS LYS B . n 
B 1 117 GLY 117 133 133 GLY GLY B . n 
B 1 118 ARG 118 134 134 ARG ARG B . n 
B 1 119 VAL 119 135 135 VAL VAL B . n 
B 1 120 ALA 120 136 136 ALA ALA B . n 
B 1 121 PHE 121 137 137 PHE PHE B . n 
B 1 122 HIS 122 138 138 HIS HIS B . n 
B 1 123 PHE 123 139 139 PHE PHE B . n 
B 1 124 SER 124 140 140 SER SER B . n 
B 1 125 VAL 125 141 141 VAL VAL B . n 
B 1 126 LEU 126 142 142 LEU LEU B . n 
B 1 127 MET 127 143 143 MET MET B . n 
B 1 128 ASP 128 144 144 ASP ASP B . n 
B 1 129 GLU 129 145 145 GLU GLU B . n 
B 1 130 TRP 130 146 146 TRP TRP B . n 
B 1 131 HIS 131 147 147 HIS HIS B . n 
B 1 132 LYS 132 148 148 LYS LYS B . n 
B 1 133 LEU 133 149 149 LEU LEU B . n 
B 1 134 ASP 134 150 150 ASP ASP B . n 
B 1 135 MET 135 151 151 MET MET B . n 
B 1 136 ILE 136 152 152 ILE ILE B . n 
B 1 137 HIS 137 153 153 HIS HIS B . n 
B 1 138 GLU 138 154 154 GLU GLU B . n 
B 1 139 HIS 139 155 155 HIS HIS B . n 
B 1 140 GLN 140 156 156 GLN GLN B . n 
B 1 141 LEU 141 157 157 LEU LEU B . n 
B 1 142 VAL 142 158 158 VAL VAL B . n 
B 1 143 PHE 143 159 159 PHE PHE B . n 
B 1 144 VAL 144 160 160 VAL VAL B . n 
B 1 145 GLU 145 161 161 GLU GLU B . n 
B 1 146 PRO 146 162 162 PRO PRO B . n 
B 1 147 SER 147 163 163 SER SER B . n 
B 1 148 ASP 148 164 164 ASP ASP B . n 
B 1 149 GLY 149 165 165 GLY GLY B . n 
B 1 150 SER 150 166 166 SER SER B . n 
B 1 151 HIS 151 167 167 HIS HIS B . n 
B 1 152 VAL 152 168 168 VAL VAL B . n 
B 1 153 PHE 153 169 169 PHE PHE B . n 
B 1 154 THR 154 170 170 THR THR B . n 
B 1 155 LEU 155 171 171 LEU LEU B . n 
B 1 156 GLN 156 172 172 GLN GLN B . n 
B 1 157 VAL 157 173 173 VAL VAL B . n 
B 1 158 GLY 158 174 174 GLY GLY B . n 
B 1 159 SER 159 175 175 SER SER B . n 
B 1 160 PRO 160 176 176 PRO PRO B . n 
B 1 161 PHE 161 177 177 PHE PHE B . n 
B 1 162 THR 162 178 178 THR THR B . n 
B 1 163 ASN 163 179 179 ASN ASN B . n 
B 1 164 PRO 164 180 180 PRO PRO B . n 
B 1 165 THR 165 181 181 THR THR B . n 
B 1 166 GLY 166 182 182 GLY GLY B . n 
B 1 167 PRO 167 183 183 PRO PRO B . n 
B 1 168 LEU 168 184 184 LEU LEU B . n 
B 1 169 PRO 169 185 185 PRO PRO B . n 
B 1 170 ALA 170 186 186 ALA ALA B . n 
B 1 171 PRO 171 187 187 PRO PRO B . n 
B 1 172 ARG 172 188 188 ARG ARG B . n 
B 1 173 ALA 173 189 189 ALA ALA B . n 
B 1 174 ASP 174 190 190 ASP ASP B . n 
B 1 175 TRP 175 191 191 TRP TRP B . n 
B 1 176 LEU 176 192 192 LEU LEU B . n 
B 1 177 LYS 177 193 193 LYS LYS B . n 
B 1 178 ILE 178 194 194 ILE ILE B . n 
B 1 179 LEU 179 195 195 LEU LEU B . n 
B 1 180 ASN 180 196 196 ASN ASN B . n 
B 1 181 HIS 181 197 197 HIS HIS B . n 
B 1 182 ASN 182 198 198 ASN ASN B . n 
B 1 183 LEU 183 199 199 LEU LEU B . n 
B 1 184 ASP 184 200 200 ASP ASP B . n 
B 1 185 VAL 185 201 201 VAL VAL B . n 
B 1 186 LEU 186 202 202 LEU LEU B . n 
B 1 187 PHE 187 203 203 PHE PHE B . n 
B 1 188 GLU 188 204 204 GLU GLU B . n 
B 1 189 THR 189 205 205 THR THR B . n 
B 1 190 GLU 190 206 206 GLU GLU B . n 
B 1 191 PHE 191 207 207 PHE PHE B . n 
B 1 192 THR 192 208 208 THR THR B . n 
B 1 193 ASP 193 209 209 ASP ASP B . n 
B 1 194 GLU 194 210 210 GLU GLU B . n 
B 1 195 THR 195 211 211 THR THR B . n 
B 1 196 TRP 196 212 212 TRP TRP B . n 
B 1 197 HIS 197 213 213 HIS HIS B . n 
B 1 198 ASN 198 214 214 ASN ASN B . n 
B 1 199 PHE 199 215 215 PHE PHE B . n 
B 1 200 ALA 200 216 216 ALA ALA B . n 
B 1 201 VAL 201 217 217 VAL VAL B . n 
B 1 202 ILE 202 218 218 ILE ILE B . n 
B 1 203 VAL 203 219 219 VAL VAL B . n 
B 1 204 ASP 204 220 220 ASP ASP B . n 
B 1 205 TRP 205 221 221 TRP TRP B . n 
B 1 206 GLU 206 222 222 GLU GLU B . n 
B 1 207 LYS 207 223 223 LYS LYS B . n 
B 1 208 ARG 208 224 224 ARG ARG B . n 
B 1 209 THR 209 225 225 THR THR B . n 
B 1 210 LEU 210 226 226 LEU LEU B . n 
B 1 211 GLN 211 227 227 GLN GLN B . n 
B 1 212 VAL 212 228 228 VAL VAL B . n 
B 1 213 TRP 213 229 229 TRP TRP B . n 
B 1 214 TYR 214 230 230 TYR TYR B . n 
B 1 215 SER 215 231 231 SER SER B . n 
B 1 216 GLN 216 232 232 GLN GLN B . n 
B 1 217 ASN 217 233 233 ASN ASN B . n 
B 1 218 GLU 218 234 234 GLU GLU B . n 
B 1 219 ASN 219 235 235 ASN ASN B . n 
B 1 220 ASN 220 236 236 ASN ASN B . n 
B 1 221 LEU 221 237 237 LEU LEU B . n 
B 1 222 VAL 222 238 238 VAL VAL B . n 
B 1 223 TRP 223 239 239 TRP TRP B . n 
B 1 224 VAL 224 240 240 VAL VAL B . n 
B 1 225 THR 225 241 241 THR THR B . n 
B 1 226 PRO 226 242 242 PRO PRO B . n 
B 1 227 VAL 227 243 243 VAL VAL B . n 
B 1 228 LEU 228 244 244 LEU LEU B . n 
B 1 229 PRO 229 245 245 PRO PRO B . n 
B 1 230 ASN 230 246 246 ASN ASN B . n 
B 1 231 GLU 231 247 247 GLU GLU B . n 
B 1 232 THR 232 248 248 THR THR B . n 
B 1 233 VAL 233 249 249 VAL VAL B . n 
B 1 234 LYS 234 250 250 LYS LYS B . n 
B 1 235 ARG 235 251 251 ARG ARG B . n 
B 1 236 GLY 236 252 252 GLY GLY B . n 
B 1 237 THR 237 253 253 THR THR B . n 
B 1 238 ALA 238 254 254 ALA ALA B . n 
B 1 239 GLY 239 255 255 GLY GLY B . n 
B 1 240 ARG 240 256 256 ARG ARG B . n 
B 1 241 GLY 241 257 257 GLY GLY B . n 
B 1 242 ASP 242 258 258 ASP ASP B . n 
B 1 243 PHE 243 259 259 PHE PHE B . n 
B 1 244 HIS 244 260 260 HIS HIS B . n 
B 1 245 PHE 245 261 261 PHE PHE B . n 
B 1 246 GLY 246 262 262 GLY GLY B . n 
B 1 247 ILE 247 263 263 ILE ILE B . n 
B 1 248 LEU 248 264 264 LEU LEU B . n 
B 1 249 LYS 249 265 265 LYS LYS B . n 
B 1 250 LEU 250 266 266 LEU LEU B . n 
B 1 251 PRO 251 267 267 PRO PRO B . n 
B 1 252 LEU 252 268 268 LEU LEU B . n 
B 1 253 VAL 253 269 269 VAL VAL B . n 
B 1 254 ASN 254 270 270 ASN ASN B . n 
B 1 255 VAL 255 271 271 VAL VAL B . n 
B 1 256 ALA 256 272 272 ALA ALA B . n 
B 1 257 ASP 257 273 273 ASP ASP B . n 
B 1 258 PRO 258 274 274 PRO PRO B . n 
B 1 259 PRO 259 275 275 PRO PRO B . n 
B 1 260 GLU 260 276 276 GLU GLU B . n 
B 1 261 VAL 261 277 277 VAL VAL B . n 
B 1 262 ARG 262 278 278 ARG ARG B . n 
B 1 263 ASP 263 279 279 ASP ASP B . n 
B 1 264 ASP 264 280 280 ASP ASP B . n 
B 1 265 VAL 265 281 281 VAL VAL B . n 
B 1 266 VAL 266 282 282 VAL VAL B . n 
B 1 267 HIS 267 283 283 HIS HIS B . n 
B 1 268 TYR 268 284 284 TYR TYR B . n 
B 1 269 GLY 269 285 285 GLY GLY B . n 
B 1 270 ILE 270 286 286 ILE ILE B . n 
B 1 271 GLN 271 287 287 GLN GLN B . n 
B 1 272 PRO 272 288 288 PRO PRO B . n 
B 1 273 PRO 273 289 289 PRO PRO B . n 
B 1 274 THR 274 290 290 THR THR B . n 
B 1 275 THR 275 291 291 THR THR B . n 
B 1 276 HIS 276 292 292 HIS HIS B . n 
B 1 277 GLY 277 293 293 GLY GLY B . n 
B 1 278 ILE 278 294 294 ILE ILE B . n 
B 1 279 MET 279 295 295 MET MET B . n 
B 1 280 TYR 280 296 296 TYR TYR B . n 
B 1 281 SER 281 297 297 SER SER B . n 
B 1 282 GLY 282 298 298 GLY GLY B . n 
B 1 283 VAL 283 299 299 VAL VAL B . n 
B 1 284 PHE 284 300 300 PHE PHE B . n 
B 1 285 ILE 285 301 301 ILE ILE B . n 
B 1 286 GLU 286 302 302 GLU GLU B . n 
B 1 287 ASP 287 303 303 ASP ASP B . n 
B 1 288 LEU 288 304 304 LEU LEU B . n 
B 1 289 GLU 289 305 305 GLU GLU B . n 
B 1 290 ASP 290 306 306 ASP ASP B . n 
B 1 291 GLY 291 307 307 GLY GLY B . n 
B 1 292 LEU 292 308 308 LEU LEU B . n 
B 1 293 SER 293 309 309 SER SER B . n 
B 1 294 VAL 294 310 310 VAL VAL B . n 
B 1 295 GLY 295 311 311 GLY GLY B . n 
B 1 296 ASN 296 312 312 ASN ASN B . n 
B 1 297 LYS 297 313 313 LYS LYS B . n 
B 1 298 PHE 298 314 314 PHE PHE B . n 
B 1 299 ILE 299 315 315 ILE ILE B . n 
B 1 300 GLN 300 316 316 GLN GLN B . n 
B 1 301 GLU 301 317 317 GLU GLU B . n 
B 1 302 VAL 302 318 318 VAL VAL B . n 
B 1 303 ALA 303 319 ?   ?   ?   B . n 
B 1 304 ALA 304 320 ?   ?   ?   B . n 
B 1 305 ALA 305 321 ?   ?   ?   B . n 
B 1 306 LEU 306 322 ?   ?   ?   B . n 
B 1 307 GLU 307 323 ?   ?   ?   B . n 
B 1 308 HIS 308 324 ?   ?   ?   B . n 
B 1 309 HIS 309 325 ?   ?   ?   B . n 
B 1 310 HIS 310 326 ?   ?   ?   B . n 
B 1 311 HIS 311 327 ?   ?   ?   B . n 
B 1 312 HIS 312 328 ?   ?   ?   B . n 
B 1 313 HIS 313 329 ?   ?   ?   B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 PEG 1   401 401 PEG PEG A . 
D 2 PEG 1   401 401 PEG PEG B . 
E 3 HOH 1   501 356 HOH HOH A . 
E 3 HOH 2   502 139 HOH HOH A . 
E 3 HOH 3   503 179 HOH HOH A . 
E 3 HOH 4   504 68  HOH HOH A . 
E 3 HOH 5   505 200 HOH HOH A . 
E 3 HOH 6   506 10  HOH HOH A . 
E 3 HOH 7   507 219 HOH HOH A . 
E 3 HOH 8   508 89  HOH HOH A . 
E 3 HOH 9   509 196 HOH HOH A . 
E 3 HOH 10  510 29  HOH HOH A . 
E 3 HOH 11  511 389 HOH HOH A . 
E 3 HOH 12  512 309 HOH HOH A . 
E 3 HOH 13  513 312 HOH HOH A . 
E 3 HOH 14  514 275 HOH HOH A . 
E 3 HOH 15  515 22  HOH HOH A . 
E 3 HOH 16  516 233 HOH HOH A . 
E 3 HOH 17  517 74  HOH HOH A . 
E 3 HOH 18  518 380 HOH HOH A . 
E 3 HOH 19  519 399 HOH HOH A . 
E 3 HOH 20  520 113 HOH HOH A . 
E 3 HOH 21  521 154 HOH HOH A . 
E 3 HOH 22  522 71  HOH HOH A . 
E 3 HOH 23  523 444 HOH HOH A . 
E 3 HOH 24  524 426 HOH HOH A . 
E 3 HOH 25  525 151 HOH HOH A . 
E 3 HOH 26  526 51  HOH HOH A . 
E 3 HOH 27  527 14  HOH HOH A . 
E 3 HOH 28  528 32  HOH HOH A . 
E 3 HOH 29  529 348 HOH HOH A . 
E 3 HOH 30  530 303 HOH HOH A . 
E 3 HOH 31  531 7   HOH HOH A . 
E 3 HOH 32  532 229 HOH HOH A . 
E 3 HOH 33  533 300 HOH HOH A . 
E 3 HOH 34  534 160 HOH HOH A . 
E 3 HOH 35  535 439 HOH HOH A . 
E 3 HOH 36  536 53  HOH HOH A . 
E 3 HOH 37  537 370 HOH HOH A . 
E 3 HOH 38  538 18  HOH HOH A . 
E 3 HOH 39  539 106 HOH HOH A . 
E 3 HOH 40  540 122 HOH HOH A . 
E 3 HOH 41  541 317 HOH HOH A . 
E 3 HOH 42  542 23  HOH HOH A . 
E 3 HOH 43  543 321 HOH HOH A . 
E 3 HOH 44  544 182 HOH HOH A . 
E 3 HOH 45  545 155 HOH HOH A . 
E 3 HOH 46  546 15  HOH HOH A . 
E 3 HOH 47  547 318 HOH HOH A . 
E 3 HOH 48  548 148 HOH HOH A . 
E 3 HOH 49  549 220 HOH HOH A . 
E 3 HOH 50  550 28  HOH HOH A . 
E 3 HOH 51  551 21  HOH HOH A . 
E 3 HOH 52  552 273 HOH HOH A . 
E 3 HOH 53  553 115 HOH HOH A . 
E 3 HOH 54  554 288 HOH HOH A . 
E 3 HOH 55  555 289 HOH HOH A . 
E 3 HOH 56  556 39  HOH HOH A . 
E 3 HOH 57  557 56  HOH HOH A . 
E 3 HOH 58  558 190 HOH HOH A . 
E 3 HOH 59  559 127 HOH HOH A . 
E 3 HOH 60  560 236 HOH HOH A . 
E 3 HOH 61  561 373 HOH HOH A . 
E 3 HOH 62  562 78  HOH HOH A . 
E 3 HOH 63  563 340 HOH HOH A . 
E 3 HOH 64  564 27  HOH HOH A . 
E 3 HOH 65  565 364 HOH HOH A . 
E 3 HOH 66  566 266 HOH HOH A . 
E 3 HOH 67  567 176 HOH HOH A . 
E 3 HOH 68  568 366 HOH HOH A . 
E 3 HOH 69  569 369 HOH HOH A . 
E 3 HOH 70  570 406 HOH HOH A . 
E 3 HOH 71  571 194 HOH HOH A . 
E 3 HOH 72  572 242 HOH HOH A . 
E 3 HOH 73  573 335 HOH HOH A . 
E 3 HOH 74  574 430 HOH HOH A . 
E 3 HOH 75  575 396 HOH HOH A . 
E 3 HOH 76  576 120 HOH HOH A . 
E 3 HOH 77  577 66  HOH HOH A . 
E 3 HOH 78  578 237 HOH HOH A . 
E 3 HOH 79  579 454 HOH HOH A . 
E 3 HOH 80  580 85  HOH HOH A . 
E 3 HOH 81  581 207 HOH HOH A . 
E 3 HOH 82  582 293 HOH HOH A . 
E 3 HOH 83  583 189 HOH HOH A . 
E 3 HOH 84  584 104 HOH HOH A . 
E 3 HOH 85  585 145 HOH HOH A . 
E 3 HOH 86  586 188 HOH HOH A . 
E 3 HOH 87  587 264 HOH HOH A . 
E 3 HOH 88  588 164 HOH HOH A . 
E 3 HOH 89  589 425 HOH HOH A . 
E 3 HOH 90  590 270 HOH HOH A . 
E 3 HOH 91  591 118 HOH HOH A . 
E 3 HOH 92  592 72  HOH HOH A . 
E 3 HOH 93  593 98  HOH HOH A . 
E 3 HOH 94  594 101 HOH HOH A . 
E 3 HOH 95  595 432 HOH HOH A . 
E 3 HOH 96  596 269 HOH HOH A . 
E 3 HOH 97  597 202 HOH HOH A . 
E 3 HOH 98  598 31  HOH HOH A . 
E 3 HOH 99  599 110 HOH HOH A . 
E 3 HOH 100 600 360 HOH HOH A . 
E 3 HOH 101 601 250 HOH HOH A . 
E 3 HOH 102 602 94  HOH HOH A . 
E 3 HOH 103 603 124 HOH HOH A . 
E 3 HOH 104 604 278 HOH HOH A . 
E 3 HOH 105 605 330 HOH HOH A . 
E 3 HOH 106 606 136 HOH HOH A . 
E 3 HOH 107 607 36  HOH HOH A . 
E 3 HOH 108 608 319 HOH HOH A . 
E 3 HOH 109 609 5   HOH HOH A . 
E 3 HOH 110 610 30  HOH HOH A . 
E 3 HOH 111 611 82  HOH HOH A . 
E 3 HOH 112 612 69  HOH HOH A . 
E 3 HOH 113 613 117 HOH HOH A . 
E 3 HOH 114 614 339 HOH HOH A . 
E 3 HOH 115 615 357 HOH HOH A . 
E 3 HOH 116 616 156 HOH HOH A . 
E 3 HOH 117 617 375 HOH HOH A . 
E 3 HOH 118 618 128 HOH HOH A . 
E 3 HOH 119 619 421 HOH HOH A . 
E 3 HOH 120 620 404 HOH HOH A . 
E 3 HOH 121 621 260 HOH HOH A . 
E 3 HOH 122 622 365 HOH HOH A . 
E 3 HOH 123 623 208 HOH HOH A . 
E 3 HOH 124 624 291 HOH HOH A . 
E 3 HOH 125 625 95  HOH HOH A . 
E 3 HOH 126 626 271 HOH HOH A . 
E 3 HOH 127 627 254 HOH HOH A . 
E 3 HOH 128 628 232 HOH HOH A . 
E 3 HOH 129 629 301 HOH HOH A . 
E 3 HOH 130 630 372 HOH HOH A . 
E 3 HOH 131 631 12  HOH HOH A . 
E 3 HOH 132 632 414 HOH HOH A . 
E 3 HOH 133 633 292 HOH HOH A . 
E 3 HOH 134 634 92  HOH HOH A . 
E 3 HOH 135 635 1   HOH HOH A . 
E 3 HOH 136 636 135 HOH HOH A . 
E 3 HOH 137 637 121 HOH HOH A . 
E 3 HOH 138 638 43  HOH HOH A . 
E 3 HOH 139 639 80  HOH HOH A . 
E 3 HOH 140 640 251 HOH HOH A . 
E 3 HOH 141 641 64  HOH HOH A . 
E 3 HOH 142 642 103 HOH HOH A . 
E 3 HOH 143 643 3   HOH HOH A . 
E 3 HOH 144 644 162 HOH HOH A . 
E 3 HOH 145 645 54  HOH HOH A . 
E 3 HOH 146 646 256 HOH HOH A . 
E 3 HOH 147 647 382 HOH HOH A . 
E 3 HOH 148 648 249 HOH HOH A . 
E 3 HOH 149 649 245 HOH HOH A . 
E 3 HOH 150 650 107 HOH HOH A . 
E 3 HOH 151 651 332 HOH HOH A . 
E 3 HOH 152 652 171 HOH HOH A . 
E 3 HOH 153 653 83  HOH HOH A . 
E 3 HOH 154 654 38  HOH HOH A . 
E 3 HOH 155 655 408 HOH HOH A . 
E 3 HOH 156 656 111 HOH HOH A . 
E 3 HOH 157 657 130 HOH HOH A . 
E 3 HOH 158 658 277 HOH HOH A . 
E 3 HOH 159 659 48  HOH HOH A . 
E 3 HOH 160 660 456 HOH HOH A . 
E 3 HOH 161 661 97  HOH HOH A . 
E 3 HOH 162 662 427 HOH HOH A . 
E 3 HOH 163 663 334 HOH HOH A . 
E 3 HOH 164 664 234 HOH HOH A . 
E 3 HOH 165 665 206 HOH HOH A . 
E 3 HOH 166 666 62  HOH HOH A . 
E 3 HOH 167 667 61  HOH HOH A . 
E 3 HOH 168 668 146 HOH HOH A . 
E 3 HOH 169 669 246 HOH HOH A . 
E 3 HOH 170 670 212 HOH HOH A . 
E 3 HOH 171 671 435 HOH HOH A . 
E 3 HOH 172 672 215 HOH HOH A . 
E 3 HOH 173 673 386 HOH HOH A . 
E 3 HOH 174 674 91  HOH HOH A . 
E 3 HOH 175 675 381 HOH HOH A . 
E 3 HOH 176 676 362 HOH HOH A . 
E 3 HOH 177 677 394 HOH HOH A . 
E 3 HOH 178 678 417 HOH HOH A . 
E 3 HOH 179 679 322 HOH HOH A . 
E 3 HOH 180 680 283 HOH HOH A . 
E 3 HOH 181 681 140 HOH HOH A . 
E 3 HOH 182 682 403 HOH HOH A . 
E 3 HOH 183 683 343 HOH HOH A . 
E 3 HOH 184 684 100 HOH HOH A . 
E 3 HOH 185 685 257 HOH HOH A . 
E 3 HOH 186 686 385 HOH HOH A . 
E 3 HOH 187 687 338 HOH HOH A . 
E 3 HOH 188 688 314 HOH HOH A . 
E 3 HOH 189 689 409 HOH HOH A . 
E 3 HOH 190 690 329 HOH HOH A . 
E 3 HOH 191 691 302 HOH HOH A . 
E 3 HOH 192 692 187 HOH HOH A . 
E 3 HOH 193 693 296 HOH HOH A . 
E 3 HOH 194 694 387 HOH HOH A . 
E 3 HOH 195 695 315 HOH HOH A . 
E 3 HOH 196 696 167 HOH HOH A . 
E 3 HOH 197 697 447 HOH HOH A . 
E 3 HOH 198 698 392 HOH HOH A . 
E 3 HOH 199 699 197 HOH HOH A . 
E 3 HOH 200 700 419 HOH HOH A . 
E 3 HOH 201 701 198 HOH HOH A . 
E 3 HOH 202 702 235 HOH HOH A . 
E 3 HOH 203 703 47  HOH HOH A . 
E 3 HOH 204 704 412 HOH HOH A . 
E 3 HOH 205 705 186 HOH HOH A . 
E 3 HOH 206 706 378 HOH HOH A . 
E 3 HOH 207 707 265 HOH HOH A . 
E 3 HOH 208 708 281 HOH HOH A . 
E 3 HOH 209 709 410 HOH HOH A . 
E 3 HOH 210 710 244 HOH HOH A . 
E 3 HOH 211 711 169 HOH HOH A . 
E 3 HOH 212 712 407 HOH HOH A . 
E 3 HOH 213 713 328 HOH HOH A . 
E 3 HOH 214 714 429 HOH HOH A . 
E 3 HOH 215 715 290 HOH HOH A . 
E 3 HOH 216 716 173 HOH HOH A . 
E 3 HOH 217 717 304 HOH HOH A . 
E 3 HOH 218 718 415 HOH HOH A . 
E 3 HOH 219 719 411 HOH HOH A . 
E 3 HOH 220 720 355 HOH HOH A . 
E 3 HOH 221 721 416 HOH HOH A . 
E 3 HOH 222 722 377 HOH HOH A . 
F 3 HOH 1   501 336 HOH HOH B . 
F 3 HOH 2   502 350 HOH HOH B . 
F 3 HOH 3   503 279 HOH HOH B . 
F 3 HOH 4   504 203 HOH HOH B . 
F 3 HOH 5   505 132 HOH HOH B . 
F 3 HOH 6   506 376 HOH HOH B . 
F 3 HOH 7   507 423 HOH HOH B . 
F 3 HOH 8   508 258 HOH HOH B . 
F 3 HOH 9   509 240 HOH HOH B . 
F 3 HOH 10  510 191 HOH HOH B . 
F 3 HOH 11  511 199 HOH HOH B . 
F 3 HOH 12  512 40  HOH HOH B . 
F 3 HOH 13  513 324 HOH HOH B . 
F 3 HOH 14  514 268 HOH HOH B . 
F 3 HOH 15  515 274 HOH HOH B . 
F 3 HOH 16  516 457 HOH HOH B . 
F 3 HOH 17  517 88  HOH HOH B . 
F 3 HOH 18  518 81  HOH HOH B . 
F 3 HOH 19  519 147 HOH HOH B . 
F 3 HOH 20  520 333 HOH HOH B . 
F 3 HOH 21  521 168 HOH HOH B . 
F 3 HOH 22  522 253 HOH HOH B . 
F 3 HOH 23  523 458 HOH HOH B . 
F 3 HOH 24  524 438 HOH HOH B . 
F 3 HOH 25  525 50  HOH HOH B . 
F 3 HOH 26  526 8   HOH HOH B . 
F 3 HOH 27  527 384 HOH HOH B . 
F 3 HOH 28  528 280 HOH HOH B . 
F 3 HOH 29  529 9   HOH HOH B . 
F 3 HOH 30  530 221 HOH HOH B . 
F 3 HOH 31  531 361 HOH HOH B . 
F 3 HOH 32  532 46  HOH HOH B . 
F 3 HOH 33  533 105 HOH HOH B . 
F 3 HOH 34  534 297 HOH HOH B . 
F 3 HOH 35  535 109 HOH HOH B . 
F 3 HOH 36  536 99  HOH HOH B . 
F 3 HOH 37  537 209 HOH HOH B . 
F 3 HOH 38  538 287 HOH HOH B . 
F 3 HOH 39  539 143 HOH HOH B . 
F 3 HOH 40  540 79  HOH HOH B . 
F 3 HOH 41  541 255 HOH HOH B . 
F 3 HOH 42  542 185 HOH HOH B . 
F 3 HOH 43  543 441 HOH HOH B . 
F 3 HOH 44  544 241 HOH HOH B . 
F 3 HOH 45  545 114 HOH HOH B . 
F 3 HOH 46  546 11  HOH HOH B . 
F 3 HOH 47  547 349 HOH HOH B . 
F 3 HOH 48  548 310 HOH HOH B . 
F 3 HOH 49  549 285 HOH HOH B . 
F 3 HOH 50  550 57  HOH HOH B . 
F 3 HOH 51  551 305 HOH HOH B . 
F 3 HOH 52  552 299 HOH HOH B . 
F 3 HOH 53  553 163 HOH HOH B . 
F 3 HOH 54  554 193 HOH HOH B . 
F 3 HOH 55  555 24  HOH HOH B . 
F 3 HOH 56  556 25  HOH HOH B . 
F 3 HOH 57  557 181 HOH HOH B . 
F 3 HOH 58  558 418 HOH HOH B . 
F 3 HOH 59  559 371 HOH HOH B . 
F 3 HOH 60  560 96  HOH HOH B . 
F 3 HOH 61  561 374 HOH HOH B . 
F 3 HOH 62  562 210 HOH HOH B . 
F 3 HOH 63  563 184 HOH HOH B . 
F 3 HOH 64  564 13  HOH HOH B . 
F 3 HOH 65  565 102 HOH HOH B . 
F 3 HOH 66  566 44  HOH HOH B . 
F 3 HOH 67  567 73  HOH HOH B . 
F 3 HOH 68  568 16  HOH HOH B . 
F 3 HOH 69  569 379 HOH HOH B . 
F 3 HOH 70  570 157 HOH HOH B . 
F 3 HOH 71  571 116 HOH HOH B . 
F 3 HOH 72  572 247 HOH HOH B . 
F 3 HOH 73  573 37  HOH HOH B . 
F 3 HOH 74  574 226 HOH HOH B . 
F 3 HOH 75  575 119 HOH HOH B . 
F 3 HOH 76  576 33  HOH HOH B . 
F 3 HOH 77  577 90  HOH HOH B . 
F 3 HOH 78  578 26  HOH HOH B . 
F 3 HOH 79  579 76  HOH HOH B . 
F 3 HOH 80  580 434 HOH HOH B . 
F 3 HOH 81  581 420 HOH HOH B . 
F 3 HOH 82  582 272 HOH HOH B . 
F 3 HOH 83  583 431 HOH HOH B . 
F 3 HOH 84  584 55  HOH HOH B . 
F 3 HOH 85  585 175 HOH HOH B . 
F 3 HOH 86  586 402 HOH HOH B . 
F 3 HOH 87  587 159 HOH HOH B . 
F 3 HOH 88  588 75  HOH HOH B . 
F 3 HOH 89  589 6   HOH HOH B . 
F 3 HOH 90  590 123 HOH HOH B . 
F 3 HOH 91  591 17  HOH HOH B . 
F 3 HOH 92  592 138 HOH HOH B . 
F 3 HOH 93  593 195 HOH HOH B . 
F 3 HOH 94  594 45  HOH HOH B . 
F 3 HOH 95  595 413 HOH HOH B . 
F 3 HOH 96  596 231 HOH HOH B . 
F 3 HOH 97  597 125 HOH HOH B . 
F 3 HOH 98  598 144 HOH HOH B . 
F 3 HOH 99  599 165 HOH HOH B . 
F 3 HOH 100 600 298 HOH HOH B . 
F 3 HOH 101 601 262 HOH HOH B . 
F 3 HOH 102 602 65  HOH HOH B . 
F 3 HOH 103 603 70  HOH HOH B . 
F 3 HOH 104 604 295 HOH HOH B . 
F 3 HOH 105 605 252 HOH HOH B . 
F 3 HOH 106 606 453 HOH HOH B . 
F 3 HOH 107 607 150 HOH HOH B . 
F 3 HOH 108 608 20  HOH HOH B . 
F 3 HOH 109 609 311 HOH HOH B . 
F 3 HOH 110 610 41  HOH HOH B . 
F 3 HOH 111 611 261 HOH HOH B . 
F 3 HOH 112 612 158 HOH HOH B . 
F 3 HOH 113 613 35  HOH HOH B . 
F 3 HOH 114 614 86  HOH HOH B . 
F 3 HOH 115 615 276 HOH HOH B . 
F 3 HOH 116 616 267 HOH HOH B . 
F 3 HOH 117 617 450 HOH HOH B . 
F 3 HOH 118 618 346 HOH HOH B . 
F 3 HOH 119 619 320 HOH HOH B . 
F 3 HOH 120 620 149 HOH HOH B . 
F 3 HOH 121 621 152 HOH HOH B . 
F 3 HOH 122 622 428 HOH HOH B . 
F 3 HOH 123 623 4   HOH HOH B . 
F 3 HOH 124 624 225 HOH HOH B . 
F 3 HOH 125 625 42  HOH HOH B . 
F 3 HOH 126 626 126 HOH HOH B . 
F 3 HOH 127 627 223 HOH HOH B . 
F 3 HOH 128 628 183 HOH HOH B . 
F 3 HOH 129 629 77  HOH HOH B . 
F 3 HOH 130 630 134 HOH HOH B . 
F 3 HOH 131 631 345 HOH HOH B . 
F 3 HOH 132 632 341 HOH HOH B . 
F 3 HOH 133 633 108 HOH HOH B . 
F 3 HOH 134 634 205 HOH HOH B . 
F 3 HOH 135 635 63  HOH HOH B . 
F 3 HOH 136 636 87  HOH HOH B . 
F 3 HOH 137 637 351 HOH HOH B . 
F 3 HOH 138 638 238 HOH HOH B . 
F 3 HOH 139 639 59  HOH HOH B . 
F 3 HOH 140 640 19  HOH HOH B . 
F 3 HOH 141 641 393 HOH HOH B . 
F 3 HOH 142 642 129 HOH HOH B . 
F 3 HOH 143 643 218 HOH HOH B . 
F 3 HOH 144 644 131 HOH HOH B . 
F 3 HOH 145 645 213 HOH HOH B . 
F 3 HOH 146 646 248 HOH HOH B . 
F 3 HOH 147 647 133 HOH HOH B . 
F 3 HOH 148 648 214 HOH HOH B . 
F 3 HOH 149 649 192 HOH HOH B . 
F 3 HOH 150 650 2   HOH HOH B . 
F 3 HOH 151 651 259 HOH HOH B . 
F 3 HOH 152 652 331 HOH HOH B . 
F 3 HOH 153 653 49  HOH HOH B . 
F 3 HOH 154 654 224 HOH HOH B . 
F 3 HOH 155 655 436 HOH HOH B . 
F 3 HOH 156 656 178 HOH HOH B . 
F 3 HOH 157 657 34  HOH HOH B . 
F 3 HOH 158 658 217 HOH HOH B . 
F 3 HOH 159 659 391 HOH HOH B . 
F 3 HOH 160 660 445 HOH HOH B . 
F 3 HOH 161 661 367 HOH HOH B . 
F 3 HOH 162 662 342 HOH HOH B . 
F 3 HOH 163 663 390 HOH HOH B . 
F 3 HOH 164 664 211 HOH HOH B . 
F 3 HOH 165 665 282 HOH HOH B . 
F 3 HOH 166 666 180 HOH HOH B . 
F 3 HOH 167 667 60  HOH HOH B . 
F 3 HOH 168 668 284 HOH HOH B . 
F 3 HOH 169 669 93  HOH HOH B . 
F 3 HOH 170 670 141 HOH HOH B . 
F 3 HOH 171 671 222 HOH HOH B . 
F 3 HOH 172 672 84  HOH HOH B . 
F 3 HOH 173 673 455 HOH HOH B . 
F 3 HOH 174 674 204 HOH HOH B . 
F 3 HOH 175 675 323 HOH HOH B . 
F 3 HOH 176 676 452 HOH HOH B . 
F 3 HOH 177 677 153 HOH HOH B . 
F 3 HOH 178 678 405 HOH HOH B . 
F 3 HOH 179 679 228 HOH HOH B . 
F 3 HOH 180 680 353 HOH HOH B . 
F 3 HOH 181 681 67  HOH HOH B . 
F 3 HOH 182 682 263 HOH HOH B . 
F 3 HOH 183 683 137 HOH HOH B . 
F 3 HOH 184 684 442 HOH HOH B . 
F 3 HOH 185 685 58  HOH HOH B . 
F 3 HOH 186 686 316 HOH HOH B . 
F 3 HOH 187 687 437 HOH HOH B . 
F 3 HOH 188 688 142 HOH HOH B . 
F 3 HOH 189 689 112 HOH HOH B . 
F 3 HOH 190 690 243 HOH HOH B . 
F 3 HOH 191 691 306 HOH HOH B . 
F 3 HOH 192 692 433 HOH HOH B . 
F 3 HOH 193 693 294 HOH HOH B . 
F 3 HOH 194 694 440 HOH HOH B . 
F 3 HOH 195 695 443 HOH HOH B . 
F 3 HOH 196 696 326 HOH HOH B . 
F 3 HOH 197 697 347 HOH HOH B . 
F 3 HOH 198 698 344 HOH HOH B . 
F 3 HOH 199 699 395 HOH HOH B . 
F 3 HOH 200 700 449 HOH HOH B . 
F 3 HOH 201 701 161 HOH HOH B . 
F 3 HOH 202 702 327 HOH HOH B . 
F 3 HOH 203 703 52  HOH HOH B . 
F 3 HOH 204 704 170 HOH HOH B . 
F 3 HOH 205 705 216 HOH HOH B . 
F 3 HOH 206 706 172 HOH HOH B . 
F 3 HOH 207 707 230 HOH HOH B . 
F 3 HOH 208 708 383 HOH HOH B . 
F 3 HOH 209 709 308 HOH HOH B . 
F 3 HOH 210 710 313 HOH HOH B . 
F 3 HOH 211 711 400 HOH HOH B . 
F 3 HOH 212 712 398 HOH HOH B . 
F 3 HOH 213 713 325 HOH HOH B . 
F 3 HOH 214 714 177 HOH HOH B . 
F 3 HOH 215 715 358 HOH HOH B . 
F 3 HOH 216 716 401 HOH HOH B . 
F 3 HOH 217 717 359 HOH HOH B . 
F 3 HOH 218 718 227 HOH HOH B . 
F 3 HOH 219 719 388 HOH HOH B . 
F 3 HOH 220 720 166 HOH HOH B . 
F 3 HOH 221 721 422 HOH HOH B . 
F 3 HOH 222 722 286 HOH HOH B . 
F 3 HOH 223 723 363 HOH HOH B . 
F 3 HOH 224 724 424 HOH HOH B . 
F 3 HOH 225 725 397 HOH HOH B . 
F 3 HOH 226 726 352 HOH HOH B . 
F 3 HOH 227 727 446 HOH HOH B . 
F 3 HOH 228 728 354 HOH HOH B . 
F 3 HOH 229 729 174 HOH HOH B . 
F 3 HOH 230 730 239 HOH HOH B . 
F 3 HOH 231 731 337 HOH HOH B . 
F 3 HOH 232 732 448 HOH HOH B . 
F 3 HOH 233 733 307 HOH HOH B . 
F 3 HOH 234 734 201 HOH HOH B . 
F 3 HOH 235 735 368 HOH HOH B . 
F 3 HOH 236 736 451 HOH HOH B . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC  ? ? ? 5.8.0415 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? MOSFLM  ? ? ? .        2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? MOLREP  ? ? ? .        4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9K7O 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     71.849 
_cell.length_a_esd                 ? 
_cell.length_b                     71.849 
_cell.length_b_esd                 ? 
_cell.length_c                     225.802 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        12 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9K7O 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                169 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 61' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9K7O 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.39 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          48.50 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              6.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    'PEG 10000, PEG 20000, MES-NaOH' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     CCD 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'ADSC QUANTUM 270' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2015-06-24 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.0 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'PHOTON FACTORY BEAMLINE AR-NE3A' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.0 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   AR-NE3A 
_diffrn_source.pdbx_synchrotron_site       'Photon Factory' 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9K7O 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.90 
_reflns.d_resolution_low                               47.9 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     51549 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           100 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                9.4 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          28.6 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                0.041 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   ? 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.119 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.90 
_reflns_shell.d_res_low                                     1.97 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           4.0 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             5122 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               0.159 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  ? 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.457 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            -0.00 
_refine.aniso_B[1][2]                            -0.00 
_refine.aniso_B[1][3]                            -0.00 
_refine.aniso_B[2][2]                            -0.00 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            0.00 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               28.388 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.960 
_refine.correlation_coeff_Fo_to_Fc_free          0.944 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9K7O 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.90 
_refine.ls_d_res_low                             36.55 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     49044 
_refine.ls_number_reflns_R_free                  2412 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.72 
_refine.ls_percent_reflns_R_free                 4.7 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.18164 
_refine.ls_R_factor_R_free                       0.21575 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.17990 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'BABINET MODEL WITH MASK' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.151 
_refine.pdbx_overall_ESU_R_Free                  0.137 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.90 
_refine_hist.d_res_low                        36.55 
_refine_hist.number_atoms_solvent             458 
_refine_hist.number_atoms_total               5265 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        4793 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         14 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.006  0.012  4951  ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.016  4587  ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.391  1.656  6773  ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 0.762  1.578  10561 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 7.829  5.000  601   ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 6.320  5.000  30    ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 13.753 10.000 748   ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.066  0.200  751   ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.007  0.020  5847  ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.009  0.020  1145  ? 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' ? 2.539  2.940  2410  ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 2.539  2.940  2410  ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 3.822  5.278  3009  ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 3.821  5.279  3010  ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 2.834  3.225  2541  ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 2.833  3.225  2542  ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 4.365  5.808  3765  ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 6.329  32.49  5511  ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 6.297  31.67  5410  ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?     ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.901 
_refine_ls_shell.d_res_low                        1.951 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             147 
_refine_ls_shell.number_reflns_R_work             3537 
_refine_ls_shell.percent_reflns_obs               96.47 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.268 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_R_complete                  ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
_refine_ls_shell.R_factor_R_free                  0.293 
# 
_struct.entry_id                     9K7O 
_struct.title                        'Coprinopsis cinerea GH131 protein CcGH131B' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        9K7O 
_struct_keywords.text            'Coprinopsis cinerea, GH131, cellobiose, cellulose, HYDROLASE' 
_struct_keywords.pdbx_keywords   HYDROLASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 2 ? 
E N N 3 ? 
F N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    D6RP27_COPC7 
_struct_ref.pdbx_db_accession          D6RP27 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;GKVLWDGRAPRNYTSFHLDASVDPYLTVVKGPRAASIYTRLLGREVTPTPLWNDRLFPEVPYPAVSTEQTLLVLIGNSSV
FTPGSSGRPQTGFRRTELIAQVNGSNIDLIPIIGKGRVAFHFSVLMDEWHKLDMIHEHQLVFVEPSDGSHVFTLQVGSPF
TNPTGPLPAPRADWLKILNHNLDVLFETEFTDETWHNFAVIVDWEKRTLQVWYSQNENNLVWVTPVLPNKTVKRGTAGRG
DFHFGILKLPLVNVADPPEVRDDVVHYGIQPPTTHGIMYSGVFIEDLEDGLSVGNKFIQEV
;
_struct_ref.pdbx_align_begin           18 
# 
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 9K7O A 2 ? 302 ? D6RP27 18 ? 318 ? 18 318 
2 1 9K7O B 2 ? 302 ? D6RP27 18 ? 318 ? 18 318 
# 
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 9K7O MET A 1   ? UNP D6RP27 ?   ?   'initiating methionine' 17  1  
1 9K7O ALA A 71  ? UNP D6RP27 THR 87  'engineered mutation'   87  2  
1 9K7O GLU A 231 ? UNP D6RP27 LYS 247 'engineered mutation'   247 3  
1 9K7O ALA A 303 ? UNP D6RP27 ?   ?   'expression tag'        319 4  
1 9K7O ALA A 304 ? UNP D6RP27 ?   ?   'expression tag'        320 5  
1 9K7O ALA A 305 ? UNP D6RP27 ?   ?   'expression tag'        321 6  
1 9K7O LEU A 306 ? UNP D6RP27 ?   ?   'expression tag'        322 7  
1 9K7O GLU A 307 ? UNP D6RP27 ?   ?   'expression tag'        323 8  
1 9K7O HIS A 308 ? UNP D6RP27 ?   ?   'expression tag'        324 9  
1 9K7O HIS A 309 ? UNP D6RP27 ?   ?   'expression tag'        325 10 
1 9K7O HIS A 310 ? UNP D6RP27 ?   ?   'expression tag'        326 11 
1 9K7O HIS A 311 ? UNP D6RP27 ?   ?   'expression tag'        327 12 
1 9K7O HIS A 312 ? UNP D6RP27 ?   ?   'expression tag'        328 13 
1 9K7O HIS A 313 ? UNP D6RP27 ?   ?   'expression tag'        329 14 
2 9K7O MET B 1   ? UNP D6RP27 ?   ?   'initiating methionine' 17  15 
2 9K7O ALA B 71  ? UNP D6RP27 THR 87  'engineered mutation'   87  16 
2 9K7O GLU B 231 ? UNP D6RP27 LYS 247 'engineered mutation'   247 17 
2 9K7O ALA B 303 ? UNP D6RP27 ?   ?   'expression tag'        319 18 
2 9K7O ALA B 304 ? UNP D6RP27 ?   ?   'expression tag'        320 19 
2 9K7O ALA B 305 ? UNP D6RP27 ?   ?   'expression tag'        321 20 
2 9K7O LEU B 306 ? UNP D6RP27 ?   ?   'expression tag'        322 21 
2 9K7O GLU B 307 ? UNP D6RP27 ?   ?   'expression tag'        323 22 
2 9K7O HIS B 308 ? UNP D6RP27 ?   ?   'expression tag'        324 23 
2 9K7O HIS B 309 ? UNP D6RP27 ?   ?   'expression tag'        325 24 
2 9K7O HIS B 310 ? UNP D6RP27 ?   ?   'expression tag'        326 25 
2 9K7O HIS B 311 ? UNP D6RP27 ?   ?   'expression tag'        327 26 
2 9K7O HIS B 312 ? UNP D6RP27 ?   ?   'expression tag'        328 27 
2 9K7O HIS B 313 ? UNP D6RP27 ?   ?   'expression tag'        329 28 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,E 
2 1 B,D,F 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                'Two monomers in an asymmetric unit.' 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 THR A 15  ? SER A 22  ? THR A 31  SER A 38  1 ? 8 
HELX_P HELX_P2  AA2 ALA A 35  ? TYR A 39  ? ALA A 51  TYR A 55  1 ? 5 
HELX_P HELX_P3  AA3 THR A 50  ? ASN A 54  ? THR A 66  ASN A 70  5 ? 5 
HELX_P HELX_P4  AA4 ASN A 107 ? ASP A 109 ? ASN A 123 ASP A 125 5 ? 3 
HELX_P HELX_P5  AA5 LEU A 110 ? GLY A 115 ? LEU A 126 GLY A 131 1 ? 6 
HELX_P HELX_P6  AA6 ARG A 235 ? GLY A 239 ? ARG A 251 GLY A 255 5 ? 5 
HELX_P HELX_P7  AA7 PRO A 258 ? ARG A 262 ? PRO A 274 ARG A 278 5 ? 5 
HELX_P HELX_P8  AA8 THR B 15  ? ALA B 21  ? THR B 31  ALA B 37  1 ? 7 
HELX_P HELX_P9  AA9 ALA B 35  ? TYR B 39  ? ALA B 51  TYR B 55  1 ? 5 
HELX_P HELX_P10 AB1 GLY B 44  ? VAL B 47  ? GLY B 60  VAL B 63  5 ? 4 
HELX_P HELX_P11 AB2 THR B 50  ? ASN B 54  ? THR B 66  ASN B 70  5 ? 5 
HELX_P HELX_P12 AB3 ASP B 109 ? GLY B 115 ? ASP B 125 GLY B 131 1 ? 7 
HELX_P HELX_P13 AB4 ARG B 235 ? GLY B 239 ? ARG B 251 GLY B 255 5 ? 5 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1  ASP 24  A . ? ASP 40  A PRO 25  A ? PRO 41  A 1 1.41   
2  PHE 58  A . ? PHE 74  A PRO 59  A ? PRO 75  A 1 2.31   
3  VAL 61  A . ? VAL 77  A PRO 62  A ? PRO 78  A 1 -1.96  
4  ASN 163 A . ? ASN 179 A PRO 164 A ? PRO 180 A 1 -0.28  
5  LEU 168 A . ? LEU 184 A PRO 169 A ? PRO 185 A 1 -1.39  
6  ASP 24  B . ? ASP 40  B PRO 25  B ? PRO 41  B 1 -5.16  
7  PHE 58  B . ? PHE 74  B PRO 59  B ? PRO 75  B 1 4.50   
8  VAL 61  B . ? VAL 77  B PRO 62  B ? PRO 78  B 1 -11.20 
9  ASN 163 B . ? ASN 179 B PRO 164 B ? PRO 180 B 1 -4.05  
10 LEU 168 B . ? LEU 184 B PRO 169 B ? PRO 185 B 1 -0.58  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 6 ? 
AA2 ? 7 ? 
AA3 ? 7 ? 
AA4 ? 4 ? 
AA5 ? 4 ? 
AA6 ? 6 ? 
AA7 ? 7 ? 
AA8 ? 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 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA3 5 6 ? anti-parallel 
AA3 6 7 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? parallel      
AA4 3 4 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? parallel      
AA5 3 4 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA6 3 4 ? anti-parallel 
AA6 4 5 ? anti-parallel 
AA6 5 6 ? anti-parallel 
AA7 1 2 ? anti-parallel 
AA7 2 3 ? anti-parallel 
AA7 3 4 ? anti-parallel 
AA7 4 5 ? anti-parallel 
AA7 5 6 ? anti-parallel 
AA7 6 7 ? anti-parallel 
AA8 1 2 ? anti-parallel 
AA8 2 3 ? anti-parallel 
AA8 3 4 ? anti-parallel 
AA8 4 5 ? anti-parallel 
AA8 5 6 ? anti-parallel 
AA8 6 7 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 VAL A 4   ? ASP A 7   ? VAL A 20  ASP A 23  
AA1 2 HIS A 276 ? ASP A 287 ? HIS A 292 ASP A 303 
AA1 3 ARG A 118 ? MET A 127 ? ARG A 134 MET A 143 
AA1 4 HIS A 197 ? ASP A 204 ? HIS A 213 ASP A 220 
AA1 5 THR A 209 ? GLN A 216 ? THR A 225 GLN A 232 
AA1 6 VAL A 222 ? TRP A 223 ? VAL A 238 TRP A 239 
AA2 1 THR A 40  ? LEU A 42  ? THR A 56  LEU A 58  
AA2 2 LEU A 72  ? ILE A 76  ? LEU A 88  ILE A 92  
AA2 3 HIS A 276 ? ASP A 287 ? HIS A 292 ASP A 303 
AA2 4 ARG A 118 ? MET A 127 ? ARG A 134 MET A 143 
AA2 5 HIS A 197 ? ASP A 204 ? HIS A 213 ASP A 220 
AA2 6 THR A 209 ? GLN A 216 ? THR A 225 GLN A 232 
AA2 7 LEU A 228 ? PRO A 229 ? LEU A 244 PRO A 245 
AA3 1 TYR A 26  ? LEU A 27  ? TYR A 42  LEU A 43  
AA3 2 ARG A 95  ? ALA A 101 ? ARG A 111 ALA A 117 
AA3 3 GLY A 241 ? LYS A 249 ? GLY A 257 LYS A 265 
AA3 4 HIS A 139 ? PRO A 146 ? HIS A 155 PRO A 162 
AA3 5 PHE A 153 ? VAL A 157 ? PHE A 169 VAL A 173 
AA3 6 TRP A 175 ? ASN A 180 ? TRP A 191 ASN A 196 
AA3 7 VAL A 185 ? GLU A 190 ? VAL A 201 GLU A 206 
AA4 1 ALA A 65  ? VAL A 66  ? ALA A 81  VAL A 82  
AA4 2 ASP A 55  ? LEU A 57  ? ASP A 71  LEU A 73  
AA4 3 PHE B 298 ? GLN B 300 ? PHE B 314 GLN B 316 
AA4 4 LEU B 292 ? GLY B 295 ? LEU B 308 GLY B 311 
AA5 1 LEU A 292 ? GLY A 295 ? LEU A 308 GLY A 311 
AA5 2 PHE A 298 ? GLN A 300 ? PHE A 314 GLN A 316 
AA5 3 ASP B 55  ? LEU B 57  ? ASP B 71  LEU B 73  
AA5 4 ALA B 65  ? VAL B 66  ? ALA B 81  VAL B 82  
AA6 1 VAL B 4   ? ASP B 7   ? VAL B 20  ASP B 23  
AA6 2 HIS B 276 ? ASP B 287 ? HIS B 292 ASP B 303 
AA6 3 ARG B 118 ? MET B 127 ? ARG B 134 MET B 143 
AA6 4 HIS B 197 ? ASP B 204 ? HIS B 213 ASP B 220 
AA6 5 THR B 209 ? GLN B 216 ? THR B 225 GLN B 232 
AA6 6 VAL B 222 ? TRP B 223 ? VAL B 238 TRP B 239 
AA7 1 THR B 40  ? LEU B 42  ? THR B 56  LEU B 58  
AA7 2 LEU B 72  ? ILE B 76  ? LEU B 88  ILE B 92  
AA7 3 HIS B 276 ? ASP B 287 ? HIS B 292 ASP B 303 
AA7 4 ARG B 118 ? MET B 127 ? ARG B 134 MET B 143 
AA7 5 HIS B 197 ? ASP B 204 ? HIS B 213 ASP B 220 
AA7 6 THR B 209 ? GLN B 216 ? THR B 225 GLN B 232 
AA7 7 LEU B 228 ? PRO B 229 ? LEU B 244 PRO B 245 
AA8 1 TYR B 26  ? LEU B 27  ? TYR B 42  LEU B 43  
AA8 2 ARG B 95  ? ALA B 101 ? ARG B 111 ALA B 117 
AA8 3 GLY B 241 ? LYS B 249 ? GLY B 257 LYS B 265 
AA8 4 HIS B 139 ? PRO B 146 ? HIS B 155 PRO B 162 
AA8 5 PHE B 153 ? VAL B 157 ? PHE B 169 VAL B 173 
AA8 6 TRP B 175 ? ASN B 180 ? TRP B 191 ASN B 196 
AA8 7 VAL B 185 ? GLU B 190 ? VAL B 201 GLU B 206 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LEU A 5   ? N LEU A 21  O ILE A 285 ? O ILE A 301 
AA1 2 3 O GLU A 286 ? O GLU A 302 N ALA A 120 ? N ALA A 136 
AA1 3 4 N VAL A 119 ? N VAL A 135 O VAL A 203 ? O VAL A 219 
AA1 4 5 N ALA A 200 ? N ALA A 216 O TRP A 213 ? O TRP A 229 
AA1 5 6 N TYR A 214 ? N TYR A 230 O VAL A 222 ? O VAL A 238 
AA2 1 2 N ARG A 41  ? N ARG A 57  O LEU A 73  ? O LEU A 89  
AA2 2 3 N VAL A 74  ? N VAL A 90  O ILE A 278 ? O ILE A 294 
AA2 3 4 O GLU A 286 ? O GLU A 302 N ALA A 120 ? N ALA A 136 
AA2 4 5 N VAL A 119 ? N VAL A 135 O VAL A 203 ? O VAL A 219 
AA2 5 6 N ALA A 200 ? N ALA A 216 O TRP A 213 ? O TRP A 229 
AA2 6 7 N LEU A 210 ? N LEU A 226 O LEU A 228 ? O LEU A 244 
AA3 1 2 N LEU A 27  ? N LEU A 43  O ILE A 100 ? O ILE A 116 
AA3 2 3 N ARG A 95  ? N ARG A 111 O LYS A 249 ? O LYS A 265 
AA3 3 4 O LEU A 248 ? O LEU A 264 N GLN A 140 ? N GLN A 156 
AA3 4 5 N LEU A 141 ? N LEU A 157 O LEU A 155 ? O LEU A 171 
AA3 5 6 N GLN A 156 ? N GLN A 172 O LYS A 177 ? O LYS A 193 
AA3 6 7 N ILE A 178 ? N ILE A 194 O LEU A 186 ? O LEU A 202 
AA4 1 2 O VAL A 66  ? O VAL A 82  N ASP A 55  ? N ASP A 71  
AA4 2 3 N ARG A 56  ? N ARG A 72  O ILE B 299 ? O ILE B 315 
AA4 3 4 O GLN B 300 ? O GLN B 316 N LEU B 292 ? N LEU B 308 
AA5 1 2 N LEU A 292 ? N LEU A 308 O GLN A 300 ? O GLN A 316 
AA5 2 3 N ILE A 299 ? N ILE A 315 O ARG B 56  ? O ARG B 72  
AA5 3 4 N ASP B 55  ? N ASP B 71  O VAL B 66  ? O VAL B 82  
AA6 1 2 N LEU B 5   ? N LEU B 21  O ILE B 285 ? O ILE B 301 
AA6 2 3 O PHE B 284 ? O PHE B 300 N HIS B 122 ? N HIS B 138 
AA6 3 4 N PHE B 121 ? N PHE B 137 O VAL B 201 ? O VAL B 217 
AA6 4 5 N ILE B 202 ? N ILE B 218 O GLN B 211 ? O GLN B 227 
AA6 5 6 N TYR B 214 ? N TYR B 230 O VAL B 222 ? O VAL B 238 
AA7 1 2 N ARG B 41  ? N ARG B 57  O LEU B 73  ? O LEU B 89  
AA7 2 3 N LEU B 72  ? N LEU B 88  O TYR B 280 ? O TYR B 296 
AA7 3 4 O PHE B 284 ? O PHE B 300 N HIS B 122 ? N HIS B 138 
AA7 4 5 N PHE B 121 ? N PHE B 137 O VAL B 201 ? O VAL B 217 
AA7 5 6 N ILE B 202 ? N ILE B 218 O GLN B 211 ? O GLN B 227 
AA7 6 7 N LEU B 210 ? N LEU B 226 O LEU B 228 ? O LEU B 244 
AA8 1 2 N LEU B 27  ? N LEU B 43  O ILE B 100 ? O ILE B 116 
AA8 2 3 N ARG B 95  ? N ARG B 111 O LYS B 249 ? O LYS B 265 
AA8 3 4 O HIS B 244 ? O HIS B 260 N PHE B 143 ? N PHE B 159 
AA8 4 5 N LEU B 141 ? N LEU B 157 O LEU B 155 ? O LEU B 171 
AA8 5 6 N THR B 154 ? N THR B 170 O LEU B 179 ? O LEU B 195 
AA8 6 7 N ILE B 178 ? N ILE B 194 O LEU B 186 ? O LEU B 202 
# 
_pdbx_entry_details.entry_id                   9K7O 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     N 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 PHE A 139 ? ? -173.88 144.90  
2 1 ASN A 233 ? ? 58.55   -123.35 
3 1 PRO A 242 ? ? -65.13  -177.38 
4 1 ASP A 306 ? ? 67.03   -39.97  
5 1 ASN B 233 ? ? 57.59   -125.15 
6 1 PRO B 242 ? ? -66.16  -175.35 
7 1 PRO B 289 ? ? -79.55  47.22   
8 1 ASP B 306 ? ? 69.29   -50.98  
# 
loop_
_pdbx_validate_planes.id 
_pdbx_validate_planes.PDB_model_num 
_pdbx_validate_planes.auth_comp_id 
_pdbx_validate_planes.auth_asym_id 
_pdbx_validate_planes.auth_seq_id 
_pdbx_validate_planes.PDB_ins_code 
_pdbx_validate_planes.label_alt_id 
_pdbx_validate_planes.rmsd 
_pdbx_validate_planes.type 
1 1 ARG A 72 ? ? 0.088 'SIDE CHAIN' 
2 1 ARG B 57 ? ? 0.098 'SIDE CHAIN' 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      B 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       736 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   5.82 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
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 17  ? A MET 1   
2  1 Y 1 A ALA 320 ? A ALA 304 
3  1 Y 1 A ALA 321 ? A ALA 305 
4  1 Y 1 A LEU 322 ? A LEU 306 
5  1 Y 1 A GLU 323 ? A GLU 307 
6  1 Y 1 A HIS 324 ? A HIS 308 
7  1 Y 1 A HIS 325 ? A HIS 309 
8  1 Y 1 A HIS 326 ? A HIS 310 
9  1 Y 1 A HIS 327 ? A HIS 311 
10 1 Y 1 A HIS 328 ? A HIS 312 
11 1 Y 1 A HIS 329 ? A HIS 313 
12 1 Y 1 B MET 17  ? B MET 1   
13 1 Y 1 B ALA 319 ? B ALA 303 
14 1 Y 1 B ALA 320 ? B ALA 304 
15 1 Y 1 B ALA 321 ? B ALA 305 
16 1 Y 1 B LEU 322 ? B LEU 306 
17 1 Y 1 B GLU 323 ? B GLU 307 
18 1 Y 1 B HIS 324 ? B HIS 308 
19 1 Y 1 B HIS 325 ? B HIS 309 
20 1 Y 1 B HIS 326 ? B HIS 310 
21 1 Y 1 B HIS 327 ? B HIS 311 
22 1 Y 1 B HIS 328 ? B HIS 312 
23 1 Y 1 B HIS 329 ? B HIS 313 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
GLN N    N N N 74  
GLN CA   C N S 75  
GLN C    C N N 76  
GLN O    O N N 77  
GLN CB   C N N 78  
GLN CG   C N N 79  
GLN CD   C N N 80  
GLN OE1  O N N 81  
GLN NE2  N N N 82  
GLN OXT  O N N 83  
GLN H    H N N 84  
GLN H2   H N N 85  
GLN HA   H N N 86  
GLN HB2  H N N 87  
GLN HB3  H N N 88  
GLN HG2  H N N 89  
GLN HG3  H N N 90  
GLN HE21 H N N 91  
GLN HE22 H N N 92  
GLN HXT  H N N 93  
GLU N    N N N 94  
GLU CA   C N S 95  
GLU C    C N N 96  
GLU O    O N N 97  
GLU CB   C N N 98  
GLU CG   C N N 99  
GLU CD   C N N 100 
GLU OE1  O N N 101 
GLU OE2  O N N 102 
GLU OXT  O N N 103 
GLU H    H N N 104 
GLU H2   H N N 105 
GLU HA   H N N 106 
GLU HB2  H N N 107 
GLU HB3  H N N 108 
GLU HG2  H N N 109 
GLU HG3  H N N 110 
GLU HE2  H N N 111 
GLU HXT  H N N 112 
GLY N    N N N 113 
GLY CA   C N N 114 
GLY C    C N N 115 
GLY O    O N N 116 
GLY OXT  O N N 117 
GLY H    H N N 118 
GLY H2   H N N 119 
GLY HA2  H N N 120 
GLY HA3  H N N 121 
GLY HXT  H N N 122 
HIS N    N N N 123 
HIS CA   C N S 124 
HIS C    C N N 125 
HIS O    O N N 126 
HIS CB   C N N 127 
HIS CG   C Y N 128 
HIS ND1  N Y N 129 
HIS CD2  C Y N 130 
HIS CE1  C Y N 131 
HIS NE2  N Y N 132 
HIS OXT  O N N 133 
HIS H    H N N 134 
HIS H2   H N N 135 
HIS HA   H N N 136 
HIS HB2  H N N 137 
HIS HB3  H N N 138 
HIS HD1  H N N 139 
HIS HD2  H N N 140 
HIS HE1  H N N 141 
HIS HE2  H N N 142 
HIS HXT  H N N 143 
HOH O    O N N 144 
HOH H1   H N N 145 
HOH H2   H N N 146 
ILE N    N N N 147 
ILE CA   C N S 148 
ILE C    C N N 149 
ILE O    O N N 150 
ILE CB   C N S 151 
ILE CG1  C N N 152 
ILE CG2  C N N 153 
ILE CD1  C N N 154 
ILE OXT  O N N 155 
ILE H    H N N 156 
ILE H2   H N N 157 
ILE HA   H N N 158 
ILE HB   H N N 159 
ILE HG12 H N N 160 
ILE HG13 H N N 161 
ILE HG21 H N N 162 
ILE HG22 H N N 163 
ILE HG23 H N N 164 
ILE HD11 H N N 165 
ILE HD12 H N N 166 
ILE HD13 H N N 167 
ILE HXT  H N N 168 
LEU N    N N N 169 
LEU CA   C N S 170 
LEU C    C N N 171 
LEU O    O N N 172 
LEU CB   C N N 173 
LEU CG   C N N 174 
LEU CD1  C N N 175 
LEU CD2  C N N 176 
LEU OXT  O N N 177 
LEU H    H N N 178 
LEU H2   H N N 179 
LEU HA   H N N 180 
LEU HB2  H N N 181 
LEU HB3  H N N 182 
LEU HG   H N N 183 
LEU HD11 H N N 184 
LEU HD12 H N N 185 
LEU HD13 H N N 186 
LEU HD21 H N N 187 
LEU HD22 H N N 188 
LEU HD23 H N N 189 
LEU HXT  H N N 190 
LYS N    N N N 191 
LYS CA   C N S 192 
LYS C    C N N 193 
LYS O    O N N 194 
LYS CB   C N N 195 
LYS CG   C N N 196 
LYS CD   C N N 197 
LYS CE   C N N 198 
LYS NZ   N N N 199 
LYS OXT  O N N 200 
LYS H    H N N 201 
LYS H2   H N N 202 
LYS HA   H N N 203 
LYS HB2  H N N 204 
LYS HB3  H N N 205 
LYS HG2  H N N 206 
LYS HG3  H N N 207 
LYS HD2  H N N 208 
LYS HD3  H N N 209 
LYS HE2  H N N 210 
LYS HE3  H N N 211 
LYS HZ1  H N N 212 
LYS HZ2  H N N 213 
LYS HZ3  H N N 214 
LYS HXT  H N N 215 
MET N    N N N 216 
MET CA   C N S 217 
MET C    C N N 218 
MET O    O N N 219 
MET CB   C N N 220 
MET CG   C N N 221 
MET SD   S N N 222 
MET CE   C N N 223 
MET OXT  O N N 224 
MET H    H N N 225 
MET H2   H N N 226 
MET HA   H N N 227 
MET HB2  H N N 228 
MET HB3  H N N 229 
MET HG2  H N N 230 
MET HG3  H N N 231 
MET HE1  H N N 232 
MET HE2  H N N 233 
MET HE3  H N N 234 
MET HXT  H N N 235 
PEG C1   C N N 236 
PEG O1   O N N 237 
PEG C2   C N N 238 
PEG O2   O N N 239 
PEG C3   C N N 240 
PEG C4   C N N 241 
PEG O4   O N N 242 
PEG H11  H N N 243 
PEG H12  H N N 244 
PEG HO1  H N N 245 
PEG H21  H N N 246 
PEG H22  H N N 247 
PEG H31  H N N 248 
PEG H32  H N N 249 
PEG H41  H N N 250 
PEG H42  H N N 251 
PEG HO4  H N N 252 
PHE N    N N N 253 
PHE CA   C N S 254 
PHE C    C N N 255 
PHE O    O N N 256 
PHE CB   C N N 257 
PHE CG   C Y N 258 
PHE CD1  C Y N 259 
PHE CD2  C Y N 260 
PHE CE1  C Y N 261 
PHE CE2  C Y N 262 
PHE CZ   C Y N 263 
PHE OXT  O N N 264 
PHE H    H N N 265 
PHE H2   H N N 266 
PHE HA   H N N 267 
PHE HB2  H N N 268 
PHE HB3  H N N 269 
PHE HD1  H N N 270 
PHE HD2  H N N 271 
PHE HE1  H N N 272 
PHE HE2  H N N 273 
PHE HZ   H N N 274 
PHE HXT  H N N 275 
PRO N    N N N 276 
PRO CA   C N S 277 
PRO C    C N N 278 
PRO O    O N N 279 
PRO CB   C N N 280 
PRO CG   C N N 281 
PRO CD   C N N 282 
PRO OXT  O N N 283 
PRO H    H N N 284 
PRO HA   H N N 285 
PRO HB2  H N N 286 
PRO HB3  H N N 287 
PRO HG2  H N N 288 
PRO HG3  H N N 289 
PRO HD2  H N N 290 
PRO HD3  H N N 291 
PRO HXT  H N N 292 
SER N    N N N 293 
SER CA   C N S 294 
SER C    C N N 295 
SER O    O N N 296 
SER CB   C N N 297 
SER OG   O N N 298 
SER OXT  O N N 299 
SER H    H N N 300 
SER H2   H N N 301 
SER HA   H N N 302 
SER HB2  H N N 303 
SER HB3  H N N 304 
SER HG   H N N 305 
SER HXT  H N N 306 
THR N    N N N 307 
THR CA   C N S 308 
THR C    C N N 309 
THR O    O N N 310 
THR CB   C N R 311 
THR OG1  O N N 312 
THR CG2  C N N 313 
THR OXT  O N N 314 
THR H    H N N 315 
THR H2   H N N 316 
THR HA   H N N 317 
THR HB   H N N 318 
THR HG1  H N N 319 
THR HG21 H N N 320 
THR HG22 H N N 321 
THR HG23 H N N 322 
THR HXT  H N N 323 
TRP N    N N N 324 
TRP CA   C N S 325 
TRP C    C N N 326 
TRP O    O N N 327 
TRP CB   C N N 328 
TRP CG   C Y N 329 
TRP CD1  C Y N 330 
TRP CD2  C Y N 331 
TRP NE1  N Y N 332 
TRP CE2  C Y N 333 
TRP CE3  C Y N 334 
TRP CZ2  C Y N 335 
TRP CZ3  C Y N 336 
TRP CH2  C Y N 337 
TRP OXT  O N N 338 
TRP H    H N N 339 
TRP H2   H N N 340 
TRP HA   H N N 341 
TRP HB2  H N N 342 
TRP HB3  H N N 343 
TRP HD1  H N N 344 
TRP HE1  H N N 345 
TRP HE3  H N N 346 
TRP HZ2  H N N 347 
TRP HZ3  H N N 348 
TRP HH2  H N N 349 
TRP HXT  H N N 350 
TYR N    N N N 351 
TYR CA   C N S 352 
TYR C    C N N 353 
TYR O    O N N 354 
TYR CB   C N N 355 
TYR CG   C Y N 356 
TYR CD1  C Y N 357 
TYR CD2  C Y N 358 
TYR CE1  C Y N 359 
TYR CE2  C Y N 360 
TYR CZ   C Y N 361 
TYR OH   O N N 362 
TYR OXT  O N N 363 
TYR H    H N N 364 
TYR H2   H N N 365 
TYR HA   H N N 366 
TYR HB2  H N N 367 
TYR HB3  H N N 368 
TYR HD1  H N N 369 
TYR HD2  H N N 370 
TYR HE1  H N N 371 
TYR HE2  H N N 372 
TYR HH   H N N 373 
TYR HXT  H N N 374 
VAL N    N N N 375 
VAL CA   C N S 376 
VAL C    C N N 377 
VAL O    O N N 378 
VAL CB   C N N 379 
VAL CG1  C N N 380 
VAL CG2  C N N 381 
VAL OXT  O N N 382 
VAL H    H N N 383 
VAL H2   H N N 384 
VAL HA   H N N 385 
VAL HB   H N N 386 
VAL HG11 H N N 387 
VAL HG12 H N N 388 
VAL HG13 H N N 389 
VAL HG21 H N N 390 
VAL HG22 H N N 391 
VAL HG23 H N N 392 
VAL HXT  H N N 393 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
GLN N   CA   sing N N 70  
GLN N   H    sing N N 71  
GLN N   H2   sing N N 72  
GLN CA  C    sing N N 73  
GLN CA  CB   sing N N 74  
GLN CA  HA   sing N N 75  
GLN C   O    doub N N 76  
GLN C   OXT  sing N N 77  
GLN CB  CG   sing N N 78  
GLN CB  HB2  sing N N 79  
GLN CB  HB3  sing N N 80  
GLN CG  CD   sing N N 81  
GLN CG  HG2  sing N N 82  
GLN CG  HG3  sing N N 83  
GLN CD  OE1  doub N N 84  
GLN CD  NE2  sing N N 85  
GLN NE2 HE21 sing N N 86  
GLN NE2 HE22 sing N N 87  
GLN OXT HXT  sing N N 88  
GLU N   CA   sing N N 89  
GLU N   H    sing N N 90  
GLU N   H2   sing N N 91  
GLU CA  C    sing N N 92  
GLU CA  CB   sing N N 93  
GLU CA  HA   sing N N 94  
GLU C   O    doub N N 95  
GLU C   OXT  sing N N 96  
GLU CB  CG   sing N N 97  
GLU CB  HB2  sing N N 98  
GLU CB  HB3  sing N N 99  
GLU CG  CD   sing N N 100 
GLU CG  HG2  sing N N 101 
GLU CG  HG3  sing N N 102 
GLU CD  OE1  doub N N 103 
GLU CD  OE2  sing N N 104 
GLU OE2 HE2  sing N N 105 
GLU OXT HXT  sing N N 106 
GLY N   CA   sing N N 107 
GLY N   H    sing N N 108 
GLY N   H2   sing N N 109 
GLY CA  C    sing N N 110 
GLY CA  HA2  sing N N 111 
GLY CA  HA3  sing N N 112 
GLY C   O    doub N N 113 
GLY C   OXT  sing N N 114 
GLY OXT HXT  sing N N 115 
HIS N   CA   sing N N 116 
HIS N   H    sing N N 117 
HIS N   H2   sing N N 118 
HIS CA  C    sing N N 119 
HIS CA  CB   sing N N 120 
HIS CA  HA   sing N N 121 
HIS C   O    doub N N 122 
HIS C   OXT  sing N N 123 
HIS CB  CG   sing N N 124 
HIS CB  HB2  sing N N 125 
HIS CB  HB3  sing N N 126 
HIS CG  ND1  sing Y N 127 
HIS CG  CD2  doub Y N 128 
HIS ND1 CE1  doub Y N 129 
HIS ND1 HD1  sing N N 130 
HIS CD2 NE2  sing Y N 131 
HIS CD2 HD2  sing N N 132 
HIS CE1 NE2  sing Y N 133 
HIS CE1 HE1  sing N N 134 
HIS NE2 HE2  sing N N 135 
HIS OXT HXT  sing N N 136 
HOH O   H1   sing N N 137 
HOH O   H2   sing N N 138 
ILE N   CA   sing N N 139 
ILE N   H    sing N N 140 
ILE N   H2   sing N N 141 
ILE CA  C    sing N N 142 
ILE CA  CB   sing N N 143 
ILE CA  HA   sing N N 144 
ILE C   O    doub N N 145 
ILE C   OXT  sing N N 146 
ILE CB  CG1  sing N N 147 
ILE CB  CG2  sing N N 148 
ILE CB  HB   sing N N 149 
ILE CG1 CD1  sing N N 150 
ILE CG1 HG12 sing N N 151 
ILE CG1 HG13 sing N N 152 
ILE CG2 HG21 sing N N 153 
ILE CG2 HG22 sing N N 154 
ILE CG2 HG23 sing N N 155 
ILE CD1 HD11 sing N N 156 
ILE CD1 HD12 sing N N 157 
ILE CD1 HD13 sing N N 158 
ILE OXT HXT  sing N N 159 
LEU N   CA   sing N N 160 
LEU N   H    sing N N 161 
LEU N   H2   sing N N 162 
LEU CA  C    sing N N 163 
LEU CA  CB   sing N N 164 
LEU CA  HA   sing N N 165 
LEU C   O    doub N N 166 
LEU C   OXT  sing N N 167 
LEU CB  CG   sing N N 168 
LEU CB  HB2  sing N N 169 
LEU CB  HB3  sing N N 170 
LEU CG  CD1  sing N N 171 
LEU CG  CD2  sing N N 172 
LEU CG  HG   sing N N 173 
LEU CD1 HD11 sing N N 174 
LEU CD1 HD12 sing N N 175 
LEU CD1 HD13 sing N N 176 
LEU CD2 HD21 sing N N 177 
LEU CD2 HD22 sing N N 178 
LEU CD2 HD23 sing N N 179 
LEU OXT HXT  sing N N 180 
LYS N   CA   sing N N 181 
LYS N   H    sing N N 182 
LYS N   H2   sing N N 183 
LYS CA  C    sing N N 184 
LYS CA  CB   sing N N 185 
LYS CA  HA   sing N N 186 
LYS C   O    doub N N 187 
LYS C   OXT  sing N N 188 
LYS CB  CG   sing N N 189 
LYS CB  HB2  sing N N 190 
LYS CB  HB3  sing N N 191 
LYS CG  CD   sing N N 192 
LYS CG  HG2  sing N N 193 
LYS CG  HG3  sing N N 194 
LYS CD  CE   sing N N 195 
LYS CD  HD2  sing N N 196 
LYS CD  HD3  sing N N 197 
LYS CE  NZ   sing N N 198 
LYS CE  HE2  sing N N 199 
LYS CE  HE3  sing N N 200 
LYS NZ  HZ1  sing N N 201 
LYS NZ  HZ2  sing N N 202 
LYS NZ  HZ3  sing N N 203 
LYS OXT HXT  sing N N 204 
MET N   CA   sing N N 205 
MET N   H    sing N N 206 
MET N   H2   sing N N 207 
MET CA  C    sing N N 208 
MET CA  CB   sing N N 209 
MET CA  HA   sing N N 210 
MET C   O    doub N N 211 
MET C   OXT  sing N N 212 
MET CB  CG   sing N N 213 
MET CB  HB2  sing N N 214 
MET CB  HB3  sing N N 215 
MET CG  SD   sing N N 216 
MET CG  HG2  sing N N 217 
MET CG  HG3  sing N N 218 
MET SD  CE   sing N N 219 
MET CE  HE1  sing N N 220 
MET CE  HE2  sing N N 221 
MET CE  HE3  sing N N 222 
MET OXT HXT  sing N N 223 
PEG C1  O1   sing N N 224 
PEG C1  C2   sing N N 225 
PEG C1  H11  sing N N 226 
PEG C1  H12  sing N N 227 
PEG O1  HO1  sing N N 228 
PEG C2  O2   sing N N 229 
PEG C2  H21  sing N N 230 
PEG C2  H22  sing N N 231 
PEG O2  C3   sing N N 232 
PEG C3  C4   sing N N 233 
PEG C3  H31  sing N N 234 
PEG C3  H32  sing N N 235 
PEG C4  O4   sing N N 236 
PEG C4  H41  sing N N 237 
PEG C4  H42  sing N N 238 
PEG O4  HO4  sing N N 239 
PHE N   CA   sing N N 240 
PHE N   H    sing N N 241 
PHE N   H2   sing N N 242 
PHE CA  C    sing N N 243 
PHE CA  CB   sing N N 244 
PHE CA  HA   sing N N 245 
PHE C   O    doub N N 246 
PHE C   OXT  sing N N 247 
PHE CB  CG   sing N N 248 
PHE CB  HB2  sing N N 249 
PHE CB  HB3  sing N N 250 
PHE CG  CD1  doub Y N 251 
PHE CG  CD2  sing Y N 252 
PHE CD1 CE1  sing Y N 253 
PHE CD1 HD1  sing N N 254 
PHE CD2 CE2  doub Y N 255 
PHE CD2 HD2  sing N N 256 
PHE CE1 CZ   doub Y N 257 
PHE CE1 HE1  sing N N 258 
PHE CE2 CZ   sing Y N 259 
PHE CE2 HE2  sing N N 260 
PHE CZ  HZ   sing N N 261 
PHE OXT HXT  sing N N 262 
PRO N   CA   sing N N 263 
PRO N   CD   sing N N 264 
PRO N   H    sing N N 265 
PRO CA  C    sing N N 266 
PRO CA  CB   sing N N 267 
PRO CA  HA   sing N N 268 
PRO C   O    doub N N 269 
PRO C   OXT  sing N N 270 
PRO CB  CG   sing N N 271 
PRO CB  HB2  sing N N 272 
PRO CB  HB3  sing N N 273 
PRO CG  CD   sing N N 274 
PRO CG  HG2  sing N N 275 
PRO CG  HG3  sing N N 276 
PRO CD  HD2  sing N N 277 
PRO CD  HD3  sing N N 278 
PRO OXT HXT  sing N N 279 
SER N   CA   sing N N 280 
SER N   H    sing N N 281 
SER N   H2   sing N N 282 
SER CA  C    sing N N 283 
SER CA  CB   sing N N 284 
SER CA  HA   sing N N 285 
SER C   O    doub N N 286 
SER C   OXT  sing N N 287 
SER CB  OG   sing N N 288 
SER CB  HB2  sing N N 289 
SER CB  HB3  sing N N 290 
SER OG  HG   sing N N 291 
SER OXT HXT  sing N N 292 
THR N   CA   sing N N 293 
THR N   H    sing N N 294 
THR N   H2   sing N N 295 
THR CA  C    sing N N 296 
THR CA  CB   sing N N 297 
THR CA  HA   sing N N 298 
THR C   O    doub N N 299 
THR C   OXT  sing N N 300 
THR CB  OG1  sing N N 301 
THR CB  CG2  sing N N 302 
THR CB  HB   sing N N 303 
THR OG1 HG1  sing N N 304 
THR CG2 HG21 sing N N 305 
THR CG2 HG22 sing N N 306 
THR CG2 HG23 sing N N 307 
THR OXT HXT  sing N N 308 
TRP N   CA   sing N N 309 
TRP N   H    sing N N 310 
TRP N   H2   sing N N 311 
TRP CA  C    sing N N 312 
TRP CA  CB   sing N N 313 
TRP CA  HA   sing N N 314 
TRP C   O    doub N N 315 
TRP C   OXT  sing N N 316 
TRP CB  CG   sing N N 317 
TRP CB  HB2  sing N N 318 
TRP CB  HB3  sing N N 319 
TRP CG  CD1  doub Y N 320 
TRP CG  CD2  sing Y N 321 
TRP CD1 NE1  sing Y N 322 
TRP CD1 HD1  sing N N 323 
TRP CD2 CE2  doub Y N 324 
TRP CD2 CE3  sing Y N 325 
TRP NE1 CE2  sing Y N 326 
TRP NE1 HE1  sing N N 327 
TRP CE2 CZ2  sing Y N 328 
TRP CE3 CZ3  doub Y N 329 
TRP CE3 HE3  sing N N 330 
TRP CZ2 CH2  doub Y N 331 
TRP CZ2 HZ2  sing N N 332 
TRP CZ3 CH2  sing Y N 333 
TRP CZ3 HZ3  sing N N 334 
TRP CH2 HH2  sing N N 335 
TRP OXT HXT  sing N N 336 
TYR N   CA   sing N N 337 
TYR N   H    sing N N 338 
TYR N   H2   sing N N 339 
TYR CA  C    sing N N 340 
TYR CA  CB   sing N N 341 
TYR CA  HA   sing N N 342 
TYR C   O    doub N N 343 
TYR C   OXT  sing N N 344 
TYR CB  CG   sing N N 345 
TYR CB  HB2  sing N N 346 
TYR CB  HB3  sing N N 347 
TYR CG  CD1  doub Y N 348 
TYR CG  CD2  sing Y N 349 
TYR CD1 CE1  sing Y N 350 
TYR CD1 HD1  sing N N 351 
TYR CD2 CE2  doub Y N 352 
TYR CD2 HD2  sing N N 353 
TYR CE1 CZ   doub Y N 354 
TYR CE1 HE1  sing N N 355 
TYR CE2 CZ   sing Y N 356 
TYR CE2 HE2  sing N N 357 
TYR CZ  OH   sing N N 358 
TYR OH  HH   sing N N 359 
TYR OXT HXT  sing N N 360 
VAL N   CA   sing N N 361 
VAL N   H    sing N N 362 
VAL N   H2   sing N N 363 
VAL CA  C    sing N N 364 
VAL CA  CB   sing N N 365 
VAL CA  HA   sing N N 366 
VAL C   O    doub N N 367 
VAL C   OXT  sing N N 368 
VAL CB  CG1  sing N N 369 
VAL CB  CG2  sing N N 370 
VAL CB  HB   sing N N 371 
VAL CG1 HG11 sing N N 372 
VAL CG1 HG12 sing N N 373 
VAL CG1 HG13 sing N N 374 
VAL CG2 HG21 sing N N 375 
VAL CG2 HG22 sing N N 376 
VAL CG2 HG23 sing N N 377 
VAL OXT HXT  sing N N 378 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'Japan Society for the Promotion of Science (JSPS)' Japan 24K08698   1 
'Japan Science and Technology'                      Japan JPMJSP2116 2 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   3W9A 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9K7O 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.013918 
_atom_sites.fract_transf_matrix[1][2]   0.008036 
_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]   0.016071 
_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]   0.004429 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
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   . GLY A 1 2   ? 7.408   -0.679  25.989 1.00 31.16  ? 18  GLY A N   1 
ATOM   2    C CA  . GLY A 1 2   ? 6.912   -1.996  25.557 1.00 31.08  ? 18  GLY A CA  1 
ATOM   3    C C   . GLY A 1 2   ? 5.759   -2.463  26.432 1.00 29.76  ? 18  GLY A C   1 
ATOM   4    O O   . GLY A 1 2   ? 5.515   -1.909  27.495 1.00 30.07  ? 18  GLY A O   1 
ATOM   5    N N   . LYS A 1 3   ? 5.061   -3.499  25.982 1.00 31.37  ? 19  LYS A N   1 
ATOM   6    C CA  . LYS A 1 3   ? 4.055   -4.105  26.830 1.00 32.00  ? 19  LYS A CA  1 
ATOM   7    C C   . LYS A 1 3   ? 4.765   -5.018  27.824 1.00 30.62  ? 19  LYS A C   1 
ATOM   8    O O   . LYS A 1 3   ? 5.677   -5.742  27.419 1.00 26.02  ? 19  LYS A O   1 
ATOM   9    C CB  . LYS A 1 3   ? 3.044   -4.910  26.011 1.00 36.50  ? 19  LYS A CB  1 
ATOM   10   C CG  . LYS A 1 3   ? 2.018   -5.650  26.866 1.00 41.26  ? 19  LYS A CG  1 
ATOM   11   C CD  . LYS A 1 3   ? 0.711   -5.997  26.171 1.00 45.61  ? 19  LYS A CD  1 
ATOM   12   C CE  . LYS A 1 3   ? 0.903   -6.659  24.826 1.00 48.76  ? 19  LYS A CE  1 
ATOM   13   N NZ  . LYS A 1 3   ? 1.814   -7.825  24.885 1.00 50.20  ? 19  LYS A NZ  1 
ATOM   14   N N   . VAL A 1 4   ? 4.302   -5.020  29.087 1.00 29.11  ? 20  VAL A N   1 
ATOM   15   C CA  . VAL A 1 4   ? 4.900   -5.864  30.108 1.00 28.08  ? 20  VAL A CA  1 
ATOM   16   C C   . VAL A 1 4   ? 4.417   -7.289  29.879 1.00 28.95  ? 20  VAL A C   1 
ATOM   17   O O   . VAL A 1 4   ? 3.218   -7.523  29.757 1.00 31.47  ? 20  VAL A O   1 
ATOM   18   C CB  . VAL A 1 4   ? 4.592   -5.373  31.535 1.00 29.46  ? 20  VAL A CB  1 
ATOM   19   C CG1 . VAL A 1 4   ? 5.272   -6.266  32.564 1.00 29.92  ? 20  VAL A CG1 1 
ATOM   20   C CG2 . VAL A 1 4   ? 4.990   -3.914  31.751 1.00 28.65  ? 20  VAL A CG2 1 
ATOM   21   N N   . LEU A 1 5   ? 5.360   -8.223  29.764 1.00 25.68  ? 21  LEU A N   1 
ATOM   22   C CA  . LEU A 1 5   ? 5.031   -9.620  29.542 1.00 26.39  ? 21  LEU A CA  1 
ATOM   23   C C   . LEU A 1 5   ? 4.943   -10.353 30.873 1.00 28.18  ? 21  LEU A C   1 
ATOM   24   O O   . LEU A 1 5   ? 4.202   -11.328 30.975 1.00 27.03  ? 21  LEU A O   1 
ATOM   25   C CB  . LEU A 1 5   ? 6.086   -10.250 28.640 1.00 25.76  ? 21  LEU A CB  1 
ATOM   26   C CG  . LEU A 1 5   ? 6.313   -9.542  27.304 1.00 27.81  ? 21  LEU A CG  1 
ATOM   27   C CD1 . LEU A 1 5   ? 7.399   -10.243 26.498 1.00 25.61  ? 21  LEU A CD1 1 
ATOM   28   C CD2 . LEU A 1 5   ? 5.015   -9.439  26.502 1.00 27.31  ? 21  LEU A CD2 1 
ATOM   29   N N   . TRP A 1 6   ? 5.745   -9.905  31.860 1.00 26.69  ? 22  TRP A N   1 
ATOM   30   C CA  . TRP A 1 6   ? 5.794   -10.476 33.190 1.00 24.82  ? 22  TRP A CA  1 
ATOM   31   C C   . TRP A 1 6   ? 6.411   -9.425  34.098 1.00 25.23  ? 22  TRP A C   1 
ATOM   32   O O   . TRP A 1 6   ? 7.434   -8.838  33.736 1.00 25.67  ? 22  TRP A O   1 
ATOM   33   C CB  . TRP A 1 6   ? 6.632   -11.771 33.204 1.00 25.99  ? 22  TRP A CB  1 
ATOM   34   C CG  . TRP A 1 6   ? 6.985   -12.264 34.586 1.00 25.22  ? 22  TRP A CG  1 
ATOM   35   C CD1 . TRP A 1 6   ? 6.238   -13.062 35.401 1.00 26.81  ? 22  TRP A CD1 1 
ATOM   36   C CD2 . TRP A 1 6   ? 8.185   -11.969 35.333 1.00 24.95  ? 22  TRP A CD2 1 
ATOM   37   N NE1 . TRP A 1 6   ? 6.868   -13.261 36.599 1.00 27.85  ? 22  TRP A NE1 1 
ATOM   38   C CE2 . TRP A 1 6   ? 8.071   -12.608 36.584 1.00 23.97  ? 22  TRP A CE2 1 
ATOM   39   C CE3 . TRP A 1 6   ? 9.327   -11.221 35.070 1.00 24.55  ? 22  TRP A CE3 1 
ATOM   40   C CZ2 . TRP A 1 6   ? 9.063   -12.524 37.561 1.00 23.45  ? 22  TRP A CZ2 1 
ATOM   41   C CZ3 . TRP A 1 6   ? 10.305  -11.138 36.035 1.00 26.62  ? 22  TRP A CZ3 1 
ATOM   42   C CH2 . TRP A 1 6   ? 10.175  -11.783 37.264 1.00 23.52  ? 22  TRP A CH2 1 
ATOM   43   N N   . ASP A 1 7   ? 5.825   -9.207  35.274 1.00 23.50  ? 23  ASP A N   1 
ATOM   44   C CA  . ASP A 1 7   ? 6.315   -8.175  36.168 1.00 23.54  ? 23  ASP A CA  1 
ATOM   45   C C   . ASP A 1 7   ? 6.740   -8.806  37.497 1.00 26.55  ? 23  ASP A C   1 
ATOM   46   O O   . ASP A 1 7   ? 5.916   -9.197  38.324 1.00 25.94  ? 23  ASP A O   1 
ATOM   47   C CB  . ASP A 1 7   ? 5.240   -7.106  36.309 1.00 25.67  ? 23  ASP A CB  1 
ATOM   48   C CG  . ASP A 1 7   ? 5.690   -5.826  36.984 1.00 25.19  ? 23  ASP A CG  1 
ATOM   49   O OD1 . ASP A 1 7   ? 6.780   -5.819  37.557 1.00 23.50  ? 23  ASP A OD1 1 
ATOM   50   O OD2 . ASP A 1 7   ? 4.940   -4.845  36.913 1.00 24.03  ? 23  ASP A OD2 1 
ATOM   51   N N   . GLY A 1 8   ? 8.057   -8.897  37.711 1.00 25.51  ? 24  GLY A N   1 
ATOM   52   C CA  . GLY A 1 8   ? 8.603   -9.322  38.991 1.00 23.77  ? 24  GLY A CA  1 
ATOM   53   C C   . GLY A 1 8   ? 8.924   -8.185  39.954 1.00 23.83  ? 24  GLY A C   1 
ATOM   54   O O   . GLY A 1 8   ? 9.627   -8.399  40.933 1.00 23.23  ? 24  GLY A O   1 
ATOM   55   N N   . ARG A 1 9   ? 8.365   -6.988  39.732 1.00 23.11  ? 25  ARG A N   1 
ATOM   56   C CA  . ARG A 1 9   ? 8.458   -5.931  40.724 1.00 24.01  ? 25  ARG A CA  1 
ATOM   57   C C   . ARG A 1 9   ? 7.453   -6.220  41.835 1.00 24.65  ? 25  ARG A C   1 
ATOM   58   O O   . ARG A 1 9   ? 6.246   -6.127  41.641 1.00 31.25  ? 25  ARG A O   1 
ATOM   59   C CB  . ARG A 1 9   ? 8.240   -4.572  40.050 1.00 25.26  ? 25  ARG A CB  1 
ATOM   60   C CG  . ARG A 1 9   ? 9.354   -4.206  39.074 1.00 25.00  ? 25  ARG A CG  1 
ATOM   61   C CD  . ARG A 1 9   ? 9.045   -3.023  38.180 1.00 27.63  ? 25  ARG A CD  1 
ATOM   62   N NE  . ARG A 1 9   ? 7.949   -3.287  37.257 1.00 28.02  ? 25  ARG A NE  1 
ATOM   63   C CZ  . ARG A 1 9   ? 7.594   -2.508  36.231 1.00 26.96  ? 25  ARG A CZ  1 
ATOM   64   N NH1 . ARG A 1 9   ? 8.254   -1.397  35.966 1.00 25.68  ? 25  ARG A NH1 1 
ATOM   65   N NH2 . ARG A 1 9   ? 6.586   -2.860  35.449 1.00 23.40  ? 25  ARG A NH2 1 
ATOM   66   N N   . ALA A 1 10  ? 7.948   -6.616  42.999 1.00 26.60  ? 26  ALA A N   1 
ATOM   67   C CA  . ALA A 1 10  ? 7.089   -7.050  44.087 1.00 23.30  ? 26  ALA A CA  1 
ATOM   68   C C   . ALA A 1 10  ? 6.124   -5.929  44.458 1.00 25.10  ? 26  ALA A C   1 
ATOM   69   O O   . ALA A 1 10  ? 6.555   -4.812  44.770 1.00 26.44  ? 26  ALA A O   1 
ATOM   70   C CB  . ALA A 1 10  ? 7.916   -7.431  45.275 1.00 21.67  ? 26  ALA A CB  1 
ATOM   71   N N   . PRO A 1 11  ? 4.793   -6.182  44.416 1.00 27.84  ? 27  PRO A N   1 
ATOM   72   C CA  . PRO A 1 11  ? 3.825   -5.208  44.908 1.00 28.00  ? 27  PRO A CA  1 
ATOM   73   C C   . PRO A 1 11  ? 4.108   -4.857  46.365 1.00 31.60  ? 27  PRO A C   1 
ATOM   74   O O   . PRO A 1 11  ? 4.631   -5.671  47.134 1.00 30.67  ? 27  PRO A O   1 
ATOM   75   C CB  . PRO A 1 11  ? 2.476   -5.918  44.727 1.00 30.12  ? 27  PRO A CB  1 
ATOM   76   C CG  . PRO A 1 11  ? 2.720   -6.867  43.581 1.00 29.69  ? 27  PRO A CG  1 
ATOM   77   C CD  . PRO A 1 11  ? 4.141   -7.354  43.801 1.00 28.17  ? 27  PRO A CD  1 
ATOM   78   N N   . ARG A 1 12  ? 3.721   -3.642  46.740 1.00 29.76  ? 28  ARG A N   1 
ATOM   79   C CA  . ARG A 1 12  ? 3.891   -3.173  48.102 1.00 35.93  ? 28  ARG A CA  1 
ATOM   80   C C   . ARG A 1 12  ? 3.086   -4.030  49.083 1.00 35.21  ? 28  ARG A C   1 
ATOM   81   O O   . ARG A 1 12  ? 3.444   -4.083  50.252 1.00 32.85  ? 28  ARG A O   1 
ATOM   82   C CB  . ARG A 1 12  ? 3.523   -1.687  48.182 1.00 36.04  ? 28  ARG A CB  1 
ATOM   83   C CG  . ARG A 1 12  ? 4.424   -0.800  47.334 1.00 42.19  ? 28  ARG A CG  1 
ATOM   84   C CD  . ARG A 1 12  ? 3.995   0.656   47.306 1.00 48.54  ? 28  ARG A CD  1 
ATOM   85   N NE  . ARG A 1 12  ? 2.584   0.850   46.968 1.00 52.89  ? 28  ARG A NE  1 
ATOM   86   C CZ  . ARG A 1 12  ? 2.102   1.776   46.137 1.00 55.80  ? 28  ARG A CZ  1 
ATOM   87   N NH1 . ARG A 1 12  ? 2.913   2.509   45.395 1.00 63.09  ? 28  ARG A NH1 1 
ATOM   88   N NH2 . ARG A 1 12  ? 0.795   1.934   46.013 1.00 51.04  ? 28  ARG A NH2 1 
ATOM   89   N N   . ASN A 1 13  ? 2.052   -4.757  48.620 1.00 40.12  ? 29  ASN A N   1 
ATOM   90   C CA  . ASN A 1 13  ? 1.254   -5.571  49.530 1.00 42.41  ? 29  ASN A CA  1 
ATOM   91   C C   . ASN A 1 13  ? 1.660   -7.044  49.467 1.00 39.95  ? 29  ASN A C   1 
ATOM   92   O O   . ASN A 1 13  ? 0.978   -7.874  50.062 1.00 37.58  ? 29  ASN A O   1 
ATOM   93   C CB  . ASN A 1 13  ? -0.256  -5.390  49.313 1.00 45.13  ? 29  ASN A CB  1 
ATOM   94   C CG  . ASN A 1 13  ? -0.731  -5.751  47.920 1.00 52.39  ? 29  ASN A CG  1 
ATOM   95   O OD1 . ASN A 1 13  ? -0.006  -6.347  47.122 1.00 57.22  ? 29  ASN A OD1 1 
ATOM   96   N ND2 . ASN A 1 13  ? -1.961  -5.377  47.610 1.00 57.13  ? 29  ASN A ND2 1 
ATOM   97   N N   . TYR A 1 14  ? 2.765   -7.375  48.767 1.00 36.90  ? 30  TYR A N   1 
ATOM   98   C CA  . TYR A 1 14  ? 3.259   -8.751  48.722 1.00 31.46  ? 30  TYR A CA  1 
ATOM   99   C C   . TYR A 1 14  ? 3.802   -9.145  50.098 1.00 29.32  ? 30  TYR A C   1 
ATOM   100  O O   . TYR A 1 14  ? 4.339   -8.323  50.819 1.00 31.57  ? 30  TYR A O   1 
ATOM   101  C CB  . TYR A 1 14  ? 4.371   -8.932  47.684 1.00 29.50  ? 30  TYR A CB  1 
ATOM   102  C CG  . TYR A 1 14  ? 4.361   -10.260 46.947 1.00 27.69  ? 30  TYR A CG  1 
ATOM   103  C CD1 . TYR A 1 14  ? 3.352   -10.557 46.032 1.00 28.11  ? 30  TYR A CD1 1 
ATOM   104  C CD2 . TYR A 1 14  ? 5.363   -11.208 47.134 1.00 27.68  ? 30  TYR A CD2 1 
ATOM   105  C CE1 . TYR A 1 14  ? 3.319   -11.766 45.349 1.00 28.20  ? 30  TYR A CE1 1 
ATOM   106  C CE2 . TYR A 1 14  ? 5.341   -12.415 46.446 1.00 27.72  ? 30  TYR A CE2 1 
ATOM   107  C CZ  . TYR A 1 14  ? 4.329   -12.696 45.543 1.00 30.22  ? 30  TYR A CZ  1 
ATOM   108  O OH  . TYR A 1 14  ? 4.300   -13.888 44.848 1.00 32.83  ? 30  TYR A OH  1 
ATOM   109  N N   . THR A 1 15  ? 3.693   -10.424 50.441 1.00 28.27  ? 31  THR A N   1 
ATOM   110  C CA  . THR A 1 15  ? 4.051   -10.919 51.755 1.00 29.71  ? 31  THR A CA  1 
ATOM   111  C C   . THR A 1 15  ? 4.850   -12.215 51.629 1.00 29.01  ? 31  THR A C   1 
ATOM   112  O O   . THR A 1 15  ? 4.766   -12.915 50.628 1.00 31.19  ? 31  THR A O   1 
ATOM   113  C CB  . THR A 1 15  ? 2.802   -11.238 52.590 1.00 29.07  ? 31  THR A CB  1 
ATOM   114  O OG1 . THR A 1 15  ? 2.216   -12.389 51.986 1.00 29.77  ? 31  THR A OG1 1 
ATOM   115  C CG2 . THR A 1 15  ? 1.815   -10.086 52.656 1.00 33.80  ? 31  THR A CG2 1 
ATOM   116  N N   . SER A 1 16  ? 5.548   -12.558 52.712 1.00 30.36  ? 32  SER A N   1 
ATOM   117  C CA  . SER A 1 16  ? 6.135   -13.866 52.909 1.00 31.55  ? 32  SER A CA  1 
ATOM   118  C C   . SER A 1 16  ? 5.167   -14.996 52.556 1.00 33.74  ? 32  SER A C   1 
ATOM   119  O O   . SER A 1 16  ? 5.602   -16.061 52.109 1.00 34.93  ? 32  SER A O   1 
ATOM   120  C CB  . SER A 1 16  ? 6.612   -13.983 54.340 1.00 35.27  ? 32  SER A CB  1 
ATOM   121  O OG  . SER A 1 16  ? 5.524   -13.950 55.248 1.00 39.10  ? 32  SER A OG  1 
ATOM   122  N N   . PHE A 1 17  ? 3.862   -14.793 52.812 1.00 30.31  ? 33  PHE A N   1 
ATOM   123  C CA  . PHE A 1 17  ? 2.879   -15.856 52.623 1.00 31.07  ? 33  PHE A CA  1 
ATOM   124  C C   . PHE A 1 17  ? 2.652   -16.121 51.137 1.00 29.93  ? 33  PHE A C   1 
ATOM   125  O O   . PHE A 1 17  ? 2.405   -17.253 50.725 1.00 32.77  ? 33  PHE A O   1 
ATOM   126  C CB  . PHE A 1 17  ? 1.588   -15.511 53.379 1.00 32.94  ? 33  PHE A CB  1 
ATOM   127  C CG  . PHE A 1 17  ? 1.775   -15.598 54.868 1.00 31.26  ? 33  PHE A CG  1 
ATOM   128  C CD1 . PHE A 1 17  ? 1.769   -16.829 55.502 1.00 34.60  ? 33  PHE A CD1 1 
ATOM   129  C CD2 . PHE A 1 17  ? 2.074   -14.471 55.609 1.00 31.02  ? 33  PHE A CD2 1 
ATOM   130  C CE1 . PHE A 1 17  ? 2.005   -16.920 56.861 1.00 33.86  ? 33  PHE A CE1 1 
ATOM   131  C CE2 . PHE A 1 17  ? 2.330   -14.570 56.965 1.00 31.62  ? 33  PHE A CE2 1 
ATOM   132  C CZ  . PHE A 1 17  ? 2.293   -15.789 57.586 1.00 33.01  ? 33  PHE A CZ  1 
ATOM   133  N N   . HIS A 1 18  ? 2.752   -15.073 50.321 1.00 32.14  ? 34  HIS A N   1 
ATOM   134  C CA  . HIS A 1 18  ? 2.686   -15.252 48.887 1.00 31.95  ? 34  HIS A CA  1 
ATOM   135  C C   . HIS A 1 18  ? 3.884   -16.092 48.458 1.00 31.76  ? 34  HIS A C   1 
ATOM   136  O O   . HIS A 1 18  ? 3.746   -17.005 47.637 1.00 29.18  ? 34  HIS A O   1 
ATOM   137  C CB  . HIS A 1 18  ? 2.708   -13.911 48.135 1.00 33.79  ? 34  HIS A CB  1 
ATOM   138  C CG  . HIS A 1 18  ? 1.512   -13.024 48.241 1.00 34.71  ? 34  HIS A CG  1 
ATOM   139  N ND1 . HIS A 1 18  ? 1.312   -12.087 49.235 1.00 34.24  ? 34  HIS A ND1 1 
ATOM   140  C CD2 . HIS A 1 18  ? 0.517   -12.867 47.373 1.00 35.41  ? 34  HIS A CD2 1 
ATOM   141  C CE1 . HIS A 1 18  ? 0.196   -11.428 48.977 1.00 37.67  ? 34  HIS A CE1 1 
ATOM   142  N NE2 . HIS A 1 18  ? -0.311  -11.894 47.860 1.00 34.91  ? 34  HIS A NE2 1 
ATOM   143  N N   . LEU A 1 19  ? 5.058   -15.740 48.999 1.00 31.09  ? 35  LEU A N   1 
ATOM   144  C CA  . LEU A 1 19  ? 6.289   -16.443 48.670 1.00 32.10  ? 35  LEU A CA  1 
ATOM   145  C C   . LEU A 1 19  ? 6.196   -17.911 49.089 1.00 33.67  ? 35  LEU A C   1 
ATOM   146  O O   . LEU A 1 19  ? 6.628   -18.804 48.364 1.00 31.80  ? 35  LEU A O   1 
ATOM   147  C CB  . LEU A 1 19  ? 7.481   -15.768 49.352 1.00 29.77  ? 35  LEU A CB  1 
ATOM   148  C CG  . LEU A 1 19  ? 7.993   -14.485 48.703 1.00 30.08  ? 35  LEU A CG  1 
ATOM   149  C CD1 . LEU A 1 19  ? 9.084   -13.865 49.560 1.00 31.45  ? 35  LEU A CD1 1 
ATOM   150  C CD2 . LEU A 1 19  ? 8.505   -14.757 47.294 1.00 29.56  ? 35  LEU A CD2 1 
ATOM   151  N N   . ASP A 1 20  ? 5.624   -18.184 50.256 1.00 36.97  ? 36  ASP A N   1 
ATOM   152  C CA  . ASP A 1 20  ? 5.565   -19.568 50.715 1.00 35.17  ? 36  ASP A CA  1 
ATOM   153  C C   . ASP A 1 20  ? 4.451   -20.344 50.000 1.00 39.17  ? 36  ASP A C   1 
ATOM   154  O O   . ASP A 1 20  ? 4.391   -21.564 50.130 1.00 45.56  ? 36  ASP A O   1 
ATOM   155  C CB  . ASP A 1 20  ? 5.450   -19.610 52.237 1.00 34.29  ? 36  ASP A CB  1 
ATOM   156  C CG  . ASP A 1 20  ? 6.639   -19.000 52.953 1.00 33.01  ? 36  ASP A CG  1 
ATOM   157  O OD1 . ASP A 1 20  ? 7.741   -18.997 52.375 1.00 30.69  ? 36  ASP A OD1 1 
ATOM   158  O OD2 . ASP A 1 20  ? 6.443   -18.476 54.060 1.00 35.65  ? 36  ASP A OD2 1 
ATOM   159  N N   . ALA A 1 21  ? 3.580   -19.668 49.233 1.00 34.54  ? 37  ALA A N   1 
ATOM   160  C CA  . ALA A 1 21  ? 2.631   -20.372 48.376 1.00 34.59  ? 37  ALA A CA  1 
ATOM   161  C C   . ALA A 1 21  ? 3.160   -20.505 46.953 1.00 33.47  ? 37  ALA A C   1 
ATOM   162  O O   . ALA A 1 21  ? 2.567   -21.214 46.157 1.00 33.97  ? 37  ALA A O   1 
ATOM   163  C CB  . ALA A 1 21  ? 1.283   -19.690 48.386 1.00 38.24  ? 37  ALA A CB  1 
ATOM   164  N N   . SER A 1 22  ? 4.290   -19.858 46.631 1.00 33.71  ? 38  SER A N   1 
ATOM   165  C CA  . SER A 1 22  ? 4.851   -19.926 45.287 1.00 32.85  ? 38  SER A CA  1 
ATOM   166  C C   . SER A 1 22  ? 3.822   -19.428 44.258 1.00 28.85  ? 38  SER A C   1 
ATOM   167  O O   . SER A 1 22  ? 3.621   -20.039 43.218 1.00 29.84  ? 38  SER A O   1 
ATOM   168  C CB  . SER A 1 22  ? 5.354   -21.332 44.974 1.00 32.23  ? 38  SER A CB  1 
ATOM   169  O OG  . SER A 1 22  ? 6.126   -21.368 43.765 1.00 31.67  ? 38  SER A OG  1 
ATOM   170  N N   . VAL A 1 23  ? 3.168   -18.298 44.532 1.00 27.87  ? 39  VAL A N   1 
ATOM   171  C CA  . VAL A 1 23  ? 2.201   -17.768 43.582 1.00 32.01  ? 39  VAL A CA  1 
ATOM   172  C C   . VAL A 1 23  ? 2.857   -16.695 42.710 1.00 34.78  ? 39  VAL A C   1 
ATOM   173  O O   . VAL A 1 23  ? 3.999   -16.251 42.929 1.00 30.24  ? 39  VAL A O   1 
ATOM   174  C CB  . VAL A 1 23  ? 0.914   -17.213 44.235 1.00 31.68  ? 39  VAL A CB  1 
ATOM   175  C CG1 . VAL A 1 23  ? 0.017   -18.330 44.736 1.00 32.93  ? 39  VAL A CG1 1 
ATOM   176  C CG2 . VAL A 1 23  ? 1.196   -16.189 45.327 1.00 31.17  ? 39  VAL A CG2 1 
ATOM   177  N N   . ASP A 1 24  ? 2.076   -16.276 41.710 1.00 32.87  ? 40  ASP A N   1 
ATOM   178  C CA  . ASP A 1 24  ? 2.506   -15.229 40.808 1.00 30.44  ? 40  ASP A CA  1 
ATOM   179  C C   . ASP A 1 24  ? 2.982   -14.044 41.646 1.00 29.96  ? 40  ASP A C   1 
ATOM   180  O O   . ASP A 1 24  ? 2.422   -13.735 42.702 1.00 31.93  ? 40  ASP A O   1 
ATOM   181  C CB  . ASP A 1 24  ? 1.404   -14.888 39.805 1.00 29.74  ? 40  ASP A CB  1 
ATOM   182  C CG  . ASP A 1 24  ? 1.186   -15.937 38.724 1.00 32.49  ? 40  ASP A CG  1 
ATOM   183  O OD1 . ASP A 1 24  ? 1.944   -16.937 38.670 1.00 32.22  ? 40  ASP A OD1 1 
ATOM   184  O OD2 . ASP A 1 24  ? 0.250   -15.756 37.935 1.00 31.20  ? 40  ASP A OD2 1 
ATOM   185  N N   . PRO A 1 25  ? 4.067   -13.358 41.228 1.00 28.76  ? 41  PRO A N   1 
ATOM   186  C CA  . PRO A 1 25  ? 4.785   -13.683 39.994 1.00 27.08  ? 41  PRO A CA  1 
ATOM   187  C C   . PRO A 1 25  ? 6.020   -14.584 40.044 1.00 26.47  ? 41  PRO A C   1 
ATOM   188  O O   . PRO A 1 25  ? 6.742   -14.650 39.053 1.00 27.87  ? 41  PRO A O   1 
ATOM   189  C CB  . PRO A 1 25  ? 5.207   -12.260 39.562 1.00 27.75  ? 41  PRO A CB  1 
ATOM   190  C CG  . PRO A 1 25  ? 5.412   -11.477 40.827 1.00 27.45  ? 41  PRO A CG  1 
ATOM   191  C CD  . PRO A 1 25  ? 4.604   -12.165 41.900 1.00 29.70  ? 41  PRO A CD  1 
ATOM   192  N N   . TYR A 1 26  ? 6.271   -15.273 41.167 1.00 28.25  ? 42  TYR A N   1 
ATOM   193  C CA  . TYR A 1 26  ? 7.512   -16.016 41.344 1.00 27.94  ? 42  TYR A CA  1 
ATOM   194  C C   . TYR A 1 26  ? 7.303   -17.495 41.678 1.00 26.97  ? 42  TYR A C   1 
ATOM   195  O O   . TYR A 1 26  ? 6.621   -17.822 42.646 1.00 26.39  ? 42  TYR A O   1 
ATOM   196  C CB  . TYR A 1 26  ? 8.267   -15.429 42.542 1.00 28.02  ? 42  TYR A CB  1 
ATOM   197  C CG  . TYR A 1 26  ? 8.346   -13.915 42.616 1.00 26.75  ? 42  TYR A CG  1 
ATOM   198  C CD1 . TYR A 1 26  ? 9.087   -13.183 41.691 1.00 28.68  ? 42  TYR A CD1 1 
ATOM   199  C CD2 . TYR A 1 26  ? 7.735   -13.218 43.647 1.00 29.42  ? 42  TYR A CD2 1 
ATOM   200  C CE1 . TYR A 1 26  ? 9.164   -11.798 41.772 1.00 28.40  ? 42  TYR A CE1 1 
ATOM   201  C CE2 . TYR A 1 26  ? 7.843   -11.840 43.767 1.00 27.39  ? 42  TYR A CE2 1 
ATOM   202  C CZ  . TYR A 1 26  ? 8.553   -11.122 42.816 1.00 28.25  ? 42  TYR A CZ  1 
ATOM   203  O OH  . TYR A 1 26  ? 8.647   -9.752  42.899 1.00 26.78  ? 42  TYR A OH  1 
ATOM   204  N N   . LEU A 1 27  ? 7.957   -18.376 40.912 1.00 25.72  ? 43  LEU A N   1 
ATOM   205  C CA  . LEU A 1 27  ? 8.170   -19.757 41.328 1.00 25.15  ? 43  LEU A CA  1 
ATOM   206  C C   . LEU A 1 27  ? 9.403   -19.802 42.235 1.00 25.73  ? 43  LEU A C   1 
ATOM   207  O O   . LEU A 1 27  ? 10.442  -19.267 41.880 1.00 22.99  ? 43  LEU A O   1 
ATOM   208  C CB  . LEU A 1 27  ? 8.310   -20.636 40.084 1.00 26.43  ? 43  LEU A CB  1 
ATOM   209  C CG  . LEU A 1 27  ? 8.897   -22.032 40.291 1.00 27.43  ? 43  LEU A CG  1 
ATOM   210  C CD1 . LEU A 1 27  ? 7.991   -22.870 41.172 1.00 30.12  ? 43  LEU A CD1 1 
ATOM   211  C CD2 . LEU A 1 27  ? 9.124   -22.725 38.956 1.00 27.87  ? 43  LEU A CD2 1 
ATOM   212  N N   . THR A 1 28  ? 9.274   -20.422 43.413 1.00 25.53  ? 44  THR A N   1 
ATOM   213  C CA  . THR A 1 28  ? 10.273  -20.329 44.470 1.00 26.36  ? 44  THR A CA  1 
ATOM   214  C C   . THR A 1 28  ? 11.004  -21.653 44.747 1.00 29.11  ? 44  THR A C   1 
ATOM   215  O O   . THR A 1 28  ? 11.690  -21.769 45.775 1.00 26.84  ? 44  THR A O   1 
ATOM   216  C CB  . THR A 1 28  ? 9.583   -19.820 45.733 1.00 26.94  ? 44  THR A CB  1 
ATOM   217  O OG1 . THR A 1 28  ? 8.533   -20.734 46.040 1.00 25.89  ? 44  THR A OG1 1 
ATOM   218  C CG2 . THR A 1 28  ? 8.990   -18.442 45.562 1.00 25.77  ? 44  THR A CG2 1 
ATOM   219  N N   . VAL A 1 29  ? 10.902  -22.626 43.822 1.00 28.16  ? 45  VAL A N   1 
ATOM   220  C CA  . VAL A 1 29  ? 11.326  -23.994 44.081 1.00 28.40  ? 45  VAL A CA  1 
ATOM   221  C C   . VAL A 1 29  ? 12.854  -24.119 44.145 1.00 30.28  ? 45  VAL A C   1 
ATOM   222  O O   . VAL A 1 29  ? 13.362  -25.055 44.753 1.00 31.00  ? 45  VAL A O   1 
ATOM   223  C CB  . VAL A 1 29  ? 10.740  -24.977 43.041 1.00 27.88  ? 45  VAL A CB  1 
ATOM   224  C CG1 . VAL A 1 29  ? 11.295  -24.768 41.642 1.00 28.39  ? 45  VAL A CG1 1 
ATOM   225  C CG2 . VAL A 1 29  ? 10.931  -26.430 43.455 1.00 30.35  ? 45  VAL A CG2 1 
ATOM   226  N N   . VAL A 1 30  ? 13.608  -23.230 43.482 1.00 32.16  ? 46  VAL A N   1 
ATOM   227  C CA  . VAL A 1 30  ? 15.059  -23.338 43.488 1.00 27.37  ? 46  VAL A CA  1 
ATOM   228  C C   . VAL A 1 30  ? 15.612  -22.698 44.760 1.00 26.36  ? 46  VAL A C   1 
ATOM   229  O O   . VAL A 1 30  ? 15.927  -21.498 44.829 1.00 22.63  ? 46  VAL A O   1 
ATOM   230  C CB  . VAL A 1 30  ? 15.706  -22.786 42.214 1.00 26.35  ? 46  VAL A CB  1 
ATOM   231  C CG1 . VAL A 1 30  ? 17.219  -22.892 42.280 1.00 24.55  ? 46  VAL A CG1 1 
ATOM   232  C CG2 . VAL A 1 30  ? 15.162  -23.536 41.012 1.00 28.01  ? 46  VAL A CG2 1 
ATOM   233  N N   . LYS A 1 31  ? 15.741  -23.559 45.778 1.00 25.23  ? 47  LYS A N   1 
ATOM   234  C CA  . LYS A 1 31  ? 16.198  -23.137 47.090 1.00 25.38  ? 47  LYS A CA  1 
ATOM   235  C C   . LYS A 1 31  ? 16.542  -24.372 47.905 1.00 25.86  ? 47  LYS A C   1 
ATOM   236  O O   . LYS A 1 31  ? 16.348  -25.500 47.448 1.00 26.50  ? 47  LYS A O   1 
ATOM   237  C CB  . LYS A 1 31  ? 15.112  -22.322 47.802 1.00 28.20  ? 47  LYS A CB  1 
ATOM   238  C CG  . LYS A 1 31  ? 13.739  -22.990 47.884 1.00 27.80  ? 47  LYS A CG  1 
ATOM   239  C CD  . LYS A 1 31  ? 12.801  -22.336 48.886 1.00 27.88  ? 47  LYS A CD  1 
ATOM   240  C CE  . LYS A 1 31  ? 11.462  -23.035 49.020 1.00 28.21  ? 47  LYS A CE  1 
ATOM   241  N NZ  . LYS A 1 31  ? 11.599  -24.274 49.814 1.00 25.78  ? 47  LYS A NZ  1 
ATOM   242  N N   . GLY A 1 32  ? 17.030  -24.123 49.123 1.00 24.77  ? 48  GLY A N   1 
ATOM   243  C CA  . GLY A 1 32  ? 17.227  -25.157 50.112 1.00 27.50  ? 48  GLY A CA  1 
ATOM   244  C C   . GLY A 1 32  ? 15.910  -25.617 50.722 1.00 30.94  ? 48  GLY A C   1 
ATOM   245  O O   . GLY A 1 32  ? 14.840  -25.168 50.311 1.00 31.66  ? 48  GLY A O   1 
ATOM   246  N N   . PRO A 1 33  ? 15.959  -26.557 51.692 1.00 34.45  ? 49  PRO A N   1 
ATOM   247  C CA  . PRO A 1 33  ? 14.740  -27.142 52.251 1.00 33.73  ? 49  PRO A CA  1 
ATOM   248  C C   . PRO A 1 33  ? 13.827  -26.185 53.007 1.00 33.00  ? 49  PRO A C   1 
ATOM   249  O O   . PRO A 1 33  ? 12.633  -26.455 53.083 1.00 43.47  ? 49  PRO A O   1 
ATOM   250  C CB  . PRO A 1 33  ? 15.239  -28.247 53.202 1.00 33.22  ? 49  PRO A CB  1 
ATOM   251  C CG  . PRO A 1 33  ? 16.692  -27.949 53.442 1.00 32.83  ? 49  PRO A CG  1 
ATOM   252  C CD  . PRO A 1 33  ? 17.179  -27.172 52.236 1.00 32.41  ? 49  PRO A CD  1 
ATOM   253  N N   . ARG A 1 34  ? 14.372  -25.090 53.562 1.00 29.69  ? 50  ARG A N   1 
ATOM   254  C CA  . ARG A 1 34  ? 13.587  -24.179 54.381 1.00 31.32  ? 50  ARG A CA  1 
ATOM   255  C C   . ARG A 1 34  ? 12.563  -23.467 53.490 1.00 30.18  ? 50  ARG A C   1 
ATOM   256  O O   . ARG A 1 34  ? 12.658  -23.533 52.264 1.00 29.97  ? 50  ARG A O   1 
ATOM   257  C CB  . ARG A 1 34  ? 14.486  -23.142 55.069 1.00 37.39  ? 50  ARG A CB  1 
ATOM   258  C CG  . ARG A 1 34  ? 15.726  -23.671 55.784 1.00 40.35  ? 50  ARG A CG  1 
ATOM   259  C CD  . ARG A 1 34  ? 15.501  -24.111 57.215 1.00 44.19  ? 50  ARG A CD  1 
ATOM   260  N NE  . ARG A 1 34  ? 14.774  -23.131 58.029 1.00 48.35  ? 50  ARG A NE  1 
ATOM   261  C CZ  . ARG A 1 34  ? 15.295  -22.093 58.693 1.00 48.51  ? 50  ARG A CZ  1 
ATOM   262  N NH1 . ARG A 1 34  ? 16.570  -21.748 58.568 1.00 44.99  ? 50  ARG A NH1 1 
ATOM   263  N NH2 . ARG A 1 34  ? 14.508  -21.381 59.485 1.00 51.62  ? 50  ARG A NH2 1 
ATOM   264  N N   . ALA A 1 35  ? 11.616  -22.739 54.103 1.00 29.02  ? 51  ALA A N   1 
ATOM   265  C CA  . ALA A 1 35  ? 10.561  -22.060 53.356 1.00 30.99  ? 51  ALA A CA  1 
ATOM   266  C C   . ALA A 1 35  ? 11.157  -20.943 52.493 1.00 28.79  ? 51  ALA A C   1 
ATOM   267  O O   . ALA A 1 35  ? 12.182  -20.356 52.850 1.00 27.40  ? 51  ALA A O   1 
ATOM   268  C CB  . ALA A 1 35  ? 9.508   -21.514 54.295 1.00 32.16  ? 51  ALA A CB  1 
ATOM   269  N N   . ALA A 1 36  ? 10.481  -20.621 51.377 1.00 28.39  ? 52  ALA A N   1 
ATOM   270  C CA  . ALA A 1 36  ? 10.962  -19.597 50.460 1.00 25.53  ? 52  ALA A CA  1 
ATOM   271  C C   . ALA A 1 36  ? 11.206  -18.299 51.218 1.00 26.75  ? 52  ALA A C   1 
ATOM   272  O O   . ALA A 1 36  ? 12.167  -17.598 50.919 1.00 26.52  ? 52  ALA A O   1 
ATOM   273  C CB  . ALA A 1 36  ? 9.996   -19.373 49.332 1.00 29.05  ? 52  ALA A CB  1 
ATOM   274  N N   . SER A 1 37  ? 10.344  -18.007 52.197 1.00 26.49  ? 53  SER A N   1 
ATOM   275  C CA  . SER A 1 37  ? 10.378  -16.762 52.952 1.00 29.21  ? 53  SER A CA  1 
ATOM   276  C C   . SER A 1 37  ? 11.586  -16.658 53.881 1.00 27.23  ? 53  SER A C   1 
ATOM   277  O O   . SER A 1 37  ? 11.892  -15.568 54.333 1.00 27.18  ? 53  SER A O   1 
ATOM   278  C CB  . SER A 1 37  ? 9.091   -16.540 53.743 1.00 31.38  ? 53  SER A CB  1 
ATOM   279  O OG  . SER A 1 37  ? 8.850   -17.597 54.649 1.00 31.58  ? 53  SER A OG  1 
ATOM   280  N N   . ILE A 1 38  ? 12.271  -17.764 54.173 1.00 29.14  ? 54  ILE A N   1 
ATOM   281  C CA  . ILE A 1 38  ? 13.461  -17.706 55.005 1.00 30.56  ? 54  ILE A CA  1 
ATOM   282  C C   . ILE A 1 38  ? 14.636  -17.192 54.172 1.00 29.59  ? 54  ILE A C   1 
ATOM   283  O O   . ILE A 1 38  ? 15.516  -16.525 54.716 1.00 28.13  ? 54  ILE A O   1 
ATOM   284  C CB  . ILE A 1 38  ? 13.750  -19.072 55.661 1.00 33.86  ? 54  ILE A CB  1 
ATOM   285  C CG1 . ILE A 1 38  ? 12.646  -19.479 56.642 1.00 34.69  ? 54  ILE A CG1 1 
ATOM   286  C CG2 . ILE A 1 38  ? 15.128  -19.094 56.326 1.00 32.94  ? 54  ILE A CG2 1 
ATOM   287  C CD1 . ILE A 1 38  ? 12.471  -18.534 57.824 1.00 33.66  ? 54  ILE A CD1 1 
ATOM   288  N N   . TYR A 1 39  ? 14.612  -17.441 52.852 1.00 29.97  ? 55  TYR A N   1 
ATOM   289  C CA  . TYR A 1 39  ? 15.721  -17.047 51.980 1.00 27.34  ? 55  TYR A CA  1 
ATOM   290  C C   . TYR A 1 39  ? 15.471  -15.705 51.298 1.00 29.71  ? 55  TYR A C   1 
ATOM   291  O O   . TYR A 1 39  ? 16.415  -15.000 50.937 1.00 29.25  ? 55  TYR A O   1 
ATOM   292  C CB  . TYR A 1 39  ? 15.963  -18.101 50.892 1.00 26.67  ? 55  TYR A CB  1 
ATOM   293  C CG  . TYR A 1 39  ? 16.289  -19.485 51.435 1.00 25.82  ? 55  TYR A CG  1 
ATOM   294  C CD1 . TYR A 1 39  ? 17.499  -19.742 52.076 1.00 27.06  ? 55  TYR A CD1 1 
ATOM   295  C CD2 . TYR A 1 39  ? 15.375  -20.523 51.346 1.00 25.10  ? 55  TYR A CD2 1 
ATOM   296  C CE1 . TYR A 1 39  ? 17.789  -20.994 52.596 1.00 27.08  ? 55  TYR A CE1 1 
ATOM   297  C CE2 . TYR A 1 39  ? 15.644  -21.764 51.886 1.00 24.16  ? 55  TYR A CE2 1 
ATOM   298  C CZ  . TYR A 1 39  ? 16.856  -22.010 52.500 1.00 27.21  ? 55  TYR A CZ  1 
ATOM   299  O OH  . TYR A 1 39  ? 17.116  -23.264 52.990 1.00 29.20  ? 55  TYR A OH  1 
ATOM   300  N N   . THR A 1 40  ? 14.204  -15.369 51.057 1.00 28.23  ? 56  THR A N   1 
ATOM   301  C CA  . THR A 1 40  ? 13.878  -14.159 50.321 1.00 27.56  ? 56  THR A CA  1 
ATOM   302  C C   . THR A 1 40  ? 12.952  -13.299 51.175 1.00 25.99  ? 56  THR A C   1 
ATOM   303  O O   . THR A 1 40  ? 11.884  -13.770 51.536 1.00 26.21  ? 56  THR A O   1 
ATOM   304  C CB  . THR A 1 40  ? 13.258  -14.475 48.962 1.00 26.97  ? 56  THR A CB  1 
ATOM   305  O OG1 . THR A 1 40  ? 14.248  -15.148 48.189 1.00 26.98  ? 56  THR A OG1 1 
ATOM   306  C CG2 . THR A 1 40  ? 12.781  -13.232 48.243 1.00 27.37  ? 56  THR A CG2 1 
ATOM   307  N N   . ARG A 1 41  ? 13.423  -12.088 51.511 1.00 26.06  ? 57  ARG A N   1 
ATOM   308  C CA  . ARG A 1 41  ? 12.750  -11.155 52.397 1.00 29.92  ? 57  ARG A CA  1 
ATOM   309  C C   . ARG A 1 41  ? 12.245  -9.977  51.567 1.00 29.49  ? 57  ARG A C   1 
ATOM   310  O O   . ARG A 1 41  ? 12.935  -9.483  50.691 1.00 31.04  ? 57  ARG A O   1 
ATOM   311  C CB  . ARG A 1 41  ? 13.679  -10.617 53.492 1.00 30.99  ? 57  ARG A CB  1 
ATOM   312  C CG  . ARG A 1 41  ? 14.448  -11.658 54.295 1.00 36.31  ? 57  ARG A CG  1 
ATOM   313  C CD  . ARG A 1 41  ? 13.545  -12.491 55.184 1.00 41.82  ? 57  ARG A CD  1 
ATOM   314  N NE  . ARG A 1 41  ? 14.145  -13.731 55.683 1.00 43.26  ? 57  ARG A NE  1 
ATOM   315  C CZ  . ARG A 1 41  ? 15.137  -13.810 56.570 1.00 46.95  ? 57  ARG A CZ  1 
ATOM   316  N NH1 . ARG A 1 41  ? 15.782  -12.724 56.976 1.00 46.29  ? 57  ARG A NH1 1 
ATOM   317  N NH2 . ARG A 1 41  ? 15.508  -14.994 57.023 1.00 45.96  ? 57  ARG A NH2 1 
ATOM   318  N N   . LEU A 1 42  ? 11.025  -9.538  51.860 1.00 27.74  ? 58  LEU A N   1 
ATOM   319  C CA  . LEU A 1 42  ? 10.435  -8.377  51.231 1.00 27.81  ? 58  LEU A CA  1 
ATOM   320  C C   . LEU A 1 42  ? 10.737  -7.172  52.106 1.00 28.50  ? 58  LEU A C   1 
ATOM   321  O O   . LEU A 1 42  ? 10.492  -7.217  53.304 1.00 28.94  ? 58  LEU A O   1 
ATOM   322  C CB  . LEU A 1 42  ? 8.934   -8.644  51.084 1.00 28.76  ? 58  LEU A CB  1 
ATOM   323  C CG  . LEU A 1 42  ? 8.623   -9.757  50.093 1.00 31.34  ? 58  LEU A CG  1 
ATOM   324  C CD1 . LEU A 1 42  ? 7.249   -10.346 50.338 1.00 35.27  ? 58  LEU A CD1 1 
ATOM   325  C CD2 . LEU A 1 42  ? 8.729   -9.247  48.662 1.00 31.64  ? 58  LEU A CD2 1 
ATOM   326  N N   . LEU A 1 43  ? 11.292  -6.105  51.532 1.00 25.60  ? 59  LEU A N   1 
ATOM   327  C CA  . LEU A 1 43  ? 11.940  -5.116  52.383 1.00 28.70  ? 59  LEU A CA  1 
ATOM   328  C C   . LEU A 1 43  ? 11.039  -3.938  52.747 1.00 30.16  ? 59  LEU A C   1 
ATOM   329  O O   . LEU A 1 43  ? 11.489  -3.033  53.440 1.00 35.32  ? 59  LEU A O   1 
ATOM   330  C CB  . LEU A 1 43  ? 13.239  -4.670  51.717 1.00 27.97  ? 59  LEU A CB  1 
ATOM   331  C CG  . LEU A 1 43  ? 14.311  -5.756  51.690 1.00 27.54  ? 59  LEU A CG  1 
ATOM   332  C CD1 . LEU A 1 43  ? 15.530  -5.265  50.955 1.00 28.66  ? 59  LEU A CD1 1 
ATOM   333  C CD2 . LEU A 1 43  ? 14.681  -6.202  53.103 1.00 30.09  ? 59  LEU A CD2 1 
ATOM   334  N N   . GLY A 1 44  ? 9.758   -3.975  52.379 1.00 30.56  ? 60  GLY A N   1 
ATOM   335  C CA  . GLY A 1 44  ? 8.870   -2.896  52.785 1.00 35.17  ? 60  GLY A CA  1 
ATOM   336  C C   . GLY A 1 44  ? 9.542   -1.528  52.629 1.00 38.28  ? 60  GLY A C   1 
ATOM   337  O O   . GLY A 1 44  ? 10.127  -1.245  51.587 1.00 37.02  ? 60  GLY A O   1 
ATOM   338  N N   . ARG A 1 45  ? 9.495   -0.700  53.681 1.00 37.08  ? 61  ARG A N   1 
ATOM   339  C CA  . ARG A 1 45  ? 9.971   0.671   53.615 1.00 37.85  ? 61  ARG A CA  1 
ATOM   340  C C   . ARG A 1 45  ? 11.427  0.753   54.078 1.00 35.95  ? 61  ARG A C   1 
ATOM   341  O O   . ARG A 1 45  ? 12.022  1.830   54.063 1.00 32.57  ? 61  ARG A O   1 
ATOM   342  C CB  . ARG A 1 45  ? 9.075   1.569   54.480 1.00 43.87  ? 61  ARG A CB  1 
ATOM   343  C CG  . ARG A 1 45  ? 7.814   2.093   53.805 1.00 53.39  ? 61  ARG A CG  1 
ATOM   344  C CD  . ARG A 1 45  ? 6.880   2.804   54.790 1.00 65.08  ? 61  ARG A CD  1 
ATOM   345  N NE  . ARG A 1 45  ? 5.727   1.994   55.195 1.00 77.42  ? 61  ARG A NE  1 
ATOM   346  C CZ  . ARG A 1 45  ? 5.627   1.247   56.299 1.00 86.49  ? 61  ARG A CZ  1 
ATOM   347  N NH1 . ARG A 1 45  ? 4.570   0.468   56.467 1.00 84.69  ? 61  ARG A NH1 1 
ATOM   348  N NH2 . ARG A 1 45  ? 6.590   1.230   57.209 1.00 93.04  ? 61  ARG A NH2 1 
ATOM   349  N N   . GLU A 1 46  ? 12.013  -0.375  54.500 1.00 35.39  ? 62  GLU A N   1 
ATOM   350  C CA  . GLU A 1 46  ? 13.389  -0.372  54.984 1.00 37.93  ? 62  GLU A CA  1 
ATOM   351  C C   . GLU A 1 46  ? 14.352  0.078   53.888 1.00 33.65  ? 62  GLU A C   1 
ATOM   352  O O   . GLU A 1 46  ? 15.358  0.708   54.183 1.00 36.78  ? 62  GLU A O   1 
ATOM   353  C CB  . GLU A 1 46  ? 13.865  -1.750  55.453 1.00 41.59  ? 62  GLU A CB  1 
ATOM   354  C CG  . GLU A 1 46  ? 13.115  -2.322  56.636 1.00 50.41  ? 62  GLU A CG  1 
ATOM   355  C CD  . GLU A 1 46  ? 13.432  -3.779  56.959 1.00 53.91  ? 62  GLU A CD  1 
ATOM   356  O OE1 . GLU A 1 46  ? 14.457  -4.322  56.451 1.00 41.43  ? 62  GLU A OE1 1 
ATOM   357  O OE2 . GLU A 1 46  ? 12.624  -4.390  57.702 1.00 62.04  ? 62  GLU A OE2 1 
ATOM   358  N N   . VAL A 1 47  ? 14.074  -0.304  52.638 1.00 32.53  ? 63  VAL A N   1 
ATOM   359  C CA  . VAL A 1 47  ? 14.941  0.002   51.511 1.00 30.75  ? 63  VAL A CA  1 
ATOM   360  C C   . VAL A 1 47  ? 14.114  0.600   50.377 1.00 28.38  ? 63  VAL A C   1 
ATOM   361  O O   . VAL A 1 47  ? 13.141  -0.006  49.924 1.00 30.77  ? 63  VAL A O   1 
ATOM   362  C CB  . VAL A 1 47  ? 15.684  -1.255  51.028 1.00 31.81  ? 63  VAL A CB  1 
ATOM   363  C CG1 . VAL A 1 47  ? 16.611  -0.936  49.866 1.00 30.51  ? 63  VAL A CG1 1 
ATOM   364  C CG2 . VAL A 1 47  ? 16.437  -1.928  52.160 1.00 31.81  ? 63  VAL A CG2 1 
ATOM   365  N N   . THR A 1 48  ? 14.546  1.768   49.912 1.00 26.33  ? 64  THR A N   1 
ATOM   366  C CA  . THR A 1 48  ? 13.952  2.406   48.760 1.00 29.05  ? 64  THR A CA  1 
ATOM   367  C C   . THR A 1 48  ? 14.408  1.661   47.504 1.00 28.74  ? 64  THR A C   1 
ATOM   368  O O   . THR A 1 48  ? 15.599  1.472   47.294 1.00 25.88  ? 64  THR A O   1 
ATOM   369  C CB  . THR A 1 48  ? 14.341  3.887   48.658 1.00 30.15  ? 64  THR A CB  1 
ATOM   370  O OG1 . THR A 1 48  ? 14.107  4.520   49.916 1.00 34.14  ? 64  THR A OG1 1 
ATOM   371  C CG2 . THR A 1 48  ? 13.563  4.617   47.583 1.00 28.44  ? 64  THR A CG2 1 
ATOM   372  N N   . PRO A 1 49  ? 13.477  1.200   46.641 1.00 27.97  ? 65  PRO A N   1 
ATOM   373  C CA  . PRO A 1 49  ? 13.854  0.446   45.445 1.00 25.82  ? 65  PRO A CA  1 
ATOM   374  C C   . PRO A 1 49  ? 14.418  1.405   44.413 1.00 25.90  ? 65  PRO A C   1 
ATOM   375  O O   . PRO A 1 49  ? 14.485  2.620   44.665 1.00 25.88  ? 65  PRO A O   1 
ATOM   376  C CB  . PRO A 1 49  ? 12.535  -0.211  45.015 1.00 26.90  ? 65  PRO A CB  1 
ATOM   377  C CG  . PRO A 1 49  ? 11.482  0.758   45.513 1.00 25.28  ? 65  PRO A CG  1 
ATOM   378  C CD  . PRO A 1 49  ? 12.017  1.285   46.816 1.00 23.70  ? 65  PRO A CD  1 
ATOM   379  N N   . THR A 1 50  ? 14.833  0.859   43.265 1.00 21.90  ? 66  THR A N   1 
ATOM   380  C CA  . THR A 1 50  ? 15.349  1.701   42.194 1.00 23.47  ? 66  THR A CA  1 
ATOM   381  C C   . THR A 1 50  ? 14.298  2.759   41.883 1.00 25.26  ? 66  THR A C   1 
ATOM   382  O O   . THR A 1 50  ? 13.106  2.458   41.891 1.00 24.96  ? 66  THR A O   1 
ATOM   383  C CB  . THR A 1 50  ? 15.722  0.933   40.914 1.00 22.81  ? 66  THR A CB  1 
ATOM   384  O OG1 . THR A 1 50  ? 16.207  1.893   39.973 1.00 24.38  ? 66  THR A OG1 1 
ATOM   385  C CG2 . THR A 1 50  ? 14.567  0.202   40.280 1.00 22.36  ? 66  THR A CG2 1 
ATOM   386  N N   . PRO A 1 51  ? 14.695  4.035   41.704 1.00 24.23  ? 67  PRO A N   1 
ATOM   387  C CA  . PRO A 1 51  ? 13.716  5.083   41.420 1.00 26.46  ? 67  PRO A CA  1 
ATOM   388  C C   . PRO A 1 51  ? 13.148  5.066   39.990 1.00 26.80  ? 67  PRO A C   1 
ATOM   389  O O   . PRO A 1 51  ? 12.225  5.825   39.683 1.00 23.90  ? 67  PRO A O   1 
ATOM   390  C CB  . PRO A 1 51  ? 14.470  6.396   41.714 1.00 26.97  ? 67  PRO A CB  1 
ATOM   391  C CG  . PRO A 1 51  ? 15.884  6.032   42.092 1.00 28.30  ? 67  PRO A CG  1 
ATOM   392  C CD  . PRO A 1 51  ? 16.066  4.543   41.864 1.00 24.51  ? 67  PRO A CD  1 
ATOM   393  N N   . LEU A 1 52  ? 13.652  4.176   39.119 1.00 24.99  ? 68  LEU A N   1 
ATOM   394  C CA  . LEU A 1 52  ? 13.274  4.238   37.707 1.00 26.93  ? 68  LEU A CA  1 
ATOM   395  C C   . LEU A 1 52  ? 11.769  4.067   37.511 1.00 27.52  ? 68  LEU A C   1 
ATOM   396  O O   . LEU A 1 52  ? 11.219  4.706   36.617 1.00 24.73  ? 68  LEU A O   1 
ATOM   397  C CB  . LEU A 1 52  ? 14.025  3.184   36.886 1.00 24.11  ? 68  LEU A CB  1 
ATOM   398  C CG  . LEU A 1 52  ? 15.523  3.438   36.706 1.00 23.03  ? 68  LEU A CG  1 
ATOM   399  C CD1 . LEU A 1 52  ? 16.146  2.442   35.727 1.00 23.99  ? 68  LEU A CD1 1 
ATOM   400  C CD2 . LEU A 1 52  ? 15.773  4.861   36.240 1.00 23.46  ? 68  LEU A CD2 1 
ATOM   401  N N   . TRP A 1 53  ? 11.117  3.216   38.317 1.00 26.17  ? 69  TRP A N   1 
ATOM   402  C CA  . TRP A 1 53  ? 9.703   2.895   38.106 1.00 26.49  ? 69  TRP A CA  1 
ATOM   403  C C   . TRP A 1 53  ? 8.787   3.585   39.133 1.00 25.69  ? 69  TRP A C   1 
ATOM   404  O O   . TRP A 1 53  ? 7.662   3.141   39.372 1.00 25.85  ? 69  TRP A O   1 
ATOM   405  C CB  . TRP A 1 53  ? 9.535   1.361   38.073 1.00 25.50  ? 69  TRP A CB  1 
ATOM   406  C CG  . TRP A 1 53  ? 10.693  0.702   37.370 1.00 23.49  ? 69  TRP A CG  1 
ATOM   407  C CD1 . TRP A 1 53  ? 11.637  -0.108  37.924 1.00 22.26  ? 69  TRP A CD1 1 
ATOM   408  C CD2 . TRP A 1 53  ? 11.106  0.918   36.003 1.00 22.16  ? 69  TRP A CD2 1 
ATOM   409  N NE1 . TRP A 1 53  ? 12.592  -0.426  36.999 1.00 22.50  ? 69  TRP A NE1 1 
ATOM   410  C CE2 . TRP A 1 53  ? 12.305  0.190   35.816 1.00 23.93  ? 69  TRP A CE2 1 
ATOM   411  C CE3 . TRP A 1 53  ? 10.591  1.650   34.925 1.00 24.75  ? 69  TRP A CE3 1 
ATOM   412  C CZ2 . TRP A 1 53  ? 12.979  0.163   34.591 1.00 23.07  ? 69  TRP A CZ2 1 
ATOM   413  C CZ3 . TRP A 1 53  ? 11.257  1.627   33.718 1.00 23.59  ? 69  TRP A CZ3 1 
ATOM   414  C CH2 . TRP A 1 53  ? 12.429  0.892   33.555 1.00 23.31  ? 69  TRP A CH2 1 
ATOM   415  N N   . ASN A 1 54  ? 9.257   4.687   39.729 1.00 24.70  ? 70  ASN A N   1 
ATOM   416  C CA  . ASN A 1 54  ? 8.471   5.465   40.674 1.00 27.53  ? 70  ASN A CA  1 
ATOM   417  C C   . ASN A 1 54  ? 7.276   6.078   39.949 1.00 26.89  ? 70  ASN A C   1 
ATOM   418  O O   . ASN A 1 54  ? 7.312   6.274   38.728 1.00 24.44  ? 70  ASN A O   1 
ATOM   419  C CB  . ASN A 1 54  ? 9.235   6.658   41.272 1.00 29.49  ? 70  ASN A CB  1 
ATOM   420  C CG  . ASN A 1 54  ? 10.223  6.285   42.357 1.00 32.49  ? 70  ASN A CG  1 
ATOM   421  O OD1 . ASN A 1 54  ? 10.245  5.156   42.857 1.00 35.31  ? 70  ASN A OD1 1 
ATOM   422  N ND2 . ASN A 1 54  ? 11.071  7.236   42.699 1.00 32.52  ? 70  ASN A ND2 1 
ATOM   423  N N   . ASP A 1 55  ? 6.244   6.398   40.741 1.00 26.40  ? 71  ASP A N   1 
ATOM   424  C CA  . ASP A 1 55  ? 5.226   7.359   40.338 1.00 29.88  ? 71  ASP A CA  1 
ATOM   425  C C   . ASP A 1 55  ? 5.560   8.702   40.981 1.00 31.13  ? 71  ASP A C   1 
ATOM   426  O O   . ASP A 1 55  ? 6.200   8.736   42.015 1.00 39.04  ? 71  ASP A O   1 
ATOM   427  C CB  . ASP A 1 55  ? 3.822   6.872   40.717 1.00 30.42  ? 71  ASP A CB  1 
ATOM   428  C CG  . ASP A 1 55  ? 3.277   5.743   39.860 1.00 30.17  ? 71  ASP A CG  1 
ATOM   429  O OD1 . ASP A 1 55  ? 3.753   5.595   38.724 1.00 32.27  ? 71  ASP A OD1 1 
ATOM   430  O OD2 . ASP A 1 55  ? 2.385   5.030   40.333 1.00 30.78  ? 71  ASP A OD2 1 
ATOM   431  N N   . ARG A 1 56  ? 5.154   9.790   40.334 1.00 32.54  ? 72  ARG A N   1 
ATOM   432  C CA  . ARG A 1 56  ? 5.454   11.141  40.772 1.00 34.62  ? 72  ARG A CA  1 
ATOM   433  C C   . ARG A 1 56  ? 4.173   11.791  41.284 1.00 32.55  ? 72  ARG A C   1 
ATOM   434  O O   . ARG A 1 56  ? 3.092   11.552  40.747 1.00 27.70  ? 72  ARG A O   1 
ATOM   435  C CB  . ARG A 1 56  ? 6.011   11.989  39.621 1.00 38.59  ? 72  ARG A CB  1 
ATOM   436  C CG  . ARG A 1 56  ? 7.415   11.621  39.152 1.00 47.14  ? 72  ARG A CG  1 
ATOM   437  C CD  . ARG A 1 56  ? 8.266   12.840  38.794 1.00 53.65  ? 72  ARG A CD  1 
ATOM   438  N NE  . ARG A 1 56  ? 8.582   13.658  39.970 1.00 54.41  ? 72  ARG A NE  1 
ATOM   439  C CZ  . ARG A 1 56  ? 8.501   14.988  40.050 1.00 54.21  ? 72  ARG A CZ  1 
ATOM   440  N NH1 . ARG A 1 56  ? 8.520   15.754  38.969 1.00 49.99  ? 72  ARG A NH1 1 
ATOM   441  N NH2 . ARG A 1 56  ? 8.474   15.552  41.243 1.00 60.36  ? 72  ARG A NH2 1 
ATOM   442  N N   . LEU A 1 57  ? 4.326   12.650  42.295 1.00 32.09  ? 73  LEU A N   1 
ATOM   443  C CA  . LEU A 1 57  ? 3.223   13.404  42.867 1.00 35.07  ? 73  LEU A CA  1 
ATOM   444  C C   . LEU A 1 57  ? 3.171   14.828  42.305 1.00 38.10  ? 73  LEU A C   1 
ATOM   445  O O   . LEU A 1 57  ? 4.182   15.413  41.923 1.00 34.77  ? 73  LEU A O   1 
ATOM   446  C CB  . LEU A 1 57  ? 3.384   13.420  44.388 1.00 37.34  ? 73  LEU A CB  1 
ATOM   447  C CG  . LEU A 1 57  ? 3.001   12.120  45.084 1.00 41.64  ? 73  LEU A CG  1 
ATOM   448  C CD1 . LEU A 1 57  ? 3.632   12.030  46.456 1.00 43.03  ? 73  LEU A CD1 1 
ATOM   449  C CD2 . LEU A 1 57  ? 1.492   12.021  45.206 1.00 44.24  ? 73  LEU A CD2 1 
ATOM   450  N N   . PHE A 1 58  ? 1.950   15.350  42.221 1.00 37.13  ? 74  PHE A N   1 
ATOM   451  C CA  . PHE A 1 58  ? 1.714   16.762  42.015 1.00 48.50  ? 74  PHE A CA  1 
ATOM   452  C C   . PHE A 1 58  ? 0.867   17.263  43.186 1.00 53.34  ? 74  PHE A C   1 
ATOM   453  O O   . PHE A 1 58  ? -0.148  16.654  43.497 1.00 49.74  ? 74  PHE A O   1 
ATOM   454  C CB  . PHE A 1 58  ? 1.051   17.006  40.661 1.00 53.65  ? 74  PHE A CB  1 
ATOM   455  C CG  . PHE A 1 58  ? 0.759   18.459  40.408 1.00 69.16  ? 74  PHE A CG  1 
ATOM   456  C CD1 . PHE A 1 58  ? -0.166  19.148  41.184 1.00 80.32  ? 74  PHE A CD1 1 
ATOM   457  C CD2 . PHE A 1 58  ? 1.447   19.149  39.427 1.00 79.20  ? 74  PHE A CD2 1 
ATOM   458  C CE1 . PHE A 1 58  ? -0.415  20.493  40.967 1.00 89.41  ? 74  PHE A CE1 1 
ATOM   459  C CE2 . PHE A 1 58  ? 1.189   20.492  39.205 1.00 93.89  ? 74  PHE A CE2 1 
ATOM   460  C CZ  . PHE A 1 58  ? 0.261   21.161  39.974 1.00 95.00  ? 74  PHE A CZ  1 
ATOM   461  N N   . PRO A 1 59  ? 1.254   18.338  43.914 1.00 71.83  ? 75  PRO A N   1 
ATOM   462  C CA  . PRO A 1 59  ? 2.455   19.122  43.622 1.00 77.70  ? 75  PRO A CA  1 
ATOM   463  C C   . PRO A 1 59  ? 3.707   18.377  44.084 1.00 75.29  ? 75  PRO A C   1 
ATOM   464  O O   . PRO A 1 59  ? 3.607   17.413  44.844 1.00 66.84  ? 75  PRO A O   1 
ATOM   465  C CB  . PRO A 1 59  ? 2.245   20.425  44.412 1.00 82.09  ? 75  PRO A CB  1 
ATOM   466  C CG  . PRO A 1 59  ? 1.321   20.048  45.567 1.00 81.17  ? 75  PRO A CG  1 
ATOM   467  C CD  . PRO A 1 59  ? 0.580   18.794  45.140 1.00 78.87  ? 75  PRO A CD  1 
ATOM   468  N N   . GLU A 1 60  ? 4.875   18.858  43.634 1.00 83.86  ? 76  GLU A N   1 
ATOM   469  C CA  . GLU A 1 60  ? 6.132   18.128  43.732 1.00 85.27  ? 76  GLU A CA  1 
ATOM   470  C C   . GLU A 1 60  ? 6.842   18.454  45.048 1.00 82.66  ? 76  GLU A C   1 
ATOM   471  O O   . GLU A 1 60  ? 7.930   17.938  45.301 1.00 65.03  ? 76  GLU A O   1 
ATOM   472  C CB  . GLU A 1 60  ? 6.964   18.425  42.482 1.00 83.23  ? 76  GLU A CB  1 
ATOM   473  C CG  . GLU A 1 60  ? 6.314   17.880  41.213 1.00 84.89  ? 76  GLU A CG  1 
ATOM   474  C CD  . GLU A 1 60  ? 6.695   18.557  39.905 1.00 86.58  ? 76  GLU A CD  1 
ATOM   475  O OE1 . GLU A 1 60  ? 5.783   18.869  39.114 1.00 86.57  ? 76  GLU A OE1 1 
ATOM   476  O OE2 . GLU A 1 60  ? 7.898   18.781  39.680 1.00 90.35  ? 76  GLU A OE2 1 
ATOM   477  N N   . VAL A 1 61  ? 6.197   19.300  45.868 1.00 94.81  ? 77  VAL A N   1 
ATOM   478  C CA  . VAL A 1 61  ? 6.467   19.493  47.289 1.00 104.30 ? 77  VAL A CA  1 
ATOM   479  C C   . VAL A 1 61  ? 5.183   19.115  48.041 1.00 110.18 ? 77  VAL A C   1 
ATOM   480  O O   . VAL A 1 61  ? 4.093   19.434  47.567 1.00 114.56 ? 77  VAL A O   1 
ATOM   481  C CB  . VAL A 1 61  ? 6.922   20.948  47.575 1.00 102.71 ? 77  VAL A CB  1 
ATOM   482  C CG1 . VAL A 1 61  ? 5.782   21.961  47.478 1.00 97.93  ? 77  VAL A CG1 1 
ATOM   483  C CG2 . VAL A 1 61  ? 7.629   21.089  48.916 1.00 97.70  ? 77  VAL A CG2 1 
ATOM   484  N N   . PRO A 1 62  ? 5.208   18.427  49.214 1.00 112.09 ? 78  PRO A N   1 
ATOM   485  C CA  . PRO A 1 62  ? 6.432   17.939  49.864 1.00 110.57 ? 78  PRO A CA  1 
ATOM   486  C C   . PRO A 1 62  ? 7.149   16.735  49.238 1.00 112.44 ? 78  PRO A C   1 
ATOM   487  O O   . PRO A 1 62  ? 8.359   16.796  49.026 1.00 114.90 ? 78  PRO A O   1 
ATOM   488  C CB  . PRO A 1 62  ? 5.964   17.586  51.291 1.00 106.58 ? 78  PRO A CB  1 
ATOM   489  C CG  . PRO A 1 62  ? 4.481   17.299  51.165 1.00 104.45 ? 78  PRO A CG  1 
ATOM   490  C CD  . PRO A 1 62  ? 4.003   18.164  50.020 1.00 104.18 ? 78  PRO A CD  1 
ATOM   491  N N   . TYR A 1 63  ? 6.423   15.642  48.951 1.00 107.95 ? 79  TYR A N   1 
ATOM   492  C CA  . TYR A 1 63  ? 7.044   14.405  48.487 1.00 99.40  ? 79  TYR A CA  1 
ATOM   493  C C   . TYR A 1 63  ? 7.069   14.412  46.954 1.00 83.47  ? 79  TYR A C   1 
ATOM   494  O O   . TYR A 1 63  ? 6.028   14.579  46.327 1.00 73.25  ? 79  TYR A O   1 
ATOM   495  C CB  . TYR A 1 63  ? 6.335   13.129  48.971 1.00 105.49 ? 79  TYR A CB  1 
ATOM   496  C CG  . TYR A 1 63  ? 5.408   13.240  50.178 1.00 114.20 ? 79  TYR A CG  1 
ATOM   497  C CD1 . TYR A 1 63  ? 5.770   13.960  51.314 1.00 119.81 ? 79  TYR A CD1 1 
ATOM   498  C CD2 . TYR A 1 63  ? 4.172   12.595  50.191 1.00 109.05 ? 79  TYR A CD2 1 
ATOM   499  C CE1 . TYR A 1 63  ? 4.928   14.057  52.410 1.00 114.80 ? 79  TYR A CE1 1 
ATOM   500  C CE2 . TYR A 1 63  ? 3.322   12.681  51.281 1.00 107.89 ? 79  TYR A CE2 1 
ATOM   501  C CZ  . TYR A 1 63  ? 3.702   13.413  52.391 1.00 111.74 ? 79  TYR A CZ  1 
ATOM   502  O OH  . TYR A 1 63  ? 2.869   13.495  53.464 1.00 110.05 ? 79  TYR A OH  1 
ATOM   503  N N   . PRO A 1 64  ? 8.234   14.259  46.278 1.00 76.18  ? 80  PRO A N   1 
ATOM   504  C CA  . PRO A 1 64  ? 8.240   14.166  44.814 1.00 65.19  ? 80  PRO A CA  1 
ATOM   505  C C   . PRO A 1 64  ? 7.625   12.887  44.228 1.00 56.01  ? 80  PRO A C   1 
ATOM   506  O O   . PRO A 1 64  ? 7.054   12.950  43.148 1.00 51.17  ? 80  PRO A O   1 
ATOM   507  C CB  . PRO A 1 64  ? 9.726   14.284  44.423 1.00 65.60  ? 80  PRO A CB  1 
ATOM   508  C CG  . PRO A 1 64  ? 10.518  13.970  45.691 1.00 66.95  ? 80  PRO A CG  1 
ATOM   509  C CD  . PRO A 1 64  ? 9.590   14.256  46.858 1.00 71.31  ? 80  PRO A CD  1 
ATOM   510  N N   . ALA A 1 65  ? 7.713   11.739  44.927 1.00 51.60  ? 81  ALA A N   1 
ATOM   511  C CA  . ALA A 1 65  ? 7.459   10.444  44.298 1.00 48.26  ? 81  ALA A CA  1 
ATOM   512  C C   . ALA A 1 65  ? 6.918   9.413   45.289 1.00 42.14  ? 81  ALA A C   1 
ATOM   513  O O   . ALA A 1 65  ? 7.086   9.572   46.492 1.00 41.33  ? 81  ALA A O   1 
ATOM   514  C CB  . ALA A 1 65  ? 8.733   9.944   43.656 1.00 47.43  ? 81  ALA A CB  1 
ATOM   515  N N   . VAL A 1 66  ? 6.272   8.367   44.748 1.00 37.97  ? 82  VAL A N   1 
ATOM   516  C CA  . VAL A 1 66  ? 5.844   7.185   45.488 1.00 39.33  ? 82  VAL A CA  1 
ATOM   517  C C   . VAL A 1 66  ? 6.478   5.933   44.862 1.00 34.88  ? 82  VAL A C   1 
ATOM   518  O O   . VAL A 1 66  ? 6.508   5.795   43.641 1.00 27.76  ? 82  VAL A O   1 
ATOM   519  C CB  . VAL A 1 66  ? 4.303   7.053   45.543 1.00 41.04  ? 82  VAL A CB  1 
ATOM   520  C CG1 . VAL A 1 66  ? 3.663   6.960   44.180 1.00 41.28  ? 82  VAL A CG1 1 
ATOM   521  C CG2 . VAL A 1 66  ? 3.864   5.855   46.366 1.00 44.13  ? 82  VAL A CG2 1 
ATOM   522  N N   . SER A 1 67  ? 6.989   5.040   45.723 1.00 32.83  ? 83  SER A N   1 
ATOM   523  C CA  . SER A 1 67  ? 7.512   3.742   45.321 1.00 34.25  ? 83  SER A CA  1 
ATOM   524  C C   . SER A 1 67  ? 6.369   2.871   44.827 1.00 32.86  ? 83  SER A C   1 
ATOM   525  O O   . SER A 1 67  ? 5.328   2.862   45.467 1.00 36.18  ? 83  SER A O   1 
ATOM   526  C CB  . SER A 1 67  ? 8.215   3.080   46.472 1.00 37.22  ? 83  SER A CB  1 
ATOM   527  O OG  . SER A 1 67  ? 9.378   3.817   46.845 1.00 43.16  ? 83  SER A OG  1 
ATOM   528  N N   . THR A 1 68  ? 6.554   2.163   43.700 1.00 30.52  ? 84  THR A N   1 
ATOM   529  C CA  . THR A 1 68  ? 5.511   1.311   43.152 1.00 30.37  ? 84  THR A CA  1 
ATOM   530  C C   . THR A 1 68  ? 5.824   -0.164  43.401 1.00 30.91  ? 84  THR A C   1 
ATOM   531  O O   . THR A 1 68  ? 5.108   -1.052  42.918 1.00 30.85  ? 84  THR A O   1 
ATOM   532  C CB  . THR A 1 68  ? 5.277   1.573   41.662 1.00 31.57  ? 84  THR A CB  1 
ATOM   533  O OG1 . THR A 1 68  ? 6.497   1.352   40.957 1.00 31.15  ? 84  THR A OG1 1 
ATOM   534  C CG2 . THR A 1 68  ? 4.779   2.976   41.392 1.00 29.74  ? 84  THR A CG2 1 
ATOM   535  N N   . GLU A 1 69  ? 6.876   -0.421  44.185 1.00 28.74  ? 85  GLU A N   1 
ATOM   536  C CA  . GLU A 1 69  ? 7.326   -1.780  44.434 1.00 28.96  ? 85  GLU A CA  1 
ATOM   537  C C   . GLU A 1 69  ? 8.097   -1.785  45.744 1.00 27.84  ? 85  GLU A C   1 
ATOM   538  O O   . GLU A 1 69  ? 8.439   -0.728  46.264 1.00 28.07  ? 85  GLU A O   1 
ATOM   539  C CB  . GLU A 1 69  ? 8.183   -2.271  43.261 1.00 27.02  ? 85  GLU A CB  1 
ATOM   540  C CG  . GLU A 1 69  ? 9.483   -1.493  43.067 1.00 25.24  ? 85  GLU A CG  1 
ATOM   541  C CD  . GLU A 1 69  ? 10.398  -2.017  41.974 1.00 26.21  ? 85  GLU A CD  1 
ATOM   542  O OE1 . GLU A 1 69  ? 10.720  -3.226  42.022 1.00 27.95  ? 85  GLU A OE1 1 
ATOM   543  O OE2 . GLU A 1 69  ? 10.811  -1.211  41.085 1.00 26.42  ? 85  GLU A OE2 1 
ATOM   544  N N   . GLN A 1 70  ? 8.352   -2.980  46.272 1.00 29.08  ? 86  GLN A N   1 
ATOM   545  C CA  . GLN A 1 70  ? 9.292   -3.116  47.364 1.00 29.00  ? 86  GLN A CA  1 
ATOM   546  C C   . GLN A 1 70  ? 10.474  -3.948  46.882 1.00 25.62  ? 86  GLN A C   1 
ATOM   547  O O   . GLN A 1 70  ? 10.323  -4.808  46.023 1.00 26.24  ? 86  GLN A O   1 
ATOM   548  C CB  . GLN A 1 70  ? 8.596   -3.645  48.624 1.00 34.35  ? 86  GLN A CB  1 
ATOM   549  C CG  . GLN A 1 70  ? 7.983   -5.037  48.514 1.00 35.94  ? 86  GLN A CG  1 
ATOM   550  C CD  . GLN A 1 70  ? 7.350   -5.443  49.828 1.00 35.67  ? 86  GLN A CD  1 
ATOM   551  O OE1 . GLN A 1 70  ? 7.934   -5.307  50.903 1.00 34.33  ? 86  GLN A OE1 1 
ATOM   552  N NE2 . GLN A 1 70  ? 6.126   -5.925  49.751 1.00 30.98  ? 86  GLN A NE2 1 
ATOM   553  N N   . ALA A 1 71  ? 11.664  -3.637  47.403 1.00 23.72  ? 87  ALA A N   1 
ATOM   554  C CA  . ALA A 1 71  ? 12.860  -4.398  47.100 1.00 24.65  ? 87  ALA A CA  1 
ATOM   555  C C   . ALA A 1 71  ? 12.757  -5.789  47.719 1.00 25.43  ? 87  ALA A C   1 
ATOM   556  O O   . ALA A 1 71  ? 12.037  -5.997  48.693 1.00 27.43  ? 87  ALA A O   1 
ATOM   557  C CB  . ALA A 1 71  ? 14.088  -3.655  47.604 1.00 26.38  ? 87  ALA A CB  1 
ATOM   558  N N   . LEU A 1 72  ? 13.498  -6.737  47.144 1.00 25.15  ? 88  LEU A N   1 
ATOM   559  C CA  . LEU A 1 72  ? 13.615  -8.085  47.675 1.00 26.29  ? 88  LEU A CA  1 
ATOM   560  C C   . LEU A 1 72  ? 15.052  -8.308  48.132 1.00 21.58  ? 88  LEU A C   1 
ATOM   561  O O   . LEU A 1 72  ? 15.946  -7.954  47.401 1.00 22.18  ? 88  LEU A O   1 
ATOM   562  C CB  . LEU A 1 72  ? 13.287  -9.058  46.544 1.00 26.27  ? 88  LEU A CB  1 
ATOM   563  C CG  . LEU A 1 72  ? 11.884  -8.962  45.957 1.00 29.74  ? 88  LEU A CG  1 
ATOM   564  C CD1 . LEU A 1 72  ? 11.941  -9.091  44.443 1.00 31.77  ? 88  LEU A CD1 1 
ATOM   565  C CD2 . LEU A 1 72  ? 10.995  -10.052 46.510 1.00 31.99  ? 88  LEU A CD2 1 
ATOM   566  N N   . LEU A 1 73  ? 15.253  -8.914  49.307 1.00 22.61  ? 89  LEU A N   1 
ATOM   567  C CA  . LEU A 1 73  ? 16.564  -9.389  49.730 1.00 22.51  ? 89  LEU A CA  1 
ATOM   568  C C   . LEU A 1 73  ? 16.606  -10.903 49.565 1.00 23.53  ? 89  LEU A C   1 
ATOM   569  O O   . LEU A 1 73  ? 15.759  -11.623 50.115 1.00 24.18  ? 89  LEU A O   1 
ATOM   570  C CB  . LEU A 1 73  ? 16.800  -8.965  51.176 1.00 24.20  ? 89  LEU A CB  1 
ATOM   571  C CG  . LEU A 1 73  ? 18.044  -9.524  51.849 1.00 26.44  ? 89  LEU A CG  1 
ATOM   572  C CD1 . LEU A 1 73  ? 19.295  -8.850  51.309 1.00 27.51  ? 89  LEU A CD1 1 
ATOM   573  C CD2 . LEU A 1 73  ? 17.951  -9.368  53.361 1.00 27.68  ? 89  LEU A CD2 1 
ATOM   574  N N   . VAL A 1 74  ? 17.544  -11.345 48.720 1.00 22.79  ? 90  VAL A N   1 
ATOM   575  C CA  . VAL A 1 74  ? 17.768  -12.746 48.430 1.00 20.96  ? 90  VAL A CA  1 
ATOM   576  C C   . VAL A 1 74  ? 19.034  -13.189 49.157 1.00 24.02  ? 90  VAL A C   1 
ATOM   577  O O   . VAL A 1 74  ? 20.106  -12.621 48.944 1.00 24.90  ? 90  VAL A O   1 
ATOM   578  C CB  . VAL A 1 74  ? 17.868  -13.002 46.915 1.00 19.11  ? 90  VAL A CB  1 
ATOM   579  C CG1 . VAL A 1 74  ? 18.255  -14.430 46.619 1.00 19.25  ? 90  VAL A CG1 1 
ATOM   580  C CG2 . VAL A 1 74  ? 16.585  -12.649 46.170 1.00 20.15  ? 90  VAL A CG2 1 
ATOM   581  N N   . LEU A 1 75  ? 18.873  -14.220 49.992 1.00 23.32  ? 91  LEU A N   1 
ATOM   582  C CA  . LEU A 1 75  ? 19.927  -14.718 50.852 1.00 25.54  ? 91  LEU A CA  1 
ATOM   583  C C   . LEU A 1 75  ? 20.208  -16.159 50.492 1.00 24.76  ? 91  LEU A C   1 
ATOM   584  O O   . LEU A 1 75  ? 19.270  -16.890 50.192 1.00 28.27  ? 91  LEU A O   1 
ATOM   585  C CB  . LEU A 1 75  ? 19.469  -14.688 52.305 1.00 23.63  ? 91  LEU A CB  1 
ATOM   586  C CG  . LEU A 1 75  ? 19.216  -13.317 52.909 1.00 25.87  ? 91  LEU A CG  1 
ATOM   587  C CD1 . LEU A 1 75  ? 18.525  -13.472 54.261 1.00 28.34  ? 91  LEU A CD1 1 
ATOM   588  C CD2 . LEU A 1 75  ? 20.513  -12.548 53.064 1.00 25.57  ? 91  LEU A CD2 1 
ATOM   589  N N   . ILE A 1 76  ? 21.486  -16.533 50.605 1.00 25.89  ? 92  ILE A N   1 
ATOM   590  C CA  . ILE A 1 76  ? 21.925  -17.911 50.683 1.00 25.26  ? 92  ILE A CA  1 
ATOM   591  C C   . ILE A 1 76  ? 22.650  -18.106 52.012 1.00 26.71  ? 92  ILE A C   1 
ATOM   592  O O   . ILE A 1 76  ? 23.261  -17.175 52.540 1.00 25.89  ? 92  ILE A O   1 
ATOM   593  C CB  . ILE A 1 76  ? 22.846  -18.286 49.512 1.00 25.28  ? 92  ILE A CB  1 
ATOM   594  C CG1 . ILE A 1 76  ? 23.997  -17.284 49.360 1.00 26.10  ? 92  ILE A CG1 1 
ATOM   595  C CG2 . ILE A 1 76  ? 22.038  -18.435 48.236 1.00 27.46  ? 92  ILE A CG2 1 
ATOM   596  C CD1 . ILE A 1 76  ? 25.157  -17.794 48.545 1.00 25.84  ? 92  ILE A CD1 1 
ATOM   597  N N   . GLY A 1 77  ? 22.568  -19.331 52.535 1.00 27.39  ? 93  GLY A N   1 
ATOM   598  C CA  . GLY A 1 77  ? 23.293  -19.725 53.728 1.00 28.54  ? 93  GLY A CA  1 
ATOM   599  C C   . GLY A 1 77  ? 23.643  -21.200 53.626 1.00 30.29  ? 93  GLY A C   1 
ATOM   600  O O   . GLY A 1 77  ? 23.547  -21.776 52.539 1.00 24.59  ? 93  GLY A O   1 
ATOM   601  N N   . ASN A 1 78  ? 24.022  -21.807 54.756 1.00 29.44  ? 94  ASN A N   1 
ATOM   602  C CA  . ASN A 1 78  ? 24.596  -23.138 54.682 1.00 33.84  ? 94  ASN A CA  1 
ATOM   603  C C   . ASN A 1 78  ? 23.530  -24.174 54.334 1.00 29.99  ? 94  ASN A C   1 
ATOM   604  O O   . ASN A 1 78  ? 23.866  -25.237 53.817 1.00 29.53  ? 94  ASN A O   1 
ATOM   605  C CB  . ASN A 1 78  ? 25.361  -23.579 55.931 1.00 37.56  ? 94  ASN A CB  1 
ATOM   606  C CG  . ASN A 1 78  ? 26.227  -24.784 55.591 1.00 47.40  ? 94  ASN A CG  1 
ATOM   607  O OD1 . ASN A 1 78  ? 26.977  -24.777 54.596 1.00 42.26  ? 94  ASN A OD1 1 
ATOM   608  N ND2 . ASN A 1 78  ? 26.081  -25.853 56.362 1.00 51.44  ? 94  ASN A ND2 1 
ATOM   609  N N   . SER A 1 79  ? 22.258  -23.842 54.555 1.00 28.31  ? 95  SER A N   1 
ATOM   610  C CA  . SER A 1 79  ? 21.182  -24.727 54.150 1.00 28.88  ? 95  SER A CA  1 
ATOM   611  C C   . SER A 1 79  ? 20.823  -24.592 52.665 1.00 25.81  ? 95  SER A C   1 
ATOM   612  O O   . SER A 1 79  ? 19.936  -25.335 52.235 1.00 24.49  ? 95  SER A O   1 
ATOM   613  C CB  . SER A 1 79  ? 19.966  -24.526 55.024 1.00 29.76  ? 95  SER A CB  1 
ATOM   614  O OG  . SER A 1 79  ? 19.286  -23.308 54.760 1.00 28.81  ? 95  SER A OG  1 
ATOM   615  N N   . SER A 1 80  ? 21.497  -23.706 51.885 1.00 23.83  ? 96  SER A N   1 
ATOM   616  C CA  . SER A 1 80  ? 21.054  -23.375 50.523 1.00 24.12  ? 96  SER A CA  1 
ATOM   617  C C   . SER A 1 80  ? 21.522  -24.410 49.494 1.00 25.76  ? 96  SER A C   1 
ATOM   618  O O   . SER A 1 80  ? 22.100  -24.078 48.466 1.00 23.90  ? 96  SER A O   1 
ATOM   619  C CB  . SER A 1 80  ? 21.441  -21.967 50.102 1.00 24.19  ? 96  SER A CB  1 
ATOM   620  O OG  . SER A 1 80  ? 20.817  -20.985 50.941 1.00 26.23  ? 96  SER A OG  1 
ATOM   621  N N   . VAL A 1 81  ? 21.205  -25.679 49.767 1.00 28.04  ? 97  VAL A N   1 
ATOM   622  C CA  . VAL A 1 81  ? 21.530  -26.808 48.916 1.00 27.48  ? 97  VAL A CA  1 
ATOM   623  C C   . VAL A 1 81  ? 20.243  -27.219 48.214 1.00 25.94  ? 97  VAL A C   1 
ATOM   624  O O   . VAL A 1 81  ? 19.269  -27.565 48.874 1.00 26.86  ? 97  VAL A O   1 
ATOM   625  C CB  . VAL A 1 81  ? 22.068  -27.968 49.769 1.00 27.82  ? 97  VAL A CB  1 
ATOM   626  C CG1 . VAL A 1 81  ? 22.313  -29.227 48.943 1.00 29.80  ? 97  VAL A CG1 1 
ATOM   627  C CG2 . VAL A 1 81  ? 23.312  -27.548 50.531 1.00 28.64  ? 97  VAL A CG2 1 
ATOM   628  N N   . PHE A 1 82  ? 20.240  -27.156 46.882 1.00 29.18  ? 98  PHE A N   1 
ATOM   629  C CA  . PHE A 1 82  ? 19.053  -27.485 46.100 1.00 27.91  ? 98  PHE A CA  1 
ATOM   630  C C   . PHE A 1 82  ? 19.021  -28.990 45.864 1.00 27.22  ? 98  PHE A C   1 
ATOM   631  O O   . PHE A 1 82  ? 20.016  -29.562 45.436 1.00 25.09  ? 98  PHE A O   1 
ATOM   632  C CB  . PHE A 1 82  ? 19.059  -26.730 44.767 1.00 27.57  ? 98  PHE A CB  1 
ATOM   633  C CG  . PHE A 1 82  ? 17.915  -27.046 43.828 1.00 29.29  ? 98  PHE A CG  1 
ATOM   634  C CD1 . PHE A 1 82  ? 16.597  -26.878 44.230 1.00 31.28  ? 98  PHE A CD1 1 
ATOM   635  C CD2 . PHE A 1 82  ? 18.153  -27.498 42.538 1.00 29.38  ? 98  PHE A CD2 1 
ATOM   636  C CE1 . PHE A 1 82  ? 15.547  -27.180 43.371 1.00 28.53  ? 98  PHE A CE1 1 
ATOM   637  C CE2 . PHE A 1 82  ? 17.104  -27.783 41.677 1.00 29.90  ? 98  PHE A CE2 1 
ATOM   638  C CZ  . PHE A 1 82  ? 15.802  -27.639 42.104 1.00 31.42  ? 98  PHE A CZ  1 
ATOM   639  N N   . THR A 1 83  ? 17.866  -29.618 46.112 1.00 27.73  ? 99  THR A N   1 
ATOM   640  C CA  . THR A 1 83  ? 17.660  -30.994 45.682 1.00 31.14  ? 99  THR A CA  1 
ATOM   641  C C   . THR A 1 83  ? 16.672  -31.005 44.509 1.00 30.35  ? 99  THR A C   1 
ATOM   642  O O   . THR A 1 83  ? 15.479  -30.776 44.714 1.00 31.98  ? 99  THR A O   1 
ATOM   643  C CB  . THR A 1 83  ? 17.170  -31.880 46.838 1.00 33.77  ? 99  THR A CB  1 
ATOM   644  O OG1 . THR A 1 83  ? 18.207  -31.954 47.818 1.00 30.30  ? 99  THR A OG1 1 
ATOM   645  C CG2 . THR A 1 83  ? 16.784  -33.275 46.394 1.00 37.00  ? 99  THR A CG2 1 
ATOM   646  N N   . PRO A 1 84  ? 17.133  -31.300 43.270 1.00 27.78  ? 100 PRO A N   1 
ATOM   647  C CA  . PRO A 1 84  ? 16.249  -31.383 42.111 1.00 32.68  ? 100 PRO A CA  1 
ATOM   648  C C   . PRO A 1 84  ? 15.226  -32.501 42.269 1.00 33.41  ? 100 PRO A C   1 
ATOM   649  O O   . PRO A 1 84  ? 15.605  -33.664 42.322 1.00 30.20  ? 100 PRO A O   1 
ATOM   650  C CB  . PRO A 1 84  ? 17.140  -31.729 40.915 1.00 32.79  ? 100 PRO A CB  1 
ATOM   651  C CG  . PRO A 1 84  ? 18.563  -31.784 41.446 1.00 30.32  ? 100 PRO A CG  1 
ATOM   652  C CD  . PRO A 1 84  ? 18.501  -31.726 42.953 1.00 29.56  ? 100 PRO A CD  1 
ATOM   653  N N   . GLY A 1 85  ? 13.946  -32.125 42.392 1.00 41.72  ? 101 GLY A N   1 
ATOM   654  C CA  . GLY A 1 85  ? 12.862  -33.077 42.588 1.00 42.53  ? 101 GLY A CA  1 
ATOM   655  C C   . GLY A 1 85  ? 12.837  -33.587 44.026 1.00 45.01  ? 101 GLY A C   1 
ATOM   656  O O   . GLY A 1 85  ? 13.417  -32.979 44.925 1.00 53.15  ? 101 GLY A O   1 
ATOM   657  N N   . SER A 1 86  ? 12.153  -34.714 44.231 1.00 41.25  ? 102 SER A N   1 
ATOM   658  C CA  . SER A 1 86  ? 12.207  -35.415 45.499 1.00 42.56  ? 102 SER A CA  1 
ATOM   659  C C   . SER A 1 86  ? 13.373  -36.393 45.518 1.00 40.17  ? 102 SER A C   1 
ATOM   660  O O   . SER A 1 86  ? 13.672  -36.947 46.570 1.00 45.30  ? 102 SER A O   1 
ATOM   661  C CB  . SER A 1 86  ? 10.929  -36.154 45.780 1.00 49.19  ? 102 SER A CB  1 
ATOM   662  O OG  . SER A 1 86  ? 9.829   -35.262 45.808 1.00 54.19  ? 102 SER A OG  1 
ATOM   663  N N   . SER A 1 87  ? 13.994  -36.660 44.360 1.00 33.05  ? 103 SER A N   1 
ATOM   664  C CA  . SER A 1 87  ? 14.864  -37.819 44.282 1.00 33.66  ? 103 SER A CA  1 
ATOM   665  C C   . SER A 1 87  ? 16.275  -37.470 43.824 1.00 29.63  ? 103 SER A C   1 
ATOM   666  O O   . SER A 1 87  ? 17.124  -38.346 43.790 1.00 28.98  ? 103 SER A O   1 
ATOM   667  C CB  . SER A 1 87  ? 14.235  -38.856 43.398 1.00 40.53  ? 103 SER A CB  1 
ATOM   668  O OG  . SER A 1 87  ? 12.938  -39.196 43.880 1.00 38.66  ? 103 SER A OG  1 
ATOM   669  N N   . GLY A 1 88  ? 16.523  -36.202 43.484 1.00 29.29  ? 104 GLY A N   1 
ATOM   670  C CA  . GLY A 1 88  ? 17.786  -35.796 42.891 1.00 29.62  ? 104 GLY A CA  1 
ATOM   671  C C   . GLY A 1 88  ? 18.923  -35.811 43.911 1.00 27.63  ? 104 GLY A C   1 
ATOM   672  O O   . GLY A 1 88  ? 18.691  -35.747 45.117 1.00 30.29  ? 104 GLY A O   1 
ATOM   673  N N   . ARG A 1 89  ? 20.147  -35.951 43.418 1.00 27.63  ? 105 ARG A N   1 
ATOM   674  C CA  . ARG A 1 89  ? 21.312  -35.817 44.276 1.00 28.27  ? 105 ARG A CA  1 
ATOM   675  C C   . ARG A 1 89  ? 21.424  -34.362 44.712 1.00 26.72  ? 105 ARG A C   1 
ATOM   676  O O   . ARG A 1 89  ? 21.455  -33.471 43.876 1.00 26.59  ? 105 ARG A O   1 
ATOM   677  C CB  . ARG A 1 89  ? 22.587  -36.264 43.560 1.00 27.22  ? 105 ARG A CB  1 
ATOM   678  C CG  . ARG A 1 89  ? 23.850  -36.057 44.381 1.00 25.36  ? 105 ARG A CG  1 
ATOM   679  C CD  . ARG A 1 89  ? 24.994  -36.654 43.610 1.00 25.14  ? 105 ARG A CD  1 
ATOM   680  N NE  . ARG A 1 89  ? 26.262  -36.461 44.265 1.00 24.92  ? 105 ARG A NE  1 
ATOM   681  C CZ  . ARG A 1 89  ? 27.415  -36.909 43.800 1.00 23.99  ? 105 ARG A CZ  1 
ATOM   682  N NH1 . ARG A 1 89  ? 27.456  -37.595 42.672 1.00 23.63  ? 105 ARG A NH1 1 
ATOM   683  N NH2 . ARG A 1 89  ? 28.529  -36.683 44.476 1.00 22.83  ? 105 ARG A NH2 1 
ATOM   684  N N   . PRO A 1 90  ? 21.522  -34.084 46.026 1.00 26.26  ? 106 PRO A N   1 
ATOM   685  C CA  . PRO A 1 90  ? 21.691  -32.717 46.514 1.00 26.99  ? 106 PRO A CA  1 
ATOM   686  C C   . PRO A 1 90  ? 22.837  -31.997 45.805 1.00 26.67  ? 106 PRO A C   1 
ATOM   687  O O   . PRO A 1 90  ? 23.903  -32.563 45.599 1.00 23.61  ? 106 PRO A O   1 
ATOM   688  C CB  . PRO A 1 90  ? 22.000  -32.915 48.015 1.00 27.01  ? 106 PRO A CB  1 
ATOM   689  C CG  . PRO A 1 90  ? 21.304  -34.211 48.354 1.00 30.14  ? 106 PRO A CG  1 
ATOM   690  C CD  . PRO A 1 90  ? 21.506  -35.069 47.119 1.00 29.71  ? 106 PRO A CD  1 
ATOM   691  N N   . GLN A 1 91  ? 22.618  -30.722 45.463 1.00 26.51  ? 107 GLN A N   1 
ATOM   692  C CA  . GLN A 1 91  ? 23.619  -29.926 44.773 1.00 25.07  ? 107 GLN A CA  1 
ATOM   693  C C   . GLN A 1 91  ? 24.572  -29.302 45.802 1.00 23.84  ? 107 GLN A C   1 
ATOM   694  O O   . GLN A 1 91  ? 24.620  -28.081 45.989 1.00 20.69  ? 107 GLN A O   1 
ATOM   695  C CB  . GLN A 1 91  ? 22.902  -28.893 43.899 1.00 25.24  ? 107 GLN A CB  1 
ATOM   696  C CG  . GLN A 1 91  ? 22.072  -29.495 42.765 1.00 24.97  ? 107 GLN A CG  1 
ATOM   697  C CD  . GLN A 1 91  ? 21.650  -28.446 41.755 1.00 25.71  ? 107 GLN A CD  1 
ATOM   698  O OE1 . GLN A 1 91  ? 21.569  -27.252 42.034 1.00 24.48  ? 107 GLN A OE1 1 
ATOM   699  N NE2 . GLN A 1 91  ? 21.403  -28.878 40.535 1.00 26.30  ? 107 GLN A NE2 1 
ATOM   700  N N   . THR A 1 92  ? 25.417  -30.154 46.392 1.00 22.78  ? 108 THR A N   1 
ATOM   701  C CA  . THR A 1 92  ? 26.276  -29.789 47.520 1.00 23.91  ? 108 THR A CA  1 
ATOM   702  C C   . THR A 1 92  ? 27.415  -28.821 47.147 1.00 23.95  ? 108 THR A C   1 
ATOM   703  O O   . THR A 1 92  ? 27.972  -28.162 48.032 1.00 25.79  ? 108 THR A O   1 
ATOM   704  C CB  . THR A 1 92  ? 26.834  -31.075 48.145 1.00 23.77  ? 108 THR A CB  1 
ATOM   705  O OG1 . THR A 1 92  ? 27.363  -31.900 47.098 1.00 25.51  ? 108 THR A OG1 1 
ATOM   706  C CG2 . THR A 1 92  ? 25.769  -31.839 48.895 1.00 24.08  ? 108 THR A CG2 1 
ATOM   707  N N   . GLY A 1 93  ? 27.787  -28.740 45.862 1.00 21.55  ? 109 GLY A N   1 
ATOM   708  C CA  . GLY A 1 93  ? 28.784  -27.780 45.404 1.00 22.68  ? 109 GLY A CA  1 
ATOM   709  C C   . GLY A 1 93  ? 28.260  -26.339 45.319 1.00 23.15  ? 109 GLY A C   1 
ATOM   710  O O   . GLY A 1 93  ? 29.037  -25.388 45.375 1.00 22.10  ? 109 GLY A O   1 
ATOM   711  N N   . PHE A 1 94  ? 26.937  -26.187 45.197 1.00 25.12  ? 110 PHE A N   1 
ATOM   712  C CA  . PHE A 1 94  ? 26.296  -24.905 44.971 1.00 25.44  ? 110 PHE A CA  1 
ATOM   713  C C   . PHE A 1 94  ? 25.678  -24.403 46.268 1.00 22.53  ? 110 PHE A C   1 
ATOM   714  O O   . PHE A 1 94  ? 25.279  -25.195 47.112 1.00 21.93  ? 110 PHE A O   1 
ATOM   715  C CB  . PHE A 1 94  ? 25.189  -25.021 43.912 1.00 24.54  ? 110 PHE A CB  1 
ATOM   716  C CG  . PHE A 1 94  ? 25.607  -25.210 42.469 1.00 25.95  ? 110 PHE A CG  1 
ATOM   717  C CD1 . PHE A 1 94  ? 26.837  -24.783 41.990 1.00 27.69  ? 110 PHE A CD1 1 
ATOM   718  C CD2 . PHE A 1 94  ? 24.737  -25.801 41.563 1.00 27.78  ? 110 PHE A CD2 1 
ATOM   719  C CE1 . PHE A 1 94  ? 27.188  -24.946 40.653 1.00 25.04  ? 110 PHE A CE1 1 
ATOM   720  C CE2 . PHE A 1 94  ? 25.104  -25.998 40.240 1.00 26.96  ? 110 PHE A CE2 1 
ATOM   721  C CZ  . PHE A 1 94  ? 26.330  -25.575 39.785 1.00 26.20  ? 110 PHE A CZ  1 
ATOM   722  N N   . ARG A 1 95  ? 25.610  -23.076 46.404 1.00 21.53  ? 111 ARG A N   1 
ATOM   723  C CA  . ARG A 1 95  ? 24.735  -22.439 47.378 1.00 20.98  ? 111 ARG A CA  1 
ATOM   724  C C   . ARG A 1 95  ? 23.831  -21.516 46.571 1.00 21.48  ? 111 ARG A C   1 
ATOM   725  O O   . ARG A 1 95  ? 24.320  -20.595 45.888 1.00 20.96  ? 111 ARG A O   1 
ATOM   726  C CB  . ARG A 1 95  ? 25.520  -21.686 48.468 1.00 22.23  ? 111 ARG A CB  1 
ATOM   727  C CG  . ARG A 1 95  ? 26.271  -22.581 49.456 1.00 23.55  ? 111 ARG A CG  1 
ATOM   728  C CD  . ARG A 1 95  ? 25.352  -23.564 50.184 1.00 23.71  ? 111 ARG A CD  1 
ATOM   729  N NE  . ARG A 1 95  ? 26.074  -24.445 51.100 1.00 24.47  ? 111 ARG A NE  1 
ATOM   730  C CZ  . ARG A 1 95  ? 26.693  -25.571 50.763 1.00 24.86  ? 111 ARG A CZ  1 
ATOM   731  N NH1 . ARG A 1 95  ? 26.591  -26.061 49.539 1.00 24.51  ? 111 ARG A NH1 1 
ATOM   732  N NH2 . ARG A 1 95  ? 27.383  -26.237 51.675 1.00 26.21  ? 111 ARG A NH2 1 
ATOM   733  N N   . ARG A 1 96  ? 22.527  -21.805 46.578 1.00 22.09  ? 112 ARG A N   1 
ATOM   734  C CA  . ARG A 1 96  ? 21.672  -21.080 45.655 1.00 25.19  ? 112 ARG A CA  1 
ATOM   735  C C   . ARG A 1 96  ? 20.293  -20.828 46.243 1.00 23.55  ? 112 ARG A C   1 
ATOM   736  O O   . ARG A 1 96  ? 19.735  -21.656 46.946 1.00 23.74  ? 112 ARG A O   1 
ATOM   737  C CB  . ARG A 1 96  ? 21.568  -21.799 44.307 1.00 25.23  ? 112 ARG A CB  1 
ATOM   738  C CG  . ARG A 1 96  ? 20.745  -23.074 44.339 1.00 26.35  ? 112 ARG A CG  1 
ATOM   739  C CD  . ARG A 1 96  ? 21.070  -23.915 43.123 1.00 28.28  ? 112 ARG A CD  1 
ATOM   740  N NE  . ARG A 1 96  ? 20.623  -23.238 41.910 1.00 29.67  ? 112 ARG A NE  1 
ATOM   741  C CZ  . ARG A 1 96  ? 20.455  -23.843 40.740 1.00 29.94  ? 112 ARG A CZ  1 
ATOM   742  N NH1 . ARG A 1 96  ? 20.747  -25.125 40.606 1.00 27.42  ? 112 ARG A NH1 1 
ATOM   743  N NH2 . ARG A 1 96  ? 19.996  -23.159 39.708 1.00 30.40  ? 112 ARG A NH2 1 
ATOM   744  N N   . THR A 1 97  ? 19.795  -19.636 45.899 1.00 23.13  ? 113 THR A N   1 
ATOM   745  C CA  . THR A 1 97  ? 18.429  -19.214 46.091 1.00 21.70  ? 113 THR A CA  1 
ATOM   746  C C   . THR A 1 97  ? 18.033  -18.450 44.832 1.00 22.24  ? 113 THR A C   1 
ATOM   747  O O   . THR A 1 97  ? 18.600  -17.386 44.555 1.00 21.51  ? 113 THR A O   1 
ATOM   748  C CB  . THR A 1 97  ? 18.260  -18.298 47.304 1.00 21.61  ? 113 THR A CB  1 
ATOM   749  O OG1 . THR A 1 97  ? 18.538  -18.963 48.541 1.00 21.94  ? 113 THR A OG1 1 
ATOM   750  C CG2 . THR A 1 97  ? 16.850  -17.751 47.361 1.00 23.02  ? 113 THR A CG2 1 
ATOM   751  N N   . GLU A 1 98  ? 17.050  -18.974 44.089 1.00 20.61  ? 114 GLU A N   1 
ATOM   752  C CA  . GLU A 1 98  ? 16.524  -18.244 42.950 1.00 23.30  ? 114 GLU A CA  1 
ATOM   753  C C   . GLU A 1 98  ? 15.001  -18.164 42.944 1.00 23.67  ? 114 GLU A C   1 
ATOM   754  O O   . GLU A 1 98  ? 14.293  -19.013 43.496 1.00 21.91  ? 114 GLU A O   1 
ATOM   755  C CB  . GLU A 1 98  ? 16.989  -18.900 41.660 1.00 24.18  ? 114 GLU A CB  1 
ATOM   756  C CG  . GLU A 1 98  ? 18.460  -18.723 41.411 1.00 26.21  ? 114 GLU A CG  1 
ATOM   757  C CD  . GLU A 1 98  ? 19.094  -20.006 40.915 1.00 27.91  ? 114 GLU A CD  1 
ATOM   758  O OE1 . GLU A 1 98  ? 18.635  -20.533 39.887 1.00 25.06  ? 114 GLU A OE1 1 
ATOM   759  O OE2 . GLU A 1 98  ? 20.029  -20.480 41.583 1.00 32.96  ? 114 GLU A OE2 1 
ATOM   760  N N   . LEU A 1 99  ? 14.537  -17.068 42.329 1.00 24.11  ? 115 LEU A N   1 
ATOM   761  C CA  . LEU A 1 99  ? 13.145  -16.886 41.952 1.00 23.25  ? 115 LEU A CA  1 
ATOM   762  C C   . LEU A 1 99  ? 13.053  -16.972 40.438 1.00 24.48  ? 115 LEU A C   1 
ATOM   763  O O   . LEU A 1 99  ? 13.913  -16.437 39.731 1.00 24.50  ? 115 LEU A O   1 
ATOM   764  C CB  . LEU A 1 99  ? 12.668  -15.503 42.400 1.00 24.81  ? 115 LEU A CB  1 
ATOM   765  C CG  . LEU A 1 99  ? 12.693  -15.227 43.901 1.00 24.45  ? 115 LEU A CG  1 
ATOM   766  C CD1 . LEU A 1 99  ? 12.421  -13.762 44.169 1.00 25.05  ? 115 LEU A CD1 1 
ATOM   767  C CD2 . LEU A 1 99  ? 11.712  -16.110 44.627 1.00 24.65  ? 115 LEU A CD2 1 
ATOM   768  N N   . ILE A 1 100 ? 11.976  -17.618 39.968 1.00 22.47  ? 116 ILE A N   1 
ATOM   769  C CA  . ILE A 1 100 ? 11.779  -17.892 38.567 1.00 23.29  ? 116 ILE A CA  1 
ATOM   770  C C   . ILE A 1 100 ? 10.462  -17.253 38.147 1.00 24.60  ? 116 ILE A C   1 
ATOM   771  O O   . ILE A 1 100 ? 9.442   -17.436 38.799 1.00 25.12  ? 116 ILE A O   1 
ATOM   772  C CB  . ILE A 1 100 ? 11.812  -19.415 38.320 1.00 24.97  ? 116 ILE A CB  1 
ATOM   773  C CG1 . ILE A 1 100 ? 13.213  -19.972 38.577 1.00 24.61  ? 116 ILE A CG1 1 
ATOM   774  C CG2 . ILE A 1 100 ? 11.321  -19.771 36.919 1.00 23.83  ? 116 ILE A CG2 1 
ATOM   775  C CD1 . ILE A 1 100 ? 13.327  -21.494 38.337 1.00 27.93  ? 116 ILE A CD1 1 
ATOM   776  N N   . ALA A 1 101 ? 10.487  -16.515 37.042 1.00 25.40  ? 117 ALA A N   1 
ATOM   777  C CA  . ALA A 1 101 ? 9.283   -15.903 36.511 1.00 25.50  ? 117 ALA A CA  1 
ATOM   778  C C   . ALA A 1 101 ? 8.239   -16.959 36.145 1.00 24.93  ? 117 ALA A C   1 
ATOM   779  O O   . ALA A 1 101 ? 8.552   -17.901 35.425 1.00 25.81  ? 117 ALA A O   1 
ATOM   780  C CB  . ALA A 1 101 ? 9.665   -15.103 35.297 1.00 27.22  ? 117 ALA A CB  1 
ATOM   781  N N   . GLN A 1 102 ? 6.994   -16.745 36.598 1.00 25.87  ? 118 GLN A N   1 
ATOM   782  C CA  . GLN A 1 102 ? 5.843   -17.514 36.155 1.00 28.12  ? 118 GLN A CA  1 
ATOM   783  C C   . GLN A 1 102 ? 4.615   -16.620 35.963 1.00 29.93  ? 118 GLN A C   1 
ATOM   784  O O   . GLN A 1 102 ? 4.542   -15.501 36.470 1.00 26.74  ? 118 GLN A O   1 
ATOM   785  C CB  . GLN A 1 102 ? 5.527   -18.627 37.153 1.00 30.68  ? 118 GLN A CB  1 
ATOM   786  C CG  . GLN A 1 102 ? 5.059   -18.126 38.507 1.00 32.96  ? 118 GLN A CG  1 
ATOM   787  C CD  . GLN A 1 102 ? 4.647   -19.203 39.484 1.00 29.00  ? 118 GLN A CD  1 
ATOM   788  O OE1 . GLN A 1 102 ? 4.051   -18.933 40.519 1.00 37.46  ? 118 GLN A OE1 1 
ATOM   789  N NE2 . GLN A 1 102 ? 4.991   -20.436 39.194 1.00 32.48  ? 118 GLN A NE2 1 
ATOM   790  N N   . VAL A 1 103 ? 3.646   -17.160 35.208 1.00 33.01  ? 119 VAL A N   1 
ATOM   791  C CA  . VAL A 1 103 ? 2.365   -16.526 34.956 1.00 35.35  ? 119 VAL A CA  1 
ATOM   792  C C   . VAL A 1 103 ? 1.317   -17.629 35.073 1.00 39.95  ? 119 VAL A C   1 
ATOM   793  O O   . VAL A 1 103 ? 1.521   -18.724 34.547 1.00 45.00  ? 119 VAL A O   1 
ATOM   794  C CB  . VAL A 1 103 ? 2.385   -15.823 33.581 1.00 41.84  ? 119 VAL A CB  1 
ATOM   795  C CG1 . VAL A 1 103 ? 2.319   -16.822 32.430 1.00 45.25  ? 119 VAL A CG1 1 
ATOM   796  C CG2 . VAL A 1 103 ? 1.300   -14.764 33.433 1.00 43.04  ? 119 VAL A CG2 1 
ATOM   797  N N   . ASN A 1 104 ? 0.264   -17.362 35.857 1.00 47.14  ? 120 ASN A N   1 
ATOM   798  C CA  . ASN A 1 104 ? -0.819  -18.298 36.154 1.00 50.70  ? 120 ASN A CA  1 
ATOM   799  C C   . ASN A 1 104 ? -0.276  -19.608 36.715 1.00 51.34  ? 120 ASN A C   1 
ATOM   800  O O   . ASN A 1 104 ? -0.716  -20.681 36.314 1.00 56.50  ? 120 ASN A O   1 
ATOM   801  C CB  . ASN A 1 104 ? -1.703  -18.579 34.934 1.00 51.21  ? 120 ASN A CB  1 
ATOM   802  C CG  . ASN A 1 104 ? -2.196  -17.307 34.275 1.00 54.32  ? 120 ASN A CG  1 
ATOM   803  O OD1 . ASN A 1 104 ? -2.910  -16.514 34.895 1.00 54.27  ? 120 ASN A OD1 1 
ATOM   804  N ND2 . ASN A 1 104 ? -1.796  -17.089 33.032 1.00 50.93  ? 120 ASN A ND2 1 
ATOM   805  N N   . GLY A 1 105 ? 0.682   -19.516 37.638 1.00 46.74  ? 121 GLY A N   1 
ATOM   806  C CA  . GLY A 1 105 ? 1.209   -20.703 38.290 1.00 45.04  ? 121 GLY A CA  1 
ATOM   807  C C   . GLY A 1 105 ? 2.251   -21.469 37.470 1.00 43.89  ? 121 GLY A C   1 
ATOM   808  O O   . GLY A 1 105 ? 2.808   -22.435 37.972 1.00 41.76  ? 121 GLY A O   1 
ATOM   809  N N   . SER A 1 106 ? 2.576   -21.037 36.243 1.00 44.94  ? 122 SER A N   1 
ATOM   810  C CA  . SER A 1 106 ? 3.422   -21.855 35.380 1.00 41.18  ? 122 SER A CA  1 
ATOM   811  C C   . SER A 1 106 ? 4.582   -21.060 34.782 1.00 36.39  ? 122 SER A C   1 
ATOM   812  O O   . SER A 1 106 ? 4.394   -19.997 34.190 1.00 34.85  ? 122 SER A O   1 
ATOM   813  C CB  . SER A 1 106 ? 2.625   -22.489 34.272 1.00 45.65  ? 122 SER A CB  1 
ATOM   814  O OG  . SER A 1 106 ? 3.420   -23.426 33.557 1.00 49.33  ? 122 SER A OG  1 
ATOM   815  N N   . ASN A 1 107 ? 5.779   -21.636 34.892 1.00 39.45  ? 123 ASN A N   1 
ATOM   816  C CA  . ASN A 1 107 ? 6.943   -21.154 34.169 1.00 41.35  ? 123 ASN A CA  1 
ATOM   817  C C   . ASN A 1 107 ? 6.849   -21.625 32.714 1.00 41.94  ? 123 ASN A C   1 
ATOM   818  O O   . ASN A 1 107 ? 7.228   -20.877 31.812 1.00 37.11  ? 123 ASN A O   1 
ATOM   819  C CB  . ASN A 1 107 ? 8.256   -21.508 34.888 1.00 43.74  ? 123 ASN A CB  1 
ATOM   820  C CG  . ASN A 1 107 ? 8.558   -22.990 34.985 1.00 41.55  ? 123 ASN A CG  1 
ATOM   821  O OD1 . ASN A 1 107 ? 9.384   -23.500 34.241 1.00 44.19  ? 123 ASN A OD1 1 
ATOM   822  N ND2 . ASN A 1 107 ? 7.909   -23.692 35.892 1.00 39.61  ? 123 ASN A ND2 1 
ATOM   823  N N   . ILE A 1 108 ? 6.239   -22.804 32.477 1.00 43.68  ? 124 ILE A N   1 
ATOM   824  C CA  . ILE A 1 108 ? 6.204   -23.402 31.145 1.00 46.19  ? 124 ILE A CA  1 
ATOM   825  C C   . ILE A 1 108 ? 5.417   -22.508 30.177 1.00 45.71  ? 124 ILE A C   1 
ATOM   826  O O   . ILE A 1 108 ? 5.897   -22.236 29.078 1.00 46.39  ? 124 ILE A O   1 
ATOM   827  C CB  . ILE A 1 108 ? 5.636   -24.841 31.154 1.00 53.04  ? 124 ILE A CB  1 
ATOM   828  C CG1 . ILE A 1 108 ? 6.360   -25.783 32.130 1.00 55.78  ? 124 ILE A CG1 1 
ATOM   829  C CG2 . ILE A 1 108 ? 5.615   -25.405 29.736 1.00 53.82  ? 124 ILE A CG2 1 
ATOM   830  C CD1 . ILE A 1 108 ? 7.847   -25.964 31.882 1.00 57.67  ? 124 ILE A CD1 1 
ATOM   831  N N   . ASP A 1 109 ? 4.209   -22.074 30.569 1.00 41.68  ? 125 ASP A N   1 
ATOM   832  C CA  . ASP A 1 109 ? 3.382   -21.219 29.725 1.00 45.35  ? 125 ASP A CA  1 
ATOM   833  C C   . ASP A 1 109 ? 4.049   -19.866 29.430 1.00 43.43  ? 125 ASP A C   1 
ATOM   834  O O   . ASP A 1 109 ? 3.656   -19.182 28.484 1.00 42.90  ? 125 ASP A O   1 
ATOM   835  C CB  . ASP A 1 109 ? 2.011   -20.950 30.355 1.00 45.98  ? 125 ASP A CB  1 
ATOM   836  C CG  . ASP A 1 109 ? 1.124   -22.179 30.507 1.00 52.01  ? 125 ASP A CG  1 
ATOM   837  O OD1 . ASP A 1 109 ? 1.424   -23.213 29.861 1.00 47.42  ? 125 ASP A OD1 1 
ATOM   838  O OD2 . ASP A 1 109 ? 0.159   -22.104 31.306 1.00 49.49  ? 125 ASP A OD2 1 
ATOM   839  N N   . LEU A 1 110 ? 5.030   -19.446 30.245 1.00 40.30  ? 126 LEU A N   1 
ATOM   840  C CA  . LEU A 1 110 ? 5.645   -18.138 30.043 1.00 35.37  ? 126 LEU A CA  1 
ATOM   841  C C   . LEU A 1 110 ? 6.734   -18.217 28.979 1.00 31.04  ? 126 LEU A C   1 
ATOM   842  O O   . LEU A 1 110 ? 7.040   -17.193 28.371 1.00 29.76  ? 126 LEU A O   1 
ATOM   843  C CB  . LEU A 1 110 ? 6.197   -17.621 31.376 1.00 35.76  ? 126 LEU A CB  1 
ATOM   844  C CG  . LEU A 1 110 ? 6.788   -16.212 31.379 1.00 34.52  ? 126 LEU A CG  1 
ATOM   845  C CD1 . LEU A 1 110 ? 5.742   -15.167 31.037 1.00 35.43  ? 126 LEU A CD1 1 
ATOM   846  C CD2 . LEU A 1 110 ? 7.382   -15.919 32.743 1.00 33.48  ? 126 LEU A CD2 1 
ATOM   847  N N   . ILE A 1 111 ? 7.292   -19.421 28.754 1.00 31.14  ? 127 ILE A N   1 
ATOM   848  C CA  . ILE A 1 111 ? 8.445   -19.617 27.879 1.00 30.96  ? 127 ILE A CA  1 
ATOM   849  C C   . ILE A 1 111 ? 8.162   -19.089 26.466 1.00 35.22  ? 127 ILE A C   1 
ATOM   850  O O   . ILE A 1 111 ? 9.021   -18.437 25.870 1.00 37.05  ? 127 ILE A O   1 
ATOM   851  C CB  . ILE A 1 111 ? 8.880   -21.099 27.815 1.00 33.93  ? 127 ILE A CB  1 
ATOM   852  C CG1 . ILE A 1 111 ? 9.349   -21.666 29.161 1.00 39.48  ? 127 ILE A CG1 1 
ATOM   853  C CG2 . ILE A 1 111 ? 9.959   -21.283 26.753 1.00 32.12  ? 127 ILE A CG2 1 
ATOM   854  C CD1 . ILE A 1 111 ? 9.602   -23.183 29.148 1.00 42.87  ? 127 ILE A CD1 1 
ATOM   855  N N   . PRO A 1 112 ? 7.004   -19.405 25.834 1.00 36.11  ? 128 PRO A N   1 
ATOM   856  C CA  . PRO A 1 112 ? 6.672   -18.848 24.523 1.00 40.09  ? 128 PRO A CA  1 
ATOM   857  C C   . PRO A 1 112 ? 6.473   -17.333 24.506 1.00 37.45  ? 128 PRO A C   1 
ATOM   858  O O   . PRO A 1 112 ? 6.779   -16.680 23.514 1.00 44.53  ? 128 PRO A O   1 
ATOM   859  C CB  . PRO A 1 112 ? 5.351   -19.551 24.158 1.00 41.04  ? 128 PRO A CB  1 
ATOM   860  C CG  . PRO A 1 112 ? 4.765   -19.936 25.487 1.00 40.63  ? 128 PRO A CG  1 
ATOM   861  C CD  . PRO A 1 112 ? 5.974   -20.351 26.294 1.00 39.56  ? 128 PRO A CD  1 
ATOM   862  N N   . ILE A 1 113 ? 5.977   -16.787 25.612 1.00 36.52  ? 129 ILE A N   1 
ATOM   863  C CA  . ILE A 1 113 ? 5.689   -15.365 25.708 1.00 38.56  ? 129 ILE A CA  1 
ATOM   864  C C   . ILE A 1 113 ? 7.002   -14.576 25.801 1.00 39.78  ? 129 ILE A C   1 
ATOM   865  O O   . ILE A 1 113 ? 7.187   -13.611 25.055 1.00 34.62  ? 129 ILE A O   1 
ATOM   866  C CB  . ILE A 1 113 ? 4.714   -15.104 26.877 1.00 40.99  ? 129 ILE A CB  1 
ATOM   867  C CG1 . ILE A 1 113 ? 3.390   -15.850 26.674 1.00 42.36  ? 129 ILE A CG1 1 
ATOM   868  C CG2 . ILE A 1 113 ? 4.482   -13.615 27.082 1.00 43.36  ? 129 ILE A CG2 1 
ATOM   869  C CD1 . ILE A 1 113 ? 2.495   -15.889 27.895 1.00 44.50  ? 129 ILE A CD1 1 
ATOM   870  N N   . ILE A 1 114 ? 7.947   -15.005 26.667 1.00 34.68  ? 130 ILE A N   1 
ATOM   871  C CA  . ILE A 1 114 ? 9.201   -14.268 26.824 1.00 30.81  ? 130 ILE A CA  1 
ATOM   872  C C   . ILE A 1 114 ? 10.247  -14.794 25.852 1.00 30.45  ? 130 ILE A C   1 
ATOM   873  O O   . ILE A 1 114 ? 11.375  -14.320 25.844 1.00 31.16  ? 130 ILE A O   1 
ATOM   874  C CB  . ILE A 1 114 ? 9.708   -14.294 28.281 1.00 27.79  ? 130 ILE A CB  1 
ATOM   875  C CG1 . ILE A 1 114 ? 10.158  -15.692 28.725 1.00 28.90  ? 130 ILE A CG1 1 
ATOM   876  C CG2 . ILE A 1 114 ? 8.657   -13.723 29.217 1.00 25.94  ? 130 ILE A CG2 1 
ATOM   877  C CD1 . ILE A 1 114 ? 10.912  -15.710 30.046 1.00 28.44  ? 130 ILE A CD1 1 
ATOM   878  N N   . GLY A 1 115 ? 9.876   -15.771 25.022 1.00 31.42  ? 131 GLY A N   1 
ATOM   879  C CA  . GLY A 1 115 ? 10.819  -16.410 24.120 1.00 32.82  ? 131 GLY A CA  1 
ATOM   880  C C   . GLY A 1 115 ? 10.580  -16.114 22.637 1.00 32.31  ? 131 GLY A C   1 
ATOM   881  O O   . GLY A 1 115 ? 11.173  -16.783 21.798 1.00 30.31  ? 131 GLY A O   1 
ATOM   882  N N   . LYS A 1 116 ? 9.757   -15.107 22.310 1.00 35.92  ? 132 LYS A N   1 
ATOM   883  C CA  . LYS A 1 116 ? 9.475   -14.770 20.913 1.00 37.03  ? 132 LYS A CA  1 
ATOM   884  C C   . LYS A 1 116 ? 9.744   -13.293 20.609 1.00 32.76  ? 132 LYS A C   1 
ATOM   885  O O   . LYS A 1 116 ? 9.383   -12.403 21.387 1.00 32.66  ? 132 LYS A O   1 
ATOM   886  C CB  . LYS A 1 116 ? 8.013   -15.064 20.562 1.00 43.04  ? 132 LYS A CB  1 
ATOM   887  C CG  . LYS A 1 116 ? 7.674   -16.529 20.332 1.00 47.60  ? 132 LYS A CG  1 
ATOM   888  C CD  . LYS A 1 116 ? 6.175   -16.788 20.245 1.00 50.44  ? 132 LYS A CD  1 
ATOM   889  C CE  . LYS A 1 116 ? 5.835   -18.268 20.261 1.00 51.97  ? 132 LYS A CE  1 
ATOM   890  N NZ  . LYS A 1 116 ? 4.423   -18.489 20.646 1.00 53.38  ? 132 LYS A NZ  1 
ATOM   891  N N   . GLY A 1 117 ? 10.311  -13.055 19.421 1.00 31.22  ? 133 GLY A N   1 
ATOM   892  C CA  . GLY A 1 117 ? 10.614  -11.719 18.938 1.00 31.78  ? 133 GLY A CA  1 
ATOM   893  C C   . GLY A 1 117 ? 11.737  -11.055 19.740 1.00 33.55  ? 133 GLY A C   1 
ATOM   894  O O   . GLY A 1 117 ? 12.719  -11.699 20.108 1.00 32.24  ? 133 GLY A O   1 
ATOM   895  N N   . ARG A 1 118 ? 11.587  -9.748  19.978 1.00 31.71  ? 134 ARG A N   1 
ATOM   896  C CA  . ARG A 1 118 ? 12.530  -8.991  20.787 1.00 31.49  ? 134 ARG A CA  1 
ATOM   897  C C   . ARG A 1 118 ? 11.937  -8.740  22.178 1.00 29.62  ? 134 ARG A C   1 
ATOM   898  O O   . ARG A 1 118 ? 10.812  -8.250  22.325 1.00 25.89  ? 134 ARG A O   1 
ATOM   899  C CB  . ARG A 1 118 ? 12.899  -7.700  20.058 1.00 35.04  ? 134 ARG A CB  1 
ATOM   900  C CG  . ARG A 1 118 ? 13.790  -7.940  18.843 1.00 38.73  ? 134 ARG A CG  1 
ATOM   901  C CD  . ARG A 1 118 ? 13.787  -6.767  17.894 1.00 42.10  ? 134 ARG A CD  1 
ATOM   902  N NE  . ARG A 1 118 ? 14.587  -5.656  18.371 1.00 47.71  ? 134 ARG A NE  1 
ATOM   903  C CZ  . ARG A 1 118 ? 14.207  -4.376  18.369 1.00 51.46  ? 134 ARG A CZ  1 
ATOM   904  N NH1 . ARG A 1 118 ? 12.978  -4.012  18.042 1.00 46.26  ? 134 ARG A NH1 1 
ATOM   905  N NH2 . ARG A 1 118 ? 15.075  -3.447  18.723 1.00 55.25  ? 134 ARG A NH2 1 
ATOM   906  N N   . VAL A 1 119 ? 12.712  -9.098  23.205 1.00 28.34  ? 135 VAL A N   1 
ATOM   907  C CA  . VAL A 1 119 ? 12.235  -9.058  24.583 1.00 26.96  ? 135 VAL A CA  1 
ATOM   908  C C   . VAL A 1 119 ? 13.320  -8.399  25.439 1.00 27.45  ? 135 VAL A C   1 
ATOM   909  O O   . VAL A 1 119 ? 14.501  -8.783  25.345 1.00 26.22  ? 135 VAL A O   1 
ATOM   910  C CB  . VAL A 1 119 ? 11.878  -10.478 25.084 1.00 25.57  ? 135 VAL A CB  1 
ATOM   911  C CG1 . VAL A 1 119 ? 11.448  -10.506 26.531 1.00 25.69  ? 135 VAL A CG1 1 
ATOM   912  C CG2 . VAL A 1 119 ? 10.798  -11.124 24.222 1.00 25.48  ? 135 VAL A CG2 1 
ATOM   913  N N   . ALA A 1 120 ? 12.898  -7.418  26.259 1.00 24.52  ? 136 ALA A N   1 
ATOM   914  C CA  . ALA A 1 120 ? 13.797  -6.754  27.193 1.00 23.86  ? 136 ALA A CA  1 
ATOM   915  C C   . ALA A 1 120 ? 13.624  -7.307  28.608 1.00 22.19  ? 136 ALA A C   1 
ATOM   916  O O   . ALA A 1 120 ? 12.550  -7.202  29.201 1.00 20.50  ? 136 ALA A O   1 
ATOM   917  C CB  . ALA A 1 120 ? 13.583  -5.263  27.150 1.00 24.58  ? 136 ALA A CB  1 
ATOM   918  N N   . PHE A 1 121 ? 14.723  -7.866  29.132 1.00 20.54  ? 137 PHE A N   1 
ATOM   919  C CA  . PHE A 1 121 ? 14.819  -8.341  30.508 1.00 21.49  ? 137 PHE A CA  1 
ATOM   920  C C   . PHE A 1 121 ? 15.447  -7.255  31.392 1.00 20.24  ? 137 PHE A C   1 
ATOM   921  O O   . PHE A 1 121 ? 16.602  -6.905  31.215 1.00 22.29  ? 137 PHE A O   1 
ATOM   922  C CB  . PHE A 1 121 ? 15.640  -9.630  30.533 1.00 22.71  ? 137 PHE A CB  1 
ATOM   923  C CG  . PHE A 1 121 ? 15.035  -10.771 29.743 1.00 23.31  ? 137 PHE A CG  1 
ATOM   924  C CD1 . PHE A 1 121 ? 15.195  -10.864 28.366 1.00 23.92  ? 137 PHE A CD1 1 
ATOM   925  C CD2 . PHE A 1 121 ? 14.297  -11.746 30.379 1.00 22.02  ? 137 PHE A CD2 1 
ATOM   926  C CE1 . PHE A 1 121 ? 14.624  -11.907 27.647 1.00 23.25  ? 137 PHE A CE1 1 
ATOM   927  C CE2 . PHE A 1 121 ? 13.715  -12.777 29.656 1.00 23.10  ? 137 PHE A CE2 1 
ATOM   928  C CZ  . PHE A 1 121 ? 13.869  -12.853 28.291 1.00 22.36  ? 137 PHE A CZ  1 
ATOM   929  N N   . HIS A 1 122 ? 14.672  -6.734  32.334 1.00 21.64  ? 138 HIS A N   1 
ATOM   930  C CA  . HIS A 1 122 ? 15.065  -5.660  33.219 1.00 22.04  ? 138 HIS A CA  1 
ATOM   931  C C   . HIS A 1 122 ? 15.377  -6.220  34.606 1.00 22.16  ? 138 HIS A C   1 
ATOM   932  O O   . HIS A 1 122 ? 14.751  -7.173  35.059 1.00 23.26  ? 138 HIS A O   1 
ATOM   933  C CB  . HIS A 1 122 ? 13.926  -4.658  33.441 1.00 22.04  ? 138 HIS A CB  1 
ATOM   934  C CG  . HIS A 1 122 ? 13.580  -3.849  32.236 1.00 23.85  ? 138 HIS A CG  1 
ATOM   935  N ND1 . HIS A 1 122 ? 14.070  -2.573  32.059 1.00 21.53  ? 138 HIS A ND1 1 
ATOM   936  C CD2 . HIS A 1 122 ? 12.853  -4.126  31.163 1.00 21.70  ? 138 HIS A CD2 1 
ATOM   937  C CE1 . HIS A 1 122 ? 13.640  -2.114  30.903 1.00 21.80  ? 138 HIS A CE1 1 
ATOM   938  N NE2 . HIS A 1 122 ? 12.888  -3.030  30.353 1.00 21.28  ? 138 HIS A NE2 1 
ATOM   939  N N   . PHE A 1 123 ? 16.342  -5.590  35.273 1.00 20.60  ? 139 PHE A N   1 
ATOM   940  C CA  . PHE A 1 123 ? 16.697  -5.949  36.632 1.00 19.43  ? 139 PHE A CA  1 
ATOM   941  C C   . PHE A 1 123 ? 17.725  -4.951  37.168 1.00 18.84  ? 139 PHE A C   1 
ATOM   942  O O   . PHE A 1 123 ? 18.658  -4.574  36.462 1.00 19.84  ? 139 PHE A O   1 
ATOM   943  C CB  . PHE A 1 123 ? 17.257  -7.378  36.704 1.00 19.08  ? 139 PHE A CB  1 
ATOM   944  C CG  . PHE A 1 123 ? 18.302  -7.697  35.663 1.00 19.55  ? 139 PHE A CG  1 
ATOM   945  C CD1 . PHE A 1 123 ? 17.943  -8.166  34.399 1.00 19.55  ? 139 PHE A CD1 1 
ATOM   946  C CD2 . PHE A 1 123 ? 19.646  -7.491  35.925 1.00 18.38  ? 139 PHE A CD2 1 
ATOM   947  C CE1 . PHE A 1 123 ? 18.906  -8.446  33.443 1.00 18.89  ? 139 PHE A CE1 1 
ATOM   948  C CE2 . PHE A 1 123 ? 20.609  -7.790  34.971 1.00 19.06  ? 139 PHE A CE2 1 
ATOM   949  C CZ  . PHE A 1 123 ? 20.244  -8.258  33.734 1.00 20.37  ? 139 PHE A CZ  1 
ATOM   950  N N   . SER A 1 124 ? 17.611  -4.671  38.463 1.00 19.28  ? 140 SER A N   1 
ATOM   951  C CA  . SER A 1 124 ? 18.432  -3.723  39.200 1.00 20.20  ? 140 SER A CA  1 
ATOM   952  C C   . SER A 1 124 ? 18.905  -4.410  40.475 1.00 20.95  ? 140 SER A C   1 
ATOM   953  O O   . SER A 1 124 ? 18.108  -5.087  41.126 1.00 19.97  ? 140 SER A O   1 
ATOM   954  C CB  . SER A 1 124 ? 17.655  -2.478  39.558 1.00 19.15  ? 140 SER A CB  1 
ATOM   955  O OG  . SER A 1 124 ? 17.179  -1.819  38.396 1.00 19.05  ? 140 SER A OG  1 
ATOM   956  N N   . VAL A 1 125 ? 20.191  -4.226  40.806 1.00 21.21  ? 141 VAL A N   1 
ATOM   957  C CA  . VAL A 1 125 ? 20.771  -4.831  41.990 1.00 21.63  ? 141 VAL A CA  1 
ATOM   958  C C   . VAL A 1 125 ? 21.387  -3.763  42.886 1.00 20.89  ? 141 VAL A C   1 
ATOM   959  O O   . VAL A 1 125 ? 21.851  -2.731  42.404 1.00 20.78  ? 141 VAL A O   1 
ATOM   960  C CB  . VAL A 1 125 ? 21.794  -5.930  41.640 1.00 21.08  ? 141 VAL A CB  1 
ATOM   961  C CG1 . VAL A 1 125 ? 21.099  -7.077  40.926 1.00 21.39  ? 141 VAL A CG1 1 
ATOM   962  C CG2 . VAL A 1 125 ? 22.982  -5.430  40.836 1.00 23.10  ? 141 VAL A CG2 1 
ATOM   963  N N   . LEU A 1 126 ? 21.340  -4.065  44.193 1.00 22.90  ? 142 LEU A N   1 
ATOM   964  C CA  . LEU A 1 126 ? 21.897  -3.259  45.268 1.00 23.35  ? 142 LEU A CA  1 
ATOM   965  C C   . LEU A 1 126 ? 22.660  -4.167  46.222 1.00 23.50  ? 142 LEU A C   1 
ATOM   966  O O   . LEU A 1 126 ? 22.141  -5.160  46.732 1.00 21.82  ? 142 LEU A O   1 
ATOM   967  C CB  . LEU A 1 126 ? 20.781  -2.509  46.005 1.00 22.75  ? 142 LEU A CB  1 
ATOM   968  C CG  . LEU A 1 126 ? 21.168  -1.799  47.305 1.00 23.04  ? 142 LEU A CG  1 
ATOM   969  C CD1 . LEU A 1 126 ? 22.000  -0.552  47.022 1.00 23.07  ? 142 LEU A CD1 1 
ATOM   970  C CD2 . LEU A 1 126 ? 19.916  -1.421  48.093 1.00 22.69  ? 142 LEU A CD2 1 
ATOM   971  N N   . MET A 1 127 ? 23.896  -3.762  46.501 1.00 22.88  ? 143 MET A N   1 
ATOM   972  C CA  . MET A 1 127 ? 24.741  -4.511  47.406 1.00 26.81  ? 143 MET A CA  1 
ATOM   973  C C   . MET A 1 127 ? 24.110  -4.584  48.801 1.00 26.72  ? 143 MET A C   1 
ATOM   974  O O   . MET A 1 127 ? 23.589  -3.595  49.307 1.00 25.88  ? 143 MET A O   1 
ATOM   975  C CB  . MET A 1 127 ? 26.116  -3.843  47.455 1.00 25.88  ? 143 MET A CB  1 
ATOM   976  C CG  . MET A 1 127 ? 27.055  -4.449  48.449 1.00 29.21  ? 143 MET A CG  1 
ATOM   977  S SD  . MET A 1 127 ? 28.736  -3.877  48.141 1.00 28.96  ? 143 MET A SD  1 
ATOM   978  C CE  . MET A 1 127 ? 29.191  -4.830  46.699 1.00 31.32  ? 143 MET A CE  1 
ATOM   979  N N   . ASP A 1 128 ? 24.142  -5.780  49.404 1.00 27.06  ? 144 ASP A N   1 
ATOM   980  C CA  . ASP A 1 128 ? 23.717  -5.983  50.786 1.00 28.47  ? 144 ASP A CA  1 
ATOM   981  C C   . ASP A 1 128 ? 24.929  -5.789  51.699 1.00 31.33  ? 144 ASP A C   1 
ATOM   982  O O   . ASP A 1 128 ? 25.857  -6.593  51.685 1.00 34.23  ? 144 ASP A O   1 
ATOM   983  C CB  . ASP A 1 128 ? 23.134  -7.386  50.971 1.00 28.18  ? 144 ASP A CB  1 
ATOM   984  C CG  . ASP A 1 128 ? 22.694  -7.745  52.390 1.00 30.80  ? 144 ASP A CG  1 
ATOM   985  O OD1 . ASP A 1 128 ? 22.554  -6.831  53.245 1.00 32.72  ? 144 ASP A OD1 1 
ATOM   986  O OD2 . ASP A 1 128 ? 22.472  -8.943  52.622 1.00 27.99  ? 144 ASP A OD2 1 
ATOM   987  N N   . GLU A 1 129 ? 24.935  -4.700  52.479 1.00 37.17  ? 145 GLU A N   1 
ATOM   988  C CA  . GLU A 1 129 ? 26.069  -4.381  53.339 1.00 42.12  ? 145 GLU A CA  1 
ATOM   989  C C   . GLU A 1 129 ? 26.049  -5.252  54.610 1.00 38.73  ? 145 GLU A C   1 
ATOM   990  O O   . GLU A 1 129 ? 27.072  -5.383  55.273 1.00 42.90  ? 145 GLU A O   1 
ATOM   991  C CB  . GLU A 1 129 ? 26.090  -2.860  53.562 1.00 53.79  ? 145 GLU A CB  1 
ATOM   992  C CG  . GLU A 1 129 ? 24.847  -2.312  54.289 1.00 62.13  ? 145 GLU A CG  1 
ATOM   993  C CD  . GLU A 1 129 ? 24.343  -0.903  53.967 1.00 66.04  ? 145 GLU A CD  1 
ATOM   994  O OE1 . GLU A 1 129 ? 23.313  -0.497  54.589 1.00 51.41  ? 145 GLU A OE1 1 
ATOM   995  O OE2 . GLU A 1 129 ? 24.961  -0.204  53.106 1.00 65.51  ? 145 GLU A OE2 1 
ATOM   996  N N   . TRP A 1 130 ? 24.911  -5.905  54.915 1.00 37.07  ? 146 TRP A N   1 
ATOM   997  C CA  . TRP A 1 130 ? 24.742  -6.710  56.125 1.00 34.93  ? 146 TRP A CA  1 
ATOM   998  C C   . TRP A 1 130 ? 25.178  -8.161  55.953 1.00 30.27  ? 146 TRP A C   1 
ATOM   999  O O   . TRP A 1 130 ? 25.375  -8.835  56.947 1.00 31.08  ? 146 TRP A O   1 
ATOM   1000 C CB  . TRP A 1 130 ? 23.271  -6.708  56.572 1.00 39.17  ? 146 TRP A CB  1 
ATOM   1001 C CG  . TRP A 1 130 ? 22.730  -5.334  56.851 1.00 44.65  ? 146 TRP A CG  1 
ATOM   1002 C CD1 . TRP A 1 130 ? 21.984  -4.545  56.024 1.00 43.96  ? 146 TRP A CD1 1 
ATOM   1003 C CD2 . TRP A 1 130 ? 22.935  -4.586  58.065 1.00 44.51  ? 146 TRP A CD2 1 
ATOM   1004 N NE1 . TRP A 1 130 ? 21.720  -3.349  56.635 1.00 45.23  ? 146 TRP A NE1 1 
ATOM   1005 C CE2 . TRP A 1 130 ? 22.291  -3.343  57.883 1.00 49.54  ? 146 TRP A CE2 1 
ATOM   1006 C CE3 . TRP A 1 130 ? 23.597  -4.847  59.271 1.00 43.68  ? 146 TRP A CE3 1 
ATOM   1007 C CZ2 . TRP A 1 130 ? 22.289  -2.367  58.879 1.00 50.82  ? 146 TRP A CZ2 1 
ATOM   1008 C CZ3 . TRP A 1 130 ? 23.600  -3.879  60.248 1.00 47.60  ? 146 TRP A CZ3 1 
ATOM   1009 C CH2 . TRP A 1 130 ? 22.959  -2.654  60.049 1.00 50.61  ? 146 TRP A CH2 1 
ATOM   1010 N N   . HIS A 1 131 ? 25.195  -8.698  54.724 1.00 30.07  ? 147 HIS A N   1 
ATOM   1011 C CA  . HIS A 1 131 ? 25.680  -10.056 54.488 1.00 28.04  ? 147 HIS A CA  1 
ATOM   1012 C C   . HIS A 1 131 ? 26.493  -10.062 53.195 1.00 29.19  ? 147 HIS A C   1 
ATOM   1013 O O   . HIS A 1 131 ? 25.981  -10.402 52.121 1.00 29.26  ? 147 HIS A O   1 
ATOM   1014 C CB  . HIS A 1 131 ? 24.542  -11.085 54.404 1.00 28.66  ? 147 HIS A CB  1 
ATOM   1015 C CG  . HIS A 1 131 ? 23.407  -10.890 55.376 1.00 30.88  ? 147 HIS A CG  1 
ATOM   1016 N ND1 . HIS A 1 131 ? 22.299  -10.107 55.113 1.00 27.28  ? 147 HIS A ND1 1 
ATOM   1017 C CD2 . HIS A 1 131 ? 23.192  -11.452 56.573 1.00 29.39  ? 147 HIS A CD2 1 
ATOM   1018 C CE1 . HIS A 1 131 ? 21.468  -10.181 56.132 1.00 33.26  ? 147 HIS A CE1 1 
ATOM   1019 N NE2 . HIS A 1 131 ? 22.007  -10.975 57.043 1.00 31.52  ? 147 HIS A NE2 1 
ATOM   1020 N N   . LYS A 1 132 ? 27.758  -9.653  53.295 1.00 26.17  ? 148 LYS A N   1 
ATOM   1021 C CA  . LYS A 1 132 ? 28.506  -9.285  52.101 1.00 28.54  ? 148 LYS A CA  1 
ATOM   1022 C C   . LYS A 1 132 ? 28.786  -10.521 51.265 1.00 23.97  ? 148 LYS A C   1 
ATOM   1023 O O   . LYS A 1 132 ? 29.172  -11.552 51.809 1.00 22.18  ? 148 LYS A O   1 
ATOM   1024 C CB  . LYS A 1 132 ? 29.847  -8.612  52.429 1.00 33.83  ? 148 LYS A CB  1 
ATOM   1025 C CG  . LYS A 1 132 ? 29.735  -7.259  53.123 1.00 42.49  ? 148 LYS A CG  1 
ATOM   1026 C CD  . LYS A 1 132 ? 31.062  -6.632  53.519 1.00 51.69  ? 148 LYS A CD  1 
ATOM   1027 C CE  . LYS A 1 132 ? 30.910  -5.681  54.694 1.00 56.36  ? 148 LYS A CE  1 
ATOM   1028 N NZ  . LYS A 1 132 ? 32.158  -4.929  54.975 1.00 59.12  ? 148 LYS A NZ  1 
ATOM   1029 N N   . LEU A 1 133 ? 28.663  -10.352 49.938 1.00 23.85  ? 149 LEU A N   1 
ATOM   1030 C CA  . LEU A 1 133 ? 29.118  -11.346 48.982 1.00 24.69  ? 149 LEU A CA  1 
ATOM   1031 C C   . LEU A 1 133 ? 30.632  -11.489 49.085 1.00 24.92  ? 149 LEU A C   1 
ATOM   1032 O O   . LEU A 1 133 ? 31.351  -10.497 49.286 1.00 24.64  ? 149 LEU A O   1 
ATOM   1033 C CB  . LEU A 1 133 ? 28.684  -10.945 47.565 1.00 25.08  ? 149 LEU A CB  1 
ATOM   1034 C CG  . LEU A 1 133 ? 27.167  -10.965 47.315 1.00 23.27  ? 149 LEU A CG  1 
ATOM   1035 C CD1 . LEU A 1 133 ? 26.809  -10.296 46.004 1.00 25.15  ? 149 LEU A CD1 1 
ATOM   1036 C CD2 . LEU A 1 133 ? 26.657  -12.376 47.318 1.00 24.81  ? 149 LEU A CD2 1 
ATOM   1037 N N   . ASP A 1 134 ? 31.094  -12.751 48.988 1.00 24.04  ? 150 ASP A N   1 
ATOM   1038 C CA  . ASP A 1 134 ? 32.510  -13.040 48.902 1.00 22.31  ? 150 ASP A CA  1 
ATOM   1039 C C   . ASP A 1 134 ? 32.911  -13.154 47.433 1.00 23.87  ? 150 ASP A C   1 
ATOM   1040 O O   . ASP A 1 134 ? 32.635  -14.164 46.795 1.00 23.05  ? 150 ASP A O   1 
ATOM   1041 C CB  . ASP A 1 134 ? 32.846  -14.314 49.673 1.00 24.03  ? 150 ASP A CB  1 
ATOM   1042 C CG  . ASP A 1 134 ? 34.310  -14.707 49.560 1.00 25.22  ? 150 ASP A CG  1 
ATOM   1043 O OD1 . ASP A 1 134 ? 35.118  -13.831 49.188 1.00 24.80  ? 150 ASP A OD1 1 
ATOM   1044 O OD2 . ASP A 1 134 ? 34.619  -15.901 49.805 1.00 24.44  ? 150 ASP A OD2 1 
ATOM   1045 N N   . MET A 1 135 ? 33.685  -12.171 46.934 1.00 22.69  ? 151 MET A N   1 
ATOM   1046 C CA  . MET A 1 135 ? 34.043  -12.085 45.525 1.00 22.95  ? 151 MET A CA  1 
ATOM   1047 C C   . MET A 1 135 ? 35.202  -13.014 45.147 1.00 22.55  ? 151 MET A C   1 
ATOM   1048 O O   . MET A 1 135 ? 35.610  -13.066 43.985 1.00 21.95  ? 151 MET A O   1 
ATOM   1049 C CB  . MET A 1 135 ? 34.409  -10.639 45.185 1.00 23.55  ? 151 MET A CB  1 
ATOM   1050 C CG  . MET A 1 135 ? 33.258  -9.666  45.410 1.00 25.06  ? 151 MET A CG  1 
ATOM   1051 S SD  . MET A 1 135 ? 31.688  -10.192 44.628 1.00 25.40  ? 151 MET A SD  1 
ATOM   1052 C CE  . MET A 1 135 ? 30.655  -8.786  45.067 1.00 24.47  ? 151 MET A CE  1 
ATOM   1053 N N   . ILE A 1 136 ? 35.703  -13.778 46.119 1.00 23.09  ? 152 ILE A N   1 
ATOM   1054 C CA  . ILE A 1 136 ? 36.590  -14.901 45.844 1.00 22.32  ? 152 ILE A CA  1 
ATOM   1055 C C   . ILE A 1 136 ? 35.827  -15.944 45.027 1.00 21.82  ? 152 ILE A C   1 
ATOM   1056 O O   . ILE A 1 136 ? 36.427  -16.642 44.225 1.00 22.90  ? 152 ILE A O   1 
ATOM   1057 C CB  . ILE A 1 136 ? 37.109  -15.489 47.170 1.00 23.34  ? 152 ILE A CB  1 
ATOM   1058 C CG1 . ILE A 1 136 ? 38.034  -14.530 47.944 1.00 24.95  ? 152 ILE A CG1 1 
ATOM   1059 C CG2 . ILE A 1 136 ? 37.757  -16.844 46.957 1.00 23.35  ? 152 ILE A CG2 1 
ATOM   1060 C CD1 . ILE A 1 136 ? 39.337  -14.220 47.272 1.00 23.23  ? 152 ILE A CD1 1 
ATOM   1061 N N   . HIS A 1 137 ? 34.504  -16.048 45.235 1.00 19.98  ? 153 HIS A N   1 
ATOM   1062 C CA  . HIS A 1 137 ? 33.685  -17.012 44.513 1.00 20.44  ? 153 HIS A CA  1 
ATOM   1063 C C   . HIS A 1 137 ? 32.873  -16.376 43.368 1.00 22.16  ? 153 HIS A C   1 
ATOM   1064 O O   . HIS A 1 137 ? 32.584  -15.171 43.344 1.00 21.94  ? 153 HIS A O   1 
ATOM   1065 C CB  . HIS A 1 137 ? 32.638  -17.660 45.430 1.00 19.79  ? 153 HIS A CB  1 
ATOM   1066 C CG  . HIS A 1 137 ? 33.146  -18.598 46.458 1.00 20.82  ? 153 HIS A CG  1 
ATOM   1067 N ND1 . HIS A 1 137 ? 32.899  -19.958 46.401 1.00 21.19  ? 153 HIS A ND1 1 
ATOM   1068 C CD2 . HIS A 1 137 ? 33.895  -18.390 47.559 1.00 22.04  ? 153 HIS A CD2 1 
ATOM   1069 C CE1 . HIS A 1 137 ? 33.447  -20.534 47.469 1.00 21.98  ? 153 HIS A CE1 1 
ATOM   1070 N NE2 . HIS A 1 137 ? 34.066  -19.605 48.180 1.00 21.43  ? 153 HIS A NE2 1 
ATOM   1071 N N   . GLU A 1 138 ? 32.465  -17.233 42.424 1.00 21.38  ? 154 GLU A N   1 
ATOM   1072 C CA  . GLU A 1 138 ? 31.629  -16.809 41.311 1.00 22.03  ? 154 GLU A CA  1 
ATOM   1073 C C   . GLU A 1 138 ? 30.155  -16.894 41.703 1.00 22.53  ? 154 GLU A C   1 
ATOM   1074 O O   . GLU A 1 138 ? 29.693  -17.906 42.241 1.00 21.13  ? 154 GLU A O   1 
ATOM   1075 C CB  . GLU A 1 138 ? 31.921  -17.686 40.090 1.00 22.96  ? 154 GLU A CB  1 
ATOM   1076 C CG  . GLU A 1 138 ? 30.937  -17.472 38.951 1.00 24.81  ? 154 GLU A CG  1 
ATOM   1077 C CD  . GLU A 1 138 ? 31.122  -18.280 37.684 1.00 22.74  ? 154 GLU A CD  1 
ATOM   1078 O OE1 . GLU A 1 138 ? 32.169  -18.894 37.528 1.00 21.93  ? 154 GLU A OE1 1 
ATOM   1079 O OE2 . GLU A 1 138 ? 30.198  -18.294 36.879 1.00 23.82  ? 154 GLU A OE2 1 
ATOM   1080 N N   . HIS A 1 139 ? 29.415  -15.819 41.403 1.00 21.44  ? 155 HIS A N   1 
ATOM   1081 C CA  . HIS A 1 139 ? 27.990  -15.772 41.634 1.00 21.06  ? 155 HIS A CA  1 
ATOM   1082 C C   . HIS A 1 139 ? 27.253  -15.529 40.319 1.00 21.96  ? 155 HIS A C   1 
ATOM   1083 O O   . HIS A 1 139 ? 27.511  -14.535 39.639 1.00 23.55  ? 155 HIS A O   1 
ATOM   1084 C CB  . HIS A 1 139 ? 27.650  -14.672 42.633 1.00 22.57  ? 155 HIS A CB  1 
ATOM   1085 C CG  . HIS A 1 139 ? 28.353  -14.798 43.926 1.00 22.59  ? 155 HIS A CG  1 
ATOM   1086 N ND1 . HIS A 1 139 ? 29.695  -14.516 44.054 1.00 22.94  ? 155 HIS A ND1 1 
ATOM   1087 C CD2 . HIS A 1 139 ? 27.907  -15.149 45.148 1.00 21.81  ? 155 HIS A CD2 1 
ATOM   1088 C CE1 . HIS A 1 139 ? 30.030  -14.702 45.325 1.00 22.13  ? 155 HIS A CE1 1 
ATOM   1089 N NE2 . HIS A 1 139 ? 28.974  -15.101 45.984 1.00 21.85  ? 155 HIS A NE2 1 
ATOM   1090 N N   . GLN A 1 140 ? 26.340  -16.441 39.964 1.00 21.44  ? 156 GLN A N   1 
ATOM   1091 C CA  . GLN A 1 140 ? 25.461  -16.232 38.818 1.00 21.26  ? 156 GLN A CA  1 
ATOM   1092 C C   . GLN A 1 140 ? 24.155  -15.672 39.361 1.00 20.06  ? 156 GLN A C   1 
ATOM   1093 O O   . GLN A 1 140 ? 23.523  -16.330 40.173 1.00 19.79  ? 156 GLN A O   1 
ATOM   1094 C CB  . GLN A 1 140 ? 25.278  -17.519 38.012 1.00 21.02  ? 156 GLN A CB  1 
ATOM   1095 C CG  . GLN A 1 140 ? 26.563  -17.986 37.318 1.00 22.67  ? 156 GLN A CG  1 
ATOM   1096 C CD  . GLN A 1 140 ? 26.571  -19.434 36.860 1.00 24.26  ? 156 GLN A CD  1 
ATOM   1097 O OE1 . GLN A 1 140 ? 25.540  -20.078 36.638 1.00 22.64  ? 156 GLN A OE1 1 
ATOM   1098 N NE2 . GLN A 1 140 ? 27.766  -19.979 36.719 1.00 24.45  ? 156 GLN A NE2 1 
ATOM   1099 N N   . LEU A 1 141 ? 23.816  -14.437 38.962 1.00 19.33  ? 157 LEU A N   1 
ATOM   1100 C CA  . LEU A 1 141 ? 22.788  -13.657 39.644 1.00 19.92  ? 157 LEU A CA  1 
ATOM   1101 C C   . LEU A 1 141 ? 21.475  -13.706 38.857 1.00 21.10  ? 157 LEU A C   1 
ATOM   1102 O O   . LEU A 1 141 ? 20.404  -13.909 39.416 1.00 20.56  ? 157 LEU A O   1 
ATOM   1103 C CB  . LEU A 1 141 ? 23.259  -12.203 39.769 1.00 19.62  ? 157 LEU A CB  1 
ATOM   1104 C CG  . LEU A 1 141 ? 24.465  -11.951 40.684 1.00 20.50  ? 157 LEU A CG  1 
ATOM   1105 C CD1 . LEU A 1 141 ? 24.787  -10.454 40.772 1.00 19.46  ? 157 LEU A CD1 1 
ATOM   1106 C CD2 . LEU A 1 141 ? 24.264  -12.544 42.072 1.00 22.10  ? 157 LEU A CD2 1 
ATOM   1107 N N   . VAL A 1 142 ? 21.572  -13.466 37.552 1.00 22.48  ? 158 VAL A N   1 
ATOM   1108 C CA  . VAL A 1 142 ? 20.406  -13.319 36.696 1.00 22.80  ? 158 VAL A CA  1 
ATOM   1109 C C   . VAL A 1 142 ? 20.737  -14.032 35.389 1.00 22.44  ? 158 VAL A C   1 
ATOM   1110 O O   . VAL A 1 142 ? 21.828  -13.847 34.853 1.00 24.56  ? 158 VAL A O   1 
ATOM   1111 C CB  . VAL A 1 142 ? 20.036  -11.836 36.449 1.00 22.61  ? 158 VAL A CB  1 
ATOM   1112 C CG1 . VAL A 1 142 ? 18.865  -11.676 35.489 1.00 23.02  ? 158 VAL A CG1 1 
ATOM   1113 C CG2 . VAL A 1 142 ? 19.705  -11.116 37.734 1.00 24.20  ? 158 VAL A CG2 1 
ATOM   1114 N N   . PHE A 1 143 ? 19.789  -14.830 34.876 1.00 21.24  ? 159 PHE A N   1 
ATOM   1115 C CA  . PHE A 1 143 ? 19.999  -15.567 33.646 1.00 22.91  ? 159 PHE A CA  1 
ATOM   1116 C C   . PHE A 1 143 ? 18.675  -16.137 33.110 1.00 26.22  ? 159 PHE A C   1 
ATOM   1117 O O   . PHE A 1 143 ? 17.700  -16.218 33.837 1.00 22.50  ? 159 PHE A O   1 
ATOM   1118 C CB  . PHE A 1 143 ? 21.037  -16.678 33.865 1.00 22.42  ? 159 PHE A CB  1 
ATOM   1119 C CG  . PHE A 1 143 ? 20.873  -17.531 35.105 1.00 21.33  ? 159 PHE A CG  1 
ATOM   1120 C CD1 . PHE A 1 143 ? 20.029  -18.632 35.111 1.00 25.10  ? 159 PHE A CD1 1 
ATOM   1121 C CD2 . PHE A 1 143 ? 21.562  -17.237 36.270 1.00 22.71  ? 159 PHE A CD2 1 
ATOM   1122 C CE1 . PHE A 1 143 ? 19.877  -19.414 36.246 1.00 23.88  ? 159 PHE A CE1 1 
ATOM   1123 C CE2 . PHE A 1 143 ? 21.402  -18.010 37.408 1.00 23.77  ? 159 PHE A CE2 1 
ATOM   1124 C CZ  . PHE A 1 143 ? 20.561  -19.101 37.391 1.00 24.06  ? 159 PHE A CZ  1 
ATOM   1125 N N   . VAL A 1 144 ? 18.658  -16.465 31.805 1.00 26.81  ? 160 VAL A N   1 
ATOM   1126 C CA  . VAL A 1 144 ? 17.605  -17.238 31.167 1.00 24.45  ? 160 VAL A CA  1 
ATOM   1127 C C   . VAL A 1 144 ? 18.218  -18.595 30.867 1.00 24.01  ? 160 VAL A C   1 
ATOM   1128 O O   . VAL A 1 144 ? 19.270  -18.656 30.245 1.00 23.66  ? 160 VAL A O   1 
ATOM   1129 C CB  . VAL A 1 144 ? 17.062  -16.537 29.907 1.00 25.30  ? 160 VAL A CB  1 
ATOM   1130 C CG1 . VAL A 1 144 ? 16.260  -17.458 28.992 1.00 24.08  ? 160 VAL A CG1 1 
ATOM   1131 C CG2 . VAL A 1 144 ? 16.243  -15.315 30.296 1.00 26.05  ? 160 VAL A CG2 1 
ATOM   1132 N N   . GLU A 1 145 ? 17.604  -19.647 31.425 1.00 25.87  ? 161 GLU A N   1 
ATOM   1133 C CA  . GLU A 1 145 ? 18.154  -20.991 31.410 1.00 27.47  ? 161 GLU A CA  1 
ATOM   1134 C C   . GLU A 1 145 ? 17.281  -21.926 30.573 1.00 27.22  ? 161 GLU A C   1 
ATOM   1135 O O   . GLU A 1 145 ? 16.244  -22.396 31.046 1.00 28.68  ? 161 GLU A O   1 
ATOM   1136 C CB  . GLU A 1 145 ? 18.207  -21.551 32.833 1.00 26.72  ? 161 GLU A CB  1 
ATOM   1137 C CG  . GLU A 1 145 ? 19.013  -22.837 32.966 1.00 29.76  ? 161 GLU A CG  1 
ATOM   1138 C CD  . GLU A 1 145 ? 19.064  -23.375 34.384 1.00 32.09  ? 161 GLU A CD  1 
ATOM   1139 O OE1 . GLU A 1 145 ? 19.385  -22.603 35.282 1.00 44.01  ? 161 GLU A OE1 1 
ATOM   1140 O OE2 . GLU A 1 145 ? 18.805  -24.548 34.579 1.00 38.22  ? 161 GLU A OE2 1 
ATOM   1141 N N   . PRO A 1 146 ? 17.706  -22.284 29.342 1.00 28.80  ? 162 PRO A N   1 
ATOM   1142 C CA  . PRO A 1 146 ? 17.044  -23.349 28.580 1.00 30.14  ? 162 PRO A CA  1 
ATOM   1143 C C   . PRO A 1 146 ? 17.129  -24.693 29.307 1.00 34.05  ? 162 PRO A C   1 
ATOM   1144 O O   . PRO A 1 146 ? 17.778  -24.785 30.351 1.00 29.53  ? 162 PRO A O   1 
ATOM   1145 C CB  . PRO A 1 146 ? 17.819  -23.401 27.259 1.00 28.88  ? 162 PRO A CB  1 
ATOM   1146 C CG  . PRO A 1 146 ? 18.503  -22.048 27.164 1.00 30.57  ? 162 PRO A CG  1 
ATOM   1147 C CD  . PRO A 1 146 ? 18.833  -21.693 28.605 1.00 28.34  ? 162 PRO A CD  1 
ATOM   1148 N N   . SER A 1 147 ? 16.423  -25.698 28.756 1.00 33.29  ? 163 SER A N   1 
ATOM   1149 C CA  . SER A 1 147 ? 16.435  -27.094 29.205 1.00 34.23  ? 163 SER A CA  1 
ATOM   1150 C C   . SER A 1 147 ? 17.820  -27.626 29.552 1.00 29.74  ? 163 SER A C   1 
ATOM   1151 O O   . SER A 1 147 ? 17.941  -28.386 30.508 1.00 29.08  ? 163 SER A O   1 
ATOM   1152 C CB  . SER A 1 147 ? 15.857  -28.004 28.135 1.00 35.15  ? 163 SER A CB  1 
ATOM   1153 O OG  . SER A 1 147 ? 14.460  -27.846 28.087 1.00 42.49  ? 163 SER A OG  1 
ATOM   1154 N N   . ASP A 1 148 ? 18.828  -27.283 28.743 1.00 27.14  ? 164 ASP A N   1 
ATOM   1155 C CA  . ASP A 1 148 ? 20.142  -27.896 28.861 1.00 28.55  ? 164 ASP A CA  1 
ATOM   1156 C C   . ASP A 1 148 ? 20.996  -27.268 29.964 1.00 29.22  ? 164 ASP A C   1 
ATOM   1157 O O   . ASP A 1 148 ? 22.140  -27.662 30.104 1.00 28.62  ? 164 ASP A O   1 
ATOM   1158 C CB  . ASP A 1 148 ? 20.904  -27.847 27.539 1.00 28.10  ? 164 ASP A CB  1 
ATOM   1159 C CG  . ASP A 1 148 ? 21.211  -26.445 27.028 1.00 34.30  ? 164 ASP A CG  1 
ATOM   1160 O OD1 . ASP A 1 148 ? 20.896  -25.463 27.750 1.00 31.06  ? 164 ASP A OD1 1 
ATOM   1161 O OD2 . ASP A 1 148 ? 21.762  -26.344 25.904 1.00 34.00  ? 164 ASP A OD2 1 
ATOM   1162 N N   . GLY A 1 149 ? 20.477  -26.299 30.733 1.00 29.49  ? 165 GLY A N   1 
ATOM   1163 C CA  . GLY A 1 149 ? 21.225  -25.746 31.852 1.00 29.40  ? 165 GLY A CA  1 
ATOM   1164 C C   . GLY A 1 149 ? 22.157  -24.595 31.462 1.00 28.27  ? 165 GLY A C   1 
ATOM   1165 O O   . GLY A 1 149 ? 22.750  -23.970 32.331 1.00 28.71  ? 165 GLY A O   1 
ATOM   1166 N N   . SER A 1 150 ? 22.274  -24.288 30.171 1.00 26.66  ? 166 SER A N   1 
ATOM   1167 C CA  . SER A 1 150 ? 23.087  -23.167 29.711 1.00 27.15  ? 166 SER A CA  1 
ATOM   1168 C C   . SER A 1 150 ? 22.392  -21.843 30.068 1.00 24.09  ? 166 SER A C   1 
ATOM   1169 O O   . SER A 1 150 ? 21.272  -21.854 30.575 1.00 23.15  ? 166 SER A O   1 
ATOM   1170 C CB  . SER A 1 150 ? 23.334  -23.294 28.208 1.00 26.00  ? 166 SER A CB  1 
ATOM   1171 O OG  . SER A 1 150 ? 22.105  -23.093 27.512 1.00 26.95  ? 166 SER A OG  1 
ATOM   1172 N N   . HIS A 1 151 ? 23.053  -20.699 29.815 1.00 23.53  ? 167 HIS A N   1 
ATOM   1173 C CA  . HIS A 1 151 ? 22.440  -19.399 30.067 1.00 25.09  ? 167 HIS A CA  1 
ATOM   1174 C C   . HIS A 1 151 ? 22.537  -18.502 28.826 1.00 23.62  ? 167 HIS A C   1 
ATOM   1175 O O   . HIS A 1 151 ? 23.623  -18.158 28.383 1.00 24.08  ? 167 HIS A O   1 
ATOM   1176 C CB  . HIS A 1 151 ? 23.090  -18.706 31.271 1.00 24.05  ? 167 HIS A CB  1 
ATOM   1177 C CG  . HIS A 1 151 ? 22.954  -19.389 32.566 1.00 21.77  ? 167 HIS A CG  1 
ATOM   1178 N ND1 . HIS A 1 151 ? 23.752  -19.021 33.623 1.00 24.38  ? 167 HIS A ND1 1 
ATOM   1179 C CD2 . HIS A 1 151 ? 22.195  -20.376 33.006 1.00 22.16  ? 167 HIS A CD2 1 
ATOM   1180 C CE1 . HIS A 1 151 ? 23.430  -19.750 34.683 1.00 21.56  ? 167 HIS A CE1 1 
ATOM   1181 N NE2 . HIS A 1 151 ? 22.507  -20.596 34.319 1.00 23.51  ? 167 HIS A NE2 1 
ATOM   1182 N N   . VAL A 1 152 ? 21.390  -18.054 28.313 1.00 24.07  ? 168 VAL A N   1 
ATOM   1183 C CA  . VAL A 1 152 ? 21.369  -17.241 27.108 1.00 25.75  ? 168 VAL A CA  1 
ATOM   1184 C C   . VAL A 1 152 ? 22.177  -15.963 27.358 1.00 24.42  ? 168 VAL A C   1 
ATOM   1185 O O   . VAL A 1 152 ? 22.893  -15.514 26.482 1.00 24.88  ? 168 VAL A O   1 
ATOM   1186 C CB  . VAL A 1 152 ? 19.916  -16.969 26.677 1.00 25.44  ? 168 VAL A CB  1 
ATOM   1187 C CG1 . VAL A 1 152 ? 19.815  -16.093 25.439 1.00 27.23  ? 168 VAL A CG1 1 
ATOM   1188 C CG2 . VAL A 1 152 ? 19.202  -18.290 26.438 1.00 27.31  ? 168 VAL A CG2 1 
ATOM   1189 N N   . PHE A 1 153 ? 22.015  -15.384 28.554 1.00 26.56  ? 169 PHE A N   1 
ATOM   1190 C CA  . PHE A 1 153 ? 22.886  -14.354 29.099 1.00 25.34  ? 169 PHE A CA  1 
ATOM   1191 C C   . PHE A 1 153 ? 22.919  -14.531 30.617 1.00 23.61  ? 169 PHE A C   1 
ATOM   1192 O O   . PHE A 1 153 ? 22.074  -15.220 31.189 1.00 23.41  ? 169 PHE A O   1 
ATOM   1193 C CB  . PHE A 1 153 ? 22.425  -12.954 28.699 1.00 22.81  ? 169 PHE A CB  1 
ATOM   1194 C CG  . PHE A 1 153 ? 21.142  -12.555 29.364 1.00 23.17  ? 169 PHE A CG  1 
ATOM   1195 C CD1 . PHE A 1 153 ? 21.138  -12.074 30.667 1.00 22.66  ? 169 PHE A CD1 1 
ATOM   1196 C CD2 . PHE A 1 153 ? 19.924  -12.785 28.734 1.00 23.97  ? 169 PHE A CD2 1 
ATOM   1197 C CE1 . PHE A 1 153 ? 19.942  -11.753 31.296 1.00 24.40  ? 169 PHE A CE1 1 
ATOM   1198 C CE2 . PHE A 1 153 ? 18.730  -12.495 29.380 1.00 24.12  ? 169 PHE A CE2 1 
ATOM   1199 C CZ  . PHE A 1 153 ? 18.742  -11.966 30.648 1.00 24.58  ? 169 PHE A CZ  1 
ATOM   1200 N N   . THR A 1 154 ? 23.932  -13.943 31.258 1.00 20.66  ? 170 THR A N   1 
ATOM   1201 C CA  . THR A 1 154 ? 24.088  -14.041 32.692 1.00 20.77  ? 170 THR A CA  1 
ATOM   1202 C C   . THR A 1 154 ? 24.490  -12.670 33.233 1.00 21.27  ? 170 THR A C   1 
ATOM   1203 O O   . THR A 1 154 ? 25.304  -11.987 32.625 1.00 19.41  ? 170 THR A O   1 
ATOM   1204 C CB  . THR A 1 154 ? 25.173  -15.063 33.071 1.00 23.29  ? 170 THR A CB  1 
ATOM   1205 O OG1 . THR A 1 154 ? 24.984  -16.303 32.390 1.00 22.38  ? 170 THR A OG1 1 
ATOM   1206 C CG2 . THR A 1 154 ? 25.244  -15.340 34.561 1.00 24.40  ? 170 THR A CG2 1 
ATOM   1207 N N   . LEU A 1 155 ? 23.957  -12.289 34.392 1.00 20.68  ? 171 LEU A N   1 
ATOM   1208 C CA  . LEU A 1 155 ? 24.638  -11.293 35.209 1.00 21.96  ? 171 LEU A CA  1 
ATOM   1209 C C   . LEU A 1 155 ? 25.476  -12.069 36.222 1.00 20.70  ? 171 LEU A C   1 
ATOM   1210 O O   . LEU A 1 155 ? 24.913  -12.861 36.936 1.00 20.50  ? 171 LEU A O   1 
ATOM   1211 C CB  . LEU A 1 155 ? 23.599  -10.403 35.901 1.00 23.33  ? 171 LEU A CB  1 
ATOM   1212 C CG  . LEU A 1 155 ? 24.165  -9.360  36.866 1.00 23.41  ? 171 LEU A CG  1 
ATOM   1213 C CD1 . LEU A 1 155 ? 24.838  -8.238  36.113 1.00 22.84  ? 171 LEU A CD1 1 
ATOM   1214 C CD2 . LEU A 1 155 ? 23.089  -8.786  37.796 1.00 23.78  ? 171 LEU A CD2 1 
ATOM   1215 N N   . GLN A 1 156 ? 26.787  -11.831 36.272 1.00 21.33  ? 172 GLN A N   1 
ATOM   1216 C CA  . GLN A 1 156 ? 27.731  -12.509 37.152 1.00 19.68  ? 172 GLN A CA  1 
ATOM   1217 C C   . GLN A 1 156 ? 28.471  -11.472 37.998 1.00 21.33  ? 172 GLN A C   1 
ATOM   1218 O O   . GLN A 1 156 ? 28.684  -10.345 37.560 1.00 21.85  ? 172 GLN A O   1 
ATOM   1219 C CB  . GLN A 1 156 ? 28.736  -13.265 36.291 1.00 20.22  ? 172 GLN A CB  1 
ATOM   1220 C CG  . GLN A 1 156 ? 29.797  -14.077 37.029 1.00 21.57  ? 172 GLN A CG  1 
ATOM   1221 C CD  . GLN A 1 156 ? 30.895  -14.459 36.063 1.00 22.07  ? 172 GLN A CD  1 
ATOM   1222 O OE1 . GLN A 1 156 ? 31.650  -13.613 35.619 1.00 22.87  ? 172 GLN A OE1 1 
ATOM   1223 N NE2 . GLN A 1 156 ? 30.978  -15.726 35.707 1.00 27.25  ? 172 GLN A NE2 1 
ATOM   1224 N N   . VAL A 1 157 ? 28.836  -11.846 39.231 1.00 22.83  ? 173 VAL A N   1 
ATOM   1225 C CA  . VAL A 1 157 ? 29.778  -11.067 40.024 1.00 22.76  ? 173 VAL A CA  1 
ATOM   1226 C C   . VAL A 1 157 ? 30.659  -12.034 40.816 1.00 23.96  ? 173 VAL A C   1 
ATOM   1227 O O   . VAL A 1 157 ? 30.264  -13.164 41.097 1.00 20.68  ? 173 VAL A O   1 
ATOM   1228 C CB  . VAL A 1 157 ? 29.068  -10.045 40.933 1.00 22.80  ? 173 VAL A CB  1 
ATOM   1229 C CG1 . VAL A 1 157 ? 28.386  -10.705 42.124 1.00 21.81  ? 173 VAL A CG1 1 
ATOM   1230 C CG2 . VAL A 1 157 ? 30.029  -8.935  41.400 1.00 23.76  ? 173 VAL A CG2 1 
ATOM   1231 N N   . GLY A 1 158 ? 31.881  -11.589 41.122 1.00 22.60  ? 174 GLY A N   1 
ATOM   1232 C CA  . GLY A 1 158 ? 32.876  -12.451 41.741 1.00 22.99  ? 174 GLY A CA  1 
ATOM   1233 C C   . GLY A 1 158 ? 33.825  -13.104 40.738 1.00 22.59  ? 174 GLY A C   1 
ATOM   1234 O O   . GLY A 1 158 ? 33.590  -13.122 39.533 1.00 21.81  ? 174 GLY A O   1 
ATOM   1235 N N   . SER A 1 159 ? 34.910  -13.670 41.276 1.00 25.53  ? 175 SER A N   1 
ATOM   1236 C CA  . SER A 1 159 ? 35.946  -14.316 40.484 1.00 23.76  ? 175 SER A CA  1 
ATOM   1237 C C   . SER A 1 159 ? 35.374  -15.556 39.809 1.00 24.05  ? 175 SER A C   1 
ATOM   1238 O O   . SER A 1 159 ? 34.926  -16.467 40.503 1.00 24.21  ? 175 SER A O   1 
ATOM   1239 C CB  . SER A 1 159 ? 37.119  -14.685 41.370 1.00 22.89  ? 175 SER A CB  1 
ATOM   1240 O OG  . SER A 1 159 ? 37.609  -13.560 42.108 1.00 22.75  ? 175 SER A OG  1 
ATOM   1241 N N   . PRO A 1 160 ? 35.391  -15.669 38.464 1.00 22.35  ? 176 PRO A N   1 
ATOM   1242 C CA  . PRO A 1 160 ? 35.006  -16.910 37.798 1.00 22.93  ? 176 PRO A CA  1 
ATOM   1243 C C   . PRO A 1 160 ? 35.700  -18.152 38.367 1.00 25.43  ? 176 PRO A C   1 
ATOM   1244 O O   . PRO A 1 160 ? 36.907  -18.131 38.669 1.00 25.64  ? 176 PRO A O   1 
ATOM   1245 C CB  . PRO A 1 160 ? 35.431  -16.702 36.328 1.00 22.16  ? 176 PRO A CB  1 
ATOM   1246 C CG  . PRO A 1 160 ? 35.354  -15.192 36.141 1.00 22.67  ? 176 PRO A CG  1 
ATOM   1247 C CD  . PRO A 1 160 ? 35.710  -14.604 37.499 1.00 24.22  ? 176 PRO A CD  1 
ATOM   1248 N N   . PHE A 1 161 ? 34.908  -19.227 38.487 1.00 24.72  ? 177 PHE A N   1 
ATOM   1249 C CA  . PHE A 1 161 ? 35.393  -20.519 38.931 1.00 24.43  ? 177 PHE A CA  1 
ATOM   1250 C C   . PHE A 1 161 ? 36.401  -21.024 37.924 1.00 27.12  ? 177 PHE A C   1 
ATOM   1251 O O   . PHE A 1 161 ? 36.113  -20.992 36.742 1.00 27.09  ? 177 PHE A O   1 
ATOM   1252 C CB  . PHE A 1 161 ? 34.271  -21.555 38.999 1.00 25.49  ? 177 PHE A CB  1 
ATOM   1253 C CG  . PHE A 1 161 ? 34.765  -22.968 39.215 1.00 26.29  ? 177 PHE A CG  1 
ATOM   1254 C CD1 . PHE A 1 161 ? 35.039  -23.433 40.494 1.00 27.07  ? 177 PHE A CD1 1 
ATOM   1255 C CD2 . PHE A 1 161 ? 35.007  -23.810 38.138 1.00 26.41  ? 177 PHE A CD2 1 
ATOM   1256 C CE1 . PHE A 1 161 ? 35.477  -24.732 40.697 1.00 26.48  ? 177 PHE A CE1 1 
ATOM   1257 C CE2 . PHE A 1 161 ? 35.472  -25.102 38.335 1.00 26.72  ? 177 PHE A CE2 1 
ATOM   1258 C CZ  . PHE A 1 161 ? 35.720  -25.554 39.614 1.00 27.60  ? 177 PHE A CZ  1 
ATOM   1259 N N   . THR A 1 162 ? 37.561  -21.502 38.385 1.00 29.62  ? 178 THR A N   1 
ATOM   1260 C CA  . THR A 1 162 ? 38.469  -22.233 37.510 1.00 29.13  ? 178 THR A CA  1 
ATOM   1261 C C   . THR A 1 162 ? 39.021  -23.454 38.241 1.00 30.00  ? 178 THR A C   1 
ATOM   1262 O O   . THR A 1 162 ? 39.214  -23.442 39.472 1.00 26.39  ? 178 THR A O   1 
ATOM   1263 C CB  . THR A 1 162 ? 39.632  -21.383 36.985 1.00 32.53  ? 178 THR A CB  1 
ATOM   1264 O OG1 . THR A 1 162 ? 40.582  -21.122 38.022 1.00 34.88  ? 178 THR A OG1 1 
ATOM   1265 C CG2 . THR A 1 162 ? 39.163  -20.067 36.402 1.00 34.48  ? 178 THR A CG2 1 
ATOM   1266 N N   . ASN A 1 163 ? 39.250  -24.497 37.439 1.00 27.47  ? 179 ASN A N   1 
ATOM   1267 C CA  . ASN A 1 163 ? 39.936  -25.693 37.886 1.00 31.41  ? 179 ASN A CA  1 
ATOM   1268 C C   . ASN A 1 163 ? 41.128  -25.938 36.971 1.00 31.96  ? 179 ASN A C   1 
ATOM   1269 O O   . ASN A 1 163 ? 40.920  -26.272 35.818 1.00 30.89  ? 179 ASN A O   1 
ATOM   1270 C CB  . ASN A 1 163 ? 39.041  -26.927 37.879 1.00 29.62  ? 179 ASN A CB  1 
ATOM   1271 C CG  . ASN A 1 163 ? 39.799  -28.173 38.297 1.00 30.34  ? 179 ASN A CG  1 
ATOM   1272 O OD1 . ASN A 1 163 ? 40.727  -28.098 39.093 1.00 31.54  ? 179 ASN A OD1 1 
ATOM   1273 N ND2 . ASN A 1 163 ? 39.461  -29.314 37.726 1.00 30.48  ? 179 ASN A ND2 1 
ATOM   1274 N N   . PRO A 1 164 ? 42.394  -25.842 37.435 1.00 32.66  ? 180 PRO A N   1 
ATOM   1275 C CA  . PRO A 1 164 ? 42.727  -25.498 38.817 1.00 32.28  ? 180 PRO A CA  1 
ATOM   1276 C C   . PRO A 1 164 ? 42.432  -24.066 39.260 1.00 32.48  ? 180 PRO A C   1 
ATOM   1277 O O   . PRO A 1 164 ? 42.204  -23.175 38.443 1.00 34.99  ? 180 PRO A O   1 
ATOM   1278 C CB  . PRO A 1 164 ? 44.255  -25.740 38.891 1.00 32.60  ? 180 PRO A CB  1 
ATOM   1279 C CG  . PRO A 1 164 ? 44.748  -25.628 37.459 1.00 32.95  ? 180 PRO A CG  1 
ATOM   1280 C CD  . PRO A 1 164 ? 43.596  -26.148 36.628 1.00 31.39  ? 180 PRO A CD  1 
ATOM   1281 N N   . THR A 1 165 ? 42.485  -23.864 40.578 1.00 29.15  ? 181 THR A N   1 
ATOM   1282 C CA  . THR A 1 165 ? 42.348  -22.552 41.165 1.00 33.32  ? 181 THR A CA  1 
ATOM   1283 C C   . THR A 1 165 ? 43.481  -21.645 40.682 1.00 37.46  ? 181 THR A C   1 
ATOM   1284 O O   . THR A 1 165 ? 44.626  -22.085 40.583 1.00 31.56  ? 181 THR A O   1 
ATOM   1285 C CB  . THR A 1 165 ? 42.329  -22.650 42.690 1.00 31.38  ? 181 THR A CB  1 
ATOM   1286 O OG1 . THR A 1 165 ? 41.264  -23.546 43.018 1.00 28.49  ? 181 THR A OG1 1 
ATOM   1287 C CG2 . THR A 1 165 ? 42.144  -21.299 43.347 1.00 31.45  ? 181 THR A CG2 1 
ATOM   1288 N N   . GLY A 1 166 ? 43.144  -20.379 40.375 1.00 33.78  ? 182 GLY A N   1 
ATOM   1289 C CA  . GLY A 1 166 ? 44.131  -19.391 39.963 1.00 33.14  ? 182 GLY A CA  1 
ATOM   1290 C C   . GLY A 1 166 ? 44.237  -18.272 40.993 1.00 33.28  ? 182 GLY A C   1 
ATOM   1291 O O   . GLY A 1 166 ? 43.688  -18.364 42.083 1.00 33.58  ? 182 GLY A O   1 
ATOM   1292 N N   . PRO A 1 167 ? 44.947  -17.169 40.688 1.00 36.95  ? 183 PRO A N   1 
ATOM   1293 C CA  . PRO A 1 167 ? 44.999  -16.036 41.609 1.00 36.37  ? 183 PRO A CA  1 
ATOM   1294 C C   . PRO A 1 167 ? 43.598  -15.526 41.951 1.00 34.94  ? 183 PRO A C   1 
ATOM   1295 O O   . PRO A 1 167 ? 42.748  -15.387 41.076 1.00 38.29  ? 183 PRO A O   1 
ATOM   1296 C CB  . PRO A 1 167 ? 45.815  -14.981 40.838 1.00 39.04  ? 183 PRO A CB  1 
ATOM   1297 C CG  . PRO A 1 167 ? 46.623  -15.791 39.833 1.00 37.97  ? 183 PRO A CG  1 
ATOM   1298 C CD  . PRO A 1 167 ? 45.738  -16.966 39.466 1.00 36.04  ? 183 PRO A CD  1 
ATOM   1299 N N   . LEU A 1 168 ? 43.366  -15.283 43.236 1.00 28.70  ? 184 LEU A N   1 
ATOM   1300 C CA  . LEU A 1 168 ? 42.079  -14.813 43.713 1.00 30.60  ? 184 LEU A CA  1 
ATOM   1301 C C   . LEU A 1 168 ? 42.328  -13.725 44.749 1.00 33.30  ? 184 LEU A C   1 
ATOM   1302 O O   . LEU A 1 168 ? 43.210  -13.862 45.594 1.00 39.15  ? 184 LEU A O   1 
ATOM   1303 C CB  . LEU A 1 168 ? 41.289  -15.975 44.334 1.00 30.28  ? 184 LEU A CB  1 
ATOM   1304 C CG  . LEU A 1 168 ? 40.795  -17.066 43.371 1.00 27.99  ? 184 LEU A CG  1 
ATOM   1305 C CD1 . LEU A 1 168 ? 40.279  -18.261 44.156 1.00 29.64  ? 184 LEU A CD1 1 
ATOM   1306 C CD2 . LEU A 1 168 ? 39.710  -16.548 42.436 1.00 26.26  ? 184 LEU A CD2 1 
ATOM   1307 N N   . PRO A 1 169 ? 41.527  -12.647 44.769 1.00 29.87  ? 185 PRO A N   1 
ATOM   1308 C CA  . PRO A 1 169 ? 40.442  -12.482 43.800 1.00 27.49  ? 185 PRO A CA  1 
ATOM   1309 C C   . PRO A 1 169 ? 40.968  -12.191 42.404 1.00 30.62  ? 185 PRO A C   1 
ATOM   1310 O O   . PRO A 1 169 ? 42.078  -11.697 42.257 1.00 33.63  ? 185 PRO A O   1 
ATOM   1311 C CB  . PRO A 1 169 ? 39.686  -11.262 44.343 1.00 29.39  ? 185 PRO A CB  1 
ATOM   1312 C CG  . PRO A 1 169 ? 40.748  -10.478 45.127 1.00 30.47  ? 185 PRO A CG  1 
ATOM   1313 C CD  . PRO A 1 169 ? 41.609  -11.557 45.762 1.00 30.60  ? 185 PRO A CD  1 
ATOM   1314 N N   . ALA A 1 170 ? 40.177  -12.518 41.381 1.00 31.49  ? 186 ALA A N   1 
ATOM   1315 C CA  . ALA A 1 170 ? 40.475  -12.144 40.011 1.00 29.22  ? 186 ALA A CA  1 
ATOM   1316 C C   . ALA A 1 170 ? 40.439  -10.623 39.870 1.00 30.69  ? 186 ALA A C   1 
ATOM   1317 O O   . ALA A 1 170 ? 39.773  -9.944  40.641 1.00 27.30  ? 186 ALA A O   1 
ATOM   1318 C CB  . ALA A 1 170 ? 39.465  -12.775 39.074 1.00 31.01  ? 186 ALA A CB  1 
ATOM   1319 N N   . PRO A 1 171 ? 41.108  -10.044 38.851 1.00 30.53  ? 187 PRO A N   1 
ATOM   1320 C CA  . PRO A 1 171 ? 40.941  -8.623  38.548 1.00 30.75  ? 187 PRO A CA  1 
ATOM   1321 C C   . PRO A 1 171 ? 39.460  -8.315  38.322 1.00 28.55  ? 187 PRO A C   1 
ATOM   1322 O O   . PRO A 1 171 ? 38.799  -9.039  37.588 1.00 27.04  ? 187 PRO A O   1 
ATOM   1323 C CB  . PRO A 1 171 ? 41.721  -8.423  37.230 1.00 33.57  ? 187 PRO A CB  1 
ATOM   1324 C CG  . PRO A 1 171 ? 42.688  -9.609  37.139 1.00 33.09  ? 187 PRO A CG  1 
ATOM   1325 C CD  . PRO A 1 171 ? 42.047  -10.727 37.941 1.00 32.48  ? 187 PRO A CD  1 
ATOM   1326 N N   . ARG A 1 172 ? 38.950  -7.239  38.929 1.00 28.57  ? 188 ARG A N   1 
ATOM   1327 C CA  . ARG A 1 172 ? 37.584  -6.787  38.688 1.00 28.91  ? 188 ARG A CA  1 
ATOM   1328 C C   . ARG A 1 172 ? 36.576  -7.841  39.147 1.00 28.14  ? 188 ARG A C   1 
ATOM   1329 O O   . ARG A 1 172 ? 35.446  -7.881  38.632 1.00 23.80  ? 188 ARG A O   1 
ATOM   1330 C CB  . ARG A 1 172 ? 37.349  -6.484  37.200 1.00 30.08  ? 188 ARG A CB  1 
ATOM   1331 C CG  . ARG A 1 172 ? 38.114  -5.277  36.671 1.00 32.71  ? 188 ARG A CG  1 
ATOM   1332 C CD  . ARG A 1 172 ? 37.849  -4.960  35.209 1.00 38.09  ? 188 ARG A CD  1 
ATOM   1333 N NE  . ARG A 1 172 ? 38.409  -3.641  34.906 1.00 47.30  ? 188 ARG A NE  1 
ATOM   1334 C CZ  . ARG A 1 172 ? 38.178  -2.927  33.801 1.00 48.70  ? 188 ARG A CZ  1 
ATOM   1335 N NH1 . ARG A 1 172 ? 37.413  -3.402  32.835 1.00 47.45  ? 188 ARG A NH1 1 
ATOM   1336 N NH2 . ARG A 1 172 ? 38.713  -1.722  33.670 1.00 51.07  ? 188 ARG A NH2 1 
ATOM   1337 N N   . ALA A 1 173 ? 36.969  -8.647  40.151 1.00 26.52  ? 189 ALA A N   1 
ATOM   1338 C CA  . ALA A 1 173 ? 36.076  -9.610  40.787 1.00 26.19  ? 189 ALA A CA  1 
ATOM   1339 C C   . ALA A 1 173 ? 34.806  -8.931  41.281 1.00 24.59  ? 189 ALA A C   1 
ATOM   1340 O O   . ALA A 1 173 ? 33.728  -9.510  41.209 1.00 22.32  ? 189 ALA A O   1 
ATOM   1341 C CB  . ALA A 1 173 ? 36.765  -10.292 41.944 1.00 30.39  ? 189 ALA A CB  1 
ATOM   1342 N N   . ASP A 1 174 ? 34.928  -7.697  41.773 1.00 22.90  ? 190 ASP A N   1 
ATOM   1343 C CA  . ASP A 1 174 ? 33.767  -7.004  42.285 1.00 26.68  ? 190 ASP A CA  1 
ATOM   1344 C C   . ASP A 1 174 ? 33.113  -6.142  41.206 1.00 24.68  ? 190 ASP A C   1 
ATOM   1345 O O   . ASP A 1 174 ? 32.366  -5.246  41.574 1.00 25.30  ? 190 ASP A O   1 
ATOM   1346 C CB  . ASP A 1 174 ? 34.126  -6.203  43.538 1.00 29.84  ? 190 ASP A CB  1 
ATOM   1347 C CG  . ASP A 1 174 ? 35.209  -5.177  43.309 1.00 30.63  ? 190 ASP A CG  1 
ATOM   1348 O OD1 . ASP A 1 174 ? 35.777  -5.163  42.195 1.00 30.67  ? 190 ASP A OD1 1 
ATOM   1349 O OD2 . ASP A 1 174 ? 35.464  -4.404  44.243 1.00 35.50  ? 190 ASP A OD2 1 
ATOM   1350 N N   . TRP A 1 175 ? 33.357  -6.437  39.912 1.00 23.07  ? 191 TRP A N   1 
ATOM   1351 C CA  . TRP A 1 175 ? 32.572  -5.871  38.827 1.00 23.59  ? 191 TRP A CA  1 
ATOM   1352 C C   . TRP A 1 175 ? 31.411  -6.786  38.437 1.00 22.56  ? 191 TRP A C   1 
ATOM   1353 O O   . TRP A 1 175 ? 31.588  -7.980  38.180 1.00 21.23  ? 191 TRP A O   1 
ATOM   1354 C CB  . TRP A 1 175 ? 33.441  -5.541  37.610 1.00 25.24  ? 191 TRP A CB  1 
ATOM   1355 C CG  . TRP A 1 175 ? 34.342  -4.346  37.827 1.00 24.57  ? 191 TRP A CG  1 
ATOM   1356 C CD1 . TRP A 1 175 ? 34.991  -4.014  38.981 1.00 26.59  ? 191 TRP A CD1 1 
ATOM   1357 C CD2 . TRP A 1 175 ? 34.711  -3.336  36.858 1.00 28.12  ? 191 TRP A CD2 1 
ATOM   1358 N NE1 . TRP A 1 175 ? 35.726  -2.870  38.800 1.00 29.16  ? 191 TRP A NE1 1 
ATOM   1359 C CE2 . TRP A 1 175 ? 35.579  -2.428  37.513 1.00 28.92  ? 191 TRP A CE2 1 
ATOM   1360 C CE3 . TRP A 1 175 ? 34.398  -3.109  35.510 1.00 27.89  ? 191 TRP A CE3 1 
ATOM   1361 C CZ2 . TRP A 1 175 ? 36.122  -1.309  36.874 1.00 28.88  ? 191 TRP A CZ2 1 
ATOM   1362 C CZ3 . TRP A 1 175 ? 34.939  -2.006  34.872 1.00 28.46  ? 191 TRP A CZ3 1 
ATOM   1363 C CH2 . TRP A 1 175 ? 35.780  -1.113  35.551 1.00 30.69  ? 191 TRP A CH2 1 
ATOM   1364 N N   . LEU A 1 176 ? 30.208  -6.196  38.398 1.00 22.15  ? 192 LEU A N   1 
ATOM   1365 C CA  . LEU A 1 176 ? 29.059  -6.808  37.742 1.00 21.30  ? 192 LEU A CA  1 
ATOM   1366 C C   . LEU A 1 176 ? 29.400  -6.961  36.263 1.00 22.56  ? 192 LEU A C   1 
ATOM   1367 O O   . LEU A 1 176 ? 29.962  -6.028  35.644 1.00 22.73  ? 192 LEU A O   1 
ATOM   1368 C CB  . LEU A 1 176 ? 27.804  -5.932  37.898 1.00 22.19  ? 192 LEU A CB  1 
ATOM   1369 C CG  . LEU A 1 176 ? 27.312  -5.688  39.322 1.00 22.84  ? 192 LEU A CG  1 
ATOM   1370 C CD1 . LEU A 1 176 ? 26.352  -4.492  39.397 1.00 22.76  ? 192 LEU A CD1 1 
ATOM   1371 C CD2 . LEU A 1 176 ? 26.633  -6.924  39.848 1.00 23.35  ? 192 LEU A CD2 1 
ATOM   1372 N N   . LYS A 1 177 ? 29.071  -8.149  35.727 1.00 19.82  ? 193 LYS A N   1 
ATOM   1373 C CA  . LYS A 1 177 ? 29.394  -8.507  34.363 1.00 21.13  ? 193 LYS A CA  1 
ATOM   1374 C C   . LYS A 1 177 ? 28.162  -9.090  33.664 1.00 20.86  ? 193 LYS A C   1 
ATOM   1375 O O   . LYS A 1 177 ? 27.461  -9.935  34.229 1.00 21.55  ? 193 LYS A O   1 
ATOM   1376 C CB  . LYS A 1 177 ? 30.532  -9.531  34.372 1.00 19.66  ? 193 LYS A CB  1 
ATOM   1377 C CG  . LYS A 1 177 ? 31.755  -9.097  35.166 1.00 19.74  ? 193 LYS A CG  1 
ATOM   1378 C CD  . LYS A 1 177 ? 32.985  -9.982  34.930 1.00 19.79  ? 193 LYS A CD  1 
ATOM   1379 C CE  . LYS A 1 177 ? 34.134  -9.642  35.862 1.00 18.73  ? 193 LYS A CE  1 
ATOM   1380 N NZ  . LYS A 1 177 ? 33.736  -9.696  37.299 1.00 17.52  ? 193 LYS A NZ  1 
ATOM   1381 N N   . ILE A 1 178 ? 27.936  -8.671  32.413 1.00 20.66  ? 194 ILE A N   1 
ATOM   1382 C CA  . ILE A 1 178 ? 26.944  -9.317  31.564 1.00 20.90  ? 194 ILE A CA  1 
ATOM   1383 C C   . ILE A 1 178 ? 27.647  -10.214 30.558 1.00 21.95  ? 194 ILE A C   1 
ATOM   1384 O O   . ILE A 1 178 ? 28.485  -9.740  29.795 1.00 22.59  ? 194 ILE A O   1 
ATOM   1385 C CB  . ILE A 1 178 ? 26.015  -8.312  30.861 1.00 21.95  ? 194 ILE A CB  1 
ATOM   1386 C CG1 . ILE A 1 178 ? 25.166  -7.521  31.866 1.00 21.14  ? 194 ILE A CG1 1 
ATOM   1387 C CG2 . ILE A 1 178 ? 25.144  -9.054  29.856 1.00 22.76  ? 194 ILE A CG2 1 
ATOM   1388 C CD1 . ILE A 1 178 ? 24.034  -8.312  32.501 1.00 20.21  ? 194 ILE A CD1 1 
ATOM   1389 N N   . LEU A 1 179 ? 27.273  -11.504 30.562 1.00 22.61  ? 195 LEU A N   1 
ATOM   1390 C CA  . LEU A 1 179 ? 27.893  -12.503 29.702 1.00 23.67  ? 195 LEU A CA  1 
ATOM   1391 C C   . LEU A 1 179 ? 26.907  -12.967 28.645 1.00 23.59  ? 195 LEU A C   1 
ATOM   1392 O O   . LEU A 1 179 ? 25.718  -13.054 28.923 1.00 24.82  ? 195 LEU A O   1 
ATOM   1393 C CB  . LEU A 1 179 ? 28.294  -13.733 30.505 1.00 23.72  ? 195 LEU A CB  1 
ATOM   1394 C CG  . LEU A 1 179 ? 29.050  -13.494 31.797 1.00 23.61  ? 195 LEU A CG  1 
ATOM   1395 C CD1 . LEU A 1 179 ? 29.390  -14.821 32.426 1.00 24.13  ? 195 LEU A CD1 1 
ATOM   1396 C CD2 . LEU A 1 179 ? 30.309  -12.690 31.560 1.00 24.70  ? 195 LEU A CD2 1 
ATOM   1397 N N   . ASN A 1 180 ? 27.425  -13.314 27.466 1.00 22.01  ? 196 ASN A N   1 
ATOM   1398 C CA  . ASN A 1 180 ? 26.627  -13.969 26.444 1.00 24.56  ? 196 ASN A CA  1 
ATOM   1399 C C   . ASN A 1 180 ? 26.606  -15.470 26.754 1.00 23.58  ? 196 ASN A C   1 
ATOM   1400 O O   . ASN A 1 180 ? 27.186  -15.929 27.737 1.00 22.62  ? 196 ASN A O   1 
ATOM   1401 C CB  . ASN A 1 180 ? 27.130  -13.619 25.040 1.00 23.91  ? 196 ASN A CB  1 
ATOM   1402 C CG  . ASN A 1 180 ? 28.429  -14.296 24.660 1.00 24.29  ? 196 ASN A CG  1 
ATOM   1403 O OD1 . ASN A 1 180 ? 28.876  -15.214 25.329 1.00 25.53  ? 196 ASN A OD1 1 
ATOM   1404 N ND2 . ASN A 1 180 ? 29.017  -13.900 23.546 1.00 26.18  ? 196 ASN A ND2 1 
ATOM   1405 N N   . HIS A 1 181 ? 25.930  -16.230 25.903 1.00 24.29  ? 197 HIS A N   1 
ATOM   1406 C CA  . HIS A 1 181 ? 25.726  -17.654 26.138 1.00 26.25  ? 197 HIS A CA  1 
ATOM   1407 C C   . HIS A 1 181 ? 27.044  -18.424 26.087 1.00 25.52  ? 197 HIS A C   1 
ATOM   1408 O O   . HIS A 1 181 ? 27.139  -19.514 26.649 1.00 28.54  ? 197 HIS A O   1 
ATOM   1409 C CB  . HIS A 1 181 ? 24.676  -18.176 25.151 1.00 26.64  ? 197 HIS A CB  1 
ATOM   1410 C CG  . HIS A 1 181 ? 24.434  -19.647 25.171 1.00 27.47  ? 197 HIS A CG  1 
ATOM   1411 N ND1 . HIS A 1 181 ? 25.275  -20.544 24.548 1.00 32.24  ? 197 HIS A ND1 1 
ATOM   1412 C CD2 . HIS A 1 181 ? 23.440  -20.375 25.685 1.00 27.26  ? 197 HIS A CD2 1 
ATOM   1413 C CE1 . HIS A 1 181 ? 24.787  -21.784 24.700 1.00 28.72  ? 197 HIS A CE1 1 
ATOM   1414 N NE2 . HIS A 1 181 ? 23.672  -21.705 25.377 1.00 28.20  ? 197 HIS A NE2 1 
ATOM   1415 N N   . ASN A 1 182 ? 28.039  -17.879 25.373 1.00 28.00  ? 198 ASN A N   1 
ATOM   1416 C CA  . ASN A 1 182 ? 29.369  -18.472 25.283 1.00 26.52  ? 198 ASN A CA  1 
ATOM   1417 C C   . ASN A 1 182 ? 30.285  -17.980 26.409 1.00 25.56  ? 198 ASN A C   1 
ATOM   1418 O O   . ASN A 1 182 ? 31.479  -18.249 26.374 1.00 25.12  ? 198 ASN A O   1 
ATOM   1419 C CB  . ASN A 1 182 ? 29.993  -18.171 23.922 1.00 27.74  ? 198 ASN A CB  1 
ATOM   1420 C CG  . ASN A 1 182 ? 31.223  -19.009 23.630 1.00 31.50  ? 198 ASN A CG  1 
ATOM   1421 O OD1 . ASN A 1 182 ? 31.158  -20.234 23.637 1.00 33.28  ? 198 ASN A OD1 1 
ATOM   1422 N ND2 . ASN A 1 182 ? 32.355  -18.356 23.417 1.00 35.13  ? 198 ASN A ND2 1 
ATOM   1423 N N   . LEU A 1 183 ? 29.724  -17.256 27.387 1.00 25.44  ? 199 LEU A N   1 
ATOM   1424 C CA  . LEU A 1 183 ? 30.412  -16.744 28.567 1.00 25.45  ? 199 LEU A CA  1 
ATOM   1425 C C   . LEU A 1 183 ? 31.370  -15.595 28.222 1.00 25.55  ? 199 LEU A C   1 
ATOM   1426 O O   . LEU A 1 183 ? 32.176  -15.186 29.063 1.00 24.59  ? 199 LEU A O   1 
ATOM   1427 C CB  . LEU A 1 183 ? 31.092  -17.902 29.319 1.00 26.17  ? 199 LEU A CB  1 
ATOM   1428 C CG  . LEU A 1 183 ? 30.146  -19.020 29.772 1.00 28.30  ? 199 LEU A CG  1 
ATOM   1429 C CD1 . LEU A 1 183 ? 30.853  -20.048 30.662 1.00 30.49  ? 199 LEU A CD1 1 
ATOM   1430 C CD2 . LEU A 1 183 ? 28.934  -18.481 30.518 1.00 27.29  ? 199 LEU A CD2 1 
ATOM   1431 N N   . ASP A 1 184 ? 31.230  -15.000 27.029 1.00 26.09  ? 200 ASP A N   1 
ATOM   1432 C CA  . ASP A 1 184 ? 32.007  -13.811 26.702 1.00 28.32  ? 200 ASP A CA  1 
ATOM   1433 C C   . ASP A 1 184 ? 31.511  -12.612 27.506 1.00 27.31  ? 200 ASP A C   1 
ATOM   1434 O O   . ASP A 1 184 ? 30.310  -12.414 27.674 1.00 25.08  ? 200 ASP A O   1 
ATOM   1435 C CB  . ASP A 1 184 ? 31.964  -13.444 25.219 1.00 30.71  ? 200 ASP A CB  1 
ATOM   1436 C CG  . ASP A 1 184 ? 32.414  -14.581 24.321 1.00 33.49  ? 200 ASP A CG  1 
ATOM   1437 O OD1 . ASP A 1 184 ? 33.492  -15.108 24.577 1.00 39.54  ? 200 ASP A OD1 1 
ATOM   1438 O OD2 . ASP A 1 184 ? 31.688  -14.921 23.386 1.00 35.19  ? 200 ASP A OD2 1 
ATOM   1439 N N   . VAL A 1 185 ? 32.463  -11.787 27.952 1.00 25.63  ? 201 VAL A N   1 
ATOM   1440 C CA  . VAL A 1 185 ? 32.155  -10.614 28.752 1.00 26.99  ? 201 VAL A CA  1 
ATOM   1441 C C   . VAL A 1 185 ? 31.738  -9.506  27.803 1.00 24.81  ? 201 VAL A C   1 
ATOM   1442 O O   . VAL A 1 185 ? 32.567  -9.050  27.023 1.00 22.95  ? 201 VAL A O   1 
ATOM   1443 C CB  . VAL A 1 185 ? 33.359  -10.206 29.624 1.00 26.41  ? 201 VAL A CB  1 
ATOM   1444 C CG1 . VAL A 1 185 ? 33.078  -8.960  30.458 1.00 25.55  ? 201 VAL A CG1 1 
ATOM   1445 C CG2 . VAL A 1 185 ? 33.797  -11.359 30.511 1.00 23.81  ? 201 VAL A CG2 1 
ATOM   1446 N N   . LEU A 1 186 ? 30.463  -9.099  27.873 1.00 23.73  ? 202 LEU A N   1 
ATOM   1447 C CA  . LEU A 1 186 ? 29.945  -8.048  26.991 1.00 25.13  ? 202 LEU A CA  1 
ATOM   1448 C C   . LEU A 1 186 ? 30.080  -6.657  27.595 1.00 23.51  ? 202 LEU A C   1 
ATOM   1449 O O   . LEU A 1 186 ? 30.286  -5.697  26.862 1.00 28.84  ? 202 LEU A O   1 
ATOM   1450 C CB  . LEU A 1 186 ? 28.476  -8.306  26.685 1.00 25.35  ? 202 LEU A CB  1 
ATOM   1451 C CG  . LEU A 1 186 ? 28.157  -9.698  26.166 1.00 24.89  ? 202 LEU A CG  1 
ATOM   1452 C CD1 . LEU A 1 186 ? 26.708  -9.740  25.709 1.00 25.08  ? 202 LEU A CD1 1 
ATOM   1453 C CD2 . LEU A 1 186 ? 29.130  -10.114 25.057 1.00 25.76  ? 202 LEU A CD2 1 
ATOM   1454 N N   . PHE A 1 187 ? 29.920  -6.558  28.915 1.00 21.97  ? 203 PHE A N   1 
ATOM   1455 C CA  . PHE A 1 187 ? 29.887  -5.297  29.621 1.00 23.33  ? 203 PHE A CA  1 
ATOM   1456 C C   . PHE A 1 187 ? 30.204  -5.582  31.072 1.00 22.82  ? 203 PHE A C   1 
ATOM   1457 O O   . PHE A 1 187 ? 29.729  -6.581  31.604 1.00 25.57  ? 203 PHE A O   1 
ATOM   1458 C CB  . PHE A 1 187 ? 28.506  -4.624  29.532 1.00 24.21  ? 203 PHE A CB  1 
ATOM   1459 C CG  . PHE A 1 187 ? 28.370  -3.383  30.379 1.00 23.16  ? 203 PHE A CG  1 
ATOM   1460 C CD1 . PHE A 1 187 ? 29.098  -2.240  30.092 1.00 25.57  ? 203 PHE A CD1 1 
ATOM   1461 C CD2 . PHE A 1 187 ? 27.546  -3.364  31.490 1.00 24.50  ? 203 PHE A CD2 1 
ATOM   1462 C CE1 . PHE A 1 187 ? 28.997  -1.111  30.893 1.00 27.58  ? 203 PHE A CE1 1 
ATOM   1463 C CE2 . PHE A 1 187 ? 27.422  -2.230  32.275 1.00 25.14  ? 203 PHE A CE2 1 
ATOM   1464 C CZ  . PHE A 1 187 ? 28.137  -1.097  31.968 1.00 25.04  ? 203 PHE A CZ  1 
ATOM   1465 N N   . GLU A 1 188 ? 31.012  -4.729  31.710 1.00 23.73  ? 204 GLU A N   1 
ATOM   1466 C CA  . GLU A 1 188 ? 31.313  -4.916  33.124 1.00 23.35  ? 204 GLU A CA  1 
ATOM   1467 C C   . GLU A 1 188 ? 31.409  -3.541  33.776 1.00 22.34  ? 204 GLU A C   1 
ATOM   1468 O O   . GLU A 1 188 ? 31.819  -2.594  33.132 1.00 23.81  ? 204 GLU A O   1 
ATOM   1469 C CB  . GLU A 1 188 ? 32.551  -5.811  33.316 1.00 24.45  ? 204 GLU A CB  1 
ATOM   1470 C CG  . GLU A 1 188 ? 33.807  -5.273  32.658 1.00 28.13  ? 204 GLU A CG  1 
ATOM   1471 C CD  . GLU A 1 188 ? 35.063  -6.120  32.774 1.00 30.80  ? 204 GLU A CD  1 
ATOM   1472 O OE1 . GLU A 1 188 ? 36.072  -5.704  32.211 1.00 32.95  ? 204 GLU A OE1 1 
ATOM   1473 O OE2 . GLU A 1 188 ? 35.025  -7.196  33.394 1.00 33.04  ? 204 GLU A OE2 1 
ATOM   1474 N N   . THR A 1 189 ? 31.002  -3.448  35.041 1.00 22.79  ? 205 THR A N   1 
ATOM   1475 C CA  . THR A 1 189 ? 30.992  -2.202  35.781 1.00 22.63  ? 205 THR A CA  1 
ATOM   1476 C C   . THR A 1 189 ? 31.105  -2.535  37.268 1.00 24.67  ? 205 THR A C   1 
ATOM   1477 O O   . THR A 1 189 ? 30.545  -3.534  37.730 1.00 25.51  ? 205 THR A O   1 
ATOM   1478 C CB  . THR A 1 189 ? 29.741  -1.378  35.439 1.00 24.15  ? 205 THR A CB  1 
ATOM   1479 O OG1 . THR A 1 189 ? 29.877  -0.051  35.946 1.00 25.37  ? 205 THR A OG1 1 
ATOM   1480 C CG2 . THR A 1 189 ? 28.453  -1.975  35.962 1.00 22.38  ? 205 THR A CG2 1 
ATOM   1481 N N   . GLU A 1 190 ? 31.826  -1.672  38.009 1.00 24.73  ? 206 GLU A N   1 
ATOM   1482 C CA  . GLU A 1 190 ? 32.096  -1.879  39.424 1.00 26.08  ? 206 GLU A CA  1 
ATOM   1483 C C   . GLU A 1 190 ? 30.780  -1.961  40.184 1.00 25.27  ? 206 GLU A C   1 
ATOM   1484 O O   . GLU A 1 190 ? 29.895  -1.127  39.993 1.00 26.99  ? 206 GLU A O   1 
ATOM   1485 C CB  . GLU A 1 190 ? 32.953  -0.732  39.991 1.00 26.94  ? 206 GLU A CB  1 
ATOM   1486 C CG  . GLU A 1 190 ? 33.347  -0.947  41.447 1.00 27.51  ? 206 GLU A CG  1 
ATOM   1487 C CD  . GLU A 1 190 ? 34.188  0.154   42.081 1.00 34.37  ? 206 GLU A CD  1 
ATOM   1488 O OE1 . GLU A 1 190 ? 34.566  1.103   41.363 1.00 38.53  ? 206 GLU A OE1 1 
ATOM   1489 O OE2 . GLU A 1 190 ? 34.437  0.071   43.302 1.00 33.87  ? 206 GLU A OE2 1 
ATOM   1490 N N   . PHE A 1 191 ? 30.659  -2.983  41.043 1.00 26.10  ? 207 PHE A N   1 
ATOM   1491 C CA  . PHE A 1 191 ? 29.532  -3.123  41.953 1.00 24.93  ? 207 PHE A CA  1 
ATOM   1492 C C   . PHE A 1 191 ? 29.670  -2.172  43.143 1.00 26.35  ? 207 PHE A C   1 
ATOM   1493 O O   . PHE A 1 191 ? 29.813  -2.608  44.284 1.00 24.26  ? 207 PHE A O   1 
ATOM   1494 C CB  . PHE A 1 191 ? 29.402  -4.575  42.452 1.00 24.16  ? 207 PHE A CB  1 
ATOM   1495 C CG  . PHE A 1 191 ? 28.056  -4.962  43.012 1.00 25.07  ? 207 PHE A CG  1 
ATOM   1496 C CD1 . PHE A 1 191 ? 27.005  -4.057  43.110 1.00 25.87  ? 207 PHE A CD1 1 
ATOM   1497 C CD2 . PHE A 1 191 ? 27.819  -6.259  43.413 1.00 27.58  ? 207 PHE A CD2 1 
ATOM   1498 C CE1 . PHE A 1 191 ? 25.778  -4.452  43.617 1.00 26.79  ? 207 PHE A CE1 1 
ATOM   1499 C CE2 . PHE A 1 191 ? 26.579  -6.655  43.901 1.00 30.10  ? 207 PHE A CE2 1 
ATOM   1500 C CZ  . PHE A 1 191 ? 25.555  -5.753  44.000 1.00 26.27  ? 207 PHE A CZ  1 
ATOM   1501 N N   . THR A 1 192 ? 29.544  -0.869  42.875 1.00 27.36  ? 208 THR A N   1 
ATOM   1502 C CA  . THR A 1 192 ? 29.615  0.149   43.910 1.00 26.93  ? 208 THR A CA  1 
ATOM   1503 C C   . THR A 1 192 ? 28.453  -0.021  44.877 1.00 27.60  ? 208 THR A C   1 
ATOM   1504 O O   . THR A 1 192 ? 27.339  -0.386  44.478 1.00 27.92  ? 208 THR A O   1 
ATOM   1505 C CB  . THR A 1 192 ? 29.623  1.556   43.289 1.00 27.19  ? 208 THR A CB  1 
ATOM   1506 O OG1 . THR A 1 192 ? 28.491  1.676   42.419 1.00 25.08  ? 208 THR A OG1 1 
ATOM   1507 C CG2 . THR A 1 192 ? 30.875  1.819   42.486 1.00 26.72  ? 208 THR A CG2 1 
ATOM   1508 N N   . ASP A 1 193 ? 28.724  0.265   46.159 1.00 27.40  ? 209 ASP A N   1 
ATOM   1509 C CA  . ASP A 1 193 ? 27.750  0.091   47.223 1.00 28.11  ? 209 ASP A CA  1 
ATOM   1510 C C   . ASP A 1 193 ? 26.748  1.249   47.203 1.00 26.88  ? 209 ASP A C   1 
ATOM   1511 O O   . ASP A 1 193 ? 26.947  2.271   46.528 1.00 22.88  ? 209 ASP A O   1 
ATOM   1512 C CB  . ASP A 1 193 ? 28.450  -0.093  48.582 1.00 34.54  ? 209 ASP A CB  1 
ATOM   1513 C CG  . ASP A 1 193 ? 29.021  1.173   49.204 1.00 39.48  ? 209 ASP A CG  1 
ATOM   1514 O OD1 . ASP A 1 193 ? 29.570  2.003   48.445 1.00 41.57  ? 209 ASP A OD1 1 
ATOM   1515 O OD2 . ASP A 1 193 ? 28.966  1.297   50.456 1.00 53.30  ? 209 ASP A OD2 1 
ATOM   1516 N N   . GLU A 1 194 ? 25.635  1.033   47.912 1.00 28.32  ? 210 GLU A N   1 
ATOM   1517 C CA  . GLU A 1 194 ? 24.590  2.033   48.106 1.00 32.62  ? 210 GLU A CA  1 
ATOM   1518 C C   . GLU A 1 194 ? 24.142  2.654   46.781 1.00 33.66  ? 210 GLU A C   1 
ATOM   1519 O O   . GLU A 1 194 ? 23.880  3.843   46.718 1.00 38.11  ? 210 GLU A O   1 
ATOM   1520 C CB  . GLU A 1 194 ? 25.101  3.100   49.069 1.00 32.33  ? 210 GLU A CB  1 
ATOM   1521 C CG  . GLU A 1 194 ? 25.336  2.566   50.471 1.00 36.95  ? 210 GLU A CG  1 
ATOM   1522 C CD  . GLU A 1 194 ? 25.879  3.583   51.462 1.00 42.82  ? 210 GLU A CD  1 
ATOM   1523 O OE1 . GLU A 1 194 ? 26.031  4.778   51.058 1.00 36.61  ? 210 GLU A OE1 1 
ATOM   1524 O OE2 . GLU A 1 194 ? 26.183  3.164   52.614 1.00 44.17  ? 210 GLU A OE2 1 
ATOM   1525 N N   . THR A 1 195 ? 24.051  1.833   45.731 1.00 28.76  ? 211 THR A N   1 
ATOM   1526 C CA  . THR A 1 195 ? 23.773  2.280   44.371 1.00 26.80  ? 211 THR A CA  1 
ATOM   1527 C C   . THR A 1 195 ? 22.882  1.235   43.701 1.00 26.46  ? 211 THR A C   1 
ATOM   1528 O O   . THR A 1 195 ? 23.170  0.033   43.777 1.00 24.53  ? 211 THR A O   1 
ATOM   1529 C CB  . THR A 1 195 ? 25.067  2.463   43.566 1.00 29.91  ? 211 THR A CB  1 
ATOM   1530 O OG1 . THR A 1 195 ? 25.881  3.430   44.232 1.00 29.17  ? 211 THR A OG1 1 
ATOM   1531 C CG2 . THR A 1 195 ? 24.844  2.883   42.126 1.00 29.81  ? 211 THR A CG2 1 
ATOM   1532 N N   . TRP A 1 196 ? 21.779  1.683   43.086 1.00 22.77  ? 212 TRP A N   1 
ATOM   1533 C CA  . TRP A 1 196 ? 20.967  0.787   42.275 1.00 21.32  ? 212 TRP A CA  1 
ATOM   1534 C C   . TRP A 1 196 ? 21.575  0.685   40.876 1.00 21.22  ? 212 TRP A C   1 
ATOM   1535 O O   . TRP A 1 196 ? 21.700  1.668   40.126 1.00 19.98  ? 212 TRP A O   1 
ATOM   1536 C CB  . TRP A 1 196 ? 19.497  1.218   42.254 1.00 21.18  ? 212 TRP A CB  1 
ATOM   1537 C CG  . TRP A 1 196 ? 18.713  0.758   43.446 1.00 21.54  ? 212 TRP A CG  1 
ATOM   1538 C CD1 . TRP A 1 196 ? 18.204  1.545   44.430 1.00 20.46  ? 212 TRP A CD1 1 
ATOM   1539 C CD2 . TRP A 1 196 ? 18.331  -0.596  43.766 1.00 21.26  ? 212 TRP A CD2 1 
ATOM   1540 N NE1 . TRP A 1 196 ? 17.546  0.783   45.346 1.00 22.53  ? 212 TRP A NE1 1 
ATOM   1541 C CE2 . TRP A 1 196 ? 17.608  -0.534  44.978 1.00 22.24  ? 212 TRP A CE2 1 
ATOM   1542 C CE3 . TRP A 1 196 ? 18.538  -1.846  43.169 1.00 20.70  ? 212 TRP A CE3 1 
ATOM   1543 C CZ2 . TRP A 1 196 ? 17.076  -1.662  45.601 1.00 21.50  ? 212 TRP A CZ2 1 
ATOM   1544 C CZ3 . TRP A 1 196 ? 18.016  -2.961  43.792 1.00 21.08  ? 212 TRP A CZ3 1 
ATOM   1545 C CH2 . TRP A 1 196 ? 17.269  -2.867  44.972 1.00 20.46  ? 212 TRP A CH2 1 
ATOM   1546 N N   . HIS A 1 197 ? 22.066  -0.517  40.582 1.00 19.02  ? 213 HIS A N   1 
ATOM   1547 C CA  . HIS A 1 197 ? 22.610  -0.805  39.278 1.00 20.84  ? 213 HIS A CA  1 
ATOM   1548 C C   . HIS A 1 197 ? 21.491  -1.374  38.415 1.00 19.75  ? 213 HIS A C   1 
ATOM   1549 O O   . HIS A 1 197 ? 21.095  -2.515  38.602 1.00 21.74  ? 213 HIS A O   1 
ATOM   1550 C CB  . HIS A 1 197 ? 23.812  -1.738  39.415 1.00 22.23  ? 213 HIS A CB  1 
ATOM   1551 C CG  . HIS A 1 197 ? 24.957  -1.146  40.183 1.00 22.31  ? 213 HIS A CG  1 
ATOM   1552 N ND1 . HIS A 1 197 ? 26.008  -0.498  39.570 1.00 23.74  ? 213 HIS A ND1 1 
ATOM   1553 C CD2 . HIS A 1 197 ? 25.196  -1.107  41.503 1.00 21.97  ? 213 HIS A CD2 1 
ATOM   1554 C CE1 . HIS A 1 197 ? 26.871  -0.121  40.502 1.00 23.72  ? 213 HIS A CE1 1 
ATOM   1555 N NE2 . HIS A 1 197 ? 26.403  -0.490  41.690 1.00 21.20  ? 213 HIS A NE2 1 
ATOM   1556 N N   . ASN A 1 198 ? 21.025  -0.545  37.478 1.00 20.16  ? 214 ASN A N   1 
ATOM   1557 C CA  . ASN A 1 198 ? 19.900  -0.818  36.610 1.00 19.78  ? 214 ASN A CA  1 
ATOM   1558 C C   . ASN A 1 198 ? 20.401  -1.394  35.293 1.00 19.49  ? 214 ASN A C   1 
ATOM   1559 O O   . ASN A 1 198 ? 21.263  -0.796  34.642 1.00 17.22  ? 214 ASN A O   1 
ATOM   1560 C CB  . ASN A 1 198 ? 19.126  0.467   36.305 1.00 19.87  ? 214 ASN A CB  1 
ATOM   1561 C CG  . ASN A 1 198 ? 18.764  1.308   37.512 1.00 20.36  ? 214 ASN A CG  1 
ATOM   1562 O OD1 . ASN A 1 198 ? 19.046  2.511   37.530 1.00 24.14  ? 214 ASN A OD1 1 
ATOM   1563 N ND2 . ASN A 1 198 ? 18.060  0.729   38.462 1.00 17.10  ? 214 ASN A ND2 1 
ATOM   1564 N N   . PHE A 1 199 ? 19.826  -2.536  34.888 1.00 20.65  ? 215 PHE A N   1 
ATOM   1565 C CA  . PHE A 1 199 ? 20.176  -3.184  33.638 1.00 18.82  ? 215 PHE A CA  1 
ATOM   1566 C C   . PHE A 1 199 ? 18.923  -3.444  32.812 1.00 22.61  ? 215 PHE A C   1 
ATOM   1567 O O   . PHE A 1 199 ? 17.825  -3.684  33.346 1.00 21.26  ? 215 PHE A O   1 
ATOM   1568 C CB  . PHE A 1 199 ? 20.842  -4.544  33.858 1.00 18.58  ? 215 PHE A CB  1 
ATOM   1569 C CG  . PHE A 1 199 ? 22.216  -4.502  34.489 1.00 18.99  ? 215 PHE A CG  1 
ATOM   1570 C CD1 . PHE A 1 199 ? 22.368  -4.362  35.850 1.00 18.62  ? 215 PHE A CD1 1 
ATOM   1571 C CD2 . PHE A 1 199 ? 23.362  -4.514  33.703 1.00 20.03  ? 215 PHE A CD2 1 
ATOM   1572 C CE1 . PHE A 1 199 ? 23.630  -4.287  36.425 1.00 18.33  ? 215 PHE A CE1 1 
ATOM   1573 C CE2 . PHE A 1 199 ? 24.620  -4.454  34.273 1.00 18.26  ? 215 PHE A CE2 1 
ATOM   1574 C CZ  . PHE A 1 199 ? 24.751  -4.347  35.636 1.00 20.14  ? 215 PHE A CZ  1 
ATOM   1575 N N   . ALA A 1 200 ? 19.127  -3.468  31.499 1.00 21.71  ? 216 ALA A N   1 
ATOM   1576 C CA  . ALA A 1 200 ? 18.207  -4.178  30.624 1.00 23.09  ? 216 ALA A CA  1 
ATOM   1577 C C   . ALA A 1 200 ? 19.030  -4.900  29.573 1.00 22.09  ? 216 ALA A C   1 
ATOM   1578 O O   . ALA A 1 200 ? 19.990  -4.357  29.050 1.00 22.65  ? 216 ALA A O   1 
ATOM   1579 C CB  . ALA A 1 200 ? 17.178  -3.254  30.014 1.00 23.94  ? 216 ALA A CB  1 
ATOM   1580 N N   . VAL A 1 201 ? 18.680  -6.154  29.326 1.00 22.78  ? 217 VAL A N   1 
ATOM   1581 C CA  . VAL A 1 201 ? 19.297  -6.929  28.280 1.00 21.44  ? 217 VAL A CA  1 
ATOM   1582 C C   . VAL A 1 201 ? 18.201  -7.209  27.247 1.00 22.62  ? 217 VAL A C   1 
ATOM   1583 O O   . VAL A 1 201 ? 17.170  -7.799  27.573 1.00 21.02  ? 217 VAL A O   1 
ATOM   1584 C CB  . VAL A 1 201 ? 19.905  -8.223  28.846 1.00 22.65  ? 217 VAL A CB  1 
ATOM   1585 C CG1 . VAL A 1 201 ? 20.511  -9.097  27.757 1.00 22.93  ? 217 VAL A CG1 1 
ATOM   1586 C CG2 . VAL A 1 201 ? 20.946  -7.951  29.923 1.00 22.33  ? 217 VAL A CG2 1 
ATOM   1587 N N   . ILE A 1 202 ? 18.403  -6.731  26.019 1.00 23.44  ? 218 ILE A N   1 
ATOM   1588 C CA  . ILE A 1 202 ? 17.475  -7.052  24.938 1.00 23.24  ? 218 ILE A CA  1 
ATOM   1589 C C   . ILE A 1 202 ? 17.896  -8.357  24.259 1.00 22.36  ? 218 ILE A C   1 
ATOM   1590 O O   . ILE A 1 202 ? 19.007  -8.454  23.730 1.00 20.52  ? 218 ILE A O   1 
ATOM   1591 C CB  . ILE A 1 202 ? 17.367  -5.913  23.914 1.00 23.38  ? 218 ILE A CB  1 
ATOM   1592 C CG1 . ILE A 1 202 ? 16.791  -4.635  24.527 1.00 23.55  ? 218 ILE A CG1 1 
ATOM   1593 C CG2 . ILE A 1 202 ? 16.520  -6.375  22.736 1.00 25.62  ? 218 ILE A CG2 1 
ATOM   1594 C CD1 . ILE A 1 202 ? 16.755  -3.449  23.561 1.00 22.45  ? 218 ILE A CD1 1 
ATOM   1595 N N   . VAL A 1 203 ? 16.991  -9.346  24.282 1.00 23.31  ? 219 VAL A N   1 
ATOM   1596 C CA  . VAL A 1 203 ? 17.170  -10.594 23.551 1.00 25.24  ? 219 VAL A CA  1 
ATOM   1597 C C   . VAL A 1 203 ? 16.307  -10.558 22.293 1.00 26.69  ? 219 VAL A C   1 
ATOM   1598 O O   . VAL A 1 203 ? 15.084  -10.455 22.385 1.00 27.21  ? 219 VAL A O   1 
ATOM   1599 C CB  . VAL A 1 203 ? 16.809  -11.801 24.431 1.00 26.79  ? 219 VAL A CB  1 
ATOM   1600 C CG1 . VAL A 1 203 ? 16.986  -13.118 23.695 1.00 27.45  ? 219 VAL A CG1 1 
ATOM   1601 C CG2 . VAL A 1 203 ? 17.625  -11.809 25.721 1.00 29.52  ? 219 VAL A CG2 1 
ATOM   1602 N N   . ASP A 1 204 ? 16.953  -10.586 21.124 1.00 26.94  ? 220 ASP A N   1 
ATOM   1603 C CA  . ASP A 1 204 ? 16.246  -10.761 19.861 1.00 25.55  ? 220 ASP A CA  1 
ATOM   1604 C C   . ASP A 1 204 ? 16.293  -12.238 19.523 1.00 26.79  ? 220 ASP A C   1 
ATOM   1605 O O   . ASP A 1 204 ? 17.339  -12.711 19.081 1.00 29.18  ? 220 ASP A O   1 
ATOM   1606 C CB  . ASP A 1 204 ? 16.867  -9.945  18.734 1.00 28.85  ? 220 ASP A CB  1 
ATOM   1607 C CG  . ASP A 1 204 ? 16.180  -10.106 17.381 1.00 30.69  ? 220 ASP A CG  1 
ATOM   1608 O OD1 . ASP A 1 204 ? 15.434  -11.107 17.176 1.00 29.05  ? 220 ASP A OD1 1 
ATOM   1609 O OD2 . ASP A 1 204 ? 16.381  -9.220  16.564 1.00 29.61  ? 220 ASP A OD2 1 
ATOM   1610 N N   . TRP A 1 205 ? 15.179  -12.928 19.796 1.00 29.32  ? 221 TRP A N   1 
ATOM   1611 C CA  . TRP A 1 205 ? 15.056  -14.377 19.657 1.00 33.62  ? 221 TRP A CA  1 
ATOM   1612 C C   . TRP A 1 205 ? 15.105  -14.858 18.188 1.00 34.87  ? 221 TRP A C   1 
ATOM   1613 O O   . TRP A 1 205 ? 15.478  -15.998 17.922 1.00 34.24  ? 221 TRP A O   1 
ATOM   1614 C CB  . TRP A 1 205 ? 13.776  -14.840 20.384 1.00 32.16  ? 221 TRP A CB  1 
ATOM   1615 C CG  . TRP A 1 205 ? 13.798  -14.713 21.890 1.00 29.41  ? 221 TRP A CG  1 
ATOM   1616 C CD1 . TRP A 1 205 ? 13.074  -13.828 22.626 1.00 30.03  ? 221 TRP A CD1 1 
ATOM   1617 C CD2 . TRP A 1 205 ? 14.529  -15.514 22.853 1.00 29.11  ? 221 TRP A CD2 1 
ATOM   1618 N NE1 . TRP A 1 205 ? 13.328  -13.982 23.965 1.00 32.63  ? 221 TRP A NE1 1 
ATOM   1619 C CE2 . TRP A 1 205 ? 14.213  -15.012 24.137 1.00 32.38  ? 221 TRP A CE2 1 
ATOM   1620 C CE3 . TRP A 1 205 ? 15.439  -16.574 22.764 1.00 29.70  ? 221 TRP A CE3 1 
ATOM   1621 C CZ2 . TRP A 1 205 ? 14.748  -15.551 25.308 1.00 33.38  ? 221 TRP A CZ2 1 
ATOM   1622 C CZ3 . TRP A 1 205 ? 15.957  -17.122 23.922 1.00 28.55  ? 221 TRP A CZ3 1 
ATOM   1623 C CH2 . TRP A 1 205 ? 15.614  -16.618 25.174 1.00 31.84  ? 221 TRP A CH2 1 
ATOM   1624 N N   . GLU A 1 206 ? 14.776  -14.005 17.207 1.00 37.00  ? 222 GLU A N   1 
ATOM   1625 C CA  . GLU A 1 206 ? 14.851  -14.415 15.813 1.00 39.27  ? 222 GLU A CA  1 
ATOM   1626 C C   . GLU A 1 206 ? 16.284  -14.337 15.304 1.00 41.59  ? 222 GLU A C   1 
ATOM   1627 O O   . GLU A 1 206 ? 16.723  -15.254 14.624 1.00 45.16  ? 222 GLU A O   1 
ATOM   1628 C CB  . GLU A 1 206 ? 14.023  -13.533 14.875 1.00 41.84  ? 222 GLU A CB  1 
ATOM   1629 C CG  . GLU A 1 206 ? 12.531  -13.651 15.052 1.00 44.64  ? 222 GLU A CG  1 
ATOM   1630 C CD  . GLU A 1 206 ? 11.738  -12.793 14.076 1.00 43.13  ? 222 GLU A CD  1 
ATOM   1631 O OE1 . GLU A 1 206 ? 11.922  -11.555 14.073 1.00 37.18  ? 222 GLU A OE1 1 
ATOM   1632 O OE2 . GLU A 1 206 ? 10.929  -13.362 13.335 1.00 40.53  ? 222 GLU A OE2 1 
ATOM   1633 N N   . LYS A 1 207 ? 16.992  -13.235 15.600 1.00 39.48  ? 223 LYS A N   1 
ATOM   1634 C CA  . LYS A 1 207 ? 18.318  -12.997 15.051 1.00 37.94  ? 223 LYS A CA  1 
ATOM   1635 C C   . LYS A 1 207 ? 19.416  -13.506 15.987 1.00 35.75  ? 223 LYS A C   1 
ATOM   1636 O O   . LYS A 1 207 ? 20.574  -13.577 15.581 1.00 36.19  ? 223 LYS A O   1 
ATOM   1637 C CB  . LYS A 1 207 ? 18.484  -11.512 14.715 1.00 41.99  ? 223 LYS A CB  1 
ATOM   1638 C CG  . LYS A 1 207 ? 17.871  -11.071 13.389 1.00 47.26  ? 223 LYS A CG  1 
ATOM   1639 C CD  . LYS A 1 207 ? 17.210  -9.703  13.434 1.00 52.53  ? 223 LYS A CD  1 
ATOM   1640 C CE  . LYS A 1 207 ? 15.738  -9.786  13.805 1.00 55.56  ? 223 LYS A CE  1 
ATOM   1641 N NZ  . LYS A 1 207 ? 15.223  -8.524  14.400 1.00 52.63  ? 223 LYS A NZ  1 
ATOM   1642 N N   . ARG A 1 208 ? 19.039  -13.913 17.211 1.00 40.80  ? 224 ARG A N   1 
ATOM   1643 C CA  . ARG A 1 208 ? 19.967  -14.371 18.248 1.00 37.71  ? 224 ARG A CA  1 
ATOM   1644 C C   . ARG A 1 208 ? 21.034  -13.300 18.493 1.00 33.34  ? 224 ARG A C   1 
ATOM   1645 O O   . ARG A 1 208 ? 22.212  -13.483 18.201 1.00 29.37  ? 224 ARG A O   1 
ATOM   1646 C CB  . ARG A 1 208 ? 20.523  -15.756 17.899 1.00 45.95  ? 224 ARG A CB  1 
ATOM   1647 C CG  . ARG A 1 208 ? 19.426  -16.787 17.656 1.00 50.70  ? 224 ARG A CG  1 
ATOM   1648 C CD  . ARG A 1 208 ? 19.817  -18.238 17.870 1.00 54.57  ? 224 ARG A CD  1 
ATOM   1649 N NE  . ARG A 1 208 ? 20.974  -18.644 17.093 1.00 50.96  ? 224 ARG A NE  1 
ATOM   1650 C CZ  . ARG A 1 208 ? 21.000  -18.779 15.780 1.00 54.68  ? 224 ARG A CZ  1 
ATOM   1651 N NH1 . ARG A 1 208 ? 19.920  -18.543 15.060 1.00 57.21  ? 224 ARG A NH1 1 
ATOM   1652 N NH2 . ARG A 1 208 ? 22.118  -19.159 15.189 1.00 64.57  ? 224 ARG A NH2 1 
ATOM   1653 N N   . THR A 1 209 ? 20.569  -12.164 19.034 1.00 31.50  ? 225 THR A N   1 
ATOM   1654 C CA  . THR A 1 209 ? 21.424  -11.070 19.452 1.00 27.13  ? 225 THR A CA  1 
ATOM   1655 C C   . THR A 1 209 ? 21.131  -10.693 20.910 1.00 28.39  ? 225 THR A C   1 
ATOM   1656 O O   . THR A 1 209 ? 20.070  -11.038 21.458 1.00 24.22  ? 225 THR A O   1 
ATOM   1657 C CB  . THR A 1 209 ? 21.275  -9.884  18.494 1.00 26.54  ? 225 THR A CB  1 
ATOM   1658 O OG1 . THR A 1 209 ? 19.984  -9.331  18.687 1.00 26.11  ? 225 THR A OG1 1 
ATOM   1659 C CG2 . THR A 1 209 ? 21.461  -10.263 17.040 1.00 28.65  ? 225 THR A CG2 1 
ATOM   1660 N N   . LEU A 1 210 ? 22.101  -9.973  21.505 1.00 26.47  ? 226 LEU A N   1 
ATOM   1661 C CA  . LEU A 1 210 ? 21.980  -9.350  22.818 1.00 25.37  ? 226 LEU A CA  1 
ATOM   1662 C C   . LEU A 1 210 ? 22.368  -7.881  22.688 1.00 25.70  ? 226 LEU A C   1 
ATOM   1663 O O   . LEU A 1 210 ? 23.194  -7.523  21.842 1.00 26.23  ? 226 LEU A O   1 
ATOM   1664 C CB  . LEU A 1 210 ? 22.917  -10.042 23.810 1.00 23.08  ? 226 LEU A CB  1 
ATOM   1665 C CG  . LEU A 1 210 ? 22.585  -11.494 24.147 1.00 24.40  ? 226 LEU A CG  1 
ATOM   1666 C CD1 . LEU A 1 210 ? 23.668  -12.115 25.016 1.00 24.35  ? 226 LEU A CD1 1 
ATOM   1667 C CD2 . LEU A 1 210 ? 21.245  -11.597 24.852 1.00 25.55  ? 226 LEU A CD2 1 
ATOM   1668 N N   . GLN A 1 211 ? 21.720  -7.036  23.495 1.00 23.16  ? 227 GLN A N   1 
ATOM   1669 C CA  . GLN A 1 211 ? 22.173  -5.668  23.678 1.00 24.38  ? 227 GLN A CA  1 
ATOM   1670 C C   . GLN A 1 211 ? 22.026  -5.318  25.149 1.00 23.30  ? 227 GLN A C   1 
ATOM   1671 O O   . GLN A 1 211 ? 20.978  -5.592  25.744 1.00 24.91  ? 227 GLN A O   1 
ATOM   1672 C CB  . GLN A 1 211 ? 21.399  -4.655  22.827 1.00 22.23  ? 227 GLN A CB  1 
ATOM   1673 C CG  . GLN A 1 211 ? 22.123  -3.322  22.764 1.00 23.59  ? 227 GLN A CG  1 
ATOM   1674 C CD  . GLN A 1 211 ? 21.385  -2.272  21.968 1.00 23.83  ? 227 GLN A CD  1 
ATOM   1675 O OE1 . GLN A 1 211 ? 20.183  -2.368  21.756 1.00 24.92  ? 227 GLN A OE1 1 
ATOM   1676 N NE2 . GLN A 1 211 ? 22.096  -1.238  21.553 1.00 24.38  ? 227 GLN A NE2 1 
ATOM   1677 N N   . VAL A 1 212 ? 23.075  -4.706  25.711 1.00 21.77  ? 228 VAL A N   1 
ATOM   1678 C CA  . VAL A 1 212 ? 23.080  -4.355  27.120 1.00 21.32  ? 228 VAL A CA  1 
ATOM   1679 C C   . VAL A 1 212 ? 22.765  -2.870  27.276 1.00 20.93  ? 228 VAL A C   1 
ATOM   1680 O O   . VAL A 1 212 ? 23.334  -2.042  26.583 1.00 22.70  ? 228 VAL A O   1 
ATOM   1681 C CB  . VAL A 1 212 ? 24.409  -4.682  27.811 1.00 20.56  ? 228 VAL A CB  1 
ATOM   1682 C CG1 . VAL A 1 212 ? 24.332  -4.319  29.289 1.00 21.95  ? 228 VAL A CG1 1 
ATOM   1683 C CG2 . VAL A 1 212 ? 24.805  -6.138  27.651 1.00 22.47  ? 228 VAL A CG2 1 
ATOM   1684 N N   . TRP A 1 213 ? 21.891  -2.579  28.237 1.00 21.67  ? 229 TRP A N   1 
ATOM   1685 C CA  . TRP A 1 213 ? 21.580  -1.233  28.693 1.00 22.83  ? 229 TRP A CA  1 
ATOM   1686 C C   . TRP A 1 213 ? 21.840  -1.155  30.197 1.00 21.74  ? 229 TRP A C   1 
ATOM   1687 O O   . TRP A 1 213 ? 21.602  -2.106  30.941 1.00 23.04  ? 229 TRP A O   1 
ATOM   1688 C CB  . TRP A 1 213 ? 20.122  -0.884  28.376 1.00 22.50  ? 229 TRP A CB  1 
ATOM   1689 C CG  . TRP A 1 213 ? 19.789  -0.869  26.912 1.00 24.19  ? 229 TRP A CG  1 
ATOM   1690 C CD1 . TRP A 1 213 ? 19.792  -1.921  26.046 1.00 23.68  ? 229 TRP A CD1 1 
ATOM   1691 C CD2 . TRP A 1 213 ? 19.420  0.297   26.141 1.00 24.04  ? 229 TRP A CD2 1 
ATOM   1692 N NE1 . TRP A 1 213 ? 19.443  -1.491  24.797 1.00 25.24  ? 229 TRP A NE1 1 
ATOM   1693 C CE2 . TRP A 1 213 ? 19.212  -0.143  24.816 1.00 23.89  ? 229 TRP A CE2 1 
ATOM   1694 C CE3 . TRP A 1 213 ? 19.251  1.654   26.448 1.00 23.52  ? 229 TRP A CE3 1 
ATOM   1695 C CZ2 . TRP A 1 213 ? 18.873  0.734   23.780 1.00 24.36  ? 229 TRP A CZ2 1 
ATOM   1696 C CZ3 . TRP A 1 213 ? 18.889  2.517   25.430 1.00 24.75  ? 229 TRP A CZ3 1 
ATOM   1697 C CH2 . TRP A 1 213 ? 18.719  2.064   24.114 1.00 23.20  ? 229 TRP A CH2 1 
ATOM   1698 N N   . TYR A 1 214 ? 22.362  -0.010  30.647 1.00 22.64  ? 230 TYR A N   1 
ATOM   1699 C CA  . TYR A 1 214 ? 22.780  0.145   32.025 1.00 21.72  ? 230 TYR A CA  1 
ATOM   1700 C C   . TYR A 1 214 ? 22.625  1.604   32.447 1.00 21.40  ? 230 TYR A C   1 
ATOM   1701 O O   . TYR A 1 214 ? 22.722  2.507   31.623 1.00 22.15  ? 230 TYR A O   1 
ATOM   1702 C CB  . TYR A 1 214 ? 24.234  -0.332  32.149 1.00 22.13  ? 230 TYR A CB  1 
ATOM   1703 C CG  . TYR A 1 214 ? 24.871  -0.062  33.501 1.00 22.66  ? 230 TYR A CG  1 
ATOM   1704 C CD1 . TYR A 1 214 ? 24.459  -0.781  34.612 1.00 22.04  ? 230 TYR A CD1 1 
ATOM   1705 C CD2 . TYR A 1 214 ? 25.808  0.952   33.684 1.00 21.57  ? 230 TYR A CD2 1 
ATOM   1706 C CE1 . TYR A 1 214 ? 24.990  -0.538  35.868 1.00 23.91  ? 230 TYR A CE1 1 
ATOM   1707 C CE2 . TYR A 1 214 ? 26.340  1.208   34.936 1.00 20.49  ? 230 TYR A CE2 1 
ATOM   1708 C CZ  . TYR A 1 214 ? 25.949  0.448   36.025 1.00 21.34  ? 230 TYR A CZ  1 
ATOM   1709 O OH  . TYR A 1 214 ? 26.450  0.631   37.275 1.00 19.63  ? 230 TYR A OH  1 
ATOM   1710 N N   . SER A 1 215 ? 22.369  1.810   33.736 1.00 20.42  ? 231 SER A N   1 
ATOM   1711 C CA  . SER A 1 215 ? 22.483  3.107   34.392 1.00 21.91  ? 231 SER A CA  1 
ATOM   1712 C C   . SER A 1 215 ? 22.574  2.884   35.901 1.00 20.45  ? 231 SER A C   1 
ATOM   1713 O O   . SER A 1 215 ? 22.473  1.742   36.361 1.00 20.35  ? 231 SER A O   1 
ATOM   1714 C CB  . SER A 1 215 ? 21.314  4.032   34.031 1.00 22.20  ? 231 SER A CB  1 
ATOM   1715 O OG  . SER A 1 215 ? 20.095  3.566   34.591 1.00 20.85  ? 231 SER A OG  1 
ATOM   1716 N N   . GLN A 1 216 ? 22.720  3.986   36.648 1.00 20.46  ? 232 GLN A N   1 
ATOM   1717 C CA  . GLN A 1 216 ? 22.705  3.984   38.106 1.00 22.01  ? 232 GLN A CA  1 
ATOM   1718 C C   . GLN A 1 216 ? 21.566  4.847   38.633 1.00 21.96  ? 232 GLN A C   1 
ATOM   1719 O O   . GLN A 1 216 ? 21.327  5.926   38.111 1.00 25.44  ? 232 GLN A O   1 
ATOM   1720 C CB  . GLN A 1 216 ? 24.045  4.503   38.650 1.00 23.28  ? 232 GLN A CB  1 
ATOM   1721 C CG  . GLN A 1 216 ? 25.238  3.663   38.197 1.00 23.86  ? 232 GLN A CG  1 
ATOM   1722 C CD  . GLN A 1 216 ? 26.514  3.959   38.948 1.00 25.28  ? 232 GLN A CD  1 
ATOM   1723 O OE1 . GLN A 1 216 ? 26.583  4.877   39.756 1.00 27.81  ? 232 GLN A OE1 1 
ATOM   1724 N NE2 . GLN A 1 216 ? 27.528  3.140   38.726 1.00 26.35  ? 232 GLN A NE2 1 
ATOM   1725 N N   . ASN A 1 217 ? 20.891  4.359   39.679 1.00 22.01  ? 233 ASN A N   1 
ATOM   1726 C CA  . ASN A 1 217 ? 19.962  5.127   40.492 1.00 24.80  ? 233 ASN A CA  1 
ATOM   1727 C C   . ASN A 1 217 ? 18.848  5.675   39.601 1.00 25.32  ? 233 ASN A C   1 
ATOM   1728 O O   . ASN A 1 217 ? 18.229  4.905   38.877 1.00 23.43  ? 233 ASN A O   1 
ATOM   1729 C CB  . ASN A 1 217 ? 20.702  6.185   41.323 1.00 24.84  ? 233 ASN A CB  1 
ATOM   1730 C CG  . ASN A 1 217 ? 21.710  5.586   42.288 1.00 26.99  ? 233 ASN A CG  1 
ATOM   1731 O OD1 . ASN A 1 217 ? 22.832  6.064   42.431 1.00 31.78  ? 233 ASN A OD1 1 
ATOM   1732 N ND2 . ASN A 1 217 ? 21.312  4.549   42.991 1.00 24.58  ? 233 ASN A ND2 1 
ATOM   1733 N N   . GLU A 1 218 ? 18.656  7.005   39.597 1.00 26.02  ? 234 GLU A N   1 
ATOM   1734 C CA  . GLU A 1 218 ? 17.521  7.613   38.924 1.00 26.54  ? 234 GLU A CA  1 
ATOM   1735 C C   . GLU A 1 218 ? 17.828  7.889   37.449 1.00 24.72  ? 234 GLU A C   1 
ATOM   1736 O O   . GLU A 1 218 ? 16.944  8.321   36.715 1.00 23.57  ? 234 GLU A O   1 
ATOM   1737 C CB  . GLU A 1 218 ? 17.085  8.882   39.673 1.00 29.42  ? 234 GLU A CB  1 
ATOM   1738 C CG  . GLU A 1 218 ? 17.977  10.099  39.473 1.00 30.66  ? 234 GLU A CG  1 
ATOM   1739 C CD  . GLU A 1 218 ? 19.293  10.199  40.233 1.00 34.79  ? 234 GLU A CD  1 
ATOM   1740 O OE1 . GLU A 1 218 ? 19.689  9.252   40.941 1.00 28.75  ? 234 GLU A OE1 1 
ATOM   1741 O OE2 . GLU A 1 218 ? 19.954  11.238  40.065 1.00 38.55  ? 234 GLU A OE2 1 
ATOM   1742 N N   . ASN A 1 219 ? 19.060  7.635   37.004 1.00 23.71  ? 235 ASN A N   1 
ATOM   1743 C CA  . ASN A 1 219 ? 19.436  7.926   35.626 1.00 25.77  ? 235 ASN A CA  1 
ATOM   1744 C C   . ASN A 1 219 ? 18.764  6.941   34.666 1.00 25.57  ? 235 ASN A C   1 
ATOM   1745 O O   . ASN A 1 219 ? 18.745  5.736   34.901 1.00 26.87  ? 235 ASN A O   1 
ATOM   1746 C CB  . ASN A 1 219 ? 20.954  7.908   35.446 1.00 25.54  ? 235 ASN A CB  1 
ATOM   1747 C CG  . ASN A 1 219 ? 21.652  8.994   36.250 1.00 28.97  ? 235 ASN A CG  1 
ATOM   1748 O OD1 . ASN A 1 219 ? 22.364  8.710   37.211 1.00 28.94  ? 235 ASN A OD1 1 
ATOM   1749 N ND2 . ASN A 1 219 ? 21.448  10.242  35.874 1.00 27.64  ? 235 ASN A ND2 1 
ATOM   1750 N N   . ASN A 1 220 ? 18.266  7.446   33.535 1.00 27.33  ? 236 ASN A N   1 
ATOM   1751 C CA  . ASN A 1 220 ? 17.680  6.601   32.507 1.00 25.63  ? 236 ASN A CA  1 
ATOM   1752 C C   . ASN A 1 220 ? 18.721  5.620   31.967 1.00 24.97  ? 236 ASN A C   1 
ATOM   1753 O O   . ASN A 1 220 ? 19.884  5.968   31.774 1.00 19.67  ? 236 ASN A O   1 
ATOM   1754 C CB  . ASN A 1 220 ? 17.153  7.442   31.345 1.00 30.18  ? 236 ASN A CB  1 
ATOM   1755 C CG  . ASN A 1 220 ? 16.020  8.364   31.746 1.00 32.62  ? 236 ASN A CG  1 
ATOM   1756 O OD1 . ASN A 1 220 ? 15.320  8.120   32.726 1.00 37.61  ? 236 ASN A OD1 1 
ATOM   1757 N ND2 . ASN A 1 220 ? 15.826  9.411   30.975 1.00 35.15  ? 236 ASN A ND2 1 
ATOM   1758 N N   . LEU A 1 221 ? 18.270  4.403   31.640 1.00 23.27  ? 237 LEU A N   1 
ATOM   1759 C CA  . LEU A 1 221 ? 19.084  3.416   30.941 1.00 21.67  ? 237 LEU A CA  1 
ATOM   1760 C C   . LEU A 1 221 ? 19.643  3.997   29.634 1.00 22.65  ? 237 LEU A C   1 
ATOM   1761 O O   . LEU A 1 221 ? 18.904  4.619   28.869 1.00 21.84  ? 237 LEU A O   1 
ATOM   1762 C CB  . LEU A 1 221 ? 18.179  2.221   30.626 1.00 22.66  ? 237 LEU A CB  1 
ATOM   1763 C CG  . LEU A 1 221 ? 17.627  1.404   31.792 1.00 23.62  ? 237 LEU A CG  1 
ATOM   1764 C CD1 . LEU A 1 221 ? 16.627  0.362   31.264 1.00 26.88  ? 237 LEU A CD1 1 
ATOM   1765 C CD2 . LEU A 1 221 ? 18.751  0.689   32.520 1.00 23.70  ? 237 LEU A CD2 1 
ATOM   1766 N N   . VAL A 1 222 ? 20.938  3.740   29.381 1.00 21.70  ? 238 VAL A N   1 
ATOM   1767 C CA  . VAL A 1 222 ? 21.604  4.026   28.124 1.00 22.72  ? 238 VAL A CA  1 
ATOM   1768 C C   . VAL A 1 222 ? 22.210  2.725   27.599 1.00 22.63  ? 238 VAL A C   1 
ATOM   1769 O O   . VAL A 1 222 ? 22.566  1.830   28.360 1.00 21.61  ? 238 VAL A O   1 
ATOM   1770 C CB  . VAL A 1 222 ? 22.695  5.112   28.278 1.00 23.54  ? 238 VAL A CB  1 
ATOM   1771 C CG1 . VAL A 1 222 ? 22.184  6.385   28.933 1.00 23.85  ? 238 VAL A CG1 1 
ATOM   1772 C CG2 . VAL A 1 222 ? 23.892  4.601   29.062 1.00 25.77  ? 238 VAL A CG2 1 
ATOM   1773 N N   . TRP A 1 223 ? 22.385  2.636   26.277 1.00 25.01  ? 239 TRP A N   1 
ATOM   1774 C CA  . TRP A 1 223 ? 22.970  1.440   25.686 1.00 25.43  ? 239 TRP A CA  1 
ATOM   1775 C C   . TRP A 1 223 ? 24.484  1.437   25.870 1.00 23.47  ? 239 TRP A C   1 
ATOM   1776 O O   . TRP A 1 223 ? 25.121  2.461   25.665 1.00 21.59  ? 239 TRP A O   1 
ATOM   1777 C CB  . TRP A 1 223 ? 22.569  1.262   24.213 1.00 25.00  ? 239 TRP A CB  1 
ATOM   1778 C CG  . TRP A 1 223 ? 22.919  2.349   23.231 1.00 23.94  ? 239 TRP A CG  1 
ATOM   1779 C CD1 . TRP A 1 223 ? 22.273  3.529   23.013 1.00 24.41  ? 239 TRP A CD1 1 
ATOM   1780 C CD2 . TRP A 1 223 ? 23.936  2.266   22.219 1.00 23.97  ? 239 TRP A CD2 1 
ATOM   1781 N NE1 . TRP A 1 223 ? 22.847  4.201   21.962 1.00 22.61  ? 239 TRP A NE1 1 
ATOM   1782 C CE2 . TRP A 1 223 ? 23.861  3.451   21.456 1.00 25.05  ? 239 TRP A CE2 1 
ATOM   1783 C CE3 . TRP A 1 223 ? 24.921  1.326   21.907 1.00 25.50  ? 239 TRP A CE3 1 
ATOM   1784 C CZ2 . TRP A 1 223 ? 24.736  3.711   20.409 1.00 27.17  ? 239 TRP A CZ2 1 
ATOM   1785 C CZ3 . TRP A 1 223 ? 25.762  1.567   20.849 1.00 24.90  ? 239 TRP A CZ3 1 
ATOM   1786 C CH2 . TRP A 1 223 ? 25.667  2.745   20.108 1.00 25.73  ? 239 TRP A CH2 1 
ATOM   1787 N N   . VAL A 1 224 ? 25.038  0.284   26.282 1.00 20.48  ? 240 VAL A N   1 
ATOM   1788 C CA  . VAL A 1 224 ? 26.452  0.184   26.602 1.00 21.18  ? 240 VAL A CA  1 
ATOM   1789 C C   . VAL A 1 224 ? 27.130  -0.895  25.755 1.00 20.97  ? 240 VAL A C   1 
ATOM   1790 O O   . VAL A 1 224 ? 28.335  -1.077  25.862 1.00 21.65  ? 240 VAL A O   1 
ATOM   1791 C CB  . VAL A 1 224 ? 26.681  -0.067  28.111 1.00 20.56  ? 240 VAL A CB  1 
ATOM   1792 C CG1 . VAL A 1 224 ? 26.216  1.117   28.940 1.00 22.09  ? 240 VAL A CG1 1 
ATOM   1793 C CG2 . VAL A 1 224 ? 26.019  -1.342  28.619 1.00 19.03  ? 240 VAL A CG2 1 
ATOM   1794 N N   . THR A 1 225 ? 26.358  -1.645  24.963 1.00 20.28  ? 241 THR A N   1 
ATOM   1795 C CA  . THR A 1 225 ? 26.887  -2.447  23.874 1.00 20.70  ? 241 THR A CA  1 
ATOM   1796 C C   . THR A 1 225 ? 26.054  -2.157  22.635 1.00 22.29  ? 241 THR A C   1 
ATOM   1797 O O   . THR A 1 225 ? 24.884  -1.789  22.760 1.00 22.53  ? 241 THR A O   1 
ATOM   1798 C CB  . THR A 1 225 ? 26.799  -3.968  24.098 1.00 19.71  ? 241 THR A CB  1 
ATOM   1799 O OG1 . THR A 1 225 ? 25.422  -4.332  24.071 1.00 22.29  ? 241 THR A OG1 1 
ATOM   1800 C CG2 . THR A 1 225 ? 27.409  -4.428  25.398 1.00 19.55  ? 241 THR A CG2 1 
ATOM   1801 N N   . PRO A 1 226 ? 26.625  -2.346  21.423 1.00 24.55  ? 242 PRO A N   1 
ATOM   1802 C CA  . PRO A 1 226 ? 25.823  -2.445  20.216 1.00 26.28  ? 242 PRO A CA  1 
ATOM   1803 C C   . PRO A 1 226 ? 24.966  -3.703  20.307 1.00 29.47  ? 242 PRO A C   1 
ATOM   1804 O O   . PRO A 1 226 ? 25.038  -4.428  21.307 1.00 29.84  ? 242 PRO A O   1 
ATOM   1805 C CB  . PRO A 1 226 ? 26.806  -2.611  19.051 1.00 27.64  ? 242 PRO A CB  1 
ATOM   1806 C CG  . PRO A 1 226 ? 28.169  -2.855  19.690 1.00 30.01  ? 242 PRO A CG  1 
ATOM   1807 C CD  . PRO A 1 226 ? 28.065  -2.517  21.166 1.00 26.73  ? 242 PRO A CD  1 
ATOM   1808 N N   . VAL A 1 227 ? 24.200  -3.973  19.239 1.00 27.36  ? 243 VAL A N   1 
ATOM   1809 C CA  . VAL A 1 227 ? 23.531  -5.261  19.087 1.00 28.31  ? 243 VAL A CA  1 
ATOM   1810 C C   . VAL A 1 227 ? 24.593  -6.295  18.733 1.00 27.27  ? 243 VAL A C   1 
ATOM   1811 O O   . VAL A 1 227 ? 25.341  -6.120  17.782 1.00 27.67  ? 243 VAL A O   1 
ATOM   1812 C CB  . VAL A 1 227 ? 22.402  -5.191  18.043 1.00 26.76  ? 243 VAL A CB  1 
ATOM   1813 C CG1 . VAL A 1 227 ? 21.812  -6.558  17.728 1.00 27.97  ? 243 VAL A CG1 1 
ATOM   1814 C CG2 . VAL A 1 227 ? 21.316  -4.221  18.481 1.00 28.97  ? 243 VAL A CG2 1 
ATOM   1815 N N   . LEU A 1 228 ? 24.663  -7.392  19.495 1.00 28.23  ? 244 LEU A N   1 
ATOM   1816 C CA  . LEU A 1 228 ? 25.790  -8.303  19.351 1.00 28.20  ? 244 LEU A CA  1 
ATOM   1817 C C   . LEU A 1 228 ? 25.283  -9.704  19.036 1.00 28.84  ? 244 LEU A C   1 
ATOM   1818 O O   . LEU A 1 228 ? 24.311  -10.153 19.633 1.00 26.26  ? 244 LEU A O   1 
ATOM   1819 C CB  . LEU A 1 228 ? 26.593  -8.314  20.653 1.00 29.42  ? 244 LEU A CB  1 
ATOM   1820 C CG  . LEU A 1 228 ? 27.358  -7.036  20.972 1.00 31.14  ? 244 LEU A CG  1 
ATOM   1821 C CD1 . LEU A 1 228 ? 27.873  -7.088  22.404 1.00 32.19  ? 244 LEU A CD1 1 
ATOM   1822 C CD2 . LEU A 1 228 ? 28.501  -6.823  19.984 1.00 29.22  ? 244 LEU A CD2 1 
ATOM   1823 N N   . PRO A 1 229 ? 25.938  -10.444 18.122 1.00 32.28  ? 245 PRO A N   1 
ATOM   1824 C CA  . PRO A 1 229 ? 25.548  -11.824 17.857 1.00 31.11  ? 245 PRO A CA  1 
ATOM   1825 C C   . PRO A 1 229 ? 25.686  -12.694 19.105 1.00 29.09  ? 245 PRO A C   1 
ATOM   1826 O O   . PRO A 1 229 ? 26.647  -12.544 19.858 1.00 31.17  ? 245 PRO A O   1 
ATOM   1827 C CB  . PRO A 1 229 ? 26.509  -12.260 16.741 1.00 32.29  ? 245 PRO A CB  1 
ATOM   1828 C CG  . PRO A 1 229 ? 27.691  -11.318 16.859 1.00 33.40  ? 245 PRO A CG  1 
ATOM   1829 C CD  . PRO A 1 229 ? 27.094  -10.011 17.317 1.00 33.46  ? 245 PRO A CD  1 
ATOM   1830 N N   . ASN A 1 230 ? 24.736  -13.624 19.288 1.00 28.06  ? 246 ASN A N   1 
ATOM   1831 C CA  . ASN A 1 230 ? 24.745  -14.562 20.400 1.00 28.58  ? 246 ASN A CA  1 
ATOM   1832 C C   . ASN A 1 230 ? 24.527  -15.969 19.839 1.00 28.40  ? 246 ASN A C   1 
ATOM   1833 O O   . ASN A 1 230 ? 23.598  -16.663 20.244 1.00 31.01  ? 246 ASN A O   1 
ATOM   1834 C CB  . ASN A 1 230 ? 23.673  -14.188 21.443 1.00 25.80  ? 246 ASN A CB  1 
ATOM   1835 C CG  . ASN A 1 230 ? 23.809  -14.876 22.790 1.00 25.38  ? 246 ASN A CG  1 
ATOM   1836 O OD1 . ASN A 1 230 ? 22.830  -15.015 23.515 1.00 29.83  ? 246 ASN A OD1 1 
ATOM   1837 N ND2 . ASN A 1 230 ? 24.995  -15.339 23.121 1.00 23.13  ? 246 ASN A ND2 1 
ATOM   1838 N N   . GLU A 1 231 ? 25.400  -16.394 18.924 1.00 33.02  ? 247 GLU A N   1 
ATOM   1839 C CA  . GLU A 1 231 ? 25.036  -17.419 17.958 1.00 37.06  ? 247 GLU A CA  1 
ATOM   1840 C C   . GLU A 1 231 ? 25.270  -18.837 18.483 1.00 36.47  ? 247 GLU A C   1 
ATOM   1841 O O   . GLU A 1 231 ? 25.020  -19.787 17.746 1.00 35.27  ? 247 GLU A O   1 
ATOM   1842 C CB  . GLU A 1 231 ? 25.811  -17.190 16.660 1.00 43.68  ? 247 GLU A CB  1 
ATOM   1843 C CG  . GLU A 1 231 ? 25.337  -15.976 15.878 1.00 48.67  ? 247 GLU A CG  1 
ATOM   1844 C CD  . GLU A 1 231 ? 24.151  -16.246 14.966 1.00 51.95  ? 247 GLU A CD  1 
ATOM   1845 O OE1 . GLU A 1 231 ? 23.293  -17.067 15.344 1.00 50.71  ? 247 GLU A OE1 1 
ATOM   1846 O OE2 . GLU A 1 231 ? 24.065  -15.609 13.896 1.00 51.64  ? 247 GLU A OE2 1 
ATOM   1847 N N   . THR A 1 232 ? 25.749  -18.992 19.730 1.00 33.88  ? 248 THR A N   1 
ATOM   1848 C CA  . THR A 1 232 ? 25.931  -20.315 20.309 1.00 32.30  ? 248 THR A CA  1 
ATOM   1849 C C   . THR A 1 232 ? 24.654  -20.792 20.998 1.00 32.20  ? 248 THR A C   1 
ATOM   1850 O O   . THR A 1 232 ? 24.600  -21.925 21.472 1.00 29.20  ? 248 THR A O   1 
ATOM   1851 C CB  . THR A 1 232 ? 27.117  -20.371 21.276 1.00 32.88  ? 248 THR A CB  1 
ATOM   1852 O OG1 . THR A 1 232 ? 26.909  -19.501 22.394 1.00 33.32  ? 248 THR A OG1 1 
ATOM   1853 C CG2 . THR A 1 232 ? 28.420  -20.064 20.572 1.00 34.93  ? 248 THR A CG2 1 
ATOM   1854 N N   . VAL A 1 233 ? 23.646  -19.913 21.068 1.00 29.71  ? 249 VAL A N   1 
ATOM   1855 C CA  . VAL A 1 233 ? 22.318  -20.279 21.520 1.00 34.77  ? 249 VAL A CA  1 
ATOM   1856 C C   . VAL A 1 233 ? 21.756  -21.307 20.539 1.00 37.69  ? 249 VAL A C   1 
ATOM   1857 O O   . VAL A 1 233 ? 21.910  -21.168 19.330 1.00 34.94  ? 249 VAL A O   1 
ATOM   1858 C CB  . VAL A 1 233 ? 21.406  -19.038 21.632 1.00 36.64  ? 249 VAL A CB  1 
ATOM   1859 C CG1 . VAL A 1 233 ? 19.943  -19.405 21.836 1.00 40.61  ? 249 VAL A CG1 1 
ATOM   1860 C CG2 . VAL A 1 233 ? 21.860  -18.103 22.742 1.00 36.87  ? 249 VAL A CG2 1 
ATOM   1861 N N   . LYS A 1 234 ? 21.092  -22.338 21.068 1.00 39.32  ? 250 LYS A N   1 
ATOM   1862 C CA  . LYS A 1 234 ? 20.557  -23.391 20.219 1.00 39.28  ? 250 LYS A CA  1 
ATOM   1863 C C   . LYS A 1 234 ? 19.355  -22.869 19.442 1.00 36.28  ? 250 LYS A C   1 
ATOM   1864 O O   . LYS A 1 234 ? 18.646  -21.969 19.890 1.00 41.44  ? 250 LYS A O   1 
ATOM   1865 C CB  . LYS A 1 234 ? 20.160  -24.613 21.049 1.00 38.51  ? 250 LYS A CB  1 
ATOM   1866 C CG  . LYS A 1 234 ? 21.329  -25.514 21.405 1.00 36.64  ? 250 LYS A CG  1 
ATOM   1867 C CD  . LYS A 1 234 ? 20.999  -26.586 22.391 1.00 35.86  ? 250 LYS A CD  1 
ATOM   1868 C CE  . LYS A 1 234 ? 22.144  -27.565 22.532 1.00 36.41  ? 250 LYS A CE  1 
ATOM   1869 N NZ  . LYS A 1 234 ? 22.142  -28.193 23.870 1.00 39.63  ? 250 LYS A NZ  1 
ATOM   1870 N N   . ARG A 1 235 ? 19.166  -23.439 18.255 1.00 38.35  ? 251 ARG A N   1 
ATOM   1871 C CA  . ARG A 1 235 ? 18.052  -23.098 17.388 1.00 40.57  ? 251 ARG A CA  1 
ATOM   1872 C C   . ARG A 1 235 ? 16.791  -23.696 17.990 1.00 35.42  ? 251 ARG A C   1 
ATOM   1873 O O   . ARG A 1 235 ? 16.855  -24.730 18.657 1.00 34.39  ? 251 ARG A O   1 
ATOM   1874 C CB  . ARG A 1 235 ? 18.223  -23.663 15.972 1.00 45.93  ? 251 ARG A CB  1 
ATOM   1875 C CG  . ARG A 1 235 ? 19.517  -23.287 15.257 1.00 51.38  ? 251 ARG A CG  1 
ATOM   1876 C CD  . ARG A 1 235 ? 19.687  -21.790 15.054 1.00 63.06  ? 251 ARG A CD  1 
ATOM   1877 N NE  . ARG A 1 235 ? 20.363  -21.425 13.805 1.00 66.00  ? 251 ARG A NE  1 
ATOM   1878 C CZ  . ARG A 1 235 ? 19.876  -21.643 12.583 1.00 63.77  ? 251 ARG A CZ  1 
ATOM   1879 N NH1 . ARG A 1 235 ? 18.739  -22.298 12.410 1.00 60.67  ? 251 ARG A NH1 1 
ATOM   1880 N NH2 . ARG A 1 235 ? 20.561  -21.249 11.523 1.00 68.44  ? 251 ARG A NH2 1 
ATOM   1881 N N   . GLY A 1 236 ? 15.668  -23.027 17.731 1.00 34.57  ? 252 GLY A N   1 
ATOM   1882 C CA  . GLY A 1 236 ? 14.355  -23.540 18.070 1.00 33.22  ? 252 GLY A CA  1 
ATOM   1883 C C   . GLY A 1 236 ? 14.046  -23.399 19.558 1.00 34.56  ? 252 GLY A C   1 
ATOM   1884 O O   . GLY A 1 236 ? 14.574  -22.510 20.233 1.00 37.88  ? 252 GLY A O   1 
ATOM   1885 N N   . THR A 1 237 ? 13.168  -24.278 20.041 1.00 30.08  ? 253 THR A N   1 
ATOM   1886 C CA  . THR A 1 237 ? 12.684  -24.256 21.415 1.00 33.03  ? 253 THR A CA  1 
ATOM   1887 C C   . THR A 1 237 ? 13.805  -24.581 22.418 1.00 31.87  ? 253 THR A C   1 
ATOM   1888 O O   . THR A 1 237 ? 13.709  -24.230 23.591 1.00 31.83  ? 253 THR A O   1 
ATOM   1889 C CB  . THR A 1 237 ? 11.524  -25.248 21.596 1.00 34.97  ? 253 THR A CB  1 
ATOM   1890 O OG1 . THR A 1 237 ? 12.051  -26.523 21.240 1.00 37.06  ? 253 THR A OG1 1 
ATOM   1891 C CG2 . THR A 1 237 ? 10.304  -24.945 20.755 1.00 34.66  ? 253 THR A CG2 1 
ATOM   1892 N N   . ALA A 1 238 ? 14.885  -25.233 21.958 1.00 34.45  ? 254 ALA A N   1 
ATOM   1893 C CA  . ALA A 1 238 ? 16.000  -25.595 22.825 1.00 34.31  ? 254 ALA A CA  1 
ATOM   1894 C C   . ALA A 1 238 ? 16.831  -24.364 23.196 1.00 36.10  ? 254 ALA A C   1 
ATOM   1895 O O   . ALA A 1 238 ? 17.711  -24.463 24.049 1.00 38.62  ? 254 ALA A O   1 
ATOM   1896 C CB  . ALA A 1 238 ? 16.870  -26.638 22.155 1.00 33.08  ? 254 ALA A CB  1 
ATOM   1897 N N   . GLY A 1 239 ? 16.571  -23.224 22.545 1.00 33.72  ? 255 GLY A N   1 
ATOM   1898 C CA  . GLY A 1 239 ? 17.301  -21.989 22.820 1.00 35.27  ? 255 GLY A CA  1 
ATOM   1899 C C   . GLY A 1 239 ? 16.616  -21.151 23.893 1.00 33.92  ? 255 GLY A C   1 
ATOM   1900 O O   . GLY A 1 239 ? 17.239  -20.247 24.448 1.00 35.77  ? 255 GLY A O   1 
ATOM   1901 N N   . ARG A 1 240 ? 15.340  -21.480 24.154 1.00 31.02  ? 256 ARG A N   1 
ATOM   1902 C CA  . ARG A 1 240 ? 14.495  -20.779 25.101 1.00 31.42  ? 256 ARG A CA  1 
ATOM   1903 C C   . ARG A 1 240 ? 14.489  -21.451 26.473 1.00 28.92  ? 256 ARG A C   1 
ATOM   1904 O O   . ARG A 1 240 ? 14.839  -22.616 26.626 1.00 29.08  ? 256 ARG A O   1 
ATOM   1905 C CB  . ARG A 1 240 ? 13.045  -20.723 24.611 1.00 31.64  ? 256 ARG A CB  1 
ATOM   1906 C CG  . ARG A 1 240 ? 12.793  -19.680 23.536 1.00 33.54  ? 256 ARG A CG  1 
ATOM   1907 C CD  . ARG A 1 240 ? 13.378  -19.994 22.171 1.00 33.38  ? 256 ARG A CD  1 
ATOM   1908 N NE  . ARG A 1 240 ? 12.797  -19.072 21.215 1.00 35.24  ? 256 ARG A NE  1 
ATOM   1909 C CZ  . ARG A 1 240 ? 13.018  -19.060 19.907 1.00 36.39  ? 256 ARG A CZ  1 
ATOM   1910 N NH1 . ARG A 1 240 ? 13.778  -19.961 19.313 1.00 37.41  ? 256 ARG A NH1 1 
ATOM   1911 N NH2 . ARG A 1 240 ? 12.434  -18.133 19.181 1.00 38.46  ? 256 ARG A NH2 1 
ATOM   1912 N N   . GLY A 1 241 ? 14.016  -20.703 27.469 1.00 28.04  ? 257 GLY A N   1 
ATOM   1913 C CA  . GLY A 1 241 ? 14.081  -21.168 28.842 1.00 28.97  ? 257 GLY A CA  1 
ATOM   1914 C C   . GLY A 1 241 ? 13.488  -20.168 29.825 1.00 27.18  ? 257 GLY A C   1 
ATOM   1915 O O   . GLY A 1 241 ? 12.917  -19.158 29.431 1.00 27.46  ? 257 GLY A O   1 
ATOM   1916 N N   . ASP A 1 242 ? 13.656  -20.495 31.101 1.00 26.39  ? 258 ASP A N   1 
ATOM   1917 C CA  . ASP A 1 242 ? 13.101  -19.773 32.234 1.00 26.34  ? 258 ASP A CA  1 
ATOM   1918 C C   . ASP A 1 242 ? 13.987  -18.602 32.655 1.00 27.83  ? 258 ASP A C   1 
ATOM   1919 O O   . ASP A 1 242 ? 15.212  -18.674 32.592 1.00 27.58  ? 258 ASP A O   1 
ATOM   1920 C CB  . ASP A 1 242 ? 12.992  -20.708 33.439 1.00 28.14  ? 258 ASP A CB  1 
ATOM   1921 C CG  . ASP A 1 242 ? 12.087  -21.901 33.170 1.00 32.30  ? 258 ASP A CG  1 
ATOM   1922 O OD1 . ASP A 1 242 ? 10.994  -21.676 32.599 1.00 31.31  ? 258 ASP A OD1 1 
ATOM   1923 O OD2 . ASP A 1 242 ? 12.499  -23.032 33.504 1.00 32.24  ? 258 ASP A OD2 1 
ATOM   1924 N N   . PHE A 1 243 ? 13.347  -17.563 33.190 1.00 28.20  ? 259 PHE A N   1 
ATOM   1925 C CA  . PHE A 1 243 ? 14.069  -16.411 33.686 1.00 24.94  ? 259 PHE A CA  1 
ATOM   1926 C C   . PHE A 1 243 ? 14.307  -16.590 35.181 1.00 22.28  ? 259 PHE A C   1 
ATOM   1927 O O   . PHE A 1 243 ? 13.333  -16.687 35.911 1.00 21.95  ? 259 PHE A O   1 
ATOM   1928 C CB  . PHE A 1 243 ? 13.267  -15.146 33.385 1.00 24.79  ? 259 PHE A CB  1 
ATOM   1929 C CG  . PHE A 1 243 ? 13.928  -13.904 33.917 1.00 24.06  ? 259 PHE A CG  1 
ATOM   1930 C CD1 . PHE A 1 243 ? 15.106  -13.450 33.361 1.00 23.79  ? 259 PHE A CD1 1 
ATOM   1931 C CD2 . PHE A 1 243 ? 13.434  -13.274 35.037 1.00 23.64  ? 259 PHE A CD2 1 
ATOM   1932 C CE1 . PHE A 1 243 ? 15.728  -12.318 33.865 1.00 22.80  ? 259 PHE A CE1 1 
ATOM   1933 C CE2 . PHE A 1 243 ? 14.047  -12.137 35.535 1.00 24.98  ? 259 PHE A CE2 1 
ATOM   1934 C CZ  . PHE A 1 243 ? 15.201  -11.666 34.953 1.00 24.13  ? 259 PHE A CZ  1 
ATOM   1935 N N   . HIS A 1 244 ? 15.579  -16.672 35.614 1.00 23.23  ? 260 HIS A N   1 
ATOM   1936 C CA  . HIS A 1 244 ? 15.921  -16.757 37.034 1.00 21.76  ? 260 HIS A CA  1 
ATOM   1937 C C   . HIS A 1 244 ? 16.575  -15.479 37.563 1.00 20.59  ? 260 HIS A C   1 
ATOM   1938 O O   . HIS A 1 244 ? 17.369  -14.823 36.881 1.00 22.00  ? 260 HIS A O   1 
ATOM   1939 C CB  . HIS A 1 244 ? 16.967  -17.845 37.323 1.00 23.67  ? 260 HIS A CB  1 
ATOM   1940 C CG  . HIS A 1 244 ? 16.595  -19.254 36.990 1.00 27.20  ? 260 HIS A CG  1 
ATOM   1941 N ND1 . HIS A 1 244 ? 16.904  -20.299 37.829 1.00 28.75  ? 260 HIS A ND1 1 
ATOM   1942 C CD2 . HIS A 1 244 ? 16.025  -19.815 35.900 1.00 30.09  ? 260 HIS A CD2 1 
ATOM   1943 C CE1 . HIS A 1 244 ? 16.521  -21.438 37.256 1.00 31.28  ? 260 HIS A CE1 1 
ATOM   1944 N NE2 . HIS A 1 244 ? 15.984  -21.167 36.087 1.00 29.45  ? 260 HIS A NE2 1 
ATOM   1945 N N   . PHE A 1 245 ? 16.304  -15.144 38.823 1.00 21.38  ? 261 PHE A N   1 
ATOM   1946 C CA  . PHE A 1 245 ? 17.143  -14.164 39.490 1.00 22.45  ? 261 PHE A CA  1 
ATOM   1947 C C   . PHE A 1 245 ? 17.293  -14.503 40.969 1.00 23.49  ? 261 PHE A C   1 
ATOM   1948 O O   . PHE A 1 245 ? 16.363  -14.989 41.624 1.00 26.04  ? 261 PHE A O   1 
ATOM   1949 C CB  . PHE A 1 245 ? 16.646  -12.733 39.286 1.00 20.47  ? 261 PHE A CB  1 
ATOM   1950 C CG  . PHE A 1 245 ? 15.351  -12.383 39.948 1.00 21.58  ? 261 PHE A CG  1 
ATOM   1951 C CD1 . PHE A 1 245 ? 14.140  -12.856 39.451 1.00 22.37  ? 261 PHE A CD1 1 
ATOM   1952 C CD2 . PHE A 1 245 ? 15.341  -11.561 41.068 1.00 20.31  ? 261 PHE A CD2 1 
ATOM   1953 C CE1 . PHE A 1 245 ? 12.951  -12.500 40.066 1.00 22.04  ? 261 PHE A CE1 1 
ATOM   1954 C CE2 . PHE A 1 245 ? 14.152  -11.203 41.669 1.00 21.71  ? 261 PHE A CE2 1 
ATOM   1955 C CZ  . PHE A 1 245 ? 12.957  -11.674 41.166 1.00 20.99  ? 261 PHE A CZ  1 
ATOM   1956 N N   . GLY A 1 246 ? 18.500  -14.224 41.472 1.00 21.72  ? 262 GLY A N   1 
ATOM   1957 C CA  . GLY A 1 246 ? 18.835  -14.535 42.848 1.00 22.46  ? 262 GLY A CA  1 
ATOM   1958 C C   . GLY A 1 246 ? 20.348  -14.581 43.031 1.00 20.82  ? 262 GLY A C   1 
ATOM   1959 O O   . GLY A 1 246 ? 21.030  -13.624 42.668 1.00 20.53  ? 262 GLY A O   1 
ATOM   1960 N N   . ILE A 1 247 ? 20.826  -15.695 43.592 1.00 20.98  ? 263 ILE A N   1 
ATOM   1961 C CA  . ILE A 1 247 ? 22.246  -15.974 43.753 1.00 22.55  ? 263 ILE A CA  1 
ATOM   1962 C C   . ILE A 1 247 ? 22.459  -17.471 43.525 1.00 22.82  ? 263 ILE A C   1 
ATOM   1963 O O   . ILE A 1 247 ? 21.913  -18.272 44.254 1.00 21.73  ? 263 ILE A O   1 
ATOM   1964 C CB  . ILE A 1 247 ? 22.766  -15.611 45.155 1.00 22.65  ? 263 ILE A CB  1 
ATOM   1965 C CG1 . ILE A 1 247 ? 22.416  -14.188 45.594 1.00 21.28  ? 263 ILE A CG1 1 
ATOM   1966 C CG2 . ILE A 1 247 ? 24.281  -15.846 45.183 1.00 24.45  ? 263 ILE A CG2 1 
ATOM   1967 C CD1 . ILE A 1 247 ? 22.645  -13.937 47.053 1.00 23.08  ? 263 ILE A CD1 1 
ATOM   1968 N N   . LEU A 1 248 ? 23.257  -17.822 42.521 1.00 21.84  ? 264 LEU A N   1 
ATOM   1969 C CA  . LEU A 1 248 ? 23.845  -19.145 42.404 1.00 23.82  ? 264 LEU A CA  1 
ATOM   1970 C C   . LEU A 1 248 ? 25.349  -19.004 42.605 1.00 21.94  ? 264 LEU A C   1 
ATOM   1971 O O   . LEU A 1 248 ? 26.060  -18.444 41.768 1.00 21.08  ? 264 LEU A O   1 
ATOM   1972 C CB  . LEU A 1 248 ? 23.477  -19.726 41.038 1.00 22.90  ? 264 LEU A CB  1 
ATOM   1973 C CG  . LEU A 1 248 ? 24.241  -20.945 40.529 1.00 24.29  ? 264 LEU A CG  1 
ATOM   1974 C CD1 . LEU A 1 248 ? 24.243  -22.095 41.502 1.00 26.46  ? 264 LEU A CD1 1 
ATOM   1975 C CD2 . LEU A 1 248 ? 23.626  -21.412 39.213 1.00 25.68  ? 264 LEU A CD2 1 
ATOM   1976 N N   . LYS A 1 249 ? 25.799  -19.470 43.765 1.00 20.72  ? 265 LYS A N   1 
ATOM   1977 C CA  . LYS A 1 249 ? 27.196  -19.362 44.143 1.00 20.52  ? 265 LYS A CA  1 
ATOM   1978 C C   . LYS A 1 249 ? 27.904  -20.682 43.866 1.00 21.63  ? 265 LYS A C   1 
ATOM   1979 O O   . LYS A 1 249 ? 27.524  -21.724 44.403 1.00 21.47  ? 265 LYS A O   1 
ATOM   1980 C CB  . LYS A 1 249 ? 27.328  -19.035 45.631 1.00 20.53  ? 265 LYS A CB  1 
ATOM   1981 C CG  . LYS A 1 249 ? 28.743  -18.768 46.112 1.00 21.90  ? 265 LYS A CG  1 
ATOM   1982 C CD  . LYS A 1 249 ? 28.771  -18.407 47.584 1.00 21.21  ? 265 LYS A CD  1 
ATOM   1983 C CE  . LYS A 1 249 ? 30.184  -18.157 48.056 1.00 22.44  ? 265 LYS A CE  1 
ATOM   1984 N NZ  . LYS A 1 249 ? 30.262  -17.844 49.500 1.00 22.90  ? 265 LYS A NZ  1 
ATOM   1985 N N   . LEU A 1 250 ? 28.969  -20.587 43.071 1.00 22.21  ? 266 LEU A N   1 
ATOM   1986 C CA  . LEU A 1 250 ? 29.825  -21.710 42.751 1.00 22.97  ? 266 LEU A CA  1 
ATOM   1987 C C   . LEU A 1 250 ? 30.865  -21.880 43.836 1.00 22.89  ? 266 LEU A C   1 
ATOM   1988 O O   . LEU A 1 250 ? 31.167  -20.944 44.576 1.00 23.23  ? 266 LEU A O   1 
ATOM   1989 C CB  . LEU A 1 250 ? 30.512  -21.490 41.399 1.00 21.70  ? 266 LEU A CB  1 
ATOM   1990 C CG  . LEU A 1 250 ? 29.793  -22.133 40.219 1.00 23.46  ? 266 LEU A CG  1 
ATOM   1991 C CD1 . LEU A 1 250 ? 28.406  -21.525 40.027 1.00 23.48  ? 266 LEU A CD1 1 
ATOM   1992 C CD2 . LEU A 1 250 ? 30.606  -21.969 38.951 1.00 22.96  ? 266 LEU A CD2 1 
ATOM   1993 N N   . PRO A 1 251 ? 31.445  -23.088 43.942 1.00 23.04  ? 267 PRO A N   1 
ATOM   1994 C CA  . PRO A 1 251 ? 32.461  -23.352 44.952 1.00 22.93  ? 267 PRO A CA  1 
ATOM   1995 C C   . PRO A 1 251 ? 33.829  -22.952 44.422 1.00 23.17  ? 267 PRO A C   1 
ATOM   1996 O O   . PRO A 1 251 ? 33.954  -22.393 43.328 1.00 22.10  ? 267 PRO A O   1 
ATOM   1997 C CB  . PRO A 1 251 ? 32.368  -24.876 45.072 1.00 22.42  ? 267 PRO A CB  1 
ATOM   1998 C CG  . PRO A 1 251 ? 32.149  -25.306 43.646 1.00 21.87  ? 267 PRO A CG  1 
ATOM   1999 C CD  . PRO A 1 251 ? 31.180  -24.273 43.109 1.00 23.33  ? 267 PRO A CD  1 
ATOM   2000 N N   . LEU A 1 252 ? 34.843  -23.229 45.238 1.00 25.35  ? 268 LEU A N   1 
ATOM   2001 C CA  . LEU A 1 252 ? 36.216  -23.319 44.787 1.00 24.99  ? 268 LEU A CA  1 
ATOM   2002 C C   . LEU A 1 252 ? 36.574  -24.803 44.754 1.00 26.75  ? 268 LEU A C   1 
ATOM   2003 O O   . LEU A 1 252 ? 36.017  -25.582 45.531 1.00 29.99  ? 268 LEU A O   1 
ATOM   2004 C CB  . LEU A 1 252 ? 37.105  -22.590 45.793 1.00 24.52  ? 268 LEU A CB  1 
ATOM   2005 C CG  . LEU A 1 252 ? 36.732  -21.149 46.105 1.00 26.97  ? 268 LEU A CG  1 
ATOM   2006 C CD1 . LEU A 1 252 ? 37.691  -20.553 47.125 1.00 27.86  ? 268 LEU A CD1 1 
ATOM   2007 C CD2 . LEU A 1 252 ? 36.721  -20.288 44.854 1.00 27.62  ? 268 LEU A CD2 1 
ATOM   2008 N N   . VAL A 1 253 ? 37.546  -25.147 43.909 1.00 27.70  ? 269 VAL A N   1 
ATOM   2009 C CA  . VAL A 1 253 ? 38.149  -26.472 43.879 1.00 28.94  ? 269 VAL A CA  1 
ATOM   2010 C C   . VAL A 1 253 ? 38.739  -26.795 45.246 1.00 31.05  ? 269 VAL A C   1 
ATOM   2011 O O   . VAL A 1 253 ? 39.431  -25.967 45.843 1.00 28.31  ? 269 VAL A O   1 
ATOM   2012 C CB  . VAL A 1 253 ? 39.237  -26.569 42.800 1.00 31.80  ? 269 VAL A CB  1 
ATOM   2013 C CG1 . VAL A 1 253 ? 40.045  -27.864 42.912 1.00 32.22  ? 269 VAL A CG1 1 
ATOM   2014 C CG2 . VAL A 1 253 ? 38.648  -26.422 41.404 1.00 31.89  ? 269 VAL A CG2 1 
ATOM   2015 N N   . ASN A 1 254 ? 38.424  -28.008 45.710 1.00 31.30  ? 270 ASN A N   1 
ATOM   2016 C CA  . ASN A 1 254 ? 39.041  -28.630 46.864 1.00 32.76  ? 270 ASN A CA  1 
ATOM   2017 C C   . ASN A 1 254 ? 39.985  -29.715 46.353 1.00 35.83  ? 270 ASN A C   1 
ATOM   2018 O O   . ASN A 1 254 ? 39.526  -30.763 45.887 1.00 34.44  ? 270 ASN A O   1 
ATOM   2019 C CB  . ASN A 1 254 ? 37.968  -29.202 47.796 1.00 31.88  ? 270 ASN A CB  1 
ATOM   2020 C CG  . ASN A 1 254 ? 38.510  -29.726 49.106 1.00 29.18  ? 270 ASN A CG  1 
ATOM   2021 O OD1 . ASN A 1 254 ? 39.716  -29.785 49.314 1.00 32.20  ? 270 ASN A OD1 1 
ATOM   2022 N ND2 . ASN A 1 254 ? 37.620  -30.119 49.998 1.00 29.75  ? 270 ASN A ND2 1 
ATOM   2023 N N   . VAL A 1 255 ? 41.296  -29.450 46.460 1.00 38.38  ? 271 VAL A N   1 
ATOM   2024 C CA  . VAL A 1 255 ? 42.324  -30.365 45.981 1.00 41.60  ? 271 VAL A CA  1 
ATOM   2025 C C   . VAL A 1 255 ? 42.270  -31.696 46.730 1.00 43.16  ? 271 VAL A C   1 
ATOM   2026 O O   . VAL A 1 255 ? 42.752  -32.693 46.210 1.00 44.43  ? 271 VAL A O   1 
ATOM   2027 C CB  . VAL A 1 255 ? 43.742  -29.771 46.051 1.00 40.39  ? 271 VAL A CB  1 
ATOM   2028 C CG1 . VAL A 1 255 ? 43.953  -28.706 44.984 1.00 40.19  ? 271 VAL A CG1 1 
ATOM   2029 C CG2 . VAL A 1 255 ? 44.085  -29.251 47.436 1.00 38.63  ? 271 VAL A CG2 1 
ATOM   2030 N N   . ALA A 1 256 ? 41.658  -31.740 47.914 1.00 42.65  ? 272 ALA A N   1 
ATOM   2031 C CA  . ALA A 1 256 ? 41.497  -33.026 48.573 1.00 44.90  ? 272 ALA A CA  1 
ATOM   2032 C C   . ALA A 1 256 ? 40.666  -33.957 47.689 1.00 46.24  ? 272 ALA A C   1 
ATOM   2033 O O   . ALA A 1 256 ? 40.851  -35.170 47.740 1.00 47.75  ? 272 ALA A O   1 
ATOM   2034 C CB  . ALA A 1 256 ? 40.887  -32.860 49.948 1.00 40.67  ? 272 ALA A CB  1 
ATOM   2035 N N   . ASP A 1 257 ? 39.756  -33.394 46.870 1.00 41.84  ? 273 ASP A N   1 
ATOM   2036 C CA  . ASP A 1 257 ? 38.880  -34.207 46.038 1.00 37.56  ? 273 ASP A CA  1 
ATOM   2037 C C   . ASP A 1 257 ? 39.693  -34.903 44.953 1.00 37.17  ? 273 ASP A C   1 
ATOM   2038 O O   . ASP A 1 257 ? 40.715  -34.404 44.511 1.00 35.92  ? 273 ASP A O   1 
ATOM   2039 C CB  . ASP A 1 257 ? 37.745  -33.412 45.378 1.00 37.08  ? 273 ASP A CB  1 
ATOM   2040 C CG  . ASP A 1 257 ? 36.678  -32.924 46.343 1.00 38.46  ? 273 ASP A CG  1 
ATOM   2041 O OD1 . ASP A 1 257 ? 36.411  -33.641 47.321 1.00 36.40  ? 273 ASP A OD1 1 
ATOM   2042 O OD2 . ASP A 1 257 ? 36.094  -31.836 46.098 1.00 41.27  ? 273 ASP A OD2 1 
ATOM   2043 N N   . PRO A 1 258 ? 39.276  -36.097 44.492 1.00 42.17  ? 274 PRO A N   1 
ATOM   2044 C CA  . PRO A 1 258 ? 39.933  -36.725 43.350 1.00 45.48  ? 274 PRO A CA  1 
ATOM   2045 C C   . PRO A 1 258 ? 39.866  -35.784 42.151 1.00 43.27  ? 274 PRO A C   1 
ATOM   2046 O O   . PRO A 1 258 ? 38.850  -35.111 41.968 1.00 39.94  ? 274 PRO A O   1 
ATOM   2047 C CB  . PRO A 1 258 ? 39.124  -38.007 43.102 1.00 44.00  ? 274 PRO A CB  1 
ATOM   2048 C CG  . PRO A 1 258 ? 38.420  -38.266 44.423 1.00 46.14  ? 274 PRO A CG  1 
ATOM   2049 C CD  . PRO A 1 258 ? 38.170  -36.900 45.033 1.00 43.06  ? 274 PRO A CD  1 
ATOM   2050 N N   . PRO A 1 259 ? 40.931  -35.713 41.315 1.00 43.69  ? 275 PRO A N   1 
ATOM   2051 C CA  . PRO A 1 259 ? 40.917  -34.923 40.085 1.00 39.94  ? 275 PRO A CA  1 
ATOM   2052 C C   . PRO A 1 259 ? 39.723  -35.180 39.182 1.00 38.52  ? 275 PRO A C   1 
ATOM   2053 O O   . PRO A 1 259 ? 39.293  -34.272 38.486 1.00 40.60  ? 275 PRO A O   1 
ATOM   2054 C CB  . PRO A 1 259 ? 42.192  -35.355 39.354 1.00 44.17  ? 275 PRO A CB  1 
ATOM   2055 C CG  . PRO A 1 259 ? 43.135  -35.732 40.484 1.00 43.71  ? 275 PRO A CG  1 
ATOM   2056 C CD  . PRO A 1 259 ? 42.244  -36.338 41.547 1.00 44.79  ? 275 PRO A CD  1 
ATOM   2057 N N   . GLU A 1 260 ? 39.162  -36.396 39.232 1.00 39.38  ? 276 GLU A N   1 
ATOM   2058 C CA  . GLU A 1 260 ? 38.066  -36.768 38.345 1.00 42.96  ? 276 GLU A CA  1 
ATOM   2059 C C   . GLU A 1 260 ? 36.738  -36.094 38.731 1.00 40.38  ? 276 GLU A C   1 
ATOM   2060 O O   . GLU A 1 260 ? 35.836  -36.070 37.907 1.00 45.11  ? 276 GLU A O   1 
ATOM   2061 C CB  . GLU A 1 260 ? 37.931  -38.294 38.275 1.00 47.58  ? 276 GLU A CB  1 
ATOM   2062 C CG  . GLU A 1 260 ? 39.234  -39.010 37.923 1.00 49.40  ? 276 GLU A CG  1 
ATOM   2063 C CD  . GLU A 1 260 ? 40.046  -39.552 39.096 1.00 57.04  ? 276 GLU A CD  1 
ATOM   2064 O OE1 . GLU A 1 260 ? 40.233  -38.815 40.092 1.00 55.41  ? 276 GLU A OE1 1 
ATOM   2065 O OE2 . GLU A 1 260 ? 40.504  -40.722 39.014 1.00 63.75  ? 276 GLU A OE2 1 
ATOM   2066 N N   . VAL A 1 261 ? 36.606  -35.488 39.928 1.00 39.18  ? 277 VAL A N   1 
ATOM   2067 C CA  . VAL A 1 261 ? 35.345  -34.855 40.315 1.00 35.06  ? 277 VAL A CA  1 
ATOM   2068 C C   . VAL A 1 261 ? 35.459  -33.326 40.459 1.00 34.77  ? 277 VAL A C   1 
ATOM   2069 O O   . VAL A 1 261 ? 34.454  -32.651 40.691 1.00 30.64  ? 277 VAL A O   1 
ATOM   2070 C CB  . VAL A 1 261 ? 34.784  -35.455 41.622 1.00 35.80  ? 277 VAL A CB  1 
ATOM   2071 C CG1 . VAL A 1 261 ? 34.434  -36.931 41.501 1.00 36.04  ? 277 VAL A CG1 1 
ATOM   2072 C CG2 . VAL A 1 261 ? 35.721  -35.224 42.803 1.00 37.14  ? 277 VAL A CG2 1 
ATOM   2073 N N   . ARG A 1 262 ? 36.654  -32.748 40.334 1.00 30.85  ? 278 ARG A N   1 
ATOM   2074 C CA  . ARG A 1 262 ? 36.838  -31.360 40.731 1.00 32.65  ? 278 ARG A CA  1 
ATOM   2075 C C   . ARG A 1 262 ? 36.075  -30.397 39.816 1.00 32.47  ? 278 ARG A C   1 
ATOM   2076 O O   . ARG A 1 262 ? 35.701  -29.312 40.263 1.00 29.95  ? 278 ARG A O   1 
ATOM   2077 C CB  . ARG A 1 262 ? 38.326  -31.014 40.751 1.00 33.11  ? 278 ARG A CB  1 
ATOM   2078 C CG  . ARG A 1 262 ? 39.099  -31.701 41.863 1.00 33.86  ? 278 ARG A CG  1 
ATOM   2079 C CD  . ARG A 1 262 ? 40.587  -31.459 41.689 1.00 37.88  ? 278 ARG A CD  1 
ATOM   2080 N NE  . ARG A 1 262 ? 41.363  -32.185 42.682 1.00 42.14  ? 278 ARG A NE  1 
ATOM   2081 C CZ  . ARG A 1 262 ? 42.653  -32.489 42.567 1.00 43.14  ? 278 ARG A CZ  1 
ATOM   2082 N NH1 . ARG A 1 262 ? 43.349  -32.056 41.535 1.00 43.47  ? 278 ARG A NH1 1 
ATOM   2083 N NH2 . ARG A 1 262 ? 43.245  -33.230 43.488 1.00 42.29  ? 278 ARG A NH2 1 
ATOM   2084 N N   . ASP A 1 263 ? 35.872  -30.785 38.547 1.00 29.95  ? 279 ASP A N   1 
ATOM   2085 C CA  . ASP A 1 263 ? 35.124  -29.977 37.603 1.00 32.48  ? 279 ASP A CA  1 
ATOM   2086 C C   . ASP A 1 263 ? 33.620  -29.973 37.901 1.00 30.21  ? 279 ASP A C   1 
ATOM   2087 O O   . ASP A 1 263 ? 32.942  -29.044 37.446 1.00 30.15  ? 279 ASP A O   1 
ATOM   2088 C CB  . ASP A 1 263 ? 35.360  -30.418 36.157 1.00 34.54  ? 279 ASP A CB  1 
ATOM   2089 C CG  . ASP A 1 263 ? 36.769  -30.166 35.663 1.00 37.43  ? 279 ASP A CG  1 
ATOM   2090 O OD1 . ASP A 1 263 ? 37.276  -29.024 35.825 1.00 33.66  ? 279 ASP A OD1 1 
ATOM   2091 O OD2 . ASP A 1 263 ? 37.351  -31.113 35.109 1.00 47.78  ? 279 ASP A OD2 1 
ATOM   2092 N N   . ASP A 1 264 ? 33.111  -30.982 38.640 1.00 27.82  ? 280 ASP A N   1 
ATOM   2093 C CA  . ASP A 1 264 ? 31.682  -31.123 38.921 1.00 27.06  ? 280 ASP A CA  1 
ATOM   2094 C C   . ASP A 1 264 ? 31.302  -30.199 40.077 1.00 27.17  ? 280 ASP A C   1 
ATOM   2095 O O   . ASP A 1 264 ? 31.168  -30.624 41.232 1.00 25.72  ? 280 ASP A O   1 
ATOM   2096 C CB  . ASP A 1 264 ? 31.278  -32.574 39.213 1.00 29.48  ? 280 ASP A CB  1 
ATOM   2097 C CG  . ASP A 1 264 ? 29.803  -32.767 39.571 1.00 29.21  ? 280 ASP A CG  1 
ATOM   2098 O OD1 . ASP A 1 264 ? 28.969  -31.912 39.201 1.00 28.77  ? 280 ASP A OD1 1 
ATOM   2099 O OD2 . ASP A 1 264 ? 29.492  -33.760 40.237 1.00 28.66  ? 280 ASP A OD2 1 
ATOM   2100 N N   . VAL A 1 265 ? 31.076  -28.929 39.724 1.00 25.72  ? 281 VAL A N   1 
ATOM   2101 C CA  . VAL A 1 265 ? 30.768  -27.886 40.686 1.00 25.41  ? 281 VAL A CA  1 
ATOM   2102 C C   . VAL A 1 265 ? 29.367  -28.053 41.263 1.00 24.78  ? 281 VAL A C   1 
ATOM   2103 O O   . VAL A 1 265 ? 29.047  -27.446 42.272 1.00 24.19  ? 281 VAL A O   1 
ATOM   2104 C CB  . VAL A 1 265 ? 30.949  -26.504 40.039 1.00 26.95  ? 281 VAL A CB  1 
ATOM   2105 C CG1 . VAL A 1 265 ? 32.422  -26.225 39.841 1.00 27.35  ? 281 VAL A CG1 1 
ATOM   2106 C CG2 . VAL A 1 265 ? 30.170  -26.358 38.727 1.00 27.89  ? 281 VAL A CG2 1 
ATOM   2107 N N   . VAL A 1 266 ? 28.536  -28.903 40.656 1.00 23.82  ? 282 VAL A N   1 
ATOM   2108 C CA  . VAL A 1 266 ? 27.204  -29.141 41.174 1.00 23.16  ? 282 VAL A CA  1 
ATOM   2109 C C   . VAL A 1 266 ? 27.332  -29.880 42.508 1.00 22.75  ? 282 VAL A C   1 
ATOM   2110 O O   . VAL A 1 266 ? 26.528  -29.688 43.407 1.00 20.92  ? 282 VAL A O   1 
ATOM   2111 C CB  . VAL A 1 266 ? 26.338  -29.944 40.186 1.00 23.57  ? 282 VAL A CB  1 
ATOM   2112 C CG1 . VAL A 1 266 ? 24.924  -30.125 40.696 1.00 23.51  ? 282 VAL A CG1 1 
ATOM   2113 C CG2 . VAL A 1 266 ? 26.325  -29.320 38.800 1.00 26.50  ? 282 VAL A CG2 1 
ATOM   2114 N N   . HIS A 1 267 ? 28.353  -30.737 42.648 1.00 23.91  ? 283 HIS A N   1 
ATOM   2115 C CA  . HIS A 1 267 ? 28.388  -31.621 43.806 1.00 22.97  ? 283 HIS A CA  1 
ATOM   2116 C C   . HIS A 1 267 ? 29.655  -31.459 44.641 1.00 24.36  ? 283 HIS A C   1 
ATOM   2117 O O   . HIS A 1 267 ? 29.647  -31.891 45.779 1.00 27.54  ? 283 HIS A O   1 
ATOM   2118 C CB  . HIS A 1 267 ? 28.207  -33.075 43.358 1.00 22.91  ? 283 HIS A CB  1 
ATOM   2119 C CG  . HIS A 1 267 ? 27.005  -33.271 42.506 1.00 22.73  ? 283 HIS A CG  1 
ATOM   2120 N ND1 . HIS A 1 267 ? 27.065  -33.641 41.186 1.00 21.64  ? 283 HIS A ND1 1 
ATOM   2121 C CD2 . HIS A 1 267 ? 25.715  -33.127 42.788 1.00 23.48  ? 283 HIS A CD2 1 
ATOM   2122 C CE1 . HIS A 1 267 ? 25.838  -33.684 40.693 1.00 21.45  ? 283 HIS A CE1 1 
ATOM   2123 N NE2 . HIS A 1 267 ? 25.011  -33.382 41.645 1.00 22.30  ? 283 HIS A NE2 1 
ATOM   2124 N N   . TYR A 1 268 ? 30.726  -30.863 44.101 1.00 25.05  ? 284 TYR A N   1 
ATOM   2125 C CA  . TYR A 1 268 ? 32.007  -30.821 44.787 1.00 25.62  ? 284 TYR A CA  1 
ATOM   2126 C C   . TYR A 1 268 ? 32.557  -29.399 44.828 1.00 25.99  ? 284 TYR A C   1 
ATOM   2127 O O   . TYR A 1 268 ? 32.377  -28.603 43.898 1.00 24.59  ? 284 TYR A O   1 
ATOM   2128 C CB  . TYR A 1 268 ? 33.045  -31.706 44.089 1.00 26.05  ? 284 TYR A CB  1 
ATOM   2129 C CG  . TYR A 1 268 ? 32.632  -33.176 44.087 1.00 28.59  ? 284 TYR A CG  1 
ATOM   2130 C CD1 . TYR A 1 268 ? 32.958  -34.027 45.145 1.00 28.74  ? 284 TYR A CD1 1 
ATOM   2131 C CD2 . TYR A 1 268 ? 31.874  -33.696 43.043 1.00 27.38  ? 284 TYR A CD2 1 
ATOM   2132 C CE1 . TYR A 1 268 ? 32.593  -35.368 45.130 1.00 32.07  ? 284 TYR A CE1 1 
ATOM   2133 C CE2 . TYR A 1 268 ? 31.471  -35.020 43.037 1.00 29.98  ? 284 TYR A CE2 1 
ATOM   2134 C CZ  . TYR A 1 268 ? 31.836  -35.865 44.076 1.00 34.39  ? 284 TYR A CZ  1 
ATOM   2135 O OH  . TYR A 1 268 ? 31.426  -37.176 44.031 1.00 29.44  ? 284 TYR A OH  1 
ATOM   2136 N N   . GLY A 1 269 ? 33.316  -29.141 45.890 1.00 24.56  ? 285 GLY A N   1 
ATOM   2137 C CA  . GLY A 1 269 ? 34.060  -27.896 46.022 1.00 26.21  ? 285 GLY A CA  1 
ATOM   2138 C C   . GLY A 1 269 ? 33.850  -27.294 47.403 1.00 25.97  ? 285 GLY A C   1 
ATOM   2139 O O   . GLY A 1 269 ? 32.935  -27.690 48.121 1.00 25.69  ? 285 GLY A O   1 
ATOM   2140 N N   . ILE A 1 270 ? 34.699  -26.319 47.736 1.00 27.14  ? 286 ILE A N   1 
ATOM   2141 C CA  . ILE A 1 270 ? 34.656  -25.650 49.021 1.00 28.35  ? 286 ILE A CA  1 
ATOM   2142 C C   . ILE A 1 270 ? 33.537  -24.602 48.989 1.00 25.01  ? 286 ILE A C   1 
ATOM   2143 O O   . ILE A 1 270 ? 33.500  -23.748 48.098 1.00 23.98  ? 286 ILE A O   1 
ATOM   2144 C CB  . ILE A 1 270 ? 36.050  -25.063 49.327 1.00 32.24  ? 286 ILE A CB  1 
ATOM   2145 C CG1 . ILE A 1 270 ? 37.081  -26.191 49.471 1.00 35.95  ? 286 ILE A CG1 1 
ATOM   2146 C CG2 . ILE A 1 270 ? 36.015  -24.174 50.553 1.00 32.09  ? 286 ILE A CG2 1 
ATOM   2147 C CD1 . ILE A 1 270 ? 38.517  -25.769 49.295 1.00 35.26  ? 286 ILE A CD1 1 
ATOM   2148 N N   . GLN A 1 271 ? 32.600  -24.751 49.927 1.00 22.37  ? 287 GLN A N   1 
ATOM   2149 C CA  . GLN A 1 271 ? 31.540  -23.804 50.223 1.00 24.18  ? 287 GLN A CA  1 
ATOM   2150 C C   . GLN A 1 271 ? 31.545  -23.523 51.724 1.00 27.32  ? 287 GLN A C   1 
ATOM   2151 O O   . GLN A 1 271 ? 31.148  -24.370 52.533 1.00 27.55  ? 287 GLN A O   1 
ATOM   2152 C CB  . GLN A 1 271 ? 30.155  -24.351 49.878 1.00 24.34  ? 287 GLN A CB  1 
ATOM   2153 C CG  . GLN A 1 271 ? 29.793  -24.323 48.405 1.00 23.66  ? 287 GLN A CG  1 
ATOM   2154 C CD  . GLN A 1 271 ? 29.631  -22.927 47.855 1.00 23.55  ? 287 GLN A CD  1 
ATOM   2155 O OE1 . GLN A 1 271 ? 29.811  -21.922 48.541 1.00 23.48  ? 287 GLN A OE1 1 
ATOM   2156 N NE2 . GLN A 1 271 ? 29.296  -22.853 46.583 1.00 25.18  ? 287 GLN A NE2 1 
ATOM   2157 N N   . PRO A 1 272 ? 31.973  -22.321 52.154 1.00 29.04  ? 288 PRO A N   1 
ATOM   2158 C CA  . PRO A 1 272 ? 31.964  -21.989 53.574 1.00 28.23  ? 288 PRO A CA  1 
ATOM   2159 C C   . PRO A 1 272 ? 30.513  -21.861 54.040 1.00 29.19  ? 288 PRO A C   1 
ATOM   2160 O O   . PRO A 1 272 ? 29.618  -21.632 53.244 1.00 30.70  ? 288 PRO A O   1 
ATOM   2161 C CB  . PRO A 1 272 ? 32.796  -20.710 53.658 1.00 29.95  ? 288 PRO A CB  1 
ATOM   2162 C CG  . PRO A 1 272 ? 32.762  -20.111 52.264 1.00 33.35  ? 288 PRO A CG  1 
ATOM   2163 C CD  . PRO A 1 272 ? 32.470  -21.238 51.299 1.00 30.16  ? 288 PRO A CD  1 
ATOM   2164 N N   . PRO A 1 273 ? 30.206  -22.125 55.326 1.00 30.56  ? 289 PRO A N   1 
ATOM   2165 C CA  . PRO A 1 273 ? 28.819  -22.106 55.794 1.00 33.38  ? 289 PRO A CA  1 
ATOM   2166 C C   . PRO A 1 273 ? 28.311  -20.724 56.206 1.00 31.08  ? 289 PRO A C   1 
ATOM   2167 O O   . PRO A 1 273 ? 27.702  -20.589 57.247 1.00 43.79  ? 289 PRO A O   1 
ATOM   2168 C CB  . PRO A 1 273 ? 28.866  -23.085 56.986 1.00 34.67  ? 289 PRO A CB  1 
ATOM   2169 C CG  . PRO A 1 273 ? 30.286  -22.950 57.534 1.00 34.15  ? 289 PRO A CG  1 
ATOM   2170 C CD  . PRO A 1 273 ? 31.163  -22.536 56.363 1.00 33.53  ? 289 PRO A CD  1 
ATOM   2171 N N   . THR A 1 274 ? 28.479  -19.727 55.335 1.00 29.02  ? 290 THR A N   1 
ATOM   2172 C CA  . THR A 1 274 ? 28.238  -18.330 55.652 1.00 26.46  ? 290 THR A CA  1 
ATOM   2173 C C   . THR A 1 274 ? 26.989  -17.826 54.922 1.00 27.70  ? 290 THR A C   1 
ATOM   2174 O O   . THR A 1 274 ? 26.508  -18.440 53.971 1.00 28.83  ? 290 THR A O   1 
ATOM   2175 C CB  . THR A 1 274 ? 29.505  -17.524 55.347 1.00 25.12  ? 290 THR A CB  1 
ATOM   2176 O OG1 . THR A 1 274 ? 30.077  -17.906 54.092 1.00 22.89  ? 290 THR A OG1 1 
ATOM   2177 C CG2 . THR A 1 274 ? 30.561  -17.723 56.420 1.00 28.62  ? 290 THR A CG2 1 
ATOM   2178 N N   . THR A 1 275 ? 26.454  -16.705 55.404 1.00 26.98  ? 291 THR A N   1 
ATOM   2179 C CA  . THR A 1 275 ? 25.268  -16.098 54.833 1.00 26.81  ? 291 THR A CA  1 
ATOM   2180 C C   . THR A 1 275 ? 25.691  -14.937 53.934 1.00 28.03  ? 291 THR A C   1 
ATOM   2181 O O   . THR A 1 275 ? 26.644  -14.229 54.259 1.00 27.16  ? 291 THR A O   1 
ATOM   2182 C CB  . THR A 1 275 ? 24.293  -15.754 55.962 1.00 26.76  ? 291 THR A CB  1 
ATOM   2183 O OG1 . THR A 1 275 ? 23.970  -17.016 56.548 1.00 25.94  ? 291 THR A OG1 1 
ATOM   2184 C CG2 . THR A 1 275 ? 23.024  -15.076 55.494 1.00 25.09  ? 291 THR A CG2 1 
ATOM   2185 N N   . HIS A 1 276 ? 25.043  -14.806 52.757 1.00 26.31  ? 292 HIS A N   1 
ATOM   2186 C CA  . HIS A 1 276 ? 25.336  -13.737 51.813 1.00 24.70  ? 292 HIS A CA  1 
ATOM   2187 C C   . HIS A 1 276 ? 24.059  -13.303 51.100 1.00 24.78  ? 292 HIS A C   1 
ATOM   2188 O O   . HIS A 1 276 ? 23.198  -14.136 50.801 1.00 24.87  ? 292 HIS A O   1 
ATOM   2189 C CB  . HIS A 1 276 ? 26.333  -14.167 50.735 1.00 26.50  ? 292 HIS A CB  1 
ATOM   2190 C CG  . HIS A 1 276 ? 27.508  -14.909 51.269 1.00 27.81  ? 292 HIS A CG  1 
ATOM   2191 N ND1 . HIS A 1 276 ? 28.712  -14.296 51.549 1.00 26.18  ? 292 HIS A ND1 1 
ATOM   2192 C CD2 . HIS A 1 276 ? 27.648  -16.209 51.582 1.00 26.13  ? 292 HIS A CD2 1 
ATOM   2193 C CE1 . HIS A 1 276 ? 29.548  -15.212 52.013 1.00 27.86  ? 292 HIS A CE1 1 
ATOM   2194 N NE2 . HIS A 1 276 ? 28.923  -16.377 52.068 1.00 26.21  ? 292 HIS A NE2 1 
ATOM   2195 N N   . GLY A 1 277 ? 23.950  -11.994 50.830 1.00 22.43  ? 293 GLY A N   1 
ATOM   2196 C CA  . GLY A 1 277 ? 22.747  -11.459 50.229 1.00 22.72  ? 293 GLY A CA  1 
ATOM   2197 C C   . GLY A 1 277 ? 23.024  -10.536 49.049 1.00 24.72  ? 293 GLY A C   1 
ATOM   2198 O O   . GLY A 1 277 ? 24.147  -10.112 48.811 1.00 27.83  ? 293 GLY A O   1 
ATOM   2199 N N   . ILE A 1 278 ? 21.944  -10.241 48.319 1.00 24.27  ? 294 ILE A N   1 
ATOM   2200 C CA  . ILE A 1 278 ? 21.887  -9.191  47.331 1.00 22.56  ? 294 ILE A CA  1 
ATOM   2201 C C   . ILE A 1 278 ? 20.430  -8.716  47.301 1.00 23.62  ? 294 ILE A C   1 
ATOM   2202 O O   . ILE A 1 278 ? 19.503  -9.466  47.614 1.00 24.66  ? 294 ILE A O   1 
ATOM   2203 C CB  . ILE A 1 278 ? 22.434  -9.698  45.984 1.00 22.30  ? 294 ILE A CB  1 
ATOM   2204 C CG1 . ILE A 1 278 ? 22.870  -8.560  45.066 1.00 24.97  ? 294 ILE A CG1 1 
ATOM   2205 C CG2 . ILE A 1 278 ? 21.449  -10.629 45.297 1.00 22.22  ? 294 ILE A CG2 1 
ATOM   2206 C CD1 . ILE A 1 278 ? 23.564  -9.036  43.805 1.00 23.99  ? 294 ILE A CD1 1 
ATOM   2207 N N   . MET A 1 279 ? 20.241  -7.436  46.990 1.00 23.39  ? 295 MET A N   1 
ATOM   2208 C CA  . MET A 1 279 ? 18.897  -6.902  46.910 1.00 22.58  ? 295 MET A CA  1 
ATOM   2209 C C   . MET A 1 279 ? 18.537  -6.644  45.444 1.00 21.26  ? 295 MET A C   1 
ATOM   2210 O O   . MET A 1 279 ? 19.376  -6.228  44.632 1.00 21.16  ? 295 MET A O   1 
ATOM   2211 C CB  . MET A 1 279 ? 18.821  -5.622  47.741 1.00 24.04  ? 295 MET A CB  1 
ATOM   2212 C CG  . MET A 1 279 ? 18.818  -5.902  49.237 1.00 25.96  ? 295 MET A CG  1 
ATOM   2213 S SD  . MET A 1 279 ? 19.038  -4.377  50.230 1.00 29.24  ? 295 MET A SD  1 
ATOM   2214 C CE  . MET A 1 279 ? 18.935  -5.028  51.897 1.00 35.26  ? 295 MET A CE  1 
ATOM   2215 N N   . TYR A 1 280 ? 17.274  -6.928  45.129 1.00 21.20  ? 296 TYR A N   1 
ATOM   2216 C CA  . TYR A 1 280 ? 16.719  -6.763  43.797 1.00 22.08  ? 296 TYR A CA  1 
ATOM   2217 C C   . TYR A 1 280 ? 15.557  -5.770  43.819 1.00 22.42  ? 296 TYR A C   1 
ATOM   2218 O O   . TYR A 1 280 ? 14.759  -5.746  44.763 1.00 20.01  ? 296 TYR A O   1 
ATOM   2219 C CB  . TYR A 1 280 ? 16.229  -8.128  43.306 1.00 20.72  ? 296 TYR A CB  1 
ATOM   2220 C CG  . TYR A 1 280 ? 17.330  -9.037  42.781 1.00 21.12  ? 296 TYR A CG  1 
ATOM   2221 C CD1 . TYR A 1 280 ? 17.877  -8.858  41.507 1.00 22.83  ? 296 TYR A CD1 1 
ATOM   2222 C CD2 . TYR A 1 280 ? 17.838  -10.063 43.571 1.00 19.50  ? 296 TYR A CD2 1 
ATOM   2223 C CE1 . TYR A 1 280 ? 18.890  -9.680  41.032 1.00 20.61  ? 296 TYR A CE1 1 
ATOM   2224 C CE2 . TYR A 1 280 ? 18.850  -10.887 43.102 1.00 20.59  ? 296 TYR A CE2 1 
ATOM   2225 C CZ  . TYR A 1 280 ? 19.378  -10.693 41.836 1.00 20.90  ? 296 TYR A CZ  1 
ATOM   2226 O OH  . TYR A 1 280 ? 20.392  -11.504 41.407 1.00 20.36  ? 296 TYR A OH  1 
ATOM   2227 N N   . SER A 1 281 ? 15.433  -5.020  42.716 1.00 21.00  ? 297 SER A N   1 
ATOM   2228 C CA  . SER A 1 281 ? 14.221  -4.284  42.400 1.00 20.96  ? 297 SER A CA  1 
ATOM   2229 C C   . SER A 1 281 ? 14.168  -4.109  40.888 1.00 21.83  ? 297 SER A C   1 
ATOM   2230 O O   . SER A 1 281 ? 15.112  -4.471  40.198 1.00 21.48  ? 297 SER A O   1 
ATOM   2231 C CB  . SER A 1 281 ? 14.099  -2.948  43.143 1.00 21.72  ? 297 SER A CB  1 
ATOM   2232 O OG  . SER A 1 281 ? 15.119  -1.998  42.811 1.00 21.37  ? 297 SER A OG  1 
ATOM   2233 N N   . GLY A 1 282 ? 13.038  -3.594  40.392 1.00 22.46  ? 298 GLY A N   1 
ATOM   2234 C CA  . GLY A 1 282 ? 12.888  -3.270  38.993 1.00 20.54  ? 298 GLY A CA  1 
ATOM   2235 C C   . GLY A 1 282 ? 13.084  -4.476  38.085 1.00 20.13  ? 298 GLY A C   1 
ATOM   2236 O O   . GLY A 1 282 ? 13.518  -4.291  36.952 1.00 19.74  ? 298 GLY A O   1 
ATOM   2237 N N   . VAL A 1 283 ? 12.708  -5.676  38.554 1.00 20.35  ? 299 VAL A N   1 
ATOM   2238 C CA  . VAL A 1 283 ? 12.850  -6.884  37.747 1.00 20.72  ? 299 VAL A CA  1 
ATOM   2239 C C   . VAL A 1 283 ? 11.553  -7.170  36.996 1.00 20.92  ? 299 VAL A C   1 
ATOM   2240 O O   . VAL A 1 283 ? 10.569  -7.536  37.633 1.00 21.28  ? 299 VAL A O   1 
ATOM   2241 C CB  . VAL A 1 283 ? 13.264  -8.086  38.619 1.00 20.19  ? 299 VAL A CB  1 
ATOM   2242 C CG1 . VAL A 1 283 ? 13.430  -9.345  37.782 1.00 19.74  ? 299 VAL A CG1 1 
ATOM   2243 C CG2 . VAL A 1 283 ? 14.526  -7.783  39.426 1.00 20.36  ? 299 VAL A CG2 1 
ATOM   2244 N N   . PHE A 1 284 ? 11.564  -7.023  35.662 1.00 22.39  ? 300 PHE A N   1 
ATOM   2245 C CA  . PHE A 1 284 ? 10.382  -7.286  34.848 1.00 22.92  ? 300 PHE A CA  1 
ATOM   2246 C C   . PHE A 1 284 ? 10.809  -7.543  33.402 1.00 24.54  ? 300 PHE A C   1 
ATOM   2247 O O   . PHE A 1 284 ? 11.969  -7.312  33.029 1.00 22.70  ? 300 PHE A O   1 
ATOM   2248 C CB  . PHE A 1 284 ? 9.379   -6.128  34.949 1.00 23.29  ? 300 PHE A CB  1 
ATOM   2249 C CG  . PHE A 1 284 ? 9.796   -4.830  34.295 1.00 23.60  ? 300 PHE A CG  1 
ATOM   2250 C CD1 . PHE A 1 284 ? 10.724  -3.994  34.894 1.00 25.59  ? 300 PHE A CD1 1 
ATOM   2251 C CD2 . PHE A 1 284 ? 9.260   -4.427  33.073 1.00 24.75  ? 300 PHE A CD2 1 
ATOM   2252 C CE1 . PHE A 1 284 ? 11.107  -2.795  34.310 1.00 24.79  ? 300 PHE A CE1 1 
ATOM   2253 C CE2 . PHE A 1 284 ? 9.663   -3.240  32.470 1.00 23.38  ? 300 PHE A CE2 1 
ATOM   2254 C CZ  . PHE A 1 284 ? 10.582  -2.423  33.091 1.00 23.98  ? 300 PHE A CZ  1 
ATOM   2255 N N   . ILE A 1 285 ? 9.851   -8.026  32.595 1.00 23.33  ? 301 ILE A N   1 
ATOM   2256 C CA  . ILE A 1 285 ? 10.101  -8.349  31.200 1.00 23.94  ? 301 ILE A CA  1 
ATOM   2257 C C   . ILE A 1 285 ? 9.046   -7.683  30.310 1.00 25.22  ? 301 ILE A C   1 
ATOM   2258 O O   . ILE A 1 285 ? 7.847   -7.784  30.585 1.00 25.37  ? 301 ILE A O   1 
ATOM   2259 C CB  . ILE A 1 285 ? 10.158  -9.877  31.002 1.00 23.16  ? 301 ILE A CB  1 
ATOM   2260 C CG1 . ILE A 1 285 ? 11.333  -10.514 31.750 1.00 23.14  ? 301 ILE A CG1 1 
ATOM   2261 C CG2 . ILE A 1 285 ? 10.228  -10.217 29.529 1.00 24.82  ? 301 ILE A CG2 1 
ATOM   2262 C CD1 . ILE A 1 285 ? 11.139  -11.963 32.049 1.00 22.27  ? 301 ILE A CD1 1 
ATOM   2263 N N   . GLU A 1 286 ? 9.506   -7.024  29.227 1.00 25.41  ? 302 GLU A N   1 
ATOM   2264 C CA  . GLU A 1 286 ? 8.623   -6.325  28.301 1.00 24.85  ? 302 GLU A CA  1 
ATOM   2265 C C   . GLU A 1 286 ? 9.039   -6.632  26.867 1.00 24.92  ? 302 GLU A C   1 
ATOM   2266 O O   . GLU A 1 286 ? 10.190  -6.969  26.605 1.00 24.84  ? 302 GLU A O   1 
ATOM   2267 C CB  . GLU A 1 286 ? 8.644   -4.809  28.534 1.00 24.63  ? 302 GLU A CB  1 
ATOM   2268 C CG  . GLU A 1 286 ? 10.027  -4.182  28.333 1.00 25.27  ? 302 GLU A CG  1 
ATOM   2269 C CD  . GLU A 1 286 ? 10.078  -2.668  28.385 1.00 26.64  ? 302 GLU A CD  1 
ATOM   2270 O OE1 . GLU A 1 286 ? 8.987   -2.031  28.366 1.00 24.74  ? 302 GLU A OE1 1 
ATOM   2271 O OE2 . GLU A 1 286 ? 11.231  -2.123  28.462 1.00 26.81  ? 302 GLU A OE2 1 
ATOM   2272 N N   . ASP A 1 287 ? 8.087   -6.526  25.928 1.00 28.17  ? 303 ASP A N   1 
ATOM   2273 C CA  . ASP A 1 287 ? 8.417   -6.563  24.508 1.00 27.32  ? 303 ASP A CA  1 
ATOM   2274 C C   . ASP A 1 287 ? 8.912   -5.165  24.140 1.00 29.82  ? 303 ASP A C   1 
ATOM   2275 O O   . ASP A 1 287 ? 9.030   -4.325  25.036 1.00 26.36  ? 303 ASP A O   1 
ATOM   2276 C CB  . ASP A 1 287 ? 7.248   -7.049  23.639 1.00 30.26  ? 303 ASP A CB  1 
ATOM   2277 C CG  . ASP A 1 287 ? 6.039   -6.128  23.576 1.00 31.33  ? 303 ASP A CG  1 
ATOM   2278 O OD1 . ASP A 1 287 ? 6.174   -4.921  23.856 1.00 25.49  ? 303 ASP A OD1 1 
ATOM   2279 O OD2 . ASP A 1 287 ? 4.949   -6.645  23.283 1.00 37.85  ? 303 ASP A OD2 1 
ATOM   2280 N N   . LEU A 1 288 ? 9.210   -4.921  22.850 1.00 28.52  ? 304 LEU A N   1 
ATOM   2281 C CA  . LEU A 1 288 ? 9.713   -3.614  22.438 1.00 30.13  ? 304 LEU A CA  1 
ATOM   2282 C C   . LEU A 1 288 ? 8.699   -2.834  21.596 1.00 31.43  ? 304 LEU A C   1 
ATOM   2283 O O   . LEU A 1 288 ? 9.098   -1.983  20.823 1.00 29.36  ? 304 LEU A O   1 
ATOM   2284 C CB  . LEU A 1 288 ? 11.053  -3.784  21.713 1.00 31.72  ? 304 LEU A CB  1 
ATOM   2285 C CG  . LEU A 1 288 ? 12.234  -4.105  22.635 1.00 33.47  ? 304 LEU A CG  1 
ATOM   2286 C CD1 . LEU A 1 288 ? 13.498  -4.318  21.840 1.00 38.04  ? 304 LEU A CD1 1 
ATOM   2287 C CD2 . LEU A 1 288 ? 12.467  -2.988  23.649 1.00 34.66  ? 304 LEU A CD2 1 
ATOM   2288 N N   . GLU A 1 289 ? 7.399   -3.037  21.839 1.00 32.82  ? 305 GLU A N   1 
ATOM   2289 C CA  . GLU A 1 289 ? 6.364   -2.169  21.300 1.00 36.50  ? 305 GLU A CA  1 
ATOM   2290 C C   . GLU A 1 289 ? 6.621   -0.708  21.675 1.00 31.23  ? 305 GLU A C   1 
ATOM   2291 O O   . GLU A 1 289 ? 6.744   -0.367  22.864 1.00 29.06  ? 305 GLU A O   1 
ATOM   2292 C CB  . GLU A 1 289 ? 4.994   -2.587  21.836 1.00 43.27  ? 305 GLU A CB  1 
ATOM   2293 C CG  . GLU A 1 289 ? 3.845   -1.747  21.288 1.00 48.00  ? 305 GLU A CG  1 
ATOM   2294 C CD  . GLU A 1 289 ? 2.457   -2.134  21.773 1.00 54.91  ? 305 GLU A CD  1 
ATOM   2295 O OE1 . GLU A 1 289 ? 2.351   -2.790  22.845 1.00 61.66  ? 305 GLU A OE1 1 
ATOM   2296 O OE2 . GLU A 1 289 ? 1.482   -1.807  21.057 1.00 59.66  ? 305 GLU A OE2 1 
ATOM   2297 N N   . ASP A 1 290 ? 6.650   0.148   20.642 1.00 29.44  ? 306 ASP A N   1 
ATOM   2298 C CA  . ASP A 1 290 ? 6.931   1.570   20.762 1.00 32.54  ? 306 ASP A CA  1 
ATOM   2299 C C   . ASP A 1 290 ? 8.374   1.835   21.195 1.00 33.87  ? 306 ASP A C   1 
ATOM   2300 O O   . ASP A 1 290 ? 8.987   2.795   20.720 1.00 35.93  ? 306 ASP A O   1 
ATOM   2301 C CB  . ASP A 1 290 ? 5.975   2.301   21.697 1.00 35.57  ? 306 ASP A CB  1 
ATOM   2302 C CG  . ASP A 1 290 ? 4.520   2.162   21.300 1.00 41.69  ? 306 ASP A CG  1 
ATOM   2303 O OD1 . ASP A 1 290 ? 4.222   2.264   20.069 1.00 37.59  ? 306 ASP A OD1 1 
ATOM   2304 O OD2 . ASP A 1 290 ? 3.702   1.947   22.231 1.00 39.41  ? 306 ASP A OD2 1 
ATOM   2305 N N   . GLY A 1 291 ? 8.910   1.035   22.123 1.00 29.25  ? 307 GLY A N   1 
ATOM   2306 C CA  . GLY A 1 291 ? 10.321  1.136   22.448 1.00 27.92  ? 307 GLY A CA  1 
ATOM   2307 C C   . GLY A 1 291 ? 10.663  0.505   23.797 1.00 28.63  ? 307 GLY A C   1 
ATOM   2308 O O   . GLY A 1 291 ? 9.835   -0.163  24.407 1.00 29.18  ? 307 GLY A O   1 
ATOM   2309 N N   . LEU A 1 292 ? 11.902  0.733   24.240 1.00 25.31  ? 308 LEU A N   1 
ATOM   2310 C CA  . LEU A 1 292 ? 12.377  0.232   25.522 1.00 25.91  ? 308 LEU A CA  1 
ATOM   2311 C C   . LEU A 1 292 ? 11.985  1.200   26.636 1.00 25.32  ? 308 LEU A C   1 
ATOM   2312 O O   . LEU A 1 292 ? 12.092  2.431   26.473 1.00 23.48  ? 308 LEU A O   1 
ATOM   2313 C CB  . LEU A 1 292 ? 13.896  0.083   25.443 1.00 24.68  ? 308 LEU A CB  1 
ATOM   2314 C CG  . LEU A 1 292 ? 14.609  -0.293  26.742 1.00 24.86  ? 308 LEU A CG  1 
ATOM   2315 C CD1 . LEU A 1 292 ? 14.328  -1.750  27.119 1.00 25.04  ? 308 LEU A CD1 1 
ATOM   2316 C CD2 . LEU A 1 292 ? 16.102  -0.089  26.576 1.00 23.65  ? 308 LEU A CD2 1 
ATOM   2317 N N   . SER A 1 293 ? 11.533  0.642   27.764 1.00 24.24  ? 309 SER A N   1 
ATOM   2318 C CA  . SER A 1 293 ? 11.334  1.447   28.964 1.00 23.28  ? 309 SER A CA  1 
ATOM   2319 C C   . SER A 1 293 ? 12.706  1.775   29.551 1.00 22.54  ? 309 SER A C   1 
ATOM   2320 O O   . SER A 1 293 ? 13.399  0.866   30.007 1.00 23.73  ? 309 SER A O   1 
ATOM   2321 C CB  . SER A 1 293 ? 10.442  0.755   29.966 1.00 23.14  ? 309 SER A CB  1 
ATOM   2322 O OG  . SER A 1 293 ? 9.207   0.393   29.385 1.00 22.96  ? 309 SER A OG  1 
ATOM   2323 N N   . VAL A 1 294 ? 13.113  3.051   29.479 1.00 21.68  ? 310 VAL A N   1 
ATOM   2324 C CA  . VAL A 1 294 ? 14.423  3.481   29.974 1.00 22.89  ? 310 VAL A CA  1 
ATOM   2325 C C   . VAL A 1 294 ? 14.346  4.084   31.378 1.00 21.60  ? 310 VAL A C   1 
ATOM   2326 O O   . VAL A 1 294 ? 15.398  4.327   31.960 1.00 22.69  ? 310 VAL A O   1 
ATOM   2327 C CB  . VAL A 1 294 ? 15.147  4.444   29.015 1.00 24.15  ? 310 VAL A CB  1 
ATOM   2328 C CG1 . VAL A 1 294 ? 15.495  3.740   27.714 1.00 24.29  ? 310 VAL A CG1 1 
ATOM   2329 C CG2 . VAL A 1 294 ? 14.387  5.731   28.753 1.00 25.69  ? 310 VAL A CG2 1 
ATOM   2330 N N   . GLY A 1 295 ? 13.125  4.253   31.935 1.00 22.77  ? 311 GLY A N   1 
ATOM   2331 C CA  . GLY A 1 295 ? 12.942  4.739   33.297 1.00 24.24  ? 311 GLY A CA  1 
ATOM   2332 C C   . GLY A 1 295 ? 12.281  6.111   33.306 1.00 24.50  ? 311 GLY A C   1 
ATOM   2333 O O   . GLY A 1 295 ? 12.245  6.773   32.273 1.00 24.69  ? 311 GLY A O   1 
ATOM   2334 N N   . ASN A 1 296 ? 11.703  6.495   34.446 1.00 24.71  ? 312 ASN A N   1 
ATOM   2335 C CA  . ASN A 1 296 ? 11.231  7.861   34.615 1.00 29.56  ? 312 ASN A CA  1 
ATOM   2336 C C   . ASN A 1 296 ? 10.134  8.183   33.586 1.00 30.42  ? 312 ASN A C   1 
ATOM   2337 O O   . ASN A 1 296 ? 10.029  9.319   33.123 1.00 32.23  ? 312 ASN A O   1 
ATOM   2338 C CB  . ASN A 1 296 ? 12.382  8.864   34.485 1.00 31.08  ? 312 ASN A CB  1 
ATOM   2339 C CG  . ASN A 1 296 ? 13.428  8.751   35.575 1.00 32.27  ? 312 ASN A CG  1 
ATOM   2340 O OD1 . ASN A 1 296 ? 14.588  8.442   35.323 1.00 34.72  ? 312 ASN A OD1 1 
ATOM   2341 N ND2 . ASN A 1 296 ? 13.025  9.011   36.797 1.00 34.65  ? 312 ASN A ND2 1 
ATOM   2342 N N   . LYS A 1 297 ? 9.366   7.166   33.181 1.00 30.38  ? 313 LYS A N   1 
ATOM   2343 C CA  . LYS A 1 297 ? 8.210   7.328   32.312 1.00 31.77  ? 313 LYS A CA  1 
ATOM   2344 C C   . LYS A 1 297 ? 8.602   7.685   30.880 1.00 32.63  ? 313 LYS A C   1 
ATOM   2345 O O   . LYS A 1 297 ? 7.818   8.333   30.181 1.00 34.37  ? 313 LYS A O   1 
ATOM   2346 C CB  . LYS A 1 297 ? 7.311   8.454   32.825 1.00 33.83  ? 313 LYS A CB  1 
ATOM   2347 C CG  . LYS A 1 297 ? 6.952   8.412   34.301 1.00 33.98  ? 313 LYS A CG  1 
ATOM   2348 C CD  . LYS A 1 297 ? 6.117   7.224   34.689 1.00 38.72  ? 313 LYS A CD  1 
ATOM   2349 C CE  . LYS A 1 297 ? 5.532   7.437   36.067 1.00 39.78  ? 313 LYS A CE  1 
ATOM   2350 N NZ  . LYS A 1 297 ? 4.805   6.236   36.506 1.00 41.76  ? 313 LYS A NZ  1 
ATOM   2351 N N   . PHE A 1 298 ? 9.818   7.304   30.460 1.00 29.24  ? 314 PHE A N   1 
ATOM   2352 C CA  . PHE A 1 298 ? 10.241  7.520   29.094 1.00 27.71  ? 314 PHE A CA  1 
ATOM   2353 C C   . PHE A 1 298 ? 10.373  6.183   28.376 1.00 28.12  ? 314 PHE A C   1 
ATOM   2354 O O   . PHE A 1 298 ? 10.785  5.197   28.977 1.00 24.97  ? 314 PHE A O   1 
ATOM   2355 C CB  . PHE A 1 298 ? 11.586  8.242   29.068 1.00 30.68  ? 314 PHE A CB  1 
ATOM   2356 C CG  . PHE A 1 298 ? 11.550  9.706   29.401 1.00 32.55  ? 314 PHE A CG  1 
ATOM   2357 C CD1 . PHE A 1 298 ? 11.074  10.631  28.483 1.00 36.19  ? 314 PHE A CD1 1 
ATOM   2358 C CD2 . PHE A 1 298 ? 12.024  10.178  30.621 1.00 35.65  ? 314 PHE A CD2 1 
ATOM   2359 C CE1 . PHE A 1 298 ? 11.062  11.992  28.775 1.00 33.04  ? 314 PHE A CE1 1 
ATOM   2360 C CE2 . PHE A 1 298 ? 12.026  11.541  30.906 1.00 34.65  ? 314 PHE A CE2 1 
ATOM   2361 C CZ  . PHE A 1 298 ? 11.529  12.442  29.991 1.00 34.67  ? 314 PHE A CZ  1 
ATOM   2362 N N   . ILE A 1 299 ? 10.041  6.179   27.081 1.00 29.19  ? 315 ILE A N   1 
ATOM   2363 C CA  . ILE A 1 299 ? 10.316  5.062   26.191 1.00 30.47  ? 315 ILE A CA  1 
ATOM   2364 C C   . ILE A 1 299 ? 11.314  5.537   25.137 1.00 30.70  ? 315 ILE A C   1 
ATOM   2365 O O   . ILE A 1 299 ? 11.332  6.718   24.783 1.00 28.78  ? 315 ILE A O   1 
ATOM   2366 C CB  . ILE A 1 299 ? 9.019   4.513   25.569 1.00 33.86  ? 315 ILE A CB  1 
ATOM   2367 C CG1 . ILE A 1 299 ? 8.264   5.585   24.795 1.00 36.55  ? 315 ILE A CG1 1 
ATOM   2368 C CG2 . ILE A 1 299 ? 8.121   3.882   26.637 1.00 34.72  ? 315 ILE A CG2 1 
ATOM   2369 C CD1 . ILE A 1 299 ? 7.279   5.001   23.809 1.00 43.23  ? 315 ILE A CD1 1 
ATOM   2370 N N   . GLN A 1 300 ? 12.181  4.623   24.690 1.00 28.29  ? 316 GLN A N   1 
ATOM   2371 C CA  . GLN A 1 300 ? 13.193  4.941   23.697 1.00 29.91  ? 316 GLN A CA  1 
ATOM   2372 C C   . GLN A 1 300 ? 13.085  3.941   22.545 1.00 31.37  ? 316 GLN A C   1 
ATOM   2373 O O   . GLN A 1 300 ? 13.184  2.733   22.740 1.00 27.47  ? 316 GLN A O   1 
ATOM   2374 C CB  . GLN A 1 300 ? 14.597  4.970   24.313 1.00 29.52  ? 316 GLN A CB  1 
ATOM   2375 C CG  . GLN A 1 300 ? 15.709  5.225   23.293 1.00 28.36  ? 316 GLN A CG  1 
ATOM   2376 C CD  . GLN A 1 300 ? 17.019  5.612   23.934 1.00 29.57  ? 316 GLN A CD  1 
ATOM   2377 O OE1 . GLN A 1 300 ? 17.082  5.989   25.101 1.00 29.33  ? 316 GLN A OE1 1 
ATOM   2378 N NE2 . GLN A 1 300 ? 18.087  5.525   23.166 1.00 28.98  ? 316 GLN A NE2 1 
ATOM   2379 N N   . GLU A 1 301 ? 12.923  4.470   21.328 1.00 32.31  ? 317 GLU A N   1 
ATOM   2380 C CA  . GLU A 1 301 ? 12.880  3.635   20.139 1.00 38.21  ? 317 GLU A CA  1 
ATOM   2381 C C   . GLU A 1 301 ? 14.207  2.901   20.021 1.00 37.84  ? 317 GLU A C   1 
ATOM   2382 O O   . GLU A 1 301 ? 15.257  3.487   20.289 1.00 31.27  ? 317 GLU A O   1 
ATOM   2383 C CB  . GLU A 1 301 ? 12.630  4.473   18.876 1.00 44.06  ? 317 GLU A CB  1 
ATOM   2384 C CG  . GLU A 1 301 ? 11.285  5.204   18.875 1.00 50.64  ? 317 GLU A CG  1 
ATOM   2385 C CD  . GLU A 1 301 ? 11.057  6.266   17.800 1.00 54.20  ? 317 GLU A CD  1 
ATOM   2386 O OE1 . GLU A 1 301 ? 11.824  6.307   16.810 1.00 53.16  ? 317 GLU A OE1 1 
ATOM   2387 O OE2 . GLU A 1 301 ? 10.122  7.076   17.973 1.00 56.37  ? 317 GLU A OE2 1 
ATOM   2388 N N   . VAL A 1 302 ? 14.121  1.623   19.632 1.00 41.49  ? 318 VAL A N   1 
ATOM   2389 C CA  . VAL A 1 302 ? 15.278  0.773   19.412 1.00 48.32  ? 318 VAL A CA  1 
ATOM   2390 C C   . VAL A 1 302 ? 15.013  -0.061  18.158 1.00 51.04  ? 318 VAL A C   1 
ATOM   2391 O O   . VAL A 1 302 ? 13.862  -0.250  17.795 1.00 52.76  ? 318 VAL A O   1 
ATOM   2392 C CB  . VAL A 1 302 ? 15.562  -0.096  20.659 1.00 53.84  ? 318 VAL A CB  1 
ATOM   2393 C CG1 . VAL A 1 302 ? 16.140  0.723   21.805 1.00 56.45  ? 318 VAL A CG1 1 
ATOM   2394 C CG2 . VAL A 1 302 ? 14.331  -0.827  21.158 1.00 55.23  ? 318 VAL A CG2 1 
ATOM   2395 N N   . ALA A 1 303 ? 16.081  -0.531  17.496 1.00 57.16  ? 319 ALA A N   1 
ATOM   2396 C CA  . ALA A 1 303 ? 15.974  -1.484  16.394 1.00 62.26  ? 319 ALA A CA  1 
ATOM   2397 C C   . ALA A 1 303 ? 17.291  -2.257  16.234 1.00 57.94  ? 319 ALA A C   1 
ATOM   2398 O O   . ALA A 1 303 ? 17.986  -2.425  17.263 1.00 48.52  ? 319 ALA A O   1 
ATOM   2399 C CB  . ALA A 1 303 ? 15.609  -0.777  15.118 1.00 63.30  ? 319 ALA A CB  1 
ATOM   2400 N N   . GLY B 1 2   ? -4.645  6.165   40.770 1.00 32.63  ? 18  GLY B N   1 
ATOM   2401 C CA  . GLY B 1 2   ? -5.067  4.912   41.418 1.00 32.22  ? 18  GLY B CA  1 
ATOM   2402 C C   . GLY B 1 2   ? -4.993  3.736   40.453 1.00 29.50  ? 18  GLY B C   1 
ATOM   2403 O O   . GLY B 1 2   ? -4.405  3.838   39.392 1.00 25.71  ? 18  GLY B O   1 
ATOM   2404 N N   . LYS B 1 3   ? -5.569  2.615   40.863 1.00 30.33  ? 19  LYS B N   1 
ATOM   2405 C CA  . LYS B 1 3   ? -5.596  1.432   40.024 1.00 32.75  ? 19  LYS B CA  1 
ATOM   2406 C C   . LYS B 1 3   ? -6.744  1.566   39.030 1.00 30.16  ? 19  LYS B C   1 
ATOM   2407 O O   . LYS B 1 3   ? -7.842  1.922   39.441 1.00 27.04  ? 19  LYS B O   1 
ATOM   2408 C CB  . LYS B 1 3   ? -5.813  0.198   40.899 1.00 38.34  ? 19  LYS B CB  1 
ATOM   2409 C CG  . LYS B 1 3   ? -5.574  -1.141  40.208 1.00 42.25  ? 19  LYS B CG  1 
ATOM   2410 C CD  . LYS B 1 3   ? -5.661  -2.327  41.159 1.00 43.79  ? 19  LYS B CD  1 
ATOM   2411 C CE  . LYS B 1 3   ? -7.013  -2.447  41.834 1.00 47.26  ? 19  LYS B CE  1 
ATOM   2412 N NZ  . LYS B 1 3   ? -8.077  -2.789  40.865 1.00 51.41  ? 19  LYS B NZ  1 
ATOM   2413 N N   . VAL B 1 4   ? -6.496  1.226   37.755 1.00 29.03  ? 20  VAL B N   1 
ATOM   2414 C CA  . VAL B 1 4   ? -7.523  1.306   36.731 1.00 28.08  ? 20  VAL B CA  1 
ATOM   2415 C C   . VAL B 1 4   ? -8.503  0.171   36.989 1.00 29.88  ? 20  VAL B C   1 
ATOM   2416 O O   . VAL B 1 4   ? -8.082  -0.968  37.163 1.00 34.02  ? 20  VAL B O   1 
ATOM   2417 C CB  . VAL B 1 4   ? -6.916  1.245   35.314 1.00 30.05  ? 20  VAL B CB  1 
ATOM   2418 C CG1 . VAL B 1 4   ? -7.988  1.356   34.240 1.00 29.54  ? 20  VAL B CG1 1 
ATOM   2419 C CG2 . VAL B 1 4   ? -5.851  2.315   35.112 1.00 30.16  ? 20  VAL B CG2 1 
ATOM   2420 N N   . LEU B 1 5   ? -9.784  0.506   37.106 1.00 27.49  ? 21  LEU B N   1 
ATOM   2421 C CA  . LEU B 1 5   ? -10.829 -0.471  37.352 1.00 27.69  ? 21  LEU B CA  1 
ATOM   2422 C C   . LEU B 1 5   ? -11.469 -0.902  36.037 1.00 29.71  ? 21  LEU B C   1 
ATOM   2423 O O   . LEU B 1 5   ? -11.947 -2.028  35.942 1.00 27.17  ? 21  LEU B O   1 
ATOM   2424 C CB  . LEU B 1 5   ? -11.892 0.127   38.268 1.00 27.00  ? 21  LEU B CB  1 
ATOM   2425 C CG  . LEU B 1 5   ? -11.398 0.705   39.593 1.00 29.69  ? 21  LEU B CG  1 
ATOM   2426 C CD1 . LEU B 1 5   ? -12.564 1.269   40.388 1.00 27.46  ? 21  LEU B CD1 1 
ATOM   2427 C CD2 . LEU B 1 5   ? -10.625 -0.332  40.411 1.00 27.47  ? 21  LEU B CD2 1 
ATOM   2428 N N   . TRP B 1 6   ? -11.523 0.023   35.066 1.00 27.20  ? 22  TRP B N   1 
ATOM   2429 C CA  . TRP B 1 6   ? -11.978 -0.252  33.714 1.00 25.78  ? 22  TRP B CA  1 
ATOM   2430 C C   . TRP B 1 6   ? -11.353 0.798   32.806 1.00 25.68  ? 22  TRP B C   1 
ATOM   2431 O O   . TRP B 1 6   ? -11.325 1.965   33.179 1.00 26.75  ? 22  TRP B O   1 
ATOM   2432 C CB  . TRP B 1 6   ? -13.512 -0.207  33.640 1.00 25.79  ? 22  TRP B CB  1 
ATOM   2433 C CG  . TRP B 1 6   ? -14.070 -0.132  32.242 1.00 24.62  ? 22  TRP B CG  1 
ATOM   2434 C CD1 . TRP B 1 6   ? -14.378 -1.162  31.402 1.00 26.92  ? 22  TRP B CD1 1 
ATOM   2435 C CD2 . TRP B 1 6   ? -14.412 1.069   31.524 1.00 24.69  ? 22  TRP B CD2 1 
ATOM   2436 N NE1 . TRP B 1 6   ? -14.839 -0.690  30.200 1.00 26.85  ? 22  TRP B NE1 1 
ATOM   2437 C CE2 . TRP B 1 6   ? -14.882 0.678   30.251 1.00 25.03  ? 22  TRP B CE2 1 
ATOM   2438 C CE3 . TRP B 1 6   ? -14.341 2.424   31.827 1.00 24.32  ? 22  TRP B CE3 1 
ATOM   2439 C CZ2 . TRP B 1 6   ? -15.285 1.603   29.293 1.00 24.50  ? 22  TRP B CZ2 1 
ATOM   2440 C CZ3 . TRP B 1 6   ? -14.760 3.339   30.887 1.00 27.86  ? 22  TRP B CZ3 1 
ATOM   2441 C CH2 . TRP B 1 6   ? -15.228 2.931   29.635 1.00 26.18  ? 22  TRP B CH2 1 
ATOM   2442 N N   . ASP B 1 7   ? -10.873 0.398   31.627 1.00 25.42  ? 23  ASP B N   1 
ATOM   2443 C CA  . ASP B 1 7   ? -10.210 1.323   30.729 1.00 24.61  ? 23  ASP B CA  1 
ATOM   2444 C C   . ASP B 1 7   ? -10.962 1.383   29.398 1.00 25.87  ? 23  ASP B C   1 
ATOM   2445 O O   . ASP B 1 7   ? -10.925 0.444   28.594 1.00 24.24  ? 23  ASP B O   1 
ATOM   2446 C CB  . ASP B 1 7   ? -8.754  0.918   30.566 1.00 25.26  ? 23  ASP B CB  1 
ATOM   2447 C CG  . ASP B 1 7   ? -7.849  1.998   29.994 1.00 24.76  ? 23  ASP B CG  1 
ATOM   2448 O OD1 . ASP B 1 7   ? -8.350  2.990   29.429 1.00 23.37  ? 23  ASP B OD1 1 
ATOM   2449 O OD2 . ASP B 1 7   ? -6.647  1.832   30.120 1.00 23.91  ? 23  ASP B OD2 1 
ATOM   2450 N N   . GLY B 1 8   ? -11.612 2.529   29.156 1.00 26.26  ? 24  GLY B N   1 
ATOM   2451 C CA  . GLY B 1 8   ? -12.299 2.800   27.897 1.00 24.46  ? 24  GLY B CA  1 
ATOM   2452 C C   . GLY B 1 8   ? -11.482 3.634   26.916 1.00 24.77  ? 24  GLY B C   1 
ATOM   2453 O O   . GLY B 1 8   ? -12.017 4.152   25.938 1.00 21.20  ? 24  GLY B O   1 
ATOM   2454 N N   . ARG B 1 9   ? -10.170 3.722   27.146 1.00 23.70  ? 25  ARG B N   1 
ATOM   2455 C CA  . ARG B 1 9   ? -9.292  4.377   26.193 1.00 24.89  ? 25  ARG B CA  1 
ATOM   2456 C C   . ARG B 1 9   ? -8.993  3.397   25.067 1.00 25.38  ? 25  ARG B C   1 
ATOM   2457 O O   . ARG B 1 9   ? -8.281  2.426   25.284 1.00 28.66  ? 25  ARG B O   1 
ATOM   2458 C CB  . ARG B 1 9   ? -8.025  4.863   26.904 1.00 25.48  ? 25  ARG B CB  1 
ATOM   2459 C CG  . ARG B 1 9   ? -8.279  6.036   27.845 1.00 24.82  ? 25  ARG B CG  1 
ATOM   2460 C CD  . ARG B 1 9   ? -7.102  6.398   28.725 1.00 25.90  ? 25  ARG B CD  1 
ATOM   2461 N NE  . ARG B 1 9   ? -6.721  5.318   29.622 1.00 25.14  ? 25  ARG B NE  1 
ATOM   2462 C CZ  . ARG B 1 9   ? -5.911  5.431   30.672 1.00 25.17  ? 25  ARG B CZ  1 
ATOM   2463 N NH1 . ARG B 1 9   ? -5.397  6.596   31.006 1.00 26.96  ? 25  ARG B NH1 1 
ATOM   2464 N NH2 . ARG B 1 9   ? -5.657  4.373   31.421 1.00 23.17  ? 25  ARG B NH2 1 
ATOM   2465 N N   . ALA B 1 10  ? -9.568  3.638   23.883 1.00 26.41  ? 26  ALA B N   1 
ATOM   2466 C CA  . ALA B 1 10  ? -9.602  2.626   22.839 1.00 23.66  ? 26  ALA B CA  1 
ATOM   2467 C C   . ALA B 1 10  ? -8.173  2.311   22.447 1.00 24.94  ? 26  ALA B C   1 
ATOM   2468 O O   . ALA B 1 10  ? -7.428  3.223   22.070 1.00 28.12  ? 26  ALA B O   1 
ATOM   2469 C CB  . ALA B 1 10  ? -10.364 3.097   21.635 1.00 23.57  ? 26  ALA B CB  1 
ATOM   2470 N N   . PRO B 1 11  ? -7.738  1.036   22.532 1.00 27.20  ? 27  PRO B N   1 
ATOM   2471 C CA  . PRO B 1 11  ? -6.417  0.669   22.031 1.00 29.82  ? 27  PRO B CA  1 
ATOM   2472 C C   . PRO B 1 11  ? -6.239  1.075   20.570 1.00 30.22  ? 27  PRO B C   1 
ATOM   2473 O O   . PRO B 1 11  ? -7.201  1.167   19.810 1.00 30.89  ? 27  PRO B O   1 
ATOM   2474 C CB  . PRO B 1 11  ? -6.379  -0.853  22.243 1.00 32.05  ? 27  PRO B CB  1 
ATOM   2475 C CG  . PRO B 1 11  ? -7.290  -1.074  23.419 1.00 29.37  ? 27  PRO B CG  1 
ATOM   2476 C CD  . PRO B 1 11  ? -8.427  -0.095  23.176 1.00 29.10  ? 27  PRO B CD  1 
ATOM   2477 N N   . ARG B 1 12  ? -4.991  1.332   20.188 1.00 30.52  ? 28  ARG B N   1 
ATOM   2478 C CA  . ARG B 1 12  ? -4.660  1.684   18.816 1.00 33.74  ? 28  ARG B CA  1 
ATOM   2479 C C   . ARG B 1 12  ? -5.026  0.546   17.863 1.00 34.17  ? 28  ARG B C   1 
ATOM   2480 O O   . ARG B 1 12  ? -5.297  0.808   16.701 1.00 34.70  ? 28  ARG B O   1 
ATOM   2481 C CB  . ARG B 1 12  ? -3.179  2.058   18.709 1.00 31.86  ? 28  ARG B CB  1 
ATOM   2482 C CG  . ARG B 1 12  ? -2.842  3.393   19.356 1.00 38.52  ? 28  ARG B CG  1 
ATOM   2483 C CD  . ARG B 1 12  ? -1.341  3.603   19.510 1.00 39.99  ? 28  ARG B CD  1 
ATOM   2484 N NE  . ARG B 1 12  ? -0.752  2.714   20.508 1.00 43.19  ? 28  ARG B NE  1 
ATOM   2485 C CZ  . ARG B 1 12  ? 0.554   2.647   20.808 1.00 45.90  ? 28  ARG B CZ  1 
ATOM   2486 N NH1 . ARG B 1 12  ? 1.426   3.417   20.181 1.00 44.89  ? 28  ARG B NH1 1 
ATOM   2487 N NH2 . ARG B 1 12  ? 0.993   1.809   21.736 1.00 41.76  ? 28  ARG B NH2 1 
ATOM   2488 N N   . ASN B 1 13  ? -5.090  -0.702  18.350 1.00 33.95  ? 29  ASN B N   1 
ATOM   2489 C CA  . ASN B 1 13  ? -5.402  -1.827  17.477 1.00 37.28  ? 29  ASN B CA  1 
ATOM   2490 C C   . ASN B 1 13  ? -6.908  -2.103  17.420 1.00 36.06  ? 29  ASN B C   1 
ATOM   2491 O O   . ASN B 1 13  ? -7.326  -2.968  16.655 1.00 34.93  ? 29  ASN B O   1 
ATOM   2492 C CB  . ASN B 1 13  ? -4.632  -3.102  17.859 1.00 40.11  ? 29  ASN B CB  1 
ATOM   2493 C CG  . ASN B 1 13  ? -4.743  -3.490  19.321 1.00 45.61  ? 29  ASN B CG  1 
ATOM   2494 O OD1 . ASN B 1 13  ? -5.817  -3.467  19.932 1.00 45.77  ? 29  ASN B OD1 1 
ATOM   2495 N ND2 . ASN B 1 13  ? -3.612  -3.849  19.905 1.00 54.40  ? 29  ASN B ND2 1 
ATOM   2496 N N   . TYR B 1 14  ? -7.723  -1.372  18.208 1.00 32.31  ? 30  TYR B N   1 
ATOM   2497 C CA  . TYR B 1 14  ? -9.166  -1.613  18.263 1.00 31.41  ? 30  TYR B CA  1 
ATOM   2498 C C   . TYR B 1 14  ? -9.816  -1.281  16.919 1.00 28.76  ? 30  TYR B C   1 
ATOM   2499 O O   . TYR B 1 14  ? -9.395  -0.357  16.247 1.00 28.76  ? 30  TYR B O   1 
ATOM   2500 C CB  . TYR B 1 14  ? -9.851  -0.762  19.340 1.00 29.78  ? 30  TYR B CB  1 
ATOM   2501 C CG  . TYR B 1 14  ? -11.031 -1.403  20.048 1.00 28.35  ? 30  TYR B CG  1 
ATOM   2502 C CD1 . TYR B 1 14  ? -10.828 -2.468  20.919 1.00 28.81  ? 30  TYR B CD1 1 
ATOM   2503 C CD2 . TYR B 1 14  ? -12.338 -0.936  19.882 1.00 28.62  ? 30  TYR B CD2 1 
ATOM   2504 C CE1 . TYR B 1 14  ? -11.886 -3.073  21.587 1.00 29.35  ? 30  TYR B CE1 1 
ATOM   2505 C CE2 . TYR B 1 14  ? -13.406 -1.543  20.539 1.00 28.80  ? 30  TYR B CE2 1 
ATOM   2506 C CZ  . TYR B 1 14  ? -13.180 -2.598  21.412 1.00 29.67  ? 30  TYR B CZ  1 
ATOM   2507 O OH  . TYR B 1 14  ? -14.203 -3.202  22.103 1.00 29.06  ? 30  TYR B OH  1 
ATOM   2508 N N   . THR B 1 15  ? -10.868 -2.025  16.562 1.00 29.02  ? 31  THR B N   1 
ATOM   2509 C CA  . THR B 1 15  ? -11.484 -1.945  15.249 1.00 31.04  ? 31  THR B CA  1 
ATOM   2510 C C   . THR B 1 15  ? -13.012 -1.922  15.339 1.00 29.64  ? 31  THR B C   1 
ATOM   2511 O O   . THR B 1 15  ? -13.623 -2.296  16.345 1.00 31.20  ? 31  THR B O   1 
ATOM   2512 C CB  . THR B 1 15  ? -11.078 -3.126  14.352 1.00 29.91  ? 31  THR B CB  1 
ATOM   2513 O OG1 . THR B 1 15  ? -11.578 -4.316  14.957 1.00 32.35  ? 31  THR B OG1 1 
ATOM   2514 C CG2 . THR B 1 15  ? -9.579  -3.210  14.137 1.00 34.53  ? 31  THR B CG2 1 
ATOM   2515 N N   . SER B 1 16  ? -13.612 -1.526  14.216 1.00 29.75  ? 32  SER B N   1 
ATOM   2516 C CA  . SER B 1 16  ? -15.036 -1.645  13.964 1.00 31.35  ? 32  SER B CA  1 
ATOM   2517 C C   . SER B 1 16  ? -15.582 -3.043  14.293 1.00 34.91  ? 32  SER B C   1 
ATOM   2518 O O   . SER B 1 16  ? -16.718 -3.183  14.758 1.00 32.10  ? 32  SER B O   1 
ATOM   2519 C CB  . SER B 1 16  ? -15.275 -1.277  12.532 1.00 33.74  ? 32  SER B CB  1 
ATOM   2520 O OG  . SER B 1 16  ? -14.720 -2.240  11.660 1.00 34.44  ? 32  SER B OG  1 
ATOM   2521 N N   . PHE B 1 17  ? -14.783 -4.088  14.052 1.00 29.25  ? 33  PHE B N   1 
ATOM   2522 C CA  . PHE B 1 17  ? -15.217 -5.464  14.264 1.00 31.18  ? 33  PHE B CA  1 
ATOM   2523 C C   . PHE B 1 17  ? -15.320 -5.785  15.754 1.00 31.35  ? 33  PHE B C   1 
ATOM   2524 O O   . PHE B 1 17  ? -16.189 -6.548  16.185 1.00 31.76  ? 33  PHE B O   1 
ATOM   2525 C CB  . PHE B 1 17  ? -14.257 -6.410  13.534 1.00 33.32  ? 33  PHE B CB  1 
ATOM   2526 C CG  . PHE B 1 17  ? -14.398 -6.284  12.045 1.00 31.95  ? 33  PHE B CG  1 
ATOM   2527 C CD1 . PHE B 1 17  ? -15.449 -6.906  11.388 1.00 36.67  ? 33  PHE B CD1 1 
ATOM   2528 C CD2 . PHE B 1 17  ? -13.577 -5.440  11.330 1.00 31.25  ? 33  PHE B CD2 1 
ATOM   2529 C CE1 . PHE B 1 17  ? -15.638 -6.721  10.030 1.00 32.08  ? 33  PHE B CE1 1 
ATOM   2530 C CE2 . PHE B 1 17  ? -13.768 -5.261  9.971  1.00 30.90  ? 33  PHE B CE2 1 
ATOM   2531 C CZ  . PHE B 1 17  ? -14.797 -5.897  9.332  1.00 31.05  ? 33  PHE B CZ  1 
ATOM   2532 N N   . HIS B 1 18  ? -14.419 -5.218  16.552 1.00 29.60  ? 34  HIS B N   1 
ATOM   2533 C CA  . HIS B 1 18  ? -14.565 -5.332  17.987 1.00 28.99  ? 34  HIS B CA  1 
ATOM   2534 C C   . HIS B 1 18  ? -15.890 -4.704  18.419 1.00 31.09  ? 34  HIS B C   1 
ATOM   2535 O O   . HIS B 1 18  ? -16.630 -5.292  19.215 1.00 30.06  ? 34  HIS B O   1 
ATOM   2536 C CB  . HIS B 1 18  ? -13.426 -4.618  18.716 1.00 32.00  ? 34  HIS B CB  1 
ATOM   2537 C CG  . HIS B 1 18  ? -12.073 -5.233  18.608 1.00 33.35  ? 34  HIS B CG  1 
ATOM   2538 N ND1 . HIS B 1 18  ? -11.175 -4.985  17.592 1.00 33.42  ? 34  HIS B ND1 1 
ATOM   2539 C CD2 . HIS B 1 18  ? -11.442 -5.996  19.494 1.00 35.56  ? 34  HIS B CD2 1 
ATOM   2540 C CE1 . HIS B 1 18  ? -10.060 -5.646  17.846 1.00 37.24  ? 34  HIS B CE1 1 
ATOM   2541 N NE2 . HIS B 1 18  ? -10.193 -6.259  19.000 1.00 36.58  ? 34  HIS B NE2 1 
ATOM   2542 N N   . LEU B 1 19  ? -16.142 -3.475  17.942 1.00 30.67  ? 35  LEU B N   1 
ATOM   2543 C CA  . LEU B 1 19  ? -17.362 -2.766  18.296 1.00 30.88  ? 35  LEU B CA  1 
ATOM   2544 C C   . LEU B 1 19  ? -18.596 -3.595  17.925 1.00 32.61  ? 35  LEU B C   1 
ATOM   2545 O O   . LEU B 1 19  ? -19.520 -3.738  18.721 1.00 32.34  ? 35  LEU B O   1 
ATOM   2546 C CB  . LEU B 1 19  ? -17.410 -1.404  17.602 1.00 28.09  ? 35  LEU B CB  1 
ATOM   2547 C CG  . LEU B 1 19  ? -16.583 -0.287  18.235 1.00 27.28  ? 35  LEU B CG  1 
ATOM   2548 C CD1 . LEU B 1 19  ? -16.628 0.954   17.369 1.00 28.53  ? 35  LEU B CD1 1 
ATOM   2549 C CD2 . LEU B 1 19  ? -17.054 0.026   19.646 1.00 26.56  ? 35  LEU B CD2 1 
ATOM   2550 N N   . ASP B 1 20  ? -18.611 -4.171  16.729 1.00 33.44  ? 36  ASP B N   1 
ATOM   2551 C CA  . ASP B 1 20  ? -19.786 -4.914  16.279 1.00 32.77  ? 36  ASP B CA  1 
ATOM   2552 C C   . ASP B 1 20  ? -19.910 -6.255  17.002 1.00 33.52  ? 36  ASP B C   1 
ATOM   2553 O O   . ASP B 1 20  ? -20.927 -6.927  16.882 1.00 36.04  ? 36  ASP B O   1 
ATOM   2554 C CB  . ASP B 1 20  ? -19.742 -5.083  14.761 1.00 34.30  ? 36  ASP B CB  1 
ATOM   2555 C CG  . ASP B 1 20  ? -19.785 -3.753  14.033 1.00 32.81  ? 36  ASP B CG  1 
ATOM   2556 O OD1 . ASP B 1 20  ? -20.305 -2.776  14.619 1.00 31.86  ? 36  ASP B OD1 1 
ATOM   2557 O OD2 . ASP B 1 20  ? -19.235 -3.682  12.933 1.00 32.59  ? 36  ASP B OD2 1 
ATOM   2558 N N   . ALA B 1 21  ? -18.870 -6.674  17.734 1.00 33.53  ? 37  ALA B N   1 
ATOM   2559 C CA  . ALA B 1 21  ? -18.958 -7.881  18.539 1.00 33.78  ? 37  ALA B CA  1 
ATOM   2560 C C   . ALA B 1 21  ? -19.341 -7.522  19.965 1.00 32.52  ? 37  ALA B C   1 
ATOM   2561 O O   . ALA B 1 21  ? -19.604 -8.416  20.770 1.00 32.03  ? 37  ALA B O   1 
ATOM   2562 C CB  . ALA B 1 21  ? -17.652 -8.640  18.483 1.00 37.03  ? 37  ALA B CB  1 
ATOM   2563 N N   . SER B 1 22  ? -19.383 -6.211  20.272 1.00 30.40  ? 38  SER B N   1 
ATOM   2564 C CA  . SER B 1 22  ? -19.694 -5.752  21.616 1.00 31.15  ? 38  SER B CA  1 
ATOM   2565 C C   . SER B 1 22  ? -18.751 -6.399  22.637 1.00 29.71  ? 38  SER B C   1 
ATOM   2566 O O   . SER B 1 22  ? -19.205 -6.887  23.664 1.00 32.16  ? 38  SER B O   1 
ATOM   2567 C CB  . SER B 1 22  ? -21.152 -6.021  21.958 1.00 32.05  ? 38  SER B CB  1 
ATOM   2568 O OG  . SER B 1 22  ? -21.512 -5.388  23.188 1.00 30.38  ? 38  SER B OG  1 
ATOM   2569 N N   . VAL B 1 23  ? -17.437 -6.403  22.368 1.00 28.54  ? 39  VAL B N   1 
ATOM   2570 C CA  . VAL B 1 23  ? -16.495 -6.975  23.322 1.00 34.01  ? 39  VAL B CA  1 
ATOM   2571 C C   . VAL B 1 23  ? -15.896 -5.882  24.217 1.00 35.96  ? 39  VAL B C   1 
ATOM   2572 O O   . VAL B 1 23  ? -16.107 -4.673  24.047 1.00 29.57  ? 39  VAL B O   1 
ATOM   2573 C CB  . VAL B 1 23  ? -15.361 -7.797  22.668 1.00 33.27  ? 39  VAL B CB  1 
ATOM   2574 C CG1 . VAL B 1 23  ? -15.862 -9.134  22.151 1.00 34.36  ? 39  VAL B CG1 1 
ATOM   2575 C CG2 . VAL B 1 23  ? -14.617 -7.017  21.591 1.00 31.63  ? 39  VAL B CG2 1 
ATOM   2576 N N   . ASP B 1 24  ? -15.119 -6.358  25.187 1.00 30.73  ? 40  ASP B N   1 
ATOM   2577 C CA  . ASP B 1 24  ? -14.434 -5.468  26.098 1.00 29.27  ? 40  ASP B CA  1 
ATOM   2578 C C   . ASP B 1 24  ? -13.638 -4.454  25.278 1.00 27.96  ? 40  ASP B C   1 
ATOM   2579 O O   . ASP B 1 24  ? -13.106 -4.755  24.204 1.00 30.29  ? 40  ASP B O   1 
ATOM   2580 C CB  . ASP B 1 24  ? -13.595 -6.279  27.089 1.00 29.32  ? 40  ASP B CB  1 
ATOM   2581 C CG  . ASP B 1 24  ? -14.395 -6.936  28.208 1.00 29.79  ? 40  ASP B CG  1 
ATOM   2582 O OD1 . ASP B 1 24  ? -15.616 -6.793  28.236 1.00 30.47  ? 40  ASP B OD1 1 
ATOM   2583 O OD2 . ASP B 1 24  ? -13.783 -7.561  29.077 1.00 28.57  ? 40  ASP B OD2 1 
ATOM   2584 N N   . PRO B 1 25  ? -13.516 -3.193  25.744 1.00 28.18  ? 41  PRO B N   1 
ATOM   2585 C CA  . PRO B 1 25  ? -14.201 -2.709  26.949 1.00 26.45  ? 41  PRO B CA  1 
ATOM   2586 C C   . PRO B 1 25  ? -15.610 -2.118  26.878 1.00 26.30  ? 41  PRO B C   1 
ATOM   2587 O O   . PRO B 1 25  ? -16.039 -1.523  27.857 1.00 25.94  ? 41  PRO B O   1 
ATOM   2588 C CB  . PRO B 1 25  ? -13.245 -1.568  27.364 1.00 26.16  ? 41  PRO B CB  1 
ATOM   2589 C CG  . PRO B 1 25  ? -12.747 -1.016  26.079 1.00 27.49  ? 41  PRO B CG  1 
ATOM   2590 C CD  . PRO B 1 25  ? -12.555 -2.225  25.206 1.00 27.92  ? 41  PRO B CD  1 
ATOM   2591 N N   . TYR B 1 26  ? -16.336 -2.269  25.763 1.00 26.01  ? 42  TYR B N   1 
ATOM   2592 C CA  . TYR B 1 26  ? -17.598 -1.551  25.602 1.00 28.18  ? 42  TYR B CA  1 
ATOM   2593 C C   . TYR B 1 26  ? -18.787 -2.448  25.254 1.00 25.00  ? 42  TYR B C   1 
ATOM   2594 O O   . TYR B 1 26  ? -18.728 -3.201  24.289 1.00 23.94  ? 42  TYR B O   1 
ATOM   2595 C CB  . TYR B 1 26  ? -17.497 -0.569  24.432 1.00 26.04  ? 42  TYR B CB  1 
ATOM   2596 C CG  . TYR B 1 26  ? -16.235 0.263   24.355 1.00 25.35  ? 42  TYR B CG  1 
ATOM   2597 C CD1 . TYR B 1 26  ? -15.972 1.278   25.271 1.00 25.26  ? 42  TYR B CD1 1 
ATOM   2598 C CD2 . TYR B 1 26  ? -15.338 0.089   23.312 1.00 27.30  ? 42  TYR B CD2 1 
ATOM   2599 C CE1 . TYR B 1 26  ? -14.815 2.040   25.178 1.00 25.47  ? 42  TYR B CE1 1 
ATOM   2600 C CE2 . TYR B 1 26  ? -14.198 0.871   23.188 1.00 24.86  ? 42  TYR B CE2 1 
ATOM   2601 C CZ  . TYR B 1 26  ? -13.923 1.833   24.139 1.00 25.09  ? 42  TYR B CZ  1 
ATOM   2602 O OH  . TYR B 1 26  ? -12.794 2.592   24.023 1.00 24.81  ? 42  TYR B OH  1 
ATOM   2603 N N   . LEU B 1 27  ? -19.880 -2.313  26.015 1.00 24.51  ? 43  LEU B N   1 
ATOM   2604 C CA  . LEU B 1 27  ? -21.186 -2.820  25.617 1.00 24.86  ? 43  LEU B CA  1 
ATOM   2605 C C   . LEU B 1 27  ? -21.864 -1.800  24.710 1.00 28.09  ? 43  LEU B C   1 
ATOM   2606 O O   . LEU B 1 27  ? -22.022 -0.647  25.099 1.00 27.39  ? 43  LEU B O   1 
ATOM   2607 C CB  . LEU B 1 27  ? -22.041 -3.076  26.854 1.00 27.30  ? 43  LEU B CB  1 
ATOM   2608 C CG  . LEU B 1 27  ? -23.510 -3.394  26.579 1.00 29.34  ? 43  LEU B CG  1 
ATOM   2609 C CD1 . LEU B 1 27  ? -23.641 -4.759  25.934 1.00 31.99  ? 43  LEU B CD1 1 
ATOM   2610 C CD2 . LEU B 1 27  ? -24.337 -3.319  27.861 1.00 29.48  ? 43  LEU B CD2 1 
ATOM   2611 N N   . THR B 1 28  ? -22.320 -2.242  23.533 1.00 26.61  ? 44  THR B N   1 
ATOM   2612 C CA  . THR B 1 28  ? -22.732 -1.325  22.491 1.00 26.20  ? 44  THR B CA  1 
ATOM   2613 C C   . THR B 1 28  ? -24.240 -1.363  22.203 1.00 29.08  ? 44  THR B C   1 
ATOM   2614 O O   . THR B 1 28  ? -24.679 -0.780  21.210 1.00 28.26  ? 44  THR B O   1 
ATOM   2615 C CB  . THR B 1 28  ? -21.906 -1.645  21.252 1.00 27.60  ? 44  THR B CB  1 
ATOM   2616 O OG1 . THR B 1 28  ? -22.244 -2.988  20.937 1.00 26.33  ? 44  THR B OG1 1 
ATOM   2617 C CG2 . THR B 1 28  ? -20.415 -1.528  21.473 1.00 26.90  ? 44  THR B CG2 1 
ATOM   2618 N N   . VAL B 1 29  ? -25.036 -1.969  23.095 1.00 27.33  ? 45  VAL B N   1 
ATOM   2619 C CA  . VAL B 1 29  ? -26.447 -2.223  22.852 1.00 28.17  ? 45  VAL B CA  1 
ATOM   2620 C C   . VAL B 1 29  ? -27.266 -0.928  22.709 1.00 30.17  ? 45  VAL B C   1 
ATOM   2621 O O   . VAL B 1 29  ? -28.292 -0.929  22.025 1.00 29.70  ? 45  VAL B O   1 
ATOM   2622 C CB  . VAL B 1 29  ? -27.049 -3.133  23.949 1.00 29.29  ? 45  VAL B CB  1 
ATOM   2623 C CG1 . VAL B 1 29  ? -27.141 -2.458  25.305 1.00 28.67  ? 45  VAL B CG1 1 
ATOM   2624 C CG2 . VAL B 1 29  ? -28.425 -3.668  23.570 1.00 31.23  ? 45  VAL B CG2 1 
ATOM   2625 N N   . VAL B 1 30  ? -26.879 0.176   23.371 1.00 28.29  ? 46  VAL B N   1 
ATOM   2626 C CA  . VAL B 1 30  ? -27.698 1.388   23.347 1.00 26.14  ? 46  VAL B CA  1 
ATOM   2627 C C   . VAL B 1 30  ? -27.426 2.169   22.063 1.00 26.19  ? 46  VAL B C   1 
ATOM   2628 O O   . VAL B 1 30  ? -26.510 2.992   21.964 1.00 24.35  ? 46  VAL B O   1 
ATOM   2629 C CB  . VAL B 1 30  ? -27.554 2.247   24.616 1.00 24.56  ? 46  VAL B CB  1 
ATOM   2630 C CG1 . VAL B 1 30  ? -28.423 3.497   24.571 1.00 23.39  ? 46  VAL B CG1 1 
ATOM   2631 C CG2 . VAL B 1 30  ? -27.916 1.415   25.832 1.00 27.12  ? 46  VAL B CG2 1 
ATOM   2632 N N   . LYS B 1 31  ? -28.259 1.877   21.058 1.00 25.58  ? 47  LYS B N   1 
ATOM   2633 C CA  . LYS B 1 31  ? -28.127 2.497   19.753 1.00 23.91  ? 47  LYS B CA  1 
ATOM   2634 C C   . LYS B 1 31  ? -29.361 2.161   18.932 1.00 25.28  ? 47  LYS B C   1 
ATOM   2635 O O   . LYS B 1 31  ? -30.213 1.387   19.378 1.00 27.29  ? 47  LYS B O   1 
ATOM   2636 C CB  . LYS B 1 31  ? -26.877 1.953   19.048 1.00 26.06  ? 47  LYS B CB  1 
ATOM   2637 C CG  . LYS B 1 31  ? -26.779 0.433   18.997 1.00 24.83  ? 47  LYS B CG  1 
ATOM   2638 C CD  . LYS B 1 31  ? -25.764 -0.061  17.995 1.00 26.55  ? 47  LYS B CD  1 
ATOM   2639 C CE  . LYS B 1 31  ? -25.704 -1.575  17.895 1.00 26.08  ? 47  LYS B CE  1 
ATOM   2640 N NZ  . LYS B 1 31  ? -26.845 -2.097  17.117 1.00 24.36  ? 47  LYS B NZ  1 
ATOM   2641 N N   . GLY B 1 32  ? -29.407 2.715   17.716 1.00 24.44  ? 48  GLY B N   1 
ATOM   2642 C CA  . GLY B 1 32  ? -30.394 2.336   16.727 1.00 27.74  ? 48  GLY B CA  1 
ATOM   2643 C C   . GLY B 1 32  ? -30.109 0.949   16.155 1.00 32.30  ? 48  GLY B C   1 
ATOM   2644 O O   . GLY B 1 32  ? -29.187 0.276   16.601 1.00 32.72  ? 48  GLY B O   1 
ATOM   2645 N N   . PRO B 1 33  ? -30.907 0.474   15.175 1.00 35.06  ? 49  PRO B N   1 
ATOM   2646 C CA  . PRO B 1 33  ? -30.756 -0.888  14.658 1.00 35.24  ? 49  PRO B CA  1 
ATOM   2647 C C   . PRO B 1 33  ? -29.518 -1.153  13.797 1.00 35.41  ? 49  PRO B C   1 
ATOM   2648 O O   . PRO B 1 33  ? -29.190 -2.310  13.560 1.00 45.54  ? 49  PRO B O   1 
ATOM   2649 C CB  . PRO B 1 33  ? -32.038 -1.085  13.823 1.00 36.44  ? 49  PRO B CB  1 
ATOM   2650 C CG  . PRO B 1 33  ? -32.441 0.309   13.403 1.00 34.01  ? 49  PRO B CG  1 
ATOM   2651 C CD  . PRO B 1 33  ? -32.044 1.187   14.574 1.00 34.14  ? 49  PRO B CD  1 
ATOM   2652 N N   . ARG B 1 34  ? -28.826 -0.113  13.321 1.00 31.01  ? 50  ARG B N   1 
ATOM   2653 C CA  . ARG B 1 34  ? -27.640 -0.334  12.509 1.00 33.38  ? 50  ARG B CA  1 
ATOM   2654 C C   . ARG B 1 34  ? -26.529 -0.914  13.390 1.00 30.12  ? 50  ARG B C   1 
ATOM   2655 O O   . ARG B 1 34  ? -26.625 -0.883  14.613 1.00 30.32  ? 50  ARG B O   1 
ATOM   2656 C CB  . ARG B 1 34  ? -27.182 0.963   11.839 1.00 37.97  ? 50  ARG B CB  1 
ATOM   2657 C CG  . ARG B 1 34  ? -28.265 1.723   11.078 1.00 42.31  ? 50  ARG B CG  1 
ATOM   2658 C CD  . ARG B 1 34  ? -28.464 1.255   9.651  1.00 48.12  ? 50  ARG B CD  1 
ATOM   2659 N NE  . ARG B 1 34  ? -27.225 1.225   8.874  1.00 49.57  ? 50  ARG B NE  1 
ATOM   2660 C CZ  . ARG B 1 34  ? -26.637 2.271   8.290  1.00 52.25  ? 50  ARG B CZ  1 
ATOM   2661 N NH1 . ARG B 1 34  ? -27.127 3.494   8.403  1.00 50.29  ? 50  ARG B NH1 1 
ATOM   2662 N NH2 . ARG B 1 34  ? -25.533 2.084   7.586  1.00 59.64  ? 50  ARG B NH2 1 
ATOM   2663 N N   . ALA B 1 35  ? -25.446 -1.394  12.770 1.00 28.93  ? 51  ALA B N   1 
ATOM   2664 C CA  . ALA B 1 35  ? -24.321 -1.937  13.523 1.00 30.18  ? 51  ALA B CA  1 
ATOM   2665 C C   . ALA B 1 35  ? -23.681 -0.842  14.375 1.00 30.10  ? 51  ALA B C   1 
ATOM   2666 O O   . ALA B 1 35  ? -23.730 0.340   14.025 1.00 28.79  ? 51  ALA B O   1 
ATOM   2667 C CB  . ALA B 1 35  ? -23.300 -2.547  12.605 1.00 29.97  ? 51  ALA B CB  1 
ATOM   2668 N N   . ALA B 1 36  ? -23.030 -1.256  15.472 1.00 29.55  ? 52  ALA B N   1 
ATOM   2669 C CA  . ALA B 1 36  ? -22.415 -0.313  16.391 1.00 26.86  ? 52  ALA B CA  1 
ATOM   2670 C C   . ALA B 1 36  ? -21.404 0.541   15.629 1.00 27.30  ? 52  ALA B C   1 
ATOM   2671 O O   . ALA B 1 36  ? -21.278 1.724   15.909 1.00 27.40  ? 52  ALA B O   1 
ATOM   2672 C CB  . ALA B 1 36  ? -21.782 -1.039  17.555 1.00 27.87  ? 52  ALA B CB  1 
ATOM   2673 N N   . SER B 1 37  ? -20.725 -0.085  14.663 1.00 29.05  ? 53  SER B N   1 
ATOM   2674 C CA  . SER B 1 37  ? -19.735 0.513   13.776 1.00 31.62  ? 53  SER B CA  1 
ATOM   2675 C C   . SER B 1 37  ? -20.268 1.715   13.007 1.00 26.96  ? 53  SER B C   1 
ATOM   2676 O O   . SER B 1 37  ? -19.493 2.599   12.684 1.00 27.50  ? 53  SER B O   1 
ATOM   2677 C CB  . SER B 1 37  ? -19.228 -0.508  12.765 1.00 36.22  ? 53  SER B CB  1 
ATOM   2678 O OG  . SER B 1 37  ? -18.128 -1.227  13.287 1.00 49.23  ? 53  SER B OG  1 
ATOM   2679 N N   . ILE B 1 38  ? -21.558 1.723   12.664 1.00 28.58  ? 54  ILE B N   1 
ATOM   2680 C CA  . ILE B 1 38  ? -22.122 2.825   11.901 1.00 29.07  ? 54  ILE B CA  1 
ATOM   2681 C C   . ILE B 1 38  ? -22.225 4.092   12.750 1.00 30.46  ? 54  ILE B C   1 
ATOM   2682 O O   . ILE B 1 38  ? -22.053 5.194   12.218 1.00 29.26  ? 54  ILE B O   1 
ATOM   2683 C CB  . ILE B 1 38  ? -23.469 2.441   11.269 1.00 32.62  ? 54  ILE B CB  1 
ATOM   2684 C CG1 . ILE B 1 38  ? -23.309 1.303   10.254 1.00 33.84  ? 54  ILE B CG1 1 
ATOM   2685 C CG2 . ILE B 1 38  ? -24.148 3.666   10.654 1.00 32.44  ? 54  ILE B CG2 1 
ATOM   2686 C CD1 . ILE B 1 38  ? -22.309 1.579   9.146  1.00 35.04  ? 54  ILE B CD1 1 
ATOM   2687 N N   . TYR B 1 39  ? -22.465 3.944   14.063 1.00 29.88  ? 55  TYR B N   1 
ATOM   2688 C CA  . TYR B 1 39  ? -22.658 5.107   14.926 1.00 27.08  ? 55  TYR B CA  1 
ATOM   2689 C C   . TYR B 1 39  ? -21.371 5.542   15.616 1.00 28.50  ? 55  TYR B C   1 
ATOM   2690 O O   . TYR B 1 39  ? -21.231 6.714   15.948 1.00 28.06  ? 55  TYR B O   1 
ATOM   2691 C CB  . TYR B 1 39  ? -23.692 4.801   16.007 1.00 26.03  ? 55  TYR B CB  1 
ATOM   2692 C CG  . TYR B 1 39  ? -25.040 4.390   15.449 1.00 25.95  ? 55  TYR B CG  1 
ATOM   2693 C CD1 . TYR B 1 39  ? -25.839 5.298   14.753 1.00 27.67  ? 55  TYR B CD1 1 
ATOM   2694 C CD2 . TYR B 1 39  ? -25.501 3.094   15.592 1.00 27.98  ? 55  TYR B CD2 1 
ATOM   2695 C CE1 . TYR B 1 39  ? -27.069 4.921   14.233 1.00 26.54  ? 55  TYR B CE1 1 
ATOM   2696 C CE2 . TYR B 1 39  ? -26.727 2.709   15.080 1.00 26.22  ? 55  TYR B CE2 1 
ATOM   2697 C CZ  . TYR B 1 39  ? -27.507 3.621   14.398 1.00 25.79  ? 55  TYR B CZ  1 
ATOM   2698 O OH  . TYR B 1 39  ? -28.713 3.213   13.913 1.00 28.05  ? 55  TYR B OH  1 
ATOM   2699 N N   . THR B 1 40  ? -20.447 4.604   15.857 1.00 28.39  ? 56  THR B N   1 
ATOM   2700 C CA  . THR B 1 40  ? -19.211 4.929   16.548 1.00 26.98  ? 56  THR B CA  1 
ATOM   2701 C C   . THR B 1 40  ? -18.018 4.575   15.654 1.00 28.38  ? 56  THR B C   1 
ATOM   2702 O O   . THR B 1 40  ? -17.900 3.434   15.233 1.00 28.80  ? 56  THR B O   1 
ATOM   2703 C CB  . THR B 1 40  ? -19.161 4.256   17.925 1.00 26.38  ? 56  THR B CB  1 
ATOM   2704 O OG1 . THR B 1 40  ? -20.226 4.737   18.747 1.00 24.77  ? 56  THR B OG1 1 
ATOM   2705 C CG2 . THR B 1 40  ? -17.842 4.491   18.626 1.00 26.01  ? 56  THR B CG2 1 
ATOM   2706 N N   . ARG B 1 41  ? -17.162 5.571   15.381 1.00 28.92  ? 57  ARG B N   1 
ATOM   2707 C CA  . ARG B 1 41  ? -16.036 5.470   14.471 1.00 32.10  ? 57  ARG B CA  1 
ATOM   2708 C C   . ARG B 1 41  ? -14.756 5.632   15.283 1.00 31.70  ? 57  ARG B C   1 
ATOM   2709 O O   . ARG B 1 41  ? -14.645 6.548   16.083 1.00 30.35  ? 57  ARG B O   1 
ATOM   2710 C CB  . ARG B 1 41  ? -16.074 6.559   13.391 1.00 35.55  ? 57  ARG B CB  1 
ATOM   2711 C CG  . ARG B 1 41  ? -17.143 6.422   12.311 1.00 40.04  ? 57  ARG B CG  1 
ATOM   2712 C CD  . ARG B 1 41  ? -16.942 7.451   11.190 1.00 47.40  ? 57  ARG B CD  1 
ATOM   2713 N NE  . ARG B 1 41  ? -15.605 7.389   10.562 1.00 47.92  ? 57  ARG B NE  1 
ATOM   2714 C CZ  . ARG B 1 41  ? -14.709 8.377   10.494 1.00 41.61  ? 57  ARG B CZ  1 
ATOM   2715 N NH1 . ARG B 1 41  ? -15.076 9.639   10.576 1.00 38.85  ? 57  ARG B NH1 1 
ATOM   2716 N NH2 . ARG B 1 41  ? -13.435 8.099   10.267 1.00 48.87  ? 57  ARG B NH2 1 
ATOM   2717 N N   . LEU B 1 42  ? -13.806 4.720   15.086 1.00 29.42  ? 58  LEU B N   1 
ATOM   2718 C CA  . LEU B 1 42  ? -12.491 4.815   15.689 1.00 29.34  ? 58  LEU B CA  1 
ATOM   2719 C C   . LEU B 1 42  ? -11.607 5.676   14.798 1.00 30.19  ? 58  LEU B C   1 
ATOM   2720 O O   . LEU B 1 42  ? -11.520 5.425   13.599 1.00 31.13  ? 58  LEU B O   1 
ATOM   2721 C CB  . LEU B 1 42  ? -11.959 3.389   15.832 1.00 32.32  ? 58  LEU B CB  1 
ATOM   2722 C CG  . LEU B 1 42  ? -12.811 2.511   16.741 1.00 36.40  ? 58  LEU B CG  1 
ATOM   2723 C CD1 . LEU B 1 42  ? -12.738 1.064   16.318 1.00 39.39  ? 58  LEU B CD1 1 
ATOM   2724 C CD2 . LEU B 1 42  ? -12.385 2.668   18.198 1.00 38.06  ? 58  LEU B CD2 1 
ATOM   2725 N N   . LEU B 1 43  ? -10.970 6.711   15.360 1.00 25.92  ? 59  LEU B N   1 
ATOM   2726 C CA  . LEU B 1 43  ? -10.446 7.771   14.514 1.00 28.46  ? 59  LEU B CA  1 
ATOM   2727 C C   . LEU B 1 43  ? -8.991  7.592   14.103 1.00 28.59  ? 59  LEU B C   1 
ATOM   2728 O O   . LEU B 1 43  ? -8.498  8.427   13.359 1.00 32.90  ? 59  LEU B O   1 
ATOM   2729 C CB  . LEU B 1 43  ? -10.644 9.112   15.214 1.00 29.87  ? 59  LEU B CB  1 
ATOM   2730 C CG  . LEU B 1 43  ? -12.107 9.505   15.376 1.00 30.22  ? 59  LEU B CG  1 
ATOM   2731 C CD1 . LEU B 1 43  ? -12.211 10.903  15.932 1.00 30.31  ? 59  LEU B CD1 1 
ATOM   2732 C CD2 . LEU B 1 43  ? -12.841 9.392   14.053 1.00 32.21  ? 59  LEU B CD2 1 
ATOM   2733 N N   . GLY B 1 44  ? -8.316  6.520   14.529 1.00 30.55  ? 60  GLY B N   1 
ATOM   2734 C CA  . GLY B 1 44  ? -6.942  6.295   14.088 1.00 32.68  ? 60  GLY B CA  1 
ATOM   2735 C C   . GLY B 1 44  ? -6.066  7.540   14.264 1.00 35.44  ? 60  GLY B C   1 
ATOM   2736 O O   . GLY B 1 44  ? -6.118  8.185   15.302 1.00 36.10  ? 60  GLY B O   1 
ATOM   2737 N N   . ARG B 1 45  ? -5.299  7.904   13.228 1.00 35.06  ? 61  ARG B N   1 
ATOM   2738 C CA  . ARG B 1 45  ? -4.345  9.001   13.292 1.00 34.60  ? 61  ARG B CA  1 
ATOM   2739 C C   . ARG B 1 45  ? -5.013  10.297  12.837 1.00 31.54  ? 61  ARG B C   1 
ATOM   2740 O O   . ARG B 1 45  ? -4.382  11.352  12.842 1.00 32.22  ? 61  ARG B O   1 
ATOM   2741 C CB  . ARG B 1 45  ? -3.138  8.700   12.390 1.00 45.81  ? 61  ARG B CB  1 
ATOM   2742 C CG  . ARG B 1 45  ? -1.966  7.988   13.055 1.00 58.59  ? 61  ARG B CG  1 
ATOM   2743 C CD  . ARG B 1 45  ? -0.990  7.392   12.040 1.00 67.39  ? 61  ARG B CD  1 
ATOM   2744 N NE  . ARG B 1 45  ? -1.086  5.930   11.986 1.00 78.19  ? 61  ARG B NE  1 
ATOM   2745 C CZ  . ARG B 1 45  ? -1.687  5.202   11.040 1.00 78.63  ? 61  ARG B CZ  1 
ATOM   2746 N NH1 . ARG B 1 45  ? -1.793  3.895   11.196 1.00 77.79  ? 61  ARG B NH1 1 
ATOM   2747 N NH2 . ARG B 1 45  ? -2.213  5.761   9.961  1.00 81.46  ? 61  ARG B NH2 1 
ATOM   2748 N N   . GLU B 1 46  ? -6.283  10.226  12.417 1.00 32.04  ? 62  GLU B N   1 
ATOM   2749 C CA  . GLU B 1 46  ? -6.969  11.401  11.896 1.00 33.80  ? 62  GLU B CA  1 
ATOM   2750 C C   . GLU B 1 46  ? -7.118  12.469  12.979 1.00 32.13  ? 62  GLU B C   1 
ATOM   2751 O O   . GLU B 1 46  ? -7.103  13.649  12.660 1.00 30.33  ? 62  GLU B O   1 
ATOM   2752 C CB  . GLU B 1 46  ? -8.372  11.107  11.377 1.00 38.85  ? 62  GLU B CB  1 
ATOM   2753 C CG  . GLU B 1 46  ? -8.486  9.960   10.400 1.00 46.63  ? 62  GLU B CG  1 
ATOM   2754 C CD  . GLU B 1 46  ? -9.938  9.637   10.077 1.00 48.23  ? 62  GLU B CD  1 
ATOM   2755 O OE1 . GLU B 1 46  ? -10.817 10.502  10.335 1.00 40.75  ? 62  GLU B OE1 1 
ATOM   2756 O OE2 . GLU B 1 46  ? -10.195 8.502   9.635  1.00 57.15  ? 62  GLU B OE2 1 
ATOM   2757 N N   . VAL B 1 47  ? -7.295  12.049  14.245 1.00 31.17  ? 63  VAL B N   1 
ATOM   2758 C CA  . VAL B 1 47  ? -7.453  12.956  15.372 1.00 29.20  ? 63  VAL B CA  1 
ATOM   2759 C C   . VAL B 1 47  ? -6.508  12.534  16.496 1.00 26.75  ? 63  VAL B C   1 
ATOM   2760 O O   . VAL B 1 47  ? -6.530  11.382  16.928 1.00 27.55  ? 63  VAL B O   1 
ATOM   2761 C CB  . VAL B 1 47  ? -8.922  12.963  15.846 1.00 32.06  ? 63  VAL B CB  1 
ATOM   2762 C CG1 . VAL B 1 47  ? -9.166  13.971  16.950 1.00 32.09  ? 63  VAL B CG1 1 
ATOM   2763 C CG2 . VAL B 1 47  ? -9.881  13.215  14.704 1.00 34.44  ? 63  VAL B CG2 1 
ATOM   2764 N N   . THR B 1 48  ? -5.700  13.486  16.969 1.00 26.08  ? 64  THR B N   1 
ATOM   2765 C CA  . THR B 1 48  ? -4.873  13.311  18.149 1.00 28.65  ? 64  THR B CA  1 
ATOM   2766 C C   . THR B 1 48  ? -5.765  13.317  19.399 1.00 28.16  ? 64  THR B C   1 
ATOM   2767 O O   . THR B 1 48  ? -6.495  14.275  19.643 1.00 24.98  ? 64  THR B O   1 
ATOM   2768 C CB  . THR B 1 48  ? -3.833  14.436  18.281 1.00 28.76  ? 64  THR B CB  1 
ATOM   2769 O OG1 . THR B 1 48  ? -3.104  14.556  17.060 1.00 33.77  ? 64  THR B OG1 1 
ATOM   2770 C CG2 . THR B 1 48  ? -2.854  14.188  19.412 1.00 28.32  ? 64  THR B CG2 1 
ATOM   2771 N N   . PRO B 1 49  ? -5.744  12.261  20.241 1.00 25.77  ? 65  PRO B N   1 
ATOM   2772 C CA  . PRO B 1 49  ? -6.583  12.245  21.447 1.00 23.56  ? 65  PRO B CA  1 
ATOM   2773 C C   . PRO B 1 49  ? -6.002  13.172  22.511 1.00 26.47  ? 65  PRO B C   1 
ATOM   2774 O O   . PRO B 1 49  ? -4.962  13.814  22.274 1.00 25.51  ? 65  PRO B O   1 
ATOM   2775 C CB  . PRO B 1 49  ? -6.534  10.776  21.857 1.00 24.84  ? 65  PRO B CB  1 
ATOM   2776 C CG  . PRO B 1 49  ? -5.140  10.355  21.406 1.00 24.26  ? 65  PRO B CG  1 
ATOM   2777 C CD  . PRO B 1 49  ? -4.982  11.016  20.059 1.00 22.77  ? 65  PRO B CD  1 
ATOM   2778 N N   . THR B 1 50  ? -6.674  13.252  23.671 1.00 23.03  ? 66  THR B N   1 
ATOM   2779 C CA  . THR B 1 50  ? -6.189  14.116  24.734 1.00 23.48  ? 66  THR B CA  1 
ATOM   2780 C C   . THR B 1 50  ? -4.753  13.729  25.058 1.00 23.56  ? 66  THR B C   1 
ATOM   2781 O O   . THR B 1 50  ? -4.413  12.552  25.084 1.00 24.55  ? 66  THR B O   1 
ATOM   2782 C CB  . THR B 1 50  ? -7.070  14.086  25.984 1.00 23.69  ? 66  THR B CB  1 
ATOM   2783 O OG1 . THR B 1 50  ? -6.488  15.031  26.877 1.00 24.46  ? 66  THR B OG1 1 
ATOM   2784 C CG2 . THR B 1 50  ? -7.166  12.732  26.643 1.00 24.53  ? 66  THR B CG2 1 
ATOM   2785 N N   . PRO B 1 51  ? -3.847  14.704  25.233 1.00 22.35  ? 67  PRO B N   1 
ATOM   2786 C CA  . PRO B 1 51  ? -2.449  14.376  25.491 1.00 24.00  ? 67  PRO B CA  1 
ATOM   2787 C C   . PRO B 1 51  ? -2.208  13.866  26.915 1.00 25.15  ? 67  PRO B C   1 
ATOM   2788 O O   . PRO B 1 51  ? -1.114  13.355  27.198 1.00 24.90  ? 67  PRO B O   1 
ATOM   2789 C CB  . PRO B 1 51  ? -1.693  15.680  25.183 1.00 25.65  ? 67  PRO B CB  1 
ATOM   2790 C CG  . PRO B 1 51  ? -2.718  16.766  25.121 1.00 24.14  ? 67  PRO B CG  1 
ATOM   2791 C CD  . PRO B 1 51  ? -4.093  16.141  25.097 1.00 21.86  ? 67  PRO B CD  1 
ATOM   2792 N N   . LEU B 1 52  ? -3.240  13.917  27.780 1.00 22.41  ? 68  LEU B N   1 
ATOM   2793 C CA  . LEU B 1 52  ? -3.034  13.626  29.192 1.00 24.97  ? 68  LEU B CA  1 
ATOM   2794 C C   . LEU B 1 52  ? -2.385  12.254  29.390 1.00 25.87  ? 68  LEU B C   1 
ATOM   2795 O O   . LEU B 1 52  ? -1.575  12.120  30.297 1.00 23.62  ? 68  LEU B O   1 
ATOM   2796 C CB  . LEU B 1 52  ? -4.351  13.742  29.972 1.00 24.40  ? 68  LEU B CB  1 
ATOM   2797 C CG  . LEU B 1 52  ? -4.848  15.170  30.240 1.00 23.79  ? 68  LEU B CG  1 
ATOM   2798 C CD1 . LEU B 1 52  ? -5.975  15.200  31.268 1.00 26.82  ? 68  LEU B CD1 1 
ATOM   2799 C CD2 . LEU B 1 52  ? -3.728  16.071  30.706 1.00 24.85  ? 68  LEU B CD2 1 
ATOM   2800 N N   . TRP B 1 53  ? -2.696  11.262  28.536 1.00 26.40  ? 69  TRP B N   1 
ATOM   2801 C CA  . TRP B 1 53  ? -2.275  9.882   28.771 1.00 25.83  ? 69  TRP B CA  1 
ATOM   2802 C C   . TRP B 1 53  ? -1.234  9.413   27.748 1.00 27.25  ? 69  TRP B C   1 
ATOM   2803 O O   . TRP B 1 53  ? -1.044  8.215   27.537 1.00 28.07  ? 69  TRP B O   1 
ATOM   2804 C CB  . TRP B 1 53  ? -3.521  8.978   28.810 1.00 26.18  ? 69  TRP B CB  1 
ATOM   2805 C CG  . TRP B 1 53  ? -4.659  9.641   29.539 1.00 24.17  ? 69  TRP B CG  1 
ATOM   2806 C CD1 . TRP B 1 53  ? -5.842  10.054  29.008 1.00 23.21  ? 69  TRP B CD1 1 
ATOM   2807 C CD2 . TRP B 1 53  ? -4.671  10.063  30.920 1.00 21.86  ? 69  TRP B CD2 1 
ATOM   2808 N NE1 . TRP B 1 53  ? -6.600  10.671  29.966 1.00 22.18  ? 69  TRP B NE1 1 
ATOM   2809 C CE2 . TRP B 1 53  ? -5.909  10.698  31.144 1.00 23.08  ? 69  TRP B CE2 1 
ATOM   2810 C CE3 . TRP B 1 53  ? -3.763  9.973   31.984 1.00 24.90  ? 69  TRP B CE3 1 
ATOM   2811 C CZ2 . TRP B 1 53  ? -6.256  11.246  32.382 1.00 22.72  ? 69  TRP B CZ2 1 
ATOM   2812 C CZ3 . TRP B 1 53  ? -4.117  10.488  33.212 1.00 23.53  ? 69  TRP B CZ3 1 
ATOM   2813 C CH2 . TRP B 1 53  ? -5.347  11.112  33.408 1.00 22.35  ? 69  TRP B CH2 1 
ATOM   2814 N N   . ASN B 1 54  ? -0.560  10.362  27.099 1.00 28.41  ? 70  ASN B N   1 
ATOM   2815 C CA  . ASN B 1 54  ? 0.535   10.056  26.191 1.00 29.27  ? 70  ASN B CA  1 
ATOM   2816 C C   . ASN B 1 54  ? 1.658   9.341   26.935 1.00 28.39  ? 70  ASN B C   1 
ATOM   2817 O O   . ASN B 1 54  ? 1.781   9.464   28.159 1.00 23.78  ? 70  ASN B O   1 
ATOM   2818 C CB  . ASN B 1 54  ? 1.209   11.313  25.627 1.00 29.25  ? 70  ASN B CB  1 
ATOM   2819 C CG  . ASN B 1 54  ? 0.423   11.994  24.533 1.00 30.22  ? 70  ASN B CG  1 
ATOM   2820 O OD1 . ASN B 1 54  ? -0.532  11.436  23.988 1.00 34.06  ? 70  ASN B OD1 1 
ATOM   2821 N ND2 . ASN B 1 54  ? 0.813   13.218  24.232 1.00 29.06  ? 70  ASN B ND2 1 
ATOM   2822 N N   . ASP B 1 55  ? 2.486   8.645   26.140 1.00 28.06  ? 71  ASP B N   1 
ATOM   2823 C CA  . ASP B 1 55  ? 3.809   8.201   26.561 1.00 31.29  ? 71  ASP B CA  1 
ATOM   2824 C C   . ASP B 1 55  ? 4.866   9.123   25.939 1.00 31.24  ? 71  ASP B C   1 
ATOM   2825 O O   . ASP B 1 55  ? 4.729   9.554   24.805 1.00 38.40  ? 71  ASP B O   1 
ATOM   2826 C CB  . ASP B 1 55  ? 4.035   6.735   26.153 1.00 31.30  ? 71  ASP B CB  1 
ATOM   2827 C CG  . ASP B 1 55  ? 3.315   5.702   27.005 1.00 32.60  ? 71  ASP B CG  1 
ATOM   2828 O OD1 . ASP B 1 55  ? 2.900   6.056   28.113 1.00 33.65  ? 71  ASP B OD1 1 
ATOM   2829 O OD2 . ASP B 1 55  ? 3.219   4.542   26.572 1.00 30.87  ? 71  ASP B OD2 1 
ATOM   2830 N N   . ARG B 1 56  ? 5.951   9.380   26.666 1.00 33.91  ? 72  ARG B N   1 
ATOM   2831 C CA  . ARG B 1 56  ? 6.972   10.325  26.232 1.00 36.03  ? 72  ARG B CA  1 
ATOM   2832 C C   . ARG B 1 56  ? 8.196   9.561   25.732 1.00 34.16  ? 72  ARG B C   1 
ATOM   2833 O O   . ARG B 1 56  ? 8.528   8.514   26.280 1.00 28.17  ? 72  ARG B O   1 
ATOM   2834 C CB  . ARG B 1 56  ? 7.356   11.225  27.408 1.00 38.37  ? 72  ARG B CB  1 
ATOM   2835 C CG  . ARG B 1 56  ? 6.186   11.859  28.149 1.00 43.61  ? 72  ARG B CG  1 
ATOM   2836 C CD  . ARG B 1 56  ? 6.655   12.817  29.230 1.00 48.20  ? 72  ARG B CD  1 
ATOM   2837 N NE  . ARG B 1 56  ? 7.522   13.849  28.662 1.00 54.76  ? 72  ARG B NE  1 
ATOM   2838 C CZ  . ARG B 1 56  ? 8.348   14.629  29.356 1.00 57.67  ? 72  ARG B CZ  1 
ATOM   2839 N NH1 . ARG B 1 56  ? 8.331   14.602  30.680 1.00 57.87  ? 72  ARG B NH1 1 
ATOM   2840 N NH2 . ARG B 1 56  ? 9.183   15.440  28.718 1.00 50.58  ? 72  ARG B NH2 1 
ATOM   2841 N N   . LEU B 1 57  ? 8.861   10.095  24.697 1.00 31.10  ? 73  LEU B N   1 
ATOM   2842 C CA  . LEU B 1 57  ? 10.010  9.448   24.097 1.00 33.33  ? 73  LEU B CA  1 
ATOM   2843 C C   . LEU B 1 57  ? 11.304  10.117  24.556 1.00 34.03  ? 73  LEU B C   1 
ATOM   2844 O O   . LEU B 1 57  ? 11.333  11.286  24.921 1.00 30.19  ? 73  LEU B O   1 
ATOM   2845 C CB  . LEU B 1 57  ? 9.871   9.469   22.575 1.00 34.45  ? 73  LEU B CB  1 
ATOM   2846 C CG  . LEU B 1 57  ? 8.835   8.494   22.028 1.00 39.93  ? 73  LEU B CG  1 
ATOM   2847 C CD1 . LEU B 1 57  ? 8.163   9.049   20.783 1.00 45.15  ? 73  LEU B CD1 1 
ATOM   2848 C CD2 . LEU B 1 57  ? 9.482   7.151   21.724 1.00 40.49  ? 73  LEU B CD2 1 
ATOM   2849 N N   . PHE B 1 58  ? 12.347  9.304   24.617 1.00 35.67  ? 74  PHE B N   1 
ATOM   2850 C CA  . PHE B 1 58  ? 13.715  9.758   24.751 1.00 48.89  ? 74  PHE B CA  1 
ATOM   2851 C C   . PHE B 1 58  ? 14.431  9.351   23.466 1.00 55.12  ? 74  PHE B C   1 
ATOM   2852 O O   . PHE B 1 58  ? 14.425  8.170   23.131 1.00 47.39  ? 74  PHE B O   1 
ATOM   2853 C CB  . PHE B 1 58  ? 14.367  9.150   25.992 1.00 52.90  ? 74  PHE B CB  1 
ATOM   2854 C CG  . PHE B 1 58  ? 15.735  9.691   26.323 1.00 65.68  ? 74  PHE B CG  1 
ATOM   2855 C CD1 . PHE B 1 58  ? 16.694  9.912   25.340 1.00 67.59  ? 74  PHE B CD1 1 
ATOM   2856 C CD2 . PHE B 1 58  ? 16.071  9.954   27.643 1.00 74.92  ? 74  PHE B CD2 1 
ATOM   2857 C CE1 . PHE B 1 58  ? 17.942  10.418  25.666 1.00 73.34  ? 74  PHE B CE1 1 
ATOM   2858 C CE2 . PHE B 1 58  ? 17.327  10.435  27.972 1.00 76.67  ? 74  PHE B CE2 1 
ATOM   2859 C CZ  . PHE B 1 58  ? 18.260  10.668  26.983 1.00 81.24  ? 74  PHE B CZ  1 
ATOM   2860 N N   . PRO B 1 59  ? 15.014  10.291  22.680 1.00 73.25  ? 75  PRO B N   1 
ATOM   2861 C CA  . PRO B 1 59  ? 15.086  11.709  23.038 1.00 78.41  ? 75  PRO B CA  1 
ATOM   2862 C C   . PRO B 1 59  ? 13.760  12.413  22.756 1.00 78.03  ? 75  PRO B C   1 
ATOM   2863 O O   . PRO B 1 59  ? 12.911  11.867  22.049 1.00 67.42  ? 75  PRO B O   1 
ATOM   2864 C CB  . PRO B 1 59  ? 16.211  12.283  22.154 1.00 80.61  ? 75  PRO B CB  1 
ATOM   2865 C CG  . PRO B 1 59  ? 16.551  11.192  21.134 1.00 82.18  ? 75  PRO B CG  1 
ATOM   2866 C CD  . PRO B 1 59  ? 15.586  10.042  21.350 1.00 79.23  ? 75  PRO B CD  1 
ATOM   2867 N N   . GLU B 1 60  ? 13.615  13.626  23.313 1.00 86.75  ? 76  GLU B N   1 
ATOM   2868 C CA  . GLU B 1 60  ? 12.410  14.436  23.185 1.00 94.06  ? 76  GLU B CA  1 
ATOM   2869 C C   . GLU B 1 60  ? 12.424  15.198  21.856 1.00 95.55  ? 76  GLU B C   1 
ATOM   2870 O O   . GLU B 1 60  ? 11.494  15.954  21.572 1.00 88.00  ? 76  GLU B O   1 
ATOM   2871 C CB  . GLU B 1 60  ? 12.300  15.367  24.395 1.00 93.25  ? 76  GLU B CB  1 
ATOM   2872 C CG  . GLU B 1 60  ? 12.068  14.621  25.703 1.00 94.11  ? 76  GLU B CG  1 
ATOM   2873 C CD  . GLU B 1 60  ? 12.421  15.377  26.977 1.00 95.16  ? 76  GLU B CD  1 
ATOM   2874 O OE1 . GLU B 1 60  ? 11.953  14.971  28.060 1.00 90.49  ? 76  GLU B OE1 1 
ATOM   2875 O OE2 . GLU B 1 60  ? 13.184  16.357  26.895 1.00 100.56 ? 76  GLU B OE2 1 
ATOM   2876 N N   . VAL B 1 61  ? 13.498  14.998  21.071 1.00 99.48  ? 77  VAL B N   1 
ATOM   2877 C CA  . VAL B 1 61  ? 13.585  15.311  19.648 1.00 103.74 ? 77  VAL B CA  1 
ATOM   2878 C C   . VAL B 1 61  ? 13.781  13.989  18.897 1.00 108.42 ? 77  VAL B C   1 
ATOM   2879 O O   . VAL B 1 61  ? 14.487  13.109  19.390 1.00 110.53 ? 77  VAL B O   1 
ATOM   2880 C CB  . VAL B 1 61  ? 14.732  16.309  19.352 1.00 101.16 ? 77  VAL B CB  1 
ATOM   2881 C CG1 . VAL B 1 61  ? 16.116  15.686  19.517 1.00 95.97  ? 77  VAL B CG1 1 
ATOM   2882 C CG2 . VAL B 1 61  ? 14.610  16.942  17.972 1.00 94.96  ? 77  VAL B CG2 1 
ATOM   2883 N N   . PRO B 1 62  ? 13.197  13.765  17.691 1.00 107.84 ? 78  PRO B N   1 
ATOM   2884 C CA  . PRO B 1 62  ? 12.158  14.626  17.102 1.00 106.43 ? 78  PRO B CA  1 
ATOM   2885 C C   . PRO B 1 62  ? 10.750  14.646  17.726 1.00 99.53  ? 78  PRO B C   1 
ATOM   2886 O O   . PRO B 1 62  ? 10.219  15.729  17.979 1.00 87.25  ? 78  PRO B O   1 
ATOM   2887 C CB  . PRO B 1 62  ? 12.073  14.143  15.638 1.00 106.60 ? 78  PRO B CB  1 
ATOM   2888 C CG  . PRO B 1 62  ? 12.663  12.745  15.625 1.00 104.77 ? 78  PRO B CG  1 
ATOM   2889 C CD  . PRO B 1 62  ? 13.648  12.708  16.772 1.00 104.58 ? 78  PRO B CD  1 
ATOM   2890 N N   . TYR B 1 63  ? 10.128  13.475  17.956 1.00 93.00  ? 79  TYR B N   1 
ATOM   2891 C CA  . TYR B 1 63  ? 8.738   13.411  18.410 1.00 85.23  ? 79  TYR B CA  1 
ATOM   2892 C C   . TYR B 1 63  ? 8.712   13.330  19.937 1.00 67.70  ? 79  TYR B C   1 
ATOM   2893 O O   . TYR B 1 63  ? 9.171   12.347  20.503 1.00 50.24  ? 79  TYR B O   1 
ATOM   2894 C CB  . TYR B 1 63  ? 7.945   12.209  17.874 1.00 92.23  ? 79  TYR B CB  1 
ATOM   2895 C CG  . TYR B 1 63  ? 8.489   11.615  16.584 1.00 105.10 ? 79  TYR B CG  1 
ATOM   2896 C CD1 . TYR B 1 63  ? 8.491   12.351  15.403 1.00 115.80 ? 79  TYR B CD1 1 
ATOM   2897 C CD2 . TYR B 1 63  ? 9.034   10.334  16.558 1.00 100.64 ? 79  TYR B CD2 1 
ATOM   2898 C CE1 . TYR B 1 63  ? 9.005   11.826  14.230 1.00 115.44 ? 79  TYR B CE1 1 
ATOM   2899 C CE2 . TYR B 1 63  ? 9.550   9.798   15.392 1.00 104.58 ? 79  TYR B CE2 1 
ATOM   2900 C CZ  . TYR B 1 63  ? 9.535   10.548  14.227 1.00 111.37 ? 79  TYR B CZ  1 
ATOM   2901 O OH  . TYR B 1 63  ? 10.036  10.058  13.062 1.00 108.95 ? 79  TYR B OH  1 
ATOM   2902 N N   . PRO B 1 64  ? 8.177   14.334  20.673 1.00 68.22  ? 80  PRO B N   1 
ATOM   2903 C CA  . PRO B 1 64  ? 8.111   14.226  22.131 1.00 59.17  ? 80  PRO B CA  1 
ATOM   2904 C C   . PRO B 1 64  ? 7.323   13.011  22.642 1.00 58.11  ? 80  PRO B C   1 
ATOM   2905 O O   . PRO B 1 64  ? 7.714   12.434  23.655 1.00 46.00  ? 80  PRO B O   1 
ATOM   2906 C CB  . PRO B 1 64  ? 7.470   15.553  22.585 1.00 62.81  ? 80  PRO B CB  1 
ATOM   2907 C CG  . PRO B 1 64  ? 6.841   16.160  21.333 1.00 64.46  ? 80  PRO B CG  1 
ATOM   2908 C CD  . PRO B 1 64  ? 7.640   15.613  20.168 1.00 66.77  ? 80  PRO B CD  1 
ATOM   2909 N N   . ALA B 1 65  ? 6.241   12.601  21.944 1.00 51.21  ? 81  ALA B N   1 
ATOM   2910 C CA  . ALA B 1 65  ? 5.244   11.730  22.559 1.00 47.11  ? 81  ALA B CA  1 
ATOM   2911 C C   . ALA B 1 65  ? 4.643   10.716  21.585 1.00 42.41  ? 81  ALA B C   1 
ATOM   2912 O O   . ALA B 1 65  ? 4.621   10.922  20.372 1.00 38.17  ? 81  ALA B O   1 
ATOM   2913 C CB  . ALA B 1 65  ? 4.155   12.572  23.185 1.00 45.71  ? 81  ALA B CB  1 
ATOM   2914 N N   . VAL B 1 66  ? 4.148   9.611   22.162 1.00 37.54  ? 82  VAL B N   1 
ATOM   2915 C CA  . VAL B 1 66  ? 3.346   8.637   21.444 1.00 38.40  ? 82  VAL B CA  1 
ATOM   2916 C C   . VAL B 1 66  ? 1.956   8.569   22.089 1.00 36.67  ? 82  VAL B C   1 
ATOM   2917 O O   . VAL B 1 66  ? 1.820   8.612   23.315 1.00 29.59  ? 82  VAL B O   1 
ATOM   2918 C CB  . VAL B 1 66  ? 4.035   7.255   21.396 1.00 42.51  ? 82  VAL B CB  1 
ATOM   2919 C CG1 . VAL B 1 66  ? 4.257   6.664   22.768 1.00 43.75  ? 82  VAL B CG1 1 
ATOM   2920 C CG2 . VAL B 1 66  ? 3.267   6.255   20.549 1.00 44.66  ? 82  VAL B CG2 1 
ATOM   2921 N N   . SER B 1 67  ? 0.935   8.525   21.220 1.00 36.54  ? 83  SER B N   1 
ATOM   2922 C CA  . SER B 1 67  ? -0.451  8.319   21.607 1.00 35.45  ? 83  SER B CA  1 
ATOM   2923 C C   . SER B 1 67  ? -0.650  6.881   22.078 1.00 33.36  ? 83  SER B C   1 
ATOM   2924 O O   . SER B 1 67  ? -0.115  5.952   21.478 1.00 38.54  ? 83  SER B O   1 
ATOM   2925 C CB  . SER B 1 67  ? -1.353  8.645   20.453 1.00 37.39  ? 83  SER B CB  1 
ATOM   2926 O OG  . SER B 1 67  ? -1.325  10.045  20.173 1.00 45.20  ? 83  SER B OG  1 
ATOM   2927 N N   . THR B 1 68  ? -1.410  6.703   23.166 1.00 30.31  ? 84  THR B N   1 
ATOM   2928 C CA  . THR B 1 68  ? -1.642  5.390   23.743 1.00 30.78  ? 84  THR B CA  1 
ATOM   2929 C C   . THR B 1 68  ? -3.079  4.943   23.516 1.00 29.38  ? 84  THR B C   1 
ATOM   2930 O O   . THR B 1 68  ? -3.513  3.931   24.071 1.00 30.68  ? 84  THR B O   1 
ATOM   2931 C CB  . THR B 1 68  ? -1.305  5.373   25.235 1.00 30.68  ? 84  THR B CB  1 
ATOM   2932 O OG1 . THR B 1 68  ? -2.062  6.396   25.880 1.00 29.17  ? 84  THR B OG1 1 
ATOM   2933 C CG2 . THR B 1 68  ? 0.170   5.591   25.497 1.00 29.86  ? 84  THR B CG2 1 
ATOM   2934 N N   . GLU B 1 69  ? -3.795  5.685   22.669 1.00 28.09  ? 85  GLU B N   1 
ATOM   2935 C CA  . GLU B 1 69  ? -5.204  5.429   22.435 1.00 29.81  ? 85  GLU B CA  1 
ATOM   2936 C C   . GLU B 1 69  ? -5.608  6.101   21.136 1.00 27.62  ? 85  GLU B C   1 
ATOM   2937 O O   . GLU B 1 69  ? -4.913  7.003   20.665 1.00 26.23  ? 85  GLU B O   1 
ATOM   2938 C CB  . GLU B 1 69  ? -6.054  5.931   23.615 1.00 29.34  ? 85  GLU B CB  1 
ATOM   2939 C CG  . GLU B 1 69  ? -6.001  7.437   23.824 1.00 26.87  ? 85  GLU B CG  1 
ATOM   2940 C CD  . GLU B 1 69  ? -6.908  7.940   24.934 1.00 27.72  ? 85  GLU B CD  1 
ATOM   2941 O OE1 . GLU B 1 69  ? -8.132  7.691   24.841 1.00 26.31  ? 85  GLU B OE1 1 
ATOM   2942 O OE2 . GLU B 1 69  ? -6.392  8.602   25.888 1.00 31.33  ? 85  GLU B OE2 1 
ATOM   2943 N N   . GLN B 1 70  ? -6.715  5.601   20.584 1.00 28.26  ? 86  GLN B N   1 
ATOM   2944 C CA  . GLN B 1 70  ? -7.461  6.230   19.507 1.00 30.50  ? 86  GLN B CA  1 
ATOM   2945 C C   . GLN B 1 70  ? -8.634  7.012   20.083 1.00 27.65  ? 86  GLN B C   1 
ATOM   2946 O O   . GLN B 1 70  ? -9.314  6.496   20.973 1.00 26.59  ? 86  GLN B O   1 
ATOM   2947 C CB  . GLN B 1 70  ? -8.175  5.187   18.635 1.00 34.34  ? 86  GLN B CB  1 
ATOM   2948 C CG  . GLN B 1 70  ? -7.291  4.195   17.921 1.00 40.21  ? 86  GLN B CG  1 
ATOM   2949 C CD  . GLN B 1 70  ? -8.087  3.464   16.868 1.00 35.19  ? 86  GLN B CD  1 
ATOM   2950 O OE1 . GLN B 1 70  ? -8.581  4.057   15.916 1.00 30.79  ? 86  GLN B OE1 1 
ATOM   2951 N NE2 . GLN B 1 70  ? -8.228  2.165   17.044 1.00 34.05  ? 86  GLN B NE2 1 
ATOM   2952 N N   . ALA B 1 71  ? -8.954  8.177   19.500 1.00 25.99  ? 87  ALA B N   1 
ATOM   2953 C CA  . ALA B 1 71  ? -10.208 8.850   19.819 1.00 25.24  ? 87  ALA B CA  1 
ATOM   2954 C C   . ALA B 1 71  ? -11.377 8.102   19.167 1.00 25.54  ? 87  ALA B C   1 
ATOM   2955 O O   . ALA B 1 71  ? -11.211 7.436   18.141 1.00 24.80  ? 87  ALA B O   1 
ATOM   2956 C CB  . ALA B 1 71  ? -10.185 10.305  19.391 1.00 26.09  ? 87  ALA B CB  1 
ATOM   2957 N N   . LEU B 1 72  ? -12.569 8.265   19.756 1.00 24.22  ? 88  LEU B N   1 
ATOM   2958 C CA  . LEU B 1 72  ? -13.818 7.726   19.239 1.00 26.38  ? 88  LEU B CA  1 
ATOM   2959 C C   . LEU B 1 72  ? -14.721 8.876   18.824 1.00 23.71  ? 88  LEU B C   1 
ATOM   2960 O O   . LEU B 1 72  ? -14.790 9.857   19.545 1.00 24.49  ? 88  LEU B O   1 
ATOM   2961 C CB  . LEU B 1 72  ? -14.500 6.946   20.358 1.00 27.25  ? 88  LEU B CB  1 
ATOM   2962 C CG  . LEU B 1 72  ? -13.745 5.718   20.830 1.00 29.82  ? 88  LEU B CG  1 
ATOM   2963 C CD1 . LEU B 1 72  ? -13.759 5.645   22.344 1.00 34.83  ? 88  LEU B CD1 1 
ATOM   2964 C CD2 . LEU B 1 72  ? -14.364 4.469   20.248 1.00 33.70  ? 88  LEU B CD2 1 
ATOM   2965 N N   . LEU B 1 73  ? -15.375 8.732   17.668 1.00 23.79  ? 89  LEU B N   1 
ATOM   2966 C CA  . LEU B 1 73  ? -16.404 9.644   17.205 1.00 23.54  ? 89  LEU B CA  1 
ATOM   2967 C C   . LEU B 1 73  ? -17.732 8.909   17.344 1.00 24.81  ? 89  LEU B C   1 
ATOM   2968 O O   . LEU B 1 73  ? -17.938 7.818   16.773 1.00 24.42  ? 89  LEU B O   1 
ATOM   2969 C CB  . LEU B 1 73  ? -16.131 10.082  15.764 1.00 25.39  ? 89  LEU B CB  1 
ATOM   2970 C CG  . LEU B 1 73  ? -17.261 10.836  15.074 1.00 26.32  ? 89  LEU B CG  1 
ATOM   2971 C CD1 . LEU B 1 73  ? -17.392 12.233  15.657 1.00 26.84  ? 89  LEU B CD1 1 
ATOM   2972 C CD2 . LEU B 1 73  ? -17.035 10.900  13.566 1.00 28.81  ? 89  LEU B CD2 1 
ATOM   2973 N N   . VAL B 1 74  ? -18.571 9.482   18.212 1.00 22.08  ? 90  VAL B N   1 
ATOM   2974 C CA  . VAL B 1 74  ? -19.905 8.967   18.444 1.00 21.46  ? 90  VAL B CA  1 
ATOM   2975 C C   . VAL B 1 74  ? -20.895 9.845   17.691 1.00 23.11  ? 90  VAL B C   1 
ATOM   2976 O O   . VAL B 1 74  ? -20.923 11.049  17.913 1.00 22.89  ? 90  VAL B O   1 
ATOM   2977 C CB  . VAL B 1 74  ? -20.227 8.907   19.943 1.00 20.43  ? 90  VAL B CB  1 
ATOM   2978 C CG1 . VAL B 1 74  ? -21.666 8.503   20.205 1.00 19.32  ? 90  VAL B CG1 1 
ATOM   2979 C CG2 . VAL B 1 74  ? -19.259 7.973   20.668 1.00 21.30  ? 90  VAL B CG2 1 
ATOM   2980 N N   . LEU B 1 75  ? -21.726 9.198   16.859 1.00 24.11  ? 91  LEU B N   1 
ATOM   2981 C CA  . LEU B 1 75  ? -22.708 9.874   16.021 1.00 24.93  ? 91  LEU B CA  1 
ATOM   2982 C C   . LEU B 1 75  ? -24.118 9.441   16.396 1.00 23.62  ? 91  LEU B C   1 
ATOM   2983 O O   . LEU B 1 75  ? -24.350 8.274   16.687 1.00 26.10  ? 91  LEU B O   1 
ATOM   2984 C CB  . LEU B 1 75  ? -22.470 9.504   14.556 1.00 23.36  ? 91  LEU B CB  1 
ATOM   2985 C CG  . LEU B 1 75  ? -21.135 9.953   13.970 1.00 24.91  ? 91  LEU B CG  1 
ATOM   2986 C CD1 . LEU B 1 75  ? -20.884 9.287   12.620 1.00 27.48  ? 91  LEU B CD1 1 
ATOM   2987 C CD2 . LEU B 1 75  ? -21.079 11.459  13.828 1.00 24.65  ? 91  LEU B CD2 1 
ATOM   2988 N N   . ILE B 1 76  ? -25.058 10.377  16.266 1.00 23.38  ? 92  ILE B N   1 
ATOM   2989 C CA  . ILE B 1 76  ? -26.479 10.074  16.227 1.00 23.74  ? 92  ILE B CA  1 
ATOM   2990 C C   . ILE B 1 76  ? -27.029 10.623  14.911 1.00 25.13  ? 92  ILE B C   1 
ATOM   2991 O O   . ILE B 1 76  ? -26.526 11.626  14.406 1.00 26.27  ? 92  ILE B O   1 
ATOM   2992 C CB  . ILE B 1 76  ? -27.231 10.662  17.436 1.00 23.28  ? 92  ILE B CB  1 
ATOM   2993 C CG1 . ILE B 1 76  ? -26.937 12.153  17.614 1.00 22.85  ? 92  ILE B CG1 1 
ATOM   2994 C CG2 . ILE B 1 76  ? -26.918 9.880   18.703 1.00 25.90  ? 92  ILE B CG2 1 
ATOM   2995 C CD1 . ILE B 1 76  ? -27.968 12.887  18.419 1.00 22.36  ? 92  ILE B CD1 1 
ATOM   2996 N N   . GLY B 1 77  ? -28.003 9.912   14.335 1.00 25.30  ? 93  GLY B N   1 
ATOM   2997 C CA  . GLY B 1 77  ? -28.755 10.368  13.174 1.00 26.18  ? 93  GLY B CA  1 
ATOM   2998 C C   . GLY B 1 77  ? -30.204 9.896   13.272 1.00 30.42  ? 93  GLY B C   1 
ATOM   2999 O O   . GLY B 1 77  ? -30.659 9.529   14.361 1.00 26.58  ? 93  GLY B O   1 
ATOM   3000 N N   . ASN B 1 78  ? -30.909 9.856   12.131 1.00 32.08  ? 94  ASN B N   1 
ATOM   3001 C CA  . ASN B 1 78  ? -32.357 9.697   12.175 1.00 34.93  ? 94  ASN B CA  1 
ATOM   3002 C C   . ASN B 1 78  ? -32.734 8.270   12.566 1.00 29.56  ? 94  ASN B C   1 
ATOM   3003 O O   . ASN B 1 78  ? -33.815 8.044   13.095 1.00 27.78  ? 94  ASN B O   1 
ATOM   3004 C CB  . ASN B 1 78  ? -33.078 10.114  10.888 1.00 37.93  ? 94  ASN B CB  1 
ATOM   3005 C CG  . ASN B 1 78  ? -34.567 10.283  11.157 1.00 47.33  ? 94  ASN B CG  1 
ATOM   3006 O OD1 . ASN B 1 78  ? -34.975 11.008  12.082 1.00 46.46  ? 94  ASN B OD1 1 
ATOM   3007 N ND2 . ASN B 1 78  ? -35.388 9.566   10.404 1.00 46.55  ? 94  ASN B ND2 1 
ATOM   3008 N N   . SER B 1 79  ? -31.812 7.328   12.365 1.00 28.34  ? 95  SER B N   1 
ATOM   3009 C CA  . SER B 1 79  ? -32.034 5.954   12.780 1.00 29.16  ? 95  SER B CA  1 
ATOM   3010 C C   . SER B 1 79  ? -31.709 5.704   14.259 1.00 26.20  ? 95  SER B C   1 
ATOM   3011 O O   . SER B 1 79  ? -31.876 4.565   14.691 1.00 27.60  ? 95  SER B O   1 
ATOM   3012 C CB  . SER B 1 79  ? -31.256 5.004   11.897 1.00 29.36  ? 95  SER B CB  1 
ATOM   3013 O OG  . SER B 1 79  ? -29.855 5.065   12.119 1.00 29.75  ? 95  SER B OG  1 
ATOM   3014 N N   . SER B 1 80  ? -31.278 6.728   15.032 1.00 25.20  ? 96  SER B N   1 
ATOM   3015 C CA  . SER B 1 80  ? -30.721 6.508   16.369 1.00 24.94  ? 96  SER B CA  1 
ATOM   3016 C C   . SER B 1 80  ? -31.826 6.391   17.413 1.00 26.14  ? 96  SER B C   1 
ATOM   3017 O O   . SER B 1 80  ? -31.792 7.040   18.453 1.00 24.35  ? 96  SER B O   1 
ATOM   3018 C CB  . SER B 1 80  ? -29.678 7.558   16.735 1.00 25.21  ? 96  SER B CB  1 
ATOM   3019 O OG  . SER B 1 80  ? -28.495 7.397   15.929 1.00 25.56  ? 96  SER B OG  1 
ATOM   3020 N N   . VAL B 1 81  ? -32.776 5.487   17.137 1.00 27.26  ? 97  VAL B N   1 
ATOM   3021 C CA  . VAL B 1 81  ? -33.917 5.217   17.985 1.00 27.34  ? 97  VAL B CA  1 
ATOM   3022 C C   . VAL B 1 81  ? -33.648 3.907   18.707 1.00 26.97  ? 97  VAL B C   1 
ATOM   3023 O O   . VAL B 1 81  ? -33.514 2.860   18.075 1.00 28.47  ? 97  VAL B O   1 
ATOM   3024 C CB  . VAL B 1 81  ? -35.196 5.102   17.138 1.00 28.12  ? 97  VAL B CB  1 
ATOM   3025 C CG1 . VAL B 1 81  ? -36.423 4.840   17.998 1.00 27.05  ? 97  VAL B CG1 1 
ATOM   3026 C CG2 . VAL B 1 81  ? -35.373 6.332   16.264 1.00 28.17  ? 97  VAL B CG2 1 
ATOM   3027 N N   . PHE B 1 82  ? -33.601 3.962   20.034 1.00 30.68  ? 98  PHE B N   1 
ATOM   3028 C CA  . PHE B 1 82  ? -33.317 2.773   20.821 1.00 27.68  ? 98  PHE B CA  1 
ATOM   3029 C C   . PHE B 1 82  ? -34.611 1.992   21.008 1.00 27.29  ? 98  PHE B C   1 
ATOM   3030 O O   . PHE B 1 82  ? -35.607 2.568   21.429 1.00 28.45  ? 98  PHE B O   1 
ATOM   3031 C CB  . PHE B 1 82  ? -32.706 3.146   22.169 1.00 27.33  ? 98  PHE B CB  1 
ATOM   3032 C CG  . PHE B 1 82  ? -32.391 1.987   23.086 1.00 27.39  ? 98  PHE B CG  1 
ATOM   3033 C CD1 . PHE B 1 82  ? -31.619 0.924   22.641 1.00 30.20  ? 98  PHE B CD1 1 
ATOM   3034 C CD2 . PHE B 1 82  ? -32.872 1.958   24.385 1.00 26.74  ? 98  PHE B CD2 1 
ATOM   3035 C CE1 . PHE B 1 82  ? -31.332 -0.136  23.486 1.00 29.63  ? 98  PHE B CE1 1 
ATOM   3036 C CE2 . PHE B 1 82  ? -32.592 0.895   25.228 1.00 29.51  ? 98  PHE B CE2 1 
ATOM   3037 C CZ  . PHE B 1 82  ? -31.820 -0.152  24.770 1.00 31.72  ? 98  PHE B CZ  1 
ATOM   3038 N N   . THR B 1 83  ? -34.578 0.683   20.712 1.00 28.52  ? 99  THR B N   1 
ATOM   3039 C CA  . THR B 1 83  ? -35.640 -0.206  21.165 1.00 31.44  ? 99  THR B CA  1 
ATOM   3040 C C   . THR B 1 83  ? -35.111 -1.104  22.294 1.00 32.26  ? 99  THR B C   1 
ATOM   3041 O O   . THR B 1 83  ? -34.299 -1.994  22.029 1.00 36.47  ? 99  THR B O   1 
ATOM   3042 C CB  . THR B 1 83  ? -36.206 -1.065  20.028 1.00 34.54  ? 99  THR B CB  1 
ATOM   3043 O OG1 . THR B 1 83  ? -36.592 -0.213  18.945 1.00 31.28  ? 99  THR B OG1 1 
ATOM   3044 C CG2 . THR B 1 83  ? -37.366 -1.919  20.498 1.00 35.77  ? 99  THR B CG2 1 
ATOM   3045 N N   . PRO B 1 84  ? -35.549 -0.892  23.561 1.00 27.02  ? 100 PRO B N   1 
ATOM   3046 C CA  . PRO B 1 84  ? -35.139 -1.734  24.684 1.00 34.28  ? 100 PRO B CA  1 
ATOM   3047 C C   . PRO B 1 84  ? -35.719 -3.146  24.595 1.00 35.51  ? 100 PRO B C   1 
ATOM   3048 O O   . PRO B 1 84  ? -36.917 -3.311  24.419 1.00 32.93  ? 100 PRO B O   1 
ATOM   3049 C CB  . PRO B 1 84  ? -35.661 -1.023  25.940 1.00 31.40  ? 100 PRO B CB  1 
ATOM   3050 C CG  . PRO B 1 84  ? -36.700 -0.011  25.455 1.00 31.99  ? 100 PRO B CG  1 
ATOM   3051 C CD  . PRO B 1 84  ? -36.531 0.125   23.956 1.00 28.23  ? 100 PRO B CD  1 
ATOM   3052 N N   . GLY B 1 85  ? -34.850 -4.159  24.711 1.00 44.17  ? 101 GLY B N   1 
ATOM   3053 C CA  . GLY B 1 85  ? -35.227 -5.544  24.472 1.00 43.66  ? 101 GLY B CA  1 
ATOM   3054 C C   . GLY B 1 85  ? -35.549 -5.756  22.995 1.00 46.37  ? 101 GLY B C   1 
ATOM   3055 O O   . GLY B 1 85  ? -35.220 -4.923  22.149 1.00 53.11  ? 101 GLY B O   1 
ATOM   3056 N N   . SER B 1 86  ? -36.212 -6.870  22.685 1.00 44.80  ? 102 SER B N   1 
ATOM   3057 C CA  . SER B 1 86  ? -36.787 -7.043  21.364 1.00 44.07  ? 102 SER B CA  1 
ATOM   3058 C C   . SER B 1 86  ? -38.187 -6.448  21.363 1.00 39.92  ? 102 SER B C   1 
ATOM   3059 O O   . SER B 1 86  ? -38.755 -6.195  20.299 1.00 44.52  ? 102 SER B O   1 
ATOM   3060 C CB  . SER B 1 86  ? -36.826 -8.490  20.952 1.00 49.69  ? 102 SER B CB  1 
ATOM   3061 O OG  . SER B 1 86  ? -36.048 -9.275  21.843 1.00 56.31  ? 102 SER B OG  1 
ATOM   3062 N N   . SER B 1 87  ? -38.753 -6.243  22.559 1.00 31.95  ? 103 SER B N   1 
ATOM   3063 C CA  . SER B 1 87  ? -40.193 -6.057  22.639 1.00 35.21  ? 103 SER B CA  1 
ATOM   3064 C C   . SER B 1 87  ? -40.577 -4.655  23.110 1.00 30.71  ? 103 SER B C   1 
ATOM   3065 O O   . SER B 1 87  ? -41.754 -4.341  23.170 1.00 29.82  ? 103 SER B O   1 
ATOM   3066 C CB  . SER B 1 87  ? -40.773 -7.135  23.513 1.00 40.51  ? 103 SER B CB  1 
ATOM   3067 O OG  . SER B 1 87  ? -40.496 -8.417  22.959 1.00 39.34  ? 103 SER B OG  1 
ATOM   3068 N N   . GLY B 1 88  ? -39.594 -3.805  23.431 1.00 31.28  ? 104 GLY B N   1 
ATOM   3069 C CA  . GLY B 1 88  ? -39.880 -2.500  24.009 1.00 30.02  ? 104 GLY B CA  1 
ATOM   3070 C C   . GLY B 1 88  ? -40.499 -1.532  22.998 1.00 28.75  ? 104 GLY B C   1 
ATOM   3071 O O   . GLY B 1 88  ? -40.343 -1.690  21.784 1.00 28.35  ? 104 GLY B O   1 
ATOM   3072 N N   . ARG B 1 89  ? -41.226 -0.545  23.515 1.00 29.42  ? 105 ARG B N   1 
ATOM   3073 C CA  . ARG B 1 89  ? -41.700 0.553   22.693 1.00 27.91  ? 105 ARG B CA  1 
ATOM   3074 C C   . ARG B 1 89  ? -40.488 1.354   22.238 1.00 26.25  ? 105 ARG B C   1 
ATOM   3075 O O   . ARG B 1 89  ? -39.673 1.695   23.072 1.00 23.85  ? 105 ARG B O   1 
ATOM   3076 C CB  . ARG B 1 89  ? -42.667 1.446   23.459 1.00 28.20  ? 105 ARG B CB  1 
ATOM   3077 C CG  . ARG B 1 89  ? -43.205 2.576   22.599 1.00 26.54  ? 105 ARG B CG  1 
ATOM   3078 C CD  . ARG B 1 89  ? -44.252 3.319   23.366 1.00 26.78  ? 105 ARG B CD  1 
ATOM   3079 N NE  . ARG B 1 89  ? -44.744 4.451   22.612 1.00 25.45  ? 105 ARG B NE  1 
ATOM   3080 C CZ  . ARG B 1 89  ? -45.681 5.276   23.053 1.00 25.16  ? 105 ARG B CZ  1 
ATOM   3081 N NH1 . ARG B 1 89  ? -46.293 5.034   24.199 1.00 25.59  ? 105 ARG B NH1 1 
ATOM   3082 N NH2 . ARG B 1 89  ? -46.028 6.329   22.333 1.00 24.78  ? 105 ARG B NH2 1 
ATOM   3083 N N   . PRO B 1 90  ? -40.298 1.612   20.922 1.00 25.31  ? 106 PRO B N   1 
ATOM   3084 C CA  . PRO B 1 90  ? -39.164 2.405   20.440 1.00 26.48  ? 106 PRO B CA  1 
ATOM   3085 C C   . PRO B 1 90  ? -39.122 3.776   21.102 1.00 28.18  ? 106 PRO B C   1 
ATOM   3086 O O   . PRO B 1 90  ? -40.169 4.393   21.310 1.00 23.25  ? 106 PRO B O   1 
ATOM   3087 C CB  . PRO B 1 90  ? -39.426 2.542   18.932 1.00 28.29  ? 106 PRO B CB  1 
ATOM   3088 C CG  . PRO B 1 90  ? -40.217 1.295   18.609 1.00 30.37  ? 106 PRO B CG  1 
ATOM   3089 C CD  . PRO B 1 90  ? -41.119 1.088   19.816 1.00 27.31  ? 106 PRO B CD  1 
ATOM   3090 N N   . GLN B 1 91  ? -37.904 4.223   21.450 1.00 26.72  ? 107 GLN B N   1 
ATOM   3091 C CA  . GLN B 1 91  ? -37.726 5.501   22.122 1.00 25.63  ? 107 GLN B CA  1 
ATOM   3092 C C   . GLN B 1 91  ? -37.666 6.635   21.095 1.00 24.34  ? 107 GLN B C   1 
ATOM   3093 O O   . GLN B 1 91  ? -36.643 7.298   20.956 1.00 20.68  ? 107 GLN B O   1 
ATOM   3094 C CB  . GLN B 1 91  ? -36.479 5.439   23.017 1.00 22.81  ? 107 GLN B CB  1 
ATOM   3095 C CG  . GLN B 1 91  ? -36.584 4.413   24.144 1.00 22.89  ? 107 GLN B CG  1 
ATOM   3096 C CD  . GLN B 1 91  ? -35.441 4.482   25.134 1.00 23.41  ? 107 GLN B CD  1 
ATOM   3097 O OE1 . GLN B 1 91  ? -34.352 4.953   24.833 1.00 24.49  ? 107 GLN B OE1 1 
ATOM   3098 N NE2 . GLN B 1 91  ? -35.702 4.085   26.367 1.00 25.97  ? 107 GLN B NE2 1 
ATOM   3099 N N   . THR B 1 92  ? -38.816 6.934   20.480 1.00 22.78  ? 108 THR B N   1 
ATOM   3100 C CA  . THR B 1 92  ? -38.940 7.877   19.367 1.00 24.86  ? 108 THR B CA  1 
ATOM   3101 C C   . THR B 1 92  ? -38.675 9.339   19.759 1.00 24.21  ? 108 THR B C   1 
ATOM   3102 O O   . THR B 1 92  ? -38.334 10.150  18.892 1.00 23.95  ? 108 THR B O   1 
ATOM   3103 C CB  . THR B 1 92  ? -40.333 7.698   18.750 1.00 24.60  ? 108 THR B CB  1 
ATOM   3104 O OG1 . THR B 1 92  ? -41.319 7.693   19.789 1.00 26.81  ? 108 THR B OG1 1 
ATOM   3105 C CG2 . THR B 1 92  ? -40.414 6.379   18.020 1.00 25.62  ? 108 THR B CG2 1 
ATOM   3106 N N   . GLY B 1 93  ? -38.815 9.679   21.054 1.00 23.34  ? 109 GLY B N   1 
ATOM   3107 C CA  . GLY B 1 93  ? -38.458 11.009  21.543 1.00 23.00  ? 109 GLY B CA  1 
ATOM   3108 C C   . GLY B 1 93  ? -36.941 11.279  21.596 1.00 22.11  ? 109 GLY B C   1 
ATOM   3109 O O   . GLY B 1 93  ? -36.506 12.421  21.528 1.00 20.48  ? 109 GLY B O   1 
ATOM   3110 N N   . PHE B 1 94  ? -36.138 10.232  21.776 1.00 22.83  ? 110 PHE B N   1 
ATOM   3111 C CA  . PHE B 1 94  ? -34.705 10.364  21.965 1.00 23.25  ? 110 PHE B CA  1 
ATOM   3112 C C   . PHE B 1 94  ? -33.957 10.099  20.660 1.00 21.73  ? 110 PHE B C   1 
ATOM   3113 O O   . PHE B 1 94  ? -34.422 9.386   19.781 1.00 21.63  ? 110 PHE B O   1 
ATOM   3114 C CB  . PHE B 1 94  ? -34.200 9.371   23.021 1.00 23.19  ? 110 PHE B CB  1 
ATOM   3115 C CG  . PHE B 1 94  ? -34.646 9.584   24.454 1.00 23.41  ? 110 PHE B CG  1 
ATOM   3116 C CD1 . PHE B 1 94  ? -34.898 10.851  24.969 1.00 24.62  ? 110 PHE B CD1 1 
ATOM   3117 C CD2 . PHE B 1 94  ? -34.726 8.509   25.320 1.00 23.91  ? 110 PHE B CD2 1 
ATOM   3118 C CE1 . PHE B 1 94  ? -35.259 11.034  26.295 1.00 24.25  ? 110 PHE B CE1 1 
ATOM   3119 C CE2 . PHE B 1 94  ? -35.079 8.688   26.650 1.00 24.37  ? 110 PHE B CE2 1 
ATOM   3120 C CZ  . PHE B 1 94  ? -35.376 9.941   27.132 1.00 24.96  ? 110 PHE B CZ  1 
ATOM   3121 N N   . ARG B 1 95  ? -32.783 10.702  20.527 1.00 21.55  ? 111 ARG B N   1 
ATOM   3122 C CA  . ARG B 1 95  ? -31.794 10.230  19.574 1.00 22.37  ? 111 ARG B CA  1 
ATOM   3123 C C   . ARG B 1 95  ? -30.550 9.887   20.377 1.00 22.40  ? 111 ARG B C   1 
ATOM   3124 O O   . ARG B 1 95  ? -30.002 10.773  21.064 1.00 20.83  ? 111 ARG B O   1 
ATOM   3125 C CB  . ARG B 1 95  ? -31.515 11.273  18.484 1.00 24.46  ? 111 ARG B CB  1 
ATOM   3126 C CG  . ARG B 1 95  ? -32.692 11.515  17.536 1.00 24.02  ? 111 ARG B CG  1 
ATOM   3127 C CD  . ARG B 1 95  ? -33.062 10.266  16.750 1.00 23.31  ? 111 ARG B CD  1 
ATOM   3128 N NE  . ARG B 1 95  ? -34.192 10.476  15.851 1.00 23.47  ? 111 ARG B NE  1 
ATOM   3129 C CZ  . ARG B 1 95  ? -35.467 10.365  16.186 1.00 23.26  ? 111 ARG B CZ  1 
ATOM   3130 N NH1 . ARG B 1 95  ? -35.831 10.013  17.412 1.00 24.66  ? 111 ARG B NH1 1 
ATOM   3131 N NH2 . ARG B 1 95  ? -36.389 10.549  15.258 1.00 24.34  ? 111 ARG B NH2 1 
ATOM   3132 N N   . ARG B 1 96  ? -30.135 8.608   20.326 1.00 22.98  ? 112 ARG B N   1 
ATOM   3133 C CA  . ARG B 1 96  ? -29.089 8.196   21.249 1.00 24.16  ? 112 ARG B CA  1 
ATOM   3134 C C   . ARG B 1 96  ? -28.188 7.116   20.668 1.00 25.07  ? 112 ARG B C   1 
ATOM   3135 O O   . ARG B 1 96  ? -28.616 6.215   19.954 1.00 25.96  ? 112 ARG B O   1 
ATOM   3136 C CB  . ARG B 1 96  ? -29.684 7.770   22.593 1.00 24.71  ? 112 ARG B CB  1 
ATOM   3137 C CG  . ARG B 1 96  ? -30.423 6.444   22.567 1.00 25.66  ? 112 ARG B CG  1 
ATOM   3138 C CD  . ARG B 1 96  ? -31.316 6.302   23.787 1.00 25.45  ? 112 ARG B CD  1 
ATOM   3139 N NE  . ARG B 1 96  ? -30.505 6.299   25.001 1.00 28.66  ? 112 ARG B NE  1 
ATOM   3140 C CZ  . ARG B 1 96  ? -30.925 5.894   26.196 1.00 27.90  ? 112 ARG B CZ  1 
ATOM   3141 N NH1 . ARG B 1 96  ? -32.165 5.472   26.365 1.00 28.07  ? 112 ARG B NH1 1 
ATOM   3142 N NH2 . ARG B 1 96  ? -30.088 5.887   27.211 1.00 27.43  ? 112 ARG B NH2 1 
ATOM   3143 N N   . THR B 1 97  ? -26.904 7.275   21.018 1.00 23.65  ? 113 THR B N   1 
ATOM   3144 C CA  . THR B 1 97  ? -25.860 6.295   20.843 1.00 21.75  ? 113 THR B CA  1 
ATOM   3145 C C   . THR B 1 97  ? -24.982 6.337   22.091 1.00 22.80  ? 113 THR B C   1 
ATOM   3146 O O   . THR B 1 97  ? -24.343 7.357   22.370 1.00 22.74  ? 113 THR B O   1 
ATOM   3147 C CB  . THR B 1 97  ? -24.965 6.602   19.644 1.00 22.51  ? 113 THR B CB  1 
ATOM   3148 O OG1 . THR B 1 97  ? -25.702 6.629   18.421 1.00 23.71  ? 113 THR B OG1 1 
ATOM   3149 C CG2 . THR B 1 97  ? -23.849 5.585   19.539 1.00 23.76  ? 113 THR B CG2 1 
ATOM   3150 N N   . GLU B 1 98  ? -24.905 5.214   22.816 1.00 22.30  ? 114 GLU B N   1 
ATOM   3151 C CA  . GLU B 1 98  ? -24.018 5.128   23.960 1.00 23.80  ? 114 GLU B CA  1 
ATOM   3152 C C   . GLU B 1 98  ? -23.157 3.882   23.906 1.00 22.89  ? 114 GLU B C   1 
ATOM   3153 O O   . GLU B 1 98  ? -23.505 2.888   23.265 1.00 19.65  ? 114 GLU B O   1 
ATOM   3154 C CB  . GLU B 1 98  ? -24.830 5.112   25.245 1.00 23.13  ? 114 GLU B CB  1 
ATOM   3155 C CG  . GLU B 1 98  ? -25.339 6.474   25.604 1.00 25.28  ? 114 GLU B CG  1 
ATOM   3156 C CD  . GLU B 1 98  ? -26.796 6.410   25.996 1.00 26.82  ? 114 GLU B CD  1 
ATOM   3157 O OE1 . GLU B 1 98  ? -27.107 5.754   27.021 1.00 24.14  ? 114 GLU B OE1 1 
ATOM   3158 O OE2 . GLU B 1 98  ? -27.606 6.952   25.229 1.00 29.21  ? 114 GLU B OE2 1 
ATOM   3159 N N   . LEU B 1 99  ? -21.996 4.023   24.556 1.00 24.64  ? 115 LEU B N   1 
ATOM   3160 C CA  . LEU B 1 99  ? -21.134 2.912   24.927 1.00 24.32  ? 115 LEU B CA  1 
ATOM   3161 C C   . LEU B 1 99  ? -21.191 2.788   26.445 1.00 25.04  ? 115 LEU B C   1 
ATOM   3162 O O   . LEU B 1 99  ? -21.240 3.802   27.135 1.00 24.17  ? 115 LEU B O   1 
ATOM   3163 C CB  . LEU B 1 99  ? -19.695 3.174   24.468 1.00 26.39  ? 115 LEU B CB  1 
ATOM   3164 C CG  . LEU B 1 99  ? -19.469 3.386   22.970 1.00 28.54  ? 115 LEU B CG  1 
ATOM   3165 C CD1 . LEU B 1 99  ? -18.031 3.811   22.704 1.00 29.03  ? 115 LEU B CD1 1 
ATOM   3166 C CD2 . LEU B 1 99  ? -19.818 2.138   22.168 1.00 30.34  ? 115 LEU B CD2 1 
ATOM   3167 N N   . ILE B 1 100 ? -21.228 1.533   26.936 1.00 23.26  ? 116 ILE B N   1 
ATOM   3168 C CA  . ILE B 1 100 ? -21.359 1.232   28.347 1.00 23.62  ? 116 ILE B CA  1 
ATOM   3169 C C   . ILE B 1 100 ? -20.147 0.413   28.783 1.00 24.03  ? 116 ILE B C   1 
ATOM   3170 O O   . ILE B 1 100 ? -19.807 -0.562  28.142 1.00 25.34  ? 116 ILE B O   1 
ATOM   3171 C CB  . ILE B 1 100 ? -22.674 0.473   28.617 1.00 23.37  ? 116 ILE B CB  1 
ATOM   3172 C CG1 . ILE B 1 100 ? -23.904 1.330   28.324 1.00 23.20  ? 116 ILE B CG1 1 
ATOM   3173 C CG2 . ILE B 1 100 ? -22.728 -0.061  30.048 1.00 23.19  ? 116 ILE B CG2 1 
ATOM   3174 C CD1 . ILE B 1 100 ? -25.232 0.541   28.450 1.00 23.79  ? 116 ILE B CD1 1 
ATOM   3175 N N   . ALA B 1 101 ? -19.530 0.789   29.899 1.00 24.71  ? 117 ALA B N   1 
ATOM   3176 C CA  . ALA B 1 101 ? -18.373 0.080   30.412 1.00 25.17  ? 117 ALA B CA  1 
ATOM   3177 C C   . ALA B 1 101 ? -18.752 -1.360  30.775 1.00 26.61  ? 117 ALA B C   1 
ATOM   3178 O O   . ALA B 1 101 ? -19.704 -1.586  31.510 1.00 25.34  ? 117 ALA B O   1 
ATOM   3179 C CB  . ALA B 1 101 ? -17.863 0.828   31.609 1.00 26.24  ? 117 ALA B CB  1 
ATOM   3180 N N   . GLN B 1 102 ? -17.915 -2.288  30.305 1.00 27.67  ? 118 GLN B N   1 
ATOM   3181 C CA  . GLN B 1 102 ? -18.060 -3.728  30.389 1.00 31.68  ? 118 GLN B CA  1 
ATOM   3182 C C   . GLN B 1 102 ? -16.737 -4.338  30.871 1.00 31.90  ? 118 GLN B C   1 
ATOM   3183 O O   . GLN B 1 102 ? -15.679 -3.859  30.476 1.00 29.24  ? 118 GLN B O   1 
ATOM   3184 C CB  . GLN B 1 102 ? -18.344 -4.179  28.956 1.00 34.23  ? 118 GLN B CB  1 
ATOM   3185 C CG  . GLN B 1 102 ? -18.775 -5.614  28.782 1.00 37.86  ? 118 GLN B CG  1 
ATOM   3186 C CD  . GLN B 1 102 ? -19.083 -5.838  27.326 1.00 34.43  ? 118 GLN B CD  1 
ATOM   3187 O OE1 . GLN B 1 102 ? -18.207 -6.054  26.491 1.00 42.61  ? 118 GLN B OE1 1 
ATOM   3188 N NE2 . GLN B 1 102 ? -20.351 -5.762  27.005 1.00 38.08  ? 118 GLN B NE2 1 
ATOM   3189 N N   . VAL B 1 103 ? -16.796 -5.405  31.687 1.00 36.88  ? 119 VAL B N   1 
ATOM   3190 C CA  . VAL B 1 103 ? -15.632 -6.240  31.973 1.00 40.01  ? 119 VAL B CA  1 
ATOM   3191 C C   . VAL B 1 103 ? -16.053 -7.707  31.854 1.00 42.77  ? 119 VAL B C   1 
ATOM   3192 O O   . VAL B 1 103 ? -17.104 -8.085  32.376 1.00 45.60  ? 119 VAL B O   1 
ATOM   3193 C CB  . VAL B 1 103 ? -15.022 -5.920  33.354 1.00 46.17  ? 119 VAL B CB  1 
ATOM   3194 C CG1 . VAL B 1 103 ? -15.755 -6.625  34.493 1.00 45.55  ? 119 VAL B CG1 1 
ATOM   3195 C CG2 . VAL B 1 103 ? -13.530 -6.235  33.410 1.00 48.87  ? 119 VAL B CG2 1 
ATOM   3196 N N   . ASN B 1 104 ? -15.257 -8.489  31.102 1.00 45.44  ? 120 ASN B N   1 
ATOM   3197 C CA  . ASN B 1 104 ? -15.479 -9.908  30.827 1.00 47.50  ? 120 ASN B CA  1 
ATOM   3198 C C   . ASN B 1 104 ? -16.807 -10.121 30.117 1.00 47.77  ? 120 ASN B C   1 
ATOM   3199 O O   . ASN B 1 104 ? -17.491 -11.108 30.366 1.00 49.95  ? 120 ASN B O   1 
ATOM   3200 C CB  . ASN B 1 104 ? -15.416 -10.774 32.090 1.00 49.92  ? 120 ASN B CB  1 
ATOM   3201 C CG  . ASN B 1 104 ? -14.144 -10.544 32.885 1.00 54.25  ? 120 ASN B CG  1 
ATOM   3202 O OD1 . ASN B 1 104 ? -13.039 -10.636 32.349 1.00 58.79  ? 120 ASN B OD1 1 
ATOM   3203 N ND2 . ASN B 1 104 ? -14.284 -10.202 34.153 1.00 53.24  ? 120 ASN B ND2 1 
ATOM   3204 N N   . GLY B 1 105 ? -17.156 -9.197  29.224 1.00 43.45  ? 121 GLY B N   1 
ATOM   3205 C CA  . GLY B 1 105 ? -18.435 -9.249  28.538 1.00 43.53  ? 121 GLY B CA  1 
ATOM   3206 C C   . GLY B 1 105 ? -19.643 -8.868  29.404 1.00 41.56  ? 121 GLY B C   1 
ATOM   3207 O O   . GLY B 1 105 ? -20.768 -9.024  28.945 1.00 40.03  ? 121 GLY B O   1 
ATOM   3208 N N   . SER B 1 106 ? -19.439 -8.312  30.610 1.00 39.04  ? 122 SER B N   1 
ATOM   3209 C CA  . SER B 1 106 ? -20.546 -8.048  31.531 1.00 38.34  ? 122 SER B CA  1 
ATOM   3210 C C   . SER B 1 106 ? -20.469 -6.631  32.106 1.00 35.32  ? 122 SER B C   1 
ATOM   3211 O O   . SER B 1 106 ? -19.439 -6.209  32.636 1.00 33.21  ? 122 SER B O   1 
ATOM   3212 C CB  . SER B 1 106 ? -20.570 -9.074  32.646 1.00 43.29  ? 122 SER B CB  1 
ATOM   3213 O OG  . SER B 1 106 ? -21.542 -8.761  33.647 1.00 44.10  ? 122 SER B OG  1 
ATOM   3214 N N   . ASN B 1 107 ? -21.589 -5.908  32.041 1.00 38.88  ? 123 ASN B N   1 
ATOM   3215 C CA  . ASN B 1 107 ? -21.713 -4.630  32.730 1.00 41.14  ? 123 ASN B CA  1 
ATOM   3216 C C   . ASN B 1 107 ? -22.129 -4.889  34.182 1.00 43.83  ? 123 ASN B C   1 
ATOM   3217 O O   . ASN B 1 107 ? -21.764 -4.108  35.068 1.00 36.91  ? 123 ASN B O   1 
ATOM   3218 C CB  . ASN B 1 107 ? -22.618 -3.643  31.978 1.00 42.08  ? 123 ASN B CB  1 
ATOM   3219 C CG  . ASN B 1 107 ? -24.062 -4.089  31.870 1.00 40.91  ? 123 ASN B CG  1 
ATOM   3220 O OD1 . ASN B 1 107 ? -24.977 -3.321  32.147 1.00 45.58  ? 123 ASN B OD1 1 
ATOM   3221 N ND2 . ASN B 1 107 ? -24.284 -5.316  31.446 1.00 38.09  ? 123 ASN B ND2 1 
ATOM   3222 N N   . ILE B 1 108 ? -22.821 -6.028  34.422 1.00 45.18  ? 124 ILE B N   1 
ATOM   3223 C CA  . ILE B 1 108 ? -23.310 -6.405  35.746 1.00 44.45  ? 124 ILE B CA  1 
ATOM   3224 C C   . ILE B 1 108 ? -22.143 -6.628  36.716 1.00 44.92  ? 124 ILE B C   1 
ATOM   3225 O O   . ILE B 1 108 ? -22.163 -6.097  37.823 1.00 48.28  ? 124 ILE B O   1 
ATOM   3226 C CB  . ILE B 1 108 ? -24.214 -7.654  35.667 1.00 49.00  ? 124 ILE B CB  1 
ATOM   3227 C CG1 . ILE B 1 108 ? -25.493 -7.406  34.856 1.00 50.39  ? 124 ILE B CG1 1 
ATOM   3228 C CG2 . ILE B 1 108 ? -24.527 -8.185  37.062 1.00 51.55  ? 124 ILE B CG2 1 
ATOM   3229 C CD1 . ILE B 1 108 ? -26.559 -6.602  35.584 1.00 52.20  ? 124 ILE B CD1 1 
ATOM   3230 N N   . ASP B 1 109 ? -21.142 -7.427  36.320 1.00 42.75  ? 125 ASP B N   1 
ATOM   3231 C CA  . ASP B 1 109 ? -19.990 -7.714  37.171 1.00 46.18  ? 125 ASP B CA  1 
ATOM   3232 C C   . ASP B 1 109 ? -19.172 -6.453  37.489 1.00 43.82  ? 125 ASP B C   1 
ATOM   3233 O O   . ASP B 1 109 ? -18.369 -6.464  38.418 1.00 39.38  ? 125 ASP B O   1 
ATOM   3234 C CB  . ASP B 1 109 ? -19.065 -8.757  36.534 1.00 44.18  ? 125 ASP B CB  1 
ATOM   3235 C CG  . ASP B 1 109 ? -19.708 -10.124 36.336 1.00 51.28  ? 125 ASP B CG  1 
ATOM   3236 O OD1 . ASP B 1 109 ? -20.691 -10.424 37.052 1.00 53.06  ? 125 ASP B OD1 1 
ATOM   3237 O OD2 . ASP B 1 109 ? -19.258 -10.864 35.433 1.00 47.77  ? 125 ASP B OD2 1 
ATOM   3238 N N   . LEU B 1 110 ? -19.353 -5.364  36.727 1.00 40.82  ? 126 LEU B N   1 
ATOM   3239 C CA  . LEU B 1 110 ? -18.557 -4.160  36.944 1.00 35.53  ? 126 LEU B CA  1 
ATOM   3240 C C   . LEU B 1 110 ? -19.194 -3.265  38.000 1.00 31.83  ? 126 LEU B C   1 
ATOM   3241 O O   . LEU B 1 110 ? -18.472 -2.513  38.650 1.00 34.59  ? 126 LEU B O   1 
ATOM   3242 C CB  . LEU B 1 110 ? -18.378 -3.413  35.620 1.00 34.25  ? 126 LEU B CB  1 
ATOM   3243 C CG  . LEU B 1 110 ? -17.349 -2.285  35.615 1.00 33.87  ? 126 LEU B CG  1 
ATOM   3244 C CD1 . LEU B 1 110 ? -15.934 -2.813  35.851 1.00 35.85  ? 126 LEU B CD1 1 
ATOM   3245 C CD2 . LEU B 1 110 ? -17.404 -1.536  34.300 1.00 30.50  ? 126 LEU B CD2 1 
ATOM   3246 N N   . ILE B 1 111 ? -20.518 -3.361  38.188 1.00 30.79  ? 127 ILE B N   1 
ATOM   3247 C CA  . ILE B 1 111 ? -21.254 -2.489  39.102 1.00 32.18  ? 127 ILE B CA  1 
ATOM   3248 C C   . ILE B 1 111 ? -20.632 -2.484  40.508 1.00 35.41  ? 127 ILE B C   1 
ATOM   3249 O O   . ILE B 1 111 ? -20.515 -1.427  41.131 1.00 34.12  ? 127 ILE B O   1 
ATOM   3250 C CB  . ILE B 1 111 ? -22.741 -2.894  39.201 1.00 35.30  ? 127 ILE B CB  1 
ATOM   3251 C CG1 . ILE B 1 111 ? -23.449 -2.970  37.840 1.00 37.72  ? 127 ILE B CG1 1 
ATOM   3252 C CG2 . ILE B 1 111 ? -23.473 -1.960  40.152 1.00 33.49  ? 127 ILE B CG2 1 
ATOM   3253 C CD1 . ILE B 1 111 ? -24.805 -3.665  37.887 1.00 39.19  ? 127 ILE B CD1 1 
ATOM   3254 N N   . PRO B 1 112 ? -20.318 -3.651  41.120 1.00 36.50  ? 128 PRO B N   1 
ATOM   3255 C CA  . PRO B 1 112 ? -19.710 -3.677  42.449 1.00 41.60  ? 128 PRO B CA  1 
ATOM   3256 C C   . PRO B 1 112 ? -18.296 -3.095  42.472 1.00 38.38  ? 128 PRO B C   1 
ATOM   3257 O O   . PRO B 1 112 ? -17.915 -2.444  43.439 1.00 45.10  ? 128 PRO B O   1 
ATOM   3258 C CB  . PRO B 1 112 ? -19.698 -5.173  42.819 1.00 43.00  ? 128 PRO B CB  1 
ATOM   3259 C CG  . PRO B 1 112 ? -19.695 -5.891  41.484 1.00 40.10  ? 128 PRO B CG  1 
ATOM   3260 C CD  . PRO B 1 112 ? -20.558 -5.013  40.607 1.00 39.99  ? 128 PRO B CD  1 
ATOM   3261 N N   . ILE B 1 113 ? -17.556 -3.293  41.384 1.00 33.87  ? 129 ILE B N   1 
ATOM   3262 C CA  . ILE B 1 113 ? -16.194 -2.802  41.268 1.00 36.03  ? 129 ILE B CA  1 
ATOM   3263 C C   . ILE B 1 113 ? -16.192 -1.268  41.177 1.00 35.48  ? 129 ILE B C   1 
ATOM   3264 O O   . ILE B 1 113 ? -15.547 -0.612  41.994 1.00 31.15  ? 129 ILE B O   1 
ATOM   3265 C CB  . ILE B 1 113 ? -15.486 -3.516  40.098 1.00 39.32  ? 129 ILE B CB  1 
ATOM   3266 C CG1 . ILE B 1 113 ? -15.435 -5.029  40.341 1.00 41.08  ? 129 ILE B CG1 1 
ATOM   3267 C CG2 . ILE B 1 113 ? -14.099 -2.941  39.841 1.00 42.86  ? 129 ILE B CG2 1 
ATOM   3268 C CD1 . ILE B 1 113 ? -15.028 -5.850  39.142 1.00 42.67  ? 129 ILE B CD1 1 
ATOM   3269 N N   . ILE B 1 114 ? -16.991 -0.672  40.273 1.00 33.06  ? 130 ILE B N   1 
ATOM   3270 C CA  . ILE B 1 114 ? -16.961 0.779   40.104 1.00 31.70  ? 130 ILE B CA  1 
ATOM   3271 C C   . ILE B 1 114 ? -17.924 1.455   41.071 1.00 31.91  ? 130 ILE B C   1 
ATOM   3272 O O   . ILE B 1 114 ? -18.014 2.684   41.102 1.00 31.67  ? 130 ILE B O   1 
ATOM   3273 C CB  . ILE B 1 114 ? -17.245 1.197   38.647 1.00 29.32  ? 130 ILE B CB  1 
ATOM   3274 C CG1 . ILE B 1 114 ? -18.698 0.917   38.247 1.00 28.68  ? 130 ILE B CG1 1 
ATOM   3275 C CG2 . ILE B 1 114 ? -16.250 0.567   37.688 1.00 26.69  ? 130 ILE B CG2 1 
ATOM   3276 C CD1 . ILE B 1 114 ? -19.109 1.544   36.940 1.00 27.87  ? 130 ILE B CD1 1 
ATOM   3277 N N   . GLY B 1 115 ? -18.616 0.669   41.898 1.00 30.12  ? 131 GLY B N   1 
ATOM   3278 C CA  . GLY B 1 115 ? -19.624 1.216   42.788 1.00 31.82  ? 131 GLY B CA  1 
ATOM   3279 C C   . GLY B 1 115 ? -19.278 1.140   44.277 1.00 30.86  ? 131 GLY B C   1 
ATOM   3280 O O   . GLY B 1 115 ? -20.167 1.298   45.114 1.00 29.17  ? 131 GLY B O   1 
ATOM   3281 N N   . LYS B 1 116 ? -18.008 0.909   44.626 1.00 31.81  ? 132 LYS B N   1 
ATOM   3282 C CA  . LYS B 1 116 ? -17.637 0.877   46.034 1.00 34.11  ? 132 LYS B CA  1 
ATOM   3283 C C   . LYS B 1 116 ? -16.464 1.813   46.313 1.00 30.12  ? 132 LYS B C   1 
ATOM   3284 O O   . LYS B 1 116 ? -15.528 1.921   45.515 1.00 31.94  ? 132 LYS B O   1 
ATOM   3285 C CB  . LYS B 1 116 ? -17.256 -0.539  46.472 1.00 40.34  ? 132 LYS B CB  1 
ATOM   3286 C CG  . LYS B 1 116 ? -18.403 -1.527  46.580 1.00 42.77  ? 132 LYS B CG  1 
ATOM   3287 C CD  . LYS B 1 116 ? -17.885 -2.954  46.711 1.00 51.90  ? 132 LYS B CD  1 
ATOM   3288 C CE  . LYS B 1 116 ? -18.966 -4.009  46.560 1.00 53.17  ? 132 LYS B CE  1 
ATOM   3289 N NZ  . LYS B 1 116 ? -18.382 -5.313  46.166 1.00 54.12  ? 132 LYS B NZ  1 
ATOM   3290 N N   . GLY B 1 117 ? -16.526 2.459   47.476 1.00 29.21  ? 133 GLY B N   1 
ATOM   3291 C CA  . GLY B 1 117 ? -15.467 3.337   47.935 1.00 30.55  ? 133 GLY B CA  1 
ATOM   3292 C C   . GLY B 1 117 ? -15.427 4.644   47.143 1.00 31.03  ? 133 GLY B C   1 
ATOM   3293 O O   . GLY B 1 117 ? -16.467 5.200   46.798 1.00 32.45  ? 133 GLY B O   1 
ATOM   3294 N N   . ARG B 1 118 ? -14.208 5.146   46.914 1.00 31.15  ? 134 ARG B N   1 
ATOM   3295 C CA  . ARG B 1 118 ? -14.002 6.352   46.128 1.00 31.73  ? 134 ARG B CA  1 
ATOM   3296 C C   . ARG B 1 118 ? -13.471 5.961   44.753 1.00 29.45  ? 134 ARG B C   1 
ATOM   3297 O O   . ARG B 1 118 ? -12.457 5.260   44.645 1.00 26.88  ? 134 ARG B O   1 
ATOM   3298 C CB  . ARG B 1 118 ? -13.057 7.301   46.863 1.00 33.93  ? 134 ARG B CB  1 
ATOM   3299 C CG  . ARG B 1 118 ? -13.758 8.084   47.967 1.00 39.34  ? 134 ARG B CG  1 
ATOM   3300 C CD  . ARG B 1 118 ? -12.782 8.702   48.938 1.00 42.32  ? 134 ARG B CD  1 
ATOM   3301 N NE  . ARG B 1 118 ? -12.083 9.855   48.419 1.00 48.46  ? 134 ARG B NE  1 
ATOM   3302 C CZ  . ARG B 1 118 ? -10.762 10.028  48.457 1.00 49.06  ? 134 ARG B CZ  1 
ATOM   3303 N NH1 . ARG B 1 118 ? -9.940  9.046   48.782 1.00 43.73  ? 134 ARG B NH1 1 
ATOM   3304 N NH2 . ARG B 1 118 ? -10.260 11.195  48.113 1.00 54.64  ? 134 ARG B NH2 1 
ATOM   3305 N N   . VAL B 1 119 ? -14.169 6.443   43.719 1.00 27.71  ? 135 VAL B N   1 
ATOM   3306 C CA  . VAL B 1 119 ? -13.893 6.061   42.336 1.00 27.58  ? 135 VAL B CA  1 
ATOM   3307 C C   . VAL B 1 119 ? -13.867 7.315   41.452 1.00 25.40  ? 135 VAL B C   1 
ATOM   3308 O O   . VAL B 1 119 ? -14.827 8.081   41.458 1.00 24.69  ? 135 VAL B O   1 
ATOM   3309 C CB  . VAL B 1 119 ? -14.949 5.044   41.852 1.00 26.77  ? 135 VAL B CB  1 
ATOM   3310 C CG1 . VAL B 1 119 ? -14.804 4.710   40.384 1.00 28.10  ? 135 VAL B CG1 1 
ATOM   3311 C CG2 . VAL B 1 119 ? -14.924 3.771   42.697 1.00 27.74  ? 135 VAL B CG2 1 
ATOM   3312 N N   . ALA B 1 120 ? -12.800 7.472   40.655 1.00 23.85  ? 136 ALA B N   1 
ATOM   3313 C CA  . ALA B 1 120 ? -12.700 8.588   39.722 1.00 25.30  ? 136 ALA B CA  1 
ATOM   3314 C C   . ALA B 1 120 ? -13.115 8.180   38.309 1.00 24.47  ? 136 ALA B C   1 
ATOM   3315 O O   . ALA B 1 120 ? -12.464 7.334   37.687 1.00 22.67  ? 136 ALA B O   1 
ATOM   3316 C CB  . ALA B 1 120 ? -11.299 9.141   39.720 1.00 27.45  ? 136 ALA B CB  1 
ATOM   3317 N N   . PHE B 1 121 ? -14.144 8.869   37.781 1.00 23.20  ? 137 PHE B N   1 
ATOM   3318 C CA  . PHE B 1 121 ? -14.621 8.674   36.409 1.00 22.88  ? 137 PHE B CA  1 
ATOM   3319 C C   . PHE B 1 121 ? -13.997 9.736   35.500 1.00 22.10  ? 137 PHE B C   1 
ATOM   3320 O O   . PHE B 1 121 ? -14.277 10.908  35.671 1.00 23.26  ? 137 PHE B O   1 
ATOM   3321 C CB  . PHE B 1 121 ? -16.152 8.752   36.356 1.00 23.46  ? 137 PHE B CB  1 
ATOM   3322 C CG  . PHE B 1 121 ? -16.855 7.650   37.117 1.00 23.66  ? 137 PHE B CG  1 
ATOM   3323 C CD1 . PHE B 1 121 ? -17.026 7.723   38.489 1.00 24.03  ? 137 PHE B CD1 1 
ATOM   3324 C CD2 . PHE B 1 121 ? -17.336 6.537   36.455 1.00 24.25  ? 137 PHE B CD2 1 
ATOM   3325 C CE1 . PHE B 1 121 ? -17.627 6.686   39.194 1.00 24.34  ? 137 PHE B CE1 1 
ATOM   3326 C CE2 . PHE B 1 121 ? -17.897 5.480   37.165 1.00 26.06  ? 137 PHE B CE2 1 
ATOM   3327 C CZ  . PHE B 1 121 ? -18.062 5.567   38.528 1.00 25.10  ? 137 PHE B CZ  1 
ATOM   3328 N N   . HIS B 1 122 ? -13.138 9.317   34.566 1.00 23.71  ? 138 HIS B N   1 
ATOM   3329 C CA  . HIS B 1 122 ? -12.435 10.197  33.654 1.00 24.17  ? 138 HIS B CA  1 
ATOM   3330 C C   . HIS B 1 122 ? -13.098 10.174  32.276 1.00 22.98  ? 138 HIS B C   1 
ATOM   3331 O O   . HIS B 1 122 ? -13.581 9.142   31.816 1.00 22.36  ? 138 HIS B O   1 
ATOM   3332 C CB  . HIS B 1 122 ? -10.982 9.746   33.442 1.00 23.92  ? 138 HIS B CB  1 
ATOM   3333 C CG  . HIS B 1 122 ? -10.109 9.845   34.639 1.00 23.19  ? 138 HIS B CG  1 
ATOM   3334 N ND1 . HIS B 1 122 ? -9.236  10.898  34.797 1.00 21.73  ? 138 HIS B ND1 1 
ATOM   3335 C CD2 . HIS B 1 122 ? -9.964  9.064   35.720 1.00 20.35  ? 138 HIS B CD2 1 
ATOM   3336 C CE1 . HIS B 1 122 ? -8.599  10.739  35.942 1.00 20.80  ? 138 HIS B CE1 1 
ATOM   3337 N NE2 . HIS B 1 122 ? -9.014  9.639   36.512 1.00 19.94  ? 138 HIS B NE2 1 
ATOM   3338 N N   . PHE B 1 123 ? -13.089 11.331  31.614 1.00 21.73  ? 139 PHE B N   1 
ATOM   3339 C CA  . PHE B 1 123 ? -13.575 11.452  30.251 1.00 20.76  ? 139 PHE B CA  1 
ATOM   3340 C C   . PHE B 1 123 ? -13.158 12.812  29.707 1.00 19.37  ? 139 PHE B C   1 
ATOM   3341 O O   . PHE B 1 123 ? -13.238 13.809  30.410 1.00 21.65  ? 139 PHE B O   1 
ATOM   3342 C CB  . PHE B 1 123 ? -15.100 11.276  30.162 1.00 19.97  ? 139 PHE B CB  1 
ATOM   3343 C CG  . PHE B 1 123 ? -15.877 11.987  31.243 1.00 20.07  ? 139 PHE B CG  1 
ATOM   3344 C CD1 . PHE B 1 123 ? -16.067 11.408  32.496 1.00 20.54  ? 139 PHE B CD1 1 
ATOM   3345 C CD2 . PHE B 1 123 ? -16.348 13.272  31.037 1.00 19.71  ? 139 PHE B CD2 1 
ATOM   3346 C CE1 . PHE B 1 123 ? -16.749 12.084  33.490 1.00 19.37  ? 139 PHE B CE1 1 
ATOM   3347 C CE2 . PHE B 1 123 ? -17.055 13.932  32.028 1.00 19.99  ? 139 PHE B CE2 1 
ATOM   3348 C CZ  . PHE B 1 123 ? -17.258 13.337  33.249 1.00 21.21  ? 139 PHE B CZ  1 
ATOM   3349 N N   . SER B 1 124 ? -12.782 12.831  28.426 1.00 20.80  ? 140 SER B N   1 
ATOM   3350 C CA  . SER B 1 124 ? -12.406 14.045  27.720 1.00 20.71  ? 140 SER B CA  1 
ATOM   3351 C C   . SER B 1 124 ? -13.233 14.144  26.442 1.00 20.28  ? 140 SER B C   1 
ATOM   3352 O O   . SER B 1 124 ? -13.454 13.129  25.783 1.00 18.40  ? 140 SER B O   1 
ATOM   3353 C CB  . SER B 1 124 ? -10.912 14.039  27.436 1.00 20.86  ? 140 SER B CB  1 
ATOM   3354 O OG  . SER B 1 124 ? -10.164 13.974  28.654 1.00 19.78  ? 140 SER B OG  1 
ATOM   3355 N N   . VAL B 1 125 ? -13.740 15.348  26.130 1.00 20.83  ? 141 VAL B N   1 
ATOM   3356 C CA  . VAL B 1 125 ? -14.538 15.546  24.929 1.00 20.99  ? 141 VAL B CA  1 
ATOM   3357 C C   . VAL B 1 125 ? -13.918 16.605  24.021 1.00 21.05  ? 141 VAL B C   1 
ATOM   3358 O O   . VAL B 1 125 ? -13.248 17.535  24.478 1.00 20.87  ? 141 VAL B O   1 
ATOM   3359 C CB  . VAL B 1 125 ? -15.999 15.915  25.237 1.00 22.57  ? 141 VAL B CB  1 
ATOM   3360 C CG1 . VAL B 1 125 ? -16.734 14.729  25.852 1.00 23.12  ? 141 VAL B CG1 1 
ATOM   3361 C CG2 . VAL B 1 125 ? -16.118 17.155  26.110 1.00 25.13  ? 141 VAL B CG2 1 
ATOM   3362 N N   . LEU B 1 126 ? -14.179 16.413  22.723 1.00 22.58  ? 142 LEU B N   1 
ATOM   3363 C CA  . LEU B 1 126 ? -13.769 17.302  21.652 1.00 21.25  ? 142 LEU B CA  1 
ATOM   3364 C C   . LEU B 1 126 ? -14.938 17.497  20.684 1.00 21.24  ? 142 LEU B C   1 
ATOM   3365 O O   . LEU B 1 126 ? -15.517 16.547  20.145 1.00 21.98  ? 142 LEU B O   1 
ATOM   3366 C CB  . LEU B 1 126 ? -12.512 16.742  20.975 1.00 21.64  ? 142 LEU B CB  1 
ATOM   3367 C CG  . LEU B 1 126 ? -12.132 17.385  19.635 1.00 21.42  ? 142 LEU B CG  1 
ATOM   3368 C CD1 . LEU B 1 126 ? -11.481 18.736  19.846 1.00 21.37  ? 142 LEU B CD1 1 
ATOM   3369 C CD2 . LEU B 1 126 ? -11.219 16.460  18.836 1.00 22.51  ? 142 LEU B CD2 1 
ATOM   3370 N N   . MET B 1 127 ? -15.255 18.773  20.438 1.00 21.39  ? 143 MET B N   1 
ATOM   3371 C CA  . MET B 1 127 ? -16.340 19.150  19.552 1.00 23.38  ? 143 MET B CA  1 
ATOM   3372 C C   . MET B 1 127 ? -16.092 18.618  18.142 1.00 24.46  ? 143 MET B C   1 
ATOM   3373 O O   . MET B 1 127 ? -14.979 18.751  17.632 1.00 27.37  ? 143 MET B O   1 
ATOM   3374 C CB  . MET B 1 127 ? -16.434 20.672  19.510 1.00 25.04  ? 143 MET B CB  1 
ATOM   3375 C CG  . MET B 1 127 ? -17.403 21.176  18.463 1.00 27.59  ? 143 MET B CG  1 
ATOM   3376 S SD  . MET B 1 127 ? -17.772 22.906  18.753 1.00 31.62  ? 143 MET B SD  1 
ATOM   3377 C CE  . MET B 1 127 ? -18.760 22.822  20.237 1.00 29.74  ? 143 MET B CE  1 
ATOM   3378 N N   . ASP B 1 128 ? -17.113 17.985  17.544 1.00 24.63  ? 144 ASP B N   1 
ATOM   3379 C CA  . ASP B 1 128 ? -17.052 17.503  16.165 1.00 27.37  ? 144 ASP B CA  1 
ATOM   3380 C C   . ASP B 1 128 ? -17.489 18.616  15.211 1.00 30.82  ? 144 ASP B C   1 
ATOM   3381 O O   . ASP B 1 128 ? -18.663 18.949  15.132 1.00 32.63  ? 144 ASP B O   1 
ATOM   3382 C CB  . ASP B 1 128 ? -17.950 16.281  15.945 1.00 30.28  ? 144 ASP B CB  1 
ATOM   3383 C CG  . ASP B 1 128 ? -18.038 15.734  14.522 1.00 30.72  ? 144 ASP B CG  1 
ATOM   3384 O OD1 . ASP B 1 128 ? -17.162 16.050  13.661 1.00 34.20  ? 144 ASP B OD1 1 
ATOM   3385 O OD2 . ASP B 1 128 ? -18.966 14.962  14.285 1.00 28.36  ? 144 ASP B OD2 1 
ATOM   3386 N N   . GLU B 1 129 ? -16.534 19.181  14.463 1.00 37.61  ? 145 GLU B N   1 
ATOM   3387 C CA  . GLU B 1 129 ? -16.825 20.328  13.609 1.00 43.94  ? 145 GLU B CA  1 
ATOM   3388 C C   . GLU B 1 129 ? -17.553 19.871  12.336 1.00 36.73  ? 145 GLU B C   1 
ATOM   3389 O O   . GLU B 1 129 ? -18.185 20.680  11.674 1.00 36.55  ? 145 GLU B O   1 
ATOM   3390 C CB  . GLU B 1 129 ? -15.527 21.117  13.372 1.00 53.90  ? 145 GLU B CB  1 
ATOM   3391 C CG  . GLU B 1 129 ? -14.445 20.324  12.632 1.00 63.72  ? 145 GLU B CG  1 
ATOM   3392 C CD  . GLU B 1 129 ? -12.980 20.642  12.923 1.00 67.52  ? 145 GLU B CD  1 
ATOM   3393 O OE1 . GLU B 1 129 ? -12.705 21.581  13.732 1.00 68.00  ? 145 GLU B OE1 1 
ATOM   3394 O OE2 . GLU B 1 129 ? -12.104 19.931  12.337 1.00 57.36  ? 145 GLU B OE2 1 
ATOM   3395 N N   . TRP B 1 130 ? -17.541 18.563  12.031 1.00 33.70  ? 146 TRP B N   1 
ATOM   3396 C CA  . TRP B 1 130 ? -18.139 18.049  10.806 1.00 31.19  ? 146 TRP B CA  1 
ATOM   3397 C C   . TRP B 1 130 ? -19.621 17.721  10.949 1.00 29.17  ? 146 TRP B C   1 
ATOM   3398 O O   . TRP B 1 130 ? -20.295 17.578  9.949  1.00 29.83  ? 146 TRP B O   1 
ATOM   3399 C CB  . TRP B 1 130 ? -17.383 16.797  10.341 1.00 36.44  ? 146 TRP B CB  1 
ATOM   3400 C CG  . TRP B 1 130 ? -15.949 17.082  9.998  1.00 42.80  ? 146 TRP B CG  1 
ATOM   3401 C CD1 . TRP B 1 130 ? -14.858 16.897  10.795 1.00 43.13  ? 146 TRP B CD1 1 
ATOM   3402 C CD2 . TRP B 1 130 ? -15.468 17.637  8.753  1.00 43.85  ? 146 TRP B CD2 1 
ATOM   3403 N NE1 . TRP B 1 130 ? -13.733 17.309  10.140 1.00 46.47  ? 146 TRP B NE1 1 
ATOM   3404 C CE2 . TRP B 1 130 ? -14.069 17.765  8.888  1.00 47.41  ? 146 TRP B CE2 1 
ATOM   3405 C CE3 . TRP B 1 130 ? -16.074 18.026  7.552  1.00 41.52  ? 146 TRP B CE3 1 
ATOM   3406 C CZ2 . TRP B 1 130 ? -13.273 18.266  7.857  1.00 47.37  ? 146 TRP B CZ2 1 
ATOM   3407 C CZ3 . TRP B 1 130 ? -15.287 18.530  6.538  1.00 42.87  ? 146 TRP B CZ3 1 
ATOM   3408 C CH2 . TRP B 1 130 ? -13.905 18.656  6.694  1.00 46.28  ? 146 TRP B CH2 1 
ATOM   3409 N N   . HIS B 1 131 ? -20.110 17.462  12.165 1.00 30.82  ? 147 HIS B N   1 
ATOM   3410 C CA  . HIS B 1 131 ? -21.531 17.209  12.376 1.00 30.14  ? 147 HIS B CA  1 
ATOM   3411 C C   . HIS B 1 131 ? -21.925 17.861  13.704 1.00 30.62  ? 147 HIS B C   1 
ATOM   3412 O O   . HIS B 1 131 ? -21.921 17.205  14.752 1.00 31.00  ? 147 HIS B O   1 
ATOM   3413 C CB  . HIS B 1 131 ? -21.873 15.709  12.404 1.00 29.34  ? 147 HIS B CB  1 
ATOM   3414 C CG  . HIS B 1 131 ? -21.037 14.809  11.537 1.00 32.04  ? 147 HIS B CG  1 
ATOM   3415 N ND1 . HIS B 1 131 ? -19.799 14.302  11.901 1.00 26.44  ? 147 HIS B ND1 1 
ATOM   3416 C CD2 . HIS B 1 131 ? -21.334 14.273  10.352 1.00 30.20  ? 147 HIS B CD2 1 
ATOM   3417 C CE1 . HIS B 1 131 ? -19.369 13.497  10.959 1.00 31.37  ? 147 HIS B CE1 1 
ATOM   3418 N NE2 . HIS B 1 131 ? -20.281 13.483  9.992  1.00 33.06  ? 147 HIS B NE2 1 
ATOM   3419 N N   . LYS B 1 132 ? -22.247 19.156  13.635 1.00 28.66  ? 148 LYS B N   1 
ATOM   3420 C CA  . LYS B 1 132 ? -22.349 20.018  14.805 1.00 30.36  ? 148 LYS B CA  1 
ATOM   3421 C C   . LYS B 1 132 ? -23.573 19.676  15.649 1.00 27.23  ? 148 LYS B C   1 
ATOM   3422 O O   . LYS B 1 132 ? -24.667 19.501  15.107 1.00 23.98  ? 148 LYS B O   1 
ATOM   3423 C CB  . LYS B 1 132 ? -22.456 21.501  14.418 1.00 35.72  ? 148 LYS B CB  1 
ATOM   3424 C CG  . LYS B 1 132 ? -21.118 22.199  14.207 1.00 46.31  ? 148 LYS B CG  1 
ATOM   3425 C CD  . LYS B 1 132 ? -21.183 23.726  14.162 1.00 50.98  ? 148 LYS B CD  1 
ATOM   3426 C CE  . LYS B 1 132 ? -19.803 24.351  14.229 1.00 60.11  ? 148 LYS B CE  1 
ATOM   3427 N NZ  . LYS B 1 132 ? -19.821 25.811  13.952 1.00 65.38  ? 148 LYS B NZ  1 
ATOM   3428 N N   . LEU B 1 133 ? -23.365 19.641  16.981 1.00 24.82  ? 149 LEU B N   1 
ATOM   3429 C CA  . LEU B 1 133 ? -24.450 19.548  17.945 1.00 24.67  ? 149 LEU B CA  1 
ATOM   3430 C C   . LEU B 1 133 ? -25.298 20.810  17.867 1.00 26.54  ? 149 LEU B C   1 
ATOM   3431 O O   . LEU B 1 133 ? -24.780 21.925  17.755 1.00 27.00  ? 149 LEU B O   1 
ATOM   3432 C CB  . LEU B 1 133 ? -23.887 19.368  19.360 1.00 26.53  ? 149 LEU B CB  1 
ATOM   3433 C CG  . LEU B 1 133 ? -23.101 18.073  19.589 1.00 24.70  ? 149 LEU B CG  1 
ATOM   3434 C CD1 . LEU B 1 133 ? -22.301 18.133  20.877 1.00 28.02  ? 149 LEU B CD1 1 
ATOM   3435 C CD2 . LEU B 1 133 ? -24.037 16.907  19.617 1.00 27.58  ? 149 LEU B CD2 1 
ATOM   3436 N N   . ASP B 1 134 ? -26.618 20.601  17.913 1.00 25.31  ? 150 ASP B N   1 
ATOM   3437 C CA  . ASP B 1 134 ? -27.560 21.689  18.038 1.00 23.95  ? 150 ASP B CA  1 
ATOM   3438 C C   . ASP B 1 134 ? -27.848 21.940  19.514 1.00 25.60  ? 150 ASP B C   1 
ATOM   3439 O O   . ASP B 1 134 ? -28.569 21.174  20.157 1.00 22.87  ? 150 ASP B O   1 
ATOM   3440 C CB  . ASP B 1 134 ? -28.823 21.329  17.265 1.00 25.41  ? 150 ASP B CB  1 
ATOM   3441 C CG  . ASP B 1 134 ? -29.887 22.392  17.393 1.00 24.55  ? 150 ASP B CG  1 
ATOM   3442 O OD1 . ASP B 1 134 ? -29.526 23.514  17.782 1.00 25.18  ? 150 ASP B OD1 1 
ATOM   3443 O OD2 . ASP B 1 134 ? -31.057 22.058  17.149 1.00 24.06  ? 150 ASP B OD2 1 
ATOM   3444 N N   . MET B 1 135 ? -27.344 23.074  20.030 1.00 24.21  ? 151 MET B N   1 
ATOM   3445 C CA  . MET B 1 135 ? -27.474 23.424  21.439 1.00 24.00  ? 151 MET B CA  1 
ATOM   3446 C C   . MET B 1 135 ? -28.862 23.981  21.779 1.00 23.83  ? 151 MET B C   1 
ATOM   3447 O O   . MET B 1 135 ? -29.122 24.339  22.923 1.00 23.56  ? 151 MET B O   1 
ATOM   3448 C CB  . MET B 1 135 ? -26.401 24.452  21.802 1.00 25.97  ? 151 MET B CB  1 
ATOM   3449 C CG  . MET B 1 135 ? -24.992 23.973  21.528 1.00 25.79  ? 151 MET B CG  1 
ATOM   3450 S SD  . MET B 1 135 ? -24.680 22.342  22.275 1.00 25.79  ? 151 MET B SD  1 
ATOM   3451 C CE  . MET B 1 135 ? -22.919 22.148  21.981 1.00 24.35  ? 151 MET B CE  1 
ATOM   3452 N N   . ILE B 1 136 ? -29.764 24.022  20.794 1.00 21.61  ? 152 ILE B N   1 
ATOM   3453 C CA  . ILE B 1 136 ? -31.183 24.221  21.055 1.00 22.31  ? 152 ILE B CA  1 
ATOM   3454 C C   . ILE B 1 136 ? -31.721 23.061  21.906 1.00 20.43  ? 152 ILE B C   1 
ATOM   3455 O O   . ILE B 1 136 ? -32.627 23.267  22.700 1.00 21.38  ? 152 ILE B O   1 
ATOM   3456 C CB  . ILE B 1 136 ? -31.930 24.350  19.708 1.00 21.92  ? 152 ILE B CB  1 
ATOM   3457 C CG1 . ILE B 1 136 ? -31.571 25.631  18.931 1.00 22.36  ? 152 ILE B CG1 1 
ATOM   3458 C CG2 . ILE B 1 136 ? -33.428 24.194  19.885 1.00 21.91  ? 152 ILE B CG2 1 
ATOM   3459 C CD1 . ILE B 1 136 ? -31.900 26.916  19.631 1.00 21.72  ? 152 ILE B CD1 1 
ATOM   3460 N N   . HIS B 1 137 ? -31.168 21.856  21.718 1.00 20.91  ? 153 HIS B N   1 
ATOM   3461 C CA  . HIS B 1 137 ? -31.575 20.659  22.445 1.00 20.83  ? 153 HIS B CA  1 
ATOM   3462 C C   . HIS B 1 137 ? -30.609 20.266  23.576 1.00 22.92  ? 153 HIS B C   1 
ATOM   3463 O O   . HIS B 1 137 ? -29.419 20.608  23.568 1.00 22.32  ? 153 HIS B O   1 
ATOM   3464 C CB  . HIS B 1 137 ? -31.582 19.426  21.533 1.00 20.03  ? 153 HIS B CB  1 
ATOM   3465 C CG  . HIS B 1 137 ? -32.635 19.369  20.493 1.00 22.36  ? 153 HIS B CG  1 
ATOM   3466 N ND1 . HIS B 1 137 ? -33.700 18.499  20.594 1.00 21.92  ? 153 HIS B ND1 1 
ATOM   3467 C CD2 . HIS B 1 137 ? -32.794 20.023  19.326 1.00 25.32  ? 153 HIS B CD2 1 
ATOM   3468 C CE1 . HIS B 1 137 ? -34.474 18.644  19.521 1.00 25.37  ? 153 HIS B CE1 1 
ATOM   3469 N NE2 . HIS B 1 137 ? -33.960 19.578  18.744 1.00 23.40  ? 153 HIS B NE2 1 
ATOM   3470 N N   . GLU B 1 138 ? -31.131 19.438  24.499 1.00 22.28  ? 154 GLU B N   1 
ATOM   3471 C CA  . GLU B 1 138 ? -30.364 18.945  25.629 1.00 22.23  ? 154 GLU B CA  1 
ATOM   3472 C C   . GLU B 1 138 ? -29.667 17.653  25.214 1.00 23.22  ? 154 GLU B C   1 
ATOM   3473 O O   . GLU B 1 138 ? -30.265 16.778  24.586 1.00 20.60  ? 154 GLU B O   1 
ATOM   3474 C CB  . GLU B 1 138 ? -31.270 18.750  26.843 1.00 22.90  ? 154 GLU B CB  1 
ATOM   3475 C CG  . GLU B 1 138 ? -30.552 18.125  28.043 1.00 24.01  ? 154 GLU B CG  1 
ATOM   3476 C CD  . GLU B 1 138 ? -31.387 17.825  29.273 1.00 23.19  ? 154 GLU B CD  1 
ATOM   3477 O OE1 . GLU B 1 138 ? -32.474 18.378  29.396 1.00 19.52  ? 154 GLU B OE1 1 
ATOM   3478 O OE2 . GLU B 1 138 ? -30.942 17.005  30.093 1.00 25.83  ? 154 GLU B OE2 1 
ATOM   3479 N N   . HIS B 1 139 ? -28.389 17.538  25.574 1.00 20.85  ? 155 HIS B N   1 
ATOM   3480 C CA  . HIS B 1 139 ? -27.655 16.326  25.299 1.00 20.79  ? 155 HIS B CA  1 
ATOM   3481 C C   . HIS B 1 139 ? -27.069 15.814  26.609 1.00 21.77  ? 155 HIS B C   1 
ATOM   3482 O O   . HIS B 1 139 ? -26.289 16.518  27.248 1.00 23.91  ? 155 HIS B O   1 
ATOM   3483 C CB  . HIS B 1 139 ? -26.535 16.541  24.275 1.00 21.09  ? 155 HIS B CB  1 
ATOM   3484 C CG  . HIS B 1 139 ? -26.959 17.125  22.988 1.00 19.81  ? 155 HIS B CG  1 
ATOM   3485 N ND1 . HIS B 1 139 ? -27.307 18.455  22.883 1.00 21.27  ? 155 HIS B ND1 1 
ATOM   3486 C CD2 . HIS B 1 139 ? -27.069 16.596  21.760 1.00 19.77  ? 155 HIS B CD2 1 
ATOM   3487 C CE1 . HIS B 1 139 ? -27.642 18.688  21.613 1.00 21.75  ? 155 HIS B CE1 1 
ATOM   3488 N NE2 . HIS B 1 139 ? -27.510 17.583  20.926 1.00 20.27  ? 155 HIS B NE2 1 
ATOM   3489 N N   . GLN B 1 140 ? -27.417 14.575  26.974 1.00 21.98  ? 156 GLN B N   1 
ATOM   3490 C CA  . GLN B 1 140 ? -26.781 13.914  28.106 1.00 21.40  ? 156 GLN B CA  1 
ATOM   3491 C C   . GLN B 1 140 ? -25.636 13.075  27.551 1.00 21.24  ? 156 GLN B C   1 
ATOM   3492 O O   . GLN B 1 140 ? -25.868 12.169  26.759 1.00 20.76  ? 156 GLN B O   1 
ATOM   3493 C CB  . GLN B 1 140 ? -27.812 13.117  28.909 1.00 21.22  ? 156 GLN B CB  1 
ATOM   3494 C CG  . GLN B 1 140 ? -28.891 14.017  29.482 1.00 22.01  ? 156 GLN B CG  1 
ATOM   3495 C CD  . GLN B 1 140 ? -30.152 13.330  29.942 1.00 24.59  ? 156 GLN B CD  1 
ATOM   3496 O OE1 . GLN B 1 140 ? -30.180 12.131  30.233 1.00 24.69  ? 156 GLN B OE1 1 
ATOM   3497 N NE2 . GLN B 1 140 ? -31.216 14.113  30.034 1.00 23.18  ? 156 GLN B NE2 1 
ATOM   3498 N N   . LEU B 1 141 ? -24.405 13.375  27.989 1.00 19.87  ? 157 LEU B N   1 
ATOM   3499 C CA  . LEU B 1 141 ? -23.219 12.899  27.295 1.00 19.40  ? 157 LEU B CA  1 
ATOM   3500 C C   . LEU B 1 141 ? -22.602 11.720  28.043 1.00 20.64  ? 157 LEU B C   1 
ATOM   3501 O O   . LEU B 1 141 ? -22.254 10.708  27.446 1.00 22.11  ? 157 LEU B O   1 
ATOM   3502 C CB  . LEU B 1 141 ? -22.213 14.051  27.161 1.00 19.11  ? 157 LEU B CB  1 
ATOM   3503 C CG  . LEU B 1 141 ? -22.634 15.220  26.253 1.00 20.26  ? 157 LEU B CG  1 
ATOM   3504 C CD1 . LEU B 1 141 ? -21.483 16.215  26.082 1.00 20.67  ? 157 LEU B CD1 1 
ATOM   3505 C CD2 . LEU B 1 141 ? -23.105 14.749  24.890 1.00 21.19  ? 157 LEU B CD2 1 
ATOM   3506 N N   . VAL B 1 142 ? -22.380 11.907  29.340 1.00 23.29  ? 158 VAL B N   1 
ATOM   3507 C CA  . VAL B 1 142 ? -21.682 10.943  30.171 1.00 23.13  ? 158 VAL B CA  1 
ATOM   3508 C C   . VAL B 1 142 ? -22.506 10.880  31.449 1.00 24.51  ? 158 VAL B C   1 
ATOM   3509 O O   . VAL B 1 142 ? -22.981 11.919  31.898 1.00 26.40  ? 158 VAL B O   1 
ATOM   3510 C CB  . VAL B 1 142 ? -20.229 11.376  30.462 1.00 22.48  ? 158 VAL B CB  1 
ATOM   3511 C CG1 . VAL B 1 142 ? -19.493 10.413  31.378 1.00 21.61  ? 158 VAL B CG1 1 
ATOM   3512 C CG2 . VAL B 1 142 ? -19.424 11.565  29.197 1.00 22.58  ? 158 VAL B CG2 1 
ATOM   3513 N N   . PHE B 1 143 ? -22.698 9.680   32.006 1.00 21.81  ? 159 PHE B N   1 
ATOM   3514 C CA  . PHE B 1 143 ? -23.454 9.547   33.236 1.00 20.94  ? 159 PHE B CA  1 
ATOM   3515 C C   . PHE B 1 143 ? -23.290 8.123   33.782 1.00 25.72  ? 159 PHE B C   1 
ATOM   3516 O O   . PHE B 1 143 ? -22.844 7.233   33.056 1.00 23.04  ? 159 PHE B O   1 
ATOM   3517 C CB  . PHE B 1 143 ? -24.924 9.930   33.005 1.00 21.62  ? 159 PHE B CB  1 
ATOM   3518 C CG  . PHE B 1 143 ? -25.590 9.339   31.777 1.00 21.48  ? 159 PHE B CG  1 
ATOM   3519 C CD1 . PHE B 1 143 ? -26.077 8.033   31.781 1.00 23.87  ? 159 PHE B CD1 1 
ATOM   3520 C CD2 . PHE B 1 143 ? -25.715 10.084  30.607 1.00 22.00  ? 159 PHE B CD2 1 
ATOM   3521 C CE1 . PHE B 1 143 ? -26.671 7.493   30.647 1.00 23.23  ? 159 PHE B CE1 1 
ATOM   3522 C CE2 . PHE B 1 143 ? -26.296 9.540   29.471 1.00 22.31  ? 159 PHE B CE2 1 
ATOM   3523 C CZ  . PHE B 1 143 ? -26.777 8.243   29.497 1.00 22.39  ? 159 PHE B CZ  1 
ATOM   3524 N N   . VAL B 1 144 ? -23.543 7.952   35.096 1.00 25.77  ? 160 VAL B N   1 
ATOM   3525 C CA  . VAL B 1 144 ? -23.732 6.646   35.703 1.00 24.26  ? 160 VAL B CA  1 
ATOM   3526 C C   . VAL B 1 144 ? -25.214 6.488   36.024 1.00 23.91  ? 160 VAL B C   1 
ATOM   3527 O O   . VAL B 1 144 ? -25.791 7.336   36.687 1.00 22.09  ? 160 VAL B O   1 
ATOM   3528 C CB  . VAL B 1 144 ? -22.872 6.477   36.964 1.00 26.31  ? 160 VAL B CB  1 
ATOM   3529 C CG1 . VAL B 1 144 ? -23.305 5.268   37.797 1.00 24.71  ? 160 VAL B CG1 1 
ATOM   3530 C CG2 . VAL B 1 144 ? -21.397 6.413   36.589 1.00 27.68  ? 160 VAL B CG2 1 
ATOM   3531 N N   . GLU B 1 145 ? -25.810 5.398   35.530 1.00 23.86  ? 161 GLU B N   1 
ATOM   3532 C CA  . GLU B 1 145 ? -27.250 5.228   35.507 1.00 25.06  ? 161 GLU B CA  1 
ATOM   3533 C C   . GLU B 1 145 ? -27.668 4.011   36.324 1.00 25.56  ? 161 GLU B C   1 
ATOM   3534 O O   . GLU B 1 145 ? -27.471 2.886   35.864 1.00 24.54  ? 161 GLU B O   1 
ATOM   3535 C CB  . GLU B 1 145 ? -27.722 4.982   34.080 1.00 24.60  ? 161 GLU B CB  1 
ATOM   3536 C CG  . GLU B 1 145 ? -29.235 4.934   33.948 1.00 27.55  ? 161 GLU B CG  1 
ATOM   3537 C CD  . GLU B 1 145 ? -29.701 4.723   32.526 1.00 31.79  ? 161 GLU B CD  1 
ATOM   3538 O OE1 . GLU B 1 145 ? -29.051 5.252   31.640 1.00 38.51  ? 161 GLU B OE1 1 
ATOM   3539 O OE2 . GLU B 1 145 ? -30.717 4.067   32.327 1.00 38.04  ? 161 GLU B OE2 1 
ATOM   3540 N N   . PRO B 1 146 ? -28.200 4.197   37.557 1.00 27.24  ? 162 PRO B N   1 
ATOM   3541 C CA  . PRO B 1 146 ? -28.790 3.087   38.316 1.00 29.18  ? 162 PRO B CA  1 
ATOM   3542 C C   . PRO B 1 146 ? -29.996 2.500   37.576 1.00 31.31  ? 162 PRO B C   1 
ATOM   3543 O O   . PRO B 1 146 ? -30.373 3.024   36.521 1.00 30.82  ? 162 PRO B O   1 
ATOM   3544 C CB  . PRO B 1 146 ? -29.186 3.706   39.663 1.00 26.31  ? 162 PRO B CB  1 
ATOM   3545 C CG  . PRO B 1 146 ? -28.320 4.962   39.765 1.00 29.55  ? 162 PRO B CG  1 
ATOM   3546 C CD  . PRO B 1 146 ? -28.186 5.451   38.333 1.00 26.76  ? 162 PRO B CD  1 
ATOM   3547 N N   . SER B 1 147 ? -30.521 1.381   38.114 1.00 31.06  ? 163 SER B N   1 
ATOM   3548 C CA  . SER B 1 147 ? -31.709 0.671   37.625 1.00 33.48  ? 163 SER B CA  1 
ATOM   3549 C C   . SER B 1 147 ? -32.871 1.603   37.321 1.00 30.49  ? 163 SER B C   1 
ATOM   3550 O O   . SER B 1 147 ? -33.623 1.338   36.388 1.00 31.35  ? 163 SER B O   1 
ATOM   3551 C CB  . SER B 1 147 ? -32.217 -0.334  38.644 1.00 34.90  ? 163 SER B CB  1 
ATOM   3552 O OG  . SER B 1 147 ? -31.165 -1.161  39.065 1.00 46.81  ? 163 SER B OG  1 
ATOM   3553 N N   . ASP B 1 148 ? -33.054 2.630   38.162 1.00 27.98  ? 164 ASP B N   1 
ATOM   3554 C CA  . ASP B 1 148 ? -34.204 3.509   38.055 1.00 29.96  ? 164 ASP B CA  1 
ATOM   3555 C C   . ASP B 1 148 ? -34.073 4.544   36.928 1.00 29.98  ? 164 ASP B C   1 
ATOM   3556 O O   . ASP B 1 148 ? -34.987 5.337   36.745 1.00 29.89  ? 164 ASP B O   1 
ATOM   3557 C CB  . ASP B 1 148 ? -34.507 4.179   39.395 1.00 28.55  ? 164 ASP B CB  1 
ATOM   3558 C CG  . ASP B 1 148 ? -33.433 5.127   39.899 1.00 35.18  ? 164 ASP B CG  1 
ATOM   3559 O OD1 . ASP B 1 148 ? -32.417 5.327   39.174 1.00 35.35  ? 164 ASP B OD1 1 
ATOM   3560 O OD2 . ASP B 1 148 ? -33.608 5.649   41.024 1.00 38.08  ? 164 ASP B OD2 1 
ATOM   3561 N N   . GLY B 1 149 ? -32.954 4.588   36.196 1.00 30.07  ? 165 GLY B N   1 
ATOM   3562 C CA  . GLY B 1 149 ? -32.838 5.479   35.048 1.00 29.51  ? 165 GLY B CA  1 
ATOM   3563 C C   . GLY B 1 149 ? -32.377 6.898   35.410 1.00 28.81  ? 165 GLY B C   1 
ATOM   3564 O O   . GLY B 1 149 ? -32.165 7.716   34.518 1.00 26.50  ? 165 GLY B O   1 
ATOM   3565 N N   . SER B 1 150 ? -32.212 7.187   36.704 1.00 25.34  ? 166 SER B N   1 
ATOM   3566 C CA  . SER B 1 150 ? -31.586 8.417   37.172 1.00 25.16  ? 166 SER B CA  1 
ATOM   3567 C C   . SER B 1 150 ? -30.090 8.462   36.804 1.00 22.71  ? 166 SER B C   1 
ATOM   3568 O O   . SER B 1 150 ? -29.518 7.475   36.339 1.00 21.86  ? 166 SER B O   1 
ATOM   3569 C CB  . SER B 1 150 ? -31.796 8.542   38.689 1.00 25.30  ? 166 SER B CB  1 
ATOM   3570 O OG  . SER B 1 150 ? -30.907 7.651   39.389 1.00 24.80  ? 166 SER B OG  1 
ATOM   3571 N N   . HIS B 1 151 ? -29.441 9.620   37.024 1.00 24.04  ? 167 HIS B N   1 
ATOM   3572 C CA  . HIS B 1 151 ? -28.000 9.745   36.809 1.00 26.52  ? 167 HIS B CA  1 
ATOM   3573 C C   . HIS B 1 151 ? -27.301 10.215  38.094 1.00 24.63  ? 167 HIS B C   1 
ATOM   3574 O O   . HIS B 1 151 ? -27.634 11.256  38.638 1.00 26.12  ? 167 HIS B O   1 
ATOM   3575 C CB  . HIS B 1 151 ? -27.718 10.671  35.623 1.00 25.26  ? 167 HIS B CB  1 
ATOM   3576 C CG  . HIS B 1 151 ? -28.254 10.216  34.318 1.00 24.66  ? 167 HIS B CG  1 
ATOM   3577 N ND1 . HIS B 1 151 ? -28.327 11.091  33.254 1.00 25.56  ? 167 HIS B ND1 1 
ATOM   3578 C CD2 . HIS B 1 151 ? -28.683 9.038   33.862 1.00 25.19  ? 167 HIS B CD2 1 
ATOM   3579 C CE1 . HIS B 1 151 ? -28.785 10.431  32.192 1.00 24.05  ? 167 HIS B CE1 1 
ATOM   3580 N NE2 . HIS B 1 151 ? -29.034 9.197   32.540 1.00 24.30  ? 167 HIS B NE2 1 
ATOM   3581 N N   . VAL B 1 152 ? -26.308 9.457   38.575 1.00 23.49  ? 168 VAL B N   1 
ATOM   3582 C CA  . VAL B 1 152 ? -25.588 9.840   39.782 1.00 24.45  ? 168 VAL B CA  1 
ATOM   3583 C C   . VAL B 1 152 ? -24.894 11.193  39.558 1.00 22.74  ? 168 VAL B C   1 
ATOM   3584 O O   . VAL B 1 152 ? -24.862 12.039  40.448 1.00 21.89  ? 168 VAL B O   1 
ATOM   3585 C CB  . VAL B 1 152 ? -24.607 8.731   40.207 1.00 24.39  ? 168 VAL B CB  1 
ATOM   3586 C CG1 . VAL B 1 152 ? -23.755 9.126   41.403 1.00 26.07  ? 168 VAL B CG1 1 
ATOM   3587 C CG2 . VAL B 1 152 ? -25.364 7.440   40.498 1.00 26.03  ? 168 VAL B CG2 1 
ATOM   3588 N N   . PHE B 1 153 ? -24.360 11.366  38.348 1.00 22.96  ? 169 PHE B N   1 
ATOM   3589 C CA  . PHE B 1 153 ? -23.855 12.626  37.824 1.00 23.35  ? 169 PHE B CA  1 
ATOM   3590 C C   . PHE B 1 153 ? -23.984 12.551  36.300 1.00 23.91  ? 169 PHE B C   1 
ATOM   3591 O O   . PHE B 1 153 ? -24.116 11.461  35.723 1.00 23.11  ? 169 PHE B O   1 
ATOM   3592 C CB  . PHE B 1 153 ? -22.410 12.885  38.276 1.00 21.82  ? 169 PHE B CB  1 
ATOM   3593 C CG  . PHE B 1 153 ? -21.417 11.979  37.597 1.00 22.77  ? 169 PHE B CG  1 
ATOM   3594 C CD1 . PHE B 1 153 ? -20.947 12.272  36.313 1.00 21.85  ? 169 PHE B CD1 1 
ATOM   3595 C CD2 . PHE B 1 153 ? -21.064 10.766  38.178 1.00 21.17  ? 169 PHE B CD2 1 
ATOM   3596 C CE1 . PHE B 1 153 ? -20.081 11.402  35.666 1.00 22.47  ? 169 PHE B CE1 1 
ATOM   3597 C CE2 . PHE B 1 153 ? -20.223 9.893   37.513 1.00 21.75  ? 169 PHE B CE2 1 
ATOM   3598 C CZ  . PHE B 1 153 ? -19.729 10.214  36.266 1.00 22.06  ? 169 PHE B CZ  1 
ATOM   3599 N N   . THR B 1 154 ? -24.002 13.725  35.663 1.00 20.50  ? 170 THR B N   1 
ATOM   3600 C CA  . THR B 1 154 ? -24.175 13.835  34.235 1.00 21.18  ? 170 THR B CA  1 
ATOM   3601 C C   . THR B 1 154 ? -23.216 14.906  33.716 1.00 21.84  ? 170 THR B C   1 
ATOM   3602 O O   . THR B 1 154 ? -23.077 15.957  34.330 1.00 19.40  ? 170 THR B O   1 
ATOM   3603 C CB  . THR B 1 154 ? -25.609 14.280  33.889 1.00 23.63  ? 170 THR B CB  1 
ATOM   3604 O OG1 . THR B 1 154 ? -26.584 13.460  34.533 1.00 21.91  ? 170 THR B OG1 1 
ATOM   3605 C CG2 . THR B 1 154 ? -25.902 14.283  32.402 1.00 25.91  ? 170 THR B CG2 1 
ATOM   3606 N N   . LEU B 1 155 ? -22.578 14.641  32.581 1.00 21.35  ? 171 LEU B N   1 
ATOM   3607 C CA  . LEU B 1 155 ? -22.063 15.696  31.729 1.00 21.32  ? 171 LEU B CA  1 
ATOM   3608 C C   . LEU B 1 155 ? -23.151 15.987  30.705 1.00 21.30  ? 171 LEU B C   1 
ATOM   3609 O O   . LEU B 1 155 ? -23.514 15.088  29.962 1.00 20.28  ? 171 LEU B O   1 
ATOM   3610 C CB  . LEU B 1 155 ? -20.788 15.218  31.024 1.00 23.23  ? 171 LEU B CB  1 
ATOM   3611 C CG  . LEU B 1 155 ? -20.153 16.240  30.075 1.00 21.21  ? 171 LEU B CG  1 
ATOM   3612 C CD1 . LEU B 1 155 ? -19.477 17.313  30.866 1.00 20.48  ? 171 LEU B CD1 1 
ATOM   3613 C CD2 . LEU B 1 155 ? -19.150 15.613  29.109 1.00 21.31  ? 171 LEU B CD2 1 
ATOM   3614 N N   . GLN B 1 156 ? -23.600 17.246  30.651 1.00 21.69  ? 172 GLN B N   1 
ATOM   3615 C CA  . GLN B 1 156 ? -24.643 17.736  29.768 1.00 19.42  ? 172 GLN B CA  1 
ATOM   3616 C C   . GLN B 1 156 ? -24.110 18.897  28.921 1.00 21.59  ? 172 GLN B C   1 
ATOM   3617 O O   . GLN B 1 156 ? -23.226 19.628  29.356 1.00 22.71  ? 172 GLN B O   1 
ATOM   3618 C CB  . GLN B 1 156 ? -25.781 18.238  30.646 1.00 21.07  ? 172 GLN B CB  1 
ATOM   3619 C CG  . GLN B 1 156 ? -27.044 18.674  29.910 1.00 22.23  ? 172 GLN B CG  1 
ATOM   3620 C CD  . GLN B 1 156 ? -27.912 19.475  30.852 1.00 22.74  ? 172 GLN B CD  1 
ATOM   3621 O OE1 . GLN B 1 156 ? -27.555 20.582  31.236 1.00 22.70  ? 172 GLN B OE1 1 
ATOM   3622 N NE2 . GLN B 1 156 ? -29.042 18.921  31.252 1.00 26.07  ? 172 GLN B NE2 1 
ATOM   3623 N N   . VAL B 1 157 ? -24.635 19.047  27.697 1.00 21.11  ? 173 VAL B N   1 
ATOM   3624 C CA  . VAL B 1 157 ? -24.438 20.244  26.896 1.00 21.03  ? 173 VAL B CA  1 
ATOM   3625 C C   . VAL B 1 157 ? -25.732 20.515  26.123 1.00 22.19  ? 173 VAL B C   1 
ATOM   3626 O O   . VAL B 1 157 ? -26.511 19.592  25.853 1.00 20.65  ? 173 VAL B O   1 
ATOM   3627 C CB  . VAL B 1 157 ? -23.200 20.131  25.983 1.00 20.94  ? 173 VAL B CB  1 
ATOM   3628 C CG1 . VAL B 1 157 ? -23.401 19.193  24.804 1.00 20.10  ? 173 VAL B CG1 1 
ATOM   3629 C CG2 . VAL B 1 157 ? -22.733 21.513  25.480 1.00 23.95  ? 173 VAL B CG2 1 
ATOM   3630 N N   . GLY B 1 158 ? -25.970 21.800  25.826 1.00 21.74  ? 174 GLY B N   1 
ATOM   3631 C CA  . GLY B 1 158 ? -27.184 22.251  25.160 1.00 21.71  ? 174 GLY B CA  1 
ATOM   3632 C C   . GLY B 1 158 ? -28.249 22.772  26.126 1.00 22.04  ? 174 GLY B C   1 
ATOM   3633 O O   . GLY B 1 158 ? -28.156 22.589  27.327 1.00 23.11  ? 174 GLY B O   1 
ATOM   3634 N N   . SER B 1 159 ? -29.289 23.414  25.576 1.00 24.47  ? 175 SER B N   1 
ATOM   3635 C CA  . SER B 1 159 ? -30.407 23.925  26.356 1.00 24.79  ? 175 SER B CA  1 
ATOM   3636 C C   . SER B 1 159 ? -31.154 22.794  27.057 1.00 24.97  ? 175 SER B C   1 
ATOM   3637 O O   . SER B 1 159 ? -31.744 21.956  26.390 1.00 24.77  ? 175 SER B O   1 
ATOM   3638 C CB  . SER B 1 159 ? -31.353 24.695  25.458 1.00 23.67  ? 175 SER B CB  1 
ATOM   3639 O OG  . SER B 1 159 ? -30.667 25.750  24.782 1.00 22.68  ? 175 SER B OG  1 
ATOM   3640 N N   . PRO B 1 160 ? -31.223 22.763  28.409 1.00 25.61  ? 176 PRO B N   1 
ATOM   3641 C CA  . PRO B 1 160 ? -32.140 21.863  29.112 1.00 24.32  ? 176 PRO B CA  1 
ATOM   3642 C C   . PRO B 1 160 ? -33.576 21.852  28.570 1.00 27.75  ? 176 PRO B C   1 
ATOM   3643 O O   . PRO B 1 160 ? -34.198 22.903  28.363 1.00 26.95  ? 176 PRO B O   1 
ATOM   3644 C CB  . PRO B 1 160 ? -32.119 22.420  30.542 1.00 23.94  ? 176 PRO B CB  1 
ATOM   3645 C CG  . PRO B 1 160 ? -30.716 22.934  30.690 1.00 23.85  ? 176 PRO B CG  1 
ATOM   3646 C CD  . PRO B 1 160 ? -30.421 23.571  29.340 1.00 25.10  ? 176 PRO B CD  1 
ATOM   3647 N N   . PHE B 1 161 ? -34.085 20.640  28.344 1.00 26.45  ? 177 PHE B N   1 
ATOM   3648 C CA  . PHE B 1 161 ? -35.454 20.431  27.912 1.00 25.95  ? 177 PHE B CA  1 
ATOM   3649 C C   . PHE B 1 161 ? -36.400 21.027  28.938 1.00 28.00  ? 177 PHE B C   1 
ATOM   3650 O O   . PHE B 1 161 ? -36.232 20.790  30.120 1.00 30.99  ? 177 PHE B O   1 
ATOM   3651 C CB  . PHE B 1 161 ? -35.776 18.936  27.800 1.00 25.72  ? 177 PHE B CB  1 
ATOM   3652 C CG  . PHE B 1 161 ? -37.246 18.651  27.599 1.00 25.19  ? 177 PHE B CG  1 
ATOM   3653 C CD1 . PHE B 1 161 ? -37.795 18.697  26.327 1.00 25.08  ? 177 PHE B CD1 1 
ATOM   3654 C CD2 . PHE B 1 161 ? -38.083 18.411  28.678 1.00 24.78  ? 177 PHE B CD2 1 
ATOM   3655 C CE1 . PHE B 1 161 ? -39.144 18.451  26.133 1.00 24.22  ? 177 PHE B CE1 1 
ATOM   3656 C CE2 . PHE B 1 161 ? -39.440 18.200  28.494 1.00 25.68  ? 177 PHE B CE2 1 
ATOM   3657 C CZ  . PHE B 1 161 ? -39.970 18.226  27.215 1.00 26.26  ? 177 PHE B CZ  1 
ATOM   3658 N N   . THR B 1 162 ? -37.411 21.780  28.493 1.00 30.80  ? 178 THR B N   1 
ATOM   3659 C CA  . THR B 1 162 ? -38.492 22.173  29.389 1.00 29.97  ? 178 THR B CA  1 
ATOM   3660 C C   . THR B 1 162 ? -39.819 22.058  28.650 1.00 30.74  ? 178 THR B C   1 
ATOM   3661 O O   . THR B 1 162 ? -39.895 22.260  27.426 1.00 27.58  ? 178 THR B O   1 
ATOM   3662 C CB  . THR B 1 162 ? -38.393 23.602  29.948 1.00 31.41  ? 178 THR B CB  1 
ATOM   3663 O OG1 . THR B 1 162 ? -38.560 24.574  28.906 1.00 30.90  ? 178 THR B OG1 1 
ATOM   3664 C CG2 . THR B 1 162 ? -37.097 23.844  30.696 1.00 31.63  ? 178 THR B CG2 1 
ATOM   3665 N N   . ASN B 1 163 ? -40.838 21.749  29.447 1.00 28.36  ? 179 ASN B N   1 
ATOM   3666 C CA  . ASN B 1 163 ? -42.216 21.763  29.005 1.00 33.10  ? 179 ASN B CA  1 
ATOM   3667 C C   . ASN B 1 163 ? -42.995 22.721  29.893 1.00 31.72  ? 179 ASN B C   1 
ATOM   3668 O O   . ASN B 1 163 ? -43.123 22.459  31.080 1.00 29.34  ? 179 ASN B O   1 
ATOM   3669 C CB  . ASN B 1 163 ? -42.851 20.380  29.084 1.00 30.85  ? 179 ASN B CB  1 
ATOM   3670 C CG  . ASN B 1 163 ? -44.293 20.399  28.625 1.00 30.98  ? 179 ASN B CG  1 
ATOM   3671 O OD1 . ASN B 1 163 ? -44.637 21.155  27.725 1.00 31.74  ? 179 ASN B OD1 1 
ATOM   3672 N ND2 . ASN B 1 163 ? -45.152 19.626  29.269 1.00 30.06  ? 179 ASN B ND2 1 
ATOM   3673 N N   . PRO B 1 164 ? -43.584 23.822  29.377 1.00 33.21  ? 180 PRO B N   1 
ATOM   3674 C CA  . PRO B 1 164 ? -43.460 24.232  27.978 1.00 33.48  ? 180 PRO B CA  1 
ATOM   3675 C C   . PRO B 1 164 ? -42.081 24.728  27.549 1.00 31.66  ? 180 PRO B C   1 
ATOM   3676 O O   . PRO B 1 164 ? -41.227 25.034  28.375 1.00 34.52  ? 180 PRO B O   1 
ATOM   3677 C CB  . PRO B 1 164 ? -44.483 25.391  27.870 1.00 34.51  ? 180 PRO B CB  1 
ATOM   3678 C CG  . PRO B 1 164 ? -44.633 25.925  29.284 1.00 34.13  ? 180 PRO B CG  1 
ATOM   3679 C CD  . PRO B 1 164 ? -44.509 24.687  30.136 1.00 32.47  ? 180 PRO B CD  1 
ATOM   3680 N N   . THR B 1 165 ? -41.898 24.852  26.243 1.00 29.23  ? 181 THR B N   1 
ATOM   3681 C CA  . THR B 1 165 ? -40.674 25.389  25.691 1.00 33.75  ? 181 THR B CA  1 
ATOM   3682 C C   . THR B 1 165 ? -40.456 26.800  26.238 1.00 35.07  ? 181 THR B C   1 
ATOM   3683 O O   . THR B 1 165 ? -41.412 27.556  26.389 1.00 29.58  ? 181 THR B O   1 
ATOM   3684 C CB  . THR B 1 165 ? -40.734 25.346  24.163 1.00 31.27  ? 181 THR B CB  1 
ATOM   3685 O OG1 . THR B 1 165 ? -41.146 24.018  23.826 1.00 30.74  ? 181 THR B OG1 1 
ATOM   3686 C CG2 . THR B 1 165 ? -39.415 25.705  23.511 1.00 30.69  ? 181 THR B CG2 1 
ATOM   3687 N N   . GLY B 1 166 ? -39.199 27.136  26.565 1.00 31.28  ? 182 GLY B N   1 
ATOM   3688 C CA  . GLY B 1 166 ? -38.853 28.484  26.995 1.00 31.65  ? 182 GLY B CA  1 
ATOM   3689 C C   . GLY B 1 166 ? -37.979 29.169  25.957 1.00 32.33  ? 182 GLY B C   1 
ATOM   3690 O O   . GLY B 1 166 ? -37.783 28.640  24.865 1.00 36.51  ? 182 GLY B O   1 
ATOM   3691 N N   . PRO B 1 167 ? -37.388 30.340  26.263 1.00 34.22  ? 183 PRO B N   1 
ATOM   3692 C CA  . PRO B 1 167 ? -36.493 30.992  25.312 1.00 34.94  ? 183 PRO B CA  1 
ATOM   3693 C C   . PRO B 1 167 ? -35.317 30.076  24.971 1.00 35.73  ? 183 PRO B C   1 
ATOM   3694 O O   . PRO B 1 167 ? -34.718 29.482  25.876 1.00 38.25  ? 183 PRO B O   1 
ATOM   3695 C CB  . PRO B 1 167 ? -36.021 32.255  26.064 1.00 37.13  ? 183 PRO B CB  1 
ATOM   3696 C CG  . PRO B 1 167 ? -37.089 32.478  27.121 1.00 36.57  ? 183 PRO B CG  1 
ATOM   3697 C CD  . PRO B 1 167 ? -37.534 31.085  27.526 1.00 33.92  ? 183 PRO B CD  1 
ATOM   3698 N N   . LEU B 1 168 ? -35.003 29.966  23.675 1.00 27.49  ? 184 LEU B N   1 
ATOM   3699 C CA  . LEU B 1 168 ? -33.939 29.084  23.219 1.00 30.28  ? 184 LEU B CA  1 
ATOM   3700 C C   . LEU B 1 168 ? -33.068 29.827  22.219 1.00 32.23  ? 184 LEU B C   1 
ATOM   3701 O O   . LEU B 1 168 ? -33.594 30.536  21.370 1.00 35.58  ? 184 LEU B O   1 
ATOM   3702 C CB  . LEU B 1 168 ? -34.536 27.828  22.567 1.00 28.13  ? 184 LEU B CB  1 
ATOM   3703 C CG  . LEU B 1 168 ? -35.178 26.799  23.510 1.00 25.72  ? 184 LEU B CG  1 
ATOM   3704 C CD1 . LEU B 1 168 ? -35.986 25.782  22.716 1.00 25.89  ? 184 LEU B CD1 1 
ATOM   3705 C CD2 . LEU B 1 168 ? -34.147 26.071  24.359 1.00 23.35  ? 184 LEU B CD2 1 
ATOM   3706 N N   . PRO B 1 169 ? -31.730 29.632  22.221 1.00 31.39  ? 185 PRO B N   1 
ATOM   3707 C CA  . PRO B 1 169 ? -31.063 28.732  23.165 1.00 28.32  ? 185 PRO B CA  1 
ATOM   3708 C C   . PRO B 1 169 ? -31.027 29.325  24.560 1.00 31.44  ? 185 PRO B C   1 
ATOM   3709 O O   . PRO B 1 169 ? -31.045 30.539  24.715 1.00 33.65  ? 185 PRO B O   1 
ATOM   3710 C CB  . PRO B 1 169 ? -29.644 28.647  22.603 1.00 29.09  ? 185 PRO B CB  1 
ATOM   3711 C CG  . PRO B 1 169 ? -29.442 30.024  21.962 1.00 31.68  ? 185 PRO B CG  1 
ATOM   3712 C CD  . PRO B 1 169 ? -30.783 30.294  21.305 1.00 32.52  ? 185 PRO B CD  1 
ATOM   3713 N N   . ALA B 1 170 ? -30.974 28.464  25.574 1.00 32.12  ? 186 ALA B N   1 
ATOM   3714 C CA  . ALA B 1 170 ? -30.796 28.906  26.947 1.00 29.70  ? 186 ALA B CA  1 
ATOM   3715 C C   . ALA B 1 170 ? -29.463 29.641  27.085 1.00 30.57  ? 186 ALA B C   1 
ATOM   3716 O O   . ALA B 1 170 ? -28.547 29.443  26.294 1.00 25.65  ? 186 ALA B O   1 
ATOM   3717 C CB  . ALA B 1 170 ? -30.838 27.722  27.887 1.00 29.81  ? 186 ALA B CB  1 
ATOM   3718 N N   . PRO B 1 171 ? -29.299 30.509  28.107 1.00 30.11  ? 187 PRO B N   1 
ATOM   3719 C CA  . PRO B 1 171 ? -27.991 31.097  28.389 1.00 30.41  ? 187 PRO B CA  1 
ATOM   3720 C C   . PRO B 1 171 ? -26.955 29.997  28.591 1.00 27.98  ? 187 PRO B C   1 
ATOM   3721 O O   . PRO B 1 171 ? -27.216 29.062  29.337 1.00 30.74  ? 187 PRO B O   1 
ATOM   3722 C CB  . PRO B 1 171 ? -28.206 31.839  29.723 1.00 31.46  ? 187 PRO B CB  1 
ATOM   3723 C CG  . PRO B 1 171 ? -29.704 32.133  29.768 1.00 32.41  ? 187 PRO B CG  1 
ATOM   3724 C CD  . PRO B 1 171 ? -30.356 30.988  29.014 1.00 31.97  ? 187 PRO B CD  1 
ATOM   3725 N N   . ARG B 1 172 ? -25.786 30.119  27.958 1.00 26.56  ? 188 ARG B N   1 
ATOM   3726 C CA  . ARG B 1 172 ? -24.690 29.187  28.191 1.00 27.69  ? 188 ARG B CA  1 
ATOM   3727 C C   . ARG B 1 172 ? -25.088 27.784  27.716 1.00 27.14  ? 188 ARG B C   1 
ATOM   3728 O O   . ARG B 1 172 ? -24.552 26.782  28.199 1.00 24.32  ? 188 ARG B O   1 
ATOM   3729 C CB  . ARG B 1 172 ? -24.321 29.166  29.680 1.00 30.38  ? 188 ARG B CB  1 
ATOM   3730 C CG  . ARG B 1 172 ? -23.568 30.387  30.197 1.00 32.02  ? 188 ARG B CG  1 
ATOM   3731 C CD  . ARG B 1 172 ? -23.292 30.279  31.691 1.00 37.61  ? 188 ARG B CD  1 
ATOM   3732 N NE  . ARG B 1 172 ? -22.507 31.434  32.120 1.00 49.85  ? 188 ARG B NE  1 
ATOM   3733 C CZ  . ARG B 1 172 ? -21.792 31.534  33.247 1.00 50.87  ? 188 ARG B CZ  1 
ATOM   3734 N NH1 . ARG B 1 172 ? -21.829 30.588  34.170 1.00 49.76  ? 188 ARG B NH1 1 
ATOM   3735 N NH2 . ARG B 1 172 ? -21.045 32.606  33.455 1.00 49.97  ? 188 ARG B NH2 1 
ATOM   3736 N N   . ALA B 1 173 ? -25.967 27.723  26.705 1.00 26.53  ? 189 ALA B N   1 
ATOM   3737 C CA  . ALA B 1 173 ? -26.355 26.473  26.079 1.00 25.74  ? 189 ALA B CA  1 
ATOM   3738 C C   . ALA B 1 173 ? -25.116 25.697  25.648 1.00 25.12  ? 189 ALA B C   1 
ATOM   3739 O O   . ALA B 1 173 ? -25.084 24.478  25.766 1.00 25.16  ? 189 ALA B O   1 
ATOM   3740 C CB  . ALA B 1 173 ? -27.263 26.731  24.899 1.00 27.66  ? 189 ALA B CB  1 
ATOM   3741 N N   . ASP B 1 174 ? -24.108 26.404  25.133 1.00 21.66  ? 190 ASP B N   1 
ATOM   3742 C CA  . ASP B 1 174 ? -22.942 25.740  24.595 1.00 24.67  ? 190 ASP B CA  1 
ATOM   3743 C C   . ASP B 1 174 ? -21.858 25.588  25.652 1.00 23.80  ? 190 ASP B C   1 
ATOM   3744 O O   . ASP B 1 174 ? -20.720 25.313  25.295 1.00 24.05  ? 190 ASP B O   1 
ATOM   3745 C CB  . ASP B 1 174 ? -22.433 26.428  23.332 1.00 28.30  ? 190 ASP B CB  1 
ATOM   3746 C CG  . ASP B 1 174 ? -21.985 27.849  23.543 1.00 28.05  ? 190 ASP B CG  1 
ATOM   3747 O OD1 . ASP B 1 174 ? -22.175 28.362  24.657 1.00 31.20  ? 190 ASP B OD1 1 
ATOM   3748 O OD2 . ASP B 1 174 ? -21.443 28.406  22.592 1.00 34.45  ? 190 ASP B OD2 1 
ATOM   3749 N N   . TRP B 1 175 ? -22.241 25.634  26.936 1.00 23.60  ? 191 TRP B N   1 
ATOM   3750 C CA  . TRP B 1 175 ? -21.343 25.246  28.018 1.00 24.10  ? 191 TRP B CA  1 
ATOM   3751 C C   . TRP B 1 175 ? -21.577 23.801  28.443 1.00 23.26  ? 191 TRP B C   1 
ATOM   3752 O O   . TRP B 1 175 ? -22.714 23.382  28.636 1.00 22.80  ? 191 TRP B O   1 
ATOM   3753 C CB  . TRP B 1 175 ? -21.505 26.177  29.215 1.00 24.48  ? 191 TRP B CB  1 
ATOM   3754 C CG  . TRP B 1 175 ? -20.972 27.572  28.978 1.00 27.00  ? 191 TRP B CG  1 
ATOM   3755 C CD1 . TRP B 1 175 ? -21.039 28.313  27.838 1.00 27.92  ? 191 TRP B CD1 1 
ATOM   3756 C CD2 . TRP B 1 175 ? -20.297 28.398  29.947 1.00 27.79  ? 191 TRP B CD2 1 
ATOM   3757 N NE1 . TRP B 1 175 ? -20.432 29.527  28.023 1.00 28.35  ? 191 TRP B NE1 1 
ATOM   3758 C CE2 . TRP B 1 175 ? -19.976 29.613  29.307 1.00 29.97  ? 191 TRP B CE2 1 
ATOM   3759 C CE3 . TRP B 1 175 ? -19.934 28.226  31.284 1.00 29.17  ? 191 TRP B CE3 1 
ATOM   3760 C CZ2 . TRP B 1 175 ? -19.294 30.642  29.958 1.00 31.12  ? 191 TRP B CZ2 1 
ATOM   3761 C CZ3 . TRP B 1 175 ? -19.252 29.240  31.927 1.00 29.76  ? 191 TRP B CZ3 1 
ATOM   3762 C CH2 . TRP B 1 175 ? -18.951 30.435  31.274 1.00 30.75  ? 191 TRP B CH2 1 
ATOM   3763 N N   . LEU B 1 176 ? -20.463 23.068  28.596 1.00 23.19  ? 192 LEU B N   1 
ATOM   3764 C CA  . LEU B 1 176 ? -20.439 21.757  29.225 1.00 22.17  ? 192 LEU B CA  1 
ATOM   3765 C C   . LEU B 1 176 ? -20.737 21.966  30.704 1.00 23.87  ? 192 LEU B C   1 
ATOM   3766 O O   . LEU B 1 176 ? -20.210 22.916  31.295 1.00 22.91  ? 192 LEU B O   1 
ATOM   3767 C CB  . LEU B 1 176 ? -19.058 21.099  29.063 1.00 21.70  ? 192 LEU B CB  1 
ATOM   3768 C CG  . LEU B 1 176 ? -18.564 20.864  27.639 1.00 23.42  ? 192 LEU B CG  1 
ATOM   3769 C CD1 . LEU B 1 176 ? -17.047 20.655  27.604 1.00 23.86  ? 192 LEU B CD1 1 
ATOM   3770 C CD2 . LEU B 1 176 ? -19.259 19.671  27.024 1.00 24.84  ? 192 LEU B CD2 1 
ATOM   3771 N N   . LYS B 1 177 ? -21.594 21.089  31.258 1.00 20.95  ? 193 LYS B N   1 
ATOM   3772 C CA  . LYS B 1 177 ? -22.082 21.222  32.616 1.00 22.17  ? 193 LYS B CA  1 
ATOM   3773 C C   . LYS B 1 177 ? -21.975 19.863  33.288 1.00 21.42  ? 193 LYS B C   1 
ATOM   3774 O O   . LYS B 1 177 ? -22.323 18.861  32.679 1.00 21.64  ? 193 LYS B O   1 
ATOM   3775 C CB  . LYS B 1 177 ? -23.527 21.730  32.601 1.00 22.33  ? 193 LYS B CB  1 
ATOM   3776 C CG  . LYS B 1 177 ? -23.775 22.923  31.678 1.00 22.57  ? 193 LYS B CG  1 
ATOM   3777 C CD  . LYS B 1 177 ? -25.087 23.640  31.961 1.00 21.56  ? 193 LYS B CD  1 
ATOM   3778 C CE  . LYS B 1 177 ? -25.380 24.799  31.029 1.00 20.26  ? 193 LYS B CE  1 
ATOM   3779 N NZ  . LYS B 1 177 ? -25.187 24.431  29.603 1.00 20.22  ? 193 LYS B NZ  1 
ATOM   3780 N N   . ILE B 1 178 ? -21.428 19.836  34.509 1.00 21.50  ? 194 ILE B N   1 
ATOM   3781 C CA  . ILE B 1 178 ? -21.525 18.658  35.347 1.00 21.41  ? 194 ILE B CA  1 
ATOM   3782 C C   . ILE B 1 178 ? -22.672 18.856  36.323 1.00 23.07  ? 194 ILE B C   1 
ATOM   3783 O O   . ILE B 1 178 ? -22.702 19.860  37.038 1.00 21.92  ? 194 ILE B O   1 
ATOM   3784 C CB  . ILE B 1 178 ? -20.216 18.350  36.086 1.00 21.73  ? 194 ILE B CB  1 
ATOM   3785 C CG1 . ILE B 1 178 ? -19.061 18.059  35.119 1.00 22.00  ? 194 ILE B CG1 1 
ATOM   3786 C CG2 . ILE B 1 178 ? -20.469 17.201  37.039 1.00 22.45  ? 194 ILE B CG2 1 
ATOM   3787 C CD1 . ILE B 1 178 ? -19.178 16.736  34.375 1.00 22.32  ? 194 ILE B CD1 1 
ATOM   3788 N N   . LEU B 1 179 ? -23.586 17.869  36.353 1.00 24.01  ? 195 LEU B N   1 
ATOM   3789 C CA  . LEU B 1 179 ? -24.751 17.901  37.228 1.00 23.63  ? 195 LEU B CA  1 
ATOM   3790 C C   . LEU B 1 179 ? -24.644 16.822  38.294 1.00 24.43  ? 195 LEU B C   1 
ATOM   3791 O O   . LEU B 1 179 ? -24.127 15.741  38.046 1.00 24.35  ? 195 LEU B O   1 
ATOM   3792 C CB  . LEU B 1 179 ? -26.031 17.640  36.422 1.00 25.15  ? 195 LEU B CB  1 
ATOM   3793 C CG  . LEU B 1 179 ? -26.178 18.400  35.114 1.00 24.72  ? 195 LEU B CG  1 
ATOM   3794 C CD1 . LEU B 1 179 ? -27.512 18.096  34.462 1.00 24.56  ? 195 LEU B CD1 1 
ATOM   3795 C CD2 . LEU B 1 179 ? -26.052 19.883  35.344 1.00 27.83  ? 195 LEU B CD2 1 
ATOM   3796 N N   . ASN B 1 180 ? -25.253 17.072  39.453 1.00 23.26  ? 196 ASN B N   1 
ATOM   3797 C CA  . ASN B 1 180 ? -25.377 16.033  40.454 1.00 25.45  ? 196 ASN B CA  1 
ATOM   3798 C C   . ASN B 1 180 ? -26.669 15.265  40.158 1.00 23.42  ? 196 ASN B C   1 
ATOM   3799 O O   . ASN B 1 180 ? -27.337 15.506  39.156 1.00 24.24  ? 196 ASN B O   1 
ATOM   3800 C CB  . ASN B 1 180 ? -25.254 16.609  41.865 1.00 24.91  ? 196 ASN B CB  1 
ATOM   3801 C CG  . ASN B 1 180 ? -26.458 17.430  42.261 1.00 27.85  ? 196 ASN B CG  1 
ATOM   3802 O OD1 . ASN B 1 180 ? -27.487 17.392  41.587 1.00 25.35  ? 196 ASN B OD1 1 
ATOM   3803 N ND2 . ASN B 1 180 ? -26.351 18.143  43.370 1.00 29.79  ? 196 ASN B ND2 1 
ATOM   3804 N N   . HIS B 1 181 ? -27.012 14.317  41.017 1.00 23.34  ? 197 HIS B N   1 
ATOM   3805 C CA  . HIS B 1 181 ? -28.129 13.416  40.751 1.00 25.24  ? 197 HIS B CA  1 
ATOM   3806 C C   . HIS B 1 181 ? -29.467 14.161  40.778 1.00 26.44  ? 197 HIS B C   1 
ATOM   3807 O O   . HIS B 1 181 ? -30.445 13.675  40.201 1.00 28.12  ? 197 HIS B O   1 
ATOM   3808 C CB  . HIS B 1 181 ? -28.081 12.256  41.743 1.00 23.69  ? 197 HIS B CB  1 
ATOM   3809 C CG  . HIS B 1 181 ? -29.234 11.312  41.707 1.00 27.12  ? 197 HIS B CG  1 
ATOM   3810 N ND1 . HIS B 1 181 ? -30.397 11.556  42.399 1.00 28.86  ? 197 HIS B ND1 1 
ATOM   3811 C CD2 . HIS B 1 181 ? -29.390 10.105  41.155 1.00 26.12  ? 197 HIS B CD2 1 
ATOM   3812 C CE1 . HIS B 1 181 ? -31.218 10.518  42.249 1.00 27.24  ? 197 HIS B CE1 1 
ATOM   3813 N NE2 . HIS B 1 181 ? -30.640 9.635   41.492 1.00 25.42  ? 197 HIS B NE2 1 
ATOM   3814 N N   . ASN B 1 182 ? -29.497 15.314  41.470 1.00 28.01  ? 198 ASN B N   1 
ATOM   3815 C CA  . ASN B 1 182 ? -30.677 16.165  41.580 1.00 28.38  ? 198 ASN B CA  1 
ATOM   3816 C C   . ASN B 1 182 ? -30.707 17.237  40.483 1.00 27.47  ? 198 ASN B C   1 
ATOM   3817 O O   . ASN B 1 182 ? -31.580 18.107  40.498 1.00 27.41  ? 198 ASN B O   1 
ATOM   3818 C CB  . ASN B 1 182 ? -30.735 16.769  42.986 1.00 31.14  ? 198 ASN B CB  1 
ATOM   3819 C CG  . ASN B 1 182 ? -32.027 17.498  43.300 1.00 34.34  ? 198 ASN B CG  1 
ATOM   3820 O OD1 . ASN B 1 182 ? -33.105 16.922  43.203 1.00 35.76  ? 198 ASN B OD1 1 
ATOM   3821 N ND2 . ASN B 1 182 ? -31.929 18.773  43.646 1.00 35.03  ? 198 ASN B ND2 1 
ATOM   3822 N N   . LEU B 1 183 ? -29.771 17.157  39.522 1.00 28.05  ? 199 LEU B N   1 
ATOM   3823 C CA  . LEU B 1 183 ? -29.682 18.023  38.344 1.00 28.34  ? 199 LEU B CA  1 
ATOM   3824 C C   . LEU B 1 183 ? -29.185 19.434  38.679 1.00 28.85  ? 199 LEU B C   1 
ATOM   3825 O O   . LEU B 1 183 ? -29.215 20.316  37.818 1.00 24.93  ? 199 LEU B O   1 
ATOM   3826 C CB  . LEU B 1 183 ? -31.031 18.058  37.611 1.00 29.18  ? 199 LEU B CB  1 
ATOM   3827 C CG  . LEU B 1 183 ? -31.580 16.674  37.264 1.00 31.09  ? 199 LEU B CG  1 
ATOM   3828 C CD1 . LEU B 1 183 ? -32.874 16.772  36.468 1.00 32.77  ? 199 LEU B CD1 1 
ATOM   3829 C CD2 . LEU B 1 183 ? -30.544 15.862  36.486 1.00 30.62  ? 199 LEU B CD2 1 
ATOM   3830 N N   . ASP B 1 184 ? -28.629 19.614  39.882 1.00 28.62  ? 200 ASP B N   1 
ATOM   3831 C CA  . ASP B 1 184 ? -27.953 20.858  40.220 1.00 29.66  ? 200 ASP B CA  1 
ATOM   3832 C C   . ASP B 1 184 ? -26.678 20.978  39.392 1.00 26.34  ? 200 ASP B C   1 
ATOM   3833 O O   . ASP B 1 184 ? -25.936 20.009  39.225 1.00 27.73  ? 200 ASP B O   1 
ATOM   3834 C CB  . ASP B 1 184 ? -27.635 20.964  41.717 1.00 29.73  ? 200 ASP B CB  1 
ATOM   3835 C CG  . ASP B 1 184 ? -28.868 20.824  42.587 1.00 32.32  ? 200 ASP B CG  1 
ATOM   3836 O OD1 . ASP B 1 184 ? -29.827 21.540  42.315 1.00 34.41  ? 200 ASP B OD1 1 
ATOM   3837 O OD2 . ASP B 1 184 ? -28.860 19.997  43.518 1.00 34.66  ? 200 ASP B OD2 1 
ATOM   3838 N N   . VAL B 1 185 ? -26.432 22.189  38.897 1.00 25.78  ? 201 VAL B N   1 
ATOM   3839 C CA  . VAL B 1 185 ? -25.246 22.501  38.113 1.00 26.57  ? 201 VAL B CA  1 
ATOM   3840 C C   . VAL B 1 185 ? -24.081 22.683  39.074 1.00 25.69  ? 201 VAL B C   1 
ATOM   3841 O O   . VAL B 1 185 ? -24.112 23.604  39.882 1.00 25.93  ? 201 VAL B O   1 
ATOM   3842 C CB  . VAL B 1 185 ? -25.476 23.770  37.260 1.00 26.01  ? 201 VAL B CB  1 
ATOM   3843 C CG1 . VAL B 1 185 ? -24.240 24.145  36.458 1.00 25.28  ? 201 VAL B CG1 1 
ATOM   3844 C CG2 . VAL B 1 185 ? -26.674 23.609  36.336 1.00 24.49  ? 201 VAL B CG2 1 
ATOM   3845 N N   . LEU B 1 186 ? -23.056 21.821  38.996 1.00 24.72  ? 202 LEU B N   1 
ATOM   3846 C CA  . LEU B 1 186 ? -21.928 21.900  39.928 1.00 24.04  ? 202 LEU B CA  1 
ATOM   3847 C C   . LEU B 1 186 ? -20.803 22.721  39.327 1.00 23.65  ? 202 LEU B C   1 
ATOM   3848 O O   . LEU B 1 186 ? -20.111 23.444  40.028 1.00 25.48  ? 202 LEU B O   1 
ATOM   3849 C CB  . LEU B 1 186 ? -21.423 20.500  40.257 1.00 24.69  ? 202 LEU B CB  1 
ATOM   3850 C CG  . LEU B 1 186 ? -22.493 19.537  40.755 1.00 26.87  ? 202 LEU B CG  1 
ATOM   3851 C CD1 . LEU B 1 186 ? -21.871 18.190  41.142 1.00 24.98  ? 202 LEU B CD1 1 
ATOM   3852 C CD2 . LEU B 1 186 ? -23.277 20.165  41.908 1.00 27.67  ? 202 LEU B CD2 1 
ATOM   3853 N N   . PHE B 1 187 ? -20.643 22.597  38.006 1.00 25.41  ? 203 PHE B N   1 
ATOM   3854 C CA  . PHE B 1 187 ? -19.559 23.234  37.295 1.00 23.54  ? 203 PHE B CA  1 
ATOM   3855 C C   . PHE B 1 187 ? -19.957 23.353  35.844 1.00 24.11  ? 203 PHE B C   1 
ATOM   3856 O O   . PHE B 1 187 ? -20.530 22.403  35.318 1.00 26.85  ? 203 PHE B O   1 
ATOM   3857 C CB  . PHE B 1 187 ? -18.287 22.382  37.343 1.00 23.96  ? 203 PHE B CB  1 
ATOM   3858 C CG  . PHE B 1 187 ? -17.145 22.921  36.513 1.00 22.30  ? 203 PHE B CG  1 
ATOM   3859 C CD1 . PHE B 1 187 ? -16.526 24.118  36.846 1.00 25.48  ? 203 PHE B CD1 1 
ATOM   3860 C CD2 . PHE B 1 187 ? -16.680 22.233  35.411 1.00 22.66  ? 203 PHE B CD2 1 
ATOM   3861 C CE1 . PHE B 1 187 ? -15.480 24.608  36.087 1.00 25.77  ? 203 PHE B CE1 1 
ATOM   3862 C CE2 . PHE B 1 187 ? -15.617 22.708  34.666 1.00 23.33  ? 203 PHE B CE2 1 
ATOM   3863 C CZ  . PHE B 1 187 ? -15.026 23.901  34.995 1.00 23.75  ? 203 PHE B CZ  1 
ATOM   3864 N N   . GLU B 1 188 ? -19.607 24.477  35.200 1.00 23.88  ? 204 GLU B N   1 
ATOM   3865 C CA  . GLU B 1 188 ? -19.908 24.642  33.783 1.00 23.34  ? 204 GLU B CA  1 
ATOM   3866 C C   . GLU B 1 188 ? -18.781 25.436  33.142 1.00 20.52  ? 204 GLU B C   1 
ATOM   3867 O O   . GLU B 1 188 ? -18.137 26.208  33.814 1.00 21.15  ? 204 GLU B O   1 
ATOM   3868 C CB  . GLU B 1 188 ? -21.304 25.257  33.563 1.00 24.96  ? 204 GLU B CB  1 
ATOM   3869 C CG  . GLU B 1 188 ? -21.475 26.613  34.224 1.00 28.51  ? 204 GLU B CG  1 
ATOM   3870 C CD  . GLU B 1 188 ? -22.861 27.229  34.130 1.00 32.34  ? 204 GLU B CD  1 
ATOM   3871 O OE1 . GLU B 1 188 ? -23.081 28.243  34.786 1.00 35.18  ? 204 GLU B OE1 1 
ATOM   3872 O OE2 . GLU B 1 188 ? -23.709 26.693  33.417 1.00 35.85  ? 204 GLU B OE2 1 
ATOM   3873 N N   . THR B 1 189 ? -18.527 25.180  31.856 1.00 21.91  ? 205 THR B N   1 
ATOM   3874 C CA  . THR B 1 189 ? -17.407 25.729  31.119 1.00 22.23  ? 205 THR B CA  1 
ATOM   3875 C C   . THR B 1 189 ? -17.753 25.676  29.628 1.00 23.15  ? 205 THR B C   1 
ATOM   3876 O O   . THR B 1 189 ? -18.330 24.697  29.152 1.00 24.30  ? 205 THR B O   1 
ATOM   3877 C CB  . THR B 1 189 ? -16.112 24.984  31.473 1.00 22.58  ? 205 THR B CB  1 
ATOM   3878 O OG1 . THR B 1 189 ? -15.020 25.789  31.046 1.00 25.99  ? 205 THR B OG1 1 
ATOM   3879 C CG2 . THR B 1 189 ? -15.981 23.610  30.848 1.00 22.39  ? 205 THR B CG2 1 
ATOM   3880 N N   . GLU B 1 190 ? -17.384 26.742  28.899 1.00 23.52  ? 206 GLU B N   1 
ATOM   3881 C CA  . GLU B 1 190 ? -17.677 26.870  27.481 1.00 24.67  ? 206 GLU B CA  1 
ATOM   3882 C C   . GLU B 1 190 ? -17.117 25.665  26.722 1.00 24.98  ? 206 GLU B C   1 
ATOM   3883 O O   . GLU B 1 190 ? -15.959 25.284  26.894 1.00 26.12  ? 206 GLU B O   1 
ATOM   3884 C CB  . GLU B 1 190 ? -17.092 28.185  26.935 1.00 25.23  ? 206 GLU B CB  1 
ATOM   3885 C CG  . GLU B 1 190 ? -17.416 28.388  25.464 1.00 26.06  ? 206 GLU B CG  1 
ATOM   3886 C CD  . GLU B 1 190 ? -16.901 29.666  24.828 1.00 30.56  ? 206 GLU B CD  1 
ATOM   3887 O OE1 . GLU B 1 190 ? -16.270 30.489  25.538 1.00 33.82  ? 206 GLU B OE1 1 
ATOM   3888 O OE2 . GLU B 1 190 ? -17.069 29.786  23.600 1.00 32.42  ? 206 GLU B OE2 1 
ATOM   3889 N N   . PHE B 1 191 ? -17.944 25.077  25.848 1.00 25.53  ? 207 PHE B N   1 
ATOM   3890 C CA  . PHE B 1 191 ? -17.497 24.032  24.937 1.00 26.12  ? 207 PHE B CA  1 
ATOM   3891 C C   . PHE B 1 191 ? -16.742 24.610  23.726 1.00 25.98  ? 207 PHE B C   1 
ATOM   3892 O O   . PHE B 1 191 ? -17.166 24.471  22.574 1.00 24.00  ? 207 PHE B O   1 
ATOM   3893 C CB  . PHE B 1 191 ? -18.686 23.157  24.504 1.00 24.91  ? 207 PHE B CB  1 
ATOM   3894 C CG  . PHE B 1 191 ? -18.325 21.802  23.943 1.00 24.33  ? 207 PHE B CG  1 
ATOM   3895 C CD1 . PHE B 1 191 ? -17.022 21.347  23.899 1.00 25.83  ? 207 PHE B CD1 1 
ATOM   3896 C CD2 . PHE B 1 191 ? -19.307 20.970  23.454 1.00 27.17  ? 207 PHE B CD2 1 
ATOM   3897 C CE1 . PHE B 1 191 ? -16.731 20.103  23.358 1.00 28.83  ? 207 PHE B CE1 1 
ATOM   3898 C CE2 . PHE B 1 191 ? -19.015 19.719  22.937 1.00 28.93  ? 207 PHE B CE2 1 
ATOM   3899 C CZ  . PHE B 1 191 ? -17.726 19.279  22.893 1.00 26.84  ? 207 PHE B CZ  1 
ATOM   3900 N N   . THR B 1 192 ? -15.546 25.140  23.993 1.00 25.87  ? 208 THR B N   1 
ATOM   3901 C CA  . THR B 1 192 ? -14.670 25.701  22.975 1.00 25.35  ? 208 THR B CA  1 
ATOM   3902 C C   . THR B 1 192 ? -14.242 24.608  22.007 1.00 27.06  ? 208 THR B C   1 
ATOM   3903 O O   . THR B 1 192 ? -13.991 23.453  22.406 1.00 25.69  ? 208 THR B O   1 
ATOM   3904 C CB  . THR B 1 192 ? -13.443 26.374  23.624 1.00 27.05  ? 208 THR B CB  1 
ATOM   3905 O OG1 . THR B 1 192 ? -12.814 25.446  24.521 1.00 25.16  ? 208 THR B OG1 1 
ATOM   3906 C CG2 . THR B 1 192 ? -13.793 27.606  24.424 1.00 26.61  ? 208 THR B CG2 1 
ATOM   3907 N N   . ASP B 1 193 ? -14.143 24.978  20.719 1.00 25.93  ? 209 ASP B N   1 
ATOM   3908 C CA  . ASP B 1 193 ? -13.824 24.005  19.694 1.00 27.53  ? 209 ASP B CA  1 
ATOM   3909 C C   . ASP B 1 193 ? -12.326 23.726  19.716 1.00 25.50  ? 209 ASP B C   1 
ATOM   3910 O O   . ASP B 1 193 ? -11.542 24.438  20.358 1.00 24.28  ? 209 ASP B O   1 
ATOM   3911 C CB  . ASP B 1 193 ? -14.371 24.403  18.312 1.00 35.63  ? 209 ASP B CB  1 
ATOM   3912 C CG  . ASP B 1 193 ? -13.775 25.652  17.690 1.00 41.47  ? 209 ASP B CG  1 
ATOM   3913 O OD1 . ASP B 1 193 ? -13.137 26.431  18.423 1.00 43.25  ? 209 ASP B OD1 1 
ATOM   3914 O OD2 . ASP B 1 193 ? -13.952 25.831  16.458 1.00 54.60  ? 209 ASP B OD2 1 
ATOM   3915 N N   . GLU B 1 194 ? -11.954 22.640  19.045 1.00 25.62  ? 210 GLU B N   1 
ATOM   3916 C CA  . GLU B 1 194 ? -10.553 22.293  18.821 1.00 30.98  ? 210 GLU B CA  1 
ATOM   3917 C C   . GLU B 1 194 ? -9.791  22.200  20.144 1.00 29.35  ? 210 GLU B C   1 
ATOM   3918 O O   . GLU B 1 194 ? -8.624  22.534  20.196 1.00 32.38  ? 210 GLU B O   1 
ATOM   3919 C CB  . GLU B 1 194 ? -9.909  23.328  17.900 1.00 31.32  ? 210 GLU B CB  1 
ATOM   3920 C CG  . GLU B 1 194 ? -10.670 23.510  16.599 1.00 37.52  ? 210 GLU B CG  1 
ATOM   3921 C CD  . GLU B 1 194 ? -9.949  24.309  15.520 1.00 45.35  ? 210 GLU B CD  1 
ATOM   3922 O OE1 . GLU B 1 194 ? -8.847  24.817  15.816 1.00 41.55  ? 210 GLU B OE1 1 
ATOM   3923 O OE2 . GLU B 1 194 ? -10.507 24.433  14.392 1.00 47.24  ? 210 GLU B OE2 1 
ATOM   3924 N N   . THR B 1 195 ? -10.469 21.751  21.205 1.00 26.75  ? 211 THR B N   1 
ATOM   3925 C CA  . THR B 1 195 ? -9.936  21.725  22.562 1.00 25.54  ? 211 THR B CA  1 
ATOM   3926 C C   . THR B 1 195 ? -10.408 20.433  23.226 1.00 26.24  ? 211 THR B C   1 
ATOM   3927 O O   . THR B 1 195 ? -11.600 20.108  23.155 1.00 23.03  ? 211 THR B O   1 
ATOM   3928 C CB  . THR B 1 195 ? -10.417 22.946  23.362 1.00 28.07  ? 211 THR B CB  1 
ATOM   3929 O OG1 . THR B 1 195 ? -10.040 24.134  22.660 1.00 27.47  ? 211 THR B OG1 1 
ATOM   3930 C CG2 . THR B 1 195 ? -9.878  22.987  24.778 1.00 27.76  ? 211 THR B CG2 1 
ATOM   3931 N N   . TRP B 1 196 ? -9.467  19.665  23.793 1.00 23.89  ? 212 TRP B N   1 
ATOM   3932 C CA  . TRP B 1 196 ? -9.813  18.526  24.627 1.00 20.73  ? 212 TRP B CA  1 
ATOM   3933 C C   . TRP B 1 196 ? -10.174 19.030  26.024 1.00 22.04  ? 212 TRP B C   1 
ATOM   3934 O O   . TRP B 1 196 ? -9.371  19.675  26.716 1.00 22.04  ? 212 TRP B O   1 
ATOM   3935 C CB  . TRP B 1 196 ? -8.683  17.493  24.657 1.00 20.21  ? 212 TRP B CB  1 
ATOM   3936 C CG  . TRP B 1 196 ? -8.667  16.580  23.469 1.00 20.22  ? 212 TRP B CG  1 
ATOM   3937 C CD1 . TRP B 1 196 ? -7.753  16.591  22.465 1.00 20.64  ? 212 TRP B CD1 1 
ATOM   3938 C CD2 . TRP B 1 196 ? -9.613  15.538  23.142 1.00 19.88  ? 212 TRP B CD2 1 
ATOM   3939 N NE1 . TRP B 1 196 ? -8.045  15.617  21.555 1.00 21.42  ? 212 TRP B NE1 1 
ATOM   3940 C CE2 . TRP B 1 196 ? -9.184  14.966  21.920 1.00 21.32  ? 212 TRP B CE2 1 
ATOM   3941 C CE3 . TRP B 1 196 ? -10.782 15.047  23.735 1.00 19.96  ? 212 TRP B CE3 1 
ATOM   3942 C CZ2 . TRP B 1 196 ? -9.864  13.920  21.288 1.00 20.16  ? 212 TRP B CZ2 1 
ATOM   3943 C CZ3 . TRP B 1 196 ? -11.453 14.015  23.110 1.00 19.40  ? 212 TRP B CZ3 1 
ATOM   3944 C CH2 . TRP B 1 196 ? -10.995 13.452  21.917 1.00 19.49  ? 212 TRP B CH2 1 
ATOM   3945 N N   . HIS B 1 197 ? -11.459 18.856  26.338 1.00 20.54  ? 213 HIS B N   1 
ATOM   3946 C CA  . HIS B 1 197 ? -12.030 19.185  27.617 1.00 20.89  ? 213 HIS B CA  1 
ATOM   3947 C C   . HIS B 1 197 ? -11.974 17.929  28.479 1.00 20.10  ? 213 HIS B C   1 
ATOM   3948 O O   . HIS B 1 197 ? -12.728 16.977  28.259 1.00 20.26  ? 213 HIS B O   1 
ATOM   3949 C CB  . HIS B 1 197 ? -13.448 19.731  27.414 1.00 23.08  ? 213 HIS B CB  1 
ATOM   3950 C CG  . HIS B 1 197 ? -13.487 21.041  26.694 1.00 23.16  ? 213 HIS B CG  1 
ATOM   3951 N ND1 . HIS B 1 197 ? -13.458 22.253  27.353 1.00 24.93  ? 213 HIS B ND1 1 
ATOM   3952 C CD2 . HIS B 1 197 ? -13.515 21.319  25.393 1.00 24.11  ? 213 HIS B CD2 1 
ATOM   3953 C CE1 . HIS B 1 197 ? -13.489 23.223  26.461 1.00 23.59  ? 213 HIS B CE1 1 
ATOM   3954 N NE2 . HIS B 1 197 ? -13.521 22.681  25.261 1.00 23.37  ? 213 HIS B NE2 1 
ATOM   3955 N N   . ASN B 1 198 ? -11.047 17.952  29.436 1.00 20.51  ? 214 ASN B N   1 
ATOM   3956 C CA  . ASN B 1 198 ? -10.689 16.819  30.269 1.00 21.02  ? 214 ASN B CA  1 
ATOM   3957 C C   . ASN B 1 198 ? -11.421 16.946  31.593 1.00 19.82  ? 214 ASN B C   1 
ATOM   3958 O O   . ASN B 1 198 ? -11.356 18.011  32.234 1.00 18.48  ? 214 ASN B O   1 
ATOM   3959 C CB  . ASN B 1 198 ? -9.178  16.786  30.562 1.00 20.27  ? 214 ASN B CB  1 
ATOM   3960 C CG  . ASN B 1 198 ? -8.259  16.893  29.356 1.00 19.72  ? 214 ASN B CG  1 
ATOM   3961 O OD1 . ASN B 1 198 ? -7.361  17.733  29.335 1.00 23.78  ? 214 ASN B OD1 1 
ATOM   3962 N ND2 . ASN B 1 198 ? -8.375  15.991  28.405 1.00 19.25  ? 214 ASN B ND2 1 
ATOM   3963 N N   . PHE B 1 199 ? -12.060 15.851  32.017 1.00 19.52  ? 215 PHE B N   1 
ATOM   3964 C CA  . PHE B 1 199 ? -12.808 15.833  33.262 1.00 19.76  ? 215 PHE B CA  1 
ATOM   3965 C C   . PHE B 1 199 ? -12.444 14.601  34.081 1.00 23.88  ? 215 PHE B C   1 
ATOM   3966 O O   . PHE B 1 199 ? -12.170 13.524  33.527 1.00 22.36  ? 215 PHE B O   1 
ATOM   3967 C CB  . PHE B 1 199 ? -14.329 15.733  33.072 1.00 20.37  ? 215 PHE B CB  1 
ATOM   3968 C CG  . PHE B 1 199 ? -14.991 16.912  32.412 1.00 20.03  ? 215 PHE B CG  1 
ATOM   3969 C CD1 . PHE B 1 199 ? -14.911 17.096  31.048 1.00 20.11  ? 215 PHE B CD1 1 
ATOM   3970 C CD2 . PHE B 1 199 ? -15.612 17.894  33.179 1.00 22.20  ? 215 PHE B CD2 1 
ATOM   3971 C CE1 . PHE B 1 199 ? -15.484 18.219  30.454 1.00 21.39  ? 215 PHE B CE1 1 
ATOM   3972 C CE2 . PHE B 1 199 ? -16.214 18.994  32.589 1.00 20.07  ? 215 PHE B CE2 1 
ATOM   3973 C CZ  . PHE B 1 199 ? -16.155 19.154  31.223 1.00 21.58  ? 215 PHE B CZ  1 
ATOM   3974 N N   . ALA B 1 200 ? -12.531 14.772  35.402 1.00 22.92  ? 216 ALA B N   1 
ATOM   3975 C CA  . ALA B 1 200 ? -12.713 13.634  36.297 1.00 23.84  ? 216 ALA B CA  1 
ATOM   3976 C C   . ALA B 1 200 ? -13.748 13.995  37.356 1.00 20.63  ? 216 ALA B C   1 
ATOM   3977 O O   . ALA B 1 200 ? -13.736 15.074  37.925 1.00 23.23  ? 216 ALA B O   1 
ATOM   3978 C CB  . ALA B 1 200 ? -11.405 13.194  36.909 1.00 24.50  ? 216 ALA B CB  1 
ATOM   3979 N N   . VAL B 1 201 ? -14.677 13.080  37.577 1.00 22.03  ? 217 VAL B N   1 
ATOM   3980 C CA  . VAL B 1 201 ? -15.652 13.196  38.634 1.00 21.91  ? 217 VAL B CA  1 
ATOM   3981 C C   . VAL B 1 201 ? -15.349 12.111  39.665 1.00 21.98  ? 217 VAL B C   1 
ATOM   3982 O O   . VAL B 1 201 ? -15.357 10.925  39.345 1.00 19.28  ? 217 VAL B O   1 
ATOM   3983 C CB  . VAL B 1 201 ? -17.077 13.059  38.098 1.00 24.13  ? 217 VAL B CB  1 
ATOM   3984 C CG1 . VAL B 1 201 ? -18.085 13.102  39.234 1.00 24.85  ? 217 VAL B CG1 1 
ATOM   3985 C CG2 . VAL B 1 201 ? -17.386 14.127  37.062 1.00 26.41  ? 217 VAL B CG2 1 
ATOM   3986 N N   . ILE B 1 202 ? -15.055 12.534  40.897 1.00 24.60  ? 218 ILE B N   1 
ATOM   3987 C CA  . ILE B 1 202 ? -14.839 11.573  41.971 1.00 24.60  ? 218 ILE B CA  1 
ATOM   3988 C C   . ILE B 1 202 ? -16.174 11.315  42.660 1.00 22.91  ? 218 ILE B C   1 
ATOM   3989 O O   . ILE B 1 202 ? -16.791 12.235  43.193 1.00 23.30  ? 218 ILE B O   1 
ATOM   3990 C CB  . ILE B 1 202 ? -13.791 12.036  42.999 1.00 24.82  ? 218 ILE B CB  1 
ATOM   3991 C CG1 . ILE B 1 202 ? -12.417 12.262  42.367 1.00 25.25  ? 218 ILE B CG1 1 
ATOM   3992 C CG2 . ILE B 1 202 ? -13.708 11.000  44.117 1.00 24.94  ? 218 ILE B CG2 1 
ATOM   3993 C CD1 . ILE B 1 202 ? -11.371 12.737  43.364 1.00 24.34  ? 218 ILE B CD1 1 
ATOM   3994 N N   . VAL B 1 203 ? -16.609 10.062  42.607 1.00 24.26  ? 219 VAL B N   1 
ATOM   3995 C CA  . VAL B 1 203 ? -17.767 9.601   43.355 1.00 26.93  ? 219 VAL B CA  1 
ATOM   3996 C C   . VAL B 1 203 ? -17.287 8.881   44.614 1.00 27.34  ? 219 VAL B C   1 
ATOM   3997 O O   . VAL B 1 203 ? -16.612 7.852   44.511 1.00 28.78  ? 219 VAL B O   1 
ATOM   3998 C CB  . VAL B 1 203 ? -18.613 8.660   42.484 1.00 26.83  ? 219 VAL B CB  1 
ATOM   3999 C CG1 . VAL B 1 203 ? -19.814 8.123   43.243 1.00 29.54  ? 219 VAL B CG1 1 
ATOM   4000 C CG2 . VAL B 1 203 ? -19.047 9.355   41.193 1.00 28.44  ? 219 VAL B CG2 1 
ATOM   4001 N N   . ASP B 1 204 ? -17.624 9.424   45.791 1.00 29.16  ? 220 ASP B N   1 
ATOM   4002 C CA  . ASP B 1 204 ? -17.446 8.692   47.042 1.00 27.16  ? 220 ASP B CA  1 
ATOM   4003 C C   . ASP B 1 204 ? -18.752 7.968   47.323 1.00 26.49  ? 220 ASP B C   1 
ATOM   4004 O O   . ASP B 1 204 ? -19.721 8.615   47.705 1.00 27.17  ? 220 ASP B O   1 
ATOM   4005 C CB  . ASP B 1 204 ? -17.098 9.617   48.210 1.00 29.57  ? 220 ASP B CB  1 
ATOM   4006 C CG  . ASP B 1 204 ? -16.789 8.885   49.513 1.00 31.97  ? 220 ASP B CG  1 
ATOM   4007 O OD1 . ASP B 1 204 ? -17.234 7.703   49.683 1.00 29.71  ? 220 ASP B OD1 1 
ATOM   4008 O OD2 . ASP B 1 204 ? -16.058 9.476   50.320 1.00 31.19  ? 220 ASP B OD2 1 
ATOM   4009 N N   . TRP B 1 205 ? -18.777 6.667   47.049 1.00 27.96  ? 221 TRP B N   1 
ATOM   4010 C CA  . TRP B 1 205 ? -19.988 5.858   47.181 1.00 31.46  ? 221 TRP B CA  1 
ATOM   4011 C C   . TRP B 1 205 ? -20.458 5.685   48.636 1.00 35.38  ? 221 TRP B C   1 
ATOM   4012 O O   . TRP B 1 205 ? -21.638 5.441   48.866 1.00 36.64  ? 221 TRP B O   1 
ATOM   4013 C CB  . TRP B 1 205 ? -19.760 4.499   46.505 1.00 31.22  ? 221 TRP B CB  1 
ATOM   4014 C CG  . TRP B 1 205 ? -19.641 4.573   45.009 1.00 29.67  ? 221 TRP B CG  1 
ATOM   4015 C CD1 . TRP B 1 205 ? -18.505 4.393   44.279 1.00 33.06  ? 221 TRP B CD1 1 
ATOM   4016 C CD2 . TRP B 1 205 ? -20.706 4.796   44.051 1.00 29.36  ? 221 TRP B CD2 1 
ATOM   4017 N NE1 . TRP B 1 205 ? -18.779 4.515   42.938 1.00 36.10  ? 221 TRP B NE1 1 
ATOM   4018 C CE2 . TRP B 1 205 ? -20.121 4.757   42.766 1.00 31.00  ? 221 TRP B CE2 1 
ATOM   4019 C CE3 . TRP B 1 205 ? -22.076 5.065   44.147 1.00 28.60  ? 221 TRP B CE3 1 
ATOM   4020 C CZ2 . TRP B 1 205 ? -20.866 4.949   41.598 1.00 32.47  ? 221 TRP B CZ2 1 
ATOM   4021 C CZ3 . TRP B 1 205 ? -22.820 5.223   42.993 1.00 28.18  ? 221 TRP B CZ3 1 
ATOM   4022 C CH2 . TRP B 1 205 ? -22.223 5.175   41.734 1.00 28.76  ? 221 TRP B CH2 1 
ATOM   4023 N N   . GLU B 1 206 ? -19.565 5.821   49.628 1.00 38.35  ? 222 GLU B N   1 
ATOM   4024 C CA  . GLU B 1 206 ? -19.947 5.642   51.020 1.00 39.72  ? 222 GLU B CA  1 
ATOM   4025 C C   . GLU B 1 206 ? -20.597 6.917   51.543 1.00 44.28  ? 222 GLU B C   1 
ATOM   4026 O O   . GLU B 1 206 ? -21.605 6.833   52.227 1.00 42.30  ? 222 GLU B O   1 
ATOM   4027 C CB  . GLU B 1 206 ? -18.750 5.360   51.930 1.00 41.57  ? 222 GLU B CB  1 
ATOM   4028 C CG  . GLU B 1 206 ? -18.034 4.056   51.673 1.00 42.78  ? 222 GLU B CG  1 
ATOM   4029 C CD  . GLU B 1 206 ? -16.944 3.760   52.699 1.00 43.37  ? 222 GLU B CD  1 
ATOM   4030 O OE1 . GLU B 1 206 ? -15.969 4.551   52.799 1.00 36.24  ? 222 GLU B OE1 1 
ATOM   4031 O OE2 . GLU B 1 206 ? -17.078 2.746   53.406 1.00 39.84  ? 222 GLU B OE2 1 
ATOM   4032 N N   . LYS B 1 207 ? -19.993 8.084   51.252 1.00 42.03  ? 223 LYS B N   1 
ATOM   4033 C CA  . LYS B 1 207 ? -20.484 9.366   51.740 1.00 41.76  ? 223 LYS B CA  1 
ATOM   4034 C C   . LYS B 1 207 ? -21.491 10.008  50.779 1.00 37.65  ? 223 LYS B C   1 
ATOM   4035 O O   . LYS B 1 207 ? -22.141 10.982  51.150 1.00 37.76  ? 223 LYS B O   1 
ATOM   4036 C CB  . LYS B 1 207 ? -19.321 10.333  51.986 1.00 48.78  ? 223 LYS B CB  1 
ATOM   4037 C CG  . LYS B 1 207 ? -18.677 10.269  53.367 1.00 58.00  ? 223 LYS B CG  1 
ATOM   4038 C CD  . LYS B 1 207 ? -17.984 8.965   53.667 1.00 63.95  ? 223 LYS B CD  1 
ATOM   4039 C CE  . LYS B 1 207 ? -17.128 9.007   54.917 1.00 67.18  ? 223 LYS B CE  1 
ATOM   4040 N NZ  . LYS B 1 207 ? -16.172 7.873   54.944 1.00 68.06  ? 223 LYS B NZ  1 
ATOM   4041 N N   . ARG B 1 208 ? -21.641 9.449   49.563 1.00 40.99  ? 224 ARG B N   1 
ATOM   4042 C CA  . ARG B 1 208 ? -22.464 10.029  48.501 1.00 36.91  ? 224 ARG B CA  1 
ATOM   4043 C C   . ARG B 1 208 ? -22.068 11.489  48.293 1.00 32.59  ? 224 ARG B C   1 
ATOM   4044 O O   . ARG B 1 208 ? -22.855 12.405  48.521 1.00 29.90  ? 224 ARG B O   1 
ATOM   4045 C CB  . ARG B 1 208 ? -23.958 9.826   48.798 1.00 46.69  ? 224 ARG B CB  1 
ATOM   4046 C CG  . ARG B 1 208 ? -24.331 8.354   48.966 1.00 53.34  ? 224 ARG B CG  1 
ATOM   4047 C CD  . ARG B 1 208 ? -25.799 7.987   48.808 1.00 57.48  ? 224 ARG B CD  1 
ATOM   4048 N NE  . ARG B 1 208 ? -26.687 8.878   49.540 1.00 58.92  ? 224 ARG B NE  1 
ATOM   4049 C CZ  . ARG B 1 208 ? -26.788 8.951   50.858 1.00 57.09  ? 224 ARG B CZ  1 
ATOM   4050 N NH1 . ARG B 1 208 ? -26.161 8.084   51.635 1.00 58.13  ? 224 ARG B NH1 1 
ATOM   4051 N NH2 . ARG B 1 208 ? -27.554 9.885   51.391 1.00 63.51  ? 224 ARG B NH2 1 
ATOM   4052 N N   . THR B 1 209 ? -20.804 11.685  47.874 1.00 30.71  ? 225 THR B N   1 
ATOM   4053 C CA  . THR B 1 209 ? -20.297 12.991  47.495 1.00 26.03  ? 225 THR B CA  1 
ATOM   4054 C C   . THR B 1 209 ? -19.859 12.952  46.031 1.00 27.51  ? 225 THR B C   1 
ATOM   4055 O O   . THR B 1 209 ? -19.669 11.867  45.470 1.00 26.31  ? 225 THR B O   1 
ATOM   4056 C CB  . THR B 1 209 ? -19.142 13.444  48.396 1.00 25.78  ? 225 THR B CB  1 
ATOM   4057 O OG1 . THR B 1 209 ? -18.062 12.547  48.185 1.00 29.18  ? 225 THR B OG1 1 
ATOM   4058 C CG2 . THR B 1 209 ? -19.478 13.490  49.872 1.00 27.43  ? 225 THR B CG2 1 
ATOM   4059 N N   . LEU B 1 210 ? -19.700 14.155  45.447 1.00 25.05  ? 226 LEU B N   1 
ATOM   4060 C CA  . LEU B 1 210 ? -19.095 14.347  44.137 1.00 24.88  ? 226 LEU B CA  1 
ATOM   4061 C C   . LEU B 1 210 ? -17.996 15.400  44.248 1.00 24.44  ? 226 LEU B C   1 
ATOM   4062 O O   . LEU B 1 210 ? -18.119 16.347  45.035 1.00 23.53  ? 226 LEU B O   1 
ATOM   4063 C CB  . LEU B 1 210 ? -20.157 14.823  43.142 1.00 24.05  ? 226 LEU B CB  1 
ATOM   4064 C CG  . LEU B 1 210 ? -21.265 13.825  42.788 1.00 24.28  ? 226 LEU B CG  1 
ATOM   4065 C CD1 . LEU B 1 210 ? -22.319 14.509  41.935 1.00 23.00  ? 226 LEU B CD1 1 
ATOM   4066 C CD2 . LEU B 1 210 ? -20.714 12.607  42.060 1.00 24.43  ? 226 LEU B CD2 1 
ATOM   4067 N N   . GLN B 1 211 ? -16.917 15.223  43.466 1.00 21.22  ? 227 GLN B N   1 
ATOM   4068 C CA  . GLN B 1 211 ? -15.986 16.316  43.237 1.00 23.83  ? 227 GLN B CA  1 
ATOM   4069 C C   . GLN B 1 211 ? -15.580 16.346  41.766 1.00 23.47  ? 227 GLN B C   1 
ATOM   4070 O O   . GLN B 1 211 ? -15.348 15.301  41.161 1.00 24.33  ? 227 GLN B O   1 
ATOM   4071 C CB  . GLN B 1 211 ? -14.769 16.229  44.155 1.00 21.77  ? 227 GLN B CB  1 
ATOM   4072 C CG  . GLN B 1 211 ? -13.853 17.426  43.988 1.00 23.25  ? 227 GLN B CG  1 
ATOM   4073 C CD  . GLN B 1 211 ? -12.647 17.329  44.896 1.00 23.96  ? 227 GLN B CD  1 
ATOM   4074 O OE1 . GLN B 1 211 ? -12.133 16.240  45.139 1.00 25.23  ? 227 GLN B OE1 1 
ATOM   4075 N NE2 . GLN B 1 211 ? -12.209 18.458  45.424 1.00 23.22  ? 227 GLN B NE2 1 
ATOM   4076 N N   . VAL B 1 212 ? -15.555 17.559  41.195 1.00 22.76  ? 228 VAL B N   1 
ATOM   4077 C CA  . VAL B 1 212 ? -15.265 17.752  39.790 1.00 21.40  ? 228 VAL B CA  1 
ATOM   4078 C C   . VAL B 1 212 ? -13.842 18.293  39.624 1.00 21.14  ? 228 VAL B C   1 
ATOM   4079 O O   . VAL B 1 212 ? -13.458 19.254  40.281 1.00 23.33  ? 228 VAL B O   1 
ATOM   4080 C CB  . VAL B 1 212 ? -16.257 18.713  39.122 1.00 21.52  ? 228 VAL B CB  1 
ATOM   4081 C CG1 . VAL B 1 212 ? -15.971 18.812  37.636 1.00 22.63  ? 228 VAL B CG1 1 
ATOM   4082 C CG2 . VAL B 1 212 ? -17.708 18.305  39.368 1.00 24.10  ? 228 VAL B CG2 1 
ATOM   4083 N N   . TRP B 1 213 ? -13.114 17.674  38.696 1.00 20.63  ? 229 TRP B N   1 
ATOM   4084 C CA  . TRP B 1 213 ? -11.806 18.091  38.229 1.00 20.46  ? 229 TRP B CA  1 
ATOM   4085 C C   . TRP B 1 213 ? -11.872 18.379  36.733 1.00 21.03  ? 229 TRP B C   1 
ATOM   4086 O O   . TRP B 1 213 ? -12.547 17.679  35.986 1.00 21.25  ? 229 TRP B O   1 
ATOM   4087 C CB  . TRP B 1 213 ? -10.800 16.971  38.511 1.00 21.15  ? 229 TRP B CB  1 
ATOM   4088 C CG  . TRP B 1 213 ? -10.602 16.689  39.969 1.00 22.43  ? 229 TRP B CG  1 
ATOM   4089 C CD1 . TRP B 1 213 ? -11.508 16.150  40.840 1.00 24.49  ? 229 TRP B CD1 1 
ATOM   4090 C CD2 . TRP B 1 213 ? -9.411  16.973  40.740 1.00 23.86  ? 229 TRP B CD2 1 
ATOM   4091 N NE1 . TRP B 1 213 ? -10.960 16.067  42.093 1.00 24.83  ? 229 TRP B NE1 1 
ATOM   4092 C CE2 . TRP B 1 213 ? -9.683  16.570  42.072 1.00 24.12  ? 229 TRP B CE2 1 
ATOM   4093 C CE3 . TRP B 1 213 ? -8.159  17.522  40.438 1.00 23.49  ? 229 TRP B CE3 1 
ATOM   4094 C CZ2 . TRP B 1 213 ? -8.752  16.715  43.103 1.00 24.42  ? 229 TRP B CZ2 1 
ATOM   4095 C CZ3 . TRP B 1 213 ? -7.232  17.656  41.461 1.00 25.98  ? 229 TRP B CZ3 1 
ATOM   4096 C CH2 . TRP B 1 213 ? -7.531  17.275  42.776 1.00 22.85  ? 229 TRP B CH2 1 
ATOM   4097 N N   . TYR B 1 214 ? -11.128 19.389  36.269 1.00 21.36  ? 230 TYR B N   1 
ATOM   4098 C CA  . TYR B 1 214 ? -11.196 19.770  34.875 1.00 21.76  ? 230 TYR B CA  1 
ATOM   4099 C C   . TYR B 1 214 ? -9.871  20.385  34.435 1.00 22.85  ? 230 TYR B C   1 
ATOM   4100 O O   . TYR B 1 214 ? -9.165  21.004  35.229 1.00 22.39  ? 230 TYR B O   1 
ATOM   4101 C CB  . TYR B 1 214 ? -12.377 20.728  34.711 1.00 21.93  ? 230 TYR B CB  1 
ATOM   4102 C CG  . TYR B 1 214 ? -12.435 21.448  33.371 1.00 23.11  ? 230 TYR B CG  1 
ATOM   4103 C CD1 . TYR B 1 214 ? -12.886 20.782  32.244 1.00 21.19  ? 230 TYR B CD1 1 
ATOM   4104 C CD2 . TYR B 1 214 ? -12.026 22.771  33.224 1.00 23.46  ? 230 TYR B CD2 1 
ATOM   4105 C CE1 . TYR B 1 214 ? -12.952 21.406  31.009 1.00 22.30  ? 230 TYR B CE1 1 
ATOM   4106 C CE2 . TYR B 1 214 ? -12.088 23.406  31.987 1.00 22.60  ? 230 TYR B CE2 1 
ATOM   4107 C CZ  . TYR B 1 214 ? -12.561 22.724  30.877 1.00 21.08  ? 230 TYR B CZ  1 
ATOM   4108 O OH  . TYR B 1 214 ? -12.648 23.265  29.621 1.00 20.20  ? 230 TYR B OH  1 
ATOM   4109 N N   . SER B 1 215 ? -9.554  20.210  33.156 1.00 20.70  ? 231 SER B N   1 
ATOM   4110 C CA  . SER B 1 215 ? -8.498  20.961  32.502 1.00 23.74  ? 231 SER B CA  1 
ATOM   4111 C C   . SER B 1 215 ? -8.750  20.935  31.000 1.00 22.63  ? 231 SER B C   1 
ATOM   4112 O O   . SER B 1 215 ? -9.682  20.269  30.538 1.00 21.17  ? 231 SER B O   1 
ATOM   4113 C CB  . SER B 1 215 ? -7.133  20.387  32.828 1.00 25.38  ? 231 SER B CB  1 
ATOM   4114 O OG  . SER B 1 215 ? -6.957  19.117  32.221 1.00 24.56  ? 231 SER B OG  1 
ATOM   4115 N N   . GLN B 1 216 ? -7.878  21.629  30.264 1.00 22.50  ? 232 GLN B N   1 
ATOM   4116 C CA  . GLN B 1 216 ? -7.876  21.628  28.811 1.00 22.77  ? 232 GLN B CA  1 
ATOM   4117 C C   . GLN B 1 216 ? -6.557  21.102  28.273 1.00 23.57  ? 232 GLN B C   1 
ATOM   4118 O O   . GLN B 1 216 ? -5.498  21.409  28.816 1.00 25.83  ? 232 GLN B O   1 
ATOM   4119 C CB  . GLN B 1 216 ? -8.111  23.043  28.275 1.00 24.58  ? 232 GLN B CB  1 
ATOM   4120 C CG  . GLN B 1 216 ? -9.450  23.616  28.699 1.00 25.15  ? 232 GLN B CG  1 
ATOM   4121 C CD  . GLN B 1 216 ? -9.826  24.893  27.991 1.00 28.05  ? 232 GLN B CD  1 
ATOM   4122 O OE1 . GLN B 1 216 ? -9.130  25.367  27.095 1.00 28.43  ? 232 GLN B OE1 1 
ATOM   4123 N NE2 . GLN B 1 216 ? -10.978 25.436  28.352 1.00 28.80  ? 232 GLN B NE2 1 
ATOM   4124 N N   . ASN B 1 217 ? -6.645  20.297  27.211 1.00 23.09  ? 233 ASN B N   1 
ATOM   4125 C CA  . ASN B 1 217 ? -5.501  19.869  26.420 1.00 25.93  ? 233 ASN B CA  1 
ATOM   4126 C C   . ASN B 1 217 ? -4.488  19.158  27.313 1.00 25.41  ? 233 ASN B C   1 
ATOM   4127 O O   . ASN B 1 217 ? -4.856  18.213  27.997 1.00 24.72  ? 233 ASN B O   1 
ATOM   4128 C CB  . ASN B 1 217 ? -4.929  21.046  25.626 1.00 24.56  ? 233 ASN B CB  1 
ATOM   4129 C CG  . ASN B 1 217 ? -5.943  21.630  24.671 1.00 27.24  ? 233 ASN B CG  1 
ATOM   4130 O OD1 . ASN B 1 217 ? -6.036  22.837  24.497 1.00 28.95  ? 233 ASN B OD1 1 
ATOM   4131 N ND2 . ASN B 1 217 ? -6.683  20.768  24.005 1.00 25.40  ? 233 ASN B ND2 1 
ATOM   4132 N N   . GLU B 1 218 ? -3.225  19.624  27.309 1.00 25.53  ? 234 GLU B N   1 
ATOM   4133 C CA  . GLU B 1 218 ? -2.146  18.951  28.008 1.00 26.87  ? 234 GLU B CA  1 
ATOM   4134 C C   . GLU B 1 218 ? -2.047  19.393  29.467 1.00 25.58  ? 234 GLU B C   1 
ATOM   4135 O O   . GLU B 1 218 ? -1.199  18.882  30.188 1.00 25.29  ? 234 GLU B O   1 
ATOM   4136 C CB  . GLU B 1 218 ? -0.810  19.187  27.296 1.00 30.00  ? 234 GLU B CB  1 
ATOM   4137 C CG  . GLU B 1 218 ? -0.225  20.587  27.456 1.00 30.79  ? 234 GLU B CG  1 
ATOM   4138 C CD  . GLU B 1 218 ? -0.796  21.724  26.611 1.00 36.88  ? 234 GLU B CD  1 
ATOM   4139 O OE1 . GLU B 1 218 ? -1.801  21.534  25.881 1.00 32.73  ? 234 GLU B OE1 1 
ATOM   4140 O OE2 . GLU B 1 218 ? -0.235  22.831  26.711 1.00 40.74  ? 234 GLU B OE2 1 
ATOM   4141 N N   . ASN B 1 219 ? -2.918  20.299  29.918 1.00 25.80  ? 235 ASN B N   1 
ATOM   4142 C CA  . ASN B 1 219 ? -2.870  20.795  31.288 1.00 27.49  ? 235 ASN B CA  1 
ATOM   4143 C C   . ASN B 1 219 ? -3.369  19.717  32.251 1.00 26.31  ? 235 ASN B C   1 
ATOM   4144 O O   . ASN B 1 219 ? -4.363  19.052  31.970 1.00 27.47  ? 235 ASN B O   1 
ATOM   4145 C CB  . ASN B 1 219 ? -3.676  22.092  31.430 1.00 26.91  ? 235 ASN B CB  1 
ATOM   4146 C CG  . ASN B 1 219 ? -3.092  23.225  30.600 1.00 31.73  ? 235 ASN B CG  1 
ATOM   4147 O OD1 . ASN B 1 219 ? -3.679  23.664  29.619 1.00 33.23  ? 235 ASN B OD1 1 
ATOM   4148 N ND2 . ASN B 1 219 ? -1.918  23.704  30.964 1.00 31.59  ? 235 ASN B ND2 1 
ATOM   4149 N N   . ASN B 1 220 ? -2.703  19.582  33.406 1.00 26.17  ? 236 ASN B N   1 
ATOM   4150 C CA  . ASN B 1 220 ? -3.114  18.655  34.450 1.00 25.12  ? 236 ASN B CA  1 
ATOM   4151 C C   . ASN B 1 220 ? -4.507  19.023  34.957 1.00 24.27  ? 236 ASN B C   1 
ATOM   4152 O O   . ASN B 1 220 ? -4.841  20.204  35.087 1.00 21.00  ? 236 ASN B O   1 
ATOM   4153 C CB  . ASN B 1 220 ? -2.177  18.684  35.662 1.00 29.42  ? 236 ASN B CB  1 
ATOM   4154 C CG  . ASN B 1 220 ? -0.781  18.138  35.411 1.00 30.22  ? 236 ASN B CG  1 
ATOM   4155 O OD1 . ASN B 1 220 ? -0.495  17.518  34.386 1.00 32.21  ? 236 ASN B OD1 1 
ATOM   4156 N ND2 . ASN B 1 220 ? 0.076   18.321  36.394 1.00 31.53  ? 236 ASN B ND2 1 
ATOM   4157 N N   . LEU B 1 221 ? -5.297  17.998  35.316 1.00 25.15  ? 237 LEU B N   1 
ATOM   4158 C CA  . LEU B 1 221 ? -6.586  18.193  35.974 1.00 23.06  ? 237 LEU B CA  1 
ATOM   4159 C C   . LEU B 1 221 ? -6.383  18.984  37.272 1.00 24.73  ? 237 LEU B C   1 
ATOM   4160 O O   . LEU B 1 221 ? -5.442  18.682  38.021 1.00 24.24  ? 237 LEU B O   1 
ATOM   4161 C CB  . LEU B 1 221 ? -7.183  16.824  36.294 1.00 21.85  ? 237 LEU B CB  1 
ATOM   4162 C CG  . LEU B 1 221 ? -7.618  15.927  35.138 1.00 23.98  ? 237 LEU B CG  1 
ATOM   4163 C CD1 . LEU B 1 221 ? -8.102  14.566  35.688 1.00 25.01  ? 237 LEU B CD1 1 
ATOM   4164 C CD2 . LEU B 1 221 ? -8.753  16.565  34.332 1.00 24.50  ? 237 LEU B CD2 1 
ATOM   4165 N N   . VAL B 1 222 ? -7.253  19.989  37.500 1.00 22.48  ? 238 VAL B N   1 
ATOM   4166 C CA  . VAL B 1 222 ? -7.356  20.712  38.756 1.00 22.83  ? 238 VAL B CA  1 
ATOM   4167 C C   . VAL B 1 222 ? -8.779  20.566  39.272 1.00 23.11  ? 238 VAL B C   1 
ATOM   4168 O O   . VAL B 1 222 ? -9.721  20.427  38.496 1.00 21.55  ? 238 VAL B O   1 
ATOM   4169 C CB  . VAL B 1 222 ? -6.994  22.207  38.619 1.00 23.21  ? 238 VAL B CB  1 
ATOM   4170 C CG1 . VAL B 1 222 ? -5.556  22.404  38.184 1.00 24.57  ? 238 VAL B CG1 1 
ATOM   4171 C CG2 . VAL B 1 222 ? -7.924  22.943  37.668 1.00 25.70  ? 238 VAL B CG2 1 
ATOM   4172 N N   . TRP B 1 223 ? -8.934  20.696  40.592 1.00 25.38  ? 239 TRP B N   1 
ATOM   4173 C CA  . TRP B 1 223 ? -10.248 20.613  41.204 1.00 24.62  ? 239 TRP B CA  1 
ATOM   4174 C C   . TRP B 1 223 ? -10.995 21.925  41.012 1.00 22.57  ? 239 TRP B C   1 
ATOM   4175 O O   . TRP B 1 223 ? -10.435 22.992  41.218 1.00 22.75  ? 239 TRP B O   1 
ATOM   4176 C CB  . TRP B 1 223 ? -10.189 20.169  42.678 1.00 24.29  ? 239 TRP B CB  1 
ATOM   4177 C CG  . TRP B 1 223 ? -9.375  20.985  43.655 1.00 23.99  ? 239 TRP B CG  1 
ATOM   4178 C CD1 . TRP B 1 223 ? -8.023  21.005  43.827 1.00 24.03  ? 239 TRP B CD1 1 
ATOM   4179 C CD2 . TRP B 1 223 ? -9.914  21.837  44.687 1.00 22.45  ? 239 TRP B CD2 1 
ATOM   4180 N NE1 . TRP B 1 223 ? -7.688  21.827  44.878 1.00 24.40  ? 239 TRP B NE1 1 
ATOM   4181 C CE2 . TRP B 1 223 ? -8.824  22.344  45.422 1.00 23.31  ? 239 TRP B CE2 1 
ATOM   4182 C CE3 . TRP B 1 223 ? -11.207 22.241  45.035 1.00 23.86  ? 239 TRP B CE3 1 
ATOM   4183 C CZ2 . TRP B 1 223 ? -9.000  23.217  46.489 1.00 25.47  ? 239 TRP B CZ2 1 
ATOM   4184 C CZ3 . TRP B 1 223 ? -11.384 23.088  46.102 1.00 23.51  ? 239 TRP B CZ3 1 
ATOM   4185 C CH2 . TRP B 1 223 ? -10.292 23.577  46.813 1.00 24.89  ? 239 TRP B CH2 1 
ATOM   4186 N N   . VAL B 1 224 ? -12.262 21.830  40.582 1.00 21.93  ? 240 VAL B N   1 
ATOM   4187 C CA  . VAL B 1 224 ? -13.079 22.996  40.268 1.00 21.40  ? 240 VAL B CA  1 
ATOM   4188 C C   . VAL B 1 224 ? -14.365 23.011  41.094 1.00 20.08  ? 240 VAL B C   1 
ATOM   4189 O O   . VAL B 1 224 ? -15.192 23.897  40.924 1.00 22.20  ? 240 VAL B O   1 
ATOM   4190 C CB  . VAL B 1 224 ? -13.368 23.067  38.754 1.00 22.34  ? 240 VAL B CB  1 
ATOM   4191 C CG1 . VAL B 1 224 ? -12.079 23.272  37.975 1.00 24.24  ? 240 VAL B CG1 1 
ATOM   4192 C CG2 . VAL B 1 224 ? -14.105 21.838  38.240 1.00 21.80  ? 240 VAL B CG2 1 
ATOM   4193 N N   . THR B 1 225 ? -14.568 22.006  41.947 1.00 22.09  ? 241 THR B N   1 
ATOM   4194 C CA  . THR B 1 225 ? -15.522 22.053  43.050 1.00 21.74  ? 241 THR B CA  1 
ATOM   4195 C C   . THR B 1 225 ? -14.843 21.490  44.293 1.00 24.08  ? 241 THR B C   1 
ATOM   4196 O O   . THR B 1 225 ? -13.937 20.656  44.184 1.00 25.83  ? 241 THR B O   1 
ATOM   4197 C CB  . THR B 1 225 ? -16.784 21.191  42.842 1.00 21.53  ? 241 THR B CB  1 
ATOM   4198 O OG1 . THR B 1 225 ? -16.429 19.797  42.819 1.00 21.63  ? 241 THR B OG1 1 
ATOM   4199 C CG2 . THR B 1 225 ? -17.539 21.536  41.577 1.00 20.16  ? 241 THR B CG2 1 
ATOM   4200 N N   . PRO B 1 226 ? -15.284 21.875  45.509 1.00 26.54  ? 242 PRO B N   1 
ATOM   4201 C CA  . PRO B 1 226 ? -14.965 21.103  46.699 1.00 28.04  ? 242 PRO B CA  1 
ATOM   4202 C C   . PRO B 1 226 ? -15.651 19.738  46.616 1.00 29.04  ? 242 PRO B C   1 
ATOM   4203 O O   . PRO B 1 226 ? -16.291 19.418  45.617 1.00 27.91  ? 242 PRO B O   1 
ATOM   4204 C CB  . PRO B 1 226 ? -15.513 21.926  47.875 1.00 30.20  ? 242 PRO B CB  1 
ATOM   4205 C CG  . PRO B 1 226 ? -16.521 22.885  47.264 1.00 32.50  ? 242 PRO B CG  1 
ATOM   4206 C CD  . PRO B 1 226 ? -16.159 23.026  45.796 1.00 30.05  ? 242 PRO B CD  1 
ATOM   4207 N N   . VAL B 1 227 ? -15.531 18.947  47.684 1.00 27.59  ? 243 VAL B N   1 
ATOM   4208 C CA  . VAL B 1 227 ? -16.289 17.707  47.809 1.00 28.32  ? 243 VAL B CA  1 
ATOM   4209 C C   . VAL B 1 227 ? -17.722 18.096  48.148 1.00 27.26  ? 243 VAL B C   1 
ATOM   4210 O O   . VAL B 1 227 ? -17.935 18.844  49.087 1.00 29.43  ? 243 VAL B O   1 
ATOM   4211 C CB  . VAL B 1 227 ? -15.657 16.785  48.863 1.00 26.57  ? 243 VAL B CB  1 
ATOM   4212 C CG1 . VAL B 1 227 ? -16.479 15.535  49.146 1.00 26.54  ? 243 VAL B CG1 1 
ATOM   4213 C CG2 . VAL B 1 227 ? -14.245 16.412  48.447 1.00 28.98  ? 243 VAL B CG2 1 
ATOM   4214 N N   . LEU B 1 228 ? -18.699 17.616  47.378 1.00 26.39  ? 244 LEU B N   1 
ATOM   4215 C CA  . LEU B 1 228 ? -20.064 18.110  47.503 1.00 26.34  ? 244 LEU B CA  1 
ATOM   4216 C C   . LEU B 1 228 ? -21.027 16.971  47.836 1.00 27.80  ? 244 LEU B C   1 
ATOM   4217 O O   . LEU B 1 228 ? -20.938 15.907  47.235 1.00 23.62  ? 244 LEU B O   1 
ATOM   4218 C CB  . LEU B 1 228 ? -20.462 18.756  46.177 1.00 27.01  ? 244 LEU B CB  1 
ATOM   4219 C CG  . LEU B 1 228 ? -19.788 20.083  45.850 1.00 28.83  ? 244 LEU B CG  1 
ATOM   4220 C CD1 . LEU B 1 228 ? -20.039 20.434  44.386 1.00 30.16  ? 244 LEU B CD1 1 
ATOM   4221 C CD2 . LEU B 1 228 ? -20.275 21.193  46.780 1.00 27.10  ? 244 LEU B CD2 1 
ATOM   4222 N N   . PRO B 1 229 ? -21.992 17.162  48.764 1.00 31.61  ? 245 PRO B N   1 
ATOM   4223 C CA  . PRO B 1 229 ? -23.047 16.171  48.990 1.00 31.35  ? 245 PRO B CA  1 
ATOM   4224 C C   . PRO B 1 229 ? -23.871 15.845  47.747 1.00 29.18  ? 245 PRO B C   1 
ATOM   4225 O O   . PRO B 1 229 ? -24.176 16.737  46.967 1.00 33.89  ? 245 PRO B O   1 
ATOM   4226 C CB  . PRO B 1 229 ? -23.933 16.844  50.042 1.00 29.60  ? 245 PRO B CB  1 
ATOM   4227 C CG  . PRO B 1 229 ? -22.976 17.722  50.790 1.00 34.20  ? 245 PRO B CG  1 
ATOM   4228 C CD  . PRO B 1 229 ? -22.084 18.288  49.707 1.00 35.34  ? 245 PRO B CD  1 
ATOM   4229 N N   . ASN B 1 230 ? -24.244 14.565  47.601 1.00 28.88  ? 246 ASN B N   1 
ATOM   4230 C CA  . ASN B 1 230 ? -25.018 14.081  46.469 1.00 29.42  ? 246 ASN B CA  1 
ATOM   4231 C C   . ASN B 1 230 ? -26.131 13.186  47.010 1.00 28.60  ? 246 ASN B C   1 
ATOM   4232 O O   . ASN B 1 230 ? -26.298 12.050  46.578 1.00 28.90  ? 246 ASN B O   1 
ATOM   4233 C CB  . ASN B 1 230 ? -24.109 13.356  45.460 1.00 26.38  ? 246 ASN B CB  1 
ATOM   4234 C CG  . ASN B 1 230 ? -24.730 13.119  44.099 1.00 23.70  ? 246 ASN B CG  1 
ATOM   4235 O OD1 . ASN B 1 230 ? -24.352 12.195  43.380 1.00 29.70  ? 246 ASN B OD1 1 
ATOM   4236 N ND2 . ASN B 1 230 ? -25.709 13.918  43.745 1.00 20.74  ? 246 ASN B ND2 1 
ATOM   4237 N N   . GLU B 1 231 ? -26.915 13.737  47.935 1.00 34.38  ? 247 GLU B N   1 
ATOM   4238 C CA  . GLU B 1 231 ? -27.690 12.943  48.873 1.00 39.92  ? 247 GLU B CA  1 
ATOM   4239 C C   . GLU B 1 231 ? -29.036 12.489  48.299 1.00 37.47  ? 247 GLU B C   1 
ATOM   4240 O O   . GLU B 1 231 ? -29.753 11.761  48.983 1.00 35.28  ? 247 GLU B O   1 
ATOM   4241 C CB  . GLU B 1 231 ? -27.913 13.757  50.152 1.00 47.72  ? 247 GLU B CB  1 
ATOM   4242 C CG  . GLU B 1 231 ? -26.631 14.081  50.912 1.00 53.14  ? 247 GLU B CG  1 
ATOM   4243 C CD  . GLU B 1 231 ? -26.187 13.004  51.892 1.00 57.17  ? 247 GLU B CD  1 
ATOM   4244 O OE1 . GLU B 1 231 ? -25.429 13.331  52.825 1.00 54.38  ? 247 GLU B OE1 1 
ATOM   4245 O OE2 . GLU B 1 231 ? -26.591 11.837  51.718 1.00 56.70  ? 247 GLU B OE2 1 
ATOM   4246 N N   . THR B 1 232 ? -29.405 12.911  47.079 1.00 36.16  ? 248 THR B N   1 
ATOM   4247 C CA  . THR B 1 232 ? -30.616 12.389  46.453 1.00 32.94  ? 248 THR B CA  1 
ATOM   4248 C C   . THR B 1 232 ? -30.385 10.986  45.882 1.00 31.98  ? 248 THR B C   1 
ATOM   4249 O O   . THR B 1 232 ? -31.337 10.314  45.496 1.00 30.51  ? 248 THR B O   1 
ATOM   4250 C CB  . THR B 1 232 ? -31.169 13.330  45.382 1.00 32.29  ? 248 THR B CB  1 
ATOM   4251 O OG1 . THR B 1 232 ? -30.226 13.473  44.321 1.00 31.52  ? 248 THR B OG1 1 
ATOM   4252 C CG2 . THR B 1 232 ? -31.523 14.681  45.956 1.00 36.17  ? 248 THR B CG2 1 
ATOM   4253 N N   . VAL B 1 233 ? -29.117 10.564  45.805 1.00 31.09  ? 249 VAL B N   1 
ATOM   4254 C CA  . VAL B 1 233 ? -28.756 9.225   45.381 1.00 36.57  ? 249 VAL B CA  1 
ATOM   4255 C C   . VAL B 1 233 ? -29.349 8.231   46.378 1.00 37.73  ? 249 VAL B C   1 
ATOM   4256 O O   . VAL B 1 233 ? -29.392 8.500   47.576 1.00 37.08  ? 249 VAL B O   1 
ATOM   4257 C CB  . VAL B 1 233 ? -27.226 9.056   45.269 1.00 36.37  ? 249 VAL B CB  1 
ATOM   4258 C CG1 . VAL B 1 233 ? -26.823 7.601   45.067 1.00 40.92  ? 249 VAL B CG1 1 
ATOM   4259 C CG2 . VAL B 1 233 ? -26.652 9.901   44.148 1.00 37.43  ? 249 VAL B CG2 1 
ATOM   4260 N N   . LYS B 1 234 ? -29.793 7.080   45.866 1.00 39.97  ? 250 LYS B N   1 
ATOM   4261 C CA  . LYS B 1 234 ? -30.482 6.107   46.701 1.00 37.40  ? 250 LYS B CA  1 
ATOM   4262 C C   . LYS B 1 234 ? -29.436 5.321   47.478 1.00 34.42  ? 250 LYS B C   1 
ATOM   4263 O O   . LYS B 1 234 ? -28.322 5.101   47.003 1.00 37.45  ? 250 LYS B O   1 
ATOM   4264 C CB  . LYS B 1 234 ? -31.364 5.188   45.855 1.00 36.03  ? 250 LYS B CB  1 
ATOM   4265 C CG  . LYS B 1 234 ? -32.645 5.827   45.346 1.00 34.79  ? 250 LYS B CG  1 
ATOM   4266 C CD  . LYS B 1 234 ? -33.562 4.922   44.547 1.00 35.23  ? 250 LYS B CD  1 
ATOM   4267 C CE  . LYS B 1 234 ? -34.891 5.616   44.302 1.00 37.54  ? 250 LYS B CE  1 
ATOM   4268 N NZ  . LYS B 1 234 ? -35.617 5.078   43.126 1.00 39.19  ? 250 LYS B NZ  1 
ATOM   4269 N N   . ARG B 1 235 ? -29.808 4.947   48.698 1.00 36.59  ? 251 ARG B N   1 
ATOM   4270 C CA  . ARG B 1 235 ? -29.008 4.090   49.554 1.00 36.88  ? 251 ARG B CA  1 
ATOM   4271 C C   . ARG B 1 235 ? -28.865 2.727   48.892 1.00 33.84  ? 251 ARG B C   1 
ATOM   4272 O O   . ARG B 1 235 ? -29.772 2.266   48.203 1.00 37.17  ? 251 ARG B O   1 
ATOM   4273 C CB  . ARG B 1 235 ? -29.698 3.907   50.914 1.00 42.33  ? 251 ARG B CB  1 
ATOM   4274 C CG  . ARG B 1 235 ? -29.802 5.162   51.773 1.00 48.92  ? 251 ARG B CG  1 
ATOM   4275 C CD  . ARG B 1 235 ? -28.580 5.316   52.653 1.00 57.90  ? 251 ARG B CD  1 
ATOM   4276 N NE  . ARG B 1 235 ? -28.664 6.297   53.731 1.00 55.53  ? 251 ARG B NE  1 
ATOM   4277 C CZ  . ARG B 1 235 ? -28.708 6.003   55.029 1.00 58.76  ? 251 ARG B CZ  1 
ATOM   4278 N NH1 . ARG B 1 235 ? -28.834 4.750   55.440 1.00 50.58  ? 251 ARG B NH1 1 
ATOM   4279 N NH2 . ARG B 1 235 ? -28.679 6.978   55.924 1.00 66.00  ? 251 ARG B NH2 1 
ATOM   4280 N N   . GLY B 1 236 ? -27.731 2.079   49.135 1.00 35.74  ? 252 GLY B N   1 
ATOM   4281 C CA  . GLY B 1 236 ? -27.578 0.671   48.820 1.00 36.63  ? 252 GLY B CA  1 
ATOM   4282 C C   . GLY B 1 236 ? -27.261 0.447   47.345 1.00 36.85  ? 252 GLY B C   1 
ATOM   4283 O O   . GLY B 1 236 ? -26.714 1.324   46.679 1.00 37.84  ? 252 GLY B O   1 
ATOM   4284 N N   . THR B 1 237 ? -27.611 -0.739  46.849 1.00 33.39  ? 253 THR B N   1 
ATOM   4285 C CA  . THR B 1 237 ? -27.325 -1.130  45.476 1.00 34.28  ? 253 THR B CA  1 
ATOM   4286 C C   . THR B 1 237 ? -28.190 -0.351  44.475 1.00 32.68  ? 253 THR B C   1 
ATOM   4287 O O   . THR B 1 237 ? -27.833 -0.252  43.303 1.00 31.98  ? 253 THR B O   1 
ATOM   4288 C CB  . THR B 1 237 ? -27.534 -2.633  45.272 1.00 34.84  ? 253 THR B CB  1 
ATOM   4289 O OG1 . THR B 1 237 ? -28.911 -2.852  45.572 1.00 36.87  ? 253 THR B OG1 1 
ATOM   4290 C CG2 . THR B 1 237 ? -26.644 -3.503  46.131 1.00 36.27  ? 253 THR B CG2 1 
ATOM   4291 N N   . ALA B 1 238 ? -29.320 0.208   44.929 1.00 36.16  ? 254 ALA B N   1 
ATOM   4292 C CA  . ALA B 1 238 ? -30.208 0.987   44.074 1.00 36.82  ? 254 ALA B CA  1 
ATOM   4293 C C   . ALA B 1 238 ? -29.536 2.297   43.651 1.00 37.72  ? 254 ALA B C   1 
ATOM   4294 O O   . ALA B 1 238 ? -30.000 2.957   42.729 1.00 41.80  ? 254 ALA B O   1 
ATOM   4295 C CB  . ALA B 1 238 ? -31.526 1.254   44.780 1.00 34.22  ? 254 ALA B CB  1 
ATOM   4296 N N   . GLY B 1 239 ? -28.444 2.671   44.325 1.00 35.71  ? 255 GLY B N   1 
ATOM   4297 C CA  . GLY B 1 239 ? -27.759 3.929   44.049 1.00 36.47  ? 255 GLY B CA  1 
ATOM   4298 C C   . GLY B 1 239 ? -26.667 3.773   42.997 1.00 33.77  ? 255 GLY B C   1 
ATOM   4299 O O   . GLY B 1 239 ? -26.173 4.773   42.485 1.00 37.16  ? 255 GLY B O   1 
ATOM   4300 N N   . ARG B 1 240 ? -26.305 2.513   42.718 1.00 30.03  ? 256 ARG B N   1 
ATOM   4301 C CA  . ARG B 1 240 ? -25.246 2.162   41.790 1.00 30.57  ? 256 ARG B CA  1 
ATOM   4302 C C   . ARG B 1 240 ? -25.813 1.827   40.412 1.00 27.43  ? 256 ARG B C   1 
ATOM   4303 O O   . ARG B 1 240 ? -27.000 1.597   40.273 1.00 28.17  ? 256 ARG B O   1 
ATOM   4304 C CB  . ARG B 1 240 ? -24.463 0.945   42.288 1.00 29.54  ? 256 ARG B CB  1 
ATOM   4305 C CG  . ARG B 1 240 ? -23.434 1.272   43.358 1.00 31.48  ? 256 ARG B CG  1 
ATOM   4306 C CD  . ARG B 1 240 ? -23.975 1.570   44.746 1.00 32.11  ? 256 ARG B CD  1 
ATOM   4307 N NE  . ARG B 1 240 ? -22.848 1.513   45.672 1.00 35.97  ? 256 ARG B NE  1 
ATOM   4308 C CZ  . ARG B 1 240 ? -22.908 1.689   46.985 1.00 35.46  ? 256 ARG B CZ  1 
ATOM   4309 N NH1 . ARG B 1 240 ? -24.050 1.925   47.606 1.00 38.36  ? 256 ARG B NH1 1 
ATOM   4310 N NH2 . ARG B 1 240 ? -21.798 1.605   47.685 1.00 38.95  ? 256 ARG B NH2 1 
ATOM   4311 N N   . GLY B 1 241 ? -24.927 1.730   39.418 1.00 27.63  ? 257 GLY B N   1 
ATOM   4312 C CA  . GLY B 1 241 ? -25.345 1.472   38.052 1.00 29.28  ? 257 GLY B CA  1 
ATOM   4313 C C   . GLY B 1 241 ? -24.177 1.533   37.077 1.00 28.39  ? 257 GLY B C   1 
ATOM   4314 O O   . GLY B 1 241 ? -23.023 1.545   37.482 1.00 29.36  ? 257 GLY B O   1 
ATOM   4315 N N   . ASP B 1 242 ? -24.531 1.589   35.796 1.00 27.70  ? 258 ASP B N   1 
ATOM   4316 C CA  . ASP B 1 242 ? -23.623 1.470   34.664 1.00 29.22  ? 258 ASP B CA  1 
ATOM   4317 C C   . ASP B 1 242 ? -23.081 2.837   34.240 1.00 27.99  ? 258 ASP B C   1 
ATOM   4318 O O   . ASP B 1 242 ? -23.750 3.857   34.373 1.00 26.80  ? 258 ASP B O   1 
ATOM   4319 C CB  . ASP B 1 242 ? -24.367 0.841   33.479 1.00 31.08  ? 258 ASP B CB  1 
ATOM   4320 C CG  . ASP B 1 242 ? -24.942 -0.520  33.827 1.00 32.01  ? 258 ASP B CG  1 
ATOM   4321 O OD1 . ASP B 1 242 ? -24.203 -1.285  34.443 1.00 30.80  ? 258 ASP B OD1 1 
ATOM   4322 O OD2 . ASP B 1 242 ? -26.123 -0.772  33.509 1.00 33.66  ? 258 ASP B OD2 1 
ATOM   4323 N N   . PHE B 1 243 ? -21.868 2.821   33.700 1.00 26.71  ? 259 PHE B N   1 
ATOM   4324 C CA  . PHE B 1 243 ? -21.203 4.005   33.204 1.00 24.56  ? 259 PHE B CA  1 
ATOM   4325 C C   . PHE B 1 243 ? -21.473 4.114   31.709 1.00 22.93  ? 259 PHE B C   1 
ATOM   4326 O O   . PHE B 1 243 ? -21.098 3.209   30.983 1.00 20.61  ? 259 PHE B O   1 
ATOM   4327 C CB  . PHE B 1 243 ? -19.689 3.917   33.461 1.00 27.10  ? 259 PHE B CB  1 
ATOM   4328 C CG  . PHE B 1 243 ? -18.934 5.119   32.956 1.00 24.81  ? 259 PHE B CG  1 
ATOM   4329 C CD1 . PHE B 1 243 ? -19.200 6.372   33.471 1.00 23.86  ? 259 PHE B CD1 1 
ATOM   4330 C CD2 . PHE B 1 243 ? -18.050 5.012   31.900 1.00 24.92  ? 259 PHE B CD2 1 
ATOM   4331 C CE1 . PHE B 1 243 ? -18.534 7.494   32.994 1.00 23.59  ? 259 PHE B CE1 1 
ATOM   4332 C CE2 . PHE B 1 243 ? -17.384 6.130   31.419 1.00 25.64  ? 259 PHE B CE2 1 
ATOM   4333 C CZ  . PHE B 1 243 ? -17.625 7.371   31.964 1.00 24.03  ? 259 PHE B CZ  1 
ATOM   4334 N N   . HIS B 1 244 ? -22.189 5.169   31.275 1.00 23.04  ? 260 HIS B N   1 
ATOM   4335 C CA  . HIS B 1 244 ? -22.455 5.410   29.864 1.00 22.61  ? 260 HIS B CA  1 
ATOM   4336 C C   . HIS B 1 244 ? -21.702 6.627   29.333 1.00 21.67  ? 260 HIS B C   1 
ATOM   4337 O O   . HIS B 1 244 ? -21.560 7.643   30.018 1.00 23.64  ? 260 HIS B O   1 
ATOM   4338 C CB  . HIS B 1 244 ? -23.924 5.768   29.626 1.00 24.45  ? 260 HIS B CB  1 
ATOM   4339 C CG  . HIS B 1 244 ? -24.928 4.730   30.000 1.00 27.58  ? 260 HIS B CG  1 
ATOM   4340 N ND1 . HIS B 1 244 ? -25.942 4.365   29.148 1.00 29.25  ? 260 HIS B ND1 1 
ATOM   4341 C CD2 . HIS B 1 244 ? -25.129 4.033   31.133 1.00 28.85  ? 260 HIS B CD2 1 
ATOM   4342 C CE1 . HIS B 1 244 ? -26.703 3.462   29.756 1.00 28.70  ? 260 HIS B CE1 1 
ATOM   4343 N NE2 . HIS B 1 244 ? -26.230 3.251   30.956 1.00 25.80  ? 260 HIS B NE2 1 
ATOM   4344 N N   . PHE B 1 245 ? -21.273 6.569   28.076 1.00 20.88  ? 261 PHE B N   1 
ATOM   4345 C CA  . PHE B 1 245 ? -20.837 7.781   27.412 1.00 21.97  ? 261 PHE B CA  1 
ATOM   4346 C C   . PHE B 1 245 ? -21.199 7.696   25.928 1.00 22.99  ? 261 PHE B C   1 
ATOM   4347 O O   . PHE B 1 245 ? -21.184 6.620   25.306 1.00 24.48  ? 261 PHE B O   1 
ATOM   4348 C CB  . PHE B 1 245 ? -19.342 8.053   27.645 1.00 21.36  ? 261 PHE B CB  1 
ATOM   4349 C CG  . PHE B 1 245 ? -18.394 7.103   26.956 1.00 22.63  ? 261 PHE B CG  1 
ATOM   4350 C CD1 . PHE B 1 245 ? -18.212 5.804   27.415 1.00 23.57  ? 261 PHE B CD1 1 
ATOM   4351 C CD2 . PHE B 1 245 ? -17.694 7.500   25.820 1.00 23.95  ? 261 PHE B CD2 1 
ATOM   4352 C CE1 . PHE B 1 245 ? -17.345 4.938   26.767 1.00 22.98  ? 261 PHE B CE1 1 
ATOM   4353 C CE2 . PHE B 1 245 ? -16.811 6.643   25.188 1.00 23.28  ? 261 PHE B CE2 1 
ATOM   4354 C CZ  . PHE B 1 245 ? -16.637 5.358   25.659 1.00 23.15  ? 261 PHE B CZ  1 
ATOM   4355 N N   . GLY B 1 246 ? -21.501 8.878   25.385 1.00 20.60  ? 262 GLY B N   1 
ATOM   4356 C CA  . GLY B 1 246 ? -21.949 9.025   24.020 1.00 21.02  ? 262 GLY B CA  1 
ATOM   4357 C C   . GLY B 1 246 ? -22.782 10.299  23.877 1.00 19.55  ? 262 GLY B C   1 
ATOM   4358 O O   . GLY B 1 246 ? -22.332 11.367  24.296 1.00 18.29  ? 262 GLY B O   1 
ATOM   4359 N N   . ILE B 1 247 ? -23.969 10.153  23.285 1.00 19.69  ? 263 ILE B N   1 
ATOM   4360 C CA  . ILE B 1 247 ? -24.933 11.237  23.122 1.00 21.91  ? 263 ILE B CA  1 
ATOM   4361 C C   . ILE B 1 247 ? -26.340 10.681  23.378 1.00 21.78  ? 263 ILE B C   1 
ATOM   4362 O O   . ILE B 1 247 ? -26.755 9.773   22.681 1.00 23.18  ? 263 ILE B O   1 
ATOM   4363 C CB  . ILE B 1 247 ? -24.874 11.855  21.711 1.00 21.94  ? 263 ILE B CB  1 
ATOM   4364 C CG1 . ILE B 1 247 ? -23.487 12.379  21.313 1.00 20.38  ? 263 ILE B CG1 1 
ATOM   4365 C CG2 . ILE B 1 247 ? -25.930 12.960  21.606 1.00 24.09  ? 263 ILE B CG2 1 
ATOM   4366 C CD1 . ILE B 1 247 ? -23.339 12.594  19.831 1.00 20.30  ? 263 ILE B CD1 1 
ATOM   4367 N N   . LEU B 1 248 ? -27.035 11.205  24.386 1.00 21.59  ? 264 LEU B N   1 
ATOM   4368 C CA  . LEU B 1 248 ? -28.479 11.043  24.513 1.00 23.55  ? 264 LEU B CA  1 
ATOM   4369 C C   . LEU B 1 248 ? -29.141 12.407  24.319 1.00 22.09  ? 264 LEU B C   1 
ATOM   4370 O O   . LEU B 1 248 ? -29.092 13.266  25.191 1.00 22.21  ? 264 LEU B O   1 
ATOM   4371 C CB  . LEU B 1 248 ? -28.816 10.380  25.860 1.00 24.17  ? 264 LEU B CB  1 
ATOM   4372 C CG  . LEU B 1 248 ? -30.229 10.561  26.424 1.00 24.68  ? 264 LEU B CG  1 
ATOM   4373 C CD1 . LEU B 1 248 ? -31.320 10.160  25.450 1.00 25.65  ? 264 LEU B CD1 1 
ATOM   4374 C CD2 . LEU B 1 248 ? -30.375 9.763   27.723 1.00 26.17  ? 264 LEU B CD2 1 
ATOM   4375 N N   . LYS B 1 249 ? -29.725 12.612  23.132 1.00 21.17  ? 265 LYS B N   1 
ATOM   4376 C CA  . LYS B 1 249 ? -30.323 13.895  22.780 1.00 20.78  ? 265 LYS B CA  1 
ATOM   4377 C C   . LYS B 1 249 ? -31.818 13.873  23.064 1.00 22.30  ? 265 LYS B C   1 
ATOM   4378 O O   . LYS B 1 249 ? -32.543 13.042  22.505 1.00 21.27  ? 265 LYS B O   1 
ATOM   4379 C CB  . LYS B 1 249 ? -30.105 14.189  21.286 1.00 21.82  ? 265 LYS B CB  1 
ATOM   4380 C CG  . LYS B 1 249 ? -30.708 15.486  20.771 1.00 22.86  ? 265 LYS B CG  1 
ATOM   4381 C CD  . LYS B 1 249 ? -30.412 15.690  19.301 1.00 22.79  ? 265 LYS B CD  1 
ATOM   4382 C CE  . LYS B 1 249 ? -30.935 17.020  18.812 1.00 23.07  ? 265 LYS B CE  1 
ATOM   4383 N NZ  . LYS B 1 249 ? -30.615 17.257  17.393 1.00 23.30  ? 265 LYS B NZ  1 
ATOM   4384 N N   . LEU B 1 250 ? -32.263 14.824  23.900 1.00 22.30  ? 266 LEU B N   1 
ATOM   4385 C CA  . LEU B 1 250 ? -33.676 14.995  24.186 1.00 23.11  ? 266 LEU B CA  1 
ATOM   4386 C C   . LEU B 1 250 ? -34.351 15.808  23.087 1.00 23.75  ? 266 LEU B C   1 
ATOM   4387 O O   . LEU B 1 250 ? -33.693 16.532  22.333 1.00 22.98  ? 266 LEU B O   1 
ATOM   4388 C CB  . LEU B 1 250 ? -33.863 15.664  25.549 1.00 22.24  ? 266 LEU B CB  1 
ATOM   4389 C CG  . LEU B 1 250 ? -34.045 14.688  26.709 1.00 23.82  ? 266 LEU B CG  1 
ATOM   4390 C CD1 . LEU B 1 250 ? -32.811 13.816  26.864 1.00 23.09  ? 266 LEU B CD1 1 
ATOM   4391 C CD2 . LEU B 1 250 ? -34.340 15.431  28.003 1.00 24.46  ? 266 LEU B CD2 1 
ATOM   4392 N N   . PRO B 1 251 ? -35.696 15.718  22.996 1.00 23.86  ? 267 PRO B N   1 
ATOM   4393 C CA  . PRO B 1 251 ? -36.456 16.443  21.979 1.00 23.48  ? 267 PRO B CA  1 
ATOM   4394 C C   . PRO B 1 251 ? -36.798 17.843  22.469 1.00 24.01  ? 267 PRO B C   1 
ATOM   4395 O O   . PRO B 1 251 ? -36.348 18.275  23.529 1.00 24.91  ? 267 PRO B O   1 
ATOM   4396 C CB  . PRO B 1 251 ? -37.719 15.594  21.874 1.00 23.22  ? 267 PRO B CB  1 
ATOM   4397 C CG  . PRO B 1 251 ? -37.967 15.175  23.306 1.00 23.39  ? 267 PRO B CG  1 
ATOM   4398 C CD  . PRO B 1 251 ? -36.569 14.912  23.859 1.00 24.01  ? 267 PRO B CD  1 
ATOM   4399 N N   . LEU B 1 252 ? -37.544 18.583  21.657 1.00 25.37  ? 268 LEU B N   1 
ATOM   4400 C CA  . LEU B 1 252 ? -38.322 19.692  22.170 1.00 23.99  ? 268 LEU B CA  1 
ATOM   4401 C C   . LEU B 1 252 ? -39.782 19.251  22.176 1.00 25.68  ? 268 LEU B C   1 
ATOM   4402 O O   . LEU B 1 252 ? -40.158 18.368  21.413 1.00 28.99  ? 268 LEU B O   1 
ATOM   4403 C CB  . LEU B 1 252 ? -38.158 20.911  21.262 1.00 25.90  ? 268 LEU B CB  1 
ATOM   4404 C CG  . LEU B 1 252 ? -36.729 21.315  20.935 1.00 28.83  ? 268 LEU B CG  1 
ATOM   4405 C CD1 . LEU B 1 252 ? -36.747 22.438  19.920 1.00 30.17  ? 268 LEU B CD1 1 
ATOM   4406 C CD2 . LEU B 1 252 ? -35.961 21.736  22.186 1.00 29.19  ? 268 LEU B CD2 1 
ATOM   4407 N N   . VAL B 1 253 ? -40.581 19.927  22.994 1.00 25.10  ? 269 VAL B N   1 
ATOM   4408 C CA  . VAL B 1 253 ? -42.026 19.786  23.005 1.00 27.12  ? 269 VAL B CA  1 
ATOM   4409 C C   . VAL B 1 253 ? -42.587 20.081  21.615 1.00 30.04  ? 269 VAL B C   1 
ATOM   4410 O O   . VAL B 1 253 ? -42.212 21.070  20.977 1.00 28.24  ? 269 VAL B O   1 
ATOM   4411 C CB  . VAL B 1 253 ? -42.646 20.741  24.041 1.00 29.77  ? 269 VAL B CB  1 
ATOM   4412 C CG1 . VAL B 1 253 ? -44.166 20.794  23.932 1.00 30.49  ? 269 VAL B CG1 1 
ATOM   4413 C CG2 . VAL B 1 253 ? -42.224 20.378  25.455 1.00 31.15  ? 269 VAL B CG2 1 
ATOM   4414 N N   . ASN B 1 254 ? -43.480 19.195  21.167 1.00 28.38  ? 270 ASN B N   1 
ATOM   4415 C CA  . ASN B 1 254 ? -44.315 19.423  20.005 1.00 30.28  ? 270 ASN B CA  1 
ATOM   4416 C C   . ASN B 1 254 ? -45.735 19.694  20.491 1.00 33.68  ? 270 ASN B C   1 
ATOM   4417 O O   . ASN B 1 254 ? -46.415 18.758  20.924 1.00 33.34  ? 270 ASN B O   1 
ATOM   4418 C CB  . ASN B 1 254 ? -44.241 18.214  19.061 1.00 31.16  ? 270 ASN B CB  1 
ATOM   4419 C CG  . ASN B 1 254 ? -44.968 18.413  17.746 1.00 30.53  ? 270 ASN B CG  1 
ATOM   4420 O OD1 . ASN B 1 254 ? -45.629 19.425  17.517 1.00 30.36  ? 270 ASN B OD1 1 
ATOM   4421 N ND2 . ASN B 1 254 ? -44.852 17.438  16.867 1.00 31.13  ? 270 ASN B ND2 1 
ATOM   4422 N N   . VAL B 1 255 ? -46.159 20.966  20.393 1.00 38.17  ? 271 VAL B N   1 
ATOM   4423 C CA  . VAL B 1 255 ? -47.463 21.434  20.860 1.00 40.73  ? 271 VAL B CA  1 
ATOM   4424 C C   . VAL B 1 255 ? -48.606 20.814  20.060 1.00 40.73  ? 271 VAL B C   1 
ATOM   4425 O O   . VAL B 1 255 ? -49.749 20.952  20.472 1.00 38.50  ? 271 VAL B O   1 
ATOM   4426 C CB  . VAL B 1 255 ? -47.624 22.971  20.847 1.00 41.09  ? 271 VAL B CB  1 
ATOM   4427 C CG1 . VAL B 1 255 ? -46.887 23.643  21.996 1.00 42.86  ? 271 VAL B CG1 1 
ATOM   4428 C CG2 . VAL B 1 255 ? -47.245 23.594  19.513 1.00 39.93  ? 271 VAL B CG2 1 
ATOM   4429 N N   . ALA B 1 256 ? -48.327 20.133  18.945 1.00 38.44  ? 272 ALA B N   1 
ATOM   4430 C CA  . ALA B 1 256 ? -49.378 19.354  18.303 1.00 40.60  ? 272 ALA B CA  1 
ATOM   4431 C C   . ALA B 1 256 ? -49.691 18.092  19.112 1.00 43.87  ? 272 ALA B C   1 
ATOM   4432 O O   . ALA B 1 256 ? -50.745 17.484  18.918 1.00 47.82  ? 272 ALA B O   1 
ATOM   4433 C CB  . ALA B 1 256 ? -48.995 19.018  16.886 1.00 35.56  ? 272 ALA B CB  1 
ATOM   4434 N N   . ASP B 1 257 ? -48.771 17.663  19.993 1.00 42.68  ? 273 ASP B N   1 
ATOM   4435 C CA  . ASP B 1 257 ? -49.036 16.514  20.849 1.00 38.99  ? 273 ASP B CA  1 
ATOM   4436 C C   . ASP B 1 257 ? -49.999 16.950  21.936 1.00 37.28  ? 273 ASP B C   1 
ATOM   4437 O O   . ASP B 1 257 ? -50.004 18.106  22.325 1.00 39.99  ? 273 ASP B O   1 
ATOM   4438 C CB  . ASP B 1 257 ? -47.778 15.930  21.504 1.00 39.68  ? 273 ASP B CB  1 
ATOM   4439 C CG  . ASP B 1 257 ? -46.820 15.267  20.532 1.00 39.04  ? 273 ASP B CG  1 
ATOM   4440 O OD1 . ASP B 1 257 ? -47.329 14.673  19.564 1.00 41.65  ? 273 ASP B OD1 1 
ATOM   4441 O OD2 . ASP B 1 257 ? -45.563 15.308  20.770 1.00 33.84  ? 273 ASP B OD2 1 
ATOM   4442 N N   . PRO B 1 258 ? -50.865 16.056  22.450 1.00 42.27  ? 274 PRO B N   1 
ATOM   4443 C CA  . PRO B 1 258 ? -51.700 16.395  23.598 1.00 45.54  ? 274 PRO B CA  1 
ATOM   4444 C C   . PRO B 1 258 ? -50.866 16.676  24.846 1.00 46.00  ? 274 PRO B C   1 
ATOM   4445 O O   . PRO B 1 258 ? -49.834 16.035  25.071 1.00 45.11  ? 274 PRO B O   1 
ATOM   4446 C CB  . PRO B 1 258 ? -52.599 15.162  23.787 1.00 44.07  ? 274 PRO B CB  1 
ATOM   4447 C CG  . PRO B 1 258 ? -51.856 14.053  23.094 1.00 44.10  ? 274 PRO B CG  1 
ATOM   4448 C CD  . PRO B 1 258 ? -51.128 14.706  21.938 1.00 43.86  ? 274 PRO B CD  1 
ATOM   4449 N N   . PRO B 1 259 ? -51.316 17.629  25.694 1.00 43.65  ? 275 PRO B N   1 
ATOM   4450 C CA  . PRO B 1 259 ? -50.683 17.917  26.982 1.00 41.71  ? 275 PRO B CA  1 
ATOM   4451 C C   . PRO B 1 259 ? -50.265 16.720  27.828 1.00 40.87  ? 275 PRO B C   1 
ATOM   4452 O O   . PRO B 1 259 ? -49.252 16.783  28.523 1.00 38.37  ? 275 PRO B O   1 
ATOM   4453 C CB  . PRO B 1 259 ? -51.792 18.673  27.732 1.00 42.69  ? 275 PRO B CB  1 
ATOM   4454 C CG  . PRO B 1 259 ? -52.525 19.423  26.640 1.00 43.07  ? 275 PRO B CG  1 
ATOM   4455 C CD  . PRO B 1 259 ? -52.454 18.527  25.424 1.00 44.15  ? 275 PRO B CD  1 
ATOM   4456 N N   . GLU B 1 260 ? -51.044 15.631  27.758 1.00 42.33  ? 276 GLU B N   1 
ATOM   4457 C CA  . GLU B 1 260 ? -50.834 14.470  28.614 1.00 45.65  ? 276 GLU B CA  1 
ATOM   4458 C C   . GLU B 1 260 ? -49.565 13.694  28.239 1.00 40.90  ? 276 GLU B C   1 
ATOM   4459 O O   . GLU B 1 260 ? -49.076 12.938  29.070 1.00 42.65  ? 276 GLU B O   1 
ATOM   4460 C CB  . GLU B 1 260 ? -52.079 13.572  28.611 1.00 51.06  ? 276 GLU B CB  1 
ATOM   4461 C CG  . GLU B 1 260 ? -53.341 14.275  29.118 1.00 56.52  ? 276 GLU B CG  1 
ATOM   4462 C CD  . GLU B 1 260 ? -54.189 14.980  28.064 1.00 64.95  ? 276 GLU B CD  1 
ATOM   4463 O OE1 . GLU B 1 260 ? -53.612 15.659  27.188 1.00 67.23  ? 276 GLU B OE1 1 
ATOM   4464 O OE2 . GLU B 1 260 ? -55.436 14.862  28.121 1.00 71.63  ? 276 GLU B OE2 1 
ATOM   4465 N N   . VAL B 1 261 ? -48.997 13.897  27.034 1.00 38.92  ? 277 VAL B N   1 
ATOM   4466 C CA  . VAL B 1 261 ? -47.828 13.131  26.607 1.00 36.66  ? 277 VAL B CA  1 
ATOM   4467 C C   . VAL B 1 261 ? -46.580 14.011  26.436 1.00 35.92  ? 277 VAL B C   1 
ATOM   4468 O O   . VAL B 1 261 ? -45.485 13.476  26.272 1.00 31.53  ? 277 VAL B O   1 
ATOM   4469 C CB  . VAL B 1 261 ? -48.087 12.328  25.310 1.00 37.40  ? 277 VAL B CB  1 
ATOM   4470 C CG1 . VAL B 1 261 ? -49.264 11.362  25.421 1.00 37.76  ? 277 VAL B CG1 1 
ATOM   4471 C CG2 . VAL B 1 261 ? -48.256 13.229  24.091 1.00 38.48  ? 277 VAL B CG2 1 
ATOM   4472 N N   . ARG B 1 262 ? -46.700 15.346  26.472 1.00 32.30  ? 278 ARG B N   1 
ATOM   4473 C CA  . ARG B 1 262 ? -45.557 16.208  26.182 1.00 32.54  ? 278 ARG B CA  1 
ATOM   4474 C C   . ARG B 1 262 ? -44.363 15.981  27.123 1.00 32.42  ? 278 ARG B C   1 
ATOM   4475 O O   . ARG B 1 262 ? -43.208 16.193  26.730 1.00 27.62  ? 278 ARG B O   1 
ATOM   4476 C CB  . ARG B 1 262 ? -46.014 17.664  26.266 1.00 35.82  ? 278 ARG B CB  1 
ATOM   4477 C CG  . ARG B 1 262 ? -46.943 18.082  25.136 1.00 37.16  ? 278 ARG B CG  1 
ATOM   4478 C CD  . ARG B 1 262 ? -47.498 19.473  25.367 1.00 38.56  ? 278 ARG B CD  1 
ATOM   4479 N NE  . ARG B 1 262 ? -48.439 19.814  24.307 1.00 43.84  ? 278 ARG B NE  1 
ATOM   4480 C CZ  . ARG B 1 262 ? -49.422 20.704  24.424 1.00 44.34  ? 278 ARG B CZ  1 
ATOM   4481 N NH1 . ARG B 1 262 ? -49.563 21.395  25.540 1.00 40.10  ? 278 ARG B NH1 1 
ATOM   4482 N NH2 . ARG B 1 262 ? -50.277 20.882  23.428 1.00 43.72  ? 278 ARG B NH2 1 
ATOM   4483 N N   . ASP B 1 263 ? -44.633 15.578  28.373 1.00 31.09  ? 279 ASP B N   1 
ATOM   4484 C CA  . ASP B 1 263 ? -43.576 15.344  29.337 1.00 33.64  ? 279 ASP B CA  1 
ATOM   4485 C C   . ASP B 1 263 ? -42.816 14.061  29.006 1.00 30.80  ? 279 ASP B C   1 
ATOM   4486 O O   . ASP B 1 263 ? -41.685 13.910  29.471 1.00 29.60  ? 279 ASP B O   1 
ATOM   4487 C CB  . ASP B 1 263 ? -44.103 15.347  30.775 1.00 36.35  ? 279 ASP B CB  1 
ATOM   4488 C CG  . ASP B 1 263 ? -44.642 16.702  31.208 1.00 39.48  ? 279 ASP B CG  1 
ATOM   4489 O OD1 . ASP B 1 263 ? -43.870 17.701  31.163 1.00 38.42  ? 279 ASP B OD1 1 
ATOM   4490 O OD2 . ASP B 1 263 ? -45.831 16.761  31.576 1.00 42.98  ? 279 ASP B OD2 1 
ATOM   4491 N N   . ASP B 1 264 ? -43.419 13.166  28.200 1.00 27.30  ? 280 ASP B N   1 
ATOM   4492 C CA  . ASP B 1 264 ? -42.836 11.861  27.906 1.00 27.27  ? 280 ASP B CA  1 
ATOM   4493 C C   . ASP B 1 264 ? -41.832 11.981  26.757 1.00 27.77  ? 280 ASP B C   1 
ATOM   4494 O O   . ASP B 1 264 ? -42.102 11.600  25.610 1.00 28.24  ? 280 ASP B O   1 
ATOM   4495 C CB  . ASP B 1 264 ? -43.906 10.803  27.626 1.00 28.36  ? 280 ASP B CB  1 
ATOM   4496 C CG  . ASP B 1 264 ? -43.306 9.438   27.329 1.00 28.46  ? 280 ASP B CG  1 
ATOM   4497 O OD1 . ASP B 1 264 ? -42.119 9.228   27.683 1.00 26.97  ? 280 ASP B OD1 1 
ATOM   4498 O OD2 . ASP B 1 264 ? -44.012 8.609   26.729 1.00 26.25  ? 280 ASP B OD2 1 
ATOM   4499 N N   . VAL B 1 265 ? -40.638 12.475  27.113 1.00 25.19  ? 281 VAL B N   1 
ATOM   4500 C CA  . VAL B 1 265 ? -39.566 12.749  26.173 1.00 24.08  ? 281 VAL B CA  1 
ATOM   4501 C C   . VAL B 1 265 ? -39.008 11.447  25.608 1.00 23.55  ? 281 VAL B C   1 
ATOM   4502 O O   . VAL B 1 265 ? -38.282 11.490  24.620 1.00 22.38  ? 281 VAL B O   1 
ATOM   4503 C CB  . VAL B 1 265 ? -38.451 13.588  26.834 1.00 25.56  ? 281 VAL B CB  1 
ATOM   4504 C CG1 . VAL B 1 265 ? -38.940 14.999  27.112 1.00 25.35  ? 281 VAL B CG1 1 
ATOM   4505 C CG2 . VAL B 1 265 ? -37.895 12.936  28.108 1.00 25.58  ? 281 VAL B CG2 1 
ATOM   4506 N N   . VAL B 1 266 ? -39.303 10.303  26.249 1.00 22.80  ? 282 VAL B N   1 
ATOM   4507 C CA  . VAL B 1 266 ? -38.811 9.021   25.768 1.00 21.48  ? 282 VAL B CA  1 
ATOM   4508 C C   . VAL B 1 266 ? -39.510 8.737   24.436 1.00 21.59  ? 282 VAL B C   1 
ATOM   4509 O O   . VAL B 1 266 ? -38.921 8.190   23.514 1.00 20.10  ? 282 VAL B O   1 
ATOM   4510 C CB  . VAL B 1 266 ? -39.029 7.879   26.789 1.00 22.98  ? 282 VAL B CB  1 
ATOM   4511 C CG1 . VAL B 1 266 ? -38.556 6.537   26.272 1.00 24.26  ? 282 VAL B CG1 1 
ATOM   4512 C CG2 . VAL B 1 266 ? -38.351 8.144   28.120 1.00 25.33  ? 282 VAL B CG2 1 
ATOM   4513 N N   . HIS B 1 267 ? -40.781 9.136   24.321 1.00 22.79  ? 283 HIS B N   1 
ATOM   4514 C CA  . HIS B 1 267 ? -41.561 8.746   23.156 1.00 22.41  ? 283 HIS B CA  1 
ATOM   4515 C C   . HIS B 1 267 ? -42.077 9.931   22.339 1.00 23.23  ? 283 HIS B C   1 
ATOM   4516 O O   . HIS B 1 267 ? -42.481 9.712   21.209 1.00 27.37  ? 283 HIS B O   1 
ATOM   4517 C CB  . HIS B 1 267 ? -42.722 7.857   23.598 1.00 22.50  ? 283 HIS B CB  1 
ATOM   4518 C CG  . HIS B 1 267 ? -42.293 6.732   24.469 1.00 23.23  ? 283 HIS B CG  1 
ATOM   4519 N ND1 . HIS B 1 267 ? -42.643 6.601   25.792 1.00 23.90  ? 283 HIS B ND1 1 
ATOM   4520 C CD2 . HIS B 1 267 ? -41.544 5.675   24.166 1.00 23.29  ? 283 HIS B CD2 1 
ATOM   4521 C CE1 . HIS B 1 267 ? -42.058 5.505   26.277 1.00 24.23  ? 283 HIS B CE1 1 
ATOM   4522 N NE2 . HIS B 1 267 ? -41.384 4.932   25.300 1.00 23.07  ? 283 HIS B NE2 1 
ATOM   4523 N N   . TYR B 1 268 ? -42.124 11.155  22.882 1.00 23.24  ? 284 TYR B N   1 
ATOM   4524 C CA  . TYR B 1 268 ? -42.727 12.269  22.163 1.00 24.06  ? 284 TYR B CA  1 
ATOM   4525 C C   . TYR B 1 268 ? -41.754 13.448  22.092 1.00 28.04  ? 284 TYR B C   1 
ATOM   4526 O O   . TYR B 1 268 ? -40.914 13.641  22.982 1.00 25.29  ? 284 TYR B O   1 
ATOM   4527 C CB  . TYR B 1 268 ? -44.058 12.685  22.803 1.00 27.14  ? 284 TYR B CB  1 
ATOM   4528 C CG  . TYR B 1 268 ? -45.126 11.587  22.839 1.00 29.22  ? 284 TYR B CG  1 
ATOM   4529 C CD1 . TYR B 1 268 ? -45.145 10.618  23.841 1.00 29.29  ? 284 TYR B CD1 1 
ATOM   4530 C CD2 . TYR B 1 268 ? -46.091 11.482  21.839 1.00 29.48  ? 284 TYR B CD2 1 
ATOM   4531 C CE1 . TYR B 1 268 ? -46.092 9.599   23.854 1.00 29.79  ? 284 TYR B CE1 1 
ATOM   4532 C CE2 . TYR B 1 268 ? -47.057 10.484  21.854 1.00 30.67  ? 284 TYR B CE2 1 
ATOM   4533 C CZ  . TYR B 1 268 ? -47.068 9.537   22.869 1.00 33.49  ? 284 TYR B CZ  1 
ATOM   4534 O OH  . TYR B 1 268 ? -48.015 8.523   22.867 1.00 26.28  ? 284 TYR B OH  1 
ATOM   4535 N N   . GLY B 1 269 ? -41.932 14.256  21.036 1.00 26.34  ? 285 GLY B N   1 
ATOM   4536 C CA  . GLY B 1 269 ? -41.266 15.546  20.888 1.00 26.23  ? 285 GLY B CA  1 
ATOM   4537 C C   . GLY B 1 269 ? -40.608 15.682  19.516 1.00 25.74  ? 285 GLY B C   1 
ATOM   4538 O O   . GLY B 1 269 ? -40.448 14.702  18.789 1.00 26.84  ? 285 GLY B O   1 
ATOM   4539 N N   . ILE B 1 270 ? -40.181 16.904  19.206 1.00 27.83  ? 286 ILE B N   1 
ATOM   4540 C CA  . ILE B 1 270 ? -39.529 17.228  17.952 1.00 29.55  ? 286 ILE B CA  1 
ATOM   4541 C C   . ILE B 1 270 ? -38.092 16.689  17.978 1.00 26.91  ? 286 ILE B C   1 
ATOM   4542 O O   . ILE B 1 270 ? -37.292 17.080  18.832 1.00 25.09  ? 286 ILE B O   1 
ATOM   4543 C CB  . ILE B 1 270 ? -39.509 18.757  17.724 1.00 33.17  ? 286 ILE B CB  1 
ATOM   4544 C CG1 . ILE B 1 270 ? -40.846 19.459  18.033 1.00 36.33  ? 286 ILE B CG1 1 
ATOM   4545 C CG2 . ILE B 1 270 ? -38.987 19.062  16.324 1.00 33.93  ? 286 ILE B CG2 1 
ATOM   4546 C CD1 . ILE B 1 270 ? -41.738 19.717  16.847 1.00 37.64  ? 286 ILE B CD1 1 
ATOM   4547 N N   . GLN B 1 271 ? -37.771 15.820  17.021 1.00 23.31  ? 287 GLN B N   1 
ATOM   4548 C CA  . GLN B 1 271 ? -36.411 15.427  16.694 1.00 25.43  ? 287 GLN B CA  1 
ATOM   4549 C C   . GLN B 1 271 ? -36.211 15.595  15.193 1.00 29.42  ? 287 GLN B C   1 
ATOM   4550 O O   . GLN B 1 271 ? -36.873 14.920  14.394 1.00 33.51  ? 287 GLN B O   1 
ATOM   4551 C CB  . GLN B 1 271 ? -36.127 13.960  17.014 1.00 24.29  ? 287 GLN B CB  1 
ATOM   4552 C CG  . GLN B 1 271 ? -35.900 13.677  18.480 1.00 23.37  ? 287 GLN B CG  1 
ATOM   4553 C CD  . GLN B 1 271 ? -34.610 14.219  19.045 1.00 22.23  ? 287 GLN B CD  1 
ATOM   4554 O OE1 . GLN B 1 271 ? -33.814 14.883  18.389 1.00 22.98  ? 287 GLN B OE1 1 
ATOM   4555 N NE2 . GLN B 1 271 ? -34.385 13.906  20.304 1.00 24.58  ? 287 GLN B NE2 1 
ATOM   4556 N N   . PRO B 1 272 ? -35.308 16.499  14.762 1.00 28.74  ? 288 PRO B N   1 
ATOM   4557 C CA  . PRO B 1 272 ? -35.028 16.650  13.340 1.00 28.45  ? 288 PRO B CA  1 
ATOM   4558 C C   . PRO B 1 272 ? -34.222 15.457  12.834 1.00 29.40  ? 288 PRO B C   1 
ATOM   4559 O O   . PRO B 1 272 ? -33.454 14.863  13.573 1.00 30.15  ? 288 PRO B O   1 
ATOM   4560 C CB  . PRO B 1 272 ? -34.256 17.959  13.240 1.00 27.36  ? 288 PRO B CB  1 
ATOM   4561 C CG  . PRO B 1 272 ? -33.746 18.263  14.637 1.00 31.36  ? 288 PRO B CG  1 
ATOM   4562 C CD  . PRO B 1 272 ? -34.512 17.393  15.609 1.00 29.75  ? 288 PRO B CD  1 
ATOM   4563 N N   . PRO B 1 273 ? -34.342 15.068  11.547 1.00 30.75  ? 289 PRO B N   1 
ATOM   4564 C CA  . PRO B 1 273 ? -33.578 13.933  11.031 1.00 30.77  ? 289 PRO B CA  1 
ATOM   4565 C C   . PRO B 1 273 ? -32.116 14.233  10.677 1.00 33.36  ? 289 PRO B C   1 
ATOM   4566 O O   . PRO B 1 273 ? -31.616 13.752  9.675  1.00 45.42  ? 289 PRO B O   1 
ATOM   4567 C CB  . PRO B 1 273 ? -34.420 13.548  9.802  1.00 33.31  ? 289 PRO B CB  1 
ATOM   4568 C CG  . PRO B 1 273 ? -34.944 14.896  9.281  1.00 33.30  ? 289 PRO B CG  1 
ATOM   4569 C CD  . PRO B 1 273 ? -35.204 15.703  10.537 1.00 33.35  ? 289 PRO B CD  1 
ATOM   4570 N N   . THR B 1 274 ? -31.386 14.911  11.566 1.00 30.11  ? 290 THR B N   1 
ATOM   4571 C CA  . THR B 1 274 ? -30.039 15.390  11.288 1.00 27.62  ? 290 THR B CA  1 
ATOM   4572 C C   . THR B 1 274 ? -29.009 14.533  12.035 1.00 29.77  ? 290 THR B C   1 
ATOM   4573 O O   . THR B 1 274 ? -29.340 13.818  12.982 1.00 28.50  ? 290 THR B O   1 
ATOM   4574 C CB  . THR B 1 274 ? -29.946 16.877  11.643 1.00 27.20  ? 290 THR B CB  1 
ATOM   4575 O OG1 . THR B 1 274 ? -30.521 17.127  12.929 1.00 25.91  ? 290 THR B OG1 1 
ATOM   4576 C CG2 . THR B 1 274 ? -30.685 17.749  10.645 1.00 28.89  ? 290 THR B CG2 1 
ATOM   4577 N N   . THR B 1 275 ? -27.761 14.602  11.573 1.00 28.67  ? 291 THR B N   1 
ATOM   4578 C CA  . THR B 1 275 ? -26.658 13.841  12.137 1.00 28.46  ? 291 THR B CA  1 
ATOM   4579 C C   . THR B 1 275 ? -25.815 14.780  12.998 1.00 26.62  ? 291 THR B C   1 
ATOM   4580 O O   . THR B 1 275 ? -25.639 15.934  12.646 1.00 25.74  ? 291 THR B O   1 
ATOM   4581 C CB  . THR B 1 275 ? -25.877 13.170  10.992 1.00 29.24  ? 291 THR B CB  1 
ATOM   4582 O OG1 . THR B 1 275 ? -26.741 12.168  10.436 1.00 29.65  ? 291 THR B OG1 1 
ATOM   4583 C CG2 . THR B 1 275 ? -24.578 12.537  11.439 1.00 27.74  ? 291 THR B CG2 1 
ATOM   4584 N N   . HIS B 1 276 ? -25.300 14.281  14.133 1.00 24.22  ? 292 HIS B N   1 
ATOM   4585 C CA  . HIS B 1 276 ? -24.542 15.077  15.080 1.00 21.92  ? 292 HIS B CA  1 
ATOM   4586 C C   . HIS B 1 276 ? -23.539 14.177  15.799 1.00 21.44  ? 292 HIS B C   1 
ATOM   4587 O O   . HIS B 1 276 ? -23.819 12.995  16.046 1.00 21.58  ? 292 HIS B O   1 
ATOM   4588 C CB  . HIS B 1 276 ? -25.451 15.681  16.146 1.00 21.97  ? 292 HIS B CB  1 
ATOM   4589 C CG  . HIS B 1 276 ? -26.693 16.329  15.624 1.00 24.28  ? 292 HIS B CG  1 
ATOM   4590 N ND1 . HIS B 1 276 ? -26.748 17.669  15.317 1.00 24.05  ? 292 HIS B ND1 1 
ATOM   4591 C CD2 . HIS B 1 276 ? -27.910 15.829  15.356 1.00 23.57  ? 292 HIS B CD2 1 
ATOM   4592 C CE1 . HIS B 1 276 ? -27.971 17.963  14.911 1.00 24.55  ? 292 HIS B CE1 1 
ATOM   4593 N NE2 . HIS B 1 276 ? -28.693 16.869  14.912 1.00 23.83  ? 292 HIS B NE2 1 
ATOM   4594 N N   . GLY B 1 277 ? -22.363 14.737  16.109 1.00 20.42  ? 293 GLY B N   1 
ATOM   4595 C CA  . GLY B 1 277 ? -21.307 13.940  16.691 1.00 21.73  ? 293 GLY B CA  1 
ATOM   4596 C C   . GLY B 1 277 ? -20.630 14.643  17.853 1.00 24.35  ? 293 GLY B C   1 
ATOM   4597 O O   . GLY B 1 277 ? -20.789 15.847  18.040 1.00 27.56  ? 293 GLY B O   1 
ATOM   4598 N N   . ILE B 1 278 ? -19.871 13.847  18.620 1.00 24.19  ? 294 ILE B N   1 
ATOM   4599 C CA  . ILE B 1 278 ? -18.920 14.337  19.601 1.00 22.00  ? 294 ILE B CA  1 
ATOM   4600 C C   . ILE B 1 278 ? -17.744 13.352  19.631 1.00 22.92  ? 294 ILE B C   1 
ATOM   4601 O O   . ILE B 1 278 ? -17.921 12.154  19.374 1.00 22.91  ? 294 ILE B O   1 
ATOM   4602 C CB  . ILE B 1 278 ? -19.604 14.501  20.965 1.00 22.88  ? 294 ILE B CB  1 
ATOM   4603 C CG1 . ILE B 1 278 ? -18.806 15.423  21.890 1.00 25.03  ? 294 ILE B CG1 1 
ATOM   4604 C CG2 . ILE B 1 278 ? -19.864 13.139  21.594 1.00 22.93  ? 294 ILE B CG2 1 
ATOM   4605 C CD1 . ILE B 1 278 ? -19.571 15.924  23.103 1.00 23.48  ? 294 ILE B CD1 1 
ATOM   4606 N N   . MET B 1 279 ? -16.537 13.860  19.924 1.00 21.58  ? 295 MET B N   1 
ATOM   4607 C CA  . MET B 1 279 ? -15.401 12.965  20.043 1.00 20.80  ? 295 MET B CA  1 
ATOM   4608 C C   . MET B 1 279 ? -15.047 12.744  21.519 1.00 20.88  ? 295 MET B C   1 
ATOM   4609 O O   . MET B 1 279 ? -15.138 13.649  22.357 1.00 21.95  ? 295 MET B O   1 
ATOM   4610 C CB  . MET B 1 279 ? -14.221 13.522  19.250 1.00 22.94  ? 295 MET B CB  1 
ATOM   4611 C CG  . MET B 1 279 ? -14.380 13.264  17.757 1.00 27.26  ? 295 MET B CG  1 
ATOM   4612 S SD  . MET B 1 279 ? -13.338 14.345  16.702 1.00 30.34  ? 295 MET B SD  1 
ATOM   4613 C CE  . MET B 1 279 ? -13.905 13.873  15.068 1.00 38.38  ? 295 MET B CE  1 
ATOM   4614 N N   . TYR B 1 280 ? -14.624 11.510  21.810 1.00 21.31  ? 296 TYR B N   1 
ATOM   4615 C CA  . TYR B 1 280 ? -14.193 11.098  23.133 1.00 22.93  ? 296 TYR B CA  1 
ATOM   4616 C C   . TYR B 1 280 ? -12.754 10.583  23.102 1.00 22.89  ? 296 TYR B C   1 
ATOM   4617 O O   . TYR B 1 280 ? -12.337 9.969   22.125 1.00 23.00  ? 296 TYR B O   1 
ATOM   4618 C CB  . TYR B 1 280 ? -15.114 9.972   23.605 1.00 20.95  ? 296 TYR B CB  1 
ATOM   4619 C CG  . TYR B 1 280 ? -16.438 10.482  24.137 1.00 22.30  ? 296 TYR B CG  1 
ATOM   4620 C CD1 . TYR B 1 280 ? -16.537 11.062  25.405 1.00 22.05  ? 296 TYR B CD1 1 
ATOM   4621 C CD2 . TYR B 1 280 ? -17.588 10.390  23.356 1.00 21.37  ? 296 TYR B CD2 1 
ATOM   4622 C CE1 . TYR B 1 280 ? -17.758 11.526  25.886 1.00 21.76  ? 296 TYR B CE1 1 
ATOM   4623 C CE2 . TYR B 1 280 ? -18.800 10.853  23.831 1.00 21.82  ? 296 TYR B CE2 1 
ATOM   4624 C CZ  . TYR B 1 280 ? -18.886 11.436  25.086 1.00 21.98  ? 296 TYR B CZ  1 
ATOM   4625 O OH  . TYR B 1 280 ? -20.113 11.915  25.475 1.00 20.73  ? 296 TYR B OH  1 
ATOM   4626 N N   . SER B 1 281 ? -12.040 10.818  24.210 1.00 22.03  ? 297 SER B N   1 
ATOM   4627 C CA  . SER B 1 281 ? -10.800 10.136  24.517 1.00 23.36  ? 297 SER B CA  1 
ATOM   4628 C C   . SER B 1 281 ? -10.582 10.193  26.029 1.00 21.46  ? 297 SER B C   1 
ATOM   4629 O O   . SER B 1 281 ? -11.299 10.880  26.747 1.00 19.94  ? 297 SER B O   1 
ATOM   4630 C CB  . SER B 1 281 ? -9.608  10.695  23.747 1.00 24.58  ? 297 SER B CB  1 
ATOM   4631 O OG  . SER B 1 281 ? -9.278  12.032  24.127 1.00 23.74  ? 297 SER B OG  1 
ATOM   4632 N N   . GLY B 1 282 ? -9.599  9.441   26.504 1.00 20.43  ? 298 GLY B N   1 
ATOM   4633 C CA  . GLY B 1 282 ? -9.246  9.471   27.904 1.00 19.83  ? 298 GLY B CA  1 
ATOM   4634 C C   . GLY B 1 282 ? -10.415 9.084   28.803 1.00 20.22  ? 298 GLY B C   1 
ATOM   4635 O O   . GLY B 1 282 ? -10.506 9.609   29.913 1.00 20.07  ? 298 GLY B O   1 
ATOM   4636 N N   . VAL B 1 283 ? -11.282 8.165   28.345 1.00 20.22  ? 299 VAL B N   1 
ATOM   4637 C CA  . VAL B 1 283 ? -12.390 7.707   29.179 1.00 21.23  ? 299 VAL B CA  1 
ATOM   4638 C C   . VAL B 1 283 ? -11.982 6.445   29.935 1.00 21.14  ? 299 VAL B C   1 
ATOM   4639 O O   . VAL B 1 283 ? -11.765 5.431   29.299 1.00 21.06  ? 299 VAL B O   1 
ATOM   4640 C CB  . VAL B 1 283 ? -13.650 7.434   28.337 1.00 21.60  ? 299 VAL B CB  1 
ATOM   4641 C CG1 . VAL B 1 283 ? -14.812 6.983   29.211 1.00 20.49  ? 299 VAL B CG1 1 
ATOM   4642 C CG2 . VAL B 1 283 ? -14.032 8.644   27.491 1.00 21.90  ? 299 VAL B CG2 1 
ATOM   4643 N N   . PHE B 1 284 ? -11.898 6.500   31.270 1.00 23.36  ? 300 PHE B N   1 
ATOM   4644 C CA  . PHE B 1 284 ? -11.525 5.338   32.071 1.00 22.06  ? 300 PHE B CA  1 
ATOM   4645 C C   . PHE B 1 284 ? -11.955 5.615   33.502 1.00 23.06  ? 300 PHE B C   1 
ATOM   4646 O O   . PHE B 1 284 ? -12.298 6.754   33.846 1.00 21.68  ? 300 PHE B O   1 
ATOM   4647 C CB  . PHE B 1 284 ? -10.025 5.013   31.977 1.00 21.92  ? 300 PHE B CB  1 
ATOM   4648 C CG  . PHE B 1 284 ? -9.084  6.016   32.610 1.00 21.40  ? 300 PHE B CG  1 
ATOM   4649 C CD1 . PHE B 1 284 ? -8.821  7.230   32.005 1.00 22.17  ? 300 PHE B CD1 1 
ATOM   4650 C CD2 . PHE B 1 284 ? -8.469  5.774   33.833 1.00 23.67  ? 300 PHE B CD2 1 
ATOM   4651 C CE1 . PHE B 1 284 ? -7.973  8.161   32.589 1.00 20.80  ? 300 PHE B CE1 1 
ATOM   4652 C CE2 . PHE B 1 284 ? -7.609  6.701   34.417 1.00 21.43  ? 300 PHE B CE2 1 
ATOM   4653 C CZ  . PHE B 1 284 ? -7.348  7.890   33.786 1.00 21.73  ? 300 PHE B CZ  1 
ATOM   4654 N N   . ILE B 1 285 ? -11.908 4.558   34.321 1.00 24.78  ? 301 ILE B N   1 
ATOM   4655 C CA  . ILE B 1 285 ? -12.283 4.618   35.724 1.00 24.38  ? 301 ILE B CA  1 
ATOM   4656 C C   . ILE B 1 285 ? -11.157 4.024   36.576 1.00 25.62  ? 301 ILE B C   1 
ATOM   4657 O O   . ILE B 1 285 ? -10.592 2.985   36.220 1.00 27.43  ? 301 ILE B O   1 
ATOM   4658 C CB  . ILE B 1 285 ? -13.639 3.913   35.922 1.00 24.84  ? 301 ILE B CB  1 
ATOM   4659 C CG1 . ILE B 1 285 ? -14.759 4.574   35.101 1.00 23.91  ? 301 ILE B CG1 1 
ATOM   4660 C CG2 . ILE B 1 285 ? -14.013 3.851   37.387 1.00 26.36  ? 301 ILE B CG2 1 
ATOM   4661 C CD1 . ILE B 1 285 ? -15.917 3.660   34.803 1.00 23.99  ? 301 ILE B CD1 1 
ATOM   4662 N N   . GLU B 1 286 ? -10.832 4.705   37.689 1.00 23.77  ? 302 GLU B N   1 
ATOM   4663 C CA  . GLU B 1 286 ? -9.779  4.293   38.610 1.00 23.89  ? 302 GLU B CA  1 
ATOM   4664 C C   . GLU B 1 286 ? -10.270 4.483   40.035 1.00 24.51  ? 302 GLU B C   1 
ATOM   4665 O O   . GLU B 1 286 ? -11.170 5.292   40.272 1.00 24.57  ? 302 GLU B O   1 
ATOM   4666 C CB  . GLU B 1 286 ? -8.494  5.103   38.436 1.00 23.46  ? 302 GLU B CB  1 
ATOM   4667 C CG  . GLU B 1 286 ? -8.667  6.604   38.666 1.00 22.72  ? 302 GLU B CG  1 
ATOM   4668 C CD  . GLU B 1 286 ? -7.381  7.390   38.560 1.00 24.84  ? 302 GLU B CD  1 
ATOM   4669 O OE1 . GLU B 1 286 ? -6.312  6.743   38.611 1.00 25.09  ? 302 GLU B OE1 1 
ATOM   4670 O OE2 . GLU B 1 286 ? -7.445  8.653   38.427 1.00 23.36  ? 302 GLU B OE2 1 
ATOM   4671 N N   . ASP B 1 287 ? -9.692  3.717   40.970 1.00 25.03  ? 303 ASP B N   1 
ATOM   4672 C CA  . ASP B 1 287 ? -9.853  4.006   42.392 1.00 25.75  ? 303 ASP B CA  1 
ATOM   4673 C C   . ASP B 1 287 ? -8.872  5.125   42.735 1.00 27.21  ? 303 ASP B C   1 
ATOM   4674 O O   . ASP B 1 287 ? -8.237  5.655   41.831 1.00 24.99  ? 303 ASP B O   1 
ATOM   4675 C CB  . ASP B 1 287 ? -9.696  2.764   43.280 1.00 27.19  ? 303 ASP B CB  1 
ATOM   4676 C CG  . ASP B 1 287 ? -8.315  2.123   43.311 1.00 28.88  ? 303 ASP B CG  1 
ATOM   4677 O OD1 . ASP B 1 287 ? -7.304  2.813   43.040 1.00 23.19  ? 303 ASP B OD1 1 
ATOM   4678 O OD2 . ASP B 1 287 ? -8.273  0.899   43.559 1.00 33.55  ? 303 ASP B OD2 1 
ATOM   4679 N N   . LEU B 1 288 ? -8.777  5.495   44.018 1.00 27.09  ? 304 LEU B N   1 
ATOM   4680 C CA  . LEU B 1 288 ? -7.916  6.593   44.425 1.00 29.80  ? 304 LEU B CA  1 
ATOM   4681 C C   . LEU B 1 288 ? -6.769  6.111   45.314 1.00 30.49  ? 304 LEU B C   1 
ATOM   4682 O O   . LEU B 1 288 ? -6.255  6.867   46.123 1.00 29.41  ? 304 LEU B O   1 
ATOM   4683 C CB  . LEU B 1 288 ? -8.769  7.664   45.111 1.00 31.30  ? 304 LEU B CB  1 
ATOM   4684 C CG  . LEU B 1 288 ? -9.609  8.516   44.157 1.00 33.32  ? 304 LEU B CG  1 
ATOM   4685 C CD1 . LEU B 1 288 ? -10.291 9.626   44.916 1.00 36.80  ? 304 LEU B CD1 1 
ATOM   4686 C CD2 . LEU B 1 288 ? -8.760  9.118   43.037 1.00 32.65  ? 304 LEU B CD2 1 
ATOM   4687 N N   . GLU B 1 289 ? -6.289  4.892   45.082 1.00 31.89  ? 305 GLU B N   1 
ATOM   4688 C CA  . GLU B 1 289 ? -5.042  4.462   45.698 1.00 35.56  ? 305 GLU B CA  1 
ATOM   4689 C C   . GLU B 1 289 ? -3.895  5.400   45.302 1.00 30.88  ? 305 GLU B C   1 
ATOM   4690 O O   . GLU B 1 289 ? -3.657  5.648   44.103 1.00 28.53  ? 305 GLU B O   1 
ATOM   4691 C CB  . GLU B 1 289 ? -4.732  3.030   45.258 1.00 41.05  ? 305 GLU B CB  1 
ATOM   4692 C CG  . GLU B 1 289 ? -3.486  2.445   45.909 1.00 49.22  ? 305 GLU B CG  1 
ATOM   4693 C CD  . GLU B 1 289 ? -2.967  1.176   45.249 1.00 54.11  ? 305 GLU B CD  1 
ATOM   4694 O OE1 . GLU B 1 289 ? -3.421  0.862   44.116 1.00 58.48  ? 305 GLU B OE1 1 
ATOM   4695 O OE2 . GLU B 1 289 ? -2.123  0.492   45.877 1.00 56.97  ? 305 GLU B OE2 1 
ATOM   4696 N N   . ASP B 1 290 ? -3.163  5.874   46.323 1.00 29.32  ? 306 ASP B N   1 
ATOM   4697 C CA  . ASP B 1 290 ? -2.057  6.812   46.187 1.00 32.99  ? 306 ASP B CA  1 
ATOM   4698 C C   . ASP B 1 290 ? -2.583  8.185   45.771 1.00 35.19  ? 306 ASP B C   1 
ATOM   4699 O O   . ASP B 1 290 ? -2.233  9.194   46.386 1.00 39.88  ? 306 ASP B O   1 
ATOM   4700 C CB  . ASP B 1 290 ? -0.956  6.340   45.232 1.00 36.72  ? 306 ASP B CB  1 
ATOM   4701 C CG  . ASP B 1 290 ? -0.342  4.997   45.594 1.00 41.18  ? 306 ASP B CG  1 
ATOM   4702 O OD1 . ASP B 1 290 ? 0.159   4.864   46.731 1.00 36.63  ? 306 ASP B OD1 1 
ATOM   4703 O OD2 . ASP B 1 290 ? -0.385  4.087   44.729 1.00 37.99  ? 306 ASP B OD2 1 
ATOM   4704 N N   . GLY B 1 291 ? -3.405  8.238   44.714 1.00 31.35  ? 307 GLY B N   1 
ATOM   4705 C CA  . GLY B 1 291 ? -4.119  9.467   44.411 1.00 29.20  ? 307 GLY B CA  1 
ATOM   4706 C C   . GLY B 1 291 ? -4.863  9.424   43.078 1.00 27.25  ? 307 GLY B C   1 
ATOM   4707 O O   . GLY B 1 291 ? -5.054  8.363   42.492 1.00 25.94  ? 307 GLY B O   1 
ATOM   4708 N N   . LEU B 1 292 ? -5.282  10.608  42.632 1.00 23.50  ? 308 LEU B N   1 
ATOM   4709 C CA  . LEU B 1 292 ? -5.964  10.762  41.355 1.00 25.88  ? 308 LEU B CA  1 
ATOM   4710 C C   . LEU B 1 292 ? -4.926  10.942  40.246 1.00 24.18  ? 308 LEU B C   1 
ATOM   4711 O O   . LEU B 1 292 ? -3.967  11.702  40.408 1.00 22.85  ? 308 LEU B O   1 
ATOM   4712 C CB  . LEU B 1 292 ? -6.871  11.994  41.466 1.00 24.40  ? 308 LEU B CB  1 
ATOM   4713 C CG  . LEU B 1 292 ? -7.571  12.450  40.197 1.00 24.76  ? 308 LEU B CG  1 
ATOM   4714 C CD1 . LEU B 1 292 ? -8.680  11.485  39.838 1.00 24.33  ? 308 LEU B CD1 1 
ATOM   4715 C CD2 . LEU B 1 292 ? -8.156  13.850  40.388 1.00 25.98  ? 308 LEU B CD2 1 
ATOM   4716 N N   . SER B 1 293 ? -5.140  10.259  39.122 1.00 25.47  ? 309 SER B N   1 
ATOM   4717 C CA  . SER B 1 293 ? -4.386  10.509  37.895 1.00 23.84  ? 309 SER B CA  1 
ATOM   4718 C C   . SER B 1 293 ? -4.791  11.863  37.318 1.00 22.29  ? 309 SER B C   1 
ATOM   4719 O O   . SER B 1 293 ? -5.933  12.003  36.888 1.00 22.34  ? 309 SER B O   1 
ATOM   4720 C CB  . SER B 1 293 ? -4.634  9.402   36.909 1.00 24.33  ? 309 SER B CB  1 
ATOM   4721 O OG  . SER B 1 293 ? -4.251  8.159   37.458 1.00 23.40  ? 309 SER B OG  1 
ATOM   4722 N N   . VAL B 1 294 ? -3.903  12.868  37.394 1.00 21.84  ? 310 VAL B N   1 
ATOM   4723 C CA  . VAL B 1 294 ? -4.214  14.211  36.897 1.00 24.05  ? 310 VAL B CA  1 
ATOM   4724 C C   . VAL B 1 294 ? -3.656  14.449  35.487 1.00 22.33  ? 310 VAL B C   1 
ATOM   4725 O O   . VAL B 1 294 ? -3.880  15.525  34.936 1.00 22.38  ? 310 VAL B O   1 
ATOM   4726 C CB  . VAL B 1 294 ? -3.758  15.325  37.863 1.00 25.25  ? 310 VAL B CB  1 
ATOM   4727 C CG1 . VAL B 1 294 ? -4.587  15.301  39.141 1.00 24.12  ? 310 VAL B CG1 1 
ATOM   4728 C CG2 . VAL B 1 294 ? -2.266  15.298  38.174 1.00 25.65  ? 310 VAL B CG2 1 
ATOM   4729 N N   . GLY B 1 295 ? -2.971  13.443  34.903 1.00 22.68  ? 311 GLY B N   1 
ATOM   4730 C CA  . GLY B 1 295 ? -2.397  13.553  33.572 1.00 23.49  ? 311 GLY B CA  1 
ATOM   4731 C C   . GLY B 1 295 ? -0.880  13.679  33.619 1.00 23.81  ? 311 GLY B C   1 
ATOM   4732 O O   . GLY B 1 295 ? -0.309  13.980  34.666 1.00 23.66  ? 311 GLY B O   1 
ATOM   4733 N N   . ASN B 1 296 ? -0.229  13.371  32.504 1.00 24.19  ? 312 ASN B N   1 
ATOM   4734 C CA  . ASN B 1 296 ? 1.178   13.704  32.361 1.00 29.13  ? 312 ASN B CA  1 
ATOM   4735 C C   . ASN B 1 296 ? 2.019   12.874  33.339 1.00 29.07  ? 312 ASN B C   1 
ATOM   4736 O O   . ASN B 1 296 ? 3.048   13.347  33.816 1.00 30.49  ? 312 ASN B O   1 
ATOM   4737 C CB  . ASN B 1 296 ? 1.399   15.211  32.556 1.00 28.13  ? 312 ASN B CB  1 
ATOM   4738 C CG  . ASN B 1 296 ? 0.807   16.056  31.442 1.00 29.89  ? 312 ASN B CG  1 
ATOM   4739 O OD1 . ASN B 1 296 ? 0.004   16.956  31.669 1.00 34.57  ? 312 ASN B OD1 1 
ATOM   4740 N ND2 . ASN B 1 296 ? 1.168   15.740  30.221 1.00 30.99  ? 312 ASN B ND2 1 
ATOM   4741 N N   . LYS B 1 297 ? 1.551   11.669  33.681 1.00 29.44  ? 313 LYS B N   1 
ATOM   4742 C CA  . LYS B 1 297 ? 2.277   10.786  34.588 1.00 34.05  ? 313 LYS B CA  1 
ATOM   4743 C C   . LYS B 1 297 ? 2.359   11.321  36.019 1.00 32.05  ? 313 LYS B C   1 
ATOM   4744 O O   . LYS B 1 297 ? 3.336   11.028  36.726 1.00 30.97  ? 313 LYS B O   1 
ATOM   4745 C CB  . LYS B 1 297 ? 3.721   10.604  34.103 1.00 34.10  ? 313 LYS B CB  1 
ATOM   4746 C CG  . LYS B 1 297 ? 3.871   10.140  32.661 1.00 34.13  ? 313 LYS B CG  1 
ATOM   4747 C CD  . LYS B 1 297 ? 3.121   8.867   32.373 1.00 36.93  ? 313 LYS B CD  1 
ATOM   4748 C CE  . LYS B 1 297 ? 3.520   8.312   31.028 1.00 38.45  ? 313 LYS B CE  1 
ATOM   4749 N NZ  . LYS B 1 297 ? 2.505   7.358   30.566 1.00 39.86  ? 313 LYS B NZ  1 
ATOM   4750 N N   . PHE B 1 298 ? 1.369   12.127  36.428 1.00 28.49  ? 314 PHE B N   1 
ATOM   4751 C CA  . PHE B 1 298 ? 1.352   12.664  37.771 1.00 29.43  ? 314 PHE B CA  1 
ATOM   4752 C C   . PHE B 1 298 ? 0.134   12.132  38.510 1.00 29.94  ? 314 PHE B C   1 
ATOM   4753 O O   . PHE B 1 298 ? -0.927  12.008  37.914 1.00 26.85  ? 314 PHE B O   1 
ATOM   4754 C CB  . PHE B 1 298 ? 1.316   14.193  37.755 1.00 32.99  ? 314 PHE B CB  1 
ATOM   4755 C CG  . PHE B 1 298 ? 2.615   14.878  37.430 1.00 33.94  ? 314 PHE B CG  1 
ATOM   4756 C CD1 . PHE B 1 298 ? 3.668   14.877  38.337 1.00 34.82  ? 314 PHE B CD1 1 
ATOM   4757 C CD2 . PHE B 1 298 ? 2.777   15.569  36.236 1.00 34.66  ? 314 PHE B CD2 1 
ATOM   4758 C CE1 . PHE B 1 298 ? 4.860   15.534  38.046 1.00 33.85  ? 314 PHE B CE1 1 
ATOM   4759 C CE2 . PHE B 1 298 ? 3.956   16.251  35.961 1.00 32.76  ? 314 PHE B CE2 1 
ATOM   4760 C CZ  . PHE B 1 298 ? 5.003   16.213  36.852 1.00 33.45  ? 314 PHE B CZ  1 
ATOM   4761 N N   . ILE B 1 299 ? 0.305   11.847  39.810 1.00 29.59  ? 315 ILE B N   1 
ATOM   4762 C CA  . ILE B 1 299 ? -0.806  11.540  40.696 1.00 30.06  ? 315 ILE B CA  1 
ATOM   4763 C C   . ILE B 1 299 ? -0.899  12.644  41.751 1.00 29.42  ? 315 ILE B C   1 
ATOM   4764 O O   . ILE B 1 299 ? 0.108   13.262  42.108 1.00 27.40  ? 315 ILE B O   1 
ATOM   4765 C CB  . ILE B 1 299 ? -0.662  10.131  41.309 1.00 34.31  ? 315 ILE B CB  1 
ATOM   4766 C CG1 . ILE B 1 299 ? 0.617   10.001  42.132 1.00 38.94  ? 315 ILE B CG1 1 
ATOM   4767 C CG2 . ILE B 1 299 ? -0.712  9.053   40.224 1.00 35.30  ? 315 ILE B CG2 1 
ATOM   4768 C CD1 . ILE B 1 299 ? 0.664   8.759   42.990 1.00 44.75  ? 315 ILE B CD1 1 
ATOM   4769 N N   . GLN B 1 300 ? -2.133  12.933  42.194 1.00 27.48  ? 316 GLN B N   1 
ATOM   4770 C CA  . GLN B 1 300 ? -2.379  13.951  43.200 1.00 28.51  ? 316 GLN B CA  1 
ATOM   4771 C C   . GLN B 1 300 ? -3.185  13.310  44.324 1.00 30.26  ? 316 GLN B C   1 
ATOM   4772 O O   . GLN B 1 300 ? -4.231  12.716  44.102 1.00 28.42  ? 316 GLN B O   1 
ATOM   4773 C CB  . GLN B 1 300 ? -3.064  15.193  42.608 1.00 26.89  ? 316 GLN B CB  1 
ATOM   4774 C CG  . GLN B 1 300 ? -3.371  16.292  43.637 1.00 26.41  ? 316 GLN B CG  1 
ATOM   4775 C CD  . GLN B 1 300 ? -3.710  17.633  43.023 1.00 28.12  ? 316 GLN B CD  1 
ATOM   4776 O OE1 . GLN B 1 300 ? -3.406  17.915  41.866 1.00 29.33  ? 316 GLN B OE1 1 
ATOM   4777 N NE2 . GLN B 1 300 ? -4.308  18.508  43.807 1.00 27.93  ? 316 GLN B NE2 1 
ATOM   4778 N N   . GLU B 1 301 ? -2.675  13.468  45.544 1.00 34.52  ? 317 GLU B N   1 
ATOM   4779 C CA  . GLU B 1 301 ? -3.314  12.945  46.737 1.00 38.42  ? 317 GLU B CA  1 
ATOM   4780 C C   . GLU B 1 301 ? -4.615  13.712  46.930 1.00 38.40  ? 317 GLU B C   1 
ATOM   4781 O O   . GLU B 1 301 ? -4.617  14.935  46.801 1.00 33.75  ? 317 GLU B O   1 
ATOM   4782 C CB  . GLU B 1 301 ? -2.350  13.110  47.921 1.00 46.52  ? 317 GLU B CB  1 
ATOM   4783 C CG  . GLU B 1 301 ? -2.299  11.915  48.856 1.00 57.27  ? 317 GLU B CG  1 
ATOM   4784 C CD  . GLU B 1 301 ? -1.209  11.994  49.918 1.00 63.10  ? 317 GLU B CD  1 
ATOM   4785 O OE1 . GLU B 1 301 ? -0.003  11.964  49.550 1.00 58.18  ? 317 GLU B OE1 1 
ATOM   4786 O OE2 . GLU B 1 301 ? -1.565  12.088  51.111 1.00 68.37  ? 317 GLU B OE2 1 
ATOM   4787 N N   . VAL B 1 302 ? -5.710  12.985  47.207 1.00 39.54  ? 318 VAL B N   1 
ATOM   4788 C CA  . VAL B 1 302 ? -7.018  13.590  47.387 1.00 44.70  ? 318 VAL B CA  1 
ATOM   4789 C C   . VAL B 1 302 ? -7.462  13.340  48.831 1.00 46.32  ? 318 VAL B C   1 
ATOM   4790 O O   . VAL B 1 302 ? -7.624  12.158  49.152 1.00 44.63  ? 318 VAL B O   1 
ATOM   4791 C CB  . VAL B 1 302 ? -8.049  13.032  46.382 1.00 48.49  ? 318 VAL B CB  1 
ATOM   4792 C CG1 . VAL B 1 302 ? -9.384  13.774  46.457 1.00 49.07  ? 318 VAL B CG1 1 
ATOM   4793 C CG2 . VAL B 1 302 ? -7.515  13.039  44.957 1.00 48.32  ? 318 VAL B CG2 1 
HETATM 4794 C C1  . PEG C 2 .   ? 19.974  -17.412 55.976 1.00 56.34  ? 401 PEG A C1  1 
HETATM 4795 O O1  . PEG C 2 .   ? 19.043  -16.930 56.909 1.00 49.45  ? 401 PEG A O1  1 
HETATM 4796 C C2  . PEG C 2 .   ? 19.605  -18.770 55.476 1.00 59.24  ? 401 PEG A C2  1 
HETATM 4797 O O2  . PEG C 2 .   ? 19.667  -19.710 56.547 1.00 58.31  ? 401 PEG A O2  1 
HETATM 4798 C C3  . PEG C 2 .   ? 20.547  -20.806 56.295 1.00 49.65  ? 401 PEG A C3  1 
HETATM 4799 C C4  . PEG C 2 .   ? 20.376  -21.840 57.361 1.00 51.43  ? 401 PEG A C4  1 
HETATM 4800 O O4  . PEG C 2 .   ? 21.565  -22.593 57.611 1.00 53.53  ? 401 PEG A O4  1 
HETATM 4801 C C1  . PEG D 2 .   ? -29.323 7.055   9.467  1.00 53.70  ? 401 PEG B C1  1 
HETATM 4802 O O1  . PEG D 2 .   ? -30.558 7.759   9.319  1.00 55.59  ? 401 PEG B O1  1 
HETATM 4803 C C2  . PEG D 2 .   ? -28.477 7.641   10.549 1.00 51.26  ? 401 PEG B C2  1 
HETATM 4804 O O2  . PEG D 2 .   ? -27.191 7.030   10.554 1.00 57.19  ? 401 PEG B O2  1 
HETATM 4805 C C3  . PEG D 2 .   ? -26.204 7.767   9.839  1.00 55.35  ? 401 PEG B C3  1 
HETATM 4806 C C4  . PEG D 2 .   ? -25.162 8.268   10.782 1.00 53.47  ? 401 PEG B C4  1 
HETATM 4807 O O4  . PEG D 2 .   ? -23.884 8.180   10.212 1.00 49.21  ? 401 PEG B O4  1 
HETATM 4808 O O   . HOH E 3 .   ? 22.753  -24.415 24.851 1.00 36.82  ? 501 HOH A O   1 
HETATM 4809 O O   . HOH E 3 .   ? 27.076  -33.018 38.088 1.00 30.38  ? 502 HOH A O   1 
HETATM 4810 O O   . HOH E 3 .   ? 34.182  -31.309 47.558 1.00 29.85  ? 503 HOH A O   1 
HETATM 4811 O O   . HOH E 3 .   ? 25.364  -22.395 35.752 1.00 27.57  ? 504 HOH A O   1 
HETATM 4812 O O   . HOH E 3 .   ? 36.410  -17.227 50.977 1.00 27.96  ? 505 HOH A O   1 
HETATM 4813 O O   . HOH E 3 .   ? 11.722  -2.079  49.713 1.00 28.58  ? 506 HOH A O   1 
HETATM 4814 O O   . HOH E 3 .   ? 5.208   -16.684 55.360 1.00 33.94  ? 507 HOH A O   1 
HETATM 4815 O O   . HOH E 3 .   ? 29.434  0.962   38.626 1.00 28.89  ? 508 HOH A O   1 
HETATM 4816 O O   . HOH E 3 .   ? 2.898   -5.215  22.323 1.00 35.51  ? 509 HOH A O   1 
HETATM 4817 O O   . HOH E 3 .   ? 10.760  -5.358  43.426 1.00 27.38  ? 510 HOH A O   1 
HETATM 4818 O O   . HOH E 3 .   ? 20.780  4.667   45.486 1.00 31.04  ? 511 HOH A O   1 
HETATM 4819 O O   . HOH E 3 .   ? 8.096   4.031   18.664 1.00 41.36  ? 512 HOH A O   1 
HETATM 4820 O O   . HOH E 3 .   ? 11.786  4.388   44.755 1.00 45.46  ? 513 HOH A O   1 
HETATM 4821 O O   . HOH E 3 .   ? -0.014  -13.223 43.318 1.00 31.97  ? 514 HOH A O   1 
HETATM 4822 O O   . HOH E 3 .   ? 32.753  -17.488 50.575 1.00 21.85  ? 515 HOH A O   1 
HETATM 4823 O O   . HOH E 3 .   ? 18.302  -29.862 49.533 1.00 33.80  ? 516 HOH A O   1 
HETATM 4824 O O   . HOH E 3 .   ? 10.840  1.364   40.961 1.00 22.66  ? 517 HOH A O   1 
HETATM 4825 O O   . HOH E 3 .   ? 38.810  -10.066 35.223 1.00 38.18  ? 518 HOH A O   1 
HETATM 4826 O O   . HOH E 3 .   ? 37.008  -33.339 49.822 1.00 47.51  ? 519 HOH A O   1 
HETATM 4827 O O   . HOH E 3 .   ? 14.961  -25.200 26.488 1.00 30.16  ? 520 HOH A O   1 
HETATM 4828 O O   . HOH E 3 .   ? 33.159  -9.622  50.922 1.00 37.28  ? 521 HOH A O   1 
HETATM 4829 O O   . HOH E 3 .   ? 7.244   -21.319 48.456 1.00 33.66  ? 522 HOH A O   1 
HETATM 4830 O O   . HOH E 3 .   ? 15.015  -2.199  36.629 1.00 18.98  ? 523 HOH A O   1 
HETATM 4831 O O   . HOH E 3 .   ? 9.981   -13.386 53.256 1.00 44.28  ? 524 HOH A O   1 
HETATM 4832 O O   . HOH E 3 .   ? 21.185  8.206   31.941 1.00 32.62  ? 525 HOH A O   1 
HETATM 4833 O O   . HOH E 3 .   ? 20.442  -7.002  54.745 1.00 30.20  ? 526 HOH A O   1 
HETATM 4834 O O   . HOH E 3 .   ? 10.419  -17.893 33.611 1.00 25.42  ? 527 HOH A O   1 
HETATM 4835 O O   . HOH E 3 .   ? 29.244  -15.150 48.575 1.00 27.50  ? 528 HOH A O   1 
HETATM 4836 O O   . HOH E 3 .   ? 1.862   -19.590 26.637 1.00 48.60  ? 529 HOH A O   1 
HETATM 4837 O O   . HOH E 3 .   ? 18.409  -7.658  17.062 1.00 30.68  ? 530 HOH A O   1 
HETATM 4838 O O   . HOH E 3 .   ? 25.014  -1.293  45.245 1.00 25.94  ? 531 HOH A O   1 
HETATM 4839 O O   . HOH E 3 .   ? 26.814  -16.893 22.071 1.00 33.72  ? 532 HOH A O   1 
HETATM 4840 O O   . HOH E 3 .   ? 24.579  -8.609  59.427 1.00 32.77  ? 533 HOH A O   1 
HETATM 4841 O O   . HOH E 3 .   ? 29.324  -22.088 23.889 1.00 42.95  ? 534 HOH A O   1 
HETATM 4842 O O   . HOH E 3 .   ? 31.343  1.030   46.779 1.00 36.84  ? 535 HOH A O   1 
HETATM 4843 O O   . HOH E 3 .   ? 22.194  -33.305 41.364 1.00 20.76  ? 536 HOH A O   1 
HETATM 4844 O O   . HOH E 3 .   ? 30.009  1.677   33.976 1.00 31.89  ? 537 HOH A O   1 
HETATM 4845 O O   . HOH E 3 .   ? 36.650  -13.098 51.195 1.00 22.59  ? 538 HOH A O   1 
HETATM 4846 O O   . HOH E 3 .   ? 38.718  -16.223 38.606 1.00 25.09  ? 539 HOH A O   1 
HETATM 4847 O O   . HOH E 3 .   ? 25.233  -7.716  47.994 1.00 26.28  ? 540 HOH A O   1 
HETATM 4848 O O   . HOH E 3 .   ? 13.990  -28.845 45.706 1.00 40.42  ? 541 HOH A O   1 
HETATM 4849 O O   . HOH E 3 .   ? 12.842  -20.727 42.119 1.00 24.06  ? 542 HOH A O   1 
HETATM 4850 O O   . HOH E 3 .   ? 12.569  -26.608 46.743 1.00 37.29  ? 543 HOH A O   1 
HETATM 4851 O O   . HOH E 3 .   ? 29.923  -25.519 54.578 1.00 38.26  ? 544 HOH A O   1 
HETATM 4852 O O   . HOH E 3 .   ? 41.609  -26.462 47.266 1.00 32.58  ? 545 HOH A O   1 
HETATM 4853 O O   . HOH E 3 .   ? 34.931  -28.473 42.655 1.00 24.87  ? 546 HOH A O   1 
HETATM 4854 O O   . HOH E 3 .   ? 40.892  -28.500 51.320 1.00 38.15  ? 547 HOH A O   1 
HETATM 4855 O O   . HOH E 3 .   ? 4.723   -2.933  38.746 1.00 31.35  ? 548 HOH A O   1 
HETATM 4856 O O   . HOH E 3 .   ? 17.914  0.965   54.869 1.00 38.75  ? 549 HOH A O   1 
HETATM 4857 O O   . HOH E 3 .   ? 32.188  -11.879 37.646 1.00 20.00  ? 550 HOH A O   1 
HETATM 4858 O O   . HOH E 3 .   ? 36.810  -30.027 44.285 1.00 27.93  ? 551 HOH A O   1 
HETATM 4859 O O   . HOH E 3 .   ? 9.034   -24.929 50.081 1.00 43.11  ? 552 HOH A O   1 
HETATM 4860 O O   . HOH E 3 .   ? 14.906  -23.301 34.610 1.00 37.37  ? 553 HOH A O   1 
HETATM 4861 O O   . HOH E 3 .   ? 28.164  -21.935 26.211 1.00 45.79  ? 554 HOH A O   1 
HETATM 4862 O O   . HOH E 3 .   ? 27.034  -10.780 57.701 1.00 31.36  ? 555 HOH A O   1 
HETATM 4863 O O   . HOH E 3 .   ? 40.343  -19.602 40.201 1.00 25.61  ? 556 HOH A O   1 
HETATM 4864 O O   . HOH E 3 .   ? 25.348  -16.607 29.702 1.00 24.42  ? 557 HOH A O   1 
HETATM 4865 O O   . HOH E 3 .   ? 6.903   -5.734  53.330 1.00 36.19  ? 558 HOH A O   1 
HETATM 4866 O O   . HOH E 3 .   ? 30.543  -28.689 48.779 1.00 32.18  ? 559 HOH A O   1 
HETATM 4867 O O   . HOH E 3 .   ? 6.386   7.175   28.234 1.00 32.10  ? 560 HOH A O   1 
HETATM 4868 O O   . HOH E 3 .   ? 8.444   0.276   48.751 1.00 37.44  ? 561 HOH A O   1 
HETATM 4869 O O   . HOH E 3 .   ? 19.046  6.520   26.981 1.00 25.47  ? 562 HOH A O   1 
HETATM 4870 O O   . HOH E 3 .   ? 9.409   6.922   37.184 1.00 38.85  ? 563 HOH A O   1 
HETATM 4871 O O   . HOH E 3 .   ? 36.168  -18.285 42.039 1.00 22.38  ? 564 HOH A O   1 
HETATM 4872 O O   . HOH E 3 .   ? 9.618   -19.584 31.626 1.00 42.33  ? 565 HOH A O   1 
HETATM 4873 O O   . HOH E 3 .   ? 28.304  4.313   41.941 1.00 35.78  ? 566 HOH A O   1 
HETATM 4874 O O   . HOH E 3 .   ? 1.329   -19.248 52.170 1.00 25.78  ? 567 HOH A O   1 
HETATM 4875 O O   . HOH E 3 .   ? 31.283  -3.229  27.285 1.00 32.75  ? 568 HOH A O   1 
HETATM 4876 O O   . HOH E 3 .   ? 33.251  -26.998 35.715 1.00 33.34  ? 569 HOH A O   1 
HETATM 4877 O O   . HOH E 3 .   ? 42.993  -14.070 38.733 1.00 42.05  ? 570 HOH A O   1 
HETATM 4878 O O   . HOH E 3 .   ? 36.447  -9.490  33.203 1.00 29.41  ? 571 HOH A O   1 
HETATM 4879 O O   . HOH E 3 .   ? 1.942   -11.983 29.639 1.00 36.28  ? 572 HOH A O   1 
HETATM 4880 O O   . HOH E 3 .   ? 21.260  0.942   20.178 1.00 34.83  ? 573 HOH A O   1 
HETATM 4881 O O   . HOH E 3 .   ? 5.557   -2.670  51.215 1.00 37.79  ? 574 HOH A O   1 
HETATM 4882 O O   . HOH E 3 .   ? 44.368  -16.044 46.739 1.00 31.20  ? 575 HOH A O   1 
HETATM 4883 O O   . HOH E 3 .   ? 35.931  -19.788 50.157 1.00 25.47  ? 576 HOH A O   1 
HETATM 4884 O O   . HOH E 3 .   ? 2.941   -13.351 36.968 1.00 22.89  ? 577 HOH A O   1 
HETATM 4885 O O   . HOH E 3 .   ? 2.557   -5.050  35.604 1.00 34.30  ? 578 HOH A O   1 
HETATM 4886 O O   . HOH E 3 .   ? 8.760   -6.282  20.530 1.00 34.02  ? 579 HOH A O   1 
HETATM 4887 O O   . HOH E 3 .   ? 29.165  -20.332 50.669 1.00 26.39  ? 580 HOH A O   1 
HETATM 4888 O O   . HOH E 3 .   ? 30.409  -36.323 39.966 1.00 34.35  ? 581 HOH A O   1 
HETATM 4889 O O   . HOH E 3 .   ? 35.135  -12.324 27.689 1.00 33.36  ? 582 HOH A O   1 
HETATM 4890 O O   . HOH E 3 .   ? 26.915  -21.718 52.812 1.00 31.83  ? 583 HOH A O   1 
HETATM 4891 O O   . HOH E 3 .   ? 30.361  -38.116 41.688 1.00 28.40  ? 584 HOH A O   1 
HETATM 4892 O O   . HOH E 3 .   ? 21.108  10.887  33.232 1.00 43.63  ? 585 HOH A O   1 
HETATM 4893 O O   . HOH E 3 .   ? 24.949  -1.160  49.410 1.00 30.16  ? 586 HOH A O   1 
HETATM 4894 O O   . HOH E 3 .   ? 18.597  10.118  33.005 1.00 36.26  ? 587 HOH A O   1 
HETATM 4895 O O   . HOH E 3 .   ? 5.343   4.311   18.624 1.00 38.34  ? 588 HOH A O   1 
HETATM 4896 O O   . HOH E 3 .   ? 30.634  -7.915  48.645 1.00 33.43  ? 589 HOH A O   1 
HETATM 4897 O O   . HOH E 3 .   ? 6.392   -0.488  17.973 1.00 47.92  ? 590 HOH A O   1 
HETATM 4898 O O   . HOH E 3 .   ? 13.440  -17.771 48.480 1.00 25.73  ? 591 HOH A O   1 
HETATM 4899 O O   . HOH E 3 .   ? 10.275  4.021   31.421 1.00 20.07  ? 592 HOH A O   1 
HETATM 4900 O O   . HOH E 3 .   ? 33.207  -15.286 31.626 1.00 25.03  ? 593 HOH A O   1 
HETATM 4901 O O   . HOH E 3 .   ? 38.696  -22.930 42.193 1.00 25.32  ? 594 HOH A O   1 
HETATM 4902 O O   . HOH E 3 .   ? 12.991  -29.893 43.737 1.00 44.81  ? 595 HOH A O   1 
HETATM 4903 O O   . HOH E 3 .   ? 8.142   -1.935  55.771 1.00 43.53  ? 596 HOH A O   1 
HETATM 4904 O O   . HOH E 3 .   ? 41.304  -17.113 39.444 1.00 28.47  ? 597 HOH A O   1 
HETATM 4905 O O   . HOH E 3 .   ? 18.359  -21.582 49.462 1.00 21.77  ? 598 HOH A O   1 
HETATM 4906 O O   . HOH E 3 .   ? 40.757  -31.922 38.198 1.00 31.98  ? 599 HOH A O   1 
HETATM 4907 O O   . HOH E 3 .   ? 30.149  -18.754 34.133 1.00 33.56  ? 600 HOH A O   1 
HETATM 4908 O O   . HOH E 3 .   ? 12.864  -10.126 16.270 1.00 39.50  ? 601 HOH A O   1 
HETATM 4909 O O   . HOH E 3 .   ? 25.066  -22.577 33.010 1.00 24.31  ? 602 HOH A O   1 
HETATM 4910 O O   . HOH E 3 .   ? 33.724  -20.140 35.579 1.00 28.29  ? 603 HOH A O   1 
HETATM 4911 O O   . HOH E 3 .   ? 27.878  -7.839  49.009 1.00 32.34  ? 604 HOH A O   1 
HETATM 4912 O O   . HOH E 3 .   ? 4.816   -3.730  41.531 1.00 33.67  ? 605 HOH A O   1 
HETATM 4913 O O   . HOH E 3 .   ? 15.822  -28.284 47.473 1.00 31.99  ? 606 HOH A O   1 
HETATM 4914 O O   . HOH E 3 .   ? 33.541  -13.300 33.585 1.00 24.14  ? 607 HOH A O   1 
HETATM 4915 O O   . HOH E 3 .   ? 9.406   -10.804 53.761 1.00 39.27  ? 608 HOH A O   1 
HETATM 4916 O O   . HOH E 3 .   ? 15.837  -1.812  34.103 1.00 19.69  ? 609 HOH A O   1 
HETATM 4917 O O   . HOH E 3 .   ? 19.374  -7.845  21.012 1.00 23.44  ? 610 HOH A O   1 
HETATM 4918 O O   . HOH E 3 .   ? 28.958  -13.808 55.796 1.00 31.80  ? 611 HOH A O   1 
HETATM 4919 O O   . HOH E 3 .   ? 33.787  -19.761 42.353 1.00 23.99  ? 612 HOH A O   1 
HETATM 4920 O O   . HOH E 3 .   ? 32.508  -16.638 53.448 1.00 21.96  ? 613 HOH A O   1 
HETATM 4921 O O   . HOH E 3 .   ? 34.015  -16.981 26.617 1.00 44.43  ? 614 HOH A O   1 
HETATM 4922 O O   . HOH E 3 .   ? 10.676  -37.846 42.874 1.00 43.40  ? 615 HOH A O   1 
HETATM 4923 O O   . HOH E 3 .   ? 9.217   4.642   34.442 1.00 36.95  ? 616 HOH A O   1 
HETATM 4924 O O   . HOH E 3 .   ? 8.293   -9.811  21.697 1.00 35.19  ? 617 HOH A O   1 
HETATM 4925 O O   . HOH E 3 .   ? 32.809  0.733   36.887 1.00 30.00  ? 618 HOH A O   1 
HETATM 4926 O O   . HOH E 3 .   ? 35.786  -26.791 34.909 1.00 33.15  ? 619 HOH A O   1 
HETATM 4927 O O   . HOH E 3 .   ? 7.056   0.288   34.022 1.00 33.94  ? 620 HOH A O   1 
HETATM 4928 O O   . HOH E 3 .   ? 27.571  -11.594 22.369 1.00 30.94  ? 621 HOH A O   1 
HETATM 4929 O O   . HOH E 3 .   ? 42.457  -25.329 44.884 1.00 41.72  ? 622 HOH A O   1 
HETATM 4930 O O   . HOH E 3 .   ? 24.663  6.137   44.606 1.00 34.16  ? 623 HOH A O   1 
HETATM 4931 O O   . HOH E 3 .   ? 26.429  -19.735 51.440 1.00 33.75  ? 624 HOH A O   1 
HETATM 4932 O O   . HOH E 3 .   ? 34.690  1.973   38.656 1.00 33.42  ? 625 HOH A O   1 
HETATM 4933 O O   . HOH E 3 .   ? 16.963  -36.826 47.108 1.00 36.03  ? 626 HOH A O   1 
HETATM 4934 O O   . HOH E 3 .   ? 27.016  -29.024 51.211 1.00 41.57  ? 627 HOH A O   1 
HETATM 4935 O O   . HOH E 3 .   ? 9.136   2.501   42.543 1.00 26.48  ? 628 HOH A O   1 
HETATM 4936 O O   . HOH E 3 .   ? -0.375  15.360  46.026 1.00 31.70  ? 629 HOH A O   1 
HETATM 4937 O O   . HOH E 3 .   ? 35.119  -10.235 48.470 1.00 32.54  ? 630 HOH A O   1 
HETATM 4938 O O   . HOH E 3 .   ? 5.870   -16.377 45.091 1.00 24.28  ? 631 HOH A O   1 
HETATM 4939 O O   . HOH E 3 .   ? 36.586  1.894   43.802 1.00 34.25  ? 632 HOH A O   1 
HETATM 4940 O O   . HOH E 3 .   ? 18.279  -26.629 25.837 1.00 42.67  ? 633 HOH A O   1 
HETATM 4941 O O   . HOH E 3 .   ? 12.128  -18.268 26.821 1.00 37.90  ? 634 HOH A O   1 
HETATM 4942 O O   . HOH E 3 .   ? 22.640  -25.868 45.942 1.00 22.84  ? 635 HOH A O   1 
HETATM 4943 O O   . HOH E 3 .   ? 20.549  -13.837 21.966 1.00 27.00  ? 636 HOH A O   1 
HETATM 4944 O O   . HOH E 3 .   ? 21.382  -31.651 39.699 1.00 30.89  ? 637 HOH A O   1 
HETATM 4945 O O   . HOH E 3 .   ? 25.842  -20.716 29.030 1.00 24.87  ? 638 HOH A O   1 
HETATM 4946 O O   . HOH E 3 .   ? 8.341   -22.484 50.766 1.00 29.17  ? 639 HOH A O   1 
HETATM 4947 O O   . HOH E 3 .   ? 26.692  -18.383 33.479 1.00 31.60  ? 640 HOH A O   1 
HETATM 4948 O O   . HOH E 3 .   ? 23.961  6.284   35.372 1.00 19.71  ? 641 HOH A O   1 
HETATM 4949 O O   . HOH E 3 .   ? 43.281  -26.145 42.217 1.00 31.47  ? 642 HOH A O   1 
HETATM 4950 O O   . HOH E 3 .   ? 11.995  -6.712  41.235 1.00 21.23  ? 643 HOH A O   1 
HETATM 4951 O O   . HOH E 3 .   ? 28.239  -22.582 35.472 1.00 30.60  ? 644 HOH A O   1 
HETATM 4952 O O   . HOH E 3 .   ? 13.296  -19.369 46.266 1.00 29.37  ? 645 HOH A O   1 
HETATM 4953 O O   . HOH E 3 .   ? 25.029  4.209   32.230 1.00 27.73  ? 646 HOH A O   1 
HETATM 4954 O O   . HOH E 3 .   ? 27.350  3.844   26.972 1.00 39.31  ? 647 HOH A O   1 
HETATM 4955 O O   . HOH E 3 .   ? -0.169  -18.147 41.426 1.00 40.00  ? 648 HOH A O   1 
HETATM 4956 O O   . HOH E 3 .   ? 2.604   -1.870  44.680 1.00 34.64  ? 649 HOH A O   1 
HETATM 4957 O O   . HOH E 3 .   ? 32.255  -17.156 33.476 1.00 25.88  ? 650 HOH A O   1 
HETATM 4958 O O   . HOH E 3 .   ? 4.617   -22.430 41.474 1.00 41.14  ? 651 HOH A O   1 
HETATM 4959 O O   . HOH E 3 .   ? 25.861  -34.550 46.535 1.00 25.30  ? 652 HOH A O   1 
HETATM 4960 O O   . HOH E 3 .   ? 18.655  -24.729 37.609 1.00 34.37  ? 653 HOH A O   1 
HETATM 4961 O O   . HOH E 3 .   ? 36.468  -10.845 37.637 1.00 23.56  ? 654 HOH A O   1 
HETATM 4962 O O   . HOH E 3 .   ? 36.112  -33.387 33.694 1.00 45.41  ? 655 HOH A O   1 
HETATM 4963 O O   . HOH E 3 .   ? 28.146  -34.744 46.795 1.00 30.37  ? 656 HOH A O   1 
HETATM 4964 O O   . HOH E 3 .   ? 36.801  -33.224 37.133 1.00 34.45  ? 657 HOH A O   1 
HETATM 4965 O O   . HOH E 3 .   ? 0.459   -3.456  46.469 1.00 34.29  ? 658 HOH A O   1 
HETATM 4966 O O   . HOH E 3 .   ? 30.476  -12.444 54.342 1.00 22.65  ? 659 HOH A O   1 
HETATM 4967 O O   . HOH E 3 .   ? 12.009  -26.322 18.194 1.00 35.59  ? 660 HOH A O   1 
HETATM 4968 O O   . HOH E 3 .   ? 3.403   -10.758 36.101 1.00 31.31  ? 661 HOH A O   1 
HETATM 4969 O O   . HOH E 3 .   ? 32.581  -3.023  29.799 1.00 29.60  ? 662 HOH A O   1 
HETATM 4970 O O   . HOH E 3 .   ? 18.031  1.773   17.483 1.00 41.67  ? 663 HOH A O   1 
HETATM 4971 O O   . HOH E 3 .   ? 28.909  -9.046  56.026 1.00 34.30  ? 664 HOH A O   1 
HETATM 4972 O O   . HOH E 3 .   ? 16.809  4.404   45.464 1.00 31.26  ? 665 HOH A O   1 
HETATM 4973 O O   . HOH E 3 .   ? 24.142  -1.869  17.047 1.00 36.37  ? 666 HOH A O   1 
HETATM 4974 O O   . HOH E 3 .   ? 28.008  -14.950 18.300 1.00 34.54  ? 667 HOH A O   1 
HETATM 4975 O O   . HOH E 3 .   ? 14.942  -17.576 13.763 1.00 41.51  ? 668 HOH A O   1 
HETATM 4976 O O   . HOH E 3 .   ? 20.349  -28.178 53.276 1.00 29.34  ? 669 HOH A O   1 
HETATM 4977 O O   . HOH E 3 .   ? 6.444   -10.194 54.462 1.00 44.39  ? 670 HOH A O   1 
HETATM 4978 O O   . HOH E 3 .   ? 40.908  -5.151  40.056 1.00 41.50  ? 671 HOH A O   1 
HETATM 4979 O O   . HOH E 3 .   ? 6.179   -0.623  38.596 1.00 30.85  ? 672 HOH A O   1 
HETATM 4980 O O   . HOH E 3 .   ? 20.557  -23.024 24.087 1.00 46.32  ? 673 HOH A O   1 
HETATM 4981 O O   . HOH E 3 .   ? 38.276  -20.444 41.285 1.00 21.64  ? 674 HOH A O   1 
HETATM 4982 O O   . HOH E 3 .   ? 19.892  -3.754  15.061 1.00 41.30  ? 675 HOH A O   1 
HETATM 4983 O O   . HOH E 3 .   ? 30.599  3.816   39.451 1.00 37.62  ? 676 HOH A O   1 
HETATM 4984 O O   . HOH E 3 .   ? 17.820  -5.713  18.464 1.00 41.71  ? 677 HOH A O   1 
HETATM 4985 O O   . HOH E 3 .   ? 17.970  3.680   47.429 1.00 38.56  ? 678 HOH A O   1 
HETATM 4986 O O   . HOH E 3 .   ? 33.775  -38.576 37.876 1.00 40.12  ? 679 HOH A O   1 
HETATM 4987 O O   . HOH E 3 .   ? 15.718  -29.302 49.883 1.00 44.78  ? 680 HOH A O   1 
HETATM 4988 O O   . HOH E 3 .   ? 18.745  -5.166  20.739 1.00 44.68  ? 681 HOH A O   1 
HETATM 4989 O O   . HOH E 3 .   ? 6.180   -11.079 23.133 1.00 47.40  ? 682 HOH A O   1 
HETATM 4990 O O   . HOH E 3 .   ? 46.368  -14.724 44.895 1.00 44.16  ? 683 HOH A O   1 
HETATM 4991 O O   . HOH E 3 .   ? 21.182  5.650   25.134 1.00 27.10  ? 684 HOH A O   1 
HETATM 4992 O O   . HOH E 3 .   ? 26.362  -20.474 31.700 1.00 27.83  ? 685 HOH A O   1 
HETATM 4993 O O   . HOH E 3 .   ? 9.732   9.780   37.903 1.00 44.89  ? 686 HOH A O   1 
HETATM 4994 O O   . HOH E 3 .   ? 15.123  -15.923 11.454 1.00 44.39  ? 687 HOH A O   1 
HETATM 4995 O O   . HOH E 3 .   ? 32.240  -36.450 37.561 1.00 33.66  ? 688 HOH A O   1 
HETATM 4996 O O   . HOH E 3 .   ? 6.817   -16.639 57.625 1.00 45.96  ? 689 HOH A O   1 
HETATM 4997 O O   . HOH E 3 .   ? 27.381  -35.796 37.923 1.00 38.58  ? 690 HOH A O   1 
HETATM 4998 O O   . HOH E 3 .   ? 25.786  4.644   34.554 1.00 35.66  ? 691 HOH A O   1 
HETATM 4999 O O   . HOH E 3 .   ? 29.147  -16.356 20.684 1.00 37.05  ? 692 HOH A O   1 
HETATM 5000 O O   . HOH E 3 .   ? 42.350  -17.728 37.133 1.00 39.42  ? 693 HOH A O   1 
HETATM 5001 O O   . HOH E 3 .   ? 6.486   -0.463  50.187 1.00 42.49  ? 694 HOH A O   1 
HETATM 5002 O O   . HOH E 3 .   ? 19.258  -30.092 51.948 1.00 37.47  ? 695 HOH A O   1 
HETATM 5003 O O   . HOH E 3 .   ? 37.658  -12.392 35.768 1.00 28.09  ? 696 HOH A O   1 
HETATM 5004 O O   . HOH E 3 .   ? 21.391  2.566   49.604 1.00 40.47  ? 697 HOH A O   1 
HETATM 5005 O O   . HOH E 3 .   ? 37.860  -10.488 47.089 1.00 35.56  ? 698 HOH A O   1 
HETATM 5006 O O   . HOH E 3 .   ? 35.684  -15.410 31.100 1.00 33.54  ? 699 HOH A O   1 
HETATM 5007 O O   . HOH E 3 .   ? 14.130  9.945   40.605 1.00 33.11  ? 700 HOH A O   1 
HETATM 5008 O O   . HOH E 3 .   ? 24.451  -32.582 37.626 1.00 29.18  ? 701 HOH A O   1 
HETATM 5009 O O   . HOH E 3 .   ? 19.692  -31.579 37.908 1.00 37.47  ? 702 HOH A O   1 
HETATM 5010 O O   . HOH E 3 .   ? 32.511  -13.893 53.209 1.00 26.60  ? 703 HOH A O   1 
HETATM 5011 O O   . HOH E 3 .   ? 14.640  11.949  39.354 1.00 40.13  ? 704 HOH A O   1 
HETATM 5012 O O   . HOH E 3 .   ? 34.257  -19.062 33.454 1.00 24.86  ? 705 HOH A O   1 
HETATM 5013 O O   . HOH E 3 .   ? 18.990  1.393   19.921 1.00 46.77  ? 706 HOH A O   1 
HETATM 5014 O O   . HOH E 3 .   ? 18.386  -15.953 21.652 1.00 30.23  ? 707 HOH A O   1 
HETATM 5015 O O   . HOH E 3 .   ? 7.813   12.991  35.790 1.00 46.45  ? 708 HOH A O   1 
HETATM 5016 O O   . HOH E 3 .   ? 19.573  -7.182  14.491 1.00 45.64  ? 709 HOH A O   1 
HETATM 5017 O O   . HOH E 3 .   ? 1.635   -9.341  37.583 1.00 40.61  ? 710 HOH A O   1 
HETATM 5018 O O   . HOH E 3 .   ? 39.054  -14.799 36.051 1.00 26.13  ? 711 HOH A O   1 
HETATM 5019 O O   . HOH E 3 .   ? 37.697  -8.470  45.205 1.00 38.89  ? 712 HOH A O   1 
HETATM 5020 O O   . HOH E 3 .   ? 23.403  -35.284 37.792 1.00 40.05  ? 713 HOH A O   1 
HETATM 5021 O O   . HOH E 3 .   ? 0.748   -21.908 25.492 1.00 43.43  ? 714 HOH A O   1 
HETATM 5022 O O   . HOH E 3 .   ? 24.749  -35.605 49.025 1.00 24.96  ? 715 HOH A O   1 
HETATM 5023 O O   . HOH E 3 .   ? 35.754  -12.087 33.769 1.00 26.21  ? 716 HOH A O   1 
HETATM 5024 O O   . HOH E 3 .   ? 41.795  -14.382 36.539 1.00 42.10  ? 717 HOH A O   1 
HETATM 5025 O O   . HOH E 3 .   ? 25.264  0.364   17.484 1.00 36.02  ? 718 HOH A O   1 
HETATM 5026 O O   . HOH E 3 .   ? 38.578  -16.504 34.204 1.00 46.46  ? 719 HOH A O   1 
HETATM 5027 O O   . HOH E 3 .   ? 20.170  -37.172 49.951 1.00 31.81  ? 720 HOH A O   1 
HETATM 5028 O O   . HOH E 3 .   ? 29.020  -34.916 51.327 1.00 39.86  ? 721 HOH A O   1 
HETATM 5029 O O   . HOH E 3 .   ? 27.058  -36.686 49.770 1.00 35.31  ? 722 HOH A O   1 
HETATM 5030 O O   . HOH F 3 .   ? -32.421 7.478   41.872 1.00 39.31  ? 501 HOH B O   1 
HETATM 5031 O O   . HOH F 3 .   ? -13.942 11.622  11.265 1.00 39.54  ? 502 HOH B O   1 
HETATM 5032 O O   . HOH F 3 .   ? -14.859 8.548   52.180 1.00 43.81  ? 503 HOH B O   1 
HETATM 5033 O O   . HOH F 3 .   ? -37.934 -9.302  23.354 1.00 43.50  ? 504 HOH B O   1 
HETATM 5034 O O   . HOH F 3 .   ? 1.038   6.562   48.247 1.00 38.58  ? 505 HOH B O   1 
HETATM 5035 O O   . HOH F 3 .   ? -30.097 7.510   31.131 1.00 34.45  ? 506 HOH B O   1 
HETATM 5036 O O   . HOH F 3 .   ? -29.338 -2.551  20.518 1.00 35.74  ? 507 HOH B O   1 
HETATM 5037 O O   . HOH F 3 .   ? -41.227 25.698  30.734 1.00 36.07  ? 508 HOH B O   1 
HETATM 5038 O O   . HOH F 3 .   ? -32.869 13.744  40.695 1.00 39.45  ? 509 HOH B O   1 
HETATM 5039 O O   . HOH F 3 .   ? -44.227 13.952  19.185 1.00 29.16  ? 510 HOH B O   1 
HETATM 5040 O O   . HOH F 3 .   ? -8.414  3.147   13.604 1.00 34.62  ? 511 HOH B O   1 
HETATM 5041 O O   . HOH F 3 .   ? -7.616  9.149   17.170 1.00 26.47  ? 512 HOH B O   1 
HETATM 5042 O O   . HOH F 3 .   ? -29.774 8.176   52.504 1.00 37.30  ? 513 HOH B O   1 
HETATM 5043 O O   . HOH F 3 .   ? -20.045 16.605  7.645  1.00 44.48  ? 514 HOH B O   1 
HETATM 5044 O O   . HOH F 3 .   ? -45.140 21.380  16.007 1.00 37.99  ? 515 HOH B O   1 
HETATM 5045 O O   . HOH F 3 .   ? -22.410 8.140   8.161  1.00 47.39  ? 516 HOH B O   1 
HETATM 5046 O O   . HOH F 3 .   ? -29.145 0.260   40.287 1.00 29.15  ? 517 HOH B O   1 
HETATM 5047 O O   . HOH F 3 .   ? -32.058 10.783  31.266 1.00 29.44  ? 518 HOH B O   1 
HETATM 5048 O O   . HOH F 3 .   ? -5.021  2.628   28.342 1.00 29.06  ? 519 HOH B O   1 
HETATM 5049 O O   . HOH F 3 .   ? -15.948 26.280  40.459 1.00 30.09  ? 520 HOH B O   1 
HETATM 5050 O O   . HOH F 3 .   ? -28.130 14.860  44.708 1.00 31.98  ? 521 HOH B O   1 
HETATM 5051 O O   . HOH F 3 .   ? -35.038 0.985   17.280 1.00 33.94  ? 522 HOH B O   1 
HETATM 5052 O O   . HOH F 3 .   ? -20.618 12.087  7.888  1.00 43.24  ? 523 HOH B O   1 
HETATM 5053 O O   . HOH F 3 .   ? -8.108  15.983  12.377 1.00 41.64  ? 524 HOH B O   1 
HETATM 5054 O O   . HOH F 3 .   ? -16.417 14.110  12.141 1.00 31.29  ? 525 HOH B O   1 
HETATM 5055 O O   . HOH F 3 .   ? -20.775 -0.013  33.255 1.00 21.55  ? 526 HOH B O   1 
HETATM 5056 O O   . HOH F 3 .   ? -19.488 -10.943 20.226 1.00 39.36  ? 527 HOH B O   1 
HETATM 5057 O O   . HOH F 3 .   ? -5.704  2.162   25.277 1.00 37.76  ? 528 HOH B O   1 
HETATM 5058 O O   . HOH F 3 .   ? -31.471 19.637  16.310 1.00 22.62  ? 529 HOH B O   1 
HETATM 5059 O O   . HOH F 3 .   ? -33.165 22.907  15.894 1.00 26.70  ? 530 HOH B O   1 
HETATM 5060 O O   . HOH F 3 .   ? -37.422 20.638  32.424 1.00 35.44  ? 531 HOH B O   1 
HETATM 5061 O O   . HOH F 3 .   ? -3.932  19.763  40.113 1.00 23.52  ? 532 HOH B O   1 
HETATM 5062 O O   . HOH F 3 .   ? -42.107 6.913   28.870 1.00 28.45  ? 533 HOH B O   1 
HETATM 5063 O O   . HOH F 3 .   ? -33.693 30.369  28.097 1.00 43.38  ? 534 HOH B O   1 
HETATM 5064 O O   . HOH F 3 .   ? -4.178  9.969   25.896 1.00 24.93  ? 535 HOH B O   1 
HETATM 5065 O O   . HOH F 3 .   ? -27.468 1.133   31.827 1.00 32.33  ? 536 HOH B O   1 
HETATM 5066 O O   . HOH F 3 .   ? -11.340 -4.243  37.173 1.00 39.17  ? 537 HOH B O   1 
HETATM 5067 O O   . HOH F 3 .   ? -5.758  -0.099  31.629 1.00 44.40  ? 538 HOH B O   1 
HETATM 5068 O O   . HOH F 3 .   ? 13.638  7.344   20.784 1.00 37.68  ? 539 HOH B O   1 
HETATM 5069 O O   . HOH F 3 .   ? -13.963 26.061  28.404 1.00 25.79  ? 540 HOH B O   1 
HETATM 5070 O O   . HOH F 3 .   ? -3.917  5.388   48.787 1.00 43.56  ? 541 HOH B O   1 
HETATM 5071 O O   . HOH F 3 .   ? -5.827  -0.105  44.596 1.00 32.19  ? 542 HOH B O   1 
HETATM 5072 O O   . HOH F 3 .   ? -9.387  11.978  30.223 1.00 22.47  ? 543 HOH B O   1 
HETATM 5073 O O   . HOH F 3 .   ? -31.683 21.133  40.483 1.00 38.28  ? 544 HOH B O   1 
HETATM 5074 O O   . HOH F 3 .   ? -47.288 15.363  29.569 1.00 30.59  ? 545 HOH B O   1 
HETATM 5075 O O   . HOH F 3 .   ? -26.293 21.873  29.307 1.00 21.40  ? 546 HOH B O   1 
HETATM 5076 O O   . HOH F 3 .   ? -2.158  12.319  22.100 1.00 39.00  ? 547 HOH B O   1 
HETATM 5077 O O   . HOH F 3 .   ? -13.618 23.895  14.633 1.00 46.53  ? 548 HOH B O   1 
HETATM 5078 O O   . HOH F 3 .   ? 1.345   11.607  29.649 1.00 36.99  ? 549 HOH B O   1 
HETATM 5079 O O   . HOH F 3 .   ? -39.936 2.549   25.563 1.00 22.35  ? 550 HOH B O   1 
HETATM 5080 O O   . HOH F 3 .   ? -37.985 -1.719  17.273 1.00 32.55  ? 551 HOH B O   1 
HETATM 5081 O O   . HOH F 3 .   ? -51.588 15.162  17.963 1.00 43.40  ? 552 HOH B O   1 
HETATM 5082 O O   . HOH F 3 .   ? -14.234 2.828   13.265 1.00 43.27  ? 553 HOH B O   1 
HETATM 5083 O O   . HOH F 3 .   ? -17.244 -8.467  14.672 1.00 30.24  ? 554 HOH B O   1 
HETATM 5084 O O   . HOH F 3 .   ? -10.184 6.608   23.517 1.00 24.71  ? 555 HOH B O   1 
HETATM 5085 O O   . HOH F 3 .   ? -42.109 16.036  24.299 1.00 25.76  ? 556 HOH B O   1 
HETATM 5086 O O   . HOH F 3 .   ? -46.548 7.943   27.253 1.00 32.83  ? 557 HOH B O   1 
HETATM 5087 O O   . HOH F 3 .   ? -49.129 12.650  31.729 1.00 47.37  ? 558 HOH B O   1 
HETATM 5088 O O   . HOH F 3 .   ? -31.551 12.016  7.637  1.00 35.14  ? 559 HOH B O   1 
HETATM 5089 O O   . HOH F 3 .   ? -31.185 16.664  32.740 1.00 31.74  ? 560 HOH B O   1 
HETATM 5090 O O   . HOH F 3 .   ? -43.177 24.171  22.083 1.00 37.24  ? 561 HOH B O   1 
HETATM 5091 O O   . HOH F 3 .   ? -23.936 18.139  44.536 1.00 31.82  ? 562 HOH B O   1 
HETATM 5092 O O   . HOH F 3 .   ? -13.501 20.987  17.502 1.00 34.50  ? 563 HOH B O   1 
HETATM 5093 O O   . HOH F 3 .   ? -13.686 20.903  21.627 1.00 25.64  ? 564 HOH B O   1 
HETATM 5094 O O   . HOH F 3 .   ? -19.337 18.033  19.047 1.00 25.91  ? 565 HOH B O   1 
HETATM 5095 O O   . HOH F 3 .   ? -27.748 17.637  18.252 1.00 27.77  ? 566 HOH B O   1 
HETATM 5096 O O   . HOH F 3 .   ? -13.062 -4.147  29.926 1.00 24.91  ? 567 HOH B O   1 
HETATM 5097 O O   . HOH F 3 .   ? -29.690 25.302  15.779 1.00 25.54  ? 568 HOH B O   1 
HETATM 5098 O O   . HOH F 3 .   ? -9.238  0.047   26.535 1.00 29.15  ? 569 HOH B O   1 
HETATM 5099 O O   . HOH F 3 .   ? -40.119 12.116  18.120 1.00 32.44  ? 570 HOH B O   1 
HETATM 5100 O O   . HOH F 3 .   ? -32.158 15.110  16.277 1.00 29.83  ? 571 HOH B O   1 
HETATM 5101 O O   . HOH F 3 .   ? -15.297 6.124   50.694 1.00 39.51  ? 572 HOH B O   1 
HETATM 5102 O O   . HOH F 3 .   ? -16.425 12.863  46.066 1.00 24.75  ? 573 HOH B O   1 
HETATM 5103 O O   . HOH F 3 .   ? -34.161 17.488  40.013 1.00 36.04  ? 574 HOH B O   1 
HETATM 5104 O O   . HOH F 3 .   ? -32.081 10.310  33.776 1.00 24.14  ? 575 HOH B O   1 
HETATM 5105 O O   . HOH F 3 .   ? -33.980 22.129  24.885 1.00 24.90  ? 576 HOH B O   1 
HETATM 5106 O O   . HOH F 3 .   ? -27.076 13.480  37.190 1.00 25.89  ? 577 HOH B O   1 
HETATM 5107 O O   . HOH F 3 .   ? -24.289 0.789   24.781 1.00 24.86  ? 578 HOH B O   1 
HETATM 5108 O O   . HOH F 3 .   ? -37.072 25.166  26.729 1.00 28.67  ? 579 HOH B O   1 
HETATM 5109 O O   . HOH F 3 .   ? -0.862  2.724   48.037 1.00 44.45  ? 580 HOH B O   1 
HETATM 5110 O O   . HOH F 3 .   ? -2.008  24.734  27.465 1.00 41.88  ? 581 HOH B O   1 
HETATM 5111 O O   . HOH F 3 .   ? -18.798 25.799  39.762 1.00 36.09  ? 582 HOH B O   1 
HETATM 5112 O O   . HOH F 3 .   ? 3.011   9.048   38.547 1.00 32.41  ? 583 HOH B O   1 
HETATM 5113 O O   . HOH F 3 .   ? -34.027 19.334  24.442 1.00 24.34  ? 584 HOH B O   1 
HETATM 5114 O O   . HOH F 3 .   ? -30.611 19.771  13.523 1.00 20.90  ? 585 HOH B O   1 
HETATM 5115 O O   . HOH F 3 .   ? -20.570 26.796  20.592 1.00 40.64  ? 586 HOH B O   1 
HETATM 5116 O O   . HOH F 3 .   ? -43.789 22.775  19.563 1.00 32.12  ? 587 HOH B O   1 
HETATM 5117 O O   . HOH F 3 .   ? -33.399 25.502  28.350 1.00 27.06  ? 588 HOH B O   1 
HETATM 5118 O O   . HOH F 3 .   ? -9.514  12.774  32.841 1.00 19.46  ? 589 HOH B O   1 
HETATM 5119 O O   . HOH F 3 .   ? -3.375  22.506  34.971 1.00 37.04  ? 590 HOH B O   1 
HETATM 5120 O O   . HOH F 3 .   ? -44.403 16.906  22.665 1.00 25.60  ? 591 HOH B O   1 
HETATM 5121 O O   . HOH F 3 .   ? -22.277 22.629  18.614 1.00 28.34  ? 592 HOH B O   1 
HETATM 5122 O O   . HOH F 3 .   ? -26.357 25.092  18.460 1.00 28.99  ? 593 HOH B O   1 
HETATM 5123 O O   . HOH F 3 .   ? -48.220 7.048   25.170 1.00 23.05  ? 594 HOH B O   1 
HETATM 5124 O O   . HOH F 3 .   ? -49.018 12.514  19.723 1.00 41.23  ? 595 HOH B O   1 
HETATM 5125 O O   . HOH F 3 .   ? -0.594  21.212  34.073 1.00 36.85  ? 596 HOH B O   1 
HETATM 5126 O O   . HOH F 3 .   ? -1.633  10.955  35.468 1.00 20.15  ? 597 HOH B O   1 
HETATM 5127 O O   . HOH F 3 .   ? -40.341 -3.557  19.752 1.00 36.88  ? 598 HOH B O   1 
HETATM 5128 O O   . HOH F 3 .   ? -16.870 -3.964  11.485 1.00 34.03  ? 599 HOH B O   1 
HETATM 5129 O O   . HOH F 3 .   ? -10.708 27.030  20.839 1.00 29.91  ? 600 HOH B O   1 
HETATM 5130 O O   . HOH F 3 .   ? -10.510 26.914  25.260 1.00 31.88  ? 601 HOH B O   1 
HETATM 5131 O O   . HOH F 3 .   ? -26.424 18.176  11.201 1.00 33.22  ? 602 HOH B O   1 
HETATM 5132 O O   . HOH F 3 .   ? -29.891 21.046  35.221 1.00 23.68  ? 603 HOH B O   1 
HETATM 5133 O O   . HOH F 3 .   ? -32.323 -0.423  19.472 1.00 30.39  ? 604 HOH B O   1 
HETATM 5134 O O   . HOH F 3 .   ? -35.048 21.192  16.754 1.00 27.60  ? 605 HOH B O   1 
HETATM 5135 O O   . HOH F 3 .   ? -9.721  4.400   46.405 1.00 37.61  ? 606 HOH B O   1 
HETATM 5136 O O   . HOH F 3 .   ? -26.473 26.828  33.787 1.00 27.14  ? 607 HOH B O   1 
HETATM 5137 O O   . HOH F 3 .   ? -28.165 22.401  33.279 1.00 21.82  ? 608 HOH B O   1 
HETATM 5138 O O   . HOH F 3 .   ? -28.235 24.320  39.148 1.00 34.11  ? 609 HOH B O   1 
HETATM 5139 O O   . HOH F 3 .   ? -23.398 1.748   20.699 1.00 28.81  ? 610 HOH B O   1 
HETATM 5140 O O   . HOH F 3 .   ? -46.503 22.813  26.426 1.00 34.94  ? 611 HOH B O   1 
HETATM 5141 O O   . HOH F 3 .   ? -22.082 2.640   18.453 1.00 27.03  ? 612 HOH B O   1 
HETATM 5142 O O   . HOH F 3 .   ? -27.842 5.080   17.446 1.00 21.86  ? 613 HOH B O   1 
HETATM 5143 O O   . HOH F 3 .   ? -34.392 19.042  31.349 1.00 32.32  ? 614 HOH B O   1 
HETATM 5144 O O   . HOH F 3 .   ? -15.164 -9.163  25.531 1.00 44.53  ? 615 HOH B O   1 
HETATM 5145 O O   . HOH F 3 .   ? -6.979  24.133  21.847 1.00 37.52  ? 616 HOH B O   1 
HETATM 5146 O O   . HOH F 3 .   ? -3.997  0.038   37.174 1.00 33.38  ? 617 HOH B O   1 
HETATM 5147 O O   . HOH F 3 .   ? -24.740 24.055  15.892 1.00 40.50  ? 618 HOH B O   1 
HETATM 5148 O O   . HOH F 3 .   ? -32.026 -3.479  22.828 1.00 42.87  ? 619 HOH B O   1 
HETATM 5149 O O   . HOH F 3 .   ? -30.319 13.088  15.537 1.00 27.85  ? 620 HOH B O   1 
HETATM 5150 O O   . HOH F 3 .   ? -15.804 28.846  29.950 1.00 29.44  ? 621 HOH B O   1 
HETATM 5151 O O   . HOH F 3 .   ? -10.108 25.487  39.909 1.00 35.73  ? 622 HOH B O   1 
HETATM 5152 O O   . HOH F 3 .   ? -33.698 6.634   20.991 1.00 21.56  ? 623 HOH B O   1 
HETATM 5153 O O   . HOH F 3 .   ? -15.122 27.642  20.059 1.00 41.93  ? 624 HOH B O   1 
HETATM 5154 O O   . HOH F 3 .   ? -30.909 12.042  37.915 1.00 24.24  ? 625 HOH B O   1 
HETATM 5155 O O   . HOH F 3 .   ? -23.552 -3.963  16.186 1.00 29.86  ? 626 HOH B O   1 
HETATM 5156 O O   . HOH F 3 .   ? -3.995  7.619   18.040 1.00 34.90  ? 627 HOH B O   1 
HETATM 5157 O O   . HOH F 3 .   ? -37.150 13.009  12.298 1.00 30.23  ? 628 HOH B O   1 
HETATM 5158 O O   . HOH F 3 .   ? -48.015 19.337  28.811 1.00 26.14  ? 629 HOH B O   1 
HETATM 5159 O O   . HOH F 3 .   ? -44.329 7.166   20.199 1.00 34.35  ? 630 HOH B O   1 
HETATM 5160 O O   . HOH F 3 .   ? -19.602 2.438   49.311 1.00 34.32  ? 631 HOH B O   1 
HETATM 5161 O O   . HOH F 3 .   ? -3.204  6.362   32.825 1.00 27.03  ? 632 HOH B O   1 
HETATM 5162 O O   . HOH F 3 .   ? -39.303 21.972  24.606 1.00 28.57  ? 633 HOH B O   1 
HETATM 5163 O O   . HOH F 3 .   ? -32.346 12.299  14.202 1.00 34.55  ? 634 HOH B O   1 
HETATM 5164 O O   . HOH F 3 .   ? -27.616 26.227  29.228 1.00 23.49  ? 635 HOH B O   1 
HETATM 5165 O O   . HOH F 3 .   ? -21.858 1.340   40.095 1.00 35.55  ? 636 HOH B O   1 
HETATM 5166 O O   . HOH F 3 .   ? -40.051 14.726  15.665 1.00 36.62  ? 637 HOH B O   1 
HETATM 5167 O O   . HOH F 3 .   ? -2.847  1.240   22.095 1.00 31.77  ? 638 HOH B O   1 
HETATM 5168 O O   . HOH F 3 .   ? -6.527  23.827  31.535 1.00 25.63  ? 639 HOH B O   1 
HETATM 5169 O O   . HOH F 3 .   ? -17.091 -3.179  21.794 1.00 27.24  ? 640 HOH B O   1 
HETATM 5170 O O   . HOH F 3 .   ? -17.807 26.519  20.655 1.00 35.05  ? 641 HOH B O   1 
HETATM 5171 O O   . HOH F 3 .   ? -38.091 2.713   27.216 1.00 35.51  ? 642 HOH B O   1 
HETATM 5172 O O   . HOH F 3 .   ? -2.343  9.218   24.323 1.00 24.22  ? 643 HOH B O   1 
HETATM 5173 O O   . HOH F 3 .   ? -44.344 24.323  24.808 1.00 28.78  ? 644 HOH B O   1 
HETATM 5174 O O   . HOH F 3 .   ? -5.508  10.133  47.604 1.00 34.18  ? 645 HOH B O   1 
HETATM 5175 O O   . HOH F 3 .   ? -38.761 9.017   15.859 1.00 34.05  ? 646 HOH B O   1 
HETATM 5176 O O   . HOH F 3 .   ? -8.942  23.851  34.795 1.00 29.21  ? 647 HOH B O   1 
HETATM 5177 O O   . HOH F 3 .   ? -22.306 10.768  44.982 1.00 27.54  ? 648 HOH B O   1 
HETATM 5178 O O   . HOH F 3 .   ? -34.386 3.500   13.693 1.00 28.35  ? 649 HOH B O   1 
HETATM 5179 O O   . HOH F 3 .   ? -11.775 7.034   25.658 1.00 20.56  ? 650 HOH B O   1 
HETATM 5180 O O   . HOH F 3 .   ? -5.286  22.240  46.461 1.00 38.11  ? 651 HOH B O   1 
HETATM 5181 O O   . HOH F 3 .   ? -0.553  10.226  32.286 1.00 36.02  ? 652 HOH B O   1 
HETATM 5182 O O   . HOH F 3 .   ? -15.583 30.954  28.339 1.00 31.39  ? 653 HOH B O   1 
HETATM 5183 O O   . HOH F 3 .   ? -29.609 11.654  10.196 1.00 32.62  ? 654 HOH B O   1 
HETATM 5184 O O   . HOH F 3 .   ? -26.774 30.522  24.235 1.00 39.02  ? 655 HOH B O   1 
HETATM 5185 O O   . HOH F 3 .   ? -42.864 5.080   20.382 1.00 27.90  ? 656 HOH B O   1 
HETATM 5186 O O   . HOH F 3 .   ? -26.076 20.294  12.660 1.00 23.73  ? 657 HOH B O   1 
HETATM 5187 O O   . HOH F 3 .   ? -9.457  12.591  51.401 1.00 45.83  ? 658 HOH B O   1 
HETATM 5188 O O   . HOH F 3 .   ? -2.345  16.783  47.051 1.00 40.64  ? 659 HOH B O   1 
HETATM 5189 O O   . HOH F 3 .   ? -12.494 2.401   45.352 1.00 33.87  ? 660 HOH B O   1 
HETATM 5190 O O   . HOH F 3 .   ? -3.256  11.598  10.128 1.00 44.60  ? 661 HOH B O   1 
HETATM 5191 O O   . HOH F 3 .   ? -44.343 10.635  19.109 1.00 36.56  ? 662 HOH B O   1 
HETATM 5192 O O   . HOH F 3 .   ? -13.750 13.963  46.107 1.00 41.40  ? 663 HOH B O   1 
HETATM 5193 O O   . HOH F 3 .   ? -35.503 27.103  27.445 1.00 29.01  ? 664 HOH B O   1 
HETATM 5194 O O   . HOH F 3 .   ? -20.461 31.183  25.574 1.00 30.69  ? 665 HOH B O   1 
HETATM 5195 O O   . HOH F 3 .   ? -29.255 13.927  33.349 1.00 30.06  ? 666 HOH B O   1 
HETATM 5196 O O   . HOH F 3 .   ? -13.839 19.904  49.916 1.00 33.28  ? 667 HOH B O   1 
HETATM 5197 O O   . HOH F 3 .   ? -20.576 20.120  17.857 1.00 33.07  ? 668 HOH B O   1 
HETATM 5198 O O   . HOH F 3 .   ? -10.960 -2.455  30.794 1.00 32.35  ? 669 HOH B O   1 
HETATM 5199 O O   . HOH F 3 .   ? -18.959 26.709  37.056 1.00 30.36  ? 670 HOH B O   1 
HETATM 5200 O O   . HOH F 3 .   ? -17.324 33.141  24.649 1.00 39.84  ? 671 HOH B O   1 
HETATM 5201 O O   . HOH F 3 .   ? -30.872 19.331  33.599 1.00 24.23  ? 672 HOH B O   1 
HETATM 5202 O O   . HOH F 3 .   ? -28.699 -2.658  48.891 1.00 30.56  ? 673 HOH B O   1 
HETATM 5203 O O   . HOH F 3 .   ? -4.383  16.673  21.542 1.00 32.05  ? 674 HOH B O   1 
HETATM 5204 O O   . HOH F 3 .   ? -2.369  19.975  23.353 1.00 35.87  ? 675 HOH B O   1 
HETATM 5205 O O   . HOH F 3 .   ? -5.519  26.069  29.751 1.00 45.51  ? 676 HOH B O   1 
HETATM 5206 O O   . HOH F 3 .   ? -33.701 13.133  31.487 1.00 30.06  ? 677 HOH B O   1 
HETATM 5207 O O   . HOH F 3 .   ? -4.682  18.723  22.960 1.00 42.21  ? 678 HOH B O   1 
HETATM 5208 O O   . HOH F 3 .   ? -13.629 18.295  14.927 1.00 42.39  ? 679 HOH B O   1 
HETATM 5209 O O   . HOH F 3 .   ? -30.226 6.373   42.894 1.00 41.74  ? 680 HOH B O   1 
HETATM 5210 O O   . HOH F 3 .   ? -36.782 22.911  25.674 1.00 23.28  ? 681 HOH B O   1 
HETATM 5211 O O   . HOH F 3 .   ? -22.297 20.541  10.826 1.00 29.86  ? 682 HOH B O   1 
HETATM 5212 O O   . HOH F 3 .   ? -30.514 3.507   29.248 1.00 34.17  ? 683 HOH B O   1 
HETATM 5213 O O   . HOH F 3 .   ? -31.794 6.943   56.345 1.00 42.73  ? 684 HOH B O   1 
HETATM 5214 O O   . HOH F 3 .   ? -26.980 16.811  48.695 1.00 34.18  ? 685 HOH B O   1 
HETATM 5215 O O   . HOH F 3 .   ? -50.432 9.971   28.944 1.00 41.15  ? 686 HOH B O   1 
HETATM 5216 O O   . HOH F 3 .   ? -19.883 -9.659  15.378 1.00 40.52  ? 687 HOH B O   1 
HETATM 5217 O O   . HOH F 3 .   ? -3.619  4.933   28.426 1.00 30.07  ? 688 HOH B O   1 
HETATM 5218 O O   . HOH F 3 .   ? -5.722  21.270  41.735 1.00 21.94  ? 689 HOH B O   1 
HETATM 5219 O O   . HOH F 3 .   ? -30.883 12.502  35.118 1.00 29.60  ? 690 HOH B O   1 
HETATM 5220 O O   . HOH F 3 .   ? -47.601 9.750   29.434 1.00 31.92  ? 691 HOH B O   1 
HETATM 5221 O O   . HOH F 3 .   ? -5.499  25.484  27.191 1.00 45.16  ? 692 HOH B O   1 
HETATM 5222 O O   . HOH F 3 .   ? -10.980 14.380  49.539 1.00 37.75  ? 693 HOH B O   1 
HETATM 5223 O O   . HOH F 3 .   ? -17.461 -2.477  9.299  1.00 48.82  ? 694 HOH B O   1 
HETATM 5224 O O   . HOH F 3 .   ? -19.346 -0.588  9.811  1.00 46.52  ? 695 HOH B O   1 
HETATM 5225 O O   . HOH F 3 .   ? -44.602 5.733   29.061 1.00 39.82  ? 696 HOH B O   1 
HETATM 5226 O O   . HOH F 3 .   ? -28.199 27.339  19.872 1.00 40.48  ? 697 HOH B O   1 
HETATM 5227 O O   . HOH F 3 .   ? -3.545  5.666   16.548 1.00 48.02  ? 698 HOH B O   1 
HETATM 5228 O O   . HOH F 3 .   ? -34.362 10.272  37.320 1.00 42.81  ? 699 HOH B O   1 
HETATM 5229 O O   . HOH F 3 .   ? -17.736 14.547  7.304  1.00 45.42  ? 700 HOH B O   1 
HETATM 5230 O O   . HOH F 3 .   ? -28.650 17.017  46.320 1.00 36.35  ? 701 HOH B O   1 
HETATM 5231 O O   . HOH F 3 .   ? -22.872 8.014   45.329 1.00 28.02  ? 702 HOH B O   1 
HETATM 5232 O O   . HOH F 3 .   ? -28.172 21.021  13.650 1.00 24.75  ? 703 HOH B O   1 
HETATM 5233 O O   . HOH F 3 .   ? -29.603 26.396  31.150 1.00 25.06  ? 704 HOH B O   1 
HETATM 5234 O O   . HOH F 3 .   ? -40.306 4.820   29.183 1.00 33.76  ? 705 HOH B O   1 
HETATM 5235 O O   . HOH F 3 .   ? -36.241 20.454  14.553 1.00 44.98  ? 706 HOH B O   1 
HETATM 5236 O O   . HOH F 3 .   ? -8.868  24.907  32.472 1.00 30.36  ? 707 HOH B O   1 
HETATM 5237 O O   . HOH F 3 .   ? -12.760 6.724   50.972 1.00 43.37  ? 708 HOH B O   1 
HETATM 5238 O O   . HOH F 3 .   ? -8.812  -3.054  29.289 1.00 41.63  ? 709 HOH B O   1 
HETATM 5239 O O   . HOH F 3 .   ? 3.170   5.827   49.500 1.00 43.74  ? 710 HOH B O   1 
HETATM 5240 O O   . HOH F 3 .   ? -33.365 14.759  33.640 1.00 44.16  ? 711 HOH B O   1 
HETATM 5241 O O   . HOH F 3 .   ? -22.081 25.256  19.782 1.00 45.64  ? 712 HOH B O   1 
HETATM 5242 O O   . HOH F 3 .   ? -49.302 21.956  29.808 1.00 34.62  ? 713 HOH B O   1 
HETATM 5243 O O   . HOH F 3 .   ? -33.595 20.190  33.489 1.00 24.68  ? 714 HOH B O   1 
HETATM 5244 O O   . HOH F 3 .   ? 0.358   18.380  23.817 1.00 43.39  ? 715 HOH B O   1 
HETATM 5245 O O   . HOH F 3 .   ? -1.031  5.889   17.209 1.00 48.20  ? 716 HOH B O   1 
HETATM 5246 O O   . HOH F 3 .   ? -34.934 9.932   40.543 1.00 39.09  ? 717 HOH B O   1 
HETATM 5247 O O   . HOH F 3 .   ? -37.334 0.871   28.952 1.00 38.40  ? 718 HOH B O   1 
HETATM 5248 O O   . HOH F 3 .   ? -33.157 7.856   29.988 1.00 45.59  ? 719 HOH B O   1 
HETATM 5249 O O   . HOH F 3 .   ? -32.423 26.367  30.845 1.00 27.47  ? 720 HOH B O   1 
HETATM 5250 O O   . HOH F 3 .   ? -12.910 -10.096 23.857 1.00 45.65  ? 721 HOH B O   1 
HETATM 5251 O O   . HOH F 3 .   ? -2.599  0.866   28.291 1.00 39.76  ? 722 HOH B O   1 
HETATM 5252 O O   . HOH F 3 .   ? -33.054 33.137  28.537 1.00 48.53  ? 723 HOH B O   1 
HETATM 5253 O O   . HOH F 3 .   ? -50.857 17.271  14.303 1.00 47.80  ? 724 HOH B O   1 
HETATM 5254 O O   . HOH F 3 .   ? -39.191 -0.963  15.193 1.00 44.19  ? 725 HOH B O   1 
HETATM 5255 O O   . HOH F 3 .   ? -26.269 28.444  21.533 1.00 35.50  ? 726 HOH B O   1 
HETATM 5256 O O   . HOH F 3 .   ? -43.220 3.596   17.831 1.00 28.31  ? 727 HOH B O   1 
HETATM 5257 O O   . HOH F 3 .   ? -43.812 0.869   17.859 1.00 29.31  ? 728 HOH B O   1 
HETATM 5258 O O   . HOH F 3 .   ? -28.298 25.006  33.177 1.00 27.68  ? 729 HOH B O   1 
HETATM 5259 O O   . HOH F 3 .   ? -12.246 22.065  49.388 1.00 36.90  ? 730 HOH B O   1 
HETATM 5260 O O   . HOH F 3 .   ? -33.270 29.046  30.479 1.00 35.27  ? 731 HOH B O   1 
HETATM 5261 O O   . HOH F 3 .   ? -13.145 24.497  48.999 1.00 27.81  ? 732 HOH B O   1 
HETATM 5262 O O   . HOH F 3 .   ? -33.572 22.856  33.890 1.00 39.66  ? 733 HOH B O   1 
HETATM 5263 O O   . HOH F 3 .   ? -11.881 25.719  35.151 1.00 27.78  ? 734 HOH B O   1 
HETATM 5264 O O   . HOH F 3 .   ? -41.332 3.664   15.833 1.00 37.31  ? 735 HOH B O   1 
HETATM 5265 O O   . HOH F 3 .   ? -30.199 25.485  35.326 1.00 31.36  ? 736 HOH B O   1 
# 
