data_8RG6
# 
_entry.id   8RG6 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.399 
_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   8RG6         pdb_00008rg6 10.2210/pdb8rg6/pdb 
WWPDB D_1292135300 ?            ?                   
# 
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 2024-12-04 
2 'Structure model' 1 1 2024-12-25 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
loop_
_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' citation        
2 2 'Structure model' citation_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' '_citation.journal_volume'          
2 2 'Structure model' '_citation.page_first'              
3 2 'Structure model' '_citation.page_last'               
4 2 'Structure model' '_citation_author.identifier_ORCID' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8RG6 
_pdbx_database_status.recvd_initial_deposition_date   2023-12-13 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_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           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              jens.petersen@astrazeneca.com 
_pdbx_contact_author.name_first         Jens 
_pdbx_contact_author.name_last          Petersen 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-5946-4756 
# 
_audit_author.name               'Petersen, J.' 
_audit_author.pdbx_ordinal       1 
_audit_author.identifier_ORCID   ? 
# 
_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                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            J.Med.Chem. 
_citation.journal_id_ASTM           JMCMAR 
_citation.journal_id_CSD            0151 
_citation.journal_id_ISSN           0022-2623 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            67 
_citation.language                  ? 
_citation.page_first                20827 
_citation.page_last                 20841 
_citation.title                     
;Discovery of (2 R ,4 R )-4-(( S )-2-Amino-3-methylbutanamido)-2-(4-boronobutyl)pyrrolidine-2-carboxylic Acid (AZD0011), an Actively Transported Prodrug of a Potent Arginase Inhibitor to Treat Cancer.
;
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acs.jmedchem.4c02309 
_citation.pdbx_database_id_PubMed   39572889 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Mlynarski, S.N.' 1  ? 
primary 'Aquila, B.M.'    2  ? 
primary 'Cantin, S.'      3  ? 
primary 'Cook, S.'        4  ? 
primary 'Doshi, A.'       5  ? 
primary 'Finlay, M.R.V.'  6  ? 
primary 'Gangl, E.T.'     7  ? 
primary 'Grebe, T.'       8  ? 
primary 'Gu, C.'          9  ? 
primary 'Kawatkar, S.P.'  10 ? 
primary 'Petersen, J.'    11 ? 
primary 'Pop-Damkov, P.'  12 ? 
primary 'Schuller, A.G.'  13 ? 
primary 'Shao, W.'        14 ? 
primary 'Shields, J.D.'   15 ? 
primary 'Simpson, I.'     16 ? 
primary 'Tavakoli, S.'    17 ? 
primary 'Tentarelli, S.'  18 ? 
primary 'Throner, S.'     19 ? 
primary 'Wang, H.'        20 ? 
primary 'Wang, J.'        21 ? 
primary 'Wu, D.'          22 ? 
primary 'Ye, Q.'          23 ? 
# 
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 'Arginase-2, mitochondrial'                                                 36653.367 3   3.5.3.1 ? ? ? 
2 non-polymer syn 'MANGANESE (II) ION'                                                        54.938    6   ?       ? ? ? 
3 non-polymer syn '(2~{S},3~{R})-3-[3-(dihydroxyboranyl)propyl]pyrrolidine-2-carboxylic acid' 201.028   3   ?       ? ? ? 
4 water       nat water                                                                       18.015    360 ?       ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Arginase II,Kidney-type arginase,Non-hepatic arginase,Type II arginase' 
# 
_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       
;MHHHHHHGGGENLYFQSVHSVAVIGAPFSQGQKRKGVEHGPAAIREAGLMKRLSSLGCHLKDFGDLSFTPVPKDDLYNNL
IVNPRSVGLANQELAEVVSRAVSDGYSCVTLGGDHSLAIGTISGHARHCPDLCVVWVDAHADINTPLTTSSGNLHGQPVS
FLLRELQDKVPQLPGFSWIKPCISSASIVYIGLRDVDPPEHFILKNYDIQYFSMRDIDRLGIQKVMERTFDLLIGKRQRP
IHLSFDIDAFDPTLAPATGTPVVGGLTYREGMYIAEEIHNTGLLSALDLVEVNPQLATSEEEAKTTANLAVDVIASSFGQ
TREGGHIVYDQLPTPS
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MHHHHHHGGGENLYFQSVHSVAVIGAPFSQGQKRKGVEHGPAAIREAGLMKRLSSLGCHLKDFGDLSFTPVPKDDLYNNL
IVNPRSVGLANQELAEVVSRAVSDGYSCVTLGGDHSLAIGTISGHARHCPDLCVVWVDAHADINTPLTTSSGNLHGQPVS
FLLRELQDKVPQLPGFSWIKPCISSASIVYIGLRDVDPPEHFILKNYDIQYFSMRDIDRLGIQKVMERTFDLLIGKRQRP
IHLSFDIDAFDPTLAPATGTPVVGGLTYREGMYIAEEIHNTGLLSALDLVEVNPQLATSEEEAKTTANLAVDVIASSFGQ
TREGGHIVYDQLPTPS
;
_entity_poly.pdbx_strand_id                 A,B,C 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'MANGANESE (II) ION'                                                        MN    
3 '(2~{S},3~{R})-3-[3-(dihydroxyboranyl)propyl]pyrrolidine-2-carboxylic acid' A1H0B 
4 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   HIS n 
1 3   HIS n 
1 4   HIS n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   GLY n 
1 9   GLY n 
1 10  GLY n 
1 11  GLU n 
1 12  ASN n 
1 13  LEU n 
1 14  TYR n 
1 15  PHE n 
1 16  GLN n 
1 17  SER n 
1 18  VAL n 
1 19  HIS n 
1 20  SER n 
1 21  VAL n 
1 22  ALA n 
1 23  VAL n 
1 24  ILE n 
1 25  GLY n 
1 26  ALA n 
1 27  PRO n 
1 28  PHE n 
1 29  SER n 
1 30  GLN n 
1 31  GLY n 
1 32  GLN n 
1 33  LYS n 
1 34  ARG n 
1 35  LYS n 
1 36  GLY n 
1 37  VAL n 
1 38  GLU n 
1 39  HIS n 
1 40  GLY n 
1 41  PRO n 
1 42  ALA n 
1 43  ALA n 
1 44  ILE n 
1 45  ARG n 
1 46  GLU n 
1 47  ALA n 
1 48  GLY n 
1 49  LEU n 
1 50  MET n 
1 51  LYS n 
1 52  ARG n 
1 53  LEU n 
1 54  SER n 
1 55  SER n 
1 56  LEU n 
1 57  GLY n 
1 58  CYS n 
1 59  HIS n 
1 60  LEU n 
1 61  LYS n 
1 62  ASP n 
1 63  PHE n 
1 64  GLY n 
1 65  ASP n 
1 66  LEU n 
1 67  SER n 
1 68  PHE n 
1 69  THR n 
1 70  PRO n 
1 71  VAL n 
1 72  PRO n 
1 73  LYS n 
1 74  ASP n 
1 75  ASP n 
1 76  LEU n 
1 77  TYR n 
1 78  ASN n 
1 79  ASN n 
1 80  LEU n 
1 81  ILE n 
1 82  VAL n 
1 83  ASN n 
1 84  PRO n 
1 85  ARG n 
1 86  SER n 
1 87  VAL n 
1 88  GLY n 
1 89  LEU n 
1 90  ALA n 
1 91  ASN n 
1 92  GLN n 
1 93  GLU n 
1 94  LEU n 
1 95  ALA n 
1 96  GLU n 
1 97  VAL n 
1 98  VAL n 
1 99  SER n 
1 100 ARG n 
1 101 ALA n 
1 102 VAL n 
1 103 SER n 
1 104 ASP n 
1 105 GLY n 
1 106 TYR n 
1 107 SER n 
1 108 CYS n 
1 109 VAL n 
1 110 THR n 
1 111 LEU n 
1 112 GLY n 
1 113 GLY n 
1 114 ASP n 
1 115 HIS n 
1 116 SER n 
1 117 LEU n 
1 118 ALA n 
1 119 ILE n 
1 120 GLY n 
1 121 THR n 
1 122 ILE n 
1 123 SER n 
1 124 GLY n 
1 125 HIS n 
1 126 ALA n 
1 127 ARG n 
1 128 HIS n 
1 129 CYS n 
1 130 PRO n 
1 131 ASP n 
1 132 LEU n 
1 133 CYS n 
1 134 VAL n 
1 135 VAL n 
1 136 TRP n 
1 137 VAL n 
1 138 ASP n 
1 139 ALA n 
1 140 HIS n 
1 141 ALA n 
1 142 ASP n 
1 143 ILE n 
1 144 ASN n 
1 145 THR n 
1 146 PRO n 
1 147 LEU n 
1 148 THR n 
1 149 THR n 
1 150 SER n 
1 151 SER n 
1 152 GLY n 
1 153 ASN n 
1 154 LEU n 
1 155 HIS n 
1 156 GLY n 
1 157 GLN n 
1 158 PRO n 
1 159 VAL n 
1 160 SER n 
1 161 PHE n 
1 162 LEU n 
1 163 LEU n 
1 164 ARG n 
1 165 GLU n 
1 166 LEU n 
1 167 GLN n 
1 168 ASP n 
1 169 LYS n 
1 170 VAL n 
1 171 PRO n 
1 172 GLN n 
1 173 LEU n 
1 174 PRO n 
1 175 GLY n 
1 176 PHE n 
1 177 SER n 
1 178 TRP n 
1 179 ILE n 
1 180 LYS n 
1 181 PRO n 
1 182 CYS n 
1 183 ILE n 
1 184 SER n 
1 185 SER n 
1 186 ALA n 
1 187 SER n 
1 188 ILE n 
1 189 VAL n 
1 190 TYR n 
1 191 ILE n 
1 192 GLY n 
1 193 LEU n 
1 194 ARG n 
1 195 ASP n 
1 196 VAL n 
1 197 ASP n 
1 198 PRO n 
1 199 PRO n 
1 200 GLU n 
1 201 HIS n 
1 202 PHE n 
1 203 ILE n 
1 204 LEU n 
1 205 LYS n 
1 206 ASN n 
1 207 TYR n 
1 208 ASP n 
1 209 ILE n 
1 210 GLN n 
1 211 TYR n 
1 212 PHE n 
1 213 SER n 
1 214 MET n 
1 215 ARG n 
1 216 ASP n 
1 217 ILE n 
1 218 ASP n 
1 219 ARG n 
1 220 LEU n 
1 221 GLY n 
1 222 ILE n 
1 223 GLN n 
1 224 LYS n 
1 225 VAL n 
1 226 MET n 
1 227 GLU n 
1 228 ARG n 
1 229 THR n 
1 230 PHE n 
1 231 ASP n 
1 232 LEU n 
1 233 LEU n 
1 234 ILE n 
1 235 GLY n 
1 236 LYS n 
1 237 ARG n 
1 238 GLN n 
1 239 ARG n 
1 240 PRO n 
1 241 ILE n 
1 242 HIS n 
1 243 LEU n 
1 244 SER n 
1 245 PHE n 
1 246 ASP n 
1 247 ILE n 
1 248 ASP n 
1 249 ALA n 
1 250 PHE n 
1 251 ASP n 
1 252 PRO n 
1 253 THR n 
1 254 LEU n 
1 255 ALA n 
1 256 PRO n 
1 257 ALA n 
1 258 THR n 
1 259 GLY n 
1 260 THR n 
1 261 PRO n 
1 262 VAL n 
1 263 VAL n 
1 264 GLY n 
1 265 GLY n 
1 266 LEU n 
1 267 THR n 
1 268 TYR n 
1 269 ARG n 
1 270 GLU n 
1 271 GLY n 
1 272 MET n 
1 273 TYR n 
1 274 ILE n 
1 275 ALA n 
1 276 GLU n 
1 277 GLU n 
1 278 ILE n 
1 279 HIS n 
1 280 ASN n 
1 281 THR n 
1 282 GLY n 
1 283 LEU n 
1 284 LEU n 
1 285 SER n 
1 286 ALA n 
1 287 LEU n 
1 288 ASP n 
1 289 LEU n 
1 290 VAL n 
1 291 GLU n 
1 292 VAL n 
1 293 ASN n 
1 294 PRO n 
1 295 GLN n 
1 296 LEU n 
1 297 ALA n 
1 298 THR n 
1 299 SER n 
1 300 GLU n 
1 301 GLU n 
1 302 GLU n 
1 303 ALA n 
1 304 LYS n 
1 305 THR n 
1 306 THR n 
1 307 ALA n 
1 308 ASN n 
1 309 LEU n 
1 310 ALA n 
1 311 VAL n 
1 312 ASP n 
1 313 VAL n 
1 314 ILE n 
1 315 ALA n 
1 316 SER n 
1 317 SER n 
1 318 PHE n 
1 319 GLY n 
1 320 GLN n 
1 321 THR n 
1 322 ARG n 
1 323 GLU n 
1 324 GLY n 
1 325 GLY n 
1 326 HIS n 
1 327 ILE n 
1 328 VAL n 
1 329 TYR n 
1 330 ASP n 
1 331 GLN n 
1 332 LEU n 
1 333 PRO n 
1 334 THR n 
1 335 PRO n 
1 336 SER 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                   336 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ARG2 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_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 
A1H0B non-polymer         . '(2~{S},3~{R})-3-[3-(dihydroxyboranyl)propyl]pyrrolidine-2-carboxylic acid' ? 'C8 H16 B N O4'  201.028 
ALA   'L-peptide linking' y ALANINE                                                                     ? 'C3 H7 N O2'     89.093  
ARG   'L-peptide linking' y ARGININE                                                                    ? 'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                                  ? 'C4 H8 N2 O3'    132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                             ? 'C4 H7 N O4'     133.103 
CYS   'L-peptide linking' y CYSTEINE                                                                    ? 'C3 H7 N O2 S'   121.158 
GLN   'L-peptide linking' y GLUTAMINE                                                                   ? 'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                             ? 'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE                                                                     ? 'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE                                                                   ? 'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER                                                                       ? 'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                                  ? 'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE                                                                     ? 'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE                                                                      ? 'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE                                                                  ? 'C5 H11 N O2 S'  149.211 
MN    non-polymer         . 'MANGANESE (II) ION'                                                        ? 'Mn 2'           54.938  
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   6   ?   ?   ?   A . n 
A 1 2   HIS 2   7   ?   ?   ?   A . n 
A 1 3   HIS 3   8   ?   ?   ?   A . n 
A 1 4   HIS 4   9   ?   ?   ?   A . n 
A 1 5   HIS 5   10  ?   ?   ?   A . n 
A 1 6   HIS 6   11  ?   ?   ?   A . n 
A 1 7   HIS 7   12  ?   ?   ?   A . n 
A 1 8   GLY 8   13  ?   ?   ?   A . n 
A 1 9   GLY 9   14  ?   ?   ?   A . n 
A 1 10  GLY 10  15  ?   ?   ?   A . n 
A 1 11  GLU 11  16  ?   ?   ?   A . n 
A 1 12  ASN 12  17  ?   ?   ?   A . n 
A 1 13  LEU 13  18  ?   ?   ?   A . n 
A 1 14  TYR 14  19  ?   ?   ?   A . n 
A 1 15  PHE 15  20  ?   ?   ?   A . n 
A 1 16  GLN 16  21  ?   ?   ?   A . n 
A 1 17  SER 17  22  ?   ?   ?   A . n 
A 1 18  VAL 18  23  23  VAL VAL A . n 
A 1 19  HIS 19  24  24  HIS HIS A . n 
A 1 20  SER 20  25  25  SER SER A . n 
A 1 21  VAL 21  26  26  VAL VAL A . n 
A 1 22  ALA 22  27  27  ALA ALA A . n 
A 1 23  VAL 23  28  28  VAL VAL A . n 
A 1 24  ILE 24  29  29  ILE ILE A . n 
A 1 25  GLY 25  30  30  GLY GLY A . n 
A 1 26  ALA 26  31  31  ALA ALA A . n 
A 1 27  PRO 27  32  32  PRO PRO A . n 
A 1 28  PHE 28  33  33  PHE PHE A . n 
A 1 29  SER 29  34  34  SER SER A . n 
A 1 30  GLN 30  35  35  GLN GLN A . n 
A 1 31  GLY 31  36  36  GLY GLY A . n 
A 1 32  GLN 32  37  37  GLN GLN A . n 
A 1 33  LYS 33  38  38  LYS LYS A . n 
A 1 34  ARG 34  39  39  ARG ARG A . n 
A 1 35  LYS 35  40  40  LYS LYS A . n 
A 1 36  GLY 36  41  41  GLY GLY A . n 
A 1 37  VAL 37  42  42  VAL VAL A . n 
A 1 38  GLU 38  43  43  GLU GLU A . n 
A 1 39  HIS 39  44  44  HIS HIS A . n 
A 1 40  GLY 40  45  45  GLY GLY A . n 
A 1 41  PRO 41  46  46  PRO PRO A . n 
A 1 42  ALA 42  47  47  ALA ALA A . n 
A 1 43  ALA 43  48  48  ALA ALA A . n 
A 1 44  ILE 44  49  49  ILE ILE A . n 
A 1 45  ARG 45  50  50  ARG ARG A . n 
A 1 46  GLU 46  51  51  GLU GLU A . n 
A 1 47  ALA 47  52  52  ALA ALA A . n 
A 1 48  GLY 48  53  53  GLY GLY A . n 
A 1 49  LEU 49  54  54  LEU LEU A . n 
A 1 50  MET 50  55  55  MET MET A . n 
A 1 51  LYS 51  56  56  LYS LYS A . n 
A 1 52  ARG 52  57  57  ARG ARG A . n 
A 1 53  LEU 53  58  58  LEU LEU A . n 
A 1 54  SER 54  59  59  SER SER A . n 
A 1 55  SER 55  60  60  SER SER A . n 
A 1 56  LEU 56  61  61  LEU LEU A . n 
A 1 57  GLY 57  62  62  GLY GLY A . n 
A 1 58  CYS 58  63  63  CYS CYS A . n 
A 1 59  HIS 59  64  64  HIS HIS A . n 
A 1 60  LEU 60  65  65  LEU LEU A . n 
A 1 61  LYS 61  66  66  LYS LYS A . n 
A 1 62  ASP 62  67  67  ASP ASP A . n 
A 1 63  PHE 63  68  68  PHE PHE A . n 
A 1 64  GLY 64  69  69  GLY GLY A . n 
A 1 65  ASP 65  70  70  ASP ASP A . n 
A 1 66  LEU 66  71  71  LEU LEU A . n 
A 1 67  SER 67  72  72  SER SER A . n 
A 1 68  PHE 68  73  73  PHE PHE A . n 
A 1 69  THR 69  74  74  THR THR A . n 
A 1 70  PRO 70  75  75  PRO PRO A . n 
A 1 71  VAL 71  76  76  VAL VAL A . n 
A 1 72  PRO 72  77  77  PRO PRO A . n 
A 1 73  LYS 73  78  78  LYS LYS A . n 
A 1 74  ASP 74  79  79  ASP ASP A . n 
A 1 75  ASP 75  80  80  ASP ASP A . n 
A 1 76  LEU 76  81  81  LEU LEU A . n 
A 1 77  TYR 77  82  82  TYR TYR A . n 
A 1 78  ASN 78  83  83  ASN ASN A . n 
A 1 79  ASN 79  84  84  ASN ASN A . n 
A 1 80  LEU 80  85  85  LEU LEU A . n 
A 1 81  ILE 81  86  86  ILE ILE A . n 
A 1 82  VAL 82  87  87  VAL VAL A . n 
A 1 83  ASN 83  88  88  ASN ASN A . n 
A 1 84  PRO 84  89  89  PRO PRO A . n 
A 1 85  ARG 85  90  90  ARG ARG A . n 
A 1 86  SER 86  91  91  SER SER A . n 
A 1 87  VAL 87  92  92  VAL VAL A . n 
A 1 88  GLY 88  93  93  GLY GLY A . n 
A 1 89  LEU 89  94  94  LEU LEU A . n 
A 1 90  ALA 90  95  95  ALA ALA A . n 
A 1 91  ASN 91  96  96  ASN ASN A . n 
A 1 92  GLN 92  97  97  GLN GLN A . n 
A 1 93  GLU 93  98  98  GLU GLU A . n 
A 1 94  LEU 94  99  99  LEU LEU A . n 
A 1 95  ALA 95  100 100 ALA ALA A . n 
A 1 96  GLU 96  101 101 GLU GLU A . n 
A 1 97  VAL 97  102 102 VAL VAL A . n 
A 1 98  VAL 98  103 103 VAL VAL A . n 
A 1 99  SER 99  104 104 SER SER A . n 
A 1 100 ARG 100 105 105 ARG ARG A . n 
A 1 101 ALA 101 106 106 ALA ALA A . n 
A 1 102 VAL 102 107 107 VAL VAL A . n 
A 1 103 SER 103 108 108 SER SER A . n 
A 1 104 ASP 104 109 109 ASP ASP A . n 
A 1 105 GLY 105 110 110 GLY GLY A . n 
A 1 106 TYR 106 111 111 TYR TYR A . n 
A 1 107 SER 107 112 112 SER SER A . n 
A 1 108 CYS 108 113 113 CYS CYS A . n 
A 1 109 VAL 109 114 114 VAL VAL A . n 
A 1 110 THR 110 115 115 THR THR A . n 
A 1 111 LEU 111 116 116 LEU LEU A . n 
A 1 112 GLY 112 117 117 GLY GLY A . n 
A 1 113 GLY 113 118 118 GLY GLY A . n 
A 1 114 ASP 114 119 119 ASP ASP A . n 
A 1 115 HIS 115 120 120 HIS HIS A . n 
A 1 116 SER 116 121 121 SER SER A . n 
A 1 117 LEU 117 122 122 LEU LEU A . n 
A 1 118 ALA 118 123 123 ALA ALA A . n 
A 1 119 ILE 119 124 124 ILE ILE A . n 
A 1 120 GLY 120 125 125 GLY GLY A . n 
A 1 121 THR 121 126 126 THR THR A . n 
A 1 122 ILE 122 127 127 ILE ILE A . n 
A 1 123 SER 123 128 128 SER SER A . n 
A 1 124 GLY 124 129 129 GLY GLY A . n 
A 1 125 HIS 125 130 130 HIS HIS A . n 
A 1 126 ALA 126 131 131 ALA ALA A . n 
A 1 127 ARG 127 132 132 ARG ARG A . n 
A 1 128 HIS 128 133 133 HIS HIS A . n 
A 1 129 CYS 129 134 134 CYS CYS A . n 
A 1 130 PRO 130 135 135 PRO PRO A . n 
A 1 131 ASP 131 136 136 ASP ASP A . n 
A 1 132 LEU 132 137 137 LEU LEU A . n 
A 1 133 CYS 133 138 138 CYS CYS A . n 
A 1 134 VAL 134 139 139 VAL VAL A . n 
A 1 135 VAL 135 140 140 VAL VAL A . n 
A 1 136 TRP 136 141 141 TRP TRP A . n 
A 1 137 VAL 137 142 142 VAL VAL A . n 
A 1 138 ASP 138 143 143 ASP ASP A . n 
A 1 139 ALA 139 144 144 ALA ALA A . n 
A 1 140 HIS 140 145 145 HIS HIS A . n 
A 1 141 ALA 141 146 146 ALA ALA A . n 
A 1 142 ASP 142 147 147 ASP ASP A . n 
A 1 143 ILE 143 148 148 ILE ILE A . n 
A 1 144 ASN 144 149 149 ASN ASN A . n 
A 1 145 THR 145 150 150 THR THR A . n 
A 1 146 PRO 146 151 151 PRO PRO A . n 
A 1 147 LEU 147 152 152 LEU LEU A . n 
A 1 148 THR 148 153 153 THR THR A . n 
A 1 149 THR 149 154 154 THR THR A . n 
A 1 150 SER 150 155 155 SER SER A . n 
A 1 151 SER 151 156 156 SER SER A . n 
A 1 152 GLY 152 157 157 GLY GLY A . n 
A 1 153 ASN 153 158 158 ASN ASN A . n 
A 1 154 LEU 154 159 159 LEU LEU A . n 
A 1 155 HIS 155 160 160 HIS HIS A . n 
A 1 156 GLY 156 161 161 GLY GLY A . n 
A 1 157 GLN 157 162 162 GLN GLN A . n 
A 1 158 PRO 158 163 163 PRO PRO A . n 
A 1 159 VAL 159 164 164 VAL VAL A . n 
A 1 160 SER 160 165 165 SER SER A . n 
A 1 161 PHE 161 166 166 PHE PHE A . n 
A 1 162 LEU 162 167 167 LEU LEU A . n 
A 1 163 LEU 163 168 168 LEU LEU A . n 
A 1 164 ARG 164 169 169 ARG ARG A . n 
A 1 165 GLU 165 170 170 GLU GLU A . n 
A 1 166 LEU 166 171 171 LEU LEU A . n 
A 1 167 GLN 167 172 172 GLN GLN A . n 
A 1 168 ASP 168 173 173 ASP ASP A . n 
A 1 169 LYS 169 174 174 LYS LYS A . n 
A 1 170 VAL 170 175 175 VAL VAL A . n 
A 1 171 PRO 171 176 176 PRO PRO A . n 
A 1 172 GLN 172 177 177 GLN GLN A . n 
A 1 173 LEU 173 178 178 LEU LEU A . n 
A 1 174 PRO 174 179 179 PRO PRO A . n 
A 1 175 GLY 175 180 180 GLY GLY A . n 
A 1 176 PHE 176 181 181 PHE PHE A . n 
A 1 177 SER 177 182 182 SER SER A . n 
A 1 178 TRP 178 183 183 TRP TRP A . n 
A 1 179 ILE 179 184 184 ILE ILE A . n 
A 1 180 LYS 180 185 185 LYS LYS A . n 
A 1 181 PRO 181 186 186 PRO PRO A . n 
A 1 182 CYS 182 187 187 CYS CYS A . n 
A 1 183 ILE 183 188 188 ILE ILE A . n 
A 1 184 SER 184 189 189 SER SER A . n 
A 1 185 SER 185 190 190 SER SER A . n 
A 1 186 ALA 186 191 191 ALA ALA A . n 
A 1 187 SER 187 192 192 SER SER A . n 
A 1 188 ILE 188 193 193 ILE ILE A . n 
A 1 189 VAL 189 194 194 VAL VAL A . n 
A 1 190 TYR 190 195 195 TYR TYR A . n 
A 1 191 ILE 191 196 196 ILE ILE A . n 
A 1 192 GLY 192 197 197 GLY GLY A . n 
A 1 193 LEU 193 198 198 LEU LEU A . n 
A 1 194 ARG 194 199 199 ARG ARG A . n 
A 1 195 ASP 195 200 200 ASP ASP A . n 
A 1 196 VAL 196 201 201 VAL VAL A . n 
A 1 197 ASP 197 202 202 ASP ASP A . n 
A 1 198 PRO 198 203 203 PRO PRO A . n 
A 1 199 PRO 199 204 204 PRO PRO A . n 
A 1 200 GLU 200 205 205 GLU GLU A . n 
A 1 201 HIS 201 206 206 HIS HIS A . n 
A 1 202 PHE 202 207 207 PHE PHE A . n 
A 1 203 ILE 203 208 208 ILE ILE A . n 
A 1 204 LEU 204 209 209 LEU LEU A . n 
A 1 205 LYS 205 210 210 LYS LYS A . n 
A 1 206 ASN 206 211 211 ASN ASN A . n 
A 1 207 TYR 207 212 212 TYR TYR A . n 
A 1 208 ASP 208 213 213 ASP ASP A . n 
A 1 209 ILE 209 214 214 ILE ILE A . n 
A 1 210 GLN 210 215 215 GLN GLN A . n 
A 1 211 TYR 211 216 216 TYR TYR A . n 
A 1 212 PHE 212 217 217 PHE PHE A . n 
A 1 213 SER 213 218 218 SER SER A . n 
A 1 214 MET 214 219 219 MET MET A . n 
A 1 215 ARG 215 220 220 ARG ARG A . n 
A 1 216 ASP 216 221 221 ASP ASP A . n 
A 1 217 ILE 217 222 222 ILE ILE A . n 
A 1 218 ASP 218 223 223 ASP ASP A . n 
A 1 219 ARG 219 224 224 ARG ARG A . n 
A 1 220 LEU 220 225 225 LEU LEU A . n 
A 1 221 GLY 221 226 226 GLY GLY A . n 
A 1 222 ILE 222 227 227 ILE ILE A . n 
A 1 223 GLN 223 228 228 GLN GLN A . n 
A 1 224 LYS 224 229 229 LYS LYS A . n 
A 1 225 VAL 225 230 230 VAL VAL A . n 
A 1 226 MET 226 231 231 MET MET A . n 
A 1 227 GLU 227 232 232 GLU GLU A . n 
A 1 228 ARG 228 233 233 ARG ARG A . n 
A 1 229 THR 229 234 234 THR THR A . n 
A 1 230 PHE 230 235 235 PHE PHE A . n 
A 1 231 ASP 231 236 236 ASP ASP A . n 
A 1 232 LEU 232 237 237 LEU LEU A . n 
A 1 233 LEU 233 238 238 LEU LEU A . n 
A 1 234 ILE 234 239 239 ILE ILE A . n 
A 1 235 GLY 235 240 240 GLY GLY A . n 
A 1 236 LYS 236 241 241 LYS LYS A . n 
A 1 237 ARG 237 242 242 ARG ARG A . n 
A 1 238 GLN 238 243 243 GLN GLN A . n 
A 1 239 ARG 239 244 244 ARG ARG A . n 
A 1 240 PRO 240 245 245 PRO PRO A . n 
A 1 241 ILE 241 246 246 ILE ILE A . n 
A 1 242 HIS 242 247 247 HIS HIS A . n 
A 1 243 LEU 243 248 248 LEU LEU A . n 
A 1 244 SER 244 249 249 SER SER A . n 
A 1 245 PHE 245 250 250 PHE PHE A . n 
A 1 246 ASP 246 251 251 ASP ASP A . n 
A 1 247 ILE 247 252 252 ILE ILE A . n 
A 1 248 ASP 248 253 253 ASP ASP A . n 
A 1 249 ALA 249 254 254 ALA ALA A . n 
A 1 250 PHE 250 255 255 PHE PHE A . n 
A 1 251 ASP 251 256 256 ASP ASP A . n 
A 1 252 PRO 252 257 257 PRO PRO A . n 
A 1 253 THR 253 258 258 THR THR A . n 
A 1 254 LEU 254 259 259 LEU LEU A . n 
A 1 255 ALA 255 260 260 ALA ALA A . n 
A 1 256 PRO 256 261 261 PRO PRO A . n 
A 1 257 ALA 257 262 262 ALA ALA A . n 
A 1 258 THR 258 263 263 THR THR A . n 
A 1 259 GLY 259 264 264 GLY GLY A . n 
A 1 260 THR 260 265 265 THR THR A . n 
A 1 261 PRO 261 266 266 PRO PRO A . n 
A 1 262 VAL 262 267 267 VAL VAL A . n 
A 1 263 VAL 263 268 268 VAL VAL A . n 
A 1 264 GLY 264 269 269 GLY GLY A . n 
A 1 265 GLY 265 270 270 GLY GLY A . n 
A 1 266 LEU 266 271 271 LEU LEU A . n 
A 1 267 THR 267 272 272 THR THR A . n 
A 1 268 TYR 268 273 273 TYR TYR A . n 
A 1 269 ARG 269 274 274 ARG ARG A . n 
A 1 270 GLU 270 275 275 GLU GLU A . n 
A 1 271 GLY 271 276 276 GLY GLY A . n 
A 1 272 MET 272 277 277 MET MET A . n 
A 1 273 TYR 273 278 278 TYR TYR A . n 
A 1 274 ILE 274 279 279 ILE ILE A . n 
A 1 275 ALA 275 280 280 ALA ALA A . n 
A 1 276 GLU 276 281 281 GLU GLU A . n 
A 1 277 GLU 277 282 282 GLU GLU A . n 
A 1 278 ILE 278 283 283 ILE ILE A . n 
A 1 279 HIS 279 284 284 HIS HIS A . n 
A 1 280 ASN 280 285 285 ASN ASN A . n 
A 1 281 THR 281 286 286 THR THR A . n 
A 1 282 GLY 282 287 287 GLY GLY A . n 
A 1 283 LEU 283 288 288 LEU LEU A . n 
A 1 284 LEU 284 289 289 LEU LEU A . n 
A 1 285 SER 285 290 290 SER SER A . n 
A 1 286 ALA 286 291 291 ALA ALA A . n 
A 1 287 LEU 287 292 292 LEU LEU A . n 
A 1 288 ASP 288 293 293 ASP ASP A . n 
A 1 289 LEU 289 294 294 LEU LEU A . n 
A 1 290 VAL 290 295 295 VAL VAL A . n 
A 1 291 GLU 291 296 296 GLU GLU A . n 
A 1 292 VAL 292 297 297 VAL VAL A . n 
A 1 293 ASN 293 298 298 ASN ASN A . n 
A 1 294 PRO 294 299 299 PRO PRO A . n 
A 1 295 GLN 295 300 300 GLN GLN A . n 
A 1 296 LEU 296 301 301 LEU LEU A . n 
A 1 297 ALA 297 302 302 ALA ALA A . n 
A 1 298 THR 298 303 303 THR THR A . n 
A 1 299 SER 299 304 304 SER SER A . n 
A 1 300 GLU 300 305 305 GLU GLU A . n 
A 1 301 GLU 301 306 306 GLU GLU A . n 
A 1 302 GLU 302 307 307 GLU GLU A . n 
A 1 303 ALA 303 308 308 ALA ALA A . n 
A 1 304 LYS 304 309 309 LYS LYS A . n 
A 1 305 THR 305 310 310 THR THR A . n 
A 1 306 THR 306 311 311 THR THR A . n 
A 1 307 ALA 307 312 312 ALA ALA A . n 
A 1 308 ASN 308 313 313 ASN ASN A . n 
A 1 309 LEU 309 314 314 LEU LEU A . n 
A 1 310 ALA 310 315 315 ALA ALA A . n 
A 1 311 VAL 311 316 316 VAL VAL A . n 
A 1 312 ASP 312 317 317 ASP ASP A . n 
A 1 313 VAL 313 318 318 VAL VAL A . n 
A 1 314 ILE 314 319 319 ILE ILE A . n 
A 1 315 ALA 315 320 320 ALA ALA A . n 
A 1 316 SER 316 321 321 SER SER A . n 
A 1 317 SER 317 322 322 SER SER A . n 
A 1 318 PHE 318 323 323 PHE PHE A . n 
A 1 319 GLY 319 324 324 GLY GLY A . n 
A 1 320 GLN 320 325 325 GLN GLN A . n 
A 1 321 THR 321 326 326 THR THR A . n 
A 1 322 ARG 322 327 327 ARG ARG A . n 
A 1 323 GLU 323 328 328 GLU GLU A . n 
A 1 324 GLY 324 329 329 GLY GLY A . n 
A 1 325 GLY 325 330 330 GLY GLY A . n 
A 1 326 HIS 326 331 331 HIS HIS A . n 
A 1 327 ILE 327 332 332 ILE ILE A . n 
A 1 328 VAL 328 333 333 VAL VAL A . n 
A 1 329 TYR 329 334 334 TYR TYR A . n 
A 1 330 ASP 330 335 335 ASP ASP A . n 
A 1 331 GLN 331 336 336 GLN GLN A . n 
A 1 332 LEU 332 337 337 LEU LEU A . n 
A 1 333 PRO 333 338 338 PRO PRO A . n 
A 1 334 THR 334 339 339 THR THR A . n 
A 1 335 PRO 335 340 340 PRO PRO A . n 
A 1 336 SER 336 341 ?   ?   ?   A . n 
B 1 1   MET 1   6   ?   ?   ?   B . n 
B 1 2   HIS 2   7   ?   ?   ?   B . n 
B 1 3   HIS 3   8   ?   ?   ?   B . n 
B 1 4   HIS 4   9   ?   ?   ?   B . n 
B 1 5   HIS 5   10  ?   ?   ?   B . n 
B 1 6   HIS 6   11  ?   ?   ?   B . n 
B 1 7   HIS 7   12  ?   ?   ?   B . n 
B 1 8   GLY 8   13  ?   ?   ?   B . n 
B 1 9   GLY 9   14  ?   ?   ?   B . n 
B 1 10  GLY 10  15  ?   ?   ?   B . n 
B 1 11  GLU 11  16  ?   ?   ?   B . n 
B 1 12  ASN 12  17  17  ASN ASN B . n 
B 1 13  LEU 13  18  18  LEU LEU B . n 
B 1 14  TYR 14  19  19  TYR TYR B . n 
B 1 15  PHE 15  20  20  PHE PHE B . n 
B 1 16  GLN 16  21  21  GLN GLN B . n 
B 1 17  SER 17  22  22  SER SER B . n 
B 1 18  VAL 18  23  23  VAL VAL B . n 
B 1 19  HIS 19  24  24  HIS HIS B . n 
B 1 20  SER 20  25  25  SER SER B . n 
B 1 21  VAL 21  26  26  VAL VAL B . n 
B 1 22  ALA 22  27  27  ALA ALA B . n 
B 1 23  VAL 23  28  28  VAL VAL B . n 
B 1 24  ILE 24  29  29  ILE ILE B . n 
B 1 25  GLY 25  30  30  GLY GLY B . n 
B 1 26  ALA 26  31  31  ALA ALA B . n 
B 1 27  PRO 27  32  32  PRO PRO B . n 
B 1 28  PHE 28  33  33  PHE PHE B . n 
B 1 29  SER 29  34  34  SER SER B . n 
B 1 30  GLN 30  35  35  GLN GLN B . n 
B 1 31  GLY 31  36  36  GLY GLY B . n 
B 1 32  GLN 32  37  37  GLN GLN B . n 
B 1 33  LYS 33  38  38  LYS LYS B . n 
B 1 34  ARG 34  39  39  ARG ARG B . n 
B 1 35  LYS 35  40  40  LYS LYS B . n 
B 1 36  GLY 36  41  41  GLY GLY B . n 
B 1 37  VAL 37  42  42  VAL VAL B . n 
B 1 38  GLU 38  43  43  GLU GLU B . n 
B 1 39  HIS 39  44  44  HIS HIS B . n 
B 1 40  GLY 40  45  45  GLY GLY B . n 
B 1 41  PRO 41  46  46  PRO PRO B . n 
B 1 42  ALA 42  47  47  ALA ALA B . n 
B 1 43  ALA 43  48  48  ALA ALA B . n 
B 1 44  ILE 44  49  49  ILE ILE B . n 
B 1 45  ARG 45  50  50  ARG ARG B . n 
B 1 46  GLU 46  51  51  GLU GLU B . n 
B 1 47  ALA 47  52  52  ALA ALA B . n 
B 1 48  GLY 48  53  53  GLY GLY B . n 
B 1 49  LEU 49  54  54  LEU LEU B . n 
B 1 50  MET 50  55  55  MET MET B . n 
B 1 51  LYS 51  56  56  LYS LYS B . n 
B 1 52  ARG 52  57  57  ARG ARG B . n 
B 1 53  LEU 53  58  58  LEU LEU B . n 
B 1 54  SER 54  59  59  SER SER B . n 
B 1 55  SER 55  60  60  SER SER B . n 
B 1 56  LEU 56  61  61  LEU LEU B . n 
B 1 57  GLY 57  62  62  GLY GLY B . n 
B 1 58  CYS 58  63  63  CYS CYS B . n 
B 1 59  HIS 59  64  64  HIS HIS B . n 
B 1 60  LEU 60  65  65  LEU LEU B . n 
B 1 61  LYS 61  66  66  LYS LYS B . n 
B 1 62  ASP 62  67  67  ASP ASP B . n 
B 1 63  PHE 63  68  68  PHE PHE B . n 
B 1 64  GLY 64  69  69  GLY GLY B . n 
B 1 65  ASP 65  70  70  ASP ASP B . n 
B 1 66  LEU 66  71  71  LEU LEU B . n 
B 1 67  SER 67  72  72  SER SER B . n 
B 1 68  PHE 68  73  73  PHE PHE B . n 
B 1 69  THR 69  74  74  THR THR B . n 
B 1 70  PRO 70  75  75  PRO PRO B . n 
B 1 71  VAL 71  76  76  VAL VAL B . n 
B 1 72  PRO 72  77  77  PRO PRO B . n 
B 1 73  LYS 73  78  78  LYS LYS B . n 
B 1 74  ASP 74  79  79  ASP ASP B . n 
B 1 75  ASP 75  80  80  ASP ASP B . n 
B 1 76  LEU 76  81  81  LEU LEU B . n 
B 1 77  TYR 77  82  82  TYR TYR B . n 
B 1 78  ASN 78  83  83  ASN ASN B . n 
B 1 79  ASN 79  84  84  ASN ASN B . n 
B 1 80  LEU 80  85  85  LEU LEU B . n 
B 1 81  ILE 81  86  86  ILE ILE B . n 
B 1 82  VAL 82  87  87  VAL VAL B . n 
B 1 83  ASN 83  88  88  ASN ASN B . n 
B 1 84  PRO 84  89  89  PRO PRO B . n 
B 1 85  ARG 85  90  90  ARG ARG B . n 
B 1 86  SER 86  91  91  SER SER B . n 
B 1 87  VAL 87  92  92  VAL VAL B . n 
B 1 88  GLY 88  93  93  GLY GLY B . n 
B 1 89  LEU 89  94  94  LEU LEU B . n 
B 1 90  ALA 90  95  95  ALA ALA B . n 
B 1 91  ASN 91  96  96  ASN ASN B . n 
B 1 92  GLN 92  97  97  GLN GLN B . n 
B 1 93  GLU 93  98  98  GLU GLU B . n 
B 1 94  LEU 94  99  99  LEU LEU B . n 
B 1 95  ALA 95  100 100 ALA ALA B . n 
B 1 96  GLU 96  101 101 GLU GLU B . n 
B 1 97  VAL 97  102 102 VAL VAL B . n 
B 1 98  VAL 98  103 103 VAL VAL B . n 
B 1 99  SER 99  104 104 SER SER B . n 
B 1 100 ARG 100 105 105 ARG ARG B . n 
B 1 101 ALA 101 106 106 ALA ALA B . n 
B 1 102 VAL 102 107 107 VAL VAL B . n 
B 1 103 SER 103 108 108 SER SER B . n 
B 1 104 ASP 104 109 109 ASP ASP B . n 
B 1 105 GLY 105 110 110 GLY GLY B . n 
B 1 106 TYR 106 111 111 TYR TYR B . n 
B 1 107 SER 107 112 112 SER SER B . n 
B 1 108 CYS 108 113 113 CYS CYS B . n 
B 1 109 VAL 109 114 114 VAL VAL B . n 
B 1 110 THR 110 115 115 THR THR B . n 
B 1 111 LEU 111 116 116 LEU LEU B . n 
B 1 112 GLY 112 117 117 GLY GLY B . n 
B 1 113 GLY 113 118 118 GLY GLY B . n 
B 1 114 ASP 114 119 119 ASP ASP B . n 
B 1 115 HIS 115 120 120 HIS HIS B . n 
B 1 116 SER 116 121 121 SER SER B . n 
B 1 117 LEU 117 122 122 LEU LEU B . n 
B 1 118 ALA 118 123 123 ALA ALA B . n 
B 1 119 ILE 119 124 124 ILE ILE B . n 
B 1 120 GLY 120 125 125 GLY GLY B . n 
B 1 121 THR 121 126 126 THR THR B . n 
B 1 122 ILE 122 127 127 ILE ILE B . n 
B 1 123 SER 123 128 128 SER SER B . n 
B 1 124 GLY 124 129 129 GLY GLY B . n 
B 1 125 HIS 125 130 130 HIS HIS B . n 
B 1 126 ALA 126 131 131 ALA ALA B . n 
B 1 127 ARG 127 132 132 ARG ARG B . n 
B 1 128 HIS 128 133 133 HIS HIS B . n 
B 1 129 CYS 129 134 134 CYS CYS B . n 
B 1 130 PRO 130 135 135 PRO PRO B . n 
B 1 131 ASP 131 136 136 ASP ASP B . n 
B 1 132 LEU 132 137 137 LEU LEU B . n 
B 1 133 CYS 133 138 138 CYS CYS B . n 
B 1 134 VAL 134 139 139 VAL VAL B . n 
B 1 135 VAL 135 140 140 VAL VAL B . n 
B 1 136 TRP 136 141 141 TRP TRP B . n 
B 1 137 VAL 137 142 142 VAL VAL B . n 
B 1 138 ASP 138 143 143 ASP ASP B . n 
B 1 139 ALA 139 144 144 ALA ALA B . n 
B 1 140 HIS 140 145 145 HIS HIS B . n 
B 1 141 ALA 141 146 146 ALA ALA B . n 
B 1 142 ASP 142 147 147 ASP ASP B . n 
B 1 143 ILE 143 148 148 ILE ILE B . n 
B 1 144 ASN 144 149 149 ASN ASN B . n 
B 1 145 THR 145 150 150 THR THR B . n 
B 1 146 PRO 146 151 151 PRO PRO B . n 
B 1 147 LEU 147 152 152 LEU LEU B . n 
B 1 148 THR 148 153 153 THR THR B . n 
B 1 149 THR 149 154 154 THR THR B . n 
B 1 150 SER 150 155 155 SER SER B . n 
B 1 151 SER 151 156 156 SER SER B . n 
B 1 152 GLY 152 157 157 GLY GLY B . n 
B 1 153 ASN 153 158 158 ASN ASN B . n 
B 1 154 LEU 154 159 159 LEU LEU B . n 
B 1 155 HIS 155 160 160 HIS HIS B . n 
B 1 156 GLY 156 161 161 GLY GLY B . n 
B 1 157 GLN 157 162 162 GLN GLN B . n 
B 1 158 PRO 158 163 163 PRO PRO B . n 
B 1 159 VAL 159 164 164 VAL VAL B . n 
B 1 160 SER 160 165 165 SER SER B . n 
B 1 161 PHE 161 166 166 PHE PHE B . n 
B 1 162 LEU 162 167 167 LEU LEU B . n 
B 1 163 LEU 163 168 168 LEU LEU B . n 
B 1 164 ARG 164 169 169 ARG ARG B . n 
B 1 165 GLU 165 170 170 GLU GLU B . n 
B 1 166 LEU 166 171 171 LEU LEU B . n 
B 1 167 GLN 167 172 172 GLN GLN B . n 
B 1 168 ASP 168 173 173 ASP ASP B . n 
B 1 169 LYS 169 174 174 LYS LYS B . n 
B 1 170 VAL 170 175 175 VAL VAL B . n 
B 1 171 PRO 171 176 176 PRO PRO B . n 
B 1 172 GLN 172 177 177 GLN GLN B . n 
B 1 173 LEU 173 178 178 LEU LEU B . n 
B 1 174 PRO 174 179 179 PRO PRO B . n 
B 1 175 GLY 175 180 180 GLY GLY B . n 
B 1 176 PHE 176 181 181 PHE PHE B . n 
B 1 177 SER 177 182 182 SER SER B . n 
B 1 178 TRP 178 183 183 TRP TRP B . n 
B 1 179 ILE 179 184 184 ILE ILE B . n 
B 1 180 LYS 180 185 185 LYS LYS B . n 
B 1 181 PRO 181 186 186 PRO PRO B . n 
B 1 182 CYS 182 187 187 CYS CYS B . n 
B 1 183 ILE 183 188 188 ILE ILE B . n 
B 1 184 SER 184 189 189 SER SER B . n 
B 1 185 SER 185 190 190 SER SER B . n 
B 1 186 ALA 186 191 191 ALA ALA B . n 
B 1 187 SER 187 192 192 SER SER B . n 
B 1 188 ILE 188 193 193 ILE ILE B . n 
B 1 189 VAL 189 194 194 VAL VAL B . n 
B 1 190 TYR 190 195 195 TYR TYR B . n 
B 1 191 ILE 191 196 196 ILE ILE B . n 
B 1 192 GLY 192 197 197 GLY GLY B . n 
B 1 193 LEU 193 198 198 LEU LEU B . n 
B 1 194 ARG 194 199 199 ARG ARG B . n 
B 1 195 ASP 195 200 200 ASP ASP B . n 
B 1 196 VAL 196 201 201 VAL VAL B . n 
B 1 197 ASP 197 202 202 ASP ASP B . n 
B 1 198 PRO 198 203 203 PRO PRO B . n 
B 1 199 PRO 199 204 204 PRO PRO B . n 
B 1 200 GLU 200 205 205 GLU GLU B . n 
B 1 201 HIS 201 206 206 HIS HIS B . n 
B 1 202 PHE 202 207 207 PHE PHE B . n 
B 1 203 ILE 203 208 208 ILE ILE B . n 
B 1 204 LEU 204 209 209 LEU LEU B . n 
B 1 205 LYS 205 210 210 LYS LYS B . n 
B 1 206 ASN 206 211 211 ASN ASN B . n 
B 1 207 TYR 207 212 212 TYR TYR B . n 
B 1 208 ASP 208 213 213 ASP ASP B . n 
B 1 209 ILE 209 214 214 ILE ILE B . n 
B 1 210 GLN 210 215 215 GLN GLN B . n 
B 1 211 TYR 211 216 216 TYR TYR B . n 
B 1 212 PHE 212 217 217 PHE PHE B . n 
B 1 213 SER 213 218 218 SER SER B . n 
B 1 214 MET 214 219 219 MET MET B . n 
B 1 215 ARG 215 220 220 ARG ARG B . n 
B 1 216 ASP 216 221 221 ASP ASP B . n 
B 1 217 ILE 217 222 222 ILE ILE B . n 
B 1 218 ASP 218 223 223 ASP ASP B . n 
B 1 219 ARG 219 224 224 ARG ARG B . n 
B 1 220 LEU 220 225 225 LEU LEU B . n 
B 1 221 GLY 221 226 226 GLY GLY B . n 
B 1 222 ILE 222 227 227 ILE ILE B . n 
B 1 223 GLN 223 228 228 GLN GLN B . n 
B 1 224 LYS 224 229 229 LYS LYS B . n 
B 1 225 VAL 225 230 230 VAL VAL B . n 
B 1 226 MET 226 231 231 MET MET B . n 
B 1 227 GLU 227 232 232 GLU GLU B . n 
B 1 228 ARG 228 233 233 ARG ARG B . n 
B 1 229 THR 229 234 234 THR THR B . n 
B 1 230 PHE 230 235 235 PHE PHE B . n 
B 1 231 ASP 231 236 236 ASP ASP B . n 
B 1 232 LEU 232 237 237 LEU LEU B . n 
B 1 233 LEU 233 238 238 LEU LEU B . n 
B 1 234 ILE 234 239 239 ILE ILE B . n 
B 1 235 GLY 235 240 240 GLY GLY B . n 
B 1 236 LYS 236 241 241 LYS LYS B . n 
B 1 237 ARG 237 242 242 ARG ARG B . n 
B 1 238 GLN 238 243 243 GLN GLN B . n 
B 1 239 ARG 239 244 244 ARG ARG B . n 
B 1 240 PRO 240 245 245 PRO PRO B . n 
B 1 241 ILE 241 246 246 ILE ILE B . n 
B 1 242 HIS 242 247 247 HIS HIS B . n 
B 1 243 LEU 243 248 248 LEU LEU B . n 
B 1 244 SER 244 249 249 SER SER B . n 
B 1 245 PHE 245 250 250 PHE PHE B . n 
B 1 246 ASP 246 251 251 ASP ASP B . n 
B 1 247 ILE 247 252 252 ILE ILE B . n 
B 1 248 ASP 248 253 253 ASP ASP B . n 
B 1 249 ALA 249 254 254 ALA ALA B . n 
B 1 250 PHE 250 255 255 PHE PHE B . n 
B 1 251 ASP 251 256 256 ASP ASP B . n 
B 1 252 PRO 252 257 257 PRO PRO B . n 
B 1 253 THR 253 258 258 THR THR B . n 
B 1 254 LEU 254 259 259 LEU LEU B . n 
B 1 255 ALA 255 260 260 ALA ALA B . n 
B 1 256 PRO 256 261 261 PRO PRO B . n 
B 1 257 ALA 257 262 262 ALA ALA B . n 
B 1 258 THR 258 263 263 THR THR B . n 
B 1 259 GLY 259 264 264 GLY GLY B . n 
B 1 260 THR 260 265 265 THR THR B . n 
B 1 261 PRO 261 266 266 PRO PRO B . n 
B 1 262 VAL 262 267 267 VAL VAL B . n 
B 1 263 VAL 263 268 268 VAL VAL B . n 
B 1 264 GLY 264 269 269 GLY GLY B . n 
B 1 265 GLY 265 270 270 GLY GLY B . n 
B 1 266 LEU 266 271 271 LEU LEU B . n 
B 1 267 THR 267 272 272 THR THR B . n 
B 1 268 TYR 268 273 273 TYR TYR B . n 
B 1 269 ARG 269 274 274 ARG ARG B . n 
B 1 270 GLU 270 275 275 GLU GLU B . n 
B 1 271 GLY 271 276 276 GLY GLY B . n 
B 1 272 MET 272 277 277 MET MET B . n 
B 1 273 TYR 273 278 278 TYR TYR B . n 
B 1 274 ILE 274 279 279 ILE ILE B . n 
B 1 275 ALA 275 280 280 ALA ALA B . n 
B 1 276 GLU 276 281 281 GLU GLU B . n 
B 1 277 GLU 277 282 282 GLU GLU B . n 
B 1 278 ILE 278 283 283 ILE ILE B . n 
B 1 279 HIS 279 284 284 HIS HIS B . n 
B 1 280 ASN 280 285 285 ASN ASN B . n 
B 1 281 THR 281 286 286 THR THR B . n 
B 1 282 GLY 282 287 287 GLY GLY B . n 
B 1 283 LEU 283 288 288 LEU LEU B . n 
B 1 284 LEU 284 289 289 LEU LEU B . n 
B 1 285 SER 285 290 290 SER SER B . n 
B 1 286 ALA 286 291 291 ALA ALA B . n 
B 1 287 LEU 287 292 292 LEU LEU B . n 
B 1 288 ASP 288 293 293 ASP ASP B . n 
B 1 289 LEU 289 294 294 LEU LEU B . n 
B 1 290 VAL 290 295 295 VAL VAL B . n 
B 1 291 GLU 291 296 296 GLU GLU B . n 
B 1 292 VAL 292 297 297 VAL VAL B . n 
B 1 293 ASN 293 298 298 ASN ASN B . n 
B 1 294 PRO 294 299 299 PRO PRO B . n 
B 1 295 GLN 295 300 300 GLN GLN B . n 
B 1 296 LEU 296 301 301 LEU LEU B . n 
B 1 297 ALA 297 302 302 ALA ALA B . n 
B 1 298 THR 298 303 303 THR THR B . n 
B 1 299 SER 299 304 304 SER SER B . n 
B 1 300 GLU 300 305 305 GLU GLU B . n 
B 1 301 GLU 301 306 306 GLU GLU B . n 
B 1 302 GLU 302 307 307 GLU GLU B . n 
B 1 303 ALA 303 308 308 ALA ALA B . n 
B 1 304 LYS 304 309 309 LYS LYS B . n 
B 1 305 THR 305 310 310 THR THR B . n 
B 1 306 THR 306 311 311 THR THR B . n 
B 1 307 ALA 307 312 312 ALA ALA B . n 
B 1 308 ASN 308 313 313 ASN ASN B . n 
B 1 309 LEU 309 314 314 LEU LEU B . n 
B 1 310 ALA 310 315 315 ALA ALA B . n 
B 1 311 VAL 311 316 316 VAL VAL B . n 
B 1 312 ASP 312 317 317 ASP ASP B . n 
B 1 313 VAL 313 318 318 VAL VAL B . n 
B 1 314 ILE 314 319 319 ILE ILE B . n 
B 1 315 ALA 315 320 320 ALA ALA B . n 
B 1 316 SER 316 321 321 SER SER B . n 
B 1 317 SER 317 322 322 SER SER B . n 
B 1 318 PHE 318 323 323 PHE PHE B . n 
B 1 319 GLY 319 324 324 GLY GLY B . n 
B 1 320 GLN 320 325 325 GLN GLN B . n 
B 1 321 THR 321 326 326 THR THR B . n 
B 1 322 ARG 322 327 327 ARG ARG B . n 
B 1 323 GLU 323 328 328 GLU GLU B . n 
B 1 324 GLY 324 329 329 GLY GLY B . n 
B 1 325 GLY 325 330 330 GLY GLY B . n 
B 1 326 HIS 326 331 331 HIS HIS B . n 
B 1 327 ILE 327 332 332 ILE ILE B . n 
B 1 328 VAL 328 333 333 VAL VAL B . n 
B 1 329 TYR 329 334 334 TYR TYR B . n 
B 1 330 ASP 330 335 335 ASP ASP B . n 
B 1 331 GLN 331 336 336 GLN GLN B . n 
B 1 332 LEU 332 337 337 LEU LEU B . n 
B 1 333 PRO 333 338 338 PRO PRO B . n 
B 1 334 THR 334 339 339 THR THR B . n 
B 1 335 PRO 335 340 340 PRO PRO B . n 
B 1 336 SER 336 341 ?   ?   ?   B . n 
C 1 1   MET 1   6   ?   ?   ?   C . n 
C 1 2   HIS 2   7   ?   ?   ?   C . n 
C 1 3   HIS 3   8   ?   ?   ?   C . n 
C 1 4   HIS 4   9   ?   ?   ?   C . n 
C 1 5   HIS 5   10  ?   ?   ?   C . n 
C 1 6   HIS 6   11  ?   ?   ?   C . n 
C 1 7   HIS 7   12  ?   ?   ?   C . n 
C 1 8   GLY 8   13  ?   ?   ?   C . n 
C 1 9   GLY 9   14  ?   ?   ?   C . n 
C 1 10  GLY 10  15  ?   ?   ?   C . n 
C 1 11  GLU 11  16  ?   ?   ?   C . n 
C 1 12  ASN 12  17  ?   ?   ?   C . n 
C 1 13  LEU 13  18  ?   ?   ?   C . n 
C 1 14  TYR 14  19  ?   ?   ?   C . n 
C 1 15  PHE 15  20  ?   ?   ?   C . n 
C 1 16  GLN 16  21  ?   ?   ?   C . n 
C 1 17  SER 17  22  ?   ?   ?   C . n 
C 1 18  VAL 18  23  23  VAL VAL C . n 
C 1 19  HIS 19  24  24  HIS HIS C . n 
C 1 20  SER 20  25  25  SER SER C . n 
C 1 21  VAL 21  26  26  VAL VAL C . n 
C 1 22  ALA 22  27  27  ALA ALA C . n 
C 1 23  VAL 23  28  28  VAL VAL C . n 
C 1 24  ILE 24  29  29  ILE ILE C . n 
C 1 25  GLY 25  30  30  GLY GLY C . n 
C 1 26  ALA 26  31  31  ALA ALA C . n 
C 1 27  PRO 27  32  32  PRO PRO C . n 
C 1 28  PHE 28  33  33  PHE PHE C . n 
C 1 29  SER 29  34  34  SER SER C . n 
C 1 30  GLN 30  35  35  GLN GLN C . n 
C 1 31  GLY 31  36  36  GLY GLY C . n 
C 1 32  GLN 32  37  37  GLN GLN C . n 
C 1 33  LYS 33  38  38  LYS LYS C . n 
C 1 34  ARG 34  39  39  ARG ARG C . n 
C 1 35  LYS 35  40  40  LYS LYS C . n 
C 1 36  GLY 36  41  41  GLY GLY C . n 
C 1 37  VAL 37  42  42  VAL VAL C . n 
C 1 38  GLU 38  43  43  GLU GLU C . n 
C 1 39  HIS 39  44  44  HIS HIS C . n 
C 1 40  GLY 40  45  45  GLY GLY C . n 
C 1 41  PRO 41  46  46  PRO PRO C . n 
C 1 42  ALA 42  47  47  ALA ALA C . n 
C 1 43  ALA 43  48  48  ALA ALA C . n 
C 1 44  ILE 44  49  49  ILE ILE C . n 
C 1 45  ARG 45  50  50  ARG ARG C . n 
C 1 46  GLU 46  51  51  GLU GLU C . n 
C 1 47  ALA 47  52  52  ALA ALA C . n 
C 1 48  GLY 48  53  53  GLY GLY C . n 
C 1 49  LEU 49  54  54  LEU LEU C . n 
C 1 50  MET 50  55  55  MET MET C . n 
C 1 51  LYS 51  56  56  LYS LYS C . n 
C 1 52  ARG 52  57  57  ARG ARG C . n 
C 1 53  LEU 53  58  58  LEU LEU C . n 
C 1 54  SER 54  59  59  SER SER C . n 
C 1 55  SER 55  60  60  SER SER C . n 
C 1 56  LEU 56  61  61  LEU LEU C . n 
C 1 57  GLY 57  62  62  GLY GLY C . n 
C 1 58  CYS 58  63  63  CYS CYS C . n 
C 1 59  HIS 59  64  64  HIS HIS C . n 
C 1 60  LEU 60  65  65  LEU LEU C . n 
C 1 61  LYS 61  66  66  LYS LYS C . n 
C 1 62  ASP 62  67  67  ASP ASP C . n 
C 1 63  PHE 63  68  68  PHE PHE C . n 
C 1 64  GLY 64  69  69  GLY GLY C . n 
C 1 65  ASP 65  70  70  ASP ASP C . n 
C 1 66  LEU 66  71  71  LEU LEU C . n 
C 1 67  SER 67  72  72  SER SER C . n 
C 1 68  PHE 68  73  73  PHE PHE C . n 
C 1 69  THR 69  74  74  THR THR C . n 
C 1 70  PRO 70  75  75  PRO PRO C . n 
C 1 71  VAL 71  76  76  VAL VAL C . n 
C 1 72  PRO 72  77  77  PRO PRO C . n 
C 1 73  LYS 73  78  78  LYS LYS C . n 
C 1 74  ASP 74  79  79  ASP ASP C . n 
C 1 75  ASP 75  80  80  ASP ASP C . n 
C 1 76  LEU 76  81  81  LEU LEU C . n 
C 1 77  TYR 77  82  82  TYR TYR C . n 
C 1 78  ASN 78  83  83  ASN ASN C . n 
C 1 79  ASN 79  84  84  ASN ASN C . n 
C 1 80  LEU 80  85  85  LEU LEU C . n 
C 1 81  ILE 81  86  86  ILE ILE C . n 
C 1 82  VAL 82  87  87  VAL VAL C . n 
C 1 83  ASN 83  88  88  ASN ASN C . n 
C 1 84  PRO 84  89  89  PRO PRO C . n 
C 1 85  ARG 85  90  90  ARG ARG C . n 
C 1 86  SER 86  91  91  SER SER C . n 
C 1 87  VAL 87  92  92  VAL VAL C . n 
C 1 88  GLY 88  93  93  GLY GLY C . n 
C 1 89  LEU 89  94  94  LEU LEU C . n 
C 1 90  ALA 90  95  95  ALA ALA C . n 
C 1 91  ASN 91  96  96  ASN ASN C . n 
C 1 92  GLN 92  97  97  GLN GLN C . n 
C 1 93  GLU 93  98  98  GLU GLU C . n 
C 1 94  LEU 94  99  99  LEU LEU C . n 
C 1 95  ALA 95  100 100 ALA ALA C . n 
C 1 96  GLU 96  101 101 GLU GLU C . n 
C 1 97  VAL 97  102 102 VAL VAL C . n 
C 1 98  VAL 98  103 103 VAL VAL C . n 
C 1 99  SER 99  104 104 SER SER C . n 
C 1 100 ARG 100 105 105 ARG ARG C . n 
C 1 101 ALA 101 106 106 ALA ALA C . n 
C 1 102 VAL 102 107 107 VAL VAL C . n 
C 1 103 SER 103 108 108 SER SER C . n 
C 1 104 ASP 104 109 109 ASP ASP C . n 
C 1 105 GLY 105 110 110 GLY GLY C . n 
C 1 106 TYR 106 111 111 TYR TYR C . n 
C 1 107 SER 107 112 112 SER SER C . n 
C 1 108 CYS 108 113 113 CYS CYS C . n 
C 1 109 VAL 109 114 114 VAL VAL C . n 
C 1 110 THR 110 115 115 THR THR C . n 
C 1 111 LEU 111 116 116 LEU LEU C . n 
C 1 112 GLY 112 117 117 GLY GLY C . n 
C 1 113 GLY 113 118 118 GLY GLY C . n 
C 1 114 ASP 114 119 119 ASP ASP C . n 
C 1 115 HIS 115 120 120 HIS HIS C . n 
C 1 116 SER 116 121 121 SER SER C . n 
C 1 117 LEU 117 122 122 LEU LEU C . n 
C 1 118 ALA 118 123 123 ALA ALA C . n 
C 1 119 ILE 119 124 124 ILE ILE C . n 
C 1 120 GLY 120 125 125 GLY GLY C . n 
C 1 121 THR 121 126 126 THR THR C . n 
C 1 122 ILE 122 127 127 ILE ILE C . n 
C 1 123 SER 123 128 128 SER SER C . n 
C 1 124 GLY 124 129 129 GLY GLY C . n 
C 1 125 HIS 125 130 130 HIS HIS C . n 
C 1 126 ALA 126 131 131 ALA ALA C . n 
C 1 127 ARG 127 132 132 ARG ARG C . n 
C 1 128 HIS 128 133 133 HIS HIS C . n 
C 1 129 CYS 129 134 134 CYS CYS C . n 
C 1 130 PRO 130 135 135 PRO PRO C . n 
C 1 131 ASP 131 136 136 ASP ASP C . n 
C 1 132 LEU 132 137 137 LEU LEU C . n 
C 1 133 CYS 133 138 138 CYS CYS C . n 
C 1 134 VAL 134 139 139 VAL VAL C . n 
C 1 135 VAL 135 140 140 VAL VAL C . n 
C 1 136 TRP 136 141 141 TRP TRP C . n 
C 1 137 VAL 137 142 142 VAL VAL C . n 
C 1 138 ASP 138 143 143 ASP ASP C . n 
C 1 139 ALA 139 144 144 ALA ALA C . n 
C 1 140 HIS 140 145 145 HIS HIS C . n 
C 1 141 ALA 141 146 146 ALA ALA C . n 
C 1 142 ASP 142 147 147 ASP ASP C . n 
C 1 143 ILE 143 148 148 ILE ILE C . n 
C 1 144 ASN 144 149 149 ASN ASN C . n 
C 1 145 THR 145 150 150 THR THR C . n 
C 1 146 PRO 146 151 151 PRO PRO C . n 
C 1 147 LEU 147 152 152 LEU LEU C . n 
C 1 148 THR 148 153 153 THR THR C . n 
C 1 149 THR 149 154 154 THR THR C . n 
C 1 150 SER 150 155 155 SER SER C . n 
C 1 151 SER 151 156 156 SER SER C . n 
C 1 152 GLY 152 157 157 GLY GLY C . n 
C 1 153 ASN 153 158 158 ASN ASN C . n 
C 1 154 LEU 154 159 159 LEU LEU C . n 
C 1 155 HIS 155 160 160 HIS HIS C . n 
C 1 156 GLY 156 161 161 GLY GLY C . n 
C 1 157 GLN 157 162 162 GLN GLN C . n 
C 1 158 PRO 158 163 163 PRO PRO C . n 
C 1 159 VAL 159 164 164 VAL VAL C . n 
C 1 160 SER 160 165 165 SER SER C . n 
C 1 161 PHE 161 166 166 PHE PHE C . n 
C 1 162 LEU 162 167 167 LEU LEU C . n 
C 1 163 LEU 163 168 168 LEU LEU C . n 
C 1 164 ARG 164 169 169 ARG ARG C . n 
C 1 165 GLU 165 170 170 GLU GLU C . n 
C 1 166 LEU 166 171 171 LEU LEU C . n 
C 1 167 GLN 167 172 172 GLN GLN C . n 
C 1 168 ASP 168 173 173 ASP ASP C . n 
C 1 169 LYS 169 174 174 LYS LYS C . n 
C 1 170 VAL 170 175 175 VAL VAL C . n 
C 1 171 PRO 171 176 176 PRO PRO C . n 
C 1 172 GLN 172 177 177 GLN GLN C . n 
C 1 173 LEU 173 178 178 LEU LEU C . n 
C 1 174 PRO 174 179 179 PRO PRO C . n 
C 1 175 GLY 175 180 180 GLY GLY C . n 
C 1 176 PHE 176 181 181 PHE PHE C . n 
C 1 177 SER 177 182 182 SER SER C . n 
C 1 178 TRP 178 183 183 TRP TRP C . n 
C 1 179 ILE 179 184 184 ILE ILE C . n 
C 1 180 LYS 180 185 185 LYS LYS C . n 
C 1 181 PRO 181 186 186 PRO PRO C . n 
C 1 182 CYS 182 187 187 CYS CYS C . n 
C 1 183 ILE 183 188 188 ILE ILE C . n 
C 1 184 SER 184 189 189 SER SER C . n 
C 1 185 SER 185 190 190 SER SER C . n 
C 1 186 ALA 186 191 191 ALA ALA C . n 
C 1 187 SER 187 192 192 SER SER C . n 
C 1 188 ILE 188 193 193 ILE ILE C . n 
C 1 189 VAL 189 194 194 VAL VAL C . n 
C 1 190 TYR 190 195 195 TYR TYR C . n 
C 1 191 ILE 191 196 196 ILE ILE C . n 
C 1 192 GLY 192 197 197 GLY GLY C . n 
C 1 193 LEU 193 198 198 LEU LEU C . n 
C 1 194 ARG 194 199 199 ARG ARG C . n 
C 1 195 ASP 195 200 200 ASP ASP C . n 
C 1 196 VAL 196 201 201 VAL VAL C . n 
C 1 197 ASP 197 202 202 ASP ASP C . n 
C 1 198 PRO 198 203 203 PRO PRO C . n 
C 1 199 PRO 199 204 204 PRO PRO C . n 
C 1 200 GLU 200 205 205 GLU GLU C . n 
C 1 201 HIS 201 206 206 HIS HIS C . n 
C 1 202 PHE 202 207 207 PHE PHE C . n 
C 1 203 ILE 203 208 208 ILE ILE C . n 
C 1 204 LEU 204 209 209 LEU LEU C . n 
C 1 205 LYS 205 210 210 LYS LYS C . n 
C 1 206 ASN 206 211 211 ASN ASN C . n 
C 1 207 TYR 207 212 212 TYR TYR C . n 
C 1 208 ASP 208 213 213 ASP ASP C . n 
C 1 209 ILE 209 214 214 ILE ILE C . n 
C 1 210 GLN 210 215 215 GLN GLN C . n 
C 1 211 TYR 211 216 216 TYR TYR C . n 
C 1 212 PHE 212 217 217 PHE PHE C . n 
C 1 213 SER 213 218 218 SER SER C . n 
C 1 214 MET 214 219 219 MET MET C . n 
C 1 215 ARG 215 220 220 ARG ARG C . n 
C 1 216 ASP 216 221 221 ASP ASP C . n 
C 1 217 ILE 217 222 222 ILE ILE C . n 
C 1 218 ASP 218 223 223 ASP ASP C . n 
C 1 219 ARG 219 224 224 ARG ARG C . n 
C 1 220 LEU 220 225 225 LEU LEU C . n 
C 1 221 GLY 221 226 226 GLY GLY C . n 
C 1 222 ILE 222 227 227 ILE ILE C . n 
C 1 223 GLN 223 228 228 GLN GLN C . n 
C 1 224 LYS 224 229 229 LYS LYS C . n 
C 1 225 VAL 225 230 230 VAL VAL C . n 
C 1 226 MET 226 231 231 MET MET C . n 
C 1 227 GLU 227 232 232 GLU GLU C . n 
C 1 228 ARG 228 233 233 ARG ARG C . n 
C 1 229 THR 229 234 234 THR THR C . n 
C 1 230 PHE 230 235 235 PHE PHE C . n 
C 1 231 ASP 231 236 236 ASP ASP C . n 
C 1 232 LEU 232 237 237 LEU LEU C . n 
C 1 233 LEU 233 238 238 LEU LEU C . n 
C 1 234 ILE 234 239 239 ILE ILE C . n 
C 1 235 GLY 235 240 240 GLY GLY C . n 
C 1 236 LYS 236 241 241 LYS LYS C . n 
C 1 237 ARG 237 242 242 ARG ARG C . n 
C 1 238 GLN 238 243 243 GLN GLN C . n 
C 1 239 ARG 239 244 244 ARG ARG C . n 
C 1 240 PRO 240 245 245 PRO PRO C . n 
C 1 241 ILE 241 246 246 ILE ILE C . n 
C 1 242 HIS 242 247 247 HIS HIS C . n 
C 1 243 LEU 243 248 248 LEU LEU C . n 
C 1 244 SER 244 249 249 SER SER C . n 
C 1 245 PHE 245 250 250 PHE PHE C . n 
C 1 246 ASP 246 251 251 ASP ASP C . n 
C 1 247 ILE 247 252 252 ILE ILE C . n 
C 1 248 ASP 248 253 253 ASP ASP C . n 
C 1 249 ALA 249 254 254 ALA ALA C . n 
C 1 250 PHE 250 255 255 PHE PHE C . n 
C 1 251 ASP 251 256 256 ASP ASP C . n 
C 1 252 PRO 252 257 257 PRO PRO C . n 
C 1 253 THR 253 258 258 THR THR C . n 
C 1 254 LEU 254 259 259 LEU LEU C . n 
C 1 255 ALA 255 260 260 ALA ALA C . n 
C 1 256 PRO 256 261 261 PRO PRO C . n 
C 1 257 ALA 257 262 262 ALA ALA C . n 
C 1 258 THR 258 263 263 THR THR C . n 
C 1 259 GLY 259 264 264 GLY GLY C . n 
C 1 260 THR 260 265 265 THR THR C . n 
C 1 261 PRO 261 266 266 PRO PRO C . n 
C 1 262 VAL 262 267 267 VAL VAL C . n 
C 1 263 VAL 263 268 268 VAL VAL C . n 
C 1 264 GLY 264 269 269 GLY GLY C . n 
C 1 265 GLY 265 270 270 GLY GLY C . n 
C 1 266 LEU 266 271 271 LEU LEU C . n 
C 1 267 THR 267 272 272 THR THR C . n 
C 1 268 TYR 268 273 273 TYR TYR C . n 
C 1 269 ARG 269 274 274 ARG ARG C . n 
C 1 270 GLU 270 275 275 GLU GLU C . n 
C 1 271 GLY 271 276 276 GLY GLY C . n 
C 1 272 MET 272 277 277 MET MET C . n 
C 1 273 TYR 273 278 278 TYR TYR C . n 
C 1 274 ILE 274 279 279 ILE ILE C . n 
C 1 275 ALA 275 280 280 ALA ALA C . n 
C 1 276 GLU 276 281 281 GLU GLU C . n 
C 1 277 GLU 277 282 282 GLU GLU C . n 
C 1 278 ILE 278 283 283 ILE ILE C . n 
C 1 279 HIS 279 284 284 HIS HIS C . n 
C 1 280 ASN 280 285 285 ASN ASN C . n 
C 1 281 THR 281 286 286 THR THR C . n 
C 1 282 GLY 282 287 287 GLY GLY C . n 
C 1 283 LEU 283 288 288 LEU LEU C . n 
C 1 284 LEU 284 289 289 LEU LEU C . n 
C 1 285 SER 285 290 290 SER SER C . n 
C 1 286 ALA 286 291 291 ALA ALA C . n 
C 1 287 LEU 287 292 292 LEU LEU C . n 
C 1 288 ASP 288 293 293 ASP ASP C . n 
C 1 289 LEU 289 294 294 LEU LEU C . n 
C 1 290 VAL 290 295 295 VAL VAL C . n 
C 1 291 GLU 291 296 296 GLU GLU C . n 
C 1 292 VAL 292 297 297 VAL VAL C . n 
C 1 293 ASN 293 298 298 ASN ASN C . n 
C 1 294 PRO 294 299 299 PRO PRO C . n 
C 1 295 GLN 295 300 300 GLN GLN C . n 
C 1 296 LEU 296 301 301 LEU LEU C . n 
C 1 297 ALA 297 302 302 ALA ALA C . n 
C 1 298 THR 298 303 303 THR THR C . n 
C 1 299 SER 299 304 304 SER SER C . n 
C 1 300 GLU 300 305 305 GLU GLU C . n 
C 1 301 GLU 301 306 306 GLU GLU C . n 
C 1 302 GLU 302 307 307 GLU GLU C . n 
C 1 303 ALA 303 308 308 ALA ALA C . n 
C 1 304 LYS 304 309 309 LYS LYS C . n 
C 1 305 THR 305 310 310 THR THR C . n 
C 1 306 THR 306 311 311 THR THR C . n 
C 1 307 ALA 307 312 312 ALA ALA C . n 
C 1 308 ASN 308 313 313 ASN ASN C . n 
C 1 309 LEU 309 314 314 LEU LEU C . n 
C 1 310 ALA 310 315 315 ALA ALA C . n 
C 1 311 VAL 311 316 316 VAL VAL C . n 
C 1 312 ASP 312 317 317 ASP ASP C . n 
C 1 313 VAL 313 318 318 VAL VAL C . n 
C 1 314 ILE 314 319 319 ILE ILE C . n 
C 1 315 ALA 315 320 320 ALA ALA C . n 
C 1 316 SER 316 321 321 SER SER C . n 
C 1 317 SER 317 322 322 SER SER C . n 
C 1 318 PHE 318 323 323 PHE PHE C . n 
C 1 319 GLY 319 324 324 GLY GLY C . n 
C 1 320 GLN 320 325 325 GLN GLN C . n 
C 1 321 THR 321 326 326 THR THR C . n 
C 1 322 ARG 322 327 327 ARG ARG C . n 
C 1 323 GLU 323 328 328 GLU GLU C . n 
C 1 324 GLY 324 329 329 GLY GLY C . n 
C 1 325 GLY 325 330 330 GLY GLY C . n 
C 1 326 HIS 326 331 331 HIS HIS C . n 
C 1 327 ILE 327 332 332 ILE ILE C . n 
C 1 328 VAL 328 333 333 VAL VAL C . n 
C 1 329 TYR 329 334 334 TYR TYR C . n 
C 1 330 ASP 330 335 335 ASP ASP C . n 
C 1 331 GLN 331 336 336 GLN GLN C . n 
C 1 332 LEU 332 337 337 LEU LEU C . n 
C 1 333 PRO 333 338 338 PRO PRO C . n 
C 1 334 THR 334 339 339 THR THR C . n 
C 1 335 PRO 335 340 340 PRO PRO C . n 
C 1 336 SER 336 341 ?   ?   ?   C . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1H0B 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1H0B 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
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 
D 2 MN    1   401 500 MN    MN  A . 
E 2 MN    1   402 501 MN    MN  A . 
F 3 A1H0B 1   403 2   A1H0B INH A . 
G 2 MN    1   401 500 MN    MN  B . 
H 2 MN    1   402 501 MN    MN  B . 
I 3 A1H0B 1   403 1   A1H0B INH B . 
J 2 MN    1   401 500 MN    MN  C . 
K 2 MN    1   402 501 MN    MN  C . 
L 3 A1H0B 1   403 3   A1H0B INH C . 
M 4 HOH   1   501 121 HOH   HOH A . 
M 4 HOH   2   502 22  HOH   HOH A . 
M 4 HOH   3   503 229 HOH   HOH A . 
M 4 HOH   4   504 247 HOH   HOH A . 
M 4 HOH   5   505 101 HOH   HOH A . 
M 4 HOH   6   506 362 HOH   HOH A . 
M 4 HOH   7   507 91  HOH   HOH A . 
M 4 HOH   8   508 274 HOH   HOH A . 
M 4 HOH   9   509 139 HOH   HOH A . 
M 4 HOH   10  510 331 HOH   HOH A . 
M 4 HOH   11  511 92  HOH   HOH A . 
M 4 HOH   12  512 99  HOH   HOH A . 
M 4 HOH   13  513 54  HOH   HOH A . 
M 4 HOH   14  514 83  HOH   HOH A . 
M 4 HOH   15  515 327 HOH   HOH A . 
M 4 HOH   16  516 292 HOH   HOH A . 
M 4 HOH   17  517 125 HOH   HOH A . 
M 4 HOH   18  518 197 HOH   HOH A . 
M 4 HOH   19  519 243 HOH   HOH A . 
M 4 HOH   20  520 105 HOH   HOH A . 
M 4 HOH   21  521 11  HOH   HOH A . 
M 4 HOH   22  522 128 HOH   HOH A . 
M 4 HOH   23  523 68  HOH   HOH A . 
M 4 HOH   24  524 10  HOH   HOH A . 
M 4 HOH   25  525 314 HOH   HOH A . 
M 4 HOH   26  526 48  HOH   HOH A . 
M 4 HOH   27  527 296 HOH   HOH A . 
M 4 HOH   28  528 156 HOH   HOH A . 
M 4 HOH   29  529 333 HOH   HOH A . 
M 4 HOH   30  530 170 HOH   HOH A . 
M 4 HOH   31  531 40  HOH   HOH A . 
M 4 HOH   32  532 194 HOH   HOH A . 
M 4 HOH   33  533 180 HOH   HOH A . 
M 4 HOH   34  534 288 HOH   HOH A . 
M 4 HOH   35  535 207 HOH   HOH A . 
M 4 HOH   36  536 135 HOH   HOH A . 
M 4 HOH   37  537 232 HOH   HOH A . 
M 4 HOH   38  538 16  HOH   HOH A . 
M 4 HOH   39  539 134 HOH   HOH A . 
M 4 HOH   40  540 25  HOH   HOH A . 
M 4 HOH   41  541 286 HOH   HOH A . 
M 4 HOH   42  542 23  HOH   HOH A . 
M 4 HOH   43  543 115 HOH   HOH A . 
M 4 HOH   44  544 82  HOH   HOH A . 
M 4 HOH   45  545 178 HOH   HOH A . 
M 4 HOH   46  546 130 HOH   HOH A . 
M 4 HOH   47  547 53  HOH   HOH A . 
M 4 HOH   48  548 8   HOH   HOH A . 
M 4 HOH   49  549 175 HOH   HOH A . 
M 4 HOH   50  550 298 HOH   HOH A . 
M 4 HOH   51  551 223 HOH   HOH A . 
M 4 HOH   52  552 26  HOH   HOH A . 
M 4 HOH   53  553 43  HOH   HOH A . 
M 4 HOH   54  554 195 HOH   HOH A . 
M 4 HOH   55  555 14  HOH   HOH A . 
M 4 HOH   56  556 205 HOH   HOH A . 
M 4 HOH   57  557 258 HOH   HOH A . 
M 4 HOH   58  558 61  HOH   HOH A . 
M 4 HOH   59  559 230 HOH   HOH A . 
M 4 HOH   60  560 244 HOH   HOH A . 
M 4 HOH   61  561 36  HOH   HOH A . 
M 4 HOH   62  562 220 HOH   HOH A . 
M 4 HOH   63  563 209 HOH   HOH A . 
M 4 HOH   64  564 212 HOH   HOH A . 
M 4 HOH   65  565 15  HOH   HOH A . 
M 4 HOH   66  566 129 HOH   HOH A . 
M 4 HOH   67  567 104 HOH   HOH A . 
M 4 HOH   68  568 272 HOH   HOH A . 
M 4 HOH   69  569 287 HOH   HOH A . 
M 4 HOH   70  570 271 HOH   HOH A . 
M 4 HOH   71  571 315 HOH   HOH A . 
M 4 HOH   72  572 57  HOH   HOH A . 
M 4 HOH   73  573 330 HOH   HOH A . 
M 4 HOH   74  574 93  HOH   HOH A . 
M 4 HOH   75  575 301 HOH   HOH A . 
M 4 HOH   76  576 133 HOH   HOH A . 
M 4 HOH   77  577 75  HOH   HOH A . 
M 4 HOH   78  578 106 HOH   HOH A . 
M 4 HOH   79  579 177 HOH   HOH A . 
M 4 HOH   80  580 312 HOH   HOH A . 
M 4 HOH   81  581 6   HOH   HOH A . 
M 4 HOH   82  582 255 HOH   HOH A . 
M 4 HOH   83  583 280 HOH   HOH A . 
M 4 HOH   84  584 39  HOH   HOH A . 
M 4 HOH   85  585 17  HOH   HOH A . 
M 4 HOH   86  586 210 HOH   HOH A . 
M 4 HOH   87  587 208 HOH   HOH A . 
M 4 HOH   88  588 77  HOH   HOH A . 
M 4 HOH   89  589 289 HOH   HOH A . 
M 4 HOH   90  590 160 HOH   HOH A . 
M 4 HOH   91  591 303 HOH   HOH A . 
M 4 HOH   92  592 188 HOH   HOH A . 
M 4 HOH   93  593 164 HOH   HOH A . 
M 4 HOH   94  594 353 HOH   HOH A . 
M 4 HOH   95  595 311 HOH   HOH A . 
M 4 HOH   96  596 199 HOH   HOH A . 
M 4 HOH   97  597 186 HOH   HOH A . 
M 4 HOH   98  598 241 HOH   HOH A . 
M 4 HOH   99  599 152 HOH   HOH A . 
M 4 HOH   100 600 276 HOH   HOH A . 
M 4 HOH   101 601 118 HOH   HOH A . 
M 4 HOH   102 602 100 HOH   HOH A . 
M 4 HOH   103 603 319 HOH   HOH A . 
M 4 HOH   104 604 329 HOH   HOH A . 
M 4 HOH   105 605 355 HOH   HOH A . 
M 4 HOH   106 606 20  HOH   HOH A . 
M 4 HOH   107 607 200 HOH   HOH A . 
M 4 HOH   108 608 323 HOH   HOH A . 
M 4 HOH   109 609 165 HOH   HOH A . 
M 4 HOH   110 610 159 HOH   HOH A . 
M 4 HOH   111 611 235 HOH   HOH A . 
M 4 HOH   112 612 341 HOH   HOH A . 
M 4 HOH   113 613 297 HOH   HOH A . 
M 4 HOH   114 614 231 HOH   HOH A . 
M 4 HOH   115 615 340 HOH   HOH A . 
M 4 HOH   116 616 260 HOH   HOH A . 
M 4 HOH   117 617 285 HOH   HOH A . 
M 4 HOH   118 618 337 HOH   HOH A . 
M 4 HOH   119 619 349 HOH   HOH A . 
M 4 HOH   120 620 346 HOH   HOH A . 
M 4 HOH   121 621 154 HOH   HOH A . 
M 4 HOH   122 622 114 HOH   HOH A . 
M 4 HOH   123 623 63  HOH   HOH A . 
M 4 HOH   124 624 291 HOH   HOH A . 
M 4 HOH   125 625 366 HOH   HOH A . 
M 4 HOH   126 626 173 HOH   HOH A . 
M 4 HOH   127 627 84  HOH   HOH A . 
N 4 HOH   1   501 237 HOH   HOH B . 
N 4 HOH   2   502 277 HOH   HOH B . 
N 4 HOH   3   503 179 HOH   HOH B . 
N 4 HOH   4   504 4   HOH   HOH B . 
N 4 HOH   5   505 268 HOH   HOH B . 
N 4 HOH   6   506 110 HOH   HOH B . 
N 4 HOH   7   507 119 HOH   HOH B . 
N 4 HOH   8   508 89  HOH   HOH B . 
N 4 HOH   9   509 202 HOH   HOH B . 
N 4 HOH   10  510 47  HOH   HOH B . 
N 4 HOH   11  511 217 HOH   HOH B . 
N 4 HOH   12  512 213 HOH   HOH B . 
N 4 HOH   13  513 221 HOH   HOH B . 
N 4 HOH   14  514 176 HOH   HOH B . 
N 4 HOH   15  515 56  HOH   HOH B . 
N 4 HOH   16  516 145 HOH   HOH B . 
N 4 HOH   17  517 273 HOH   HOH B . 
N 4 HOH   18  518 7   HOH   HOH B . 
N 4 HOH   19  519 345 HOH   HOH B . 
N 4 HOH   20  520 5   HOH   HOH B . 
N 4 HOH   21  521 332 HOH   HOH B . 
N 4 HOH   22  522 73  HOH   HOH B . 
N 4 HOH   23  523 70  HOH   HOH B . 
N 4 HOH   24  524 72  HOH   HOH B . 
N 4 HOH   25  525 351 HOH   HOH B . 
N 4 HOH   26  526 218 HOH   HOH B . 
N 4 HOH   27  527 167 HOH   HOH B . 
N 4 HOH   28  528 60  HOH   HOH B . 
N 4 HOH   29  529 290 HOH   HOH B . 
N 4 HOH   30  530 142 HOH   HOH B . 
N 4 HOH   31  531 112 HOH   HOH B . 
N 4 HOH   32  532 19  HOH   HOH B . 
N 4 HOH   33  533 182 HOH   HOH B . 
N 4 HOH   34  534 13  HOH   HOH B . 
N 4 HOH   35  535 45  HOH   HOH B . 
N 4 HOH   36  536 90  HOH   HOH B . 
N 4 HOH   37  537 28  HOH   HOH B . 
N 4 HOH   38  538 267 HOH   HOH B . 
N 4 HOH   39  539 103 HOH   HOH B . 
N 4 HOH   40  540 27  HOH   HOH B . 
N 4 HOH   41  541 281 HOH   HOH B . 
N 4 HOH   42  542 279 HOH   HOH B . 
N 4 HOH   43  543 32  HOH   HOH B . 
N 4 HOH   44  544 69  HOH   HOH B . 
N 4 HOH   45  545 98  HOH   HOH B . 
N 4 HOH   46  546 141 HOH   HOH B . 
N 4 HOH   47  547 191 HOH   HOH B . 
N 4 HOH   48  548 132 HOH   HOH B . 
N 4 HOH   49  549 102 HOH   HOH B . 
N 4 HOH   50  550 80  HOH   HOH B . 
N 4 HOH   51  551 136 HOH   HOH B . 
N 4 HOH   52  552 240 HOH   HOH B . 
N 4 HOH   53  553 264 HOH   HOH B . 
N 4 HOH   54  554 143 HOH   HOH B . 
N 4 HOH   55  555 352 HOH   HOH B . 
N 4 HOH   56  556 65  HOH   HOH B . 
N 4 HOH   57  557 2   HOH   HOH B . 
N 4 HOH   58  558 124 HOH   HOH B . 
N 4 HOH   59  559 34  HOH   HOH B . 
N 4 HOH   60  560 198 HOH   HOH B . 
N 4 HOH   61  561 120 HOH   HOH B . 
N 4 HOH   62  562 131 HOH   HOH B . 
N 4 HOH   63  563 59  HOH   HOH B . 
N 4 HOH   64  564 222 HOH   HOH B . 
N 4 HOH   65  565 357 HOH   HOH B . 
N 4 HOH   66  566 117 HOH   HOH B . 
N 4 HOH   67  567 88  HOH   HOH B . 
N 4 HOH   68  568 52  HOH   HOH B . 
N 4 HOH   69  569 140 HOH   HOH B . 
N 4 HOH   70  570 148 HOH   HOH B . 
N 4 HOH   71  571 108 HOH   HOH B . 
N 4 HOH   72  572 146 HOH   HOH B . 
N 4 HOH   73  573 9   HOH   HOH B . 
N 4 HOH   74  574 269 HOH   HOH B . 
N 4 HOH   75  575 338 HOH   HOH B . 
N 4 HOH   76  576 51  HOH   HOH B . 
N 4 HOH   77  577 257 HOH   HOH B . 
N 4 HOH   78  578 325 HOH   HOH B . 
N 4 HOH   79  579 55  HOH   HOH B . 
N 4 HOH   80  580 37  HOH   HOH B . 
N 4 HOH   81  581 184 HOH   HOH B . 
N 4 HOH   82  582 234 HOH   HOH B . 
N 4 HOH   83  583 74  HOH   HOH B . 
N 4 HOH   84  584 78  HOH   HOH B . 
N 4 HOH   85  585 318 HOH   HOH B . 
N 4 HOH   86  586 76  HOH   HOH B . 
N 4 HOH   87  587 66  HOH   HOH B . 
N 4 HOH   88  588 317 HOH   HOH B . 
N 4 HOH   89  589 171 HOH   HOH B . 
N 4 HOH   90  590 238 HOH   HOH B . 
N 4 HOH   91  591 166 HOH   HOH B . 
N 4 HOH   92  592 236 HOH   HOH B . 
N 4 HOH   93  593 261 HOH   HOH B . 
N 4 HOH   94  594 50  HOH   HOH B . 
N 4 HOH   95  595 295 HOH   HOH B . 
N 4 HOH   96  596 339 HOH   HOH B . 
N 4 HOH   97  597 137 HOH   HOH B . 
N 4 HOH   98  598 248 HOH   HOH B . 
N 4 HOH   99  599 219 HOH   HOH B . 
N 4 HOH   100 600 228 HOH   HOH B . 
N 4 HOH   101 601 138 HOH   HOH B . 
N 4 HOH   102 602 307 HOH   HOH B . 
N 4 HOH   103 603 111 HOH   HOH B . 
N 4 HOH   104 604 33  HOH   HOH B . 
N 4 HOH   105 605 183 HOH   HOH B . 
N 4 HOH   106 606 203 HOH   HOH B . 
N 4 HOH   107 607 67  HOH   HOH B . 
N 4 HOH   108 608 96  HOH   HOH B . 
N 4 HOH   109 609 354 HOH   HOH B . 
N 4 HOH   110 610 107 HOH   HOH B . 
N 4 HOH   111 611 226 HOH   HOH B . 
N 4 HOH   112 612 149 HOH   HOH B . 
N 4 HOH   113 613 250 HOH   HOH B . 
N 4 HOH   114 614 253 HOH   HOH B . 
N 4 HOH   115 615 300 HOH   HOH B . 
N 4 HOH   116 616 161 HOH   HOH B . 
N 4 HOH   117 617 214 HOH   HOH B . 
N 4 HOH   118 618 153 HOH   HOH B . 
N 4 HOH   119 619 71  HOH   HOH B . 
N 4 HOH   120 620 158 HOH   HOH B . 
N 4 HOH   121 621 344 HOH   HOH B . 
N 4 HOH   122 622 328 HOH   HOH B . 
N 4 HOH   123 623 169 HOH   HOH B . 
N 4 HOH   124 624 263 HOH   HOH B . 
N 4 HOH   125 625 266 HOH   HOH B . 
N 4 HOH   126 626 316 HOH   HOH B . 
N 4 HOH   127 627 85  HOH   HOH B . 
N 4 HOH   128 628 265 HOH   HOH B . 
N 4 HOH   129 629 87  HOH   HOH B . 
N 4 HOH   130 630 302 HOH   HOH B . 
N 4 HOH   131 631 360 HOH   HOH B . 
N 4 HOH   132 632 364 HOH   HOH B . 
N 4 HOH   133 633 359 HOH   HOH B . 
N 4 HOH   134 634 367 HOH   HOH B . 
N 4 HOH   135 635 368 HOH   HOH B . 
N 4 HOH   136 636 155 HOH   HOH B . 
N 4 HOH   137 637 116 HOH   HOH B . 
O 4 HOH   1   501 206 HOH   HOH C . 
O 4 HOH   2   502 42  HOH   HOH C . 
O 4 HOH   3   503 192 HOH   HOH C . 
O 4 HOH   4   504 94  HOH   HOH C . 
O 4 HOH   5   505 62  HOH   HOH C . 
O 4 HOH   6   506 224 HOH   HOH C . 
O 4 HOH   7   507 147 HOH   HOH C . 
O 4 HOH   8   508 49  HOH   HOH C . 
O 4 HOH   9   509 126 HOH   HOH C . 
O 4 HOH   10  510 336 HOH   HOH C . 
O 4 HOH   11  511 162 HOH   HOH C . 
O 4 HOH   12  512 211 HOH   HOH C . 
O 4 HOH   13  513 157 HOH   HOH C . 
O 4 HOH   14  514 181 HOH   HOH C . 
O 4 HOH   15  515 12  HOH   HOH C . 
O 4 HOH   16  516 79  HOH   HOH C . 
O 4 HOH   17  517 309 HOH   HOH C . 
O 4 HOH   18  518 46  HOH   HOH C . 
O 4 HOH   19  519 95  HOH   HOH C . 
O 4 HOH   20  520 347 HOH   HOH C . 
O 4 HOH   21  521 196 HOH   HOH C . 
O 4 HOH   22  522 58  HOH   HOH C . 
O 4 HOH   23  523 204 HOH   HOH C . 
O 4 HOH   24  524 24  HOH   HOH C . 
O 4 HOH   25  525 113 HOH   HOH C . 
O 4 HOH   26  526 242 HOH   HOH C . 
O 4 HOH   27  527 201 HOH   HOH C . 
O 4 HOH   28  528 41  HOH   HOH C . 
O 4 HOH   29  529 249 HOH   HOH C . 
O 4 HOH   30  530 18  HOH   HOH C . 
O 4 HOH   31  531 174 HOH   HOH C . 
O 4 HOH   32  532 38  HOH   HOH C . 
O 4 HOH   33  533 270 HOH   HOH C . 
O 4 HOH   34  534 299 HOH   HOH C . 
O 4 HOH   35  535 44  HOH   HOH C . 
O 4 HOH   36  536 29  HOH   HOH C . 
O 4 HOH   37  537 348 HOH   HOH C . 
O 4 HOH   38  538 150 HOH   HOH C . 
O 4 HOH   39  539 227 HOH   HOH C . 
O 4 HOH   40  540 151 HOH   HOH C . 
O 4 HOH   41  541 358 HOH   HOH C . 
O 4 HOH   42  542 189 HOH   HOH C . 
O 4 HOH   43  543 81  HOH   HOH C . 
O 4 HOH   44  544 193 HOH   HOH C . 
O 4 HOH   45  545 30  HOH   HOH C . 
O 4 HOH   46  546 262 HOH   HOH C . 
O 4 HOH   47  547 254 HOH   HOH C . 
O 4 HOH   48  548 1   HOH   HOH C . 
O 4 HOH   49  549 225 HOH   HOH C . 
O 4 HOH   50  550 313 HOH   HOH C . 
O 4 HOH   51  551 3   HOH   HOH C . 
O 4 HOH   52  552 293 HOH   HOH C . 
O 4 HOH   53  553 185 HOH   HOH C . 
O 4 HOH   54  554 190 HOH   HOH C . 
O 4 HOH   55  555 31  HOH   HOH C . 
O 4 HOH   56  556 122 HOH   HOH C . 
O 4 HOH   57  557 239 HOH   HOH C . 
O 4 HOH   58  558 109 HOH   HOH C . 
O 4 HOH   59  559 86  HOH   HOH C . 
O 4 HOH   60  560 163 HOH   HOH C . 
O 4 HOH   61  561 308 HOH   HOH C . 
O 4 HOH   62  562 123 HOH   HOH C . 
O 4 HOH   63  563 256 HOH   HOH C . 
O 4 HOH   64  564 172 HOH   HOH C . 
O 4 HOH   65  565 251 HOH   HOH C . 
O 4 HOH   66  566 283 HOH   HOH C . 
O 4 HOH   67  567 245 HOH   HOH C . 
O 4 HOH   68  568 284 HOH   HOH C . 
O 4 HOH   69  569 64  HOH   HOH C . 
O 4 HOH   70  570 35  HOH   HOH C . 
O 4 HOH   71  571 275 HOH   HOH C . 
O 4 HOH   72  572 127 HOH   HOH C . 
O 4 HOH   73  573 343 HOH   HOH C . 
O 4 HOH   74  574 252 HOH   HOH C . 
O 4 HOH   75  575 144 HOH   HOH C . 
O 4 HOH   76  576 282 HOH   HOH C . 
O 4 HOH   77  577 97  HOH   HOH C . 
O 4 HOH   78  578 216 HOH   HOH C . 
O 4 HOH   79  579 334 HOH   HOH C . 
O 4 HOH   80  580 304 HOH   HOH C . 
O 4 HOH   81  581 306 HOH   HOH C . 
O 4 HOH   82  582 326 HOH   HOH C . 
O 4 HOH   83  583 350 HOH   HOH C . 
O 4 HOH   84  584 168 HOH   HOH C . 
O 4 HOH   85  585 233 HOH   HOH C . 
O 4 HOH   86  586 324 HOH   HOH C . 
O 4 HOH   87  587 321 HOH   HOH C . 
O 4 HOH   88  588 187 HOH   HOH C . 
O 4 HOH   89  589 363 HOH   HOH C . 
O 4 HOH   90  590 335 HOH   HOH C . 
O 4 HOH   91  591 21  HOH   HOH C . 
O 4 HOH   92  592 361 HOH   HOH C . 
O 4 HOH   93  593 246 HOH   HOH C . 
O 4 HOH   94  594 365 HOH   HOH C . 
O 4 HOH   95  595 278 HOH   HOH C . 
O 4 HOH   96  596 215 HOH   HOH C . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1 1 Y 1 B HIS 133 ? CA  ? B HIS 128 CA  
2 1 Y 1 B HIS 133 ? CB  ? B HIS 128 CB  
3 1 Y 1 B HIS 133 ? CG  ? B HIS 128 CG  
4 1 Y 1 B HIS 133 ? ND1 ? B HIS 128 ND1 
5 1 Y 1 B HIS 133 ? CD2 ? B HIS 128 CD2 
6 1 Y 1 B HIS 133 ? CE1 ? B HIS 128 CE1 
7 1 Y 1 B HIS 133 ? NE2 ? B HIS 128 NE2 
# 
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     ? ? ? ? ? ? ? ? ? ? ? BUSTER  ? ? ? '2.11.7 PACIOREK' 1 
? 'data scaling' ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .                 2 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8RG6 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     48.510 
_cell.length_a_esd                 ? 
_cell.length_b                     134.290 
_cell.length_b_esd                 ? 
_cell.length_c                     145.020 
_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                         8RG6 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_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                   8RG6 
_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             2.15 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          42.73 
_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, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_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    
;13-18% PEG3350, 
0.2-0.35M Am. Cit. pH7.0
;
_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                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 2M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2017-08-25 
_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   0.976 
_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                        'ESRF BEAMLINE ID30B' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.976 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ID30B 
_diffrn_source.pdbx_synchrotron_site       ESRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8RG6 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.617 
_reflns.d_resolution_low                               60.931 
_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                                     121702 
_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                           99.9 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.0 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          20.9 
_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                                0.042 
_reflns.pdbx_Rpim_I_all                                0.017 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       728815 
_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                              0.038 
_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                                    1.617 
_reflns_shell.d_res_low                                     1.645 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           20523 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             5944 
_reflns_shell.percent_possible_obs                          99.8 
_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                               3.5 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     2.2 
_reflns_shell.pdbx_Rrim_I_all                               0.560 
_reflns_shell.pdbx_Rpim_I_all                               0.295 
_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                                  0.473 
_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]                            -12.51750 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            0.00000 
_refine.aniso_B[2][2]                            4.58980 
_refine.aniso_B[2][3]                            0.00000 
_refine.aniso_B[3][3]                            7.92770 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               39.29 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.928 
_refine.correlation_coeff_Fo_to_Fc_free          0.920 
_refine.details                                  ? 
_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                                 8RG6 
_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                            1.62 
_refine.ls_d_res_low                             49.27 
_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                     121127 
_refine.ls_number_reflns_R_free                  6076 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.9 
_refine.ls_percent_reflns_R_free                 5.020 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.229 
_refine.ls_R_factor_R_free                       0.249 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.228 
_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                    ? 
_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                          0.000 
_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       ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_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   0.102 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.101 
_refine.pdbx_overall_SU_R_Blow_DPI               0.108 
_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             0.108 
_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_analyze.entry_id                        8RG6 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_coordinate_error_obs    0.27 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_sigma_a_free_details    ? 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_sigma_a_obs_details     ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
_refine_analyze.RG_d_res_high                   ? 
_refine_analyze.RG_d_res_low                    ? 
_refine_analyze.RG_free                         ? 
_refine_analyze.RG_work                         ? 
_refine_analyze.RG_free_work_ratio              ? 
_refine_analyze.pdbx_Luzzati_d_res_high_obs     ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.62 
_refine_hist.d_res_low                        49.27 
_refine_hist.number_atoms_solvent             360 
_refine_hist.number_atoms_total               7745 
_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        7337 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         48 
_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' ? 0.010 ? 7547  ? t_bond_d                  2.00  HARMONIC     
'X-RAY DIFFRACTION' ? 1.05  ? 10280 ? t_angle_deg               2.00  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 2546  ? t_dihedral_angle_d        2.00  SINUSOIDAL   
'X-RAY DIFFRACTION' ? ?     ? ?     ? t_incorr_chiral_ct        ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?     ? t_pseud_angle             ?     ?            
'X-RAY DIFFRACTION' ? ?     ? 179   ? t_trig_c_planes           2.00  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 1106  ? t_gen_planes              5.00  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 7547  ? t_it                      20.00 HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 1     ? t_nbd                     5.00  SEMIHARMONIC 
'X-RAY DIFFRACTION' ? 3.48  ? ?     ? t_omega_torsion           ?     ?            
'X-RAY DIFFRACTION' ? 17.08 ? ?     ? t_other_torsion           ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?     ? t_improper_torsion        ?     ?            
'X-RAY DIFFRACTION' ? ?     ? 998   ? t_chiral_improper_torsion 5.00  SEMIHARMONIC 
'X-RAY DIFFRACTION' ? ?     ? ?     ? t_sum_occupancies         ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?     ? t_utility_distance        ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?     ? t_utility_angle           ?     ?            
'X-RAY DIFFRACTION' ? ?     ? ?     ? t_utility_torsion         ?     ?            
'X-RAY DIFFRACTION' ? ?     ? 9188  ? t_ideal_dist_contact      4.00  SEMIHARMONIC 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.62 
_refine_ls_shell.d_res_low                        1.66 
_refine_ls_shell.number_reflns_all                8833 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             413 
_refine_ls_shell.number_reflns_R_work             8420 
_refine_ls_shell.percent_reflns_obs               99.84 
_refine_ls_shell.percent_reflns_R_free            4.68 
_refine_ls_shell.R_factor_all                     0.2754 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.2752 
_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                  0.2800 
# 
_struct.entry_id                     8RG6 
_struct.title                        'Arginase 2 in complex with inhibitor' 
_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        8RG6 
_struct_keywords.text            'arginase, inhibitor, complex, 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 1 ? 
D N N 2 ? 
E N N 2 ? 
F N N 3 ? 
G N N 2 ? 
H N N 2 ? 
I N N 3 ? 
J N N 2 ? 
K N N 2 ? 
L N N 3 ? 
M N N 4 ? 
N N N 4 ? 
O N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    ARGI2_HUMAN 
_struct_ref.pdbx_db_accession          P78540 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SVHSVAVIGAPFSQGQKRKGVEHGPAAIREAGLMKRLSSLGCHLKDFGDLSFTPVPKDDLYNNLIVNPRSVGLANQELAE
VVSRAVSDGYSCVTLGGDHSLAIGTISGHARHCPDLCVVWVDAHADINTPLTTSSGNLHGQPVSFLLRELQDKVPQLPGF
SWIKPCISSASIVYIGLRDVDPPEHFILKNYDIQYFSMRDIDRLGIQKVMERTFDLLIGKRQRPIHLSFDIDAFDPTLAP
ATGTPVVGGLTYREGMYIAEEIHNTGLLSALDLVEVNPQLATSEEEAKTTANLAVDVIASSFGQTREGGHIVYDQLPTPS

;
_struct_ref.pdbx_align_begin           22 
# 
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 8RG6 A 17 ? 336 ? P78540 22 ? 341 ? 22 341 
2 1 8RG6 B 17 ? 336 ? P78540 22 ? 341 ? 22 341 
3 1 8RG6 C 17 ? 336 ? P78540 22 ? 341 ? 22 341 
# 
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 8RG6 MET A 1  ? UNP P78540 ? ? 'initiating methionine' 6  1  
1 8RG6 HIS A 2  ? UNP P78540 ? ? 'expression tag'        7  2  
1 8RG6 HIS A 3  ? UNP P78540 ? ? 'expression tag'        8  3  
1 8RG6 HIS A 4  ? UNP P78540 ? ? 'expression tag'        9  4  
1 8RG6 HIS A 5  ? UNP P78540 ? ? 'expression tag'        10 5  
1 8RG6 HIS A 6  ? UNP P78540 ? ? 'expression tag'        11 6  
1 8RG6 HIS A 7  ? UNP P78540 ? ? 'expression tag'        12 7  
1 8RG6 GLY A 8  ? UNP P78540 ? ? 'expression tag'        13 8  
1 8RG6 GLY A 9  ? UNP P78540 ? ? 'expression tag'        14 9  
1 8RG6 GLY A 10 ? UNP P78540 ? ? 'expression tag'        15 10 
1 8RG6 GLU A 11 ? UNP P78540 ? ? 'expression tag'        16 11 
1 8RG6 ASN A 12 ? UNP P78540 ? ? 'expression tag'        17 12 
1 8RG6 LEU A 13 ? UNP P78540 ? ? 'expression tag'        18 13 
1 8RG6 TYR A 14 ? UNP P78540 ? ? 'expression tag'        19 14 
1 8RG6 PHE A 15 ? UNP P78540 ? ? 'expression tag'        20 15 
1 8RG6 GLN A 16 ? UNP P78540 ? ? 'expression tag'        21 16 
2 8RG6 MET B 1  ? UNP P78540 ? ? 'initiating methionine' 6  17 
2 8RG6 HIS B 2  ? UNP P78540 ? ? 'expression tag'        7  18 
2 8RG6 HIS B 3  ? UNP P78540 ? ? 'expression tag'        8  19 
2 8RG6 HIS B 4  ? UNP P78540 ? ? 'expression tag'        9  20 
2 8RG6 HIS B 5  ? UNP P78540 ? ? 'expression tag'        10 21 
2 8RG6 HIS B 6  ? UNP P78540 ? ? 'expression tag'        11 22 
2 8RG6 HIS B 7  ? UNP P78540 ? ? 'expression tag'        12 23 
2 8RG6 GLY B 8  ? UNP P78540 ? ? 'expression tag'        13 24 
2 8RG6 GLY B 9  ? UNP P78540 ? ? 'expression tag'        14 25 
2 8RG6 GLY B 10 ? UNP P78540 ? ? 'expression tag'        15 26 
2 8RG6 GLU B 11 ? UNP P78540 ? ? 'expression tag'        16 27 
2 8RG6 ASN B 12 ? UNP P78540 ? ? 'expression tag'        17 28 
2 8RG6 LEU B 13 ? UNP P78540 ? ? 'expression tag'        18 29 
2 8RG6 TYR B 14 ? UNP P78540 ? ? 'expression tag'        19 30 
2 8RG6 PHE B 15 ? UNP P78540 ? ? 'expression tag'        20 31 
2 8RG6 GLN B 16 ? UNP P78540 ? ? 'expression tag'        21 32 
3 8RG6 MET C 1  ? UNP P78540 ? ? 'initiating methionine' 6  33 
3 8RG6 HIS C 2  ? UNP P78540 ? ? 'expression tag'        7  34 
3 8RG6 HIS C 3  ? UNP P78540 ? ? 'expression tag'        8  35 
3 8RG6 HIS C 4  ? UNP P78540 ? ? 'expression tag'        9  36 
3 8RG6 HIS C 5  ? UNP P78540 ? ? 'expression tag'        10 37 
3 8RG6 HIS C 6  ? UNP P78540 ? ? 'expression tag'        11 38 
3 8RG6 HIS C 7  ? UNP P78540 ? ? 'expression tag'        12 39 
3 8RG6 GLY C 8  ? UNP P78540 ? ? 'expression tag'        13 40 
3 8RG6 GLY C 9  ? UNP P78540 ? ? 'expression tag'        14 41 
3 8RG6 GLY C 10 ? UNP P78540 ? ? 'expression tag'        15 42 
3 8RG6 GLU C 11 ? UNP P78540 ? ? 'expression tag'        16 43 
3 8RG6 ASN C 12 ? UNP P78540 ? ? 'expression tag'        17 44 
3 8RG6 LEU C 13 ? UNP P78540 ? ? 'expression tag'        18 45 
3 8RG6 TYR C 14 ? UNP P78540 ? ? 'expression tag'        19 46 
3 8RG6 PHE C 15 ? UNP P78540 ? ? 'expression tag'        20 47 
3 8RG6 GLN C 16 ? UNP P78540 ? ? 'expression tag'        21 48 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   trimeric 
_pdbx_struct_assembly.oligomeric_count     3 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 6750  ? 
1 MORE         -38   ? 
1 'SSA (A^2)'  35530 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N,O 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_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 GLY A 36  ? GLU A 38  ? GLY A 41  GLU A 43  5 ? 3  
HELX_P HELX_P2  AA2 HIS A 39  ? ALA A 47  ? HIS A 44  ALA A 52  1 ? 9  
HELX_P HELX_P3  AA3 GLY A 48  ? LEU A 56  ? GLY A 53  LEU A 61  1 ? 9  
HELX_P HELX_P4  AA4 ASN A 83  ? ASP A 104 ? ASN A 88  ASP A 109 1 ? 22 
HELX_P HELX_P5  AA5 ASP A 114 ? SER A 116 ? ASP A 119 SER A 121 5 ? 3  
HELX_P HELX_P6  AA6 LEU A 117 ? ARG A 127 ? LEU A 122 ARG A 132 1 ? 11 
HELX_P HELX_P7  AA7 ASN A 153 ? GLY A 156 ? ASN A 158 GLY A 161 5 ? 4  
HELX_P HELX_P8  AA8 GLN A 157 ? LEU A 163 ? GLN A 162 LEU A 168 1 ? 7  
HELX_P HELX_P9  AA9 ARG A 164 ? VAL A 170 ? ARG A 169 VAL A 175 5 ? 7  
HELX_P HELX_P10 AB1 SER A 184 ? ALA A 186 ? SER A 189 ALA A 191 5 ? 3  
HELX_P HELX_P11 AB2 ASP A 197 ? TYR A 207 ? ASP A 202 TYR A 212 1 ? 11 
HELX_P HELX_P12 AB3 MET A 214 ? GLY A 221 ? MET A 219 GLY A 226 1 ? 8  
HELX_P HELX_P13 AB4 GLY A 221 ? GLY A 235 ? GLY A 226 GLY A 240 1 ? 15 
HELX_P HELX_P14 AB5 ASP A 248 ? PHE A 250 ? ASP A 253 PHE A 255 5 ? 3  
HELX_P HELX_P15 AB6 THR A 267 ? GLY A 282 ? THR A 272 GLY A 287 1 ? 16 
HELX_P HELX_P16 AB7 ASN A 293 ? ALA A 297 ? ASN A 298 ALA A 302 5 ? 5  
HELX_P HELX_P17 AB8 SER A 299 ? PHE A 318 ? SER A 304 PHE A 323 1 ? 20 
HELX_P HELX_P18 AB9 GLY B 36  ? GLU B 38  ? GLY B 41  GLU B 43  5 ? 3  
HELX_P HELX_P19 AC1 HIS B 39  ? ALA B 47  ? HIS B 44  ALA B 52  1 ? 9  
HELX_P HELX_P20 AC2 GLY B 48  ? LEU B 56  ? GLY B 53  LEU B 61  1 ? 9  
HELX_P HELX_P21 AC3 ASN B 83  ? ASP B 104 ? ASN B 88  ASP B 109 1 ? 22 
HELX_P HELX_P22 AC4 ASP B 114 ? SER B 116 ? ASP B 119 SER B 121 5 ? 3  
HELX_P HELX_P23 AC5 LEU B 117 ? ARG B 127 ? LEU B 122 ARG B 132 1 ? 11 
HELX_P HELX_P24 AC6 ASN B 153 ? GLY B 156 ? ASN B 158 GLY B 161 5 ? 4  
HELX_P HELX_P25 AC7 GLN B 157 ? LEU B 163 ? GLN B 162 LEU B 168 1 ? 7  
HELX_P HELX_P26 AC8 ARG B 164 ? VAL B 170 ? ARG B 169 VAL B 175 5 ? 7  
HELX_P HELX_P27 AC9 SER B 184 ? ALA B 186 ? SER B 189 ALA B 191 5 ? 3  
HELX_P HELX_P28 AD1 ASP B 197 ? TYR B 207 ? ASP B 202 TYR B 212 1 ? 11 
HELX_P HELX_P29 AD2 MET B 214 ? GLY B 221 ? MET B 219 GLY B 226 1 ? 8  
HELX_P HELX_P30 AD3 GLY B 221 ? GLY B 235 ? GLY B 226 GLY B 240 1 ? 15 
HELX_P HELX_P31 AD4 ASP B 248 ? PHE B 250 ? ASP B 253 PHE B 255 5 ? 3  
HELX_P HELX_P32 AD5 THR B 267 ? GLY B 282 ? THR B 272 GLY B 287 1 ? 16 
HELX_P HELX_P33 AD6 ASN B 293 ? ALA B 297 ? ASN B 298 ALA B 302 5 ? 5  
HELX_P HELX_P34 AD7 SER B 299 ? PHE B 318 ? SER B 304 PHE B 323 1 ? 20 
HELX_P HELX_P35 AD8 GLY C 36  ? GLU C 38  ? GLY C 41  GLU C 43  5 ? 3  
HELX_P HELX_P36 AD9 HIS C 39  ? ALA C 47  ? HIS C 44  ALA C 52  1 ? 9  
HELX_P HELX_P37 AE1 GLY C 48  ? LEU C 56  ? GLY C 53  LEU C 61  1 ? 9  
HELX_P HELX_P38 AE2 LEU C 76  ? LEU C 80  ? LEU C 81  LEU C 85  5 ? 5  
HELX_P HELX_P39 AE3 ASN C 83  ? ASP C 104 ? ASN C 88  ASP C 109 1 ? 22 
HELX_P HELX_P40 AE4 ASP C 114 ? SER C 116 ? ASP C 119 SER C 121 5 ? 3  
HELX_P HELX_P41 AE5 LEU C 117 ? CYS C 129 ? LEU C 122 CYS C 134 1 ? 13 
HELX_P HELX_P42 AE6 ASN C 153 ? GLY C 156 ? ASN C 158 GLY C 161 5 ? 4  
HELX_P HELX_P43 AE7 GLN C 157 ? LEU C 163 ? GLN C 162 LEU C 168 1 ? 7  
HELX_P HELX_P44 AE8 ARG C 164 ? VAL C 170 ? ARG C 169 VAL C 175 5 ? 7  
HELX_P HELX_P45 AE9 SER C 184 ? ALA C 186 ? SER C 189 ALA C 191 5 ? 3  
HELX_P HELX_P46 AF1 ASP C 197 ? TYR C 207 ? ASP C 202 TYR C 212 1 ? 11 
HELX_P HELX_P47 AF2 SER C 213 ? GLY C 221 ? SER C 218 GLY C 226 1 ? 9  
HELX_P HELX_P48 AF3 GLY C 221 ? GLY C 235 ? GLY C 226 GLY C 240 1 ? 15 
HELX_P HELX_P49 AF4 ASP C 248 ? PHE C 250 ? ASP C 253 PHE C 255 5 ? 3  
HELX_P HELX_P50 AF5 THR C 267 ? THR C 281 ? THR C 272 THR C 286 1 ? 15 
HELX_P HELX_P51 AF6 ASN C 293 ? ALA C 297 ? ASN C 298 ALA C 302 5 ? 5  
HELX_P HELX_P52 AF7 SER C 299 ? PHE C 318 ? SER C 304 PHE C 323 1 ? 20 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1  metalc ? ? A HIS 115 ND1 ? ? ? 1_555 D MN    . MN ? ? A HIS 120 A MN    401 1_555 ? ? ? ? ? ? ? 2.311 ? ? 
metalc2  metalc ? ? A ASP 138 OD2 ? ? ? 1_555 D MN    . MN ? ? A ASP 143 A MN    401 1_555 ? ? ? ? ? ? ? 2.143 ? ? 
metalc3  metalc ? ? A ASP 138 OD1 ? ? ? 1_555 E MN    . MN ? ? A ASP 143 A MN    402 1_555 ? ? ? ? ? ? ? 2.161 ? ? 
metalc4  metalc ? ? A HIS 140 ND1 ? ? ? 1_555 E MN    . MN ? ? A HIS 145 A MN    402 1_555 ? ? ? ? ? ? ? 2.227 ? ? 
metalc5  metalc ? ? A ASP 142 OD2 ? ? ? 1_555 D MN    . MN ? ? A ASP 147 A MN    401 1_555 ? ? ? ? ? ? ? 2.163 ? ? 
metalc6  metalc ? ? A ASP 246 OD2 ? ? ? 1_555 D MN    . MN ? ? A ASP 251 A MN    401 1_555 ? ? ? ? ? ? ? 2.342 ? ? 
metalc7  metalc ? ? A ASP 246 OD2 ? ? ? 1_555 E MN    . MN ? ? A ASP 251 A MN    402 1_555 ? ? ? ? ? ? ? 2.304 ? ? 
metalc8  metalc ? ? A ASP 248 OD1 ? ? ? 1_555 E MN    . MN ? ? A ASP 253 A MN    402 1_555 ? ? ? ? ? ? ? 2.531 ? ? 
metalc9  metalc ? ? A ASP 248 OD2 ? ? ? 1_555 E MN    . MN ? ? A ASP 253 A MN    402 1_555 ? ? ? ? ? ? ? 2.327 ? ? 
metalc10 metalc ? ? D MN  .   MN  ? ? ? 1_555 F A1H0B . O3 ? ? A MN  401 A A1H0B 403 1_555 ? ? ? ? ? ? ? 2.179 ? ? 
metalc11 metalc ? ? E MN  .   MN  ? ? ? 1_555 F A1H0B . O1 ? ? A MN  402 A A1H0B 403 1_555 ? ? ? ? ? ? ? 2.757 ? ? 
metalc12 metalc ? ? E MN  .   MN  ? ? ? 1_555 F A1H0B . O3 ? ? A MN  402 A A1H0B 403 1_555 ? ? ? ? ? ? ? 2.292 ? ? 
metalc13 metalc ? ? B HIS 115 ND1 ? ? ? 1_555 G MN    . MN ? ? B HIS 120 B MN    401 1_555 ? ? ? ? ? ? ? 2.191 ? ? 
metalc14 metalc ? ? B ASP 138 OD2 ? ? ? 1_555 G MN    . MN ? ? B ASP 143 B MN    401 1_555 ? ? ? ? ? ? ? 2.147 ? ? 
metalc15 metalc ? ? B ASP 138 OD1 ? ? ? 1_555 H MN    . MN ? ? B ASP 143 B MN    402 1_555 ? ? ? ? ? ? ? 2.168 ? ? 
metalc16 metalc ? ? B HIS 140 ND1 ? ? ? 1_555 H MN    . MN ? ? B HIS 145 B MN    402 1_555 ? ? ? ? ? ? ? 2.202 ? ? 
metalc17 metalc ? ? B ASP 142 OD2 ? ? ? 1_555 G MN    . MN ? ? B ASP 147 B MN    401 1_555 ? ? ? ? ? ? ? 2.133 ? ? 
metalc18 metalc ? ? B ASP 246 OD2 ? ? ? 1_555 G MN    . MN ? ? B ASP 251 B MN    401 1_555 ? ? ? ? ? ? ? 2.300 ? ? 
metalc19 metalc ? ? B ASP 246 OD2 ? ? ? 1_555 H MN    . MN ? ? B ASP 251 B MN    402 1_555 ? ? ? ? ? ? ? 2.298 ? ? 
metalc20 metalc ? ? B ASP 248 OD1 ? ? ? 1_555 H MN    . MN ? ? B ASP 253 B MN    402 1_555 ? ? ? ? ? ? ? 2.532 ? ? 
metalc21 metalc ? ? B ASP 248 OD2 ? ? ? 1_555 H MN    . MN ? ? B ASP 253 B MN    402 1_555 ? ? ? ? ? ? ? 2.153 ? ? 
metalc22 metalc ? ? G MN  .   MN  ? ? ? 1_555 I A1H0B . O3 ? ? B MN  401 B A1H0B 403 1_555 ? ? ? ? ? ? ? 2.300 ? ? 
metalc23 metalc ? ? H MN  .   MN  ? ? ? 1_555 I A1H0B . O1 ? ? B MN  402 B A1H0B 403 1_555 ? ? ? ? ? ? ? 2.660 ? ? 
metalc24 metalc ? ? H MN  .   MN  ? ? ? 1_555 I A1H0B . O3 ? ? B MN  402 B A1H0B 403 1_555 ? ? ? ? ? ? ? 2.229 ? ? 
metalc25 metalc ? ? C HIS 115 ND1 ? ? ? 1_555 J MN    . MN ? ? C HIS 120 C MN    401 1_555 ? ? ? ? ? ? ? 2.191 ? ? 
metalc26 metalc ? ? C ASP 138 OD2 ? ? ? 1_555 J MN    . MN ? ? C ASP 143 C MN    401 1_555 ? ? ? ? ? ? ? 2.187 ? ? 
metalc27 metalc ? ? C ASP 138 OD1 ? ? ? 1_555 K MN    . MN ? ? C ASP 143 C MN    402 1_555 ? ? ? ? ? ? ? 2.217 ? ? 
metalc28 metalc ? ? C HIS 140 ND1 ? ? ? 1_555 K MN    . MN ? ? C HIS 145 C MN    402 1_555 ? ? ? ? ? ? ? 2.326 ? ? 
metalc29 metalc ? ? C ASP 142 OD2 ? ? ? 1_555 J MN    . MN ? ? C ASP 147 C MN    401 1_555 ? ? ? ? ? ? ? 2.086 ? ? 
metalc30 metalc ? ? C ASP 246 OD2 ? ? ? 1_555 J MN    . MN ? ? C ASP 251 C MN    401 1_555 ? ? ? ? ? ? ? 2.271 ? ? 
metalc31 metalc ? ? C ASP 246 OD2 ? ? ? 1_555 K MN    . MN ? ? C ASP 251 C MN    402 1_555 ? ? ? ? ? ? ? 2.371 ? ? 
metalc32 metalc ? ? C ASP 248 OD1 ? ? ? 1_555 K MN    . MN ? ? C ASP 253 C MN    402 1_555 ? ? ? ? ? ? ? 2.548 ? ? 
metalc33 metalc ? ? C ASP 248 OD2 ? ? ? 1_555 K MN    . MN ? ? C ASP 253 C MN    402 1_555 ? ? ? ? ? ? ? 2.005 ? ? 
metalc34 metalc ? ? J MN  .   MN  ? ? ? 1_555 L A1H0B . O3 ? ? C MN  401 C A1H0B 403 1_555 ? ? ? ? ? ? ? 2.240 ? ? 
metalc35 metalc ? ? K MN  .   MN  ? ? ? 1_555 L A1H0B . O1 ? ? C MN  402 C A1H0B 403 1_555 ? ? ? ? ? ? ? 2.771 ? ? 
metalc36 metalc ? ? K MN  .   MN  ? ? ? 1_555 L A1H0B . O3 ? ? C MN  402 C A1H0B 403 1_555 ? ? ? ? ? ? ? 2.208 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  ND1 ? A HIS   115 ? A HIS   120 ? 1_555 MN ? D MN . ? A MN 401 ? 1_555 OD2 ? A ASP   138 ? A ASP   143 ? 1_555 84.9  ? 
2  ND1 ? A HIS   115 ? A HIS   120 ? 1_555 MN ? D MN . ? A MN 401 ? 1_555 OD2 ? A ASP   142 ? A ASP   147 ? 1_555 88.6  ? 
3  OD2 ? A ASP   138 ? A ASP   143 ? 1_555 MN ? D MN . ? A MN 401 ? 1_555 OD2 ? A ASP   142 ? A ASP   147 ? 1_555 92.2  ? 
4  ND1 ? A HIS   115 ? A HIS   120 ? 1_555 MN ? D MN . ? A MN 401 ? 1_555 OD2 ? A ASP   246 ? A ASP   251 ? 1_555 102.3 ? 
5  OD2 ? A ASP   138 ? A ASP   143 ? 1_555 MN ? D MN . ? A MN 401 ? 1_555 OD2 ? A ASP   246 ? A ASP   251 ? 1_555 84.6  ? 
6  OD2 ? A ASP   142 ? A ASP   147 ? 1_555 MN ? D MN . ? A MN 401 ? 1_555 OD2 ? A ASP   246 ? A ASP   251 ? 1_555 168.3 ? 
7  ND1 ? A HIS   115 ? A HIS   120 ? 1_555 MN ? D MN . ? A MN 401 ? 1_555 O3  ? F A1H0B .   ? A A1H0B 403 ? 1_555 172.0 ? 
8  OD2 ? A ASP   138 ? A ASP   143 ? 1_555 MN ? D MN . ? A MN 401 ? 1_555 O3  ? F A1H0B .   ? A A1H0B 403 ? 1_555 102.5 ? 
9  OD2 ? A ASP   142 ? A ASP   147 ? 1_555 MN ? D MN . ? A MN 401 ? 1_555 O3  ? F A1H0B .   ? A A1H0B 403 ? 1_555 88.1  ? 
10 OD2 ? A ASP   246 ? A ASP   251 ? 1_555 MN ? D MN . ? A MN 401 ? 1_555 O3  ? F A1H0B .   ? A A1H0B 403 ? 1_555 81.7  ? 
11 OD1 ? A ASP   138 ? A ASP   143 ? 1_555 MN ? E MN . ? A MN 402 ? 1_555 ND1 ? A HIS   140 ? A HIS   145 ? 1_555 97.7  ? 
12 OD1 ? A ASP   138 ? A ASP   143 ? 1_555 MN ? E MN . ? A MN 402 ? 1_555 OD2 ? A ASP   246 ? A ASP   251 ? 1_555 85.0  ? 
13 ND1 ? A HIS   140 ? A HIS   145 ? 1_555 MN ? E MN . ? A MN 402 ? 1_555 OD2 ? A ASP   246 ? A ASP   251 ? 1_555 171.3 ? 
14 OD1 ? A ASP   138 ? A ASP   143 ? 1_555 MN ? E MN . ? A MN 402 ? 1_555 OD1 ? A ASP   248 ? A ASP   253 ? 1_555 77.6  ? 
15 ND1 ? A HIS   140 ? A HIS   145 ? 1_555 MN ? E MN . ? A MN 402 ? 1_555 OD1 ? A ASP   248 ? A ASP   253 ? 1_555 103.1 ? 
16 OD2 ? A ASP   246 ? A ASP   251 ? 1_555 MN ? E MN . ? A MN 402 ? 1_555 OD1 ? A ASP   248 ? A ASP   253 ? 1_555 85.5  ? 
17 OD1 ? A ASP   138 ? A ASP   143 ? 1_555 MN ? E MN . ? A MN 402 ? 1_555 OD2 ? A ASP   248 ? A ASP   253 ? 1_555 131.0 ? 
18 ND1 ? A HIS   140 ? A HIS   145 ? 1_555 MN ? E MN . ? A MN 402 ? 1_555 OD2 ? A ASP   248 ? A ASP   253 ? 1_555 90.2  ? 
19 OD2 ? A ASP   246 ? A ASP   251 ? 1_555 MN ? E MN . ? A MN 402 ? 1_555 OD2 ? A ASP   248 ? A ASP   253 ? 1_555 94.2  ? 
20 OD1 ? A ASP   248 ? A ASP   253 ? 1_555 MN ? E MN . ? A MN 402 ? 1_555 OD2 ? A ASP   248 ? A ASP   253 ? 1_555 53.6  ? 
21 OD1 ? A ASP   138 ? A ASP   143 ? 1_555 MN ? E MN . ? A MN 402 ? 1_555 O1  ? F A1H0B .   ? A A1H0B 403 ? 1_555 151.0 ? 
22 ND1 ? A HIS   140 ? A HIS   145 ? 1_555 MN ? E MN . ? A MN 402 ? 1_555 O1  ? F A1H0B .   ? A A1H0B 403 ? 1_555 91.4  ? 
23 OD2 ? A ASP   246 ? A ASP   251 ? 1_555 MN ? E MN . ? A MN 402 ? 1_555 O1  ? F A1H0B .   ? A A1H0B 403 ? 1_555 82.5  ? 
24 OD1 ? A ASP   248 ? A ASP   253 ? 1_555 MN ? E MN . ? A MN 402 ? 1_555 O1  ? F A1H0B .   ? A A1H0B 403 ? 1_555 127.0 ? 
25 OD2 ? A ASP   248 ? A ASP   253 ? 1_555 MN ? E MN . ? A MN 402 ? 1_555 O1  ? F A1H0B .   ? A A1H0B 403 ? 1_555 76.1  ? 
26 OD1 ? A ASP   138 ? A ASP   143 ? 1_555 MN ? E MN . ? A MN 402 ? 1_555 O3  ? F A1H0B .   ? A A1H0B 403 ? 1_555 95.6  ? 
27 ND1 ? A HIS   140 ? A HIS   145 ? 1_555 MN ? E MN . ? A MN 402 ? 1_555 O3  ? F A1H0B .   ? A A1H0B 403 ? 1_555 91.3  ? 
28 OD2 ? A ASP   246 ? A ASP   251 ? 1_555 MN ? E MN . ? A MN 402 ? 1_555 O3  ? F A1H0B .   ? A A1H0B 403 ? 1_555 80.2  ? 
29 OD1 ? A ASP   248 ? A ASP   253 ? 1_555 MN ? E MN . ? A MN 402 ? 1_555 O3  ? F A1H0B .   ? A A1H0B 403 ? 1_555 164.7 ? 
30 OD2 ? A ASP   248 ? A ASP   253 ? 1_555 MN ? E MN . ? A MN 402 ? 1_555 O3  ? F A1H0B .   ? A A1H0B 403 ? 1_555 132.6 ? 
31 O1  ? F A1H0B .   ? A A1H0B 403 ? 1_555 MN ? E MN . ? A MN 402 ? 1_555 O3  ? F A1H0B .   ? A A1H0B 403 ? 1_555 56.5  ? 
32 ND1 ? B HIS   115 ? B HIS   120 ? 1_555 MN ? G MN . ? B MN 401 ? 1_555 OD2 ? B ASP   138 ? B ASP   143 ? 1_555 91.1  ? 
33 ND1 ? B HIS   115 ? B HIS   120 ? 1_555 MN ? G MN . ? B MN 401 ? 1_555 OD2 ? B ASP   142 ? B ASP   147 ? 1_555 87.9  ? 
34 OD2 ? B ASP   138 ? B ASP   143 ? 1_555 MN ? G MN . ? B MN 401 ? 1_555 OD2 ? B ASP   142 ? B ASP   147 ? 1_555 88.0  ? 
35 ND1 ? B HIS   115 ? B HIS   120 ? 1_555 MN ? G MN . ? B MN 401 ? 1_555 OD2 ? B ASP   246 ? B ASP   251 ? 1_555 104.2 ? 
36 OD2 ? B ASP   138 ? B ASP   143 ? 1_555 MN ? G MN . ? B MN 401 ? 1_555 OD2 ? B ASP   246 ? B ASP   251 ? 1_555 86.3  ? 
37 OD2 ? B ASP   142 ? B ASP   147 ? 1_555 MN ? G MN . ? B MN 401 ? 1_555 OD2 ? B ASP   246 ? B ASP   251 ? 1_555 166.7 ? 
38 ND1 ? B HIS   115 ? B HIS   120 ? 1_555 MN ? G MN . ? B MN 401 ? 1_555 O3  ? I A1H0B .   ? B A1H0B 403 ? 1_555 171.8 ? 
39 OD2 ? B ASP   138 ? B ASP   143 ? 1_555 MN ? G MN . ? B MN 401 ? 1_555 O3  ? I A1H0B .   ? B A1H0B 403 ? 1_555 95.7  ? 
40 OD2 ? B ASP   142 ? B ASP   147 ? 1_555 MN ? G MN . ? B MN 401 ? 1_555 O3  ? I A1H0B .   ? B A1H0B 403 ? 1_555 87.8  ? 
41 OD2 ? B ASP   246 ? B ASP   251 ? 1_555 MN ? G MN . ? B MN 401 ? 1_555 O3  ? I A1H0B .   ? B A1H0B 403 ? 1_555 80.8  ? 
42 OD1 ? B ASP   138 ? B ASP   143 ? 1_555 MN ? H MN . ? B MN 402 ? 1_555 ND1 ? B HIS   140 ? B HIS   145 ? 1_555 96.3  ? 
43 OD1 ? B ASP   138 ? B ASP   143 ? 1_555 MN ? H MN . ? B MN 402 ? 1_555 OD2 ? B ASP   246 ? B ASP   251 ? 1_555 85.8  ? 
44 ND1 ? B HIS   140 ? B HIS   145 ? 1_555 MN ? H MN . ? B MN 402 ? 1_555 OD2 ? B ASP   246 ? B ASP   251 ? 1_555 172.1 ? 
45 OD1 ? B ASP   138 ? B ASP   143 ? 1_555 MN ? H MN . ? B MN 402 ? 1_555 OD1 ? B ASP   248 ? B ASP   253 ? 1_555 77.8  ? 
46 ND1 ? B HIS   140 ? B HIS   145 ? 1_555 MN ? H MN . ? B MN 402 ? 1_555 OD1 ? B ASP   248 ? B ASP   253 ? 1_555 101.5 ? 
47 OD2 ? B ASP   246 ? B ASP   251 ? 1_555 MN ? H MN . ? B MN 402 ? 1_555 OD1 ? B ASP   248 ? B ASP   253 ? 1_555 86.4  ? 
48 OD1 ? B ASP   138 ? B ASP   143 ? 1_555 MN ? H MN . ? B MN 402 ? 1_555 OD2 ? B ASP   248 ? B ASP   253 ? 1_555 134.1 ? 
49 ND1 ? B HIS   140 ? B HIS   145 ? 1_555 MN ? H MN . ? B MN 402 ? 1_555 OD2 ? B ASP   248 ? B ASP   253 ? 1_555 90.7  ? 
50 OD2 ? B ASP   246 ? B ASP   251 ? 1_555 MN ? H MN . ? B MN 402 ? 1_555 OD2 ? B ASP   248 ? B ASP   253 ? 1_555 93.3  ? 
51 OD1 ? B ASP   248 ? B ASP   253 ? 1_555 MN ? H MN . ? B MN 402 ? 1_555 OD2 ? B ASP   248 ? B ASP   253 ? 1_555 56.3  ? 
52 OD1 ? B ASP   138 ? B ASP   143 ? 1_555 MN ? H MN . ? B MN 402 ? 1_555 O1  ? I A1H0B .   ? B A1H0B 403 ? 1_555 148.3 ? 
53 ND1 ? B HIS   140 ? B HIS   145 ? 1_555 MN ? H MN . ? B MN 402 ? 1_555 O1  ? I A1H0B .   ? B A1H0B 403 ? 1_555 94.3  ? 
54 OD2 ? B ASP   246 ? B ASP   251 ? 1_555 MN ? H MN . ? B MN 402 ? 1_555 O1  ? I A1H0B .   ? B A1H0B 403 ? 1_555 80.2  ? 
55 OD1 ? B ASP   248 ? B ASP   253 ? 1_555 MN ? H MN . ? B MN 402 ? 1_555 O1  ? I A1H0B .   ? B A1H0B 403 ? 1_555 128.8 ? 
56 OD2 ? B ASP   248 ? B ASP   253 ? 1_555 MN ? H MN . ? B MN 402 ? 1_555 O1  ? I A1H0B .   ? B A1H0B 403 ? 1_555 75.4  ? 
57 OD1 ? B ASP   138 ? B ASP   143 ? 1_555 MN ? H MN . ? B MN 402 ? 1_555 O3  ? I A1H0B .   ? B A1H0B 403 ? 1_555 92.2  ? 
58 ND1 ? B HIS   140 ? B HIS   145 ? 1_555 MN ? H MN . ? B MN 402 ? 1_555 O3  ? I A1H0B .   ? B A1H0B 403 ? 1_555 89.9  ? 
59 OD2 ? B ASP   246 ? B ASP   251 ? 1_555 MN ? H MN . ? B MN 402 ? 1_555 O3  ? I A1H0B .   ? B A1H0B 403 ? 1_555 82.4  ? 
60 OD1 ? B ASP   248 ? B ASP   253 ? 1_555 MN ? H MN . ? B MN 402 ? 1_555 O3  ? I A1H0B .   ? B A1H0B 403 ? 1_555 165.5 ? 
61 OD2 ? B ASP   248 ? B ASP   253 ? 1_555 MN ? H MN . ? B MN 402 ? 1_555 O3  ? I A1H0B .   ? B A1H0B 403 ? 1_555 133.3 ? 
62 O1  ? I A1H0B .   ? B A1H0B 403 ? 1_555 MN ? H MN . ? B MN 402 ? 1_555 O3  ? I A1H0B .   ? B A1H0B 403 ? 1_555 58.1  ? 
63 ND1 ? C HIS   115 ? C HIS   120 ? 1_555 MN ? J MN . ? C MN 401 ? 1_555 OD2 ? C ASP   138 ? C ASP   143 ? 1_555 91.6  ? 
64 ND1 ? C HIS   115 ? C HIS   120 ? 1_555 MN ? J MN . ? C MN 401 ? 1_555 OD2 ? C ASP   142 ? C ASP   147 ? 1_555 87.6  ? 
65 OD2 ? C ASP   138 ? C ASP   143 ? 1_555 MN ? J MN . ? C MN 401 ? 1_555 OD2 ? C ASP   142 ? C ASP   147 ? 1_555 82.2  ? 
66 ND1 ? C HIS   115 ? C HIS   120 ? 1_555 MN ? J MN . ? C MN 401 ? 1_555 OD2 ? C ASP   246 ? C ASP   251 ? 1_555 104.5 ? 
67 OD2 ? C ASP   138 ? C ASP   143 ? 1_555 MN ? J MN . ? C MN 401 ? 1_555 OD2 ? C ASP   246 ? C ASP   251 ? 1_555 89.2  ? 
68 OD2 ? C ASP   142 ? C ASP   147 ? 1_555 MN ? J MN . ? C MN 401 ? 1_555 OD2 ? C ASP   246 ? C ASP   251 ? 1_555 165.4 ? 
69 ND1 ? C HIS   115 ? C HIS   120 ? 1_555 MN ? J MN . ? C MN 401 ? 1_555 O3  ? L A1H0B .   ? C A1H0B 403 ? 1_555 172.5 ? 
70 OD2 ? C ASP   138 ? C ASP   143 ? 1_555 MN ? J MN . ? C MN 401 ? 1_555 O3  ? L A1H0B .   ? C A1H0B 403 ? 1_555 94.5  ? 
71 OD2 ? C ASP   142 ? C ASP   147 ? 1_555 MN ? J MN . ? C MN 401 ? 1_555 O3  ? L A1H0B .   ? C A1H0B 403 ? 1_555 89.0  ? 
72 OD2 ? C ASP   246 ? C ASP   251 ? 1_555 MN ? J MN . ? C MN 401 ? 1_555 O3  ? L A1H0B .   ? C A1H0B 403 ? 1_555 79.9  ? 
73 OD1 ? C ASP   138 ? C ASP   143 ? 1_555 MN ? K MN . ? C MN 402 ? 1_555 ND1 ? C HIS   140 ? C HIS   145 ? 1_555 94.3  ? 
74 OD1 ? C ASP   138 ? C ASP   143 ? 1_555 MN ? K MN . ? C MN 402 ? 1_555 OD2 ? C ASP   246 ? C ASP   251 ? 1_555 88.8  ? 
75 ND1 ? C HIS   140 ? C HIS   145 ? 1_555 MN ? K MN . ? C MN 402 ? 1_555 OD2 ? C ASP   246 ? C ASP   251 ? 1_555 170.8 ? 
76 OD1 ? C ASP   138 ? C ASP   143 ? 1_555 MN ? K MN . ? C MN 402 ? 1_555 OD1 ? C ASP   248 ? C ASP   253 ? 1_555 75.2  ? 
77 ND1 ? C HIS   140 ? C HIS   145 ? 1_555 MN ? K MN . ? C MN 402 ? 1_555 OD1 ? C ASP   248 ? C ASP   253 ? 1_555 101.1 ? 
78 OD2 ? C ASP   246 ? C ASP   251 ? 1_555 MN ? K MN . ? C MN 402 ? 1_555 OD1 ? C ASP   248 ? C ASP   253 ? 1_555 88.1  ? 
79 OD1 ? C ASP   138 ? C ASP   143 ? 1_555 MN ? K MN . ? C MN 402 ? 1_555 OD2 ? C ASP   248 ? C ASP   253 ? 1_555 131.3 ? 
80 ND1 ? C HIS   140 ? C HIS   145 ? 1_555 MN ? K MN . ? C MN 402 ? 1_555 OD2 ? C ASP   248 ? C ASP   253 ? 1_555 93.1  ? 
81 OD2 ? C ASP   246 ? C ASP   251 ? 1_555 MN ? K MN . ? C MN 402 ? 1_555 OD2 ? C ASP   248 ? C ASP   253 ? 1_555 91.3  ? 
82 OD1 ? C ASP   248 ? C ASP   253 ? 1_555 MN ? K MN . ? C MN 402 ? 1_555 OD2 ? C ASP   248 ? C ASP   253 ? 1_555 56.1  ? 
83 OD1 ? C ASP   138 ? C ASP   143 ? 1_555 MN ? K MN . ? C MN 402 ? 1_555 O1  ? L A1H0B .   ? C A1H0B 403 ? 1_555 149.6 ? 
84 ND1 ? C HIS   140 ? C HIS   145 ? 1_555 MN ? K MN . ? C MN 402 ? 1_555 O1  ? L A1H0B .   ? C A1H0B 403 ? 1_555 96.1  ? 
85 OD2 ? C ASP   246 ? C ASP   251 ? 1_555 MN ? K MN . ? C MN 402 ? 1_555 O1  ? L A1H0B .   ? C A1H0B 403 ? 1_555 77.1  ? 
86 OD1 ? C ASP   248 ? C ASP   253 ? 1_555 MN ? K MN . ? C MN 402 ? 1_555 O1  ? L A1H0B .   ? C A1H0B 403 ? 1_555 130.1 ? 
87 OD2 ? C ASP   248 ? C ASP   253 ? 1_555 MN ? K MN . ? C MN 402 ? 1_555 O1  ? L A1H0B .   ? C A1H0B 403 ? 1_555 76.6  ? 
88 OD1 ? C ASP   138 ? C ASP   143 ? 1_555 MN ? K MN . ? C MN 402 ? 1_555 O3  ? L A1H0B .   ? C A1H0B 403 ? 1_555 94.3  ? 
89 ND1 ? C HIS   140 ? C HIS   145 ? 1_555 MN ? K MN . ? C MN 402 ? 1_555 O3  ? L A1H0B .   ? C A1H0B 403 ? 1_555 92.7  ? 
90 OD2 ? C ASP   246 ? C ASP   251 ? 1_555 MN ? K MN . ? C MN 402 ? 1_555 O3  ? L A1H0B .   ? C A1H0B 403 ? 1_555 78.4  ? 
91 OD1 ? C ASP   248 ? C ASP   253 ? 1_555 MN ? K MN . ? C MN 402 ? 1_555 O3  ? L A1H0B .   ? C A1H0B 403 ? 1_555 163.1 ? 
92 OD2 ? C ASP   248 ? C ASP   253 ? 1_555 MN ? K MN . ? C MN 402 ? 1_555 O3  ? L A1H0B .   ? C A1H0B 403 ? 1_555 133.3 ? 
93 O1  ? L A1H0B .   ? C A1H0B 403 ? 1_555 MN ? K MN . ? C MN 402 ? 1_555 O3  ? L A1H0B .   ? C A1H0B 403 ? 1_555 56.7  ? 
# 
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 GLY 112 A . ? GLY 117 A GLY 113 A ? GLY 118 A 1 -0.32 
2 GLY 112 B . ? GLY 117 B GLY 113 B ? GLY 118 B 1 1.09  
3 GLY 112 C . ? GLY 117 C GLY 113 C ? GLY 118 C 1 1.90  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8 ? 
AA2 ? 8 ? 
AA3 ? 8 ? 
# 
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 ? parallel 
AA1 2 3 ? parallel 
AA1 3 4 ? parallel 
AA1 4 5 ? parallel 
AA1 5 6 ? parallel 
AA1 6 7 ? parallel 
AA1 7 8 ? parallel 
AA2 1 2 ? parallel 
AA2 2 3 ? parallel 
AA2 3 4 ? parallel 
AA2 4 5 ? parallel 
AA2 5 6 ? parallel 
AA2 6 7 ? parallel 
AA2 7 8 ? parallel 
AA3 1 2 ? parallel 
AA3 2 3 ? parallel 
AA3 3 4 ? parallel 
AA3 4 5 ? parallel 
AA3 5 6 ? parallel 
AA3 6 7 ? parallel 
AA3 7 8 ? 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 HIS A 59  ? ASP A 65  ? HIS A 64  ASP A 70  
AA1 2 SER A 20  ? GLY A 25  ? SER A 25  GLY A 30  
AA1 3 SER A 107 ? LEU A 111 ? SER A 112 LEU A 116 
AA1 4 LEU A 284 ? VAL A 290 ? LEU A 289 VAL A 295 
AA1 5 ILE A 241 ? ASP A 246 ? ILE A 246 ASP A 251 
AA1 6 CYS A 133 ? VAL A 137 ? CYS A 138 VAL A 142 
AA1 7 ILE A 188 ? LEU A 193 ? ILE A 193 LEU A 198 
AA1 8 GLN A 210 ? SER A 213 ? GLN A 215 SER A 218 
AA2 1 HIS B 59  ? ASP B 65  ? HIS B 64  ASP B 70  
AA2 2 SER B 20  ? GLY B 25  ? SER B 25  GLY B 30  
AA2 3 SER B 107 ? LEU B 111 ? SER B 112 LEU B 116 
AA2 4 LEU B 284 ? VAL B 290 ? LEU B 289 VAL B 295 
AA2 5 ILE B 241 ? ASP B 246 ? ILE B 246 ASP B 251 
AA2 6 CYS B 133 ? VAL B 137 ? CYS B 138 VAL B 142 
AA2 7 ILE B 188 ? LEU B 193 ? ILE B 193 LEU B 198 
AA2 8 TYR B 211 ? SER B 213 ? TYR B 216 SER B 218 
AA3 1 HIS C 59  ? ASP C 65  ? HIS C 64  ASP C 70  
AA3 2 SER C 20  ? GLY C 25  ? SER C 25  GLY C 30  
AA3 3 SER C 107 ? LEU C 111 ? SER C 112 LEU C 116 
AA3 4 LEU C 284 ? VAL C 290 ? LEU C 289 VAL C 295 
AA3 5 ILE C 241 ? ASP C 246 ? ILE C 246 ASP C 251 
AA3 6 CYS C 133 ? VAL C 137 ? CYS C 138 VAL C 142 
AA3 7 ILE C 188 ? ILE C 191 ? ILE C 193 ILE C 196 
AA3 8 TYR C 211 ? PHE C 212 ? TYR C 216 PHE C 217 
# 
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 O HIS A 59  ? O HIS A 64  N VAL A 21  ? N VAL A 26  
AA1 2 3 N ALA A 22  ? N ALA A 27  O VAL A 109 ? O VAL A 114 
AA1 3 4 N THR A 110 ? N THR A 115 O LEU A 289 ? O LEU A 294 
AA1 4 5 O SER A 285 ? O SER A 290 N ILE A 241 ? N ILE A 246 
AA1 5 6 O ASP A 246 ? O ASP A 251 N VAL A 137 ? N VAL A 142 
AA1 6 7 N TRP A 136 ? N TRP A 141 O VAL A 189 ? O VAL A 194 
AA1 7 8 N TYR A 190 ? N TYR A 195 O PHE A 212 ? O PHE A 217 
AA2 1 2 O HIS B 59  ? O HIS B 64  N VAL B 21  ? N VAL B 26  
AA2 2 3 N ALA B 22  ? N ALA B 27  O VAL B 109 ? O VAL B 114 
AA2 3 4 N THR B 110 ? N THR B 115 O LEU B 287 ? O LEU B 292 
AA2 4 5 O SER B 285 ? O SER B 290 N ILE B 241 ? N ILE B 246 
AA2 5 6 O ASP B 246 ? O ASP B 251 N VAL B 137 ? N VAL B 142 
AA2 6 7 N TRP B 136 ? N TRP B 141 O VAL B 189 ? O VAL B 194 
AA2 7 8 N TYR B 190 ? N TYR B 195 O PHE B 212 ? O PHE B 217 
AA3 1 2 O PHE C 63  ? O PHE C 68  N VAL C 23  ? N VAL C 28  
AA3 2 3 N SER C 20  ? N SER C 25  O SER C 107 ? O SER C 112 
AA3 3 4 N CYS C 108 ? N CYS C 113 O LEU C 287 ? O LEU C 292 
AA3 4 5 O SER C 285 ? O SER C 290 N ILE C 241 ? N ILE C 246 
AA3 5 6 O ASP C 246 ? O ASP C 251 N VAL C 137 ? N VAL C 142 
AA3 6 7 N TRP C 136 ? N TRP C 141 O VAL C 189 ? O VAL C 194 
AA3 7 8 N TYR C 190 ? N TYR C 195 O PHE C 212 ? O PHE C 217 
# 
_pdbx_entry_details.entry_id                   8RG6 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_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 ALA A 31  ? ? -118.59 78.35  
2  1 ASP A 79  ? ? -156.03 63.92  
3  1 LEU A 81  ? ? -37.50  125.37 
4  1 LEU A 85  ? ? -146.89 -61.88 
5  1 ARG A 199 ? ? -154.19 -6.95  
6  1 LYS B 78  ? ? -105.73 57.67  
7  1 LEU B 85  ? ? -141.24 -54.06 
8  1 ARG B 199 ? ? -156.14 -2.33  
9  1 SER C 34  ? ? -146.08 -21.26 
10 1 LEU C 85  ? ? -147.28 -59.39 
11 1 ARG C 199 ? ? -154.21 -5.05  
# 
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 6   ? A MET 1   
2  1 Y 1 A HIS 7   ? A HIS 2   
3  1 Y 1 A HIS 8   ? A HIS 3   
4  1 Y 1 A HIS 9   ? A HIS 4   
5  1 Y 1 A HIS 10  ? A HIS 5   
6  1 Y 1 A HIS 11  ? A HIS 6   
7  1 Y 1 A HIS 12  ? A HIS 7   
8  1 Y 1 A GLY 13  ? A GLY 8   
9  1 Y 1 A GLY 14  ? A GLY 9   
10 1 Y 1 A GLY 15  ? A GLY 10  
11 1 Y 1 A GLU 16  ? A GLU 11  
12 1 Y 1 A ASN 17  ? A ASN 12  
13 1 Y 1 A LEU 18  ? A LEU 13  
14 1 Y 1 A TYR 19  ? A TYR 14  
15 1 Y 1 A PHE 20  ? A PHE 15  
16 1 Y 1 A GLN 21  ? A GLN 16  
17 1 Y 1 A SER 22  ? A SER 17  
18 1 Y 1 A SER 341 ? A SER 336 
19 1 Y 1 B MET 6   ? B MET 1   
20 1 Y 1 B HIS 7   ? B HIS 2   
21 1 Y 1 B HIS 8   ? B HIS 3   
22 1 Y 1 B HIS 9   ? B HIS 4   
23 1 Y 1 B HIS 10  ? B HIS 5   
24 1 Y 1 B HIS 11  ? B HIS 6   
25 1 Y 1 B HIS 12  ? B HIS 7   
26 1 Y 1 B GLY 13  ? B GLY 8   
27 1 Y 1 B GLY 14  ? B GLY 9   
28 1 Y 1 B GLY 15  ? B GLY 10  
29 1 Y 1 B GLU 16  ? B GLU 11  
30 1 Y 1 B SER 341 ? B SER 336 
31 1 Y 1 C MET 6   ? C MET 1   
32 1 Y 1 C HIS 7   ? C HIS 2   
33 1 Y 1 C HIS 8   ? C HIS 3   
34 1 Y 1 C HIS 9   ? C HIS 4   
35 1 Y 1 C HIS 10  ? C HIS 5   
36 1 Y 1 C HIS 11  ? C HIS 6   
37 1 Y 1 C HIS 12  ? C HIS 7   
38 1 Y 1 C GLY 13  ? C GLY 8   
39 1 Y 1 C GLY 14  ? C GLY 9   
40 1 Y 1 C GLY 15  ? C GLY 10  
41 1 Y 1 C GLU 16  ? C GLU 11  
42 1 Y 1 C ASN 17  ? C ASN 12  
43 1 Y 1 C LEU 18  ? C LEU 13  
44 1 Y 1 C TYR 19  ? C TYR 14  
45 1 Y 1 C PHE 20  ? C PHE 15  
46 1 Y 1 C GLN 21  ? C GLN 16  
47 1 Y 1 C SER 22  ? C SER 17  
48 1 Y 1 C SER 341 ? C SER 336 
# 
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 
A1H0B C7   C  N R 1   
A1H0B C9   C  N N 2   
A1H0B C10  C  N N 3   
A1H0B C12  C  N S 4   
A1H0B C14  C  N N 5   
A1H0B O1   O  N N 6   
A1H0B B2   B  N N 7   
A1H0B O3   O  N N 8   
A1H0B C4   C  N N 9   
A1H0B C5   C  N N 10  
A1H0B C6   C  N N 11  
A1H0B N11  N  N N 12  
A1H0B O15  O  N N 13  
A1H0B O16  O  N N 14  
A1H0B H8   H  N N 15  
A1H0B H1   H  N N 16  
A1H0B H2   H  N N 17  
A1H0B H3   H  N N 18  
A1H0B H4   H  N N 19  
A1H0B H13  H  N N 20  
A1H0B H5   H  N N 21  
A1H0B H6   H  N N 22  
A1H0B H7   H  N N 23  
A1H0B H9   H  N N 24  
A1H0B H10  H  N N 25  
A1H0B H11  H  N N 26  
A1H0B H12  H  N N 27  
A1H0B H14  H  N N 28  
A1H0B H15  H  N N 29  
A1H0B H17  H  N N 30  
ALA   N    N  N N 31  
ALA   CA   C  N S 32  
ALA   C    C  N N 33  
ALA   O    O  N N 34  
ALA   CB   C  N N 35  
ALA   OXT  O  N N 36  
ALA   H    H  N N 37  
ALA   H2   H  N N 38  
ALA   HA   H  N N 39  
ALA   HB1  H  N N 40  
ALA   HB2  H  N N 41  
ALA   HB3  H  N N 42  
ALA   HXT  H  N N 43  
ARG   N    N  N N 44  
ARG   CA   C  N S 45  
ARG   C    C  N N 46  
ARG   O    O  N N 47  
ARG   CB   C  N N 48  
ARG   CG   C  N N 49  
ARG   CD   C  N N 50  
ARG   NE   N  N N 51  
ARG   CZ   C  N N 52  
ARG   NH1  N  N N 53  
ARG   NH2  N  N N 54  
ARG   OXT  O  N N 55  
ARG   H    H  N N 56  
ARG   H2   H  N N 57  
ARG   HA   H  N N 58  
ARG   HB2  H  N N 59  
ARG   HB3  H  N N 60  
ARG   HG2  H  N N 61  
ARG   HG3  H  N N 62  
ARG   HD2  H  N N 63  
ARG   HD3  H  N N 64  
ARG   HE   H  N N 65  
ARG   HH11 H  N N 66  
ARG   HH12 H  N N 67  
ARG   HH21 H  N N 68  
ARG   HH22 H  N N 69  
ARG   HXT  H  N N 70  
ASN   N    N  N N 71  
ASN   CA   C  N S 72  
ASN   C    C  N N 73  
ASN   O    O  N N 74  
ASN   CB   C  N N 75  
ASN   CG   C  N N 76  
ASN   OD1  O  N N 77  
ASN   ND2  N  N N 78  
ASN   OXT  O  N N 79  
ASN   H    H  N N 80  
ASN   H2   H  N N 81  
ASN   HA   H  N N 82  
ASN   HB2  H  N N 83  
ASN   HB3  H  N N 84  
ASN   HD21 H  N N 85  
ASN   HD22 H  N N 86  
ASN   HXT  H  N N 87  
ASP   N    N  N N 88  
ASP   CA   C  N S 89  
ASP   C    C  N N 90  
ASP   O    O  N N 91  
ASP   CB   C  N N 92  
ASP   CG   C  N N 93  
ASP   OD1  O  N N 94  
ASP   OD2  O  N N 95  
ASP   OXT  O  N N 96  
ASP   H    H  N N 97  
ASP   H2   H  N N 98  
ASP   HA   H  N N 99  
ASP   HB2  H  N N 100 
ASP   HB3  H  N N 101 
ASP   HD2  H  N N 102 
ASP   HXT  H  N N 103 
CYS   N    N  N N 104 
CYS   CA   C  N R 105 
CYS   C    C  N N 106 
CYS   O    O  N N 107 
CYS   CB   C  N N 108 
CYS   SG   S  N N 109 
CYS   OXT  O  N N 110 
CYS   H    H  N N 111 
CYS   H2   H  N N 112 
CYS   HA   H  N N 113 
CYS   HB2  H  N N 114 
CYS   HB3  H  N N 115 
CYS   HG   H  N N 116 
CYS   HXT  H  N N 117 
GLN   N    N  N N 118 
GLN   CA   C  N S 119 
GLN   C    C  N N 120 
GLN   O    O  N N 121 
GLN   CB   C  N N 122 
GLN   CG   C  N N 123 
GLN   CD   C  N N 124 
GLN   OE1  O  N N 125 
GLN   NE2  N  N N 126 
GLN   OXT  O  N N 127 
GLN   H    H  N N 128 
GLN   H2   H  N N 129 
GLN   HA   H  N N 130 
GLN   HB2  H  N N 131 
GLN   HB3  H  N N 132 
GLN   HG2  H  N N 133 
GLN   HG3  H  N N 134 
GLN   HE21 H  N N 135 
GLN   HE22 H  N N 136 
GLN   HXT  H  N N 137 
GLU   N    N  N N 138 
GLU   CA   C  N S 139 
GLU   C    C  N N 140 
GLU   O    O  N N 141 
GLU   CB   C  N N 142 
GLU   CG   C  N N 143 
GLU   CD   C  N N 144 
GLU   OE1  O  N N 145 
GLU   OE2  O  N N 146 
GLU   OXT  O  N N 147 
GLU   H    H  N N 148 
GLU   H2   H  N N 149 
GLU   HA   H  N N 150 
GLU   HB2  H  N N 151 
GLU   HB3  H  N N 152 
GLU   HG2  H  N N 153 
GLU   HG3  H  N N 154 
GLU   HE2  H  N N 155 
GLU   HXT  H  N N 156 
GLY   N    N  N N 157 
GLY   CA   C  N N 158 
GLY   C    C  N N 159 
GLY   O    O  N N 160 
GLY   OXT  O  N N 161 
GLY   H    H  N N 162 
GLY   H2   H  N N 163 
GLY   HA2  H  N N 164 
GLY   HA3  H  N N 165 
GLY   HXT  H  N N 166 
HIS   N    N  N N 167 
HIS   CA   C  N S 168 
HIS   C    C  N N 169 
HIS   O    O  N N 170 
HIS   CB   C  N N 171 
HIS   CG   C  Y N 172 
HIS   ND1  N  Y N 173 
HIS   CD2  C  Y N 174 
HIS   CE1  C  Y N 175 
HIS   NE2  N  Y N 176 
HIS   OXT  O  N N 177 
HIS   H    H  N N 178 
HIS   H2   H  N N 179 
HIS   HA   H  N N 180 
HIS   HB2  H  N N 181 
HIS   HB3  H  N N 182 
HIS   HD1  H  N N 183 
HIS   HD2  H  N N 184 
HIS   HE1  H  N N 185 
HIS   HE2  H  N N 186 
HIS   HXT  H  N N 187 
HOH   O    O  N N 188 
HOH   H1   H  N N 189 
HOH   H2   H  N N 190 
ILE   N    N  N N 191 
ILE   CA   C  N S 192 
ILE   C    C  N N 193 
ILE   O    O  N N 194 
ILE   CB   C  N S 195 
ILE   CG1  C  N N 196 
ILE   CG2  C  N N 197 
ILE   CD1  C  N N 198 
ILE   OXT  O  N N 199 
ILE   H    H  N N 200 
ILE   H2   H  N N 201 
ILE   HA   H  N N 202 
ILE   HB   H  N N 203 
ILE   HG12 H  N N 204 
ILE   HG13 H  N N 205 
ILE   HG21 H  N N 206 
ILE   HG22 H  N N 207 
ILE   HG23 H  N N 208 
ILE   HD11 H  N N 209 
ILE   HD12 H  N N 210 
ILE   HD13 H  N N 211 
ILE   HXT  H  N N 212 
LEU   N    N  N N 213 
LEU   CA   C  N S 214 
LEU   C    C  N N 215 
LEU   O    O  N N 216 
LEU   CB   C  N N 217 
LEU   CG   C  N N 218 
LEU   CD1  C  N N 219 
LEU   CD2  C  N N 220 
LEU   OXT  O  N N 221 
LEU   H    H  N N 222 
LEU   H2   H  N N 223 
LEU   HA   H  N N 224 
LEU   HB2  H  N N 225 
LEU   HB3  H  N N 226 
LEU   HG   H  N N 227 
LEU   HD11 H  N N 228 
LEU   HD12 H  N N 229 
LEU   HD13 H  N N 230 
LEU   HD21 H  N N 231 
LEU   HD22 H  N N 232 
LEU   HD23 H  N N 233 
LEU   HXT  H  N N 234 
LYS   N    N  N N 235 
LYS   CA   C  N S 236 
LYS   C    C  N N 237 
LYS   O    O  N N 238 
LYS   CB   C  N N 239 
LYS   CG   C  N N 240 
LYS   CD   C  N N 241 
LYS   CE   C  N N 242 
LYS   NZ   N  N N 243 
LYS   OXT  O  N N 244 
LYS   H    H  N N 245 
LYS   H2   H  N N 246 
LYS   HA   H  N N 247 
LYS   HB2  H  N N 248 
LYS   HB3  H  N N 249 
LYS   HG2  H  N N 250 
LYS   HG3  H  N N 251 
LYS   HD2  H  N N 252 
LYS   HD3  H  N N 253 
LYS   HE2  H  N N 254 
LYS   HE3  H  N N 255 
LYS   HZ1  H  N N 256 
LYS   HZ2  H  N N 257 
LYS   HZ3  H  N N 258 
LYS   HXT  H  N N 259 
MET   N    N  N N 260 
MET   CA   C  N S 261 
MET   C    C  N N 262 
MET   O    O  N N 263 
MET   CB   C  N N 264 
MET   CG   C  N N 265 
MET   SD   S  N N 266 
MET   CE   C  N N 267 
MET   OXT  O  N N 268 
MET   H    H  N N 269 
MET   H2   H  N N 270 
MET   HA   H  N N 271 
MET   HB2  H  N N 272 
MET   HB3  H  N N 273 
MET   HG2  H  N N 274 
MET   HG3  H  N N 275 
MET   HE1  H  N N 276 
MET   HE2  H  N N 277 
MET   HE3  H  N N 278 
MET   HXT  H  N N 279 
MN    MN   MN N N 280 
PHE   N    N  N N 281 
PHE   CA   C  N S 282 
PHE   C    C  N N 283 
PHE   O    O  N N 284 
PHE   CB   C  N N 285 
PHE   CG   C  Y N 286 
PHE   CD1  C  Y N 287 
PHE   CD2  C  Y N 288 
PHE   CE1  C  Y N 289 
PHE   CE2  C  Y N 290 
PHE   CZ   C  Y N 291 
PHE   OXT  O  N N 292 
PHE   H    H  N N 293 
PHE   H2   H  N N 294 
PHE   HA   H  N N 295 
PHE   HB2  H  N N 296 
PHE   HB3  H  N N 297 
PHE   HD1  H  N N 298 
PHE   HD2  H  N N 299 
PHE   HE1  H  N N 300 
PHE   HE2  H  N N 301 
PHE   HZ   H  N N 302 
PHE   HXT  H  N N 303 
PRO   N    N  N N 304 
PRO   CA   C  N S 305 
PRO   C    C  N N 306 
PRO   O    O  N N 307 
PRO   CB   C  N N 308 
PRO   CG   C  N N 309 
PRO   CD   C  N N 310 
PRO   OXT  O  N N 311 
PRO   H    H  N N 312 
PRO   HA   H  N N 313 
PRO   HB2  H  N N 314 
PRO   HB3  H  N N 315 
PRO   HG2  H  N N 316 
PRO   HG3  H  N N 317 
PRO   HD2  H  N N 318 
PRO   HD3  H  N N 319 
PRO   HXT  H  N N 320 
SER   N    N  N N 321 
SER   CA   C  N S 322 
SER   C    C  N N 323 
SER   O    O  N N 324 
SER   CB   C  N N 325 
SER   OG   O  N N 326 
SER   OXT  O  N N 327 
SER   H    H  N N 328 
SER   H2   H  N N 329 
SER   HA   H  N N 330 
SER   HB2  H  N N 331 
SER   HB3  H  N N 332 
SER   HG   H  N N 333 
SER   HXT  H  N N 334 
THR   N    N  N N 335 
THR   CA   C  N S 336 
THR   C    C  N N 337 
THR   O    O  N N 338 
THR   CB   C  N R 339 
THR   OG1  O  N N 340 
THR   CG2  C  N N 341 
THR   OXT  O  N N 342 
THR   H    H  N N 343 
THR   H2   H  N N 344 
THR   HA   H  N N 345 
THR   HB   H  N N 346 
THR   HG1  H  N N 347 
THR   HG21 H  N N 348 
THR   HG22 H  N N 349 
THR   HG23 H  N N 350 
THR   HXT  H  N N 351 
TRP   N    N  N N 352 
TRP   CA   C  N S 353 
TRP   C    C  N N 354 
TRP   O    O  N N 355 
TRP   CB   C  N N 356 
TRP   CG   C  Y N 357 
TRP   CD1  C  Y N 358 
TRP   CD2  C  Y N 359 
TRP   NE1  N  Y N 360 
TRP   CE2  C  Y N 361 
TRP   CE3  C  Y N 362 
TRP   CZ2  C  Y N 363 
TRP   CZ3  C  Y N 364 
TRP   CH2  C  Y N 365 
TRP   OXT  O  N N 366 
TRP   H    H  N N 367 
TRP   H2   H  N N 368 
TRP   HA   H  N N 369 
TRP   HB2  H  N N 370 
TRP   HB3  H  N N 371 
TRP   HD1  H  N N 372 
TRP   HE1  H  N N 373 
TRP   HE3  H  N N 374 
TRP   HZ2  H  N N 375 
TRP   HZ3  H  N N 376 
TRP   HH2  H  N N 377 
TRP   HXT  H  N N 378 
TYR   N    N  N N 379 
TYR   CA   C  N S 380 
TYR   C    C  N N 381 
TYR   O    O  N N 382 
TYR   CB   C  N N 383 
TYR   CG   C  Y N 384 
TYR   CD1  C  Y N 385 
TYR   CD2  C  Y N 386 
TYR   CE1  C  Y N 387 
TYR   CE2  C  Y N 388 
TYR   CZ   C  Y N 389 
TYR   OH   O  N N 390 
TYR   OXT  O  N N 391 
TYR   H    H  N N 392 
TYR   H2   H  N N 393 
TYR   HA   H  N N 394 
TYR   HB2  H  N N 395 
TYR   HB3  H  N N 396 
TYR   HD1  H  N N 397 
TYR   HD2  H  N N 398 
TYR   HE1  H  N N 399 
TYR   HE2  H  N N 400 
TYR   HH   H  N N 401 
TYR   HXT  H  N N 402 
VAL   N    N  N N 403 
VAL   CA   C  N S 404 
VAL   C    C  N N 405 
VAL   O    O  N N 406 
VAL   CB   C  N N 407 
VAL   CG1  C  N N 408 
VAL   CG2  C  N N 409 
VAL   OXT  O  N N 410 
VAL   H    H  N N 411 
VAL   H2   H  N N 412 
VAL   HA   H  N N 413 
VAL   HB   H  N N 414 
VAL   HG11 H  N N 415 
VAL   HG12 H  N N 416 
VAL   HG13 H  N N 417 
VAL   HG21 H  N N 418 
VAL   HG22 H  N N 419 
VAL   HG23 H  N N 420 
VAL   HXT  H  N N 421 
# 
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 
A1H0B N11 C10  sing N N 1   
A1H0B N11 C12  sing N N 2   
A1H0B C10 C9   sing N N 3   
A1H0B C12 C14  sing N N 4   
A1H0B C12 C7   sing N N 5   
A1H0B O15 C14  doub N N 6   
A1H0B C14 O16  sing N N 7   
A1H0B C9  C7   sing N N 8   
A1H0B C7  C6   sing N N 9   
A1H0B C6  C5   sing N N 10  
A1H0B C5  C4   sing N N 11  
A1H0B C4  B2   sing N N 12  
A1H0B B2  O3   sing N N 13  
A1H0B B2  O1   sing N N 14  
A1H0B C7  H8   sing N N 15  
A1H0B C9  H1   sing N N 16  
A1H0B C9  H2   sing N N 17  
A1H0B C10 H3   sing N N 18  
A1H0B C10 H4   sing N N 19  
A1H0B C12 H13  sing N N 20  
A1H0B O1  H5   sing N N 21  
A1H0B O3  H6   sing N N 22  
A1H0B C4  H7   sing N N 23  
A1H0B C4  H9   sing N N 24  
A1H0B C5  H10  sing N N 25  
A1H0B C5  H11  sing N N 26  
A1H0B C6  H12  sing N N 27  
A1H0B C6  H14  sing N N 28  
A1H0B N11 H15  sing N N 29  
A1H0B O16 H17  sing N N 30  
ALA   N   CA   sing N N 31  
ALA   N   H    sing N N 32  
ALA   N   H2   sing N N 33  
ALA   CA  C    sing N N 34  
ALA   CA  CB   sing N N 35  
ALA   CA  HA   sing N N 36  
ALA   C   O    doub N N 37  
ALA   C   OXT  sing N N 38  
ALA   CB  HB1  sing N N 39  
ALA   CB  HB2  sing N N 40  
ALA   CB  HB3  sing N N 41  
ALA   OXT HXT  sing N N 42  
ARG   N   CA   sing N N 43  
ARG   N   H    sing N N 44  
ARG   N   H2   sing N N 45  
ARG   CA  C    sing N N 46  
ARG   CA  CB   sing N N 47  
ARG   CA  HA   sing N N 48  
ARG   C   O    doub N N 49  
ARG   C   OXT  sing N N 50  
ARG   CB  CG   sing N N 51  
ARG   CB  HB2  sing N N 52  
ARG   CB  HB3  sing N N 53  
ARG   CG  CD   sing N N 54  
ARG   CG  HG2  sing N N 55  
ARG   CG  HG3  sing N N 56  
ARG   CD  NE   sing N N 57  
ARG   CD  HD2  sing N N 58  
ARG   CD  HD3  sing N N 59  
ARG   NE  CZ   sing N N 60  
ARG   NE  HE   sing N N 61  
ARG   CZ  NH1  sing N N 62  
ARG   CZ  NH2  doub N N 63  
ARG   NH1 HH11 sing N N 64  
ARG   NH1 HH12 sing N N 65  
ARG   NH2 HH21 sing N N 66  
ARG   NH2 HH22 sing N N 67  
ARG   OXT HXT  sing N N 68  
ASN   N   CA   sing N N 69  
ASN   N   H    sing N N 70  
ASN   N   H2   sing N N 71  
ASN   CA  C    sing N N 72  
ASN   CA  CB   sing N N 73  
ASN   CA  HA   sing N N 74  
ASN   C   O    doub N N 75  
ASN   C   OXT  sing N N 76  
ASN   CB  CG   sing N N 77  
ASN   CB  HB2  sing N N 78  
ASN   CB  HB3  sing N N 79  
ASN   CG  OD1  doub N N 80  
ASN   CG  ND2  sing N N 81  
ASN   ND2 HD21 sing N N 82  
ASN   ND2 HD22 sing N N 83  
ASN   OXT HXT  sing N N 84  
ASP   N   CA   sing N N 85  
ASP   N   H    sing N N 86  
ASP   N   H2   sing N N 87  
ASP   CA  C    sing N N 88  
ASP   CA  CB   sing N N 89  
ASP   CA  HA   sing N N 90  
ASP   C   O    doub N N 91  
ASP   C   OXT  sing N N 92  
ASP   CB  CG   sing N N 93  
ASP   CB  HB2  sing N N 94  
ASP   CB  HB3  sing N N 95  
ASP   CG  OD1  doub N N 96  
ASP   CG  OD2  sing N N 97  
ASP   OD2 HD2  sing N N 98  
ASP   OXT HXT  sing N N 99  
CYS   N   CA   sing N N 100 
CYS   N   H    sing N N 101 
CYS   N   H2   sing N N 102 
CYS   CA  C    sing N N 103 
CYS   CA  CB   sing N N 104 
CYS   CA  HA   sing N N 105 
CYS   C   O    doub N N 106 
CYS   C   OXT  sing N N 107 
CYS   CB  SG   sing N N 108 
CYS   CB  HB2  sing N N 109 
CYS   CB  HB3  sing N N 110 
CYS   SG  HG   sing N N 111 
CYS   OXT HXT  sing N N 112 
GLN   N   CA   sing N N 113 
GLN   N   H    sing N N 114 
GLN   N   H2   sing N N 115 
GLN   CA  C    sing N N 116 
GLN   CA  CB   sing N N 117 
GLN   CA  HA   sing N N 118 
GLN   C   O    doub N N 119 
GLN   C   OXT  sing N N 120 
GLN   CB  CG   sing N N 121 
GLN   CB  HB2  sing N N 122 
GLN   CB  HB3  sing N N 123 
GLN   CG  CD   sing N N 124 
GLN   CG  HG2  sing N N 125 
GLN   CG  HG3  sing N N 126 
GLN   CD  OE1  doub N N 127 
GLN   CD  NE2  sing N N 128 
GLN   NE2 HE21 sing N N 129 
GLN   NE2 HE22 sing N N 130 
GLN   OXT HXT  sing N N 131 
GLU   N   CA   sing N N 132 
GLU   N   H    sing N N 133 
GLU   N   H2   sing N N 134 
GLU   CA  C    sing N N 135 
GLU   CA  CB   sing N N 136 
GLU   CA  HA   sing N N 137 
GLU   C   O    doub N N 138 
GLU   C   OXT  sing N N 139 
GLU   CB  CG   sing N N 140 
GLU   CB  HB2  sing N N 141 
GLU   CB  HB3  sing N N 142 
GLU   CG  CD   sing N N 143 
GLU   CG  HG2  sing N N 144 
GLU   CG  HG3  sing N N 145 
GLU   CD  OE1  doub N N 146 
GLU   CD  OE2  sing N N 147 
GLU   OE2 HE2  sing N N 148 
GLU   OXT HXT  sing N N 149 
GLY   N   CA   sing N N 150 
GLY   N   H    sing N N 151 
GLY   N   H2   sing N N 152 
GLY   CA  C    sing N N 153 
GLY   CA  HA2  sing N N 154 
GLY   CA  HA3  sing N N 155 
GLY   C   O    doub N N 156 
GLY   C   OXT  sing N N 157 
GLY   OXT HXT  sing N N 158 
HIS   N   CA   sing N N 159 
HIS   N   H    sing N N 160 
HIS   N   H2   sing N N 161 
HIS   CA  C    sing N N 162 
HIS   CA  CB   sing N N 163 
HIS   CA  HA   sing N N 164 
HIS   C   O    doub N N 165 
HIS   C   OXT  sing N N 166 
HIS   CB  CG   sing N N 167 
HIS   CB  HB2  sing N N 168 
HIS   CB  HB3  sing N N 169 
HIS   CG  ND1  sing Y N 170 
HIS   CG  CD2  doub Y N 171 
HIS   ND1 CE1  doub Y N 172 
HIS   ND1 HD1  sing N N 173 
HIS   CD2 NE2  sing Y N 174 
HIS   CD2 HD2  sing N N 175 
HIS   CE1 NE2  sing Y N 176 
HIS   CE1 HE1  sing N N 177 
HIS   NE2 HE2  sing N N 178 
HIS   OXT HXT  sing N N 179 
HOH   O   H1   sing N N 180 
HOH   O   H2   sing N N 181 
ILE   N   CA   sing N N 182 
ILE   N   H    sing N N 183 
ILE   N   H2   sing N N 184 
ILE   CA  C    sing N N 185 
ILE   CA  CB   sing N N 186 
ILE   CA  HA   sing N N 187 
ILE   C   O    doub N N 188 
ILE   C   OXT  sing N N 189 
ILE   CB  CG1  sing N N 190 
ILE   CB  CG2  sing N N 191 
ILE   CB  HB   sing N N 192 
ILE   CG1 CD1  sing N N 193 
ILE   CG1 HG12 sing N N 194 
ILE   CG1 HG13 sing N N 195 
ILE   CG2 HG21 sing N N 196 
ILE   CG2 HG22 sing N N 197 
ILE   CG2 HG23 sing N N 198 
ILE   CD1 HD11 sing N N 199 
ILE   CD1 HD12 sing N N 200 
ILE   CD1 HD13 sing N N 201 
ILE   OXT HXT  sing N N 202 
LEU   N   CA   sing N N 203 
LEU   N   H    sing N N 204 
LEU   N   H2   sing N N 205 
LEU   CA  C    sing N N 206 
LEU   CA  CB   sing N N 207 
LEU   CA  HA   sing N N 208 
LEU   C   O    doub N N 209 
LEU   C   OXT  sing N N 210 
LEU   CB  CG   sing N N 211 
LEU   CB  HB2  sing N N 212 
LEU   CB  HB3  sing N N 213 
LEU   CG  CD1  sing N N 214 
LEU   CG  CD2  sing N N 215 
LEU   CG  HG   sing N N 216 
LEU   CD1 HD11 sing N N 217 
LEU   CD1 HD12 sing N N 218 
LEU   CD1 HD13 sing N N 219 
LEU   CD2 HD21 sing N N 220 
LEU   CD2 HD22 sing N N 221 
LEU   CD2 HD23 sing N N 222 
LEU   OXT HXT  sing N N 223 
LYS   N   CA   sing N N 224 
LYS   N   H    sing N N 225 
LYS   N   H2   sing N N 226 
LYS   CA  C    sing N N 227 
LYS   CA  CB   sing N N 228 
LYS   CA  HA   sing N N 229 
LYS   C   O    doub N N 230 
LYS   C   OXT  sing N N 231 
LYS   CB  CG   sing N N 232 
LYS   CB  HB2  sing N N 233 
LYS   CB  HB3  sing N N 234 
LYS   CG  CD   sing N N 235 
LYS   CG  HG2  sing N N 236 
LYS   CG  HG3  sing N N 237 
LYS   CD  CE   sing N N 238 
LYS   CD  HD2  sing N N 239 
LYS   CD  HD3  sing N N 240 
LYS   CE  NZ   sing N N 241 
LYS   CE  HE2  sing N N 242 
LYS   CE  HE3  sing N N 243 
LYS   NZ  HZ1  sing N N 244 
LYS   NZ  HZ2  sing N N 245 
LYS   NZ  HZ3  sing N N 246 
LYS   OXT HXT  sing N N 247 
MET   N   CA   sing N N 248 
MET   N   H    sing N N 249 
MET   N   H2   sing N N 250 
MET   CA  C    sing N N 251 
MET   CA  CB   sing N N 252 
MET   CA  HA   sing N N 253 
MET   C   O    doub N N 254 
MET   C   OXT  sing N N 255 
MET   CB  CG   sing N N 256 
MET   CB  HB2  sing N N 257 
MET   CB  HB3  sing N N 258 
MET   CG  SD   sing N N 259 
MET   CG  HG2  sing N N 260 
MET   CG  HG3  sing N N 261 
MET   SD  CE   sing N N 262 
MET   CE  HE1  sing N N 263 
MET   CE  HE2  sing N N 264 
MET   CE  HE3  sing N N 265 
MET   OXT HXT  sing N N 266 
PHE   N   CA   sing N N 267 
PHE   N   H    sing N N 268 
PHE   N   H2   sing N N 269 
PHE   CA  C    sing N N 270 
PHE   CA  CB   sing N N 271 
PHE   CA  HA   sing N N 272 
PHE   C   O    doub N N 273 
PHE   C   OXT  sing N N 274 
PHE   CB  CG   sing N N 275 
PHE   CB  HB2  sing N N 276 
PHE   CB  HB3  sing N N 277 
PHE   CG  CD1  doub Y N 278 
PHE   CG  CD2  sing Y N 279 
PHE   CD1 CE1  sing Y N 280 
PHE   CD1 HD1  sing N N 281 
PHE   CD2 CE2  doub Y N 282 
PHE   CD2 HD2  sing N N 283 
PHE   CE1 CZ   doub Y N 284 
PHE   CE1 HE1  sing N N 285 
PHE   CE2 CZ   sing Y N 286 
PHE   CE2 HE2  sing N N 287 
PHE   CZ  HZ   sing N N 288 
PHE   OXT HXT  sing N N 289 
PRO   N   CA   sing N N 290 
PRO   N   CD   sing N N 291 
PRO   N   H    sing N N 292 
PRO   CA  C    sing N N 293 
PRO   CA  CB   sing N N 294 
PRO   CA  HA   sing N N 295 
PRO   C   O    doub N N 296 
PRO   C   OXT  sing N N 297 
PRO   CB  CG   sing N N 298 
PRO   CB  HB2  sing N N 299 
PRO   CB  HB3  sing N N 300 
PRO   CG  CD   sing N N 301 
PRO   CG  HG2  sing N N 302 
PRO   CG  HG3  sing N N 303 
PRO   CD  HD2  sing N N 304 
PRO   CD  HD3  sing N N 305 
PRO   OXT HXT  sing N N 306 
SER   N   CA   sing N N 307 
SER   N   H    sing N N 308 
SER   N   H2   sing N N 309 
SER   CA  C    sing N N 310 
SER   CA  CB   sing N N 311 
SER   CA  HA   sing N N 312 
SER   C   O    doub N N 313 
SER   C   OXT  sing N N 314 
SER   CB  OG   sing N N 315 
SER   CB  HB2  sing N N 316 
SER   CB  HB3  sing N N 317 
SER   OG  HG   sing N N 318 
SER   OXT HXT  sing N N 319 
THR   N   CA   sing N N 320 
THR   N   H    sing N N 321 
THR   N   H2   sing N N 322 
THR   CA  C    sing N N 323 
THR   CA  CB   sing N N 324 
THR   CA  HA   sing N N 325 
THR   C   O    doub N N 326 
THR   C   OXT  sing N N 327 
THR   CB  OG1  sing N N 328 
THR   CB  CG2  sing N N 329 
THR   CB  HB   sing N N 330 
THR   OG1 HG1  sing N N 331 
THR   CG2 HG21 sing N N 332 
THR   CG2 HG22 sing N N 333 
THR   CG2 HG23 sing N N 334 
THR   OXT HXT  sing N N 335 
TRP   N   CA   sing N N 336 
TRP   N   H    sing N N 337 
TRP   N   H2   sing N N 338 
TRP   CA  C    sing N N 339 
TRP   CA  CB   sing N N 340 
TRP   CA  HA   sing N N 341 
TRP   C   O    doub N N 342 
TRP   C   OXT  sing N N 343 
TRP   CB  CG   sing N N 344 
TRP   CB  HB2  sing N N 345 
TRP   CB  HB3  sing N N 346 
TRP   CG  CD1  doub Y N 347 
TRP   CG  CD2  sing Y N 348 
TRP   CD1 NE1  sing Y N 349 
TRP   CD1 HD1  sing N N 350 
TRP   CD2 CE2  doub Y N 351 
TRP   CD2 CE3  sing Y N 352 
TRP   NE1 CE2  sing Y N 353 
TRP   NE1 HE1  sing N N 354 
TRP   CE2 CZ2  sing Y N 355 
TRP   CE3 CZ3  doub Y N 356 
TRP   CE3 HE3  sing N N 357 
TRP   CZ2 CH2  doub Y N 358 
TRP   CZ2 HZ2  sing N N 359 
TRP   CZ3 CH2  sing Y N 360 
TRP   CZ3 HZ3  sing N N 361 
TRP   CH2 HH2  sing N N 362 
TRP   OXT HXT  sing N N 363 
TYR   N   CA   sing N N 364 
TYR   N   H    sing N N 365 
TYR   N   H2   sing N N 366 
TYR   CA  C    sing N N 367 
TYR   CA  CB   sing N N 368 
TYR   CA  HA   sing N N 369 
TYR   C   O    doub N N 370 
TYR   C   OXT  sing N N 371 
TYR   CB  CG   sing N N 372 
TYR   CB  HB2  sing N N 373 
TYR   CB  HB3  sing N N 374 
TYR   CG  CD1  doub Y N 375 
TYR   CG  CD2  sing Y N 376 
TYR   CD1 CE1  sing Y N 377 
TYR   CD1 HD1  sing N N 378 
TYR   CD2 CE2  doub Y N 379 
TYR   CD2 HD2  sing N N 380 
TYR   CE1 CZ   doub Y N 381 
TYR   CE1 HE1  sing N N 382 
TYR   CE2 CZ   sing Y N 383 
TYR   CE2 HE2  sing N N 384 
TYR   CZ  OH   sing N N 385 
TYR   OH  HH   sing N N 386 
TYR   OXT HXT  sing N N 387 
VAL   N   CA   sing N N 388 
VAL   N   H    sing N N 389 
VAL   N   H2   sing N N 390 
VAL   CA  C    sing N N 391 
VAL   CA  CB   sing N N 392 
VAL   CA  HA   sing N N 393 
VAL   C   O    doub N N 394 
VAL   C   OXT  sing N N 395 
VAL   CB  CG1  sing N N 396 
VAL   CB  CG2  sing N N 397 
VAL   CB  HB   sing N N 398 
VAL   CG1 HG11 sing N N 399 
VAL   CG1 HG12 sing N N 400 
VAL   CG1 HG13 sing N N 401 
VAL   CG2 HG21 sing N N 402 
VAL   CG2 HG22 sing N N 403 
VAL   CG2 HG23 sing N N 404 
VAL   OXT HXT  sing N N 405 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_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      Other 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          'Inhouse model' 
# 
_atom_sites.entry_id                    8RG6 
_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]   0.020614 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.007447 
_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]   0.006896 
_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 
B  
C  
H  
MN 
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . VAL   A 1 18  ? 10.912  13.957  -17.999 1.00 56.38  ? 23  VAL   A N   1 
ATOM   2    C  CA  . VAL   A 1 18  ? 9.792   13.984  -18.944 1.00 56.05  ? 23  VAL   A CA  1 
ATOM   3    C  C   . VAL   A 1 18  ? 9.601   12.580  -19.566 1.00 57.73  ? 23  VAL   A C   1 
ATOM   4    O  O   . VAL   A 1 18  ? 10.577  11.950  -19.987 1.00 57.96  ? 23  VAL   A O   1 
ATOM   5    C  CB  . VAL   A 1 18  ? 9.929   15.115  -20.012 1.00 60.50  ? 23  VAL   A CB  1 
ATOM   6    C  CG1 . VAL   A 1 18  ? 8.658   15.252  -20.848 1.00 60.24  ? 23  VAL   A CG1 1 
ATOM   7    C  CG2 . VAL   A 1 18  ? 10.275  16.459  -19.362 1.00 60.50  ? 23  VAL   A CG2 1 
ATOM   8    N  N   . HIS   A 1 19  ? 8.353   12.082  -19.573 1.00 51.20  ? 24  HIS   A N   1 
ATOM   9    C  CA  . HIS   A 1 19  ? 8.010   10.762  -20.116 1.00 49.56  ? 24  HIS   A CA  1 
ATOM   10   C  C   . HIS   A 1 19  ? 6.833   10.863  -21.076 1.00 49.15  ? 24  HIS   A C   1 
ATOM   11   O  O   . HIS   A 1 19  ? 5.842   11.526  -20.761 1.00 48.26  ? 24  HIS   A O   1 
ATOM   12   C  CB  . HIS   A 1 19  ? 7.598   9.782   -18.989 1.00 50.40  ? 24  HIS   A CB  1 
ATOM   13   C  CG  . HIS   A 1 19  ? 8.526   9.713   -17.817 1.00 53.93  ? 24  HIS   A CG  1 
ATOM   14   N  ND1 . HIS   A 1 19  ? 9.722   9.027   -17.885 1.00 55.88  ? 24  HIS   A ND1 1 
ATOM   15   C  CD2 . HIS   A 1 19  ? 8.369   10.195  -16.562 1.00 55.66  ? 24  HIS   A CD2 1 
ATOM   16   C  CE1 . HIS   A 1 19  ? 10.273  9.143   -16.686 1.00 55.31  ? 24  HIS   A CE1 1 
ATOM   17   N  NE2 . HIS   A 1 19  ? 9.496   9.840   -15.858 1.00 55.49  ? 24  HIS   A NE2 1 
ATOM   18   N  N   . SER   A 1 20  ? 6.911   10.156  -22.215 1.00 42.23  ? 25  SER   A N   1 
ATOM   19   C  CA  . SER   A 1 20  ? 5.796   10.066  -23.153 1.00 41.17  ? 25  SER   A CA  1 
ATOM   20   C  C   . SER   A 1 20  ? 4.949   8.897   -22.665 1.00 41.10  ? 25  SER   A C   1 
ATOM   21   O  O   . SER   A 1 20  ? 5.437   7.768   -22.605 1.00 41.37  ? 25  SER   A O   1 
ATOM   22   C  CB  . SER   A 1 20  ? 6.292   9.832   -24.576 1.00 45.53  ? 25  SER   A CB  1 
ATOM   23   O  OG  . SER   A 1 20  ? 6.834   11.026  -25.117 1.00 56.64  ? 25  SER   A OG  1 
ATOM   24   N  N   . VAL   A 1 21  ? 3.718   9.182   -22.230 1.00 34.78  ? 26  VAL   A N   1 
ATOM   25   C  CA  . VAL   A 1 21  ? 2.834   8.187   -21.636 1.00 34.44  ? 26  VAL   A CA  1 
ATOM   26   C  C   . VAL   A 1 21  ? 1.500   8.057   -22.384 1.00 37.12  ? 26  VAL   A C   1 
ATOM   27   O  O   . VAL   A 1 21  ? 0.747   9.020   -22.484 1.00 37.55  ? 26  VAL   A O   1 
ATOM   28   C  CB  . VAL   A 1 21  ? 2.616   8.467   -20.106 1.00 37.73  ? 26  VAL   A CB  1 
ATOM   29   C  CG1 . VAL   A 1 21  ? 1.668   7.449   -19.476 1.00 37.82  ? 26  VAL   A CG1 1 
ATOM   30   C  CG2 . VAL   A 1 21  ? 3.943   8.507   -19.351 1.00 37.30  ? 26  VAL   A CG2 1 
ATOM   31   N  N   . ALA   A 1 22  ? 1.189   6.844   -22.850 1.00 32.98  ? 27  ALA   A N   1 
ATOM   32   C  CA  . ALA   A 1 22  ? -0.095  6.562   -23.473 1.00 32.30  ? 27  ALA   A CA  1 
ATOM   33   C  C   . ALA   A 1 22  ? -0.977  5.866   -22.447 1.00 36.91  ? 27  ALA   A C   1 
ATOM   34   O  O   . ALA   A 1 22  ? -0.484  5.040   -21.672 1.00 36.21  ? 27  ALA   A O   1 
ATOM   35   C  CB  . ALA   A 1 22  ? 0.082   5.668   -24.683 1.00 32.75  ? 27  ALA   A CB  1 
ATOM   36   N  N   . VAL   A 1 23  ? -2.282  6.178   -22.447 1.00 34.12  ? 28  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 23  ? -3.261  5.565   -21.552 1.00 33.13  ? 28  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 23  ? -4.362  4.866   -22.345 1.00 37.50  ? 28  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 23  ? -4.971  5.468   -23.226 1.00 38.03  ? 28  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 23  ? -3.825  6.550   -20.484 1.00 36.14  ? 28  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 23  ? -4.917  5.894   -19.639 1.00 36.27  ? 28  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 23  ? -2.715  7.082   -19.587 1.00 35.54  ? 28  VAL   A CG2 1 
ATOM   43   N  N   . ILE   A 1 24  ? -4.611  3.596   -22.031 1.00 33.55  ? 29  ILE   A N   1 
ATOM   44   C  CA  . ILE   A 1 24  ? -5.646  2.801   -22.683 1.00 32.63  ? 29  ILE   A CA  1 
ATOM   45   C  C   . ILE   A 1 24  ? -6.528  2.186   -21.613 1.00 38.11  ? 29  ILE   A C   1 
ATOM   46   O  O   . ILE   A 1 24  ? -6.035  1.445   -20.755 1.00 36.17  ? 29  ILE   A O   1 
ATOM   47   C  CB  . ILE   A 1 24  ? -5.065  1.681   -23.604 1.00 34.97  ? 29  ILE   A CB  1 
ATOM   48   C  CG1 . ILE   A 1 24  ? -4.041  2.204   -24.629 1.00 35.20  ? 29  ILE   A CG1 1 
ATOM   49   C  CG2 . ILE   A 1 24  ? -6.182  0.897   -24.280 1.00 36.08  ? 29  ILE   A CG2 1 
ATOM   50   C  CD1 . ILE   A 1 24  ? -3.141  1.099   -25.206 1.00 42.06  ? 29  ILE   A CD1 1 
ATOM   51   N  N   . GLY   A 1 25  ? -7.825  2.437   -21.711 1.00 35.87  ? 30  GLY   A N   1 
ATOM   52   C  CA  . GLY   A 1 25  ? -8.811  1.831   -20.834 1.00 36.54  ? 30  GLY   A CA  1 
ATOM   53   C  C   . GLY   A 1 25  ? -9.285  0.542   -21.463 1.00 40.55  ? 30  GLY   A C   1 
ATOM   54   O  O   . GLY   A 1 25  ? -9.683  0.534   -22.634 1.00 41.75  ? 30  GLY   A O   1 
ATOM   55   N  N   . ALA   A 1 26  ? -9.203  -0.566  -20.723 1.00 36.74  ? 31  ALA   A N   1 
ATOM   56   C  CA  . ALA   A 1 26  ? -9.646  -1.875  -21.192 1.00 36.67  ? 31  ALA   A CA  1 
ATOM   57   C  C   . ALA   A 1 26  ? -10.784 -2.421  -20.297 1.00 41.28  ? 31  ALA   A C   1 
ATOM   58   O  O   . ALA   A 1 26  ? -10.545 -3.255  -19.415 1.00 40.18  ? 31  ALA   A O   1 
ATOM   59   C  CB  . ALA   A 1 26  ? -8.463  -2.838  -21.277 1.00 37.16  ? 31  ALA   A CB  1 
ATOM   60   N  N   . PRO   A 1 27  ? -12.041 -1.918  -20.496 1.00 39.13  ? 32  PRO   A N   1 
ATOM   61   C  CA  . PRO   A 1 27  ? -13.168 -2.360  -19.650 1.00 39.59  ? 32  PRO   A CA  1 
ATOM   62   C  C   . PRO   A 1 27  ? -13.663 -3.771  -19.967 1.00 44.36  ? 32  PRO   A C   1 
ATOM   63   O  O   . PRO   A 1 27  ? -14.760 -3.939  -20.510 1.00 44.78  ? 32  PRO   A O   1 
ATOM   64   C  CB  . PRO   A 1 27  ? -14.245 -1.301  -19.929 1.00 41.64  ? 32  PRO   A CB  1 
ATOM   65   C  CG  . PRO   A 1 27  ? -13.963 -0.826  -21.312 1.00 45.45  ? 32  PRO   A CG  1 
ATOM   66   C  CD  . PRO   A 1 27  ? -12.475 -0.916  -21.497 1.00 40.43  ? 32  PRO   A CD  1 
ATOM   67   N  N   . PHE   A 1 28  ? -12.879 -4.789  -19.577 1.00 39.97  ? 33  PHE   A N   1 
ATOM   68   C  CA  . PHE   A 1 28  ? -13.163 -6.184  -19.887 1.00 39.50  ? 33  PHE   A CA  1 
ATOM   69   C  C   . PHE   A 1 28  ? -13.271 -7.069  -18.650 1.00 41.56  ? 33  PHE   A C   1 
ATOM   70   O  O   . PHE   A 1 28  ? -12.429 -6.988  -17.754 1.00 39.65  ? 33  PHE   A O   1 
ATOM   71   C  CB  . PHE   A 1 28  ? -12.105 -6.689  -20.869 1.00 41.27  ? 33  PHE   A CB  1 
ATOM   72   C  CG  . PHE   A 1 28  ? -12.328 -8.064  -21.427 1.00 42.86  ? 33  PHE   A CG  1 
ATOM   73   C  CD1 . PHE   A 1 28  ? -13.333 -8.298  -22.360 1.00 46.39  ? 33  PHE   A CD1 1 
ATOM   74   C  CD2 . PHE   A 1 28  ? -11.507 -9.124  -21.053 1.00 45.18  ? 33  PHE   A CD2 1 
ATOM   75   C  CE1 . PHE   A 1 28  ? -13.545 -9.577  -22.872 1.00 47.51  ? 33  PHE   A CE1 1 
ATOM   76   C  CE2 . PHE   A 1 28  ? -11.705 -10.400 -21.584 1.00 48.02  ? 33  PHE   A CE2 1 
ATOM   77   C  CZ  . PHE   A 1 28  ? -12.711 -10.613 -22.500 1.00 46.63  ? 33  PHE   A CZ  1 
ATOM   78   N  N   . SER   A 1 29  ? -14.306 -7.925  -18.611 1.00 37.05  ? 34  SER   A N   1 
ATOM   79   C  CA  . SER   A 1 29  ? -14.564 -8.770  -17.446 1.00 36.08  ? 34  SER   A CA  1 
ATOM   80   C  C   . SER   A 1 29  ? -14.661 -10.280 -17.706 1.00 39.39  ? 34  SER   A C   1 
ATOM   81   O  O   . SER   A 1 29  ? -14.664 -11.032 -16.730 1.00 38.95  ? 34  SER   A O   1 
ATOM   82   C  CB  . SER   A 1 29  ? -15.823 -8.288  -16.726 1.00 39.62  ? 34  SER   A CB  1 
ATOM   83   O  OG  . SER   A 1 29  ? -16.979 -8.474  -17.527 1.00 46.95  ? 34  SER   A OG  1 
ATOM   84   N  N   . GLN   A 1 30  ? -14.686 -10.736 -18.988 1.00 38.18  ? 35  GLN   A N   1 
ATOM   85   C  CA  . GLN   A 1 30  ? -14.862 -12.162 -19.369 1.00 37.80  ? 35  GLN   A CA  1 
ATOM   86   C  C   . GLN   A 1 30  ? -13.728 -13.134 -18.968 1.00 40.56  ? 35  GLN   A C   1 
ATOM   87   O  O   . GLN   A 1 30  ? -13.866 -14.353 -19.180 1.00 39.39  ? 35  GLN   A O   1 
ATOM   88   C  CB  . GLN   A 1 30  ? -15.149 -12.293 -20.871 1.00 39.29  ? 35  GLN   A CB  1 
ATOM   89   C  CG  . GLN   A 1 30  ? -16.642 -12.263 -21.239 1.00 67.19  ? 35  GLN   A CG  1 
ATOM   90   C  CD  . GLN   A 1 30  ? -17.315 -10.937 -20.973 1.00 93.40  ? 35  GLN   A CD  1 
ATOM   91   O  OE1 . GLN   A 1 30  ? -17.950 -10.735 -19.930 1.00 89.90  ? 35  GLN   A OE1 1 
ATOM   92   N  NE2 . GLN   A 1 30  ? -17.200 -10.010 -21.917 1.00 86.91  ? 35  GLN   A NE2 1 
ATOM   93   N  N   . GLY   A 1 31  ? -12.646 -12.618 -18.377 1.00 36.32  ? 36  GLY   A N   1 
ATOM   94   C  CA  . GLY   A 1 31  ? -11.558 -13.466 -17.888 1.00 36.14  ? 36  GLY   A CA  1 
ATOM   95   C  C   . GLY   A 1 31  ? -11.882 -14.059 -16.529 1.00 39.28  ? 36  GLY   A C   1 
ATOM   96   O  O   . GLY   A 1 31  ? -11.158 -14.933 -16.043 1.00 39.02  ? 36  GLY   A O   1 
ATOM   97   N  N   . GLN   A 1 32  ? -13.004 -13.621 -15.925 1.00 36.43  ? 37  GLN   A N   1 
ATOM   98   C  CA  . GLN   A 1 32  ? -13.483 -14.066 -14.617 1.00 36.01  ? 37  GLN   A CA  1 
ATOM   99   C  C   . GLN   A 1 32  ? -15.024 -13.960 -14.484 1.00 43.65  ? 37  GLN   A C   1 
ATOM   100  O  O   . GLN   A 1 32  ? -15.674 -13.466 -15.404 1.00 43.84  ? 37  GLN   A O   1 
ATOM   101  C  CB  . GLN   A 1 32  ? -12.734 -13.360 -13.476 1.00 35.91  ? 37  GLN   A CB  1 
ATOM   102  C  CG  . GLN   A 1 32  ? -12.619 -11.853 -13.616 1.00 34.40  ? 37  GLN   A CG  1 
ATOM   103  C  CD  . GLN   A 1 32  ? -13.817 -11.161 -13.029 1.00 45.18  ? 37  GLN   A CD  1 
ATOM   104  O  OE1 . GLN   A 1 32  ? -14.060 -11.199 -11.815 1.00 41.71  ? 37  GLN   A OE1 1 
ATOM   105  N  NE2 . GLN   A 1 32  ? -14.593 -10.528 -13.885 1.00 38.94  ? 37  GLN   A NE2 1 
ATOM   106  N  N   . LYS   A 1 33  ? -15.596 -14.445 -13.357 1.00 42.21  ? 38  LYS   A N   1 
ATOM   107  C  CA  . LYS   A 1 33  ? -17.056 -14.537 -13.161 1.00 43.33  ? 38  LYS   A CA  1 
ATOM   108  C  C   . LYS   A 1 33  ? -17.732 -13.367 -12.425 1.00 49.10  ? 38  LYS   A C   1 
ATOM   109  O  O   . LYS   A 1 33  ? -18.933 -13.169 -12.621 1.00 49.09  ? 38  LYS   A O   1 
ATOM   110  C  CB  . LYS   A 1 33  ? -17.416 -15.859 -12.466 1.00 46.00  ? 38  LYS   A CB  1 
ATOM   111  C  CG  . LYS   A 1 33  ? -17.304 -17.077 -13.387 1.00 62.43  ? 38  LYS   A CG  1 
ATOM   112  C  CD  . LYS   A 1 33  ? -17.843 -18.345 -12.728 1.00 72.34  ? 38  LYS   A CD  1 
ATOM   113  C  CE  . LYS   A 1 33  ? -17.525 -19.593 -13.520 1.00 82.60  ? 38  LYS   A CE  1 
ATOM   114  N  NZ  . LYS   A 1 33  ? -16.155 -20.103 -13.240 1.00 89.87  ? 38  LYS   A NZ  1 
ATOM   115  N  N   . ARG   A 1 34  ? -16.998 -12.606 -11.589 1.00 46.76  ? 39  ARG   A N   1 
ATOM   116  C  CA  . ARG   A 1 34  ? -17.597 -11.483 -10.850 1.00 46.65  ? 39  ARG   A CA  1 
ATOM   117  C  C   . ARG   A 1 34  ? -17.807 -10.259 -11.744 1.00 50.36  ? 39  ARG   A C   1 
ATOM   118  O  O   . ARG   A 1 34  ? -16.886 -9.834  -12.439 1.00 49.41  ? 39  ARG   A O   1 
ATOM   119  C  CB  . ARG   A 1 34  ? -16.777 -11.117 -9.599  1.00 46.25  ? 39  ARG   A CB  1 
ATOM   120  C  CG  . ARG   A 1 34  ? -16.693 -12.247 -8.571  1.00 56.79  ? 39  ARG   A CG  1 
ATOM   121  C  CD  . ARG   A 1 34  ? -17.090 -11.776 -7.185  1.00 66.04  ? 39  ARG   A CD  1 
ATOM   122  N  NE  . ARG   A 1 34  ? -15.989 -11.903 -6.231  1.00 68.42  ? 39  ARG   A NE  1 
ATOM   123  C  CZ  . ARG   A 1 34  ? -16.096 -11.689 -4.923  1.00 78.16  ? 39  ARG   A CZ  1 
ATOM   124  N  NH1 . ARG   A 1 34  ? -17.263 -11.338 -4.392  1.00 53.23  ? 39  ARG   A NH1 1 
ATOM   125  N  NH2 . ARG   A 1 34  ? -15.039 -11.827 -4.133  1.00 66.70  ? 39  ARG   A NH2 1 
ATOM   126  N  N   . LYS   A 1 35  ? -19.022 -9.702  -11.743 1.00 47.07  ? 40  LYS   A N   1 
ATOM   127  C  CA  . LYS   A 1 35  ? -19.286 -8.504  -12.544 1.00 46.56  ? 40  LYS   A CA  1 
ATOM   128  C  C   . LYS   A 1 35  ? -18.805 -7.244  -11.819 1.00 47.94  ? 40  LYS   A C   1 
ATOM   129  O  O   . LYS   A 1 35  ? -18.780 -7.210  -10.583 1.00 47.99  ? 40  LYS   A O   1 
ATOM   130  C  CB  . LYS   A 1 35  ? -20.765 -8.404  -12.984 1.00 49.93  ? 40  LYS   A CB  1 
ATOM   131  C  CG  . LYS   A 1 35  ? -21.801 -8.576  -11.872 1.00 66.63  ? 40  LYS   A CG  1 
ATOM   132  C  CD  . LYS   A 1 35  ? -23.201 -8.845  -12.444 1.00 78.75  ? 40  LYS   A CD  1 
ATOM   133  C  CE  . LYS   A 1 35  ? -23.471 -10.309 -12.718 1.00 89.29  ? 40  LYS   A CE  1 
ATOM   134  N  NZ  . LYS   A 1 35  ? -24.795 -10.517 -13.361 1.00 98.09  ? 40  LYS   A NZ  1 
ATOM   135  N  N   . GLY   A 1 36  ? -18.376 -6.251  -12.594 1.00 42.94  ? 41  GLY   A N   1 
ATOM   136  C  CA  . GLY   A 1 36  ? -17.934 -4.970  -12.058 1.00 41.55  ? 41  GLY   A CA  1 
ATOM   137  C  C   . GLY   A 1 36  ? -16.517 -4.529  -12.363 1.00 41.86  ? 41  GLY   A C   1 
ATOM   138  O  O   . GLY   A 1 36  ? -16.246 -3.328  -12.294 1.00 40.43  ? 41  GLY   A O   1 
ATOM   139  N  N   . VAL   A 1 37  ? -15.587 -5.484  -12.659 1.00 37.78  ? 42  VAL   A N   1 
ATOM   140  C  CA  . VAL   A 1 37  ? -14.169 -5.178  -12.966 1.00 37.43  ? 42  VAL   A CA  1 
ATOM   141  C  C   . VAL   A 1 37  ? -14.054 -4.315  -14.243 1.00 41.29  ? 42  VAL   A C   1 
ATOM   142  O  O   . VAL   A 1 37  ? -13.087 -3.573  -14.396 1.00 40.04  ? 42  VAL   A O   1 
ATOM   143  C  CB  . VAL   A 1 37  ? -13.262 -6.446  -12.985 1.00 40.41  ? 42  VAL   A CB  1 
ATOM   144  C  CG1 . VAL   A 1 37  ? -13.460 -7.279  -14.249 1.00 39.99  ? 42  VAL   A CG1 1 
ATOM   145  C  CG2 . VAL   A 1 37  ? -11.790 -6.083  -12.808 1.00 40.06  ? 42  VAL   A CG2 1 
ATOM   146  N  N   . GLU   A 1 38  ? -15.090 -4.366  -15.119 1.00 39.55  ? 43  GLU   A N   1 
ATOM   147  C  CA  . GLU   A 1 38  ? -15.172 -3.544  -16.332 1.00 39.47  ? 43  GLU   A CA  1 
ATOM   148  C  C   . GLU   A 1 38  ? -15.254 -2.033  -16.007 1.00 42.77  ? 43  GLU   A C   1 
ATOM   149  O  O   . GLU   A 1 38  ? -15.003 -1.212  -16.883 1.00 43.25  ? 43  GLU   A O   1 
ATOM   150  C  CB  . GLU   A 1 38  ? -16.344 -3.996  -17.240 1.00 40.85  ? 43  GLU   A CB  1 
ATOM   151  C  CG  . GLU   A 1 38  ? -17.742 -3.764  -16.676 1.00 49.26  ? 43  GLU   A CG  1 
ATOM   152  C  CD  . GLU   A 1 38  ? -18.341 -4.868  -15.823 1.00 72.10  ? 43  GLU   A CD  1 
ATOM   153  O  OE1 . GLU   A 1 38  ? -17.579 -5.711  -15.294 1.00 61.08  ? 43  GLU   A OE1 1 
ATOM   154  O  OE2 . GLU   A 1 38  ? -19.584 -4.876  -15.669 1.00 66.33  ? 43  GLU   A OE2 1 
ATOM   155  N  N   . HIS   A 1 39  ? -15.619 -1.678  -14.765 1.00 39.99  ? 44  HIS   A N   1 
ATOM   156  C  CA  . HIS   A 1 39  ? -15.704 -0.294  -14.290 1.00 39.85  ? 44  HIS   A CA  1 
ATOM   157  C  C   . HIS   A 1 39  ? -14.382 0.216   -13.682 1.00 40.56  ? 44  HIS   A C   1 
ATOM   158  O  O   . HIS   A 1 39  ? -14.261 1.400   -13.362 1.00 37.59  ? 44  HIS   A O   1 
ATOM   159  C  CB  . HIS   A 1 39  ? -16.877 -0.121  -13.320 1.00 41.67  ? 44  HIS   A CB  1 
ATOM   160  C  CG  . HIS   A 1 39  ? -18.199 -0.501  -13.921 1.00 45.93  ? 44  HIS   A CG  1 
ATOM   161  N  ND1 . HIS   A 1 39  ? -18.689 0.135   -15.047 1.00 48.25  ? 44  HIS   A ND1 1 
ATOM   162  C  CD2 . HIS   A 1 39  ? -19.080 -1.453  -13.538 1.00 48.66  ? 44  HIS   A CD2 1 
ATOM   163  C  CE1 . HIS   A 1 39  ? -19.850 -0.444  -15.309 1.00 48.18  ? 44  HIS   A CE1 1 
ATOM   164  N  NE2 . HIS   A 1 39  ? -20.131 -1.401  -14.425 1.00 48.70  ? 44  HIS   A NE2 1 
ATOM   165  N  N   . GLY   A 1 40  ? -13.394 -0.679  -13.581 1.00 36.57  ? 45  GLY   A N   1 
ATOM   166  C  CA  . GLY   A 1 40  ? -12.057 -0.340  -13.108 1.00 35.23  ? 45  GLY   A CA  1 
ATOM   167  C  C   . GLY   A 1 40  ? -11.456 0.853   -13.838 1.00 37.72  ? 45  GLY   A C   1 
ATOM   168  O  O   . GLY   A 1 40  ? -11.048 1.816   -13.180 1.00 36.31  ? 45  GLY   A O   1 
ATOM   169  N  N   . PRO   A 1 41  ? -11.419 0.881   -15.203 1.00 35.33  ? 46  PRO   A N   1 
ATOM   170  C  CA  . PRO   A 1 41  ? -10.832 2.046   -15.879 1.00 34.80  ? 46  PRO   A CA  1 
ATOM   171  C  C   . PRO   A 1 41  ? -11.506 3.367   -15.503 1.00 38.43  ? 46  PRO   A C   1 
ATOM   172  O  O   . PRO   A 1 41  ? -10.801 4.337   -15.257 1.00 37.70  ? 46  PRO   A O   1 
ATOM   173  C  CB  . PRO   A 1 41  ? -10.977 1.705   -17.367 1.00 36.33  ? 46  PRO   A CB  1 
ATOM   174  C  CG  . PRO   A 1 41  ? -11.031 0.216   -17.396 1.00 40.98  ? 46  PRO   A CG  1 
ATOM   175  C  CD  . PRO   A 1 41  ? -11.835 -0.141  -16.188 1.00 36.78  ? 46  PRO   A CD  1 
ATOM   176  N  N   . ALA   A 1 42  ? -12.859 3.385   -15.403 1.00 36.61  ? 47  ALA   A N   1 
ATOM   177  C  CA  . ALA   A 1 42  ? -13.634 4.572   -14.999 1.00 37.05  ? 47  ALA   A CA  1 
ATOM   178  C  C   . ALA   A 1 42  ? -13.225 5.032   -13.583 1.00 38.61  ? 47  ALA   A C   1 
ATOM   179  O  O   . ALA   A 1 42  ? -12.894 6.204   -13.403 1.00 36.67  ? 47  ALA   A O   1 
ATOM   180  C  CB  . ALA   A 1 42  ? -15.136 4.270   -15.042 1.00 38.18  ? 47  ALA   A CB  1 
ATOM   181  N  N   . ALA   A 1 43  ? -13.195 4.088   -12.609 1.00 35.71  ? 48  ALA   A N   1 
ATOM   182  C  CA  . ALA   A 1 43  ? -12.804 4.335   -11.207 1.00 34.59  ? 48  ALA   A CA  1 
ATOM   183  C  C   . ALA   A 1 43  ? -11.413 4.951   -11.106 1.00 38.76  ? 48  ALA   A C   1 
ATOM   184  O  O   . ALA   A 1 43  ? -11.245 5.938   -10.381 1.00 39.30  ? 48  ALA   A O   1 
ATOM   185  C  CB  . ALA   A 1 43  ? -12.865 3.042   -10.400 1.00 35.50  ? 48  ALA   A CB  1 
ATOM   186  N  N   . ILE   A 1 44  ? -10.422 4.409   -11.859 1.00 33.51  ? 49  ILE   A N   1 
ATOM   187  C  CA  . ILE   A 1 44  ? -9.049  4.934   -11.847 1.00 31.94  ? 49  ILE   A CA  1 
ATOM   188  C  C   . ILE   A 1 44  ? -8.988  6.357   -12.436 1.00 36.86  ? 49  ILE   A C   1 
ATOM   189  O  O   . ILE   A 1 44  ? -8.313  7.220   -11.877 1.00 37.23  ? 49  ILE   A O   1 
ATOM   190  C  CB  . ILE   A 1 44  ? -8.029  3.955   -12.505 1.00 33.46  ? 49  ILE   A CB  1 
ATOM   191  C  CG1 . ILE   A 1 44  ? -8.034  2.584   -11.779 1.00 32.93  ? 49  ILE   A CG1 1 
ATOM   192  C  CG2 . ILE   A 1 44  ? -6.614  4.572   -12.586 1.00 34.31  ? 49  ILE   A CG2 1 
ATOM   193  C  CD1 . ILE   A 1 44  ? -7.357  1.460   -12.545 1.00 32.45  ? 49  ILE   A CD1 1 
ATOM   194  N  N   . ARG   A 1 45  ? -9.718  6.605   -13.544 1.00 35.56  ? 50  ARG   A N   1 
ATOM   195  C  CA  . ARG   A 1 45  ? -9.759  7.927   -14.195 1.00 35.21  ? 50  ARG   A CA  1 
ATOM   196  C  C   . ARG   A 1 45  ? -10.378 8.990   -13.276 1.00 38.94  ? 50  ARG   A C   1 
ATOM   197  O  O   . ARG   A 1 45  ? -9.857  10.102  -13.193 1.00 37.84  ? 50  ARG   A O   1 
ATOM   198  C  CB  . ARG   A 1 45  ? -10.545 7.853   -15.518 1.00 36.09  ? 50  ARG   A CB  1 
ATOM   199  C  CG  . ARG   A 1 45  ? -9.799  7.183   -16.659 1.00 41.82  ? 50  ARG   A CG  1 
ATOM   200  C  CD  . ARG   A 1 45  ? -10.684 7.156   -17.903 1.00 42.68  ? 50  ARG   A CD  1 
ATOM   201  N  NE  . ARG   A 1 45  ? -10.070 6.464   -19.041 1.00 42.74  ? 50  ARG   A NE  1 
ATOM   202  C  CZ  . ARG   A 1 45  ? -9.167  7.002   -19.853 1.00 55.04  ? 50  ARG   A CZ  1 
ATOM   203  N  NH1 . ARG   A 1 45  ? -8.728  8.238   -19.643 1.00 38.55  ? 50  ARG   A NH1 1 
ATOM   204  N  NH2 . ARG   A 1 45  ? -8.681  6.303   -20.872 1.00 43.90  ? 50  ARG   A NH2 1 
ATOM   205  N  N   . GLU   A 1 46  ? -11.483 8.629   -12.583 1.00 38.43  ? 51  GLU   A N   1 
ATOM   206  C  CA  . GLU   A 1 46  ? -12.222 9.474   -11.626 1.00 38.89  ? 51  GLU   A CA  1 
ATOM   207  C  C   . GLU   A 1 46  ? -11.373 9.787   -10.388 1.00 44.28  ? 51  GLU   A C   1 
ATOM   208  O  O   . GLU   A 1 46  ? -11.548 10.840  -9.761  1.00 44.67  ? 51  GLU   A O   1 
ATOM   209  C  CB  . GLU   A 1 46  ? -13.531 8.793   -11.222 1.00 40.60  ? 51  GLU   A CB  1 
ATOM   210  C  CG  . GLU   A 1 46  ? -14.618 8.924   -12.286 1.00 56.24  ? 51  GLU   A CG  1 
ATOM   211  C  CD  . GLU   A 1 46  ? -15.838 8.029   -12.165 1.00 80.62  ? 51  GLU   A CD  1 
ATOM   212  O  OE1 . GLU   A 1 46  ? -16.032 7.399   -11.099 1.00 72.97  ? 51  GLU   A OE1 1 
ATOM   213  O  OE2 . GLU   A 1 46  ? -16.616 7.972   -13.146 1.00 81.81  ? 51  GLU   A OE2 1 
ATOM   214  N  N   . ALA   A 1 47  ? -10.408 8.895   -10.070 1.00 38.68  ? 52  ALA   A N   1 
ATOM   215  C  CA  . ALA   A 1 47  ? -9.478  9.113   -8.966  1.00 38.33  ? 52  ALA   A CA  1 
ATOM   216  C  C   . ALA   A 1 47  ? -8.382  10.132  -9.346  1.00 41.69  ? 52  ALA   A C   1 
ATOM   217  O  O   . ALA   A 1 47  ? -7.533  10.466  -8.522  1.00 43.26  ? 52  ALA   A O   1 
ATOM   218  C  CB  . ALA   A 1 47  ? -8.878  7.792   -8.510  1.00 38.83  ? 52  ALA   A CB  1 
ATOM   219  N  N   . GLY   A 1 48  ? -8.435  10.644  -10.573 1.00 37.58  ? 53  GLY   A N   1 
ATOM   220  C  CA  . GLY   A 1 48  ? -7.547  11.706  -11.049 1.00 35.90  ? 53  GLY   A CA  1 
ATOM   221  C  C   . GLY   A 1 48  ? -6.259  11.302  -11.725 1.00 37.53  ? 53  GLY   A C   1 
ATOM   222  O  O   . GLY   A 1 48  ? -5.291  12.064  -11.676 1.00 36.39  ? 53  GLY   A O   1 
ATOM   223  N  N   . LEU   A 1 49  ? -6.247  10.126  -12.399 1.00 33.83  ? 54  LEU   A N   1 
ATOM   224  C  CA  . LEU   A 1 49  ? -5.051  9.615   -13.076 1.00 33.36  ? 54  LEU   A CA  1 
ATOM   225  C  C   . LEU   A 1 49  ? -4.362  10.630  -14.007 1.00 38.30  ? 54  LEU   A C   1 
ATOM   226  O  O   . LEU   A 1 49  ? -3.172  10.902  -13.820 1.00 36.30  ? 54  LEU   A O   1 
ATOM   227  C  CB  . LEU   A 1 49  ? -5.335  8.291   -13.829 1.00 33.11  ? 54  LEU   A CB  1 
ATOM   228  C  CG  . LEU   A 1 49  ? -4.121  7.696   -14.600 1.00 37.33  ? 54  LEU   A CG  1 
ATOM   229  C  CD1 . LEU   A 1 49  ? -3.009  7.261   -13.625 1.00 37.13  ? 54  LEU   A CD1 1 
ATOM   230  C  CD2 . LEU   A 1 49  ? -4.536  6.517   -15.454 1.00 38.61  ? 54  LEU   A CD2 1 
ATOM   231  N  N   . MET   A 1 50  ? -5.094  11.190  -14.999 1.00 36.83  ? 55  MET   A N   1 
ATOM   232  C  CA  . MET   A 1 50  ? -4.487  12.094  -15.998 1.00 36.89  ? 55  MET   A CA  1 
ATOM   233  C  C   . MET   A 1 50  ? -3.879  13.357  -15.391 1.00 39.71  ? 55  MET   A C   1 
ATOM   234  O  O   . MET   A 1 50  ? -2.749  13.717  -15.741 1.00 39.14  ? 55  MET   A O   1 
ATOM   235  C  CB  . MET   A 1 50  ? -5.454  12.428  -17.147 1.00 39.49  ? 55  MET   A CB  1 
ATOM   236  C  CG  . MET   A 1 50  ? -6.060  11.196  -17.825 1.00 43.06  ? 55  MET   A CG  1 
ATOM   237  S  SD  . MET   A 1 50  ? -4.827  9.968   -18.356 1.00 47.00  ? 55  MET   A SD  1 
ATOM   238  C  CE  . MET   A 1 50  ? -4.154  10.776  -19.824 1.00 43.91  ? 55  MET   A CE  1 
ATOM   239  N  N   . LYS   A 1 51  ? -4.581  13.977  -14.432 1.00 37.68  ? 56  LYS   A N   1 
ATOM   240  C  CA  . LYS   A 1 51  ? -4.099  15.167  -13.719 1.00 37.85  ? 56  LYS   A CA  1 
ATOM   241  C  C   . LYS   A 1 51  ? -2.764  14.887  -12.983 1.00 39.30  ? 56  LYS   A C   1 
ATOM   242  O  O   . LYS   A 1 51  ? -1.839  15.696  -13.055 1.00 39.38  ? 56  LYS   A O   1 
ATOM   243  C  CB  . LYS   A 1 51  ? -5.192  15.683  -12.755 1.00 41.60  ? 56  LYS   A CB  1 
ATOM   244  C  CG  . LYS   A 1 51  ? -4.864  17.005  -12.063 1.00 63.49  ? 56  LYS   A CG  1 
ATOM   245  C  CD  . LYS   A 1 51  ? -6.034  17.514  -11.223 1.00 77.47  ? 56  LYS   A CD  1 
ATOM   246  C  CE  . LYS   A 1 51  ? -5.782  18.906  -10.690 1.00 93.97  ? 56  LYS   A CE  1 
ATOM   247  N  NZ  . LYS   A 1 51  ? -7.029  19.543  -10.188 1.00 104.10 ? 56  LYS   A NZ  1 
ATOM   248  N  N   . ARG   A 1 52  ? -2.665  13.726  -12.304 1.00 35.56  ? 57  ARG   A N   1 
ATOM   249  C  CA  . ARG   A 1 52  ? -1.456  13.320  -11.594 1.00 34.32  ? 57  ARG   A CA  1 
ATOM   250  C  C   . ARG   A 1 52  ? -0.275  13.134  -12.540 1.00 36.23  ? 57  ARG   A C   1 
ATOM   251  O  O   . ARG   A 1 52  ? 0.817   13.626  -12.254 1.00 37.03  ? 57  ARG   A O   1 
ATOM   252  C  CB  . ARG   A 1 52  ? -1.708  12.034  -10.783 1.00 35.44  ? 57  ARG   A CB  1 
ATOM   253  C  CG  . ARG   A 1 52  ? -0.585  11.731  -9.809  1.00 42.63  ? 57  ARG   A CG  1 
ATOM   254  C  CD  . ARG   A 1 52  ? -0.677  12.534  -8.511  1.00 44.19  ? 57  ARG   A CD  1 
ATOM   255  N  NE  . ARG   A 1 52  ? -1.915  12.243  -7.794  1.00 45.22  ? 57  ARG   A NE  1 
ATOM   256  C  CZ  . ARG   A 1 52  ? -2.088  11.216  -6.969  1.00 53.30  ? 57  ARG   A CZ  1 
ATOM   257  N  NH1 . ARG   A 1 52  ? -3.254  11.030  -6.373  1.00 48.59  ? 57  ARG   A NH1 1 
ATOM   258  N  NH2 . ARG   A 1 52  ? -1.095  10.373  -6.729  1.00 39.77  ? 57  ARG   A NH2 1 
ATOM   259  N  N   . LEU   A 1 53  ? -0.482  12.418  -13.657 1.00 34.13  ? 58  LEU   A N   1 
ATOM   260  C  CA  . LEU   A 1 53  ? 0.584   12.205  -14.629 1.00 33.87  ? 58  LEU   A CA  1 
ATOM   261  C  C   . LEU   A 1 53  ? 1.012   13.537  -15.266 1.00 37.66  ? 58  LEU   A C   1 
ATOM   262  O  O   . LEU   A 1 53  ? 2.210   13.774  -15.405 1.00 35.08  ? 58  LEU   A O   1 
ATOM   263  C  CB  . LEU   A 1 53  ? 0.207   11.144  -15.677 1.00 33.90  ? 58  LEU   A CB  1 
ATOM   264  C  CG  . LEU   A 1 53  ? -0.116  9.731   -15.147 1.00 39.21  ? 58  LEU   A CG  1 
ATOM   265  C  CD1 . LEU   A 1 53  ? -0.801  8.883   -16.225 1.00 39.57  ? 58  LEU   A CD1 1 
ATOM   266  C  CD2 . LEU   A 1 53  ? 1.137   9.025   -14.614 1.00 42.91  ? 58  LEU   A CD2 1 
ATOM   267  N  N   . SER   A 1 54  ? 0.037   14.441  -15.551 1.00 38.59  ? 59  SER   A N   1 
ATOM   268  C  CA  . SER   A 1 54  ? 0.305   15.799  -16.070 1.00 39.29  ? 59  SER   A CA  1 
ATOM   269  C  C   . SER   A 1 54  ? 1.210   16.563  -15.095 1.00 43.40  ? 59  SER   A C   1 
ATOM   270  O  O   . SER   A 1 54  ? 2.232   17.121  -15.518 1.00 43.18  ? 59  SER   A O   1 
ATOM   271  C  CB  . SER   A 1 54  ? -0.995  16.579  -16.253 1.00 44.08  ? 59  SER   A CB  1 
ATOM   272  O  OG  . SER   A 1 54  ? -1.878  15.941  -17.159 1.00 56.93  ? 59  SER   A OG  1 
ATOM   273  N  N   . SER   A 1 55  ? 0.877   16.513  -13.776 1.00 40.21  ? 60  SER   A N   1 
ATOM   274  C  CA  . SER   A 1 55  ? 1.641   17.191  -12.726 1.00 39.87  ? 60  SER   A CA  1 
ATOM   275  C  C   . SER   A 1 55  ? 3.079   16.681  -12.588 1.00 42.04  ? 60  SER   A C   1 
ATOM   276  O  O   . SER   A 1 55  ? 3.915   17.417  -12.076 1.00 40.42  ? 60  SER   A O   1 
ATOM   277  C  CB  . SER   A 1 55  ? 0.898   17.169  -11.393 1.00 44.66  ? 60  SER   A CB  1 
ATOM   278  O  OG  . SER   A 1 55  ? 0.848   15.882  -10.800 1.00 55.16  ? 60  SER   A OG  1 
ATOM   279  N  N   . LEU   A 1 56  ? 3.390   15.452  -13.091 1.00 38.39  ? 61  LEU   A N   1 
ATOM   280  C  CA  . LEU   A 1 56  ? 4.757   14.911  -13.061 1.00 37.93  ? 61  LEU   A CA  1 
ATOM   281  C  C   . LEU   A 1 56  ? 5.554   15.255  -14.343 1.00 43.31  ? 61  LEU   A C   1 
ATOM   282  O  O   . LEU   A 1 56  ? 6.713   14.853  -14.488 1.00 43.03  ? 61  LEU   A O   1 
ATOM   283  C  CB  . LEU   A 1 56  ? 4.760   13.375  -12.808 1.00 37.51  ? 61  LEU   A CB  1 
ATOM   284  C  CG  . LEU   A 1 56  ? 4.142   12.884  -11.488 1.00 41.78  ? 61  LEU   A CG  1 
ATOM   285  C  CD1 . LEU   A 1 56  ? 3.797   11.396  -11.557 1.00 41.88  ? 61  LEU   A CD1 1 
ATOM   286  C  CD2 . LEU   A 1 56  ? 5.058   13.162  -10.295 1.00 41.72  ? 61  LEU   A CD2 1 
ATOM   287  N  N   . GLY   A 1 57  ? 4.932   16.017  -15.241 1.00 42.06  ? 62  GLY   A N   1 
ATOM   288  C  CA  . GLY   A 1 57  ? 5.550   16.440  -16.492 1.00 41.87  ? 62  GLY   A CA  1 
ATOM   289  C  C   . GLY   A 1 57  ? 5.428   15.454  -17.637 1.00 45.63  ? 62  GLY   A C   1 
ATOM   290  O  O   . GLY   A 1 57  ? 6.153   15.590  -18.625 1.00 46.05  ? 62  GLY   A O   1 
ATOM   291  N  N   . CYS   A 1 58  ? 4.489   14.482  -17.545 1.00 40.66  ? 63  CYS   A N   1 
ATOM   292  C  CA  . CYS   A 1 58  ? 4.286   13.488  -18.606 1.00 39.89  ? 63  CYS   A CA  1 
ATOM   293  C  C   . CYS   A 1 58  ? 3.614   14.087  -19.841 1.00 45.62  ? 63  CYS   A C   1 
ATOM   294  O  O   . CYS   A 1 58  ? 2.593   14.773  -19.713 1.00 45.15  ? 63  CYS   A O   1 
ATOM   295  C  CB  . CYS   A 1 58  ? 3.494   12.283  -18.106 1.00 39.37  ? 63  CYS   A CB  1 
ATOM   296  S  SG  . CYS   A 1 58  ? 4.300   11.351  -16.782 1.00 42.21  ? 63  CYS   A SG  1 
ATOM   297  N  N   . HIS   A 1 59  ? 4.142   13.753  -21.037 1.00 44.21  ? 64  HIS   A N   1 
ATOM   298  C  CA  . HIS   A 1 59  ? 3.540   14.122  -22.321 1.00 44.79  ? 64  HIS   A CA  1 
ATOM   299  C  C   . HIS   A 1 59  ? 2.540   12.996  -22.545 1.00 45.21  ? 64  HIS   A C   1 
ATOM   300  O  O   . HIS   A 1 59  ? 2.943   11.835  -22.677 1.00 45.05  ? 64  HIS   A O   1 
ATOM   301  C  CB  . HIS   A 1 59  ? 4.605   14.194  -23.433 1.00 47.44  ? 64  HIS   A CB  1 
ATOM   302  C  CG  . HIS   A 1 59  ? 4.034   14.275  -24.820 1.00 52.54  ? 64  HIS   A CG  1 
ATOM   303  N  ND1 . HIS   A 1 59  ? 3.198   15.316  -25.203 1.00 55.05  ? 64  HIS   A ND1 1 
ATOM   304  C  CD2 . HIS   A 1 59  ? 4.205   13.441  -25.877 1.00 55.31  ? 64  HIS   A CD2 1 
ATOM   305  C  CE1 . HIS   A 1 59  ? 2.876   15.071  -26.464 1.00 54.93  ? 64  HIS   A CE1 1 
ATOM   306  N  NE2 . HIS   A 1 59  ? 3.460   13.954  -26.913 1.00 55.18  ? 64  HIS   A NE2 1 
ATOM   307  N  N   . LEU   A 1 60  ? 1.247   13.301  -22.445 1.00 39.66  ? 65  LEU   A N   1 
ATOM   308  C  CA  . LEU   A 1 60  ? 0.223   12.262  -22.492 1.00 39.41  ? 65  LEU   A CA  1 
ATOM   309  C  C   . LEU   A 1 60  ? -0.510  12.100  -23.807 1.00 44.30  ? 65  LEU   A C   1 
ATOM   310  O  O   . LEU   A 1 60  ? -0.644  13.055  -24.573 1.00 45.41  ? 65  LEU   A O   1 
ATOM   311  C  CB  . LEU   A 1 60  ? -0.803  12.471  -21.369 1.00 39.24  ? 65  LEU   A CB  1 
ATOM   312  C  CG  . LEU   A 1 60  ? -0.287  12.293  -19.930 1.00 43.97  ? 65  LEU   A CG  1 
ATOM   313  C  CD1 . LEU   A 1 60  ? -1.052  13.167  -18.980 1.00 45.17  ? 65  LEU   A CD1 1 
ATOM   314  C  CD2 . LEU   A 1 60  ? -0.379  10.854  -19.489 1.00 43.57  ? 65  LEU   A CD2 1 
ATOM   315  N  N   . LYS   A 1 61  ? -1.013  10.872  -24.040 1.00 39.34  ? 66  LYS   A N   1 
ATOM   316  C  CA  . LYS   A 1 61  ? -1.881  10.500  -25.148 1.00 38.41  ? 66  LYS   A CA  1 
ATOM   317  C  C   . LYS   A 1 61  ? -2.956  9.574   -24.597 1.00 41.33  ? 66  LYS   A C   1 
ATOM   318  O  O   . LYS   A 1 61  ? -2.656  8.484   -24.105 1.00 40.21  ? 66  LYS   A O   1 
ATOM   319  C  CB  . LYS   A 1 61  ? -1.113  9.879   -26.337 1.00 41.30  ? 66  LYS   A CB  1 
ATOM   320  C  CG  . LYS   A 1 61  ? -2.014  9.641   -27.552 1.00 49.83  ? 66  LYS   A CG  1 
ATOM   321  C  CD  . LYS   A 1 61  ? -1.256  9.268   -28.813 1.00 55.55  ? 66  LYS   A CD  1 
ATOM   322  C  CE  . LYS   A 1 61  ? -2.210  9.031   -29.967 1.00 69.65  ? 66  LYS   A CE  1 
ATOM   323  N  NZ  . LYS   A 1 61  ? -1.512  8.499   -31.169 1.00 80.21  ? 66  LYS   A NZ  1 
ATOM   324  N  N   . ASP   A 1 62  ? -4.200  10.028  -24.617 1.00 37.67  ? 67  ASP   A N   1 
ATOM   325  C  CA  . ASP   A 1 62  ? -5.297  9.211   -24.128 1.00 37.99  ? 67  ASP   A CA  1 
ATOM   326  C  C   . ASP   A 1 62  ? -5.970  8.494   -25.307 1.00 43.53  ? 67  ASP   A C   1 
ATOM   327  O  O   . ASP   A 1 62  ? -6.542  9.149   -26.183 1.00 44.21  ? 67  ASP   A O   1 
ATOM   328  C  CB  . ASP   A 1 62  ? -6.290  10.081  -23.336 1.00 39.26  ? 67  ASP   A CB  1 
ATOM   329  C  CG  . ASP   A 1 62  ? -7.248  9.358   -22.409 1.00 45.59  ? 67  ASP   A CG  1 
ATOM   330  O  OD1 . ASP   A 1 62  ? -7.470  8.139   -22.603 1.00 46.09  ? 67  ASP   A OD1 1 
ATOM   331  O  OD2 . ASP   A 1 62  ? -7.809  10.016  -21.518 1.00 48.90  ? 67  ASP   A OD2 1 
ATOM   332  N  N   . PHE   A 1 63  ? -5.901  7.149   -25.332 1.00 39.71  ? 68  PHE   A N   1 
ATOM   333  C  CA  . PHE   A 1 63  ? -6.543  6.345   -26.390 1.00 39.03  ? 68  PHE   A CA  1 
ATOM   334  C  C   . PHE   A 1 63  ? -8.020  6.059   -26.048 1.00 42.38  ? 68  PHE   A C   1 
ATOM   335  O  O   . PHE   A 1 63  ? -8.730  5.434   -26.842 1.00 42.70  ? 68  PHE   A O   1 
ATOM   336  C  CB  . PHE   A 1 63  ? -5.773  5.024   -26.622 1.00 40.34  ? 68  PHE   A CB  1 
ATOM   337  C  CG  . PHE   A 1 63  ? -4.478  5.158   -27.386 1.00 40.98  ? 68  PHE   A CG  1 
ATOM   338  C  CD1 . PHE   A 1 63  ? -3.330  5.636   -26.766 1.00 42.63  ? 68  PHE   A CD1 1 
ATOM   339  C  CD2 . PHE   A 1 63  ? -4.397  4.774   -28.720 1.00 42.57  ? 68  PHE   A CD2 1 
ATOM   340  C  CE1 . PHE   A 1 63  ? -2.134  5.766   -27.478 1.00 43.46  ? 68  PHE   A CE1 1 
ATOM   341  C  CE2 . PHE   A 1 63  ? -3.195  4.885   -29.424 1.00 44.78  ? 68  PHE   A CE2 1 
ATOM   342  C  CZ  . PHE   A 1 63  ? -2.069  5.369   -28.795 1.00 42.82  ? 68  PHE   A CZ  1 
ATOM   343  N  N   . GLY   A 1 64  ? -8.450  6.510   -24.866 1.00 37.87  ? 69  GLY   A N   1 
ATOM   344  C  CA  . GLY   A 1 64  ? -9.799  6.329   -24.353 1.00 37.71  ? 69  GLY   A CA  1 
ATOM   345  C  C   . GLY   A 1 64  ? -10.008 4.931   -23.820 1.00 43.81  ? 69  GLY   A C   1 
ATOM   346  O  O   . GLY   A 1 64  ? -9.036  4.206   -23.562 1.00 41.34  ? 69  GLY   A O   1 
ATOM   347  N  N   . ASP   A 1 65  ? -11.279 4.555   -23.641 1.00 42.82  ? 70  ASP   A N   1 
ATOM   348  C  CA  . ASP   A 1 65  ? -11.680 3.235   -23.160 1.00 43.78  ? 70  ASP   A CA  1 
ATOM   349  C  C   . ASP   A 1 65  ? -12.200 2.432   -24.342 1.00 49.14  ? 70  ASP   A C   1 
ATOM   350  O  O   . ASP   A 1 65  ? -13.181 2.832   -24.986 1.00 49.73  ? 70  ASP   A O   1 
ATOM   351  C  CB  . ASP   A 1 65  ? -12.732 3.350   -22.039 1.00 45.50  ? 70  ASP   A CB  1 
ATOM   352  C  CG  . ASP   A 1 65  ? -12.269 4.093   -20.797 1.00 56.08  ? 70  ASP   A CG  1 
ATOM   353  O  OD1 . ASP   A 1 65  ? -11.040 4.296   -20.645 1.00 53.62  ? 70  ASP   A OD1 1 
ATOM   354  O  OD2 . ASP   A 1 65  ? -13.134 4.460   -19.968 1.00 65.89  ? 70  ASP   A OD2 1 
ATOM   355  N  N   . LEU   A 1 66  ? -11.515 1.319   -24.652 1.00 45.55  ? 71  LEU   A N   1 
ATOM   356  C  CA  . LEU   A 1 66  ? -11.831 0.458   -25.793 1.00 45.50  ? 71  LEU   A CA  1 
ATOM   357  C  C   . LEU   A 1 66  ? -13.179 -0.223  -25.705 1.00 51.00  ? 71  LEU   A C   1 
ATOM   358  O  O   . LEU   A 1 66  ? -13.599 -0.630  -24.623 1.00 51.08  ? 71  LEU   A O   1 
ATOM   359  C  CB  . LEU   A 1 66  ? -10.724 -0.586  -26.023 1.00 45.30  ? 71  LEU   A CB  1 
ATOM   360  C  CG  . LEU   A 1 66  ? -9.304  -0.053  -26.261 1.00 50.00  ? 71  LEU   A CG  1 
ATOM   361  C  CD1 . LEU   A 1 66  ? -8.326  -1.188  -26.356 1.00 50.20  ? 71  LEU   A CD1 1 
ATOM   362  C  CD2 . LEU   A 1 66  ? -9.225  0.835   -27.514 1.00 52.41  ? 71  LEU   A CD2 1 
ATOM   363  N  N   . SER   A 1 67  ? -13.861 -0.340  -26.853 1.00 48.47  ? 72  SER   A N   1 
ATOM   364  C  CA  . SER   A 1 67  ? -15.152 -1.008  -26.964 1.00 49.09  ? 72  SER   A CA  1 
ATOM   365  C  C   . SER   A 1 67  ? -14.875 -2.348  -27.647 1.00 54.23  ? 72  SER   A C   1 
ATOM   366  O  O   . SER   A 1 67  ? -14.750 -2.420  -28.876 1.00 54.09  ? 72  SER   A O   1 
ATOM   367  C  CB  . SER   A 1 67  ? -16.133 -0.156  -27.770 1.00 53.69  ? 72  SER   A CB  1 
ATOM   368  O  OG  . SER   A 1 67  ? -17.368 -0.833  -27.941 1.00 67.39  ? 72  SER   A OG  1 
ATOM   369  N  N   . PHE   A 1 68  ? -14.699 -3.393  -26.835 1.00 51.68  ? 73  PHE   A N   1 
ATOM   370  C  CA  . PHE   A 1 68  ? -14.364 -4.723  -27.331 1.00 52.23  ? 73  PHE   A CA  1 
ATOM   371  C  C   . PHE   A 1 68  ? -15.506 -5.349  -28.120 1.00 58.44  ? 73  PHE   A C   1 
ATOM   372  O  O   . PHE   A 1 68  ? -16.658 -5.265  -27.691 1.00 58.42  ? 73  PHE   A O   1 
ATOM   373  C  CB  . PHE   A 1 68  ? -13.865 -5.636  -26.191 1.00 53.56  ? 73  PHE   A CB  1 
ATOM   374  C  CG  . PHE   A 1 68  ? -12.591 -5.147  -25.536 1.00 54.55  ? 73  PHE   A CG  1 
ATOM   375  C  CD1 . PHE   A 1 68  ? -11.393 -5.106  -26.245 1.00 57.32  ? 73  PHE   A CD1 1 
ATOM   376  C  CD2 . PHE   A 1 68  ? -12.592 -4.712  -24.216 1.00 56.42  ? 73  PHE   A CD2 1 
ATOM   377  C  CE1 . PHE   A 1 68  ? -10.217 -4.650  -25.641 1.00 58.29  ? 73  PHE   A CE1 1 
ATOM   378  C  CE2 . PHE   A 1 68  ? -11.416 -4.253  -23.613 1.00 59.02  ? 73  PHE   A CE2 1 
ATOM   379  C  CZ  . PHE   A 1 68  ? -10.238 -4.223  -24.329 1.00 57.10  ? 73  PHE   A CZ  1 
ATOM   380  N  N   . THR   A 1 69  ? -15.181 -5.926  -29.302 1.00 56.72  ? 74  THR   A N   1 
ATOM   381  C  CA  . THR   A 1 69  ? -16.139 -6.591  -30.193 1.00 57.26  ? 74  THR   A CA  1 
ATOM   382  C  C   . THR   A 1 69  ? -16.711 -7.801  -29.435 1.00 64.33  ? 74  THR   A C   1 
ATOM   383  O  O   . THR   A 1 69  ? -15.944 -8.694  -29.050 1.00 64.19  ? 74  THR   A O   1 
ATOM   384  C  CB  . THR   A 1 69  ? -15.473 -7.002  -31.532 1.00 62.17  ? 74  THR   A CB  1 
ATOM   385  O  OG1 . THR   A 1 69  ? -14.739 -5.905  -32.078 1.00 59.02  ? 74  THR   A OG1 1 
ATOM   386  C  CG2 . THR   A 1 69  ? -16.474 -7.533  -32.564 1.00 60.37  ? 74  THR   A CG2 1 
ATOM   387  N  N   . PRO   A 1 70  ? -18.029 -7.816  -29.139 1.00 62.79  ? 75  PRO   A N   1 
ATOM   388  C  CA  . PRO   A 1 70  ? -18.582 -8.953  -28.391 1.00 63.38  ? 75  PRO   A CA  1 
ATOM   389  C  C   . PRO   A 1 70  ? -18.776 -10.198 -29.251 1.00 68.98  ? 75  PRO   A C   1 
ATOM   390  O  O   . PRO   A 1 70  ? -18.944 -10.096 -30.467 1.00 68.29  ? 75  PRO   A O   1 
ATOM   391  C  CB  . PRO   A 1 70  ? -19.905 -8.412  -27.848 1.00 65.17  ? 75  PRO   A CB  1 
ATOM   392  C  CG  . PRO   A 1 70  ? -20.313 -7.363  -28.824 1.00 69.35  ? 75  PRO   A CG  1 
ATOM   393  C  CD  . PRO   A 1 70  ? -19.077 -6.833  -29.493 1.00 64.51  ? 75  PRO   A CD  1 
ATOM   394  N  N   . VAL   A 1 71  ? -18.720 -11.376 -28.613 1.00 67.28  ? 76  VAL   A N   1 
ATOM   395  C  CA  . VAL   A 1 71  ? -18.940 -12.665 -29.271 1.00 67.76  ? 76  VAL   A CA  1 
ATOM   396  C  C   . VAL   A 1 71  ? -20.256 -13.205 -28.677 1.00 73.36  ? 76  VAL   A C   1 
ATOM   397  O  O   . VAL   A 1 71  ? -20.308 -13.451 -27.467 1.00 73.47  ? 76  VAL   A O   1 
ATOM   398  C  CB  . VAL   A 1 71  ? -17.752 -13.661 -29.143 1.00 71.39  ? 76  VAL   A CB  1 
ATOM   399  C  CG1 . VAL   A 1 71  ? -17.960 -14.878 -30.042 1.00 71.14  ? 76  VAL   A CG1 1 
ATOM   400  C  CG2 . VAL   A 1 71  ? -16.420 -12.986 -29.468 1.00 71.21  ? 76  VAL   A CG2 1 
ATOM   401  N  N   . PRO   A 1 72  ? -21.348 -13.300 -29.480 1.00 70.41  ? 77  PRO   A N   1 
ATOM   402  C  CA  . PRO   A 1 72  ? -22.641 -13.742 -28.921 1.00 70.33  ? 77  PRO   A CA  1 
ATOM   403  C  C   . PRO   A 1 72  ? -22.670 -15.196 -28.449 1.00 73.98  ? 77  PRO   A C   1 
ATOM   404  O  O   . PRO   A 1 72  ? -23.098 -15.454 -27.321 1.00 73.56  ? 77  PRO   A O   1 
ATOM   405  C  CB  . PRO   A 1 72  ? -23.645 -13.472 -30.056 1.00 72.19  ? 77  PRO   A CB  1 
ATOM   406  C  CG  . PRO   A 1 72  ? -22.904 -12.631 -31.062 1.00 76.71  ? 77  PRO   A CG  1 
ATOM   407  C  CD  . PRO   A 1 72  ? -21.467 -12.999 -30.920 1.00 72.14  ? 77  PRO   A CD  1 
ATOM   408  N  N   . LYS   A 1 73  ? -22.217 -16.136 -29.302 1.00 70.12  ? 78  LYS   A N   1 
ATOM   409  C  CA  . LYS   A 1 73  ? -22.172 -17.560 -28.968 1.00 69.59  ? 78  LYS   A CA  1 
ATOM   410  C  C   . LYS   A 1 73  ? -20.757 -17.878 -28.484 1.00 70.65  ? 78  LYS   A C   1 
ATOM   411  O  O   . LYS   A 1 73  ? -19.814 -17.926 -29.282 1.00 70.15  ? 78  LYS   A O   1 
ATOM   412  C  CB  . LYS   A 1 73  ? -22.592 -18.435 -30.166 1.00 72.83  ? 78  LYS   A CB  1 
ATOM   413  C  CG  . LYS   A 1 73  ? -22.872 -19.890 -29.792 1.00 92.73  ? 78  LYS   A CG  1 
ATOM   414  C  CD  . LYS   A 1 73  ? -23.172 -20.751 -31.019 1.00 104.38 ? 78  LYS   A CD  1 
ATOM   415  C  CE  . LYS   A 1 73  ? -23.351 -22.214 -30.680 1.00 114.34 ? 78  LYS   A CE  1 
ATOM   416  N  NZ  . LYS   A 1 73  ? -24.643 -22.482 -29.991 1.00 122.46 ? 78  LYS   A NZ  1 
ATOM   417  N  N   . ASP   A 1 74  ? -20.612 -18.029 -27.155 1.00 64.72  ? 79  ASP   A N   1 
ATOM   418  C  CA  . ASP   A 1 74  ? -19.335 -18.280 -26.492 1.00 63.06  ? 79  ASP   A CA  1 
ATOM   419  C  C   . ASP   A 1 74  ? -19.547 -18.975 -25.134 1.00 65.70  ? 79  ASP   A C   1 
ATOM   420  O  O   . ASP   A 1 74  ? -19.245 -18.414 -24.072 1.00 65.04  ? 79  ASP   A O   1 
ATOM   421  C  CB  . ASP   A 1 74  ? -18.553 -16.955 -26.346 1.00 63.59  ? 79  ASP   A CB  1 
ATOM   422  C  CG  . ASP   A 1 74  ? -17.106 -17.089 -25.915 1.00 60.68  ? 79  ASP   A CG  1 
ATOM   423  O  OD1 . ASP   A 1 74  ? -16.499 -18.156 -26.172 1.00 57.97  ? 79  ASP   A OD1 1 
ATOM   424  O  OD2 . ASP   A 1 74  ? -16.573 -16.123 -25.360 1.00 60.86  ? 79  ASP   A OD2 1 
ATOM   425  N  N   . ASP   A 1 75  ? -20.089 -20.199 -25.171 1.00 61.27  ? 80  ASP   A N   1 
ATOM   426  C  CA  . ASP   A 1 75  ? -20.313 -20.935 -23.930 1.00 60.38  ? 80  ASP   A CA  1 
ATOM   427  C  C   . ASP   A 1 75  ? -19.127 -21.844 -23.593 1.00 59.11  ? 80  ASP   A C   1 
ATOM   428  O  O   . ASP   A 1 75  ? -18.173 -21.947 -24.376 1.00 57.88  ? 80  ASP   A O   1 
ATOM   429  C  CB  . ASP   A 1 75  ? -21.665 -21.683 -23.921 1.00 63.03  ? 80  ASP   A CB  1 
ATOM   430  C  CG  . ASP   A 1 75  ? -22.241 -21.869 -22.519 1.00 81.01  ? 80  ASP   A CG  1 
ATOM   431  O  OD1 . ASP   A 1 75  ? -22.460 -20.846 -21.821 1.00 82.81  ? 80  ASP   A OD1 1 
ATOM   432  O  OD2 . ASP   A 1 75  ? -22.445 -23.037 -22.110 1.00 88.51  ? 80  ASP   A OD2 1 
ATOM   433  N  N   . LEU   A 1 76  ? -19.176 -22.436 -22.387 1.00 52.77  ? 81  LEU   A N   1 
ATOM   434  C  CA  . LEU   A 1 76  ? -18.198 -23.330 -21.775 1.00 51.34  ? 81  LEU   A CA  1 
ATOM   435  C  C   . LEU   A 1 76  ? -17.547 -24.286 -22.765 1.00 49.40  ? 81  LEU   A C   1 
ATOM   436  O  O   . LEU   A 1 76  ? -18.245 -24.973 -23.523 1.00 48.51  ? 81  LEU   A O   1 
ATOM   437  C  CB  . LEU   A 1 76  ? -18.877 -24.091 -20.623 1.00 51.90  ? 81  LEU   A CB  1 
ATOM   438  C  CG  . LEU   A 1 76  ? -18.011 -24.554 -19.451 1.00 57.27  ? 81  LEU   A CG  1 
ATOM   439  C  CD1 . LEU   A 1 76  ? -17.327 -23.380 -18.760 1.00 57.35  ? 81  LEU   A CD1 1 
ATOM   440  C  CD2 . LEU   A 1 76  ? -18.872 -25.266 -18.421 1.00 60.87  ? 81  LEU   A CD2 1 
ATOM   441  N  N   . TYR   A 1 77  ? -16.201 -24.270 -22.800 1.00 41.46  ? 82  TYR   A N   1 
ATOM   442  C  CA  . TYR   A 1 77  ? -15.406 -25.097 -23.698 1.00 39.14  ? 82  TYR   A CA  1 
ATOM   443  C  C   . TYR   A 1 77  ? -14.828 -26.278 -22.925 1.00 42.65  ? 82  TYR   A C   1 
ATOM   444  O  O   . TYR   A 1 77  ? -14.162 -26.085 -21.904 1.00 41.20  ? 82  TYR   A O   1 
ATOM   445  C  CB  . TYR   A 1 77  ? -14.320 -24.261 -24.369 1.00 38.65  ? 82  TYR   A CB  1 
ATOM   446  C  CG  . TYR   A 1 77  ? -13.492 -24.999 -25.399 1.00 39.35  ? 82  TYR   A CG  1 
ATOM   447  C  CD1 . TYR   A 1 77  ? -13.980 -25.221 -26.685 1.00 41.23  ? 82  TYR   A CD1 1 
ATOM   448  C  CD2 . TYR   A 1 77  ? -12.191 -25.399 -25.117 1.00 39.60  ? 82  TYR   A CD2 1 
ATOM   449  C  CE1 . TYR   A 1 77  ? -13.201 -25.850 -27.656 1.00 41.90  ? 82  TYR   A CE1 1 
ATOM   450  C  CE2 . TYR   A 1 77  ? -11.398 -26.019 -26.083 1.00 40.37  ? 82  TYR   A CE2 1 
ATOM   451  C  CZ  . TYR   A 1 77  ? -11.908 -26.241 -27.353 1.00 46.22  ? 82  TYR   A CZ  1 
ATOM   452  O  OH  . TYR   A 1 77  ? -11.141 -26.869 -28.304 1.00 48.20  ? 82  TYR   A OH  1 
ATOM   453  N  N   . ASN   A 1 78  ? -15.116 -27.503 -23.402 1.00 39.79  ? 83  ASN   A N   1 
ATOM   454  C  CA  . ASN   A 1 78  ? -14.712 -28.773 -22.766 1.00 39.55  ? 83  ASN   A CA  1 
ATOM   455  C  C   . ASN   A 1 78  ? -15.165 -28.859 -21.301 1.00 41.70  ? 83  ASN   A C   1 
ATOM   456  O  O   . ASN   A 1 78  ? -14.444 -29.398 -20.450 1.00 41.25  ? 83  ASN   A O   1 
ATOM   457  C  CB  . ASN   A 1 78  ? -13.213 -29.053 -22.931 1.00 39.69  ? 83  ASN   A CB  1 
ATOM   458  C  CG  . ASN   A 1 78  ? -12.860 -29.534 -24.306 1.00 50.67  ? 83  ASN   A CG  1 
ATOM   459  O  OD1 . ASN   A 1 78  ? -13.616 -30.281 -24.944 1.00 44.28  ? 83  ASN   A OD1 1 
ATOM   460  N  ND2 . ASN   A 1 78  ? -11.697 -29.132 -24.783 1.00 40.55  ? 83  ASN   A ND2 1 
ATOM   461  N  N   . ASN   A 1 79  ? -16.353 -28.289 -21.012 1.00 37.65  ? 84  ASN   A N   1 
ATOM   462  C  CA  . ASN   A 1 79  ? -16.994 -28.260 -19.688 1.00 37.57  ? 84  ASN   A CA  1 
ATOM   463  C  C   . ASN   A 1 79  ? -16.052 -27.632 -18.627 1.00 42.12  ? 84  ASN   A C   1 
ATOM   464  O  O   . ASN   A 1 79  ? -16.097 -27.991 -17.447 1.00 40.53  ? 84  ASN   A O   1 
ATOM   465  C  CB  . ASN   A 1 79  ? -17.478 -29.688 -19.301 1.00 38.20  ? 84  ASN   A CB  1 
ATOM   466  C  CG  . ASN   A 1 79  ? -18.406 -29.774 -18.125 1.00 63.84  ? 84  ASN   A CG  1 
ATOM   467  O  OD1 . ASN   A 1 79  ? -19.447 -29.116 -18.066 1.00 60.97  ? 84  ASN   A OD1 1 
ATOM   468  N  ND2 . ASN   A 1 79  ? -18.069 -30.642 -17.182 1.00 59.37  ? 84  ASN   A ND2 1 
ATOM   469  N  N   . LEU   A 1 80  ? -15.189 -26.688 -19.068 1.00 39.15  ? 85  LEU   A N   1 
ATOM   470  C  CA  . LEU   A 1 80  ? -14.224 -26.040 -18.188 1.00 38.12  ? 85  LEU   A CA  1 
ATOM   471  C  C   . LEU   A 1 80  ? -13.916 -24.584 -18.532 1.00 40.37  ? 85  LEU   A C   1 
ATOM   472  O  O   . LEU   A 1 80  ? -14.126 -23.728 -17.676 1.00 39.21  ? 85  LEU   A O   1 
ATOM   473  C  CB  . LEU   A 1 80  ? -12.921 -26.862 -18.119 1.00 38.12  ? 85  LEU   A CB  1 
ATOM   474  C  CG  . LEU   A 1 80  ? -11.828 -26.400 -17.145 1.00 42.52  ? 85  LEU   A CG  1 
ATOM   475  C  CD1 . LEU   A 1 80  ? -12.291 -26.506 -15.682 1.00 42.45  ? 85  LEU   A CD1 1 
ATOM   476  C  CD2 . LEU   A 1 80  ? -10.543 -27.194 -17.360 1.00 43.64  ? 85  LEU   A CD2 1 
ATOM   477  N  N   . ILE   A 1 81  ? -13.363 -24.312 -19.732 1.00 36.76  ? 86  ILE   A N   1 
ATOM   478  C  CA  . ILE   A 1 81  ? -12.918 -22.957 -20.114 1.00 35.68  ? 86  ILE   A CA  1 
ATOM   479  C  C   . ILE   A 1 81  ? -14.106 -22.022 -20.359 1.00 40.07  ? 86  ILE   A C   1 
ATOM   480  O  O   . ILE   A 1 81  ? -14.966 -22.309 -21.188 1.00 39.68  ? 86  ILE   A O   1 
ATOM   481  C  CB  . ILE   A 1 81  ? -11.888 -22.967 -21.286 1.00 38.44  ? 86  ILE   A CB  1 
ATOM   482  C  CG1 . ILE   A 1 81  ? -10.809 -24.068 -21.123 1.00 38.29  ? 86  ILE   A CG1 1 
ATOM   483  C  CG2 . ILE   A 1 81  ? -11.247 -21.585 -21.496 1.00 39.33  ? 86  ILE   A CG2 1 
ATOM   484  C  CD1 . ILE   A 1 81  ? -9.929  -24.052 -19.783 1.00 40.27  ? 86  ILE   A CD1 1 
ATOM   485  N  N   . VAL   A 1 82  ? -14.123 -20.885 -19.624 1.00 36.09  ? 87  VAL   A N   1 
ATOM   486  C  CA  . VAL   A 1 82  ? -15.165 -19.852 -19.653 1.00 35.80  ? 87  VAL   A CA  1 
ATOM   487  C  C   . VAL   A 1 82  ? -14.813 -18.749 -20.649 1.00 37.35  ? 87  VAL   A C   1 
ATOM   488  O  O   . VAL   A 1 82  ? -13.703 -18.219 -20.633 1.00 35.18  ? 87  VAL   A O   1 
ATOM   489  C  CB  . VAL   A 1 82  ? -15.467 -19.276 -18.243 1.00 40.40  ? 87  VAL   A CB  1 
ATOM   490  C  CG1 . VAL   A 1 82  ? -16.678 -18.342 -18.269 1.00 40.38  ? 87  VAL   A CG1 1 
ATOM   491  C  CG2 . VAL   A 1 82  ? -15.671 -20.387 -17.212 1.00 40.80  ? 87  VAL   A CG2 1 
ATOM   492  N  N   . ASN   A 1 83  ? -15.771 -18.428 -21.539 1.00 36.08  ? 88  ASN   A N   1 
ATOM   493  C  CA  . ASN   A 1 83  ? -15.676 -17.395 -22.580 1.00 36.56  ? 88  ASN   A CA  1 
ATOM   494  C  C   . ASN   A 1 83  ? -14.327 -17.359 -23.365 1.00 39.43  ? 88  ASN   A C   1 
ATOM   495  O  O   . ASN   A 1 83  ? -13.738 -16.278 -23.472 1.00 40.20  ? 88  ASN   A O   1 
ATOM   496  C  CB  . ASN   A 1 83  ? -15.991 -16.020 -21.972 1.00 39.33  ? 88  ASN   A CB  1 
ATOM   497  C  CG  . ASN   A 1 83  ? -17.295 -15.970 -21.215 1.00 65.26  ? 88  ASN   A CG  1 
ATOM   498  O  OD1 . ASN   A 1 83  ? -18.328 -16.483 -21.656 1.00 66.24  ? 88  ASN   A OD1 1 
ATOM   499  N  ND2 . ASN   A 1 83  ? -17.269 -15.371 -20.041 1.00 55.79  ? 88  ASN   A ND2 1 
ATOM   500  N  N   . PRO   A 1 84  ? -13.813 -18.486 -23.931 1.00 35.62  ? 89  PRO   A N   1 
ATOM   501  C  CA  . PRO   A 1 84  ? -12.525 -18.416 -24.647 1.00 35.27  ? 89  PRO   A CA  1 
ATOM   502  C  C   . PRO   A 1 84  ? -12.538 -17.485 -25.862 1.00 40.17  ? 89  PRO   A C   1 
ATOM   503  O  O   . PRO   A 1 84  ? -11.612 -16.681 -26.018 1.00 38.63  ? 89  PRO   A O   1 
ATOM   504  C  CB  . PRO   A 1 84  ? -12.246 -19.876 -25.031 1.00 36.93  ? 89  PRO   A CB  1 
ATOM   505  C  CG  . PRO   A 1 84  ? -13.596 -20.519 -25.046 1.00 41.02  ? 89  PRO   A CG  1 
ATOM   506  C  CD  . PRO   A 1 84  ? -14.362 -19.860 -23.961 1.00 36.53  ? 89  PRO   A CD  1 
ATOM   507  N  N   . ARG   A 1 85  ? -13.599 -17.560 -26.699 1.00 37.81  ? 90  ARG   A N   1 
ATOM   508  C  CA  . ARG   A 1 85  ? -13.715 -16.706 -27.894 1.00 38.15  ? 90  ARG   A CA  1 
ATOM   509  C  C   . ARG   A 1 85  ? -13.686 -15.203 -27.571 1.00 41.80  ? 90  ARG   A C   1 
ATOM   510  O  O   . ARG   A 1 85  ? -12.928 -14.476 -28.217 1.00 42.93  ? 90  ARG   A O   1 
ATOM   511  C  CB  . ARG   A 1 85  ? -14.947 -17.077 -28.747 1.00 39.66  ? 90  ARG   A CB  1 
ATOM   512  C  CG  . ARG   A 1 85  ? -14.830 -18.437 -29.423 1.00 52.78  ? 90  ARG   A CG  1 
ATOM   513  C  CD  . ARG   A 1 85  ? -16.168 -18.931 -29.943 1.00 68.56  ? 90  ARG   A CD  1 
ATOM   514  N  NE  . ARG   A 1 85  ? -16.024 -20.142 -30.757 1.00 83.46  ? 90  ARG   A NE  1 
ATOM   515  C  CZ  . ARG   A 1 85  ? -16.180 -21.384 -30.303 1.00 100.06 ? 90  ARG   A CZ  1 
ATOM   516  N  NH1 . ARG   A 1 85  ? -16.492 -21.600 -29.029 1.00 85.93  ? 90  ARG   A NH1 1 
ATOM   517  N  NH2 . ARG   A 1 85  ? -16.025 -22.419 -31.120 1.00 86.50  ? 90  ARG   A NH2 1 
ATOM   518  N  N   . SER   A 1 86  ? -14.468 -14.745 -26.564 1.00 38.51  ? 91  SER   A N   1 
ATOM   519  C  CA  . SER   A 1 86  ? -14.512 -13.332 -26.136 1.00 38.63  ? 91  SER   A CA  1 
ATOM   520  C  C   . SER   A 1 86  ? -13.166 -12.870 -25.573 1.00 40.64  ? 91  SER   A C   1 
ATOM   521  O  O   . SER   A 1 86  ? -12.725 -11.765 -25.893 1.00 38.80  ? 91  SER   A O   1 
ATOM   522  C  CB  . SER   A 1 86  ? -15.608 -13.087 -25.100 1.00 42.93  ? 91  SER   A CB  1 
ATOM   523  O  OG  . SER   A 1 86  ? -16.889 -13.444 -25.593 1.00 54.20  ? 91  SER   A OG  1 
ATOM   524  N  N   . VAL   A 1 87  ? -12.511 -13.712 -24.744 1.00 36.44  ? 92  VAL   A N   1 
ATOM   525  C  CA  . VAL   A 1 87  ? -11.198 -13.357 -24.171 1.00 35.65  ? 92  VAL   A CA  1 
ATOM   526  C  C   . VAL   A 1 87  ? -10.132 -13.258 -25.258 1.00 39.57  ? 92  VAL   A C   1 
ATOM   527  O  O   . VAL   A 1 87  ? -9.364  -12.297 -25.268 1.00 39.37  ? 92  VAL   A O   1 
ATOM   528  C  CB  . VAL   A 1 87  ? -10.779 -14.297 -23.007 1.00 38.02  ? 92  VAL   A CB  1 
ATOM   529  C  CG1 . VAL   A 1 87  ? -9.333  -14.042 -22.561 1.00 37.63  ? 92  VAL   A CG1 1 
ATOM   530  C  CG2 . VAL   A 1 87  ? -11.741 -14.174 -21.834 1.00 37.49  ? 92  VAL   A CG2 1 
ATOM   531  N  N   . GLY   A 1 88  ? -10.106 -14.241 -26.164 1.00 36.75  ? 93  GLY   A N   1 
ATOM   532  C  CA  . GLY   A 1 88  ? -9.160  -14.286 -27.267 1.00 35.96  ? 93  GLY   A CA  1 
ATOM   533  C  C   . GLY   A 1 88  ? -9.284  -13.084 -28.186 1.00 38.65  ? 93  GLY   A C   1 
ATOM   534  O  O   . GLY   A 1 88  ? -8.271  -12.502 -28.577 1.00 36.83  ? 93  GLY   A O   1 
ATOM   535  N  N   . LEU   A 1 89  ? -10.525 -12.693 -28.503 1.00 36.46  ? 94  LEU   A N   1 
ATOM   536  C  CA  . LEU   A 1 89  ? -10.805 -11.576 -29.408 1.00 37.18  ? 94  LEU   A CA  1 
ATOM   537  C  C   . LEU   A 1 89  ? -10.486 -10.225 -28.785 1.00 40.82  ? 94  LEU   A C   1 
ATOM   538  O  O   . LEU   A 1 89  ? -9.794  -9.426  -29.423 1.00 40.40  ? 94  LEU   A O   1 
ATOM   539  C  CB  . LEU   A 1 89  ? -12.248 -11.623 -29.975 1.00 37.80  ? 94  LEU   A CB  1 
ATOM   540  C  CG  . LEU   A 1 89  ? -12.585 -10.547 -31.064 1.00 42.68  ? 94  LEU   A CG  1 
ATOM   541  C  CD1 . LEU   A 1 89  ? -11.675 -10.662 -32.299 1.00 42.54  ? 94  LEU   A CD1 1 
ATOM   542  C  CD2 . LEU   A 1 89  ? -14.050 -10.596 -31.458 1.00 46.13  ? 94  LEU   A CD2 1 
ATOM   543  N  N   . ALA   A 1 90  ? -10.964 -9.971  -27.540 1.00 36.95  ? 95  ALA   A N   1 
ATOM   544  C  CA  . ALA   A 1 90  ? -10.679 -8.715  -26.838 1.00 36.35  ? 95  ALA   A CA  1 
ATOM   545  C  C   . ALA   A 1 90  ? -9.178  -8.503  -26.705 1.00 36.74  ? 95  ALA   A C   1 
ATOM   546  O  O   . ALA   A 1 90  ? -8.704  -7.406  -26.985 1.00 35.00  ? 95  ALA   A O   1 
ATOM   547  C  CB  . ALA   A 1 90  ? -11.346 -8.685  -25.475 1.00 36.98  ? 95  ALA   A CB  1 
ATOM   548  N  N   . ASN   A 1 91  ? -8.424  -9.575  -26.371 1.00 33.14  ? 96  ASN   A N   1 
ATOM   549  C  CA  . ASN   A 1 91  ? -6.961  -9.508  -26.273 1.00 32.05  ? 96  ASN   A CA  1 
ATOM   550  C  C   . ASN   A 1 91  ? -6.277  -9.262  -27.616 1.00 37.25  ? 96  ASN   A C   1 
ATOM   551  O  O   . ASN   A 1 91  ? -5.281  -8.543  -27.663 1.00 35.56  ? 96  ASN   A O   1 
ATOM   552  C  CB  . ASN   A 1 91  ? -6.409  -10.729 -25.569 1.00 32.06  ? 96  ASN   A CB  1 
ATOM   553  C  CG  . ASN   A 1 91  ? -6.530  -10.547 -24.085 1.00 38.75  ? 96  ASN   A CG  1 
ATOM   554  O  OD1 . ASN   A 1 91  ? -5.860  -9.696  -23.508 1.00 36.87  ? 96  ASN   A OD1 1 
ATOM   555  N  ND2 . ASN   A 1 91  ? -7.473  -11.231 -23.464 1.00 36.57  ? 96  ASN   A ND2 1 
ATOM   556  N  N   . GLN   A 1 92  ? -6.829  -9.814  -28.717 1.00 34.94  ? 97  GLN   A N   1 
ATOM   557  C  CA  . GLN   A 1 92  ? -6.271  -9.565  -30.052 1.00 34.24  ? 97  GLN   A CA  1 
ATOM   558  C  C   . GLN   A 1 92  ? -6.405  -8.073  -30.389 1.00 36.40  ? 97  GLN   A C   1 
ATOM   559  O  O   . GLN   A 1 92  ? -5.453  -7.465  -30.869 1.00 35.24  ? 97  GLN   A O   1 
ATOM   560  C  CB  . GLN   A 1 92  ? -6.974  -10.431 -31.116 1.00 35.31  ? 97  GLN   A CB  1 
ATOM   561  C  CG  . GLN   A 1 92  ? -6.255  -10.347 -32.471 1.00 44.76  ? 97  GLN   A CG  1 
ATOM   562  C  CD  . GLN   A 1 92  ? -6.864  -11.169 -33.582 1.00 57.14  ? 97  GLN   A CD  1 
ATOM   563  O  OE1 . GLN   A 1 92  ? -8.074  -11.404 -33.634 1.00 52.53  ? 97  GLN   A OE1 1 
ATOM   564  N  NE2 . GLN   A 1 92  ? -6.028  -11.572 -34.531 1.00 47.11  ? 97  GLN   A NE2 1 
ATOM   565  N  N   . GLU   A 1 93  ? -7.579  -7.495  -30.104 1.00 34.41  ? 98  GLU   A N   1 
ATOM   566  C  CA  . GLU   A 1 93  ? -7.889  -6.074  -30.329 1.00 33.74  ? 98  GLU   A CA  1 
ATOM   567  C  C   . GLU   A 1 93  ? -7.020  -5.163  -29.462 1.00 39.03  ? 98  GLU   A C   1 
ATOM   568  O  O   . GLU   A 1 93  ? -6.491  -4.160  -29.948 1.00 39.05  ? 98  GLU   A O   1 
ATOM   569  C  CB  . GLU   A 1 93  ? -9.384  -5.816  -30.069 1.00 35.37  ? 98  GLU   A CB  1 
ATOM   570  C  CG  . GLU   A 1 93  ? -10.242 -6.234  -31.255 1.00 46.56  ? 98  GLU   A CG  1 
ATOM   571  C  CD  . GLU   A 1 93  ? -11.713 -6.509  -31.021 1.00 67.60  ? 98  GLU   A CD  1 
ATOM   572  O  OE1 . GLU   A 1 93  ? -12.286 -6.001  -30.029 1.00 51.19  ? 98  GLU   A OE1 1 
ATOM   573  O  OE2 . GLU   A 1 93  ? -12.301 -7.227  -31.863 1.00 67.77  ? 98  GLU   A OE2 1 
ATOM   574  N  N   . LEU   A 1 94  ? -6.836  -5.544  -28.185 1.00 34.78  ? 99  LEU   A N   1 
ATOM   575  C  CA  . LEU   A 1 94  ? -5.994  -4.797  -27.256 1.00 33.08  ? 99  LEU   A CA  1 
ATOM   576  C  C   . LEU   A 1 94  ? -4.534  -4.814  -27.733 1.00 35.40  ? 99  LEU   A C   1 
ATOM   577  O  O   . LEU   A 1 94  ? -3.908  -3.753  -27.763 1.00 35.20  ? 99  LEU   A O   1 
ATOM   578  C  CB  . LEU   A 1 94  ? -6.162  -5.335  -25.814 1.00 32.64  ? 99  LEU   A CB  1 
ATOM   579  C  CG  . LEU   A 1 94  ? -5.302  -4.698  -24.692 1.00 35.30  ? 99  LEU   A CG  1 
ATOM   580  C  CD1 . LEU   A 1 94  ? -5.464  -3.198  -24.644 1.00 34.36  ? 99  LEU   A CD1 1 
ATOM   581  C  CD2 . LEU   A 1 94  ? -5.667  -5.284  -23.353 1.00 36.73  ? 99  LEU   A CD2 1 
ATOM   582  N  N   . ALA   A 1 95  ? -4.022  -5.987  -28.191 1.00 32.91  ? 100 ALA   A N   1 
ATOM   583  C  CA  . ALA   A 1 95  ? -2.643  -6.109  -28.699 1.00 32.65  ? 100 ALA   A CA  1 
ATOM   584  C  C   . ALA   A 1 95  ? -2.363  -5.088  -29.823 1.00 36.15  ? 100 ALA   A C   1 
ATOM   585  O  O   . ALA   A 1 95  ? -1.284  -4.490  -29.874 1.00 34.06  ? 100 ALA   A O   1 
ATOM   586  C  CB  . ALA   A 1 95  ? -2.389  -7.532  -29.189 1.00 33.74  ? 100 ALA   A CB  1 
ATOM   587  N  N   . GLU   A 1 96  ? -3.375  -4.848  -30.692 1.00 35.83  ? 101 GLU   A N   1 
ATOM   588  C  CA  . GLU   A 1 96  ? -3.257  -3.885  -31.784 1.00 35.98  ? 101 GLU   A CA  1 
ATOM   589  C  C   . GLU   A 1 96  ? -3.061  -2.443  -31.260 1.00 37.60  ? 101 GLU   A C   1 
ATOM   590  O  O   . GLU   A 1 96  ? -2.150  -1.739  -31.720 1.00 36.95  ? 101 GLU   A O   1 
ATOM   591  C  CB  . GLU   A 1 96  ? -4.473  -3.994  -32.726 1.00 37.75  ? 101 GLU   A CB  1 
ATOM   592  C  CG  . GLU   A 1 96  ? -4.528  -5.280  -33.546 1.00 51.29  ? 101 GLU   A CG  1 
ATOM   593  C  CD  . GLU   A 1 96  ? -3.422  -5.533  -34.561 1.00 81.19  ? 101 GLU   A CD  1 
ATOM   594  O  OE1 . GLU   A 1 96  ? -3.214  -6.718  -34.910 1.00 84.08  ? 101 GLU   A OE1 1 
ATOM   595  O  OE2 . GLU   A 1 96  ? -2.775  -4.561  -35.015 1.00 78.03  ? 101 GLU   A OE2 1 
ATOM   596  N  N   . VAL   A 1 97  ? -3.869  -2.038  -30.260 1.00 34.12  ? 102 VAL   A N   1 
ATOM   597  C  CA  . VAL   A 1 97  ? -3.814  -0.688  -29.653 1.00 33.55  ? 102 VAL   A CA  1 
ATOM   598  C  C   . VAL   A 1 97  ? -2.471  -0.482  -28.887 1.00 36.28  ? 102 VAL   A C   1 
ATOM   599  O  O   . VAL   A 1 97  ? -1.819  0.551   -29.030 1.00 35.01  ? 102 VAL   A O   1 
ATOM   600  C  CB  . VAL   A 1 97  ? -5.072  -0.369  -28.797 1.00 38.51  ? 102 VAL   A CB  1 
ATOM   601  C  CG1 . VAL   A 1 97  ? -5.052  1.075   -28.281 1.00 38.71  ? 102 VAL   A CG1 1 
ATOM   602  C  CG2 . VAL   A 1 97  ? -6.363  -0.630  -29.586 1.00 38.61  ? 102 VAL   A CG2 1 
ATOM   603  N  N   . VAL   A 1 98  ? -2.057  -1.475  -28.092 1.00 32.56  ? 103 VAL   A N   1 
ATOM   604  C  CA  . VAL   A 1 98  ? -0.771  -1.418  -27.371 1.00 31.61  ? 103 VAL   A CA  1 
ATOM   605  C  C   . VAL   A 1 98  ? 0.399   -1.303  -28.367 1.00 33.91  ? 103 VAL   A C   1 
ATOM   606  O  O   . VAL   A 1 98  ? 1.287   -0.467  -28.182 1.00 32.36  ? 103 VAL   A O   1 
ATOM   607  C  CB  . VAL   A 1 98  ? -0.633  -2.628  -26.404 1.00 33.65  ? 103 VAL   A CB  1 
ATOM   608  C  CG1 . VAL   A 1 98  ? 0.780   -2.742  -25.839 1.00 33.32  ? 103 VAL   A CG1 1 
ATOM   609  C  CG2 . VAL   A 1 98  ? -1.673  -2.553  -25.292 1.00 33.50  ? 103 VAL   A CG2 1 
ATOM   610  N  N   . SER   A 1 99  ? 0.358   -2.105  -29.460 1.00 31.10  ? 104 SER   A N   1 
ATOM   611  C  CA  . SER   A 1 99  ? 1.366   -2.092  -30.525 1.00 31.87  ? 104 SER   A CA  1 
ATOM   612  C  C   . SER   A 1 99  ? 1.487   -0.683  -31.120 1.00 35.46  ? 104 SER   A C   1 
ATOM   613  O  O   . SER   A 1 99  ? 2.598   -0.185  -31.290 1.00 34.62  ? 104 SER   A O   1 
ATOM   614  C  CB  . SER   A 1 99  ? 0.989   -3.094  -31.614 1.00 35.49  ? 104 SER   A CB  1 
ATOM   615  O  OG  . SER   A 1 99  ? 1.738   -2.921  -32.803 1.00 40.70  ? 104 SER   A OG  1 
ATOM   616  N  N   . ARG   A 1 100 ? 0.341   -0.047  -31.399 1.00 34.54  ? 105 ARG   A N   1 
ATOM   617  C  CA  . ARG   A 1 100 ? 0.256   1.319   -31.926 1.00 35.03  ? 105 ARG   A CA  1 
ATOM   618  C  C   . ARG   A 1 100 ? 0.921   2.330   -30.981 1.00 38.93  ? 105 ARG   A C   1 
ATOM   619  O  O   . ARG   A 1 100 ? 1.730   3.132   -31.436 1.00 37.87  ? 105 ARG   A O   1 
ATOM   620  C  CB  . ARG   A 1 100 ? -1.214  1.713   -32.194 1.00 38.46  ? 105 ARG   A CB  1 
ATOM   621  C  CG  . ARG   A 1 100 ? -1.678  1.335   -33.594 1.00 57.26  ? 105 ARG   A CG  1 
ATOM   622  C  CD  . ARG   A 1 100 ? -3.110  1.755   -33.871 1.00 79.96  ? 105 ARG   A CD  1 
ATOM   623  N  NE  . ARG   A 1 100 ? -3.511  1.433   -35.245 1.00 98.24  ? 105 ARG   A NE  1 
ATOM   624  C  CZ  . ARG   A 1 100 ? -4.208  0.356   -35.599 1.00 116.33 ? 105 ARG   A CZ  1 
ATOM   625  N  NH1 . ARG   A 1 100 ? -4.608  -0.518  -34.682 1.00 107.36 ? 105 ARG   A NH1 1 
ATOM   626  N  NH2 . ARG   A 1 100 ? -4.520  0.149   -36.872 1.00 102.10 ? 105 ARG   A NH2 1 
ATOM   627  N  N   . ALA   A 1 101 ? 0.627   2.248   -29.663 1.00 35.23  ? 106 ALA   A N   1 
ATOM   628  C  CA  . ALA   A 1 101 ? 1.202   3.162   -28.669 1.00 35.02  ? 106 ALA   A CA  1 
ATOM   629  C  C   . ALA   A 1 101 ? 2.716   3.020   -28.531 1.00 35.31  ? 106 ALA   A C   1 
ATOM   630  O  O   . ALA   A 1 101 ? 3.416   4.023   -28.532 1.00 34.83  ? 106 ALA   A O   1 
ATOM   631  C  CB  . ALA   A 1 101 ? 0.522   2.978   -27.319 1.00 36.07  ? 106 ALA   A CB  1 
ATOM   632  N  N   . VAL   A 1 102 ? 3.217   1.771   -28.442 1.00 31.12  ? 107 VAL   A N   1 
ATOM   633  C  CA  . VAL   A 1 102 ? 4.644   1.473   -28.301 1.00 29.27  ? 107 VAL   A CA  1 
ATOM   634  C  C   . VAL   A 1 102 ? 5.449   1.875   -29.557 1.00 35.97  ? 107 VAL   A C   1 
ATOM   635  O  O   . VAL   A 1 102 ? 6.556   2.420   -29.428 1.00 34.65  ? 107 VAL   A O   1 
ATOM   636  C  CB  . VAL   A 1 102 ? 4.877   -0.003  -27.876 1.00 31.11  ? 107 VAL   A CB  1 
ATOM   637  C  CG1 . VAL   A 1 102 ? 6.363   -0.321  -27.802 1.00 30.47  ? 107 VAL   A CG1 1 
ATOM   638  C  CG2 . VAL   A 1 102 ? 4.200   -0.291  -26.528 1.00 30.16  ? 107 VAL   A CG2 1 
ATOM   639  N  N   . SER   A 1 103 ? 4.909   1.586   -30.762 1.00 35.69  ? 108 SER   A N   1 
ATOM   640  C  CA  . SER   A 1 103 ? 5.575   1.946   -32.018 1.00 36.62  ? 108 SER   A CA  1 
ATOM   641  C  C   . SER   A 1 103 ? 5.638   3.466   -32.189 1.00 42.24  ? 108 SER   A C   1 
ATOM   642  O  O   . SER   A 1 103 ? 6.598   3.961   -32.774 1.00 43.25  ? 108 SER   A O   1 
ATOM   643  C  CB  . SER   A 1 103 ? 4.927   1.261   -33.218 1.00 38.33  ? 108 SER   A CB  1 
ATOM   644  O  OG  . SER   A 1 103 ? 3.529   1.478   -33.264 1.00 41.53  ? 108 SER   A OG  1 
ATOM   645  N  N   . ASP   A 1 104 ? 4.669   4.203   -31.599 1.00 39.71  ? 109 ASP   A N   1 
ATOM   646  C  CA  . ASP   A 1 104 ? 4.647   5.675   -31.591 1.00 40.22  ? 109 ASP   A CA  1 
ATOM   647  C  C   . ASP   A 1 104 ? 5.584   6.316   -30.523 1.00 44.34  ? 109 ASP   A C   1 
ATOM   648  O  O   . ASP   A 1 104 ? 5.670   7.541   -30.455 1.00 43.93  ? 109 ASP   A O   1 
ATOM   649  C  CB  . ASP   A 1 104 ? 3.209   6.204   -31.436 1.00 43.29  ? 109 ASP   A CB  1 
ATOM   650  C  CG  . ASP   A 1 104 ? 2.322   6.055   -32.663 1.00 61.52  ? 109 ASP   A CG  1 
ATOM   651  O  OD1 . ASP   A 1 104 ? 2.871   5.904   -33.786 1.00 63.72  ? 109 ASP   A OD1 1 
ATOM   652  O  OD2 . ASP   A 1 104 ? 1.079   6.108   -32.507 1.00 68.05  ? 109 ASP   A OD2 1 
ATOM   653  N  N   . GLY   A 1 105 ? 6.279   5.493   -29.724 1.00 39.85  ? 110 GLY   A N   1 
ATOM   654  C  CA  . GLY   A 1 105 ? 7.252   5.961   -28.738 1.00 38.58  ? 110 GLY   A CA  1 
ATOM   655  C  C   . GLY   A 1 105 ? 6.735   6.246   -27.340 1.00 41.43  ? 110 GLY   A C   1 
ATOM   656  O  O   . GLY   A 1 105 ? 7.423   6.896   -26.551 1.00 42.21  ? 110 GLY   A O   1 
ATOM   657  N  N   . TYR   A 1 106 ? 5.546   5.741   -27.007 1.00 35.30  ? 111 TYR   A N   1 
ATOM   658  C  CA  . TYR   A 1 106 ? 4.949   5.945   -25.687 1.00 34.44  ? 111 TYR   A CA  1 
ATOM   659  C  C   . TYR   A 1 106 ? 5.157   4.774   -24.749 1.00 36.00  ? 111 TYR   A C   1 
ATOM   660  O  O   . TYR   A 1 106 ? 5.073   3.614   -25.168 1.00 35.12  ? 111 TYR   A O   1 
ATOM   661  C  CB  . TYR   A 1 106 ? 3.434   6.115   -25.817 1.00 34.99  ? 111 TYR   A CB  1 
ATOM   662  C  CG  . TYR   A 1 106 ? 3.019   7.399   -26.495 1.00 39.02  ? 111 TYR   A CG  1 
ATOM   663  C  CD1 . TYR   A 1 106 ? 2.933   8.590   -25.779 1.00 41.77  ? 111 TYR   A CD1 1 
ATOM   664  C  CD2 . TYR   A 1 106 ? 2.695   7.423   -27.849 1.00 40.39  ? 111 TYR   A CD2 1 
ATOM   665  C  CE1 . TYR   A 1 106 ? 2.549   9.778   -26.394 1.00 43.96  ? 111 TYR   A CE1 1 
ATOM   666  C  CE2 . TYR   A 1 106 ? 2.307   8.607   -28.476 1.00 41.63  ? 111 TYR   A CE2 1 
ATOM   667  C  CZ  . TYR   A 1 106 ? 2.228   9.782   -27.742 1.00 50.47  ? 111 TYR   A CZ  1 
ATOM   668  O  OH  . TYR   A 1 106 ? 1.840   10.960  -28.335 1.00 53.67  ? 111 TYR   A OH  1 
ATOM   669  N  N   . SER   A 1 107 ? 5.305   5.089   -23.448 1.00 32.82  ? 112 SER   A N   1 
ATOM   670  C  CA  . SER   A 1 107 ? 5.277   4.097   -22.371 1.00 32.28  ? 112 SER   A CA  1 
ATOM   671  C  C   . SER   A 1 107 ? 3.771   3.819   -22.216 1.00 34.84  ? 112 SER   A C   1 
ATOM   672  O  O   . SER   A 1 107 ? 2.987   4.748   -22.008 1.00 35.46  ? 112 SER   A O   1 
ATOM   673  C  CB  . SER   A 1 107 ? 5.860   4.682   -21.091 1.00 35.11  ? 112 SER   A CB  1 
ATOM   674  O  OG  . SER   A 1 107 ? 7.265   4.779   -21.226 1.00 41.27  ? 112 SER   A OG  1 
ATOM   675  N  N   . CYS   A 1 108 ? 3.354   2.571   -22.426 1.00 31.05  ? 113 CYS   A N   1 
ATOM   676  C  CA  . CYS   A 1 108 ? 1.939   2.229   -22.503 1.00 31.15  ? 113 CYS   A CA  1 
ATOM   677  C  C   . CYS   A 1 108 ? 1.291   1.785   -21.187 1.00 34.45  ? 113 CYS   A C   1 
ATOM   678  O  O   . CYS   A 1 108 ? 1.569   0.693   -20.692 1.00 33.30  ? 113 CYS   A O   1 
ATOM   679  C  CB  . CYS   A 1 108 ? 1.715   1.197   -23.604 1.00 32.01  ? 113 CYS   A CB  1 
ATOM   680  S  SG  . CYS   A 1 108 ? -0.015  0.972   -24.042 1.00 36.82  ? 113 CYS   A SG  1 
ATOM   681  N  N   . VAL   A 1 109 ? 0.346   2.607   -20.679 1.00 30.42  ? 114 VAL   A N   1 
ATOM   682  C  CA  . VAL   A 1 109 ? -0.424  2.311   -19.468 1.00 29.70  ? 114 VAL   A CA  1 
ATOM   683  C  C   . VAL   A 1 109 ? -1.797  1.732   -19.832 1.00 32.80  ? 114 VAL   A C   1 
ATOM   684  O  O   . VAL   A 1 109 ? -2.601  2.420   -20.462 1.00 32.59  ? 114 VAL   A O   1 
ATOM   685  C  CB  . VAL   A 1 109 ? -0.539  3.532   -18.509 1.00 32.31  ? 114 VAL   A CB  1 
ATOM   686  C  CG1 . VAL   A 1 109 ? -1.453  3.222   -17.317 1.00 32.44  ? 114 VAL   A CG1 1 
ATOM   687  C  CG2 . VAL   A 1 109 ? 0.833   3.978   -18.026 1.00 32.04  ? 114 VAL   A CG2 1 
ATOM   688  N  N   . THR   A 1 110 ? -2.061  0.470   -19.452 1.00 29.28  ? 115 THR   A N   1 
ATOM   689  C  CA  . THR   A 1 110 ? -3.366  -0.144  -19.698 1.00 29.18  ? 115 THR   A CA  1 
ATOM   690  C  C   . THR   A 1 110 ? -4.104  -0.303  -18.369 1.00 33.41  ? 115 THR   A C   1 
ATOM   691  O  O   . THR   A 1 110 ? -3.573  -0.898  -17.429 1.00 32.39  ? 115 THR   A O   1 
ATOM   692  C  CB  . THR   A 1 110 ? -3.249  -1.466  -20.470 1.00 37.09  ? 115 THR   A CB  1 
ATOM   693  O  OG1 . THR   A 1 110 ? -2.470  -1.241  -21.648 1.00 36.18  ? 115 THR   A OG1 1 
ATOM   694  C  CG2 . THR   A 1 110 ? -4.616  -2.052  -20.849 1.00 35.57  ? 115 THR   A CG2 1 
ATOM   695  N  N   . LEU   A 1 111 ? -5.354  0.184   -18.322 1.00 30.92  ? 116 LEU   A N   1 
ATOM   696  C  CA  . LEU   A 1 111 ? -6.205  0.098   -17.143 1.00 30.51  ? 116 LEU   A CA  1 
ATOM   697  C  C   . LEU   A 1 111 ? -7.202  -1.031  -17.324 1.00 35.19  ? 116 LEU   A C   1 
ATOM   698  O  O   . LEU   A 1 111 ? -7.946  -1.057  -18.311 1.00 35.59  ? 116 LEU   A O   1 
ATOM   699  C  CB  . LEU   A 1 111 ? -6.952  1.428   -16.900 1.00 30.90  ? 116 LEU   A CB  1 
ATOM   700  C  CG  . LEU   A 1 111 ? -6.127  2.714   -16.941 1.00 33.64  ? 116 LEU   A CG  1 
ATOM   701  C  CD1 . LEU   A 1 111 ? -7.027  3.936   -16.844 1.00 33.92  ? 116 LEU   A CD1 1 
ATOM   702  C  CD2 . LEU   A 1 111 ? -5.045  2.737   -15.837 1.00 32.83  ? 116 LEU   A CD2 1 
ATOM   703  N  N   . GLY   A 1 112 ? -7.200  -1.963  -16.389 1.00 30.52  ? 117 GLY   A N   1 
ATOM   704  C  CA  . GLY   A 1 112 ? -8.121  -3.086  -16.428 1.00 29.78  ? 117 GLY   A CA  1 
ATOM   705  C  C   . GLY   A 1 112 ? -9.365  -2.847  -15.595 1.00 33.45  ? 117 GLY   A C   1 
ATOM   706  O  O   . GLY   A 1 112 ? -9.438  -1.841  -14.899 1.00 33.91  ? 117 GLY   A O   1 
ATOM   707  N  N   . GLY   A 1 113 ? -10.339 -3.765  -15.623 1.00 31.54  ? 118 GLY   A N   1 
ATOM   708  C  CA  . GLY   A 1 113 ? -10.315 -4.995  -16.402 1.00 31.35  ? 118 GLY   A CA  1 
ATOM   709  C  C   . GLY   A 1 113 ? -9.596  -6.122  -15.681 1.00 34.48  ? 118 GLY   A C   1 
ATOM   710  O  O   . GLY   A 1 113 ? -8.727  -5.874  -14.835 1.00 33.08  ? 118 GLY   A O   1 
ATOM   711  N  N   . ASP   A 1 114 ? -9.969  -7.365  -15.988 1.00 30.54  ? 119 ASP   A N   1 
ATOM   712  C  CA  . ASP   A 1 114 ? -9.358  -8.518  -15.344 1.00 29.88  ? 119 ASP   A CA  1 
ATOM   713  C  C   . ASP   A 1 114 ? -7.952  -8.794  -15.906 1.00 33.33  ? 119 ASP   A C   1 
ATOM   714  O  O   . ASP   A 1 114 ? -7.588  -8.256  -16.964 1.00 33.70  ? 119 ASP   A O   1 
ATOM   715  C  CB  . ASP   A 1 114 ? -10.287 -9.744  -15.376 1.00 31.04  ? 119 ASP   A CB  1 
ATOM   716  C  CG  . ASP   A 1 114 ? -10.461 -10.328 -16.746 1.00 35.05  ? 119 ASP   A CG  1 
ATOM   717  O  OD1 . ASP   A 1 114 ? -9.508  -10.927 -17.248 1.00 33.15  ? 119 ASP   A OD1 1 
ATOM   718  O  OD2 . ASP   A 1 114 ? -11.573 -10.248 -17.281 1.00 38.19  ? 119 ASP   A OD2 1 
ATOM   719  N  N   . HIS   A 1 115 ? -7.164  -9.643  -15.211 1.00 29.35  ? 120 HIS   A N   1 
ATOM   720  C  CA  . HIS   A 1 115 ? -5.781  -9.873  -15.610 1.00 27.84  ? 120 HIS   A CA  1 
ATOM   721  C  C   . HIS   A 1 115 ? -5.600  -10.717 -16.895 1.00 31.61  ? 120 HIS   A C   1 
ATOM   722  O  O   . HIS   A 1 115 ? -4.470  -10.777 -17.399 1.00 30.59  ? 120 HIS   A O   1 
ATOM   723  C  CB  . HIS   A 1 115 ? -4.941  -10.444 -14.455 1.00 27.67  ? 120 HIS   A CB  1 
ATOM   724  C  CG  . HIS   A 1 115 ? -3.549  -9.865  -14.425 1.00 29.68  ? 120 HIS   A CG  1 
ATOM   725  N  ND1 . HIS   A 1 115 ? -2.798  -9.882  -13.269 1.00 31.05  ? 120 HIS   A ND1 1 
ATOM   726  C  CD2 . HIS   A 1 115 ? -2.844  -9.222  -15.392 1.00 30.66  ? 120 HIS   A CD2 1 
ATOM   727  C  CE1 . HIS   A 1 115 ? -1.674  -9.254  -13.557 1.00 30.09  ? 120 HIS   A CE1 1 
ATOM   728  N  NE2 . HIS   A 1 115 ? -1.653  -8.847  -14.828 1.00 30.35  ? 120 HIS   A NE2 1 
ATOM   729  N  N   . SER   A 1 116 ? -6.688  -11.295 -17.479 1.00 29.07  ? 121 SER   A N   1 
ATOM   730  C  CA  . SER   A 1 116 ? -6.540  -12.019 -18.769 1.00 28.63  ? 121 SER   A CA  1 
ATOM   731  C  C   . SER   A 1 116 ? -6.031  -11.026 -19.842 1.00 32.01  ? 121 SER   A C   1 
ATOM   732  O  O   . SER   A 1 116 ? -5.430  -11.451 -20.827 1.00 33.32  ? 121 SER   A O   1 
ATOM   733  C  CB  . SER   A 1 116 ? -7.863  -12.642 -19.228 1.00 31.11  ? 121 SER   A CB  1 
ATOM   734  O  OG  . SER   A 1 116 ? -8.801  -11.683 -19.697 1.00 34.44  ? 121 SER   A OG  1 
ATOM   735  N  N   . LEU   A 1 117 ? -6.236  -9.711  -19.604 1.00 29.46  ? 122 LEU   A N   1 
ATOM   736  C  CA  . LEU   A 1 117 ? -5.809  -8.610  -20.483 1.00 29.89  ? 122 LEU   A CA  1 
ATOM   737  C  C   . LEU   A 1 117 ? -4.306  -8.501  -20.652 1.00 32.96  ? 122 LEU   A C   1 
ATOM   738  O  O   . LEU   A 1 117 ? -3.872  -7.855  -21.604 1.00 32.19  ? 122 LEU   A O   1 
ATOM   739  C  CB  . LEU   A 1 117 ? -6.389  -7.256  -20.069 1.00 30.56  ? 122 LEU   A CB  1 
ATOM   740  C  CG  . LEU   A 1 117 ? -7.912  -7.103  -20.125 1.00 36.20  ? 122 LEU   A CG  1 
ATOM   741  C  CD1 . LEU   A 1 117 ? -8.335  -5.885  -19.365 1.00 36.79  ? 122 LEU   A CD1 1 
ATOM   742  C  CD2 . LEU   A 1 117 ? -8.442  -7.054  -21.581 1.00 40.54  ? 122 LEU   A CD2 1 
ATOM   743  N  N   . ALA   A 1 118 ? -3.497  -9.160  -19.772 1.00 29.46  ? 123 ALA   A N   1 
ATOM   744  C  CA  . ALA   A 1 118 ? -2.050  -9.173  -19.968 1.00 29.33  ? 123 ALA   A CA  1 
ATOM   745  C  C   . ALA   A 1 118 ? -1.693  -9.995  -21.241 1.00 30.93  ? 123 ALA   A C   1 
ATOM   746  O  O   . ALA   A 1 118 ? -0.626  -9.781  -21.816 1.00 29.71  ? 123 ALA   A O   1 
ATOM   747  C  CB  . ALA   A 1 118 ? -1.347  -9.759  -18.759 1.00 30.45  ? 123 ALA   A CB  1 
ATOM   748  N  N   . ILE   A 1 119 ? -2.590  -10.907 -21.697 1.00 27.05  ? 124 ILE   A N   1 
ATOM   749  C  CA  . ILE   A 1 119 ? -2.343  -11.649 -22.955 1.00 27.26  ? 124 ILE   A CA  1 
ATOM   750  C  C   . ILE   A 1 119 ? -2.182  -10.592 -24.096 1.00 31.87  ? 124 ILE   A C   1 
ATOM   751  O  O   . ILE   A 1 119 ? -1.224  -10.652 -24.872 1.00 32.58  ? 124 ILE   A O   1 
ATOM   752  C  CB  . ILE   A 1 119 ? -3.477  -12.673 -23.285 1.00 29.85  ? 124 ILE   A CB  1 
ATOM   753  C  CG1 . ILE   A 1 119 ? -3.576  -13.811 -22.227 1.00 30.17  ? 124 ILE   A CG1 1 
ATOM   754  C  CG2 . ILE   A 1 119 ? -3.284  -13.275 -24.695 1.00 31.30  ? 124 ILE   A CG2 1 
ATOM   755  C  CD1 . ILE   A 1 119 ? -4.948  -14.546 -22.188 1.00 32.13  ? 124 ILE   A CD1 1 
ATOM   756  N  N   . GLY   A 1 120 ? -3.091  -9.625  -24.127 1.00 30.04  ? 125 GLY   A N   1 
ATOM   757  C  CA  . GLY   A 1 120 ? -3.103  -8.557  -25.118 1.00 30.21  ? 125 GLY   A CA  1 
ATOM   758  C  C   . GLY   A 1 120 ? -1.996  -7.533  -24.973 1.00 32.68  ? 125 GLY   A C   1 
ATOM   759  O  O   . GLY   A 1 120 ? -1.323  -7.193  -25.951 1.00 31.04  ? 125 GLY   A O   1 
ATOM   760  N  N   . THR   A 1 121 ? -1.780  -7.027  -23.739 1.00 28.60  ? 126 THR   A N   1 
ATOM   761  C  CA  . THR   A 1 121 ? -0.768  -5.999  -23.527 1.00 26.26  ? 126 THR   A CA  1 
ATOM   762  C  C   . THR   A 1 121 ? 0.652   -6.502  -23.757 1.00 28.54  ? 126 THR   A C   1 
ATOM   763  O  O   . THR   A 1 121 ? 1.440   -5.790  -24.375 1.00 27.29  ? 126 THR   A O   1 
ATOM   764  C  CB  . THR   A 1 121 ? -0.925  -5.358  -22.136 1.00 32.31  ? 126 THR   A CB  1 
ATOM   765  O  OG1 . THR   A 1 121 ? -0.641  -6.360  -21.167 1.00 31.56  ? 126 THR   A OG1 1 
ATOM   766  C  CG2 . THR   A 1 121 ? -2.326  -4.841  -21.893 1.00 31.59  ? 126 THR   A CG2 1 
ATOM   767  N  N   . ILE   A 1 122 ? 0.982   -7.720  -23.248 1.00 26.67  ? 127 ILE   A N   1 
ATOM   768  C  CA  . ILE   A 1 122 ? 2.320   -8.277  -23.424 1.00 25.28  ? 127 ILE   A CA  1 
ATOM   769  C  C   . ILE   A 1 122 ? 2.559   -8.655  -24.917 1.00 29.22  ? 127 ILE   A C   1 
ATOM   770  O  O   . ILE   A 1 122 ? 3.607   -8.329  -25.460 1.00 28.79  ? 127 ILE   A O   1 
ATOM   771  C  CB  . ILE   A 1 122 ? 2.614   -9.414  -22.418 1.00 27.00  ? 127 ILE   A CB  1 
ATOM   772  C  CG1 . ILE   A 1 122 ? 2.574   -8.809  -20.967 1.00 26.61  ? 127 ILE   A CG1 1 
ATOM   773  C  CG2 . ILE   A 1 122 ? 3.956   -10.061 -22.729 1.00 26.95  ? 127 ILE   A CG2 1 
ATOM   774  C  CD1 . ILE   A 1 122 ? 2.677   -9.808  -19.801 1.00 29.14  ? 127 ILE   A CD1 1 
ATOM   775  N  N   . SER   A 1 123 ? 1.569   -9.276  -25.564 1.00 28.20  ? 128 SER   A N   1 
ATOM   776  C  CA  . SER   A 1 123 ? 1.657   -9.636  -26.998 1.00 27.73  ? 128 SER   A CA  1 
ATOM   777  C  C   . SER   A 1 123 ? 1.894   -8.371  -27.853 1.00 31.40  ? 128 SER   A C   1 
ATOM   778  O  O   . SER   A 1 123 ? 2.786   -8.362  -28.708 1.00 31.10  ? 128 SER   A O   1 
ATOM   779  C  CB  . SER   A 1 123 ? 0.374   -10.329 -27.455 1.00 28.19  ? 128 SER   A CB  1 
ATOM   780  O  OG  . SER   A 1 123 ? 0.329   -11.657 -26.968 1.00 32.60  ? 128 SER   A OG  1 
ATOM   781  N  N   . GLY   A 1 124 ? 1.143   -7.308  -27.564 1.00 29.13  ? 129 GLY   A N   1 
ATOM   782  C  CA  . GLY   A 1 124 ? 1.247   -6.028  -28.260 1.00 28.01  ? 129 GLY   A CA  1 
ATOM   783  C  C   . GLY   A 1 124 ? 2.607   -5.377  -28.106 1.00 31.63  ? 129 GLY   A C   1 
ATOM   784  O  O   . GLY   A 1 124 ? 3.190   -4.881  -29.077 1.00 31.63  ? 129 GLY   A O   1 
ATOM   785  N  N   . HIS   A 1 125 ? 3.131   -5.390  -26.856 1.00 26.68  ? 130 HIS   A N   1 
ATOM   786  C  CA  . HIS   A 1 125 ? 4.430   -4.838  -26.512 1.00 26.41  ? 130 HIS   A CA  1 
ATOM   787  C  C   . HIS   A 1 125 ? 5.580   -5.640  -27.162 1.00 29.75  ? 130 HIS   A C   1 
ATOM   788  O  O   . HIS   A 1 125 ? 6.563   -5.046  -27.630 1.00 28.47  ? 130 HIS   A O   1 
ATOM   789  C  CB  . HIS   A 1 125 ? 4.555   -4.900  -24.971 1.00 26.29  ? 130 HIS   A CB  1 
ATOM   790  C  CG  . HIS   A 1 125 ? 5.629   -4.068  -24.354 1.00 29.06  ? 130 HIS   A CG  1 
ATOM   791  N  ND1 . HIS   A 1 125 ? 5.808   -4.069  -22.978 1.00 29.50  ? 130 HIS   A ND1 1 
ATOM   792  C  CD2 . HIS   A 1 125 ? 6.546   -3.238  -24.915 1.00 29.99  ? 130 HIS   A CD2 1 
ATOM   793  C  CE1 . HIS   A 1 125 ? 6.826   -3.258  -22.743 1.00 29.75  ? 130 HIS   A CE1 1 
ATOM   794  N  NE2 . HIS   A 1 125 ? 7.310   -2.735  -23.874 1.00 30.18  ? 130 HIS   A NE2 1 
ATOM   795  N  N   . ALA   A 1 126 ? 5.479   -6.996  -27.156 1.00 27.77  ? 131 ALA   A N   1 
ATOM   796  C  CA  . ALA   A 1 126 ? 6.527   -7.856  -27.706 1.00 28.18  ? 131 ALA   A CA  1 
ATOM   797  C  C   . ALA   A 1 126 ? 6.688   -7.710  -29.239 1.00 32.84  ? 131 ALA   A C   1 
ATOM   798  O  O   . ALA   A 1 126 ? 7.720   -8.090  -29.784 1.00 32.47  ? 131 ALA   A O   1 
ATOM   799  C  CB  . ALA   A 1 126 ? 6.266   -9.309  -27.337 1.00 29.41  ? 131 ALA   A CB  1 
ATOM   800  N  N   . ARG   A 1 127 ? 5.686   -7.133  -29.909 1.00 30.13  ? 132 ARG   A N   1 
ATOM   801  C  CA  . ARG   A 1 127 ? 5.736   -6.875  -31.359 1.00 29.04  ? 132 ARG   A CA  1 
ATOM   802  C  C   . ARG   A 1 127 ? 6.773   -5.821  -31.726 1.00 33.22  ? 132 ARG   A C   1 
ATOM   803  O  O   . ARG   A 1 127 ? 7.112   -5.684  -32.912 1.00 32.13  ? 132 ARG   A O   1 
ATOM   804  C  CB  . ARG   A 1 127 ? 4.356   -6.458  -31.860 1.00 29.95  ? 132 ARG   A CB  1 
ATOM   805  C  CG  . ARG   A 1 127 ? 3.479   -7.657  -32.165 1.00 38.00  ? 132 ARG   A CG  1 
ATOM   806  C  CD  . ARG   A 1 127 ? 2.092   -7.242  -32.549 1.00 40.10  ? 132 ARG   A CD  1 
ATOM   807  N  NE  . ARG   A 1 127 ? 1.142   -8.317  -32.285 1.00 41.21  ? 132 ARG   A NE  1 
ATOM   808  C  CZ  . ARG   A 1 127 ? -0.172  -8.173  -32.347 1.00 48.75  ? 132 ARG   A CZ  1 
ATOM   809  N  NH1 . ARG   A 1 127 ? -0.703  -7.005  -32.692 1.00 37.19  ? 132 ARG   A NH1 1 
ATOM   810  N  NH2 . ARG   A 1 127 ? -0.968  -9.193  -32.071 1.00 43.64  ? 132 ARG   A NH2 1 
ATOM   811  N  N   . HIS   A 1 128 ? 7.292   -5.078  -30.713 1.00 29.03  ? 133 HIS   A N   1 
ATOM   812  C  CA  . HIS   A 1 128 ? 8.267   -4.015  -30.897 1.00 28.38  ? 133 HIS   A CA  1 
ATOM   813  C  C   . HIS   A 1 128 ? 9.483   -4.158  -30.017 1.00 30.92  ? 133 HIS   A C   1 
ATOM   814  O  O   . HIS   A 1 128 ? 10.522  -3.562  -30.303 1.00 29.27  ? 133 HIS   A O   1 
ATOM   815  C  CB  . HIS   A 1 128 ? 7.571   -2.649  -30.689 1.00 29.48  ? 133 HIS   A CB  1 
ATOM   816  C  CG  . HIS   A 1 128 ? 6.372   -2.505  -31.568 1.00 32.85  ? 133 HIS   A CG  1 
ATOM   817  N  ND1 . HIS   A 1 128 ? 6.505   -2.341  -32.936 1.00 34.75  ? 133 HIS   A ND1 1 
ATOM   818  C  CD2 . HIS   A 1 128 ? 5.061   -2.664  -31.271 1.00 34.96  ? 133 HIS   A CD2 1 
ATOM   819  C  CE1 . HIS   A 1 128 ? 5.273   -2.351  -33.417 1.00 34.46  ? 133 HIS   A CE1 1 
ATOM   820  N  NE2 . HIS   A 1 128 ? 4.371   -2.524  -32.452 1.00 35.10  ? 133 HIS   A NE2 1 
ATOM   821  N  N   . CYS   A 1 129 ? 9.389   -5.015  -28.978 1.00 28.97  ? 134 CYS   A N   1 
ATOM   822  C  CA  . CYS   A 1 129 ? 10.458  -5.230  -28.014 1.00 28.73  ? 134 CYS   A CA  1 
ATOM   823  C  C   . CYS   A 1 129 ? 10.826  -6.726  -27.935 1.00 32.63  ? 134 CYS   A C   1 
ATOM   824  O  O   . CYS   A 1 129 ? 10.246  -7.449  -27.132 1.00 31.84  ? 134 CYS   A O   1 
ATOM   825  C  CB  . CYS   A 1 129 ? 10.014  -4.678  -26.664 1.00 28.45  ? 134 CYS   A CB  1 
ATOM   826  S  SG  . CYS   A 1 129 ? 9.652   -2.910  -26.698 1.00 31.91  ? 134 CYS   A SG  1 
ATOM   827  N  N   . PRO   A 1 130 ? 11.782  -7.197  -28.767 1.00 28.14  ? 135 PRO   A N   1 
ATOM   828  C  CA  . PRO   A 1 130 ? 12.128  -8.631  -28.761 1.00 28.24  ? 135 PRO   A CA  1 
ATOM   829  C  C   . PRO   A 1 130 ? 12.761  -9.079  -27.438 1.00 31.72  ? 135 PRO   A C   1 
ATOM   830  O  O   . PRO   A 1 130 ? 12.686  -10.263 -27.060 1.00 32.25  ? 135 PRO   A O   1 
ATOM   831  C  CB  . PRO   A 1 130 ? 13.132  -8.754  -29.917 1.00 30.46  ? 135 PRO   A CB  1 
ATOM   832  C  CG  . PRO   A 1 130 ? 13.714  -7.378  -30.074 1.00 33.78  ? 135 PRO   A CG  1 
ATOM   833  C  CD  . PRO   A 1 130 ? 12.556  -6.470  -29.799 1.00 29.78  ? 135 PRO   A CD  1 
ATOM   834  N  N   . ASP   A 1 131 ? 13.418  -8.136  -26.754 1.00 26.25  ? 136 ASP   A N   1 
ATOM   835  C  CA  . ASP   A 1 131 ? 14.073  -8.458  -25.516 1.00 25.63  ? 136 ASP   A CA  1 
ATOM   836  C  C   . ASP   A 1 131 ? 13.293  -7.956  -24.314 1.00 27.86  ? 136 ASP   A C   1 
ATOM   837  O  O   . ASP   A 1 131 ? 13.906  -7.751  -23.279 1.00 27.55  ? 136 ASP   A O   1 
ATOM   838  C  CB  . ASP   A 1 131 ? 15.524  -7.971  -25.534 1.00 26.72  ? 136 ASP   A CB  1 
ATOM   839  C  CG  . ASP   A 1 131 ? 16.447  -8.750  -24.637 1.00 30.07  ? 136 ASP   A CG  1 
ATOM   840  O  OD1 . ASP   A 1 131 ? 16.079  -9.886  -24.236 1.00 31.63  ? 136 ASP   A OD1 1 
ATOM   841  O  OD2 . ASP   A 1 131 ? 17.519  -8.251  -24.345 1.00 32.30  ? 136 ASP   A OD2 1 
ATOM   842  N  N   . LEU   A 1 132 ? 11.950  -7.828  -24.416 1.00 25.59  ? 137 LEU   A N   1 
ATOM   843  C  CA  . LEU   A 1 132 ? 11.208  -7.368  -23.243 1.00 26.92  ? 137 LEU   A CA  1 
ATOM   844  C  C   . LEU   A 1 132 ? 11.324  -8.339  -22.054 1.00 28.49  ? 137 LEU   A C   1 
ATOM   845  O  O   . LEU   A 1 132 ? 11.467  -9.558  -22.245 1.00 26.86  ? 137 LEU   A O   1 
ATOM   846  C  CB  . LEU   A 1 132 ? 9.721   -7.003  -23.535 1.00 28.54  ? 137 LEU   A CB  1 
ATOM   847  C  CG  . LEU   A 1 132 ? 8.604   -8.045  -23.634 1.00 34.75  ? 137 LEU   A CG  1 
ATOM   848  C  CD1 . LEU   A 1 132 ? 8.333   -8.703  -22.316 1.00 38.48  ? 137 LEU   A CD1 1 
ATOM   849  C  CD2 . LEU   A 1 132 ? 7.273   -7.379  -23.917 1.00 33.12  ? 137 LEU   A CD2 1 
ATOM   850  N  N   . CYS   A 1 133 ? 11.218  -7.787  -20.844 1.00 24.18  ? 138 CYS   A N   1 
ATOM   851  C  CA  . CYS   A 1 133 ? 11.143  -8.600  -19.634 1.00 23.99  ? 138 CYS   A CA  1 
ATOM   852  C  C   . CYS   A 1 133 ? 9.893   -8.157  -18.863 1.00 27.68  ? 138 CYS   A C   1 
ATOM   853  O  O   . CYS   A 1 133 ? 9.347   -7.083  -19.129 1.00 25.86  ? 138 CYS   A O   1 
ATOM   854  C  CB  . CYS   A 1 133 ? 12.407  -8.536  -18.786 1.00 24.65  ? 138 CYS   A CB  1 
ATOM   855  S  SG  . CYS   A 1 133 ? 12.778  -6.889  -18.162 1.00 28.09  ? 138 CYS   A SG  1 
ATOM   856  N  N   . VAL   A 1 134 ? 9.408   -9.016  -17.963 1.00 23.74  ? 139 VAL   A N   1 
ATOM   857  C  CA  . VAL   A 1 134 ? 8.150   -8.773  -17.269 1.00 23.74  ? 139 VAL   A CA  1 
ATOM   858  C  C   . VAL   A 1 134 ? 8.332   -8.833  -15.760 1.00 24.65  ? 139 VAL   A C   1 
ATOM   859  O  O   . VAL   A 1 134 ? 8.978   -9.752  -15.261 1.00 22.41  ? 139 VAL   A O   1 
ATOM   860  C  CB  . VAL   A 1 134 ? 7.049   -9.772  -17.727 1.00 26.63  ? 139 VAL   A CB  1 
ATOM   861  C  CG1 . VAL   A 1 134 ? 5.718   -9.522  -17.021 1.00 26.36  ? 139 VAL   A CG1 1 
ATOM   862  C  CG2 . VAL   A 1 134 ? 6.851   -9.753  -19.250 1.00 26.43  ? 139 VAL   A CG2 1 
ATOM   863  N  N   . VAL   A 1 135 ? 7.754   -7.849  -15.045 1.00 23.09  ? 140 VAL   A N   1 
ATOM   864  C  CA  . VAL   A 1 135 ? 7.702   -7.885  -13.575 1.00 21.45  ? 140 VAL   A CA  1 
ATOM   865  C  C   . VAL   A 1 135 ? 6.201   -8.005  -13.316 1.00 23.84  ? 140 VAL   A C   1 
ATOM   866  O  O   . VAL   A 1 135 ? 5.459   -7.091  -13.669 1.00 22.26  ? 140 VAL   A O   1 
ATOM   867  C  CB  . VAL   A 1 135 ? 8.324   -6.649  -12.888 1.00 24.74  ? 140 VAL   A CB  1 
ATOM   868  C  CG1 . VAL   A 1 135 ? 8.109   -6.709  -11.362 1.00 24.54  ? 140 VAL   A CG1 1 
ATOM   869  C  CG2 . VAL   A 1 135 ? 9.824   -6.534  -13.205 1.00 23.37  ? 140 VAL   A CG2 1 
ATOM   870  N  N   . TRP   A 1 136 ? 5.778   -9.127  -12.704 1.00 20.60  ? 141 TRP   A N   1 
ATOM   871  C  CA  . TRP   A 1 136 ? 4.381   -9.462  -12.487 1.00 21.78  ? 141 TRP   A CA  1 
ATOM   872  C  C   . TRP   A 1 136 ? 4.115   -9.353  -10.988 1.00 24.40  ? 141 TRP   A C   1 
ATOM   873  O  O   . TRP   A 1 136 ? 4.589   -10.183 -10.206 1.00 21.90  ? 141 TRP   A O   1 
ATOM   874  C  CB  . TRP   A 1 136 ? 4.127   -10.891 -13.005 1.00 21.95  ? 141 TRP   A CB  1 
ATOM   875  C  CG  . TRP   A 1 136 ? 2.687   -11.246 -13.125 1.00 23.31  ? 141 TRP   A CG  1 
ATOM   876  C  CD1 . TRP   A 1 136 ? 1.828   -11.545 -12.112 1.00 25.90  ? 141 TRP   A CD1 1 
ATOM   877  C  CD2 . TRP   A 1 136 ? 1.932   -11.343 -14.338 1.00 23.04  ? 141 TRP   A CD2 1 
ATOM   878  N  NE1 . TRP   A 1 136 ? 0.571   -11.786 -12.612 1.00 25.91  ? 141 TRP   A NE1 1 
ATOM   879  C  CE2 . TRP   A 1 136 ? 0.606   -11.667 -13.982 1.00 27.26  ? 141 TRP   A CE2 1 
ATOM   880  C  CE3 . TRP   A 1 136 ? 2.242   -11.152 -15.695 1.00 25.10  ? 141 TRP   A CE3 1 
ATOM   881  C  CZ2 . TRP   A 1 136 ? -0.392  -11.899 -14.937 1.00 27.42  ? 141 TRP   A CZ2 1 
ATOM   882  C  CZ3 . TRP   A 1 136 ? 1.241   -11.346 -16.641 1.00 27.14  ? 141 TRP   A CZ3 1 
ATOM   883  C  CH2 . TRP   A 1 136 ? -0.055  -11.717 -16.262 1.00 27.56  ? 141 TRP   A CH2 1 
ATOM   884  N  N   . VAL   A 1 137 ? 3.412   -8.287  -10.597 1.00 22.73  ? 142 VAL   A N   1 
ATOM   885  C  CA  . VAL   A 1 137 ? 3.137   -7.998  -9.183  1.00 21.40  ? 142 VAL   A CA  1 
ATOM   886  C  C   . VAL   A 1 137 ? 1.715   -8.398  -8.882  1.00 24.14  ? 142 VAL   A C   1 
ATOM   887  O  O   . VAL   A 1 137 ? 0.781   -7.801  -9.419  1.00 23.39  ? 142 VAL   A O   1 
ATOM   888  C  CB  . VAL   A 1 137 ? 3.452   -6.528  -8.830  1.00 23.86  ? 142 VAL   A CB  1 
ATOM   889  C  CG1 . VAL   A 1 137 ? 3.300   -6.302  -7.332  1.00 23.72  ? 142 VAL   A CG1 1 
ATOM   890  C  CG2 . VAL   A 1 137 ? 4.870   -6.156  -9.253  1.00 22.98  ? 142 VAL   A CG2 1 
ATOM   891  N  N   . ASP   A 1 138 ? 1.557   -9.459  -8.074  1.00 22.91  ? 143 ASP   A N   1 
ATOM   892  C  CA  . ASP   A 1 138 ? 0.245   -10.076 -7.867  1.00 22.87  ? 143 ASP   A CA  1 
ATOM   893  C  C   . ASP   A 1 138 ? 0.258   -11.031 -6.685  1.00 24.77  ? 143 ASP   A C   1 
ATOM   894  O  O   . ASP   A 1 138 ? 1.302   -11.575 -6.339  1.00 23.73  ? 143 ASP   A O   1 
ATOM   895  C  CB  . ASP   A 1 138 ? -0.020  -10.896 -9.157  1.00 24.85  ? 143 ASP   A CB  1 
ATOM   896  C  CG  . ASP   A 1 138 ? -1.452  -11.201 -9.545  1.00 29.16  ? 143 ASP   A CG  1 
ATOM   897  O  OD1 . ASP   A 1 138 ? -2.249  -11.550 -8.644  1.00 27.31  ? 143 ASP   A OD1 1 
ATOM   898  O  OD2 . ASP   A 1 138 ? -1.749  -11.184 -10.767 1.00 28.06  ? 143 ASP   A OD2 1 
ATOM   899  N  N   . ALA   A 1 139 ? -0.917  -11.288 -6.082  1.00 24.46  ? 144 ALA   A N   1 
ATOM   900  C  CA  . ALA   A 1 139 ? -1.042  -12.306 -5.050  1.00 24.61  ? 144 ALA   A CA  1 
ATOM   901  C  C   . ALA   A 1 139 ? -0.994  -13.708 -5.724  1.00 26.28  ? 144 ALA   A C   1 
ATOM   902  O  O   . ALA   A 1 139 ? -0.741  -14.721 -5.078  1.00 28.13  ? 144 ALA   A O   1 
ATOM   903  C  CB  . ALA   A 1 139 ? -2.390  -12.136 -4.354  1.00 24.87  ? 144 ALA   A CB  1 
ATOM   904  N  N   . HIS   A 1 140 ? -1.211  -13.729 -7.043  1.00 25.65  ? 145 HIS   A N   1 
ATOM   905  C  CA  . HIS   A 1 140 ? -1.358  -14.957 -7.847  1.00 25.60  ? 145 HIS   A CA  1 
ATOM   906  C  C   . HIS   A 1 140 ? -0.365  -15.060 -9.008  1.00 28.59  ? 145 HIS   A C   1 
ATOM   907  O  O   . HIS   A 1 140 ? 0.080   -14.037 -9.533  1.00 26.65  ? 145 HIS   A O   1 
ATOM   908  C  CB  . HIS   A 1 140 ? -2.767  -14.955 -8.451  1.00 27.60  ? 145 HIS   A CB  1 
ATOM   909  C  CG  . HIS   A 1 140 ? -3.843  -14.757 -7.439  1.00 30.72  ? 145 HIS   A CG  1 
ATOM   910  N  ND1 . HIS   A 1 140 ? -4.517  -13.565 -7.331  1.00 32.13  ? 145 HIS   A ND1 1 
ATOM   911  C  CD2 . HIS   A 1 140 ? -4.292  -15.607 -6.485  1.00 31.36  ? 145 HIS   A CD2 1 
ATOM   912  C  CE1 . HIS   A 1 140 ? -5.380  -13.739 -6.337  1.00 30.75  ? 145 HIS   A CE1 1 
ATOM   913  N  NE2 . HIS   A 1 140 ? -5.277  -14.953 -5.808  1.00 30.85  ? 145 HIS   A NE2 1 
ATOM   914  N  N   . ALA   A 1 141 ? -0.036  -16.302 -9.419  1.00 25.16  ? 146 ALA   A N   1 
ATOM   915  C  CA  . ALA   A 1 141 ? 0.894   -16.520 -10.531 1.00 26.18  ? 146 ALA   A CA  1 
ATOM   916  C  C   . ALA   A 1 141 ? 0.208   -16.407 -11.900 1.00 27.69  ? 146 ALA   A C   1 
ATOM   917  O  O   . ALA   A 1 141 ? 0.880   -16.129 -12.889 1.00 26.59  ? 146 ALA   A O   1 
ATOM   918  C  CB  . ALA   A 1 141 ? 1.599   -17.860 -10.377 1.00 26.89  ? 146 ALA   A CB  1 
ATOM   919  N  N   . ASP   A 1 142 ? -1.132  -16.636 -11.978 1.00 25.67  ? 147 ASP   A N   1 
ATOM   920  C  CA  . ASP   A 1 142 ? -1.893  -16.532 -13.244 1.00 25.73  ? 147 ASP   A CA  1 
ATOM   921  C  C   . ASP   A 1 142 ? -1.229  -17.371 -14.354 1.00 29.85  ? 147 ASP   A C   1 
ATOM   922  O  O   . ASP   A 1 142 ? -1.153  -16.952 -15.517 1.00 29.82  ? 147 ASP   A O   1 
ATOM   923  C  CB  . ASP   A 1 142 ? -2.021  -15.050 -13.666 1.00 27.00  ? 147 ASP   A CB  1 
ATOM   924  C  CG  . ASP   A 1 142 ? -2.824  -14.191 -12.702 1.00 31.68  ? 147 ASP   A CG  1 
ATOM   925  O  OD1 . ASP   A 1 142 ? -3.297  -14.729 -11.680 1.00 30.29  ? 147 ASP   A OD1 1 
ATOM   926  O  OD2 . ASP   A 1 142 ? -2.976  -12.988 -12.974 1.00 34.50  ? 147 ASP   A OD2 1 
ATOM   927  N  N   . ILE   A 1 143 ? -0.689  -18.532 -13.955 1.00 27.49  ? 148 ILE   A N   1 
ATOM   928  C  CA  . ILE   A 1 143 ? 0.079   -19.380 -14.849 1.00 26.14  ? 148 ILE   A CA  1 
ATOM   929  C  C   . ILE   A 1 143 ? -0.540  -20.792 -15.007 1.00 29.65  ? 148 ILE   A C   1 
ATOM   930  O  O   . ILE   A 1 143 ? 0.129   -21.690 -15.525 1.00 30.05  ? 148 ILE   A O   1 
ATOM   931  C  CB  . ILE   A 1 143 ? 1.570   -19.400 -14.423 1.00 28.57  ? 148 ILE   A CB  1 
ATOM   932  C  CG1 . ILE   A 1 143 ? 2.508   -19.752 -15.625 1.00 28.62  ? 148 ILE   A CG1 1 
ATOM   933  C  CG2 . ILE   A 1 143 ? 1.827   -20.281 -13.179 1.00 28.29  ? 148 ILE   A CG2 1 
ATOM   934  C  CD1 . ILE   A 1 143 ? 3.977   -19.475 -15.376 1.00 37.14  ? 148 ILE   A CD1 1 
ATOM   935  N  N   . ASN   A 1 144 ? -1.810  -20.974 -14.627 1.00 27.39  ? 149 ASN   A N   1 
ATOM   936  C  CA  . ASN   A 1 144 ? -2.453  -22.264 -14.928 1.00 27.55  ? 149 ASN   A CA  1 
ATOM   937  C  C   . ASN   A 1 144 ? -2.552  -22.390 -16.448 1.00 31.83  ? 149 ASN   A C   1 
ATOM   938  O  O   . ASN   A 1 144 ? -2.734  -21.382 -17.124 1.00 29.94  ? 149 ASN   A O   1 
ATOM   939  C  CB  . ASN   A 1 144 ? -3.866  -22.348 -14.366 1.00 28.87  ? 149 ASN   A CB  1 
ATOM   940  C  CG  . ASN   A 1 144 ? -3.905  -22.891 -12.952 1.00 37.26  ? 149 ASN   A CG  1 
ATOM   941  O  OD1 . ASN   A 1 144 ? -3.344  -23.961 -12.639 1.00 32.10  ? 149 ASN   A OD1 1 
ATOM   942  N  ND2 . ASN   A 1 144 ? -4.466  -22.098 -12.058 1.00 32.17  ? 149 ASN   A ND2 1 
ATOM   943  N  N   . THR   A 1 145 ? -2.429  -23.612 -16.988 1.00 29.08  ? 150 THR   A N   1 
ATOM   944  C  CA  . THR   A 1 145 ? -2.651  -23.822 -18.425 1.00 28.93  ? 150 THR   A CA  1 
ATOM   945  C  C   . THR   A 1 145 ? -4.161  -24.126 -18.542 1.00 34.25  ? 150 THR   A C   1 
ATOM   946  O  O   . THR   A 1 145 ? -4.790  -24.408 -17.518 1.00 32.33  ? 150 THR   A O   1 
ATOM   947  C  CB  . THR   A 1 145 ? -1.848  -25.027 -18.957 1.00 34.05  ? 150 THR   A CB  1 
ATOM   948  O  OG1 . THR   A 1 145 ? -2.431  -26.255 -18.485 1.00 32.87  ? 150 THR   A OG1 1 
ATOM   949  C  CG2 . THR   A 1 145 ? -0.345  -24.961 -18.656 1.00 31.67  ? 150 THR   A CG2 1 
ATOM   950  N  N   . PRO   A 1 146 ? -4.764  -24.171 -19.753 1.00 33.04  ? 151 PRO   A N   1 
ATOM   951  C  CA  . PRO   A 1 146 ? -6.175  -24.579 -19.851 1.00 33.20  ? 151 PRO   A CA  1 
ATOM   952  C  C   . PRO   A 1 146 ? -6.430  -26.021 -19.387 1.00 34.83  ? 151 PRO   A C   1 
ATOM   953  O  O   . PRO   A 1 146 ? -7.577  -26.371 -19.144 1.00 35.25  ? 151 PRO   A O   1 
ATOM   954  C  CB  . PRO   A 1 146 ? -6.485  -24.392 -21.340 1.00 35.15  ? 151 PRO   A CB  1 
ATOM   955  C  CG  . PRO   A 1 146 ? -5.482  -23.329 -21.783 1.00 38.08  ? 151 PRO   A CG  1 
ATOM   956  C  CD  . PRO   A 1 146 ? -4.243  -23.787 -21.084 1.00 33.88  ? 151 PRO   A CD  1 
ATOM   957  N  N   . LEU   A 1 147 ? -5.362  -26.818 -19.187 1.00 31.59  ? 152 LEU   A N   1 
ATOM   958  C  CA  . LEU   A 1 147 ? -5.465  -28.200 -18.684 1.00 31.64  ? 152 LEU   A CA  1 
ATOM   959  C  C   . LEU   A 1 147 ? -5.263  -28.312 -17.161 1.00 36.53  ? 152 LEU   A C   1 
ATOM   960  O  O   . LEU   A 1 147 ? -5.728  -29.295 -16.574 1.00 35.57  ? 152 LEU   A O   1 
ATOM   961  C  CB  . LEU   A 1 147 ? -4.513  -29.147 -19.417 1.00 31.18  ? 152 LEU   A CB  1 
ATOM   962  C  CG  . LEU   A 1 147 ? -4.613  -29.194 -20.953 1.00 35.17  ? 152 LEU   A CG  1 
ATOM   963  C  CD1 . LEU   A 1 147 ? -3.516  -30.032 -21.534 1.00 35.46  ? 152 LEU   A CD1 1 
ATOM   964  C  CD2 . LEU   A 1 147 ? -5.968  -29.669 -21.425 1.00 36.96  ? 152 LEU   A CD2 1 
ATOM   965  N  N   . THR   A 1 148 ? -4.540  -27.348 -16.527 1.00 31.99  ? 153 THR   A N   1 
ATOM   966  C  CA  . THR   A 1 148 ? -4.316  -27.389 -15.072 1.00 31.58  ? 153 THR   A CA  1 
ATOM   967  C  C   . THR   A 1 148 ? -5.359  -26.609 -14.291 1.00 35.41  ? 153 THR   A C   1 
ATOM   968  O  O   . THR   A 1 148 ? -5.540  -26.838 -13.087 1.00 33.48  ? 153 THR   A O   1 
ATOM   969  C  CB  . THR   A 1 148 ? -2.904  -26.946 -14.668 1.00 34.47  ? 153 THR   A CB  1 
ATOM   970  O  OG1 . THR   A 1 148 ? -2.756  -25.534 -14.845 1.00 32.53  ? 153 THR   A OG1 1 
ATOM   971  C  CG2 . THR   A 1 148 ? -1.812  -27.726 -15.360 1.00 31.92  ? 153 THR   A CG2 1 
ATOM   972  N  N   . THR   A 1 149 ? -6.042  -25.666 -14.966 1.00 31.54  ? 154 THR   A N   1 
ATOM   973  C  CA  . THR   A 1 149 ? -7.049  -24.851 -14.306 1.00 31.45  ? 154 THR   A CA  1 
ATOM   974  C  C   . THR   A 1 149 ? -8.206  -25.655 -13.681 1.00 37.69  ? 154 THR   A C   1 
ATOM   975  O  O   . THR   A 1 149 ? -8.669  -26.632 -14.270 1.00 36.57  ? 154 THR   A O   1 
ATOM   976  C  CB  . THR   A 1 149 ? -7.567  -23.774 -15.267 1.00 32.09  ? 154 THR   A CB  1 
ATOM   977  O  OG1 . THR   A 1 149 ? -8.472  -22.946 -14.560 1.00 28.82  ? 154 THR   A OG1 1 
ATOM   978  C  CG2 . THR   A 1 149 ? -8.255  -24.353 -16.490 1.00 30.31  ? 154 THR   A CG2 1 
ATOM   979  N  N   . SER   A 1 150 ? -8.659  -25.229 -12.489 1.00 37.16  ? 155 SER   A N   1 
ATOM   980  C  CA  . SER   A 1 150 ? -9.803  -25.826 -11.792 1.00 38.42  ? 155 SER   A CA  1 
ATOM   981  C  C   . SER   A 1 150 ? -11.038 -24.936 -11.958 1.00 41.71  ? 155 SER   A C   1 
ATOM   982  O  O   . SER   A 1 150 ? -12.167 -25.431 -11.921 1.00 41.55  ? 155 SER   A O   1 
ATOM   983  C  CB  . SER   A 1 150 ? -9.497  -25.997 -10.307 1.00 43.57  ? 155 SER   A CB  1 
ATOM   984  O  OG  . SER   A 1 150 ? -8.705  -27.152 -10.088 1.00 55.57  ? 155 SER   A OG  1 
ATOM   985  N  N   . SER   A 1 151 ? -10.824 -23.620 -12.135 1.00 36.16  ? 156 SER   A N   1 
ATOM   986  C  CA  . SER   A 1 151 ? -11.930 -22.670 -12.281 1.00 34.70  ? 156 SER   A CA  1 
ATOM   987  C  C   . SER   A 1 151 ? -12.380 -22.503 -13.719 1.00 38.59  ? 156 SER   A C   1 
ATOM   988  O  O   . SER   A 1 151 ? -13.547 -22.203 -13.949 1.00 40.13  ? 156 SER   A O   1 
ATOM   989  C  CB  . SER   A 1 151 ? -11.526 -21.302 -11.742 1.00 35.83  ? 156 SER   A CB  1 
ATOM   990  O  OG  . SER   A 1 151 ? -10.521 -20.773 -12.597 1.00 37.60  ? 156 SER   A OG  1 
ATOM   991  N  N   . GLY   A 1 152 ? -11.444 -22.617 -14.663 1.00 34.67  ? 157 GLY   A N   1 
ATOM   992  C  CA  . GLY   A 1 152 ? -11.728 -22.366 -16.071 1.00 34.65  ? 157 GLY   A CA  1 
ATOM   993  C  C   . GLY   A 1 152 ? -11.679 -20.884 -16.414 1.00 38.61  ? 157 GLY   A C   1 
ATOM   994  O  O   . GLY   A 1 152 ? -11.871 -20.513 -17.579 1.00 38.28  ? 157 GLY   A O   1 
ATOM   995  N  N   . ASN   A 1 153 ? -11.382 -20.019 -15.405 1.00 33.41  ? 158 ASN   A N   1 
ATOM   996  C  CA  . ASN   A 1 153 ? -11.309 -18.559 -15.572 1.00 32.14  ? 158 ASN   A CA  1 
ATOM   997  C  C   . ASN   A 1 153 ? -9.966  -18.170 -16.158 1.00 34.09  ? 158 ASN   A C   1 
ATOM   998  O  O   . ASN   A 1 153 ? -8.906  -18.511 -15.609 1.00 31.44  ? 158 ASN   A O   1 
ATOM   999  C  CB  . ASN   A 1 153 ? -11.598 -17.820 -14.257 1.00 31.74  ? 158 ASN   A CB  1 
ATOM   1000 C  CG  . ASN   A 1 153 ? -12.938 -18.144 -13.652 1.00 44.39  ? 158 ASN   A CG  1 
ATOM   1001 O  OD1 . ASN   A 1 153 ? -13.920 -18.425 -14.353 1.00 36.62  ? 158 ASN   A OD1 1 
ATOM   1002 N  ND2 . ASN   A 1 153 ? -13.011 -18.107 -12.336 1.00 37.87  ? 158 ASN   A ND2 1 
ATOM   1003 N  N   . LEU   A 1 154 ? -10.018 -17.506 -17.323 1.00 31.07  ? 159 LEU   A N   1 
ATOM   1004 C  CA  . LEU   A 1 154 ? -8.820  -17.172 -18.086 1.00 30.29  ? 159 LEU   A CA  1 
ATOM   1005 C  C   . LEU   A 1 154 ? -7.932  -16.116 -17.438 1.00 33.25  ? 159 LEU   A C   1 
ATOM   1006 O  O   . LEU   A 1 154 ? -6.763  -16.038 -17.824 1.00 32.36  ? 159 LEU   A O   1 
ATOM   1007 C  CB  . LEU   A 1 154 ? -9.155  -16.806 -19.543 1.00 30.54  ? 159 LEU   A CB  1 
ATOM   1008 C  CG  . LEU   A 1 154 ? -9.512  -18.054 -20.406 1.00 34.10  ? 159 LEU   A CG  1 
ATOM   1009 C  CD1 . LEU   A 1 154 ? -10.235 -17.670 -21.666 1.00 34.52  ? 159 LEU   A CD1 1 
ATOM   1010 C  CD2 . LEU   A 1 154 ? -8.270  -18.850 -20.794 1.00 33.98  ? 159 LEU   A CD2 1 
ATOM   1011 N  N   . HIS   A 1 155 ? -8.424  -15.386 -16.412 1.00 30.55  ? 160 HIS   A N   1 
ATOM   1012 C  CA  . HIS   A 1 155 ? -7.567  -14.421 -15.697 1.00 29.89  ? 160 HIS   A CA  1 
ATOM   1013 C  C   . HIS   A 1 155 ? -6.528  -15.142 -14.824 1.00 32.93  ? 160 HIS   A C   1 
ATOM   1014 O  O   . HIS   A 1 155 ? -5.546  -14.526 -14.416 1.00 31.99  ? 160 HIS   A O   1 
ATOM   1015 C  CB  . HIS   A 1 155 ? -8.383  -13.360 -14.914 1.00 30.51  ? 160 HIS   A CB  1 
ATOM   1016 C  CG  . HIS   A 1 155 ? -9.011  -13.828 -13.637 1.00 33.17  ? 160 HIS   A CG  1 
ATOM   1017 N  ND1 . HIS   A 1 155 ? -9.346  -12.928 -12.631 1.00 34.79  ? 160 HIS   A ND1 1 
ATOM   1018 C  CD2 . HIS   A 1 155 ? -9.363  -15.076 -13.238 1.00 33.54  ? 160 HIS   A CD2 1 
ATOM   1019 C  CE1 . HIS   A 1 155 ? -9.887  -13.656 -11.664 1.00 33.47  ? 160 HIS   A CE1 1 
ATOM   1020 N  NE2 . HIS   A 1 155 ? -9.909  -14.954 -11.984 1.00 33.30  ? 160 HIS   A NE2 1 
ATOM   1021 N  N   . GLY   A 1 156 ? -6.733  -16.445 -14.613 1.00 27.67  ? 161 GLY   A N   1 
ATOM   1022 C  CA  . GLY   A 1 156 ? -5.838  -17.306 -13.848 1.00 27.21  ? 161 GLY   A CA  1 
ATOM   1023 C  C   . GLY   A 1 156 ? -4.851  -18.067 -14.710 1.00 28.86  ? 161 GLY   A C   1 
ATOM   1024 O  O   . GLY   A 1 156 ? -4.061  -18.875 -14.201 1.00 28.87  ? 161 GLY   A O   1 
ATOM   1025 N  N   . GLN   A 1 157 ? -4.896  -17.821 -16.034 1.00 28.11  ? 162 GLN   A N   1 
ATOM   1026 C  CA  . GLN   A 1 157 ? -4.086  -18.514 -17.027 1.00 28.35  ? 162 GLN   A CA  1 
ATOM   1027 C  C   . GLN   A 1 157 ? -3.242  -17.635 -17.991 1.00 31.00  ? 162 GLN   A C   1 
ATOM   1028 O  O   . GLN   A 1 157 ? -2.586  -18.238 -18.852 1.00 28.73  ? 162 GLN   A O   1 
ATOM   1029 C  CB  . GLN   A 1 157 ? -5.058  -19.346 -17.904 1.00 29.88  ? 162 GLN   A CB  1 
ATOM   1030 C  CG  . GLN   A 1 157 ? -5.858  -20.394 -17.131 1.00 35.19  ? 162 GLN   A CG  1 
ATOM   1031 C  CD  . GLN   A 1 157 ? -6.912  -20.987 -18.008 1.00 36.69  ? 162 GLN   A CD  1 
ATOM   1032 O  OE1 . GLN   A 1 157 ? -6.613  -21.592 -19.043 1.00 32.47  ? 162 GLN   A OE1 1 
ATOM   1033 N  NE2 . GLN   A 1 157 ? -8.157  -20.740 -17.654 1.00 29.48  ? 162 GLN   A NE2 1 
ATOM   1034 N  N   . PRO   A 1 158 ? -3.247  -16.266 -17.964 1.00 28.38  ? 163 PRO   A N   1 
ATOM   1035 C  CA  . PRO   A 1 158 ? -2.593  -15.522 -19.064 1.00 29.04  ? 163 PRO   A CA  1 
ATOM   1036 C  C   . PRO   A 1 158 ? -1.141  -15.833 -19.334 1.00 30.76  ? 163 PRO   A C   1 
ATOM   1037 O  O   . PRO   A 1 158 ? -0.776  -15.939 -20.513 1.00 29.99  ? 163 PRO   A O   1 
ATOM   1038 C  CB  . PRO   A 1 158 ? -2.794  -14.045 -18.680 1.00 30.24  ? 163 PRO   A CB  1 
ATOM   1039 C  CG  . PRO   A 1 158 ? -3.003  -14.070 -17.171 1.00 33.34  ? 163 PRO   A CG  1 
ATOM   1040 C  CD  . PRO   A 1 158 ? -3.877  -15.316 -17.026 1.00 29.07  ? 163 PRO   A CD  1 
ATOM   1041 N  N   . VAL   A 1 159 ? -0.331  -16.033 -18.283 1.00 25.74  ? 164 VAL   A N   1 
ATOM   1042 C  CA  . VAL   A 1 159 ? 1.091   -16.296 -18.480 1.00 24.98  ? 164 VAL   A CA  1 
ATOM   1043 C  C   . VAL   A 1 159 ? 1.335   -17.616 -19.271 1.00 30.61  ? 164 VAL   A C   1 
ATOM   1044 O  O   . VAL   A 1 159 ? 2.349   -17.717 -19.964 1.00 29.34  ? 164 VAL   A O   1 
ATOM   1045 C  CB  . VAL   A 1 159 ? 1.881   -16.229 -17.150 1.00 28.23  ? 164 VAL   A CB  1 
ATOM   1046 C  CG1 . VAL   A 1 159 ? 3.372   -16.465 -17.358 1.00 27.97  ? 164 VAL   A CG1 1 
ATOM   1047 C  CG2 . VAL   A 1 159 ? 1.660   -14.888 -16.457 1.00 28.09  ? 164 VAL   A CG2 1 
ATOM   1048 N  N   . SER   A 1 160 ? 0.420   -18.613 -19.156 1.00 28.54  ? 165 SER   A N   1 
ATOM   1049 C  CA  . SER   A 1 160 ? 0.619   -19.894 -19.842 1.00 28.38  ? 165 SER   A CA  1 
ATOM   1050 C  C   . SER   A 1 160 ? 0.666   -19.773 -21.377 1.00 32.51  ? 165 SER   A C   1 
ATOM   1051 O  O   . SER   A 1 160 ? 1.400   -20.529 -22.016 1.00 30.95  ? 165 SER   A O   1 
ATOM   1052 C  CB  . SER   A 1 160 ? -0.422  -20.923 -19.407 1.00 29.88  ? 165 SER   A CB  1 
ATOM   1053 O  OG  . SER   A 1 160 ? -1.697  -20.697 -19.984 1.00 30.11  ? 165 SER   A OG  1 
ATOM   1054 N  N   . PHE   A 1 161 ? -0.058  -18.788 -21.934 1.00 29.48  ? 166 PHE   A N   1 
ATOM   1055 C  CA  . PHE   A 1 161 ? -0.115  -18.525 -23.378 1.00 30.17  ? 166 PHE   A CA  1 
ATOM   1056 C  C   . PHE   A 1 161 ? 1.078   -17.715 -23.875 1.00 33.03  ? 166 PHE   A C   1 
ATOM   1057 O  O   . PHE   A 1 161 ? 1.374   -17.724 -25.084 1.00 31.85  ? 166 PHE   A O   1 
ATOM   1058 C  CB  . PHE   A 1 161 ? -1.413  -17.788 -23.732 1.00 31.57  ? 166 PHE   A CB  1 
ATOM   1059 C  CG  . PHE   A 1 161 ? -2.670  -18.447 -23.225 1.00 33.54  ? 166 PHE   A CG  1 
ATOM   1060 C  CD1 . PHE   A 1 161 ? -3.211  -19.550 -23.882 1.00 36.09  ? 166 PHE   A CD1 1 
ATOM   1061 C  CD2 . PHE   A 1 161 ? -3.314  -17.973 -22.086 1.00 34.07  ? 166 PHE   A CD2 1 
ATOM   1062 C  CE1 . PHE   A 1 161 ? -4.369  -20.171 -23.399 1.00 37.44  ? 166 PHE   A CE1 1 
ATOM   1063 C  CE2 . PHE   A 1 161 ? -4.482  -18.583 -21.616 1.00 35.82  ? 166 PHE   A CE2 1 
ATOM   1064 C  CZ  . PHE   A 1 161 ? -4.990  -19.689 -22.266 1.00 34.86  ? 166 PHE   A CZ  1 
ATOM   1065 N  N   . LEU   A 1 162 ? 1.755   -16.992 -22.954 1.00 28.58  ? 167 LEU   A N   1 
ATOM   1066 C  CA  . LEU   A 1 162 ? 2.871   -16.150 -23.338 1.00 27.32  ? 167 LEU   A CA  1 
ATOM   1067 C  C   . LEU   A 1 162 ? 4.229   -16.809 -23.209 1.00 29.88  ? 167 LEU   A C   1 
ATOM   1068 O  O   . LEU   A 1 162 ? 5.165   -16.367 -23.863 1.00 30.48  ? 167 LEU   A O   1 
ATOM   1069 C  CB  . LEU   A 1 162 ? 2.828   -14.825 -22.542 1.00 26.72  ? 167 LEU   A CB  1 
ATOM   1070 C  CG  . LEU   A 1 162 ? 1.496   -14.067 -22.527 1.00 30.84  ? 167 LEU   A CG  1 
ATOM   1071 C  CD1 . LEU   A 1 162 ? 1.484   -13.048 -21.403 1.00 30.93  ? 167 LEU   A CD1 1 
ATOM   1072 C  CD2 . LEU   A 1 162 ? 1.208   -13.377 -23.880 1.00 34.17  ? 167 LEU   A CD2 1 
ATOM   1073 N  N   . LEU   A 1 163 ? 4.364   -17.798 -22.327 1.00 28.14  ? 168 LEU   A N   1 
ATOM   1074 C  CA  . LEU   A 1 163 ? 5.629   -18.453 -22.030 1.00 28.47  ? 168 LEU   A CA  1 
ATOM   1075 C  C   . LEU   A 1 163 ? 6.004   -19.477 -23.086 1.00 33.29  ? 168 LEU   A C   1 
ATOM   1076 O  O   . LEU   A 1 163 ? 5.247   -20.423 -23.321 1.00 31.42  ? 168 LEU   A O   1 
ATOM   1077 C  CB  . LEU   A 1 163 ? 5.595   -19.108 -20.642 1.00 28.96  ? 168 LEU   A CB  1 
ATOM   1078 C  CG  . LEU   A 1 163 ? 6.935   -19.213 -19.950 1.00 34.46  ? 168 LEU   A CG  1 
ATOM   1079 C  CD1 . LEU   A 1 163 ? 7.316   -17.868 -19.311 1.00 34.00  ? 168 LEU   A CD1 1 
ATOM   1080 C  CD2 . LEU   A 1 163 ? 6.889   -20.283 -18.868 1.00 36.39  ? 168 LEU   A CD2 1 
ATOM   1081 N  N   . ARG   A 1 164 ? 7.180   -19.282 -23.719 1.00 30.81  ? 169 ARG   A N   1 
ATOM   1082 C  CA  . ARG   A 1 164 ? 7.666   -20.171 -24.793 1.00 30.50  ? 169 ARG   A CA  1 
ATOM   1083 C  C   . ARG   A 1 164 ? 7.755   -21.639 -24.344 1.00 34.69  ? 169 ARG   A C   1 
ATOM   1084 O  O   . ARG   A 1 164 ? 7.301   -22.525 -25.067 1.00 35.53  ? 169 ARG   A O   1 
ATOM   1085 C  CB  . ARG   A 1 164 ? 9.031   -19.708 -25.328 1.00 30.69  ? 169 ARG   A CB  1 
ATOM   1086 C  CG  . ARG   A 1 164 ? 9.004   -18.370 -26.090 1.00 34.32  ? 169 ARG   A CG  1 
ATOM   1087 C  CD  . ARG   A 1 164 ? 10.357  -18.104 -26.726 1.00 42.31  ? 169 ARG   A CD  1 
ATOM   1088 N  NE  . ARG   A 1 164 ? 10.773  -16.698 -26.660 1.00 55.99  ? 169 ARG   A NE  1 
ATOM   1089 C  CZ  . ARG   A 1 164 ? 10.476  -15.772 -27.568 1.00 70.15  ? 169 ARG   A CZ  1 
ATOM   1090 N  NH1 . ARG   A 1 164 ? 9.728   -16.079 -28.623 1.00 68.32  ? 169 ARG   A NH1 1 
ATOM   1091 N  NH2 . ARG   A 1 164 ? 10.921  -14.530 -27.427 1.00 42.33  ? 169 ARG   A NH2 1 
ATOM   1092 N  N   . GLU   A 1 165 ? 8.309   -21.876 -23.147 1.00 29.96  ? 170 GLU   A N   1 
ATOM   1093 C  CA  . GLU   A 1 165 ? 8.543   -23.209 -22.567 1.00 29.91  ? 170 GLU   A CA  1 
ATOM   1094 C  C   . GLU   A 1 165 ? 7.273   -24.006 -22.307 1.00 34.67  ? 170 GLU   A C   1 
ATOM   1095 O  O   . GLU   A 1 165 ? 7.352   -25.233 -22.238 1.00 34.47  ? 170 GLU   A O   1 
ATOM   1096 C  CB  . GLU   A 1 165 ? 9.403   -23.128 -21.299 1.00 30.90  ? 170 GLU   A CB  1 
ATOM   1097 C  CG  . GLU   A 1 165 ? 10.828  -22.643 -21.516 1.00 37.21  ? 170 GLU   A CG  1 
ATOM   1098 C  CD  . GLU   A 1 165 ? 11.004  -21.128 -21.543 1.00 49.73  ? 170 GLU   A CD  1 
ATOM   1099 O  OE1 . GLU   A 1 165 ? 9.989   -20.394 -21.501 1.00 35.12  ? 170 GLU   A OE1 1 
ATOM   1100 O  OE2 . GLU   A 1 165 ? 12.167  -20.678 -21.633 1.00 42.70  ? 170 GLU   A OE2 1 
ATOM   1101 N  N   . LEU   A 1 166 ? 6.118   -23.345 -22.200 1.00 31.62  ? 171 LEU   A N   1 
ATOM   1102 C  CA  . LEU   A 1 166 ? 4.835   -24.021 -21.947 1.00 32.34  ? 171 LEU   A CA  1 
ATOM   1103 C  C   . LEU   A 1 166 ? 4.011   -24.306 -23.220 1.00 35.23  ? 171 LEU   A C   1 
ATOM   1104 O  O   . LEU   A 1 166 ? 2.892   -24.817 -23.111 1.00 33.64  ? 171 LEU   A O   1 
ATOM   1105 C  CB  . LEU   A 1 166 ? 3.970   -23.199 -20.958 1.00 32.55  ? 171 LEU   A CB  1 
ATOM   1106 C  CG  . LEU   A 1 166 ? 4.376   -23.228 -19.471 1.00 36.90  ? 171 LEU   A CG  1 
ATOM   1107 C  CD1 . LEU   A 1 166 ? 3.612   -22.178 -18.697 1.00 36.06  ? 171 LEU   A CD1 1 
ATOM   1108 C  CD2 . LEU   A 1 166 ? 4.157   -24.634 -18.840 1.00 38.06  ? 171 LEU   A CD2 1 
ATOM   1109 N  N   . GLN   A 1 167 ? 4.530   -23.933 -24.413 1.00 32.60  ? 172 GLN   A N   1 
ATOM   1110 C  CA  . GLN   A 1 167 ? 3.789   -24.081 -25.667 1.00 33.15  ? 172 GLN   A CA  1 
ATOM   1111 C  C   . GLN   A 1 167 ? 3.249   -25.495 -25.874 1.00 36.75  ? 172 GLN   A C   1 
ATOM   1112 O  O   . GLN   A 1 167 ? 2.065   -25.636 -26.123 1.00 36.72  ? 172 GLN   A O   1 
ATOM   1113 C  CB  . GLN   A 1 167 ? 4.605   -23.601 -26.881 1.00 34.15  ? 172 GLN   A CB  1 
ATOM   1114 C  CG  . GLN   A 1 167 ? 3.752   -23.490 -28.155 1.00 47.75  ? 172 GLN   A CG  1 
ATOM   1115 C  CD  . GLN   A 1 167 ? 4.408   -22.708 -29.270 1.00 60.48  ? 172 GLN   A CD  1 
ATOM   1116 O  OE1 . GLN   A 1 167 ? 5.637   -22.665 -29.410 1.00 50.65  ? 172 GLN   A OE1 1 
ATOM   1117 N  NE2 . GLN   A 1 167 ? 3.590   -22.075 -30.096 1.00 58.04  ? 172 GLN   A NE2 1 
ATOM   1118 N  N   . ASP   A 1 168 ? 4.091   -26.513 -25.686 1.00 37.66  ? 173 ASP   A N   1 
ATOM   1119 C  CA  . ASP   A 1 168 ? 3.700   -27.923 -25.847 1.00 38.70  ? 173 ASP   A CA  1 
ATOM   1120 C  C   . ASP   A 1 168 ? 2.727   -28.410 -24.762 1.00 43.31  ? 173 ASP   A C   1 
ATOM   1121 O  O   . ASP   A 1 168 ? 2.135   -29.480 -24.918 1.00 42.82  ? 173 ASP   A O   1 
ATOM   1122 C  CB  . ASP   A 1 168 ? 4.942   -28.826 -25.927 1.00 41.81  ? 173 ASP   A CB  1 
ATOM   1123 C  CG  . ASP   A 1 168 ? 5.753   -28.915 -24.653 1.00 62.79  ? 173 ASP   A CG  1 
ATOM   1124 O  OD1 . ASP   A 1 168 ? 5.803   -27.906 -23.907 1.00 66.49  ? 173 ASP   A OD1 1 
ATOM   1125 O  OD2 . ASP   A 1 168 ? 6.364   -29.983 -24.413 1.00 69.06  ? 173 ASP   A OD2 1 
ATOM   1126 N  N   . LYS   A 1 169 ? 2.551   -27.628 -23.671 1.00 37.80  ? 174 LYS   A N   1 
ATOM   1127 C  CA  . LYS   A 1 169 ? 1.616   -27.994 -22.602 1.00 36.11  ? 174 LYS   A CA  1 
ATOM   1128 C  C   . LYS   A 1 169 ? 0.298   -27.242 -22.749 1.00 36.84  ? 174 LYS   A C   1 
ATOM   1129 O  O   . LYS   A 1 169 ? -0.616  -27.475 -21.971 1.00 36.06  ? 174 LYS   A O   1 
ATOM   1130 C  CB  . LYS   A 1 169 ? 2.221   -27.714 -21.199 1.00 36.76  ? 174 LYS   A CB  1 
ATOM   1131 C  CG  . LYS   A 1 169 ? 3.605   -28.296 -20.943 1.00 41.80  ? 174 LYS   A CG  1 
ATOM   1132 C  CD  . LYS   A 1 169 ? 3.622   -29.843 -20.907 1.00 44.48  ? 174 LYS   A CD  1 
ATOM   1133 C  CE  . LYS   A 1 169 ? 5.034   -30.355 -20.751 1.00 54.09  ? 174 LYS   A CE  1 
ATOM   1134 N  NZ  . LYS   A 1 169 ? 5.133   -31.818 -20.973 1.00 61.80  ? 174 LYS   A NZ  1 
ATOM   1135 N  N   . VAL   A 1 170 ? 0.183   -26.336 -23.742 1.00 32.21  ? 175 VAL   A N   1 
ATOM   1136 C  CA  . VAL   A 1 170 ? -1.019  -25.515 -23.872 1.00 31.20  ? 175 VAL   A CA  1 
ATOM   1137 C  C   . VAL   A 1 170 ? -1.891  -25.903 -25.082 1.00 37.26  ? 175 VAL   A C   1 
ATOM   1138 O  O   . VAL   A 1 170 ? -1.419  -25.790 -26.215 1.00 38.90  ? 175 VAL   A O   1 
ATOM   1139 C  CB  . VAL   A 1 170 ? -0.623  -23.996 -23.876 1.00 34.04  ? 175 VAL   A CB  1 
ATOM   1140 C  CG1 . VAL   A 1 170 ? -1.804  -23.086 -24.229 1.00 32.87  ? 175 VAL   A CG1 1 
ATOM   1141 C  CG2 . VAL   A 1 170 ? -0.019  -23.587 -22.526 1.00 33.83  ? 175 VAL   A CG2 1 
ATOM   1142 N  N   . PRO   A 1 171 ? -3.166  -26.330 -24.891 1.00 35.47  ? 176 PRO   A N   1 
ATOM   1143 C  CA  . PRO   A 1 171 ? -4.007  -26.634 -26.066 1.00 36.60  ? 176 PRO   A CA  1 
ATOM   1144 C  C   . PRO   A 1 171 ? -4.450  -25.357 -26.791 1.00 42.38  ? 176 PRO   A C   1 
ATOM   1145 O  O   . PRO   A 1 171 ? -4.478  -24.280 -26.190 1.00 39.47  ? 176 PRO   A O   1 
ATOM   1146 C  CB  . PRO   A 1 171 ? -5.217  -27.339 -25.462 1.00 38.44  ? 176 PRO   A CB  1 
ATOM   1147 C  CG  . PRO   A 1 171 ? -5.315  -26.792 -24.079 1.00 42.14  ? 176 PRO   A CG  1 
ATOM   1148 C  CD  . PRO   A 1 171 ? -3.906  -26.545 -23.629 1.00 37.44  ? 176 PRO   A CD  1 
ATOM   1149 N  N   . GLN   A 1 172 ? -4.801  -25.488 -28.085 1.00 42.55  ? 177 GLN   A N   1 
ATOM   1150 C  CA  . GLN   A 1 172 ? -5.279  -24.377 -28.896 1.00 42.79  ? 177 GLN   A CA  1 
ATOM   1151 C  C   . GLN   A 1 172 ? -6.741  -24.154 -28.562 1.00 45.23  ? 177 GLN   A C   1 
ATOM   1152 O  O   . GLN   A 1 172 ? -7.575  -25.036 -28.795 1.00 46.75  ? 177 GLN   A O   1 
ATOM   1153 C  CB  . GLN   A 1 172 ? -5.071  -24.657 -30.400 1.00 45.21  ? 177 GLN   A CB  1 
ATOM   1154 C  CG  . GLN   A 1 172 ? -4.020  -23.755 -31.051 1.00 66.37  ? 177 GLN   A CG  1 
ATOM   1155 C  CD  . GLN   A 1 172 ? -4.280  -23.534 -32.529 1.00 93.77  ? 177 GLN   A CD  1 
ATOM   1156 O  OE1 . GLN   A 1 172 ? -3.589  -24.084 -33.394 1.00 91.26  ? 177 GLN   A OE1 1 
ATOM   1157 N  NE2 . GLN   A 1 172 ? -5.278  -22.716 -32.855 1.00 85.33  ? 177 GLN   A NE2 1 
ATOM   1158 N  N   . LEU   A 1 173 ? -7.039  -23.014 -27.924 1.00 37.49  ? 178 LEU   A N   1 
ATOM   1159 C  CA  . LEU   A 1 173 ? -8.394  -22.634 -27.528 1.00 35.52  ? 178 LEU   A CA  1 
ATOM   1160 C  C   . LEU   A 1 173 ? -9.061  -21.854 -28.675 1.00 40.24  ? 178 LEU   A C   1 
ATOM   1161 O  O   . LEU   A 1 173 ? -8.342  -21.174 -29.416 1.00 39.21  ? 178 LEU   A O   1 
ATOM   1162 C  CB  . LEU   A 1 173 ? -8.300  -21.701 -26.304 1.00 34.89  ? 178 LEU   A CB  1 
ATOM   1163 C  CG  . LEU   A 1 173 ? -8.616  -22.219 -24.899 1.00 39.66  ? 178 LEU   A CG  1 
ATOM   1164 C  CD1 . LEU   A 1 173 ? -8.222  -23.671 -24.689 1.00 39.61  ? 178 LEU   A CD1 1 
ATOM   1165 C  CD2 . LEU   A 1 173 ? -7.974  -21.312 -23.844 1.00 37.71  ? 178 LEU   A CD2 1 
ATOM   1166 N  N   . PRO   A 1 174 ? -10.415 -21.860 -28.802 1.00 39.57  ? 179 PRO   A N   1 
ATOM   1167 C  CA  . PRO   A 1 174 ? -11.044 -21.043 -29.857 1.00 39.68  ? 179 PRO   A CA  1 
ATOM   1168 C  C   . PRO   A 1 174 ? -10.804 -19.553 -29.601 1.00 42.76  ? 179 PRO   A C   1 
ATOM   1169 O  O   . PRO   A 1 174 ? -11.010 -19.077 -28.475 1.00 42.06  ? 179 PRO   A O   1 
ATOM   1170 C  CB  . PRO   A 1 174 ? -12.528 -21.402 -29.770 1.00 41.61  ? 179 PRO   A CB  1 
ATOM   1171 C  CG  . PRO   A 1 174 ? -12.722 -21.974 -28.413 1.00 46.76  ? 179 PRO   A CG  1 
ATOM   1172 C  CD  . PRO   A 1 174 ? -11.427 -22.611 -28.023 1.00 42.21  ? 179 PRO   A CD  1 
ATOM   1173 N  N   . GLY   A 1 175 ? -10.318 -18.862 -30.634 1.00 38.34  ? 180 GLY   A N   1 
ATOM   1174 C  CA  . GLY   A 1 175 ? -10.006 -17.436 -30.601 1.00 36.89  ? 180 GLY   A CA  1 
ATOM   1175 C  C   . GLY   A 1 175 ? -8.596  -17.101 -30.160 1.00 39.00  ? 180 GLY   A C   1 
ATOM   1176 O  O   . GLY   A 1 175 ? -8.227  -15.926 -30.140 1.00 39.01  ? 180 GLY   A O   1 
ATOM   1177 N  N   . PHE   A 1 176 ? -7.790  -18.122 -29.812 1.00 34.85  ? 181 PHE   A N   1 
ATOM   1178 C  CA  . PHE   A 1 176 ? -6.421  -17.963 -29.324 1.00 34.37  ? 181 PHE   A CA  1 
ATOM   1179 C  C   . PHE   A 1 176 ? -5.327  -18.257 -30.366 1.00 38.93  ? 181 PHE   A C   1 
ATOM   1180 O  O   . PHE   A 1 176 ? -4.143  -18.205 -30.020 1.00 38.59  ? 181 PHE   A O   1 
ATOM   1181 C  CB  . PHE   A 1 176 ? -6.225  -18.850 -28.069 1.00 36.29  ? 181 PHE   A CB  1 
ATOM   1182 C  CG  . PHE   A 1 176 ? -6.722  -18.247 -26.778 1.00 37.63  ? 181 PHE   A CG  1 
ATOM   1183 C  CD1 . PHE   A 1 176 ? -8.082  -18.053 -26.557 1.00 40.02  ? 181 PHE   A CD1 1 
ATOM   1184 C  CD2 . PHE   A 1 176 ? -5.835  -17.932 -25.752 1.00 39.00  ? 181 PHE   A CD2 1 
ATOM   1185 C  CE1 . PHE   A 1 176 ? -8.539  -17.488 -25.360 1.00 41.04  ? 181 PHE   A CE1 1 
ATOM   1186 C  CE2 . PHE   A 1 176 ? -6.293  -17.351 -24.563 1.00 40.93  ? 181 PHE   A CE2 1 
ATOM   1187 C  CZ  . PHE   A 1 176 ? -7.638  -17.142 -24.373 1.00 39.09  ? 181 PHE   A CZ  1 
ATOM   1188 N  N   . SER   A 1 177 ? -5.704  -18.565 -31.636 1.00 37.83  ? 182 SER   A N   1 
ATOM   1189 C  CA  . SER   A 1 177 ? -4.732  -18.922 -32.681 1.00 38.04  ? 182 SER   A CA  1 
ATOM   1190 C  C   . SER   A 1 177 ? -3.719  -17.826 -33.008 1.00 42.32  ? 182 SER   A C   1 
ATOM   1191 O  O   . SER   A 1 177 ? -2.571  -18.139 -33.328 1.00 43.28  ? 182 SER   A O   1 
ATOM   1192 C  CB  . SER   A 1 177 ? -5.432  -19.407 -33.951 1.00 41.22  ? 182 SER   A CB  1 
ATOM   1193 O  OG  . SER   A 1 177 ? -6.347  -18.451 -34.458 1.00 48.38  ? 182 SER   A OG  1 
ATOM   1194 N  N   . TRP   A 1 178 ? -4.122  -16.557 -32.878 1.00 39.15  ? 183 TRP   A N   1 
ATOM   1195 C  CA  . TRP   A 1 178 ? -3.268  -15.399 -33.146 1.00 39.59  ? 183 TRP   A CA  1 
ATOM   1196 C  C   . TRP   A 1 178 ? -2.090  -15.224 -32.149 1.00 42.40  ? 183 TRP   A C   1 
ATOM   1197 O  O   . TRP   A 1 178 ? -1.116  -14.559 -32.494 1.00 42.13  ? 183 TRP   A O   1 
ATOM   1198 C  CB  . TRP   A 1 178 ? -4.124  -14.131 -33.179 1.00 38.65  ? 183 TRP   A CB  1 
ATOM   1199 C  CG  . TRP   A 1 178 ? -4.659  -13.760 -31.822 1.00 39.65  ? 183 TRP   A CG  1 
ATOM   1200 C  CD1 . TRP   A 1 178 ? -5.805  -14.218 -31.239 1.00 42.53  ? 183 TRP   A CD1 1 
ATOM   1201 C  CD2 . TRP   A 1 178 ? -4.025  -12.909 -30.853 1.00 39.28  ? 183 TRP   A CD2 1 
ATOM   1202 N  NE1 . TRP   A 1 178 ? -5.941  -13.681 -29.978 1.00 41.96  ? 183 TRP   A NE1 1 
ATOM   1203 C  CE2 . TRP   A 1 178 ? -4.856  -12.887 -29.709 1.00 43.12  ? 183 TRP   A CE2 1 
ATOM   1204 C  CE3 . TRP   A 1 178 ? -2.824  -12.173 -30.835 1.00 40.06  ? 183 TRP   A CE3 1 
ATOM   1205 C  CZ2 . TRP   A 1 178 ? -4.520  -12.165 -28.551 1.00 42.16  ? 183 TRP   A CZ2 1 
ATOM   1206 C  CZ3 . TRP   A 1 178 ? -2.505  -11.440 -29.697 1.00 41.54  ? 183 TRP   A CZ3 1 
ATOM   1207 C  CH2 . TRP   A 1 178 ? -3.362  -11.416 -28.586 1.00 42.02  ? 183 TRP   A CH2 1 
ATOM   1208 N  N   . ILE   A 1 179 ? -2.183  -15.781 -30.917 1.00 39.02  ? 184 ILE   A N   1 
ATOM   1209 C  CA  . ILE   A 1 179 ? -1.129  -15.598 -29.902 1.00 39.00  ? 184 ILE   A CA  1 
ATOM   1210 C  C   . ILE   A 1 179 ? 0.154   -16.361 -30.236 1.00 44.46  ? 184 ILE   A C   1 
ATOM   1211 O  O   . ILE   A 1 179 ? 0.122   -17.564 -30.485 1.00 46.37  ? 184 ILE   A O   1 
ATOM   1212 C  CB  . ILE   A 1 179 ? -1.633  -15.915 -28.452 1.00 41.87  ? 184 ILE   A CB  1 
ATOM   1213 C  CG1 . ILE   A 1 179 ? -2.811  -15.032 -28.081 1.00 42.57  ? 184 ILE   A CG1 1 
ATOM   1214 C  CG2 . ILE   A 1 179 ? -0.529  -15.747 -27.386 1.00 42.15  ? 184 ILE   A CG2 1 
ATOM   1215 C  CD1 . ILE   A 1 179 ? -3.913  -15.713 -27.444 1.00 51.24  ? 184 ILE   A CD1 1 
ATOM   1216 N  N   . LYS   A 1 180 ? 1.281   -15.653 -30.203 1.00 40.57  ? 185 LYS   A N   1 
ATOM   1217 C  CA  . LYS   A 1 180 ? 2.609   -16.228 -30.397 1.00 40.75  ? 185 LYS   A CA  1 
ATOM   1218 C  C   . LYS   A 1 180 ? 3.349   -16.162 -29.038 1.00 42.13  ? 185 LYS   A C   1 
ATOM   1219 O  O   . LYS   A 1 180 ? 3.542   -15.051 -28.557 1.00 40.21  ? 185 LYS   A O   1 
ATOM   1220 C  CB  . LYS   A 1 180 ? 3.394   -15.431 -31.471 1.00 44.83  ? 185 LYS   A CB  1 
ATOM   1221 C  CG  . LYS   A 1 180 ? 2.911   -15.674 -32.902 1.00 70.53  ? 185 LYS   A CG  1 
ATOM   1222 C  CD  . LYS   A 1 180 ? 3.365   -14.574 -33.866 1.00 82.36  ? 185 LYS   A CD  1 
ATOM   1223 C  CE  . LYS   A 1 180 ? 3.048   -14.886 -35.316 1.00 94.55  ? 185 LYS   A CE  1 
ATOM   1224 N  NZ  . LYS   A 1 180 ? 1.592   -14.801 -35.617 1.00 104.04 ? 185 LYS   A NZ  1 
ATOM   1225 N  N   . PRO   A 1 181 ? 3.762   -17.289 -28.384 1.00 39.01  ? 186 PRO   A N   1 
ATOM   1226 C  CA  . PRO   A 1 181 ? 4.551   -17.162 -27.134 1.00 38.09  ? 186 PRO   A CA  1 
ATOM   1227 C  C   . PRO   A 1 181 ? 5.706   -16.183 -27.367 1.00 39.99  ? 186 PRO   A C   1 
ATOM   1228 O  O   . PRO   A 1 181 ? 6.348   -16.236 -28.424 1.00 39.43  ? 186 PRO   A O   1 
ATOM   1229 C  CB  . PRO   A 1 181 ? 5.048   -18.587 -26.877 1.00 40.02  ? 186 PRO   A CB  1 
ATOM   1230 C  CG  . PRO   A 1 181 ? 4.054   -19.456 -27.559 1.00 44.43  ? 186 PRO   A CG  1 
ATOM   1231 C  CD  . PRO   A 1 181 ? 3.623   -18.706 -28.785 1.00 40.06  ? 186 PRO   A CD  1 
ATOM   1232 N  N   . CYS   A 1 182 ? 5.901   -15.226 -26.446 1.00 34.47  ? 187 CYS   A N   1 
ATOM   1233 C  CA  . CYS   A 1 182 ? 6.869   -14.143 -26.656 1.00 34.65  ? 187 CYS   A CA  1 
ATOM   1234 C  C   . CYS   A 1 182 ? 7.787   -13.854 -25.474 1.00 39.46  ? 187 CYS   A C   1 
ATOM   1235 O  O   . CYS   A 1 182 ? 8.554   -12.879 -25.521 1.00 39.08  ? 187 CYS   A O   1 
ATOM   1236 C  CB  . CYS   A 1 182 ? 6.119   -12.888 -27.084 1.00 34.62  ? 187 CYS   A CB  1 
ATOM   1237 S  SG  . CYS   A 1 182 ? 4.762   -12.429 -25.969 1.00 38.06  ? 187 CYS   A SG  1 
ATOM   1238 N  N   . ILE   A 1 183 ? 7.686   -14.643 -24.399 1.00 34.50  ? 188 ILE   A N   1 
ATOM   1239 C  CA  . ILE   A 1 183 ? 8.540   -14.464 -23.232 1.00 35.22  ? 188 ILE   A CA  1 
ATOM   1240 C  C   . ILE   A 1 183 ? 9.108   -15.801 -22.780 1.00 35.25  ? 188 ILE   A C   1 
ATOM   1241 O  O   . ILE   A 1 183 ? 8.423   -16.818 -22.866 1.00 34.11  ? 188 ILE   A O   1 
ATOM   1242 C  CB  . ILE   A 1 183 ? 7.864   -13.652 -22.068 1.00 39.68  ? 188 ILE   A CB  1 
ATOM   1243 C  CG1 . ILE   A 1 183 ? 6.528   -14.260 -21.614 1.00 40.07  ? 188 ILE   A CG1 1 
ATOM   1244 C  CG2 . ILE   A 1 183 ? 7.699   -12.162 -22.427 1.00 42.13  ? 188 ILE   A CG2 1 
ATOM   1245 C  CD1 . ILE   A 1 183 ? 6.104   -13.851 -20.173 1.00 45.98  ? 188 ILE   A CD1 1 
ATOM   1246 N  N   . SER   A 1 184 ? 10.370  -15.814 -22.358 1.00 31.04  ? 189 SER   A N   1 
ATOM   1247 C  CA  . SER   A 1 184 ? 10.983  -17.025 -21.861 1.00 31.25  ? 189 SER   A CA  1 
ATOM   1248 C  C   . SER   A 1 184 ? 10.871  -17.037 -20.351 1.00 32.90  ? 189 SER   A C   1 
ATOM   1249 O  O   . SER   A 1 184 ? 10.719  -15.976 -19.720 1.00 30.56  ? 189 SER   A O   1 
ATOM   1250 C  CB  . SER   A 1 184 ? 12.440  -17.154 -22.309 1.00 36.39  ? 189 SER   A CB  1 
ATOM   1251 O  OG  . SER   A 1 184 ? 13.320  -16.306 -21.588 1.00 51.07  ? 189 SER   A OG  1 
ATOM   1252 N  N   . SER   A 1 185 ? 10.993  -18.229 -19.775 1.00 31.58  ? 190 SER   A N   1 
ATOM   1253 C  CA  . SER   A 1 185 ? 10.932  -18.463 -18.334 1.00 30.95  ? 190 SER   A CA  1 
ATOM   1254 C  C   . SER   A 1 185 ? 11.897  -17.572 -17.515 1.00 33.39  ? 190 SER   A C   1 
ATOM   1255 O  O   . SER   A 1 185 ? 11.523  -17.137 -16.424 1.00 33.65  ? 190 SER   A O   1 
ATOM   1256 C  CB  . SER   A 1 185 ? 11.151  -19.952 -18.048 1.00 33.51  ? 190 SER   A CB  1 
ATOM   1257 O  OG  . SER   A 1 185 ? 12.512  -20.308 -18.217 1.00 40.64  ? 190 SER   A OG  1 
ATOM   1258 N  N   . ALA   A 1 186 ? 13.107  -17.264 -18.034 1.00 29.61  ? 191 ALA   A N   1 
ATOM   1259 C  CA  . ALA   A 1 186 ? 14.095  -16.442 -17.333 1.00 29.88  ? 191 ALA   A CA  1 
ATOM   1260 C  C   . ALA   A 1 186 ? 13.780  -14.933 -17.440 1.00 28.59  ? 191 ALA   A C   1 
ATOM   1261 O  O   . ALA   A 1 186 ? 14.488  -14.123 -16.849 1.00 29.31  ? 191 ALA   A O   1 
ATOM   1262 C  CB  . ALA   A 1 186 ? 15.499  -16.711 -17.900 1.00 31.42  ? 191 ALA   A CB  1 
ATOM   1263 N  N   . SER   A 1 187 ? 12.727  -14.576 -18.202 1.00 24.93  ? 192 SER   A N   1 
ATOM   1264 C  CA  . SER   A 1 187 ? 12.398  -13.179 -18.495 1.00 24.54  ? 192 SER   A CA  1 
ATOM   1265 C  C   . SER   A 1 187 ? 11.154  -12.629 -17.764 1.00 25.98  ? 192 SER   A C   1 
ATOM   1266 O  O   . SER   A 1 187 ? 10.760  -11.481 -18.002 1.00 24.62  ? 192 SER   A O   1 
ATOM   1267 C  CB  . SER   A 1 187 ? 12.285  -12.976 -20.002 1.00 27.88  ? 192 SER   A CB  1 
ATOM   1268 O  OG  . SER   A 1 187 ? 13.566  -13.188 -20.589 1.00 33.21  ? 192 SER   A OG  1 
ATOM   1269 N  N   . ILE   A 1 188 ? 10.592  -13.415 -16.823 1.00 23.22  ? 193 ILE   A N   1 
ATOM   1270 C  CA  . ILE   A 1 188 ? 9.442   -12.976 -16.020 1.00 22.60  ? 193 ILE   A CA  1 
ATOM   1271 C  C   . ILE   A 1 188 ? 9.791   -13.191 -14.547 1.00 25.95  ? 193 ILE   A C   1 
ATOM   1272 O  O   . ILE   A 1 188 ? 10.296  -14.261 -14.188 1.00 24.49  ? 193 ILE   A O   1 
ATOM   1273 C  CB  . ILE   A 1 188 ? 8.099   -13.657 -16.421 1.00 24.85  ? 193 ILE   A CB  1 
ATOM   1274 C  CG1 . ILE   A 1 188 ? 6.942   -13.225 -15.460 1.00 24.93  ? 193 ILE   A CG1 1 
ATOM   1275 C  CG2 . ILE   A 1 188 ? 8.225   -15.221 -16.498 1.00 23.90  ? 193 ILE   A CG2 1 
ATOM   1276 C  CD1 . ILE   A 1 188 ? 5.567   -13.423 -15.936 1.00 27.13  ? 193 ILE   A CD1 1 
ATOM   1277 N  N   . VAL   A 1 189 ? 9.547   -12.181 -13.697 1.00 22.18  ? 194 VAL   A N   1 
ATOM   1278 C  CA  . VAL   A 1 189 ? 9.789   -12.365 -12.260 1.00 21.83  ? 194 VAL   A CA  1 
ATOM   1279 C  C   . VAL   A 1 189 ? 8.494   -11.953 -11.595 1.00 25.35  ? 194 VAL   A C   1 
ATOM   1280 O  O   . VAL   A 1 189 ? 7.964   -10.876 -11.888 1.00 23.71  ? 194 VAL   A O   1 
ATOM   1281 C  CB  . VAL   A 1 189 ? 10.978  -11.538 -11.704 1.00 24.75  ? 194 VAL   A CB  1 
ATOM   1282 C  CG1 . VAL   A 1 189 ? 11.032  -11.601 -10.164 1.00 25.03  ? 194 VAL   A CG1 1 
ATOM   1283 C  CG2 . VAL   A 1 189 ? 12.309  -11.993 -12.308 1.00 25.22  ? 194 VAL   A CG2 1 
ATOM   1284 N  N   . TYR   A 1 190 ? 8.045   -12.785 -10.638 1.00 22.55  ? 195 TYR   A N   1 
ATOM   1285 C  CA  . TYR   A 1 190 ? 6.853   -12.520 -9.845  1.00 22.29  ? 195 TYR   A CA  1 
ATOM   1286 C  C   . TYR   A 1 190 ? 7.208   -11.919 -8.504  1.00 23.09  ? 195 TYR   A C   1 
ATOM   1287 O  O   . TYR   A 1 190 ? 8.195   -12.327 -7.882  1.00 23.01  ? 195 TYR   A O   1 
ATOM   1288 C  CB  . TYR   A 1 190 ? 6.112   -13.822 -9.553  1.00 22.75  ? 195 TYR   A CB  1 
ATOM   1289 C  CG  . TYR   A 1 190 ? 5.416   -14.400 -10.749 1.00 23.43  ? 195 TYR   A CG  1 
ATOM   1290 C  CD1 . TYR   A 1 190 ? 4.130   -13.997 -11.089 1.00 24.55  ? 195 TYR   A CD1 1 
ATOM   1291 C  CD2 . TYR   A 1 190 ? 6.029   -15.379 -11.531 1.00 24.40  ? 195 TYR   A CD2 1 
ATOM   1292 C  CE1 . TYR   A 1 190 ? 3.452   -14.579 -12.152 1.00 26.20  ? 195 TYR   A CE1 1 
ATOM   1293 C  CE2 . TYR   A 1 190 ? 5.369   -15.949 -12.616 1.00 24.03  ? 195 TYR   A CE2 1 
ATOM   1294 C  CZ  . TYR   A 1 190 ? 4.068   -15.573 -12.895 1.00 27.98  ? 195 TYR   A CZ  1 
ATOM   1295 O  OH  . TYR   A 1 190 ? 3.394   -16.186 -13.911 1.00 28.51  ? 195 TYR   A OH  1 
ATOM   1296 N  N   . ILE   A 1 191 ? 6.368   -10.991 -8.031  1.00 20.47  ? 196 ILE   A N   1 
ATOM   1297 C  CA  . ILE   A 1 191 ? 6.499   -10.382 -6.708  1.00 19.26  ? 196 ILE   A CA  1 
ATOM   1298 C  C   . ILE   A 1 191 ? 5.122   -10.344 -6.046  1.00 24.18  ? 196 ILE   A C   1 
ATOM   1299 O  O   . ILE   A 1 191 ? 4.186   -9.807  -6.639  1.00 23.78  ? 196 ILE   A O   1 
ATOM   1300 C  CB  . ILE   A 1 191 ? 7.123   -8.944  -6.765  1.00 21.18  ? 196 ILE   A CB  1 
ATOM   1301 C  CG1 . ILE   A 1 191 ? 8.543   -8.942  -7.408  1.00 21.29  ? 196 ILE   A CG1 1 
ATOM   1302 C  CG2 . ILE   A 1 191 ? 7.157   -8.317  -5.366  1.00 22.27  ? 196 ILE   A CG2 1 
ATOM   1303 C  CD1 . ILE   A 1 191 ? 9.056   -7.547  -7.792  1.00 22.71  ? 196 ILE   A CD1 1 
ATOM   1304 N  N   . GLY   A 1 192 ? 5.035   -10.865 -4.812  1.00 22.81  ? 197 GLY   A N   1 
ATOM   1305 C  CA  . GLY   A 1 192 ? 3.817   -10.758 -4.006  1.00 23.12  ? 197 GLY   A CA  1 
ATOM   1306 C  C   . GLY   A 1 192 ? 2.981   -12.006 -3.855  1.00 27.58  ? 197 GLY   A C   1 
ATOM   1307 O  O   . GLY   A 1 192 ? 1.924   -11.960 -3.203  1.00 26.20  ? 197 GLY   A O   1 
ATOM   1308 N  N   . LEU   A 1 193 ? 3.448   -13.126 -4.451  1.00 24.45  ? 198 LEU   A N   1 
ATOM   1309 C  CA  . LEU   A 1 193 ? 2.694   -14.379 -4.467  1.00 24.48  ? 198 LEU   A CA  1 
ATOM   1310 C  C   . LEU   A 1 193 ? 2.305   -14.845 -3.096  1.00 26.31  ? 198 LEU   A C   1 
ATOM   1311 O  O   . LEU   A 1 193 ? 3.116   -14.821 -2.173  1.00 25.37  ? 198 LEU   A O   1 
ATOM   1312 C  CB  . LEU   A 1 193 ? 3.451   -15.501 -5.176  1.00 23.76  ? 198 LEU   A CB  1 
ATOM   1313 C  CG  . LEU   A 1 193 ? 3.846   -15.209 -6.631  1.00 26.45  ? 198 LEU   A CG  1 
ATOM   1314 C  CD1 . LEU   A 1 193 ? 4.490   -16.468 -7.268  1.00 27.21  ? 198 LEU   A CD1 1 
ATOM   1315 C  CD2 . LEU   A 1 193 ? 2.655   -14.735 -7.442  1.00 24.84  ? 198 LEU   A CD2 1 
ATOM   1316 N  N   . ARG   A 1 194 ? 1.045   -15.299 -2.974  1.00 25.61  ? 199 ARG   A N   1 
ATOM   1317 C  CA  . ARG   A 1 194 ? 0.585   -15.881 -1.712  1.00 25.57  ? 199 ARG   A CA  1 
ATOM   1318 C  C   . ARG   A 1 194 ? -0.565  -16.875 -1.879  1.00 30.57  ? 199 ARG   A C   1 
ATOM   1319 O  O   . ARG   A 1 194 ? -0.911  -17.539 -0.914  1.00 30.50  ? 199 ARG   A O   1 
ATOM   1320 C  CB  . ARG   A 1 194 ? 0.246   -14.812 -0.665  1.00 23.60  ? 199 ARG   A CB  1 
ATOM   1321 C  CG  . ARG   A 1 194 ? -0.730  -13.778 -1.135  1.00 24.64  ? 199 ARG   A CG  1 
ATOM   1322 C  CD  . ARG   A 1 194 ? -0.736  -12.669 -0.097  1.00 27.07  ? 199 ARG   A CD  1 
ATOM   1323 N  NE  . ARG   A 1 194 ? -1.753  -11.652 -0.351  1.00 25.24  ? 199 ARG   A NE  1 
ATOM   1324 C  CZ  . ARG   A 1 194 ? -1.626  -10.599 -1.161  1.00 30.23  ? 199 ARG   A CZ  1 
ATOM   1325 N  NH1 . ARG   A 1 194 ? -0.523  -10.444 -1.908  1.00 24.06  ? 199 ARG   A NH1 1 
ATOM   1326 N  NH2 . ARG   A 1 194 ? -2.606  -9.711  -1.259  1.00 24.87  ? 199 ARG   A NH2 1 
ATOM   1327 N  N   . ASP   A 1 195 ? -1.122  -17.012 -3.078  1.00 27.75  ? 200 ASP   A N   1 
ATOM   1328 C  CA  . ASP   A 1 195 ? -2.212  -17.970 -3.310  1.00 26.58  ? 200 ASP   A CA  1 
ATOM   1329 C  C   . ASP   A 1 195 ? -1.922  -18.671 -4.651  1.00 28.43  ? 200 ASP   A C   1 
ATOM   1330 O  O   . ASP   A 1 195 ? -2.380  -18.218 -5.694  1.00 28.83  ? 200 ASP   A O   1 
ATOM   1331 C  CB  . ASP   A 1 195 ? -3.566  -17.231 -3.313  1.00 28.84  ? 200 ASP   A CB  1 
ATOM   1332 C  CG  . ASP   A 1 195 ? -4.779  -18.096 -3.655  1.00 41.06  ? 200 ASP   A CG  1 
ATOM   1333 O  OD1 . ASP   A 1 195 ? -4.702  -19.338 -3.460  1.00 41.58  ? 200 ASP   A OD1 1 
ATOM   1334 O  OD2 . ASP   A 1 195 ? -5.810  -17.526 -4.105  1.00 43.29  ? 200 ASP   A OD2 1 
ATOM   1335 N  N   . VAL   A 1 196 ? -1.086  -19.713 -4.599  1.00 26.67  ? 201 VAL   A N   1 
ATOM   1336 C  CA  . VAL   A 1 196 ? -0.581  -20.414 -5.774  1.00 26.43  ? 201 VAL   A CA  1 
ATOM   1337 C  C   . VAL   A 1 196 ? -1.128  -21.835 -5.805  1.00 31.63  ? 201 VAL   A C   1 
ATOM   1338 O  O   . VAL   A 1 196 ? -1.005  -22.579 -4.826  1.00 30.45  ? 201 VAL   A O   1 
ATOM   1339 C  CB  . VAL   A 1 196 ? 0.975   -20.382 -5.736  1.00 29.20  ? 201 VAL   A CB  1 
ATOM   1340 C  CG1 . VAL   A 1 196 ? 1.598   -21.092 -6.938  1.00 29.08  ? 201 VAL   A CG1 1 
ATOM   1341 C  CG2 . VAL   A 1 196 ? 1.494   -18.944 -5.627  1.00 28.97  ? 201 VAL   A CG2 1 
ATOM   1342 N  N   . ASP   A 1 197 ? -1.667  -22.228 -6.950  1.00 29.13  ? 202 ASP   A N   1 
ATOM   1343 C  CA  . ASP   A 1 197 ? -2.200  -23.585 -7.101  1.00 29.07  ? 202 ASP   A CA  1 
ATOM   1344 C  C   . ASP   A 1 197 ? -1.080  -24.628 -7.199  1.00 31.96  ? 202 ASP   A C   1 
ATOM   1345 O  O   . ASP   A 1 197 ? 0.003   -24.286 -7.687  1.00 28.20  ? 202 ASP   A O   1 
ATOM   1346 C  CB  . ASP   A 1 197 ? -3.135  -23.632 -8.308  1.00 31.08  ? 202 ASP   A CB  1 
ATOM   1347 C  CG  . ASP   A 1 197 ? -4.364  -22.756 -8.164  1.00 36.13  ? 202 ASP   A CG  1 
ATOM   1348 O  OD1 . ASP   A 1 197 ? -4.752  -22.446 -7.008  1.00 38.32  ? 202 ASP   A OD1 1 
ATOM   1349 O  OD2 . ASP   A 1 197 ? -4.961  -22.410 -9.190  1.00 34.79  ? 202 ASP   A OD2 1 
ATOM   1350 N  N   . PRO   A 1 198 ? -1.284  -25.907 -6.759  1.00 29.04  ? 203 PRO   A N   1 
ATOM   1351 C  CA  . PRO   A 1 198 ? -0.194  -26.899 -6.900  1.00 29.07  ? 203 PRO   A CA  1 
ATOM   1352 C  C   . PRO   A 1 198 ? 0.385   -26.986 -8.326  1.00 30.68  ? 203 PRO   A C   1 
ATOM   1353 O  O   . PRO   A 1 198 ? 1.613   -26.993 -8.434  1.00 31.02  ? 203 PRO   A O   1 
ATOM   1354 C  CB  . PRO   A 1 198 ? -0.836  -28.219 -6.444  1.00 31.30  ? 203 PRO   A CB  1 
ATOM   1355 C  CG  . PRO   A 1 198 ? -1.973  -27.798 -5.541  1.00 35.88  ? 203 PRO   A CG  1 
ATOM   1356 C  CD  . PRO   A 1 198 ? -2.486  -26.501 -6.125  1.00 32.20  ? 203 PRO   A CD  1 
ATOM   1357 N  N   . PRO   A 1 199 ? -0.404  -26.977 -9.430  1.00 27.08  ? 204 PRO   A N   1 
ATOM   1358 C  CA  . PRO   A 1 199 ? 0.233   -27.037 -10.766 1.00 27.25  ? 204 PRO   A CA  1 
ATOM   1359 C  C   . PRO   A 1 199 ? 1.069   -25.803 -11.069 1.00 31.08  ? 204 PRO   A C   1 
ATOM   1360 O  O   . PRO   A 1 199 ? 2.070   -25.901 -11.772 1.00 32.04  ? 204 PRO   A O   1 
ATOM   1361 C  CB  . PRO   A 1 199 ? -0.945  -27.119 -11.729 1.00 28.96  ? 204 PRO   A CB  1 
ATOM   1362 C  CG  . PRO   A 1 199 ? -2.127  -26.652 -10.981 1.00 34.25  ? 204 PRO   A CG  1 
ATOM   1363 C  CD  . PRO   A 1 199 ? -1.882  -27.010 -9.549  1.00 29.90  ? 204 PRO   A CD  1 
ATOM   1364 N  N   . GLU   A 1 200 ? 0.666   -24.657 -10.511 1.00 27.26  ? 205 GLU   A N   1 
ATOM   1365 C  CA  . GLU   A 1 200 ? 1.394   -23.390 -10.706 1.00 26.55  ? 205 GLU   A CA  1 
ATOM   1366 C  C   . GLU   A 1 200 ? 2.720   -23.458 -9.993  1.00 30.25  ? 205 GLU   A C   1 
ATOM   1367 O  O   . GLU   A 1 200 ? 3.742   -23.067 -10.560 1.00 28.01  ? 205 GLU   A O   1 
ATOM   1368 C  CB  . GLU   A 1 200 ? 0.564   -22.184 -10.253 1.00 28.20  ? 205 GLU   A CB  1 
ATOM   1369 C  CG  . GLU   A 1 200 ? -0.698  -21.941 -11.064 1.00 26.47  ? 205 GLU   A CG  1 
ATOM   1370 C  CD  . GLU   A 1 200 ? -1.439  -20.714 -10.581 1.00 36.98  ? 205 GLU   A CD  1 
ATOM   1371 O  OE1 . GLU   A 1 200 ? -1.932  -20.738 -9.427  1.00 30.18  ? 205 GLU   A OE1 1 
ATOM   1372 O  OE2 . GLU   A 1 200 ? -1.524  -19.725 -11.350 1.00 32.42  ? 205 GLU   A OE2 1 
ATOM   1373 N  N   . HIS   A 1 201 ? 2.722   -23.993 -8.764  1.00 26.64  ? 206 HIS   A N   1 
ATOM   1374 C  CA  . HIS   A 1 201 ? 3.945   -24.209 -7.996  1.00 27.66  ? 206 HIS   A CA  1 
ATOM   1375 C  C   . HIS   A 1 201 ? 4.909   -25.104 -8.798  1.00 30.17  ? 206 HIS   A C   1 
ATOM   1376 O  O   . HIS   A 1 201 ? 6.094   -24.783 -8.895  1.00 29.20  ? 206 HIS   A O   1 
ATOM   1377 C  CB  . HIS   A 1 201 ? 3.627   -24.831 -6.620  1.00 29.40  ? 206 HIS   A CB  1 
ATOM   1378 C  CG  . HIS   A 1 201 ? 4.837   -25.024 -5.753  1.00 33.59  ? 206 HIS   A CG  1 
ATOM   1379 N  ND1 . HIS   A 1 201 ? 5.457   -26.252 -5.646  1.00 35.95  ? 206 HIS   A ND1 1 
ATOM   1380 C  CD2 . HIS   A 1 201 ? 5.523   -24.121 -5.011  1.00 36.34  ? 206 HIS   A CD2 1 
ATOM   1381 C  CE1 . HIS   A 1 201 ? 6.478   -26.068 -4.821  1.00 35.80  ? 206 HIS   A CE1 1 
ATOM   1382 N  NE2 . HIS   A 1 201 ? 6.551   -24.803 -4.405  1.00 36.37  ? 206 HIS   A NE2 1 
ATOM   1383 N  N   . PHE   A 1 202 ? 4.404   -26.234 -9.348  1.00 29.40  ? 207 PHE   A N   1 
ATOM   1384 C  CA  . PHE   A 1 202 ? 5.217   -27.135 -10.164 1.00 28.57  ? 207 PHE   A CA  1 
ATOM   1385 C  C   . PHE   A 1 202 ? 5.808   -26.395 -11.370 1.00 31.38  ? 207 PHE   A C   1 
ATOM   1386 O  O   . PHE   A 1 202 ? 7.016   -26.481 -11.589 1.00 31.63  ? 207 PHE   A O   1 
ATOM   1387 C  CB  . PHE   A 1 202 ? 4.427   -28.365 -10.622 1.00 30.31  ? 207 PHE   A CB  1 
ATOM   1388 C  CG  . PHE   A 1 202 ? 5.242   -29.259 -11.532 1.00 31.43  ? 207 PHE   A CG  1 
ATOM   1389 C  CD1 . PHE   A 1 202 ? 6.249   -30.073 -11.017 1.00 34.91  ? 207 PHE   A CD1 1 
ATOM   1390 C  CD2 . PHE   A 1 202 ? 5.034   -29.254 -12.907 1.00 33.78  ? 207 PHE   A CD2 1 
ATOM   1391 C  CE1 . PHE   A 1 202 ? 7.033   -30.864 -11.863 1.00 36.24  ? 207 PHE   A CE1 1 
ATOM   1392 C  CE2 . PHE   A 1 202 ? 5.808   -30.051 -13.747 1.00 36.36  ? 207 PHE   A CE2 1 
ATOM   1393 C  CZ  . PHE   A 1 202 ? 6.816   -30.832 -13.223 1.00 35.21  ? 207 PHE   A CZ  1 
ATOM   1394 N  N   . ILE   A 1 203 ? 4.979   -25.621 -12.089 1.00 27.01  ? 208 ILE   A N   1 
ATOM   1395 C  CA  . ILE   A 1 203 ? 5.438   -24.828 -13.257 1.00 27.06  ? 208 ILE   A CA  1 
ATOM   1396 C  C   . ILE   A 1 203 ? 6.562   -23.865 -12.862 1.00 29.03  ? 208 ILE   A C   1 
ATOM   1397 O  O   . ILE   A 1 203 ? 7.597   -23.801 -13.538 1.00 28.66  ? 208 ILE   A O   1 
ATOM   1398 C  CB  . ILE   A 1 203 ? 4.278   -24.086 -13.976 1.00 29.86  ? 208 ILE   A CB  1 
ATOM   1399 C  CG1 . ILE   A 1 203 ? 3.369   -25.079 -14.717 1.00 30.35  ? 208 ILE   A CG1 1 
ATOM   1400 C  CG2 . ILE   A 1 203 ? 4.836   -23.036 -14.985 1.00 29.96  ? 208 ILE   A CG2 1 
ATOM   1401 C  CD1 . ILE   A 1 203 ? 1.972   -24.588 -14.992 1.00 26.52  ? 208 ILE   A CD1 1 
ATOM   1402 N  N   . LEU   A 1 204 ? 6.362   -23.104 -11.761 1.00 26.69  ? 209 LEU   A N   1 
ATOM   1403 C  CA  . LEU   A 1 204 ? 7.399   -22.173 -11.319 1.00 25.73  ? 209 LEU   A CA  1 
ATOM   1404 C  C   . LEU   A 1 204 ? 8.708   -22.854 -10.982 1.00 28.97  ? 209 LEU   A C   1 
ATOM   1405 O  O   . LEU   A 1 204 ? 9.765   -22.412 -11.426 1.00 28.04  ? 209 LEU   A O   1 
ATOM   1406 C  CB  . LEU   A 1 204 ? 6.915   -21.329 -10.099 1.00 24.75  ? 209 LEU   A CB  1 
ATOM   1407 C  CG  . LEU   A 1 204 ? 5.686   -20.458 -10.353 1.00 28.21  ? 209 LEU   A CG  1 
ATOM   1408 C  CD1 . LEU   A 1 204 ? 5.051   -19.982 -9.014  1.00 29.64  ? 209 LEU   A CD1 1 
ATOM   1409 C  CD2 . LEU   A 1 204 ? 6.040   -19.252 -11.221 1.00 27.73  ? 209 LEU   A CD2 1 
ATOM   1410 N  N   . LYS   A 1 205 ? 8.650   -23.959 -10.219 1.00 27.23  ? 210 LYS   A N   1 
ATOM   1411 C  CA  . LYS   A 1 205 ? 9.886   -24.621 -9.796  1.00 27.23  ? 210 LYS   A CA  1 
ATOM   1412 C  C   . LYS   A 1 205 ? 10.558  -25.347 -10.946 1.00 32.52  ? 210 LYS   A C   1 
ATOM   1413 O  O   . LYS   A 1 205 ? 11.776  -25.225 -11.135 1.00 32.30  ? 210 LYS   A O   1 
ATOM   1414 C  CB  . LYS   A 1 205 ? 9.594   -25.623 -8.667  1.00 29.21  ? 210 LYS   A CB  1 
ATOM   1415 C  CG  . LYS   A 1 205 ? 9.151   -24.962 -7.360  1.00 34.15  ? 210 LYS   A CG  1 
ATOM   1416 C  CD  . LYS   A 1 205 ? 10.336  -24.303 -6.625  1.00 39.65  ? 210 LYS   A CD  1 
ATOM   1417 C  CE  . LYS   A 1 205 ? 9.946   -23.736 -5.291  1.00 42.45  ? 210 LYS   A CE  1 
ATOM   1418 N  NZ  . LYS   A 1 205 ? 11.082  -23.027 -4.643  1.00 54.10  ? 210 LYS   A NZ  1 
ATOM   1419 N  N   . ASN   A 1 206 ? 9.763   -26.106 -11.691 1.00 30.03  ? 211 ASN   A N   1 
ATOM   1420 C  CA  . ASN   A 1 206 ? 10.248  -26.959 -12.773 1.00 30.55  ? 211 ASN   A CA  1 
ATOM   1421 C  C   . ASN   A 1 206 ? 10.916  -26.170 -13.882 1.00 34.13  ? 211 ASN   A C   1 
ATOM   1422 O  O   . ASN   A 1 206 ? 12.008  -26.551 -14.334 1.00 33.13  ? 211 ASN   A O   1 
ATOM   1423 C  CB  . ASN   A 1 206 ? 9.135   -27.836 -13.316 1.00 30.04  ? 211 ASN   A CB  1 
ATOM   1424 C  CG  . ASN   A 1 206 ? 9.675   -28.947 -14.189 1.00 45.67  ? 211 ASN   A CG  1 
ATOM   1425 O  OD1 . ASN   A 1 206 ? 10.436  -29.816 -13.731 1.00 38.39  ? 211 ASN   A OD1 1 
ATOM   1426 N  ND2 . ASN   A 1 206 ? 9.378   -28.875 -15.473 1.00 38.53  ? 211 ASN   A ND2 1 
ATOM   1427 N  N   . TYR   A 1 207 ? 10.308  -25.025 -14.251 1.00 29.68  ? 212 TYR   A N   1 
ATOM   1428 C  CA  . TYR   A 1 207 ? 10.821  -24.182 -15.331 1.00 29.95  ? 212 TYR   A CA  1 
ATOM   1429 C  C   . TYR   A 1 207 ? 11.738  -23.069 -14.865 1.00 33.93  ? 212 TYR   A C   1 
ATOM   1430 O  O   . TYR   A 1 207 ? 12.110  -22.227 -15.679 1.00 34.75  ? 212 TYR   A O   1 
ATOM   1431 C  CB  . TYR   A 1 207 ? 9.667   -23.664 -16.193 1.00 31.46  ? 212 TYR   A CB  1 
ATOM   1432 C  CG  . TYR   A 1 207 ? 9.030   -24.811 -16.941 1.00 33.30  ? 212 TYR   A CG  1 
ATOM   1433 C  CD1 . TYR   A 1 207 ? 9.607   -25.315 -18.107 1.00 35.44  ? 212 TYR   A CD1 1 
ATOM   1434 C  CD2 . TYR   A 1 207 ? 7.906   -25.460 -16.436 1.00 33.35  ? 212 TYR   A CD2 1 
ATOM   1435 C  CE1 . TYR   A 1 207 ? 9.074   -26.426 -18.756 1.00 36.42  ? 212 TYR   A CE1 1 
ATOM   1436 C  CE2 . TYR   A 1 207 ? 7.366   -26.576 -17.075 1.00 34.29  ? 212 TYR   A CE2 1 
ATOM   1437 C  CZ  . TYR   A 1 207 ? 7.954   -27.052 -18.238 1.00 39.60  ? 212 TYR   A CZ  1 
ATOM   1438 O  OH  . TYR   A 1 207 ? 7.441   -28.152 -18.881 1.00 37.06  ? 212 TYR   A OH  1 
ATOM   1439 N  N   . ASP   A 1 208 ? 12.186  -23.117 -13.589 1.00 30.11  ? 213 ASP   A N   1 
ATOM   1440 C  CA  . ASP   A 1 208 ? 13.112  -22.155 -13.004 1.00 29.60  ? 213 ASP   A CA  1 
ATOM   1441 C  C   . ASP   A 1 208 ? 12.608  -20.717 -13.161 1.00 31.38  ? 213 ASP   A C   1 
ATOM   1442 O  O   . ASP   A 1 208 ? 13.388  -19.833 -13.518 1.00 31.52  ? 213 ASP   A O   1 
ATOM   1443 C  CB  . ASP   A 1 208 ? 14.524  -22.300 -13.613 1.00 31.25  ? 213 ASP   A CB  1 
ATOM   1444 C  CG  . ASP   A 1 208 ? 15.084  -23.702 -13.522 1.00 44.36  ? 213 ASP   A CG  1 
ATOM   1445 O  OD1 . ASP   A 1 208 ? 15.295  -24.176 -12.396 1.00 44.32  ? 213 ASP   A OD1 1 
ATOM   1446 O  OD2 . ASP   A 1 208 ? 15.323  -24.318 -14.590 1.00 48.19  ? 213 ASP   A OD2 1 
ATOM   1447 N  N   . ILE   A 1 209 ? 11.311  -20.503 -12.925 1.00 27.62  ? 214 ILE   A N   1 
ATOM   1448 C  CA  . ILE   A 1 209 ? 10.736  -19.156 -12.977 1.00 26.61  ? 214 ILE   A CA  1 
ATOM   1449 C  C   . ILE   A 1 209 ? 10.938  -18.538 -11.606 1.00 29.49  ? 214 ILE   A C   1 
ATOM   1450 O  O   . ILE   A 1 209 ? 10.520  -19.098 -10.591 1.00 29.56  ? 214 ILE   A O   1 
ATOM   1451 C  CB  . ILE   A 1 209 ? 9.279   -19.105 -13.442 1.00 27.90  ? 214 ILE   A CB  1 
ATOM   1452 C  CG1 . ILE   A 1 209 ? 9.125   -19.715 -14.866 1.00 27.84  ? 214 ILE   A CG1 1 
ATOM   1453 C  CG2 . ILE   A 1 209 ? 8.735   -17.627 -13.371 1.00 28.36  ? 214 ILE   A CG2 1 
ATOM   1454 C  CD1 . ILE   A 1 209 ? 7.705   -20.056 -15.182 1.00 30.09  ? 214 ILE   A CD1 1 
ATOM   1455 N  N   . GLN   A 1 210 ? 11.623  -17.406 -11.581 1.00 25.64  ? 215 GLN   A N   1 
ATOM   1456 C  CA  . GLN   A 1 210 ? 11.975  -16.742 -10.346 1.00 25.62  ? 215 GLN   A CA  1 
ATOM   1457 C  C   . GLN   A 1 210 ? 10.809  -15.952 -9.757  1.00 26.42  ? 215 GLN   A C   1 
ATOM   1458 O  O   . GLN   A 1 210 ? 10.115  -15.233 -10.456 1.00 23.94  ? 215 GLN   A O   1 
ATOM   1459 C  CB  . GLN   A 1 210 ? 13.219  -15.884 -10.544 1.00 27.36  ? 215 GLN   A CB  1 
ATOM   1460 C  CG  . GLN   A 1 210 ? 14.446  -16.691 -11.081 1.00 30.39  ? 215 GLN   A CG  1 
ATOM   1461 C  CD  . GLN   A 1 210 ? 14.741  -17.960 -10.305 1.00 39.75  ? 215 GLN   A CD  1 
ATOM   1462 O  OE1 . GLN   A 1 210 ? 15.039  -17.936 -9.106  1.00 39.61  ? 215 GLN   A OE1 1 
ATOM   1463 N  NE2 . GLN   A 1 210 ? 14.589  -19.105 -10.959 1.00 33.76  ? 215 GLN   A NE2 1 
ATOM   1464 N  N   . TYR   A 1 211 ? 10.552  -16.164 -8.470  1.00 25.01  ? 216 TYR   A N   1 
ATOM   1465 C  CA  . TYR   A 1 211 ? 9.463   -15.464 -7.802  1.00 24.62  ? 216 TYR   A CA  1 
ATOM   1466 C  C   . TYR   A 1 211 ? 9.869   -15.055 -6.406  1.00 26.38  ? 216 TYR   A C   1 
ATOM   1467 O  O   . TYR   A 1 211 ? 10.673  -15.743 -5.742  1.00 26.00  ? 216 TYR   A O   1 
ATOM   1468 C  CB  . TYR   A 1 211 ? 8.151   -16.274 -7.773  1.00 24.33  ? 216 TYR   A CB  1 
ATOM   1469 C  CG  . TYR   A 1 211 ? 8.211   -17.557 -6.973  1.00 26.16  ? 216 TYR   A CG  1 
ATOM   1470 C  CD1 . TYR   A 1 211 ? 8.563   -18.763 -7.579  1.00 27.48  ? 216 TYR   A CD1 1 
ATOM   1471 C  CD2 . TYR   A 1 211 ? 7.845   -17.582 -5.627  1.00 27.21  ? 216 TYR   A CD2 1 
ATOM   1472 C  CE1 . TYR   A 1 211 ? 8.617   -19.950 -6.848  1.00 27.61  ? 216 TYR   A CE1 1 
ATOM   1473 C  CE2 . TYR   A 1 211 ? 7.912   -18.758 -4.882  1.00 28.47  ? 216 TYR   A CE2 1 
ATOM   1474 C  CZ  . TYR   A 1 211 ? 8.283   -19.943 -5.502  1.00 34.71  ? 216 TYR   A CZ  1 
ATOM   1475 O  OH  . TYR   A 1 211 ? 8.341   -21.106 -4.777  1.00 37.64  ? 216 TYR   A OH  1 
ATOM   1476 N  N   . PHE   A 1 212 ? 9.296   -13.935 -5.949  1.00 21.63  ? 217 PHE   A N   1 
ATOM   1477 C  CA  . PHE   A 1 212 ? 9.481   -13.452 -4.582  1.00 21.79  ? 217 PHE   A CA  1 
ATOM   1478 C  C   . PHE   A 1 212 ? 8.102   -13.443 -3.955  1.00 24.17  ? 217 PHE   A C   1 
ATOM   1479 O  O   . PHE   A 1 212 ? 7.337   -12.518 -4.163  1.00 24.87  ? 217 PHE   A O   1 
ATOM   1480 C  CB  . PHE   A 1 212 ? 10.182  -12.082 -4.537  1.00 23.14  ? 217 PHE   A CB  1 
ATOM   1481 C  CG  . PHE   A 1 212 ? 11.587  -12.160 -5.088  1.00 24.40  ? 217 PHE   A CG  1 
ATOM   1482 C  CD1 . PHE   A 1 212 ? 12.635  -12.625 -4.298  1.00 26.62  ? 217 PHE   A CD1 1 
ATOM   1483 C  CD2 . PHE   A 1 212 ? 11.846  -11.859 -6.425  1.00 25.39  ? 217 PHE   A CD2 1 
ATOM   1484 C  CE1 . PHE   A 1 212 ? 13.931  -12.722 -4.810  1.00 27.12  ? 217 PHE   A CE1 1 
ATOM   1485 C  CE2 . PHE   A 1 212 ? 13.135  -11.996 -6.947  1.00 27.61  ? 217 PHE   A CE2 1 
ATOM   1486 C  CZ  . PHE   A 1 212 ? 14.168  -12.423 -6.135  1.00 26.97  ? 217 PHE   A CZ  1 
ATOM   1487 N  N   . SER   A 1 213 ? 7.754   -14.527 -3.264  1.00 21.93  ? 218 SER   A N   1 
ATOM   1488 C  CA  . SER   A 1 213 ? 6.440   -14.640 -2.604  1.00 22.11  ? 218 SER   A CA  1 
ATOM   1489 C  C   . SER   A 1 213 ? 6.431   -13.692 -1.393  1.00 24.42  ? 218 SER   A C   1 
ATOM   1490 O  O   . SER   A 1 213 ? 7.460   -13.141 -1.037  1.00 22.83  ? 218 SER   A O   1 
ATOM   1491 C  CB  . SER   A 1 213 ? 6.245   -16.059 -2.079  1.00 23.02  ? 218 SER   A CB  1 
ATOM   1492 O  OG  . SER   A 1 213 ? 7.114   -16.286 -0.978  1.00 27.41  ? 218 SER   A OG  1 
ATOM   1493 N  N   . MET   A 1 214 ? 5.282   -13.533 -0.735  1.00 23.44  ? 219 MET   A N   1 
ATOM   1494 C  CA  . MET   A 1 214 ? 5.199   -12.722 0.486   1.00 22.63  ? 219 MET   A CA  1 
ATOM   1495 C  C   . MET   A 1 214 ? 6.172   -13.273 1.540   1.00 24.96  ? 219 MET   A C   1 
ATOM   1496 O  O   . MET   A 1 214 ? 6.739   -12.498 2.292   1.00 24.85  ? 219 MET   A O   1 
ATOM   1497 C  CB  . MET   A 1 214 ? 3.767   -12.704 1.049   1.00 22.70  ? 219 MET   A CB  1 
ATOM   1498 C  CG  . MET   A 1 214 ? 2.768   -11.980 0.192   1.00 24.73  ? 219 MET   A CG  1 
ATOM   1499 S  SD  . MET   A 1 214 ? 3.211   -10.320 -0.402  1.00 25.31  ? 219 MET   A SD  1 
ATOM   1500 C  CE  . MET   A 1 214 ? 3.563   -9.476  1.130   1.00 22.60  ? 219 MET   A CE  1 
ATOM   1501 N  N   . ARG   A 1 215 ? 6.374   -14.613 1.584   1.00 23.31  ? 220 ARG   A N   1 
ATOM   1502 C  CA  . ARG   A 1 215 ? 7.340   -15.243 2.491   1.00 24.10  ? 220 ARG   A CA  1 
ATOM   1503 C  C   . ARG   A 1 215 ? 8.777   -14.760 2.154   1.00 24.06  ? 220 ARG   A C   1 
ATOM   1504 O  O   . ARG   A 1 215 ? 9.541   -14.422 3.064   1.00 22.82  ? 220 ARG   A O   1 
ATOM   1505 C  CB  . ARG   A 1 215 ? 7.245   -16.779 2.406   1.00 25.36  ? 220 ARG   A CB  1 
ATOM   1506 C  CG  . ARG   A 1 215 ? 8.241   -17.472 3.302   1.00 31.27  ? 220 ARG   A CG  1 
ATOM   1507 C  CD  . ARG   A 1 215 ? 8.181   -18.986 3.164   1.00 32.63  ? 220 ARG   A CD  1 
ATOM   1508 N  NE  . ARG   A 1 215 ? 9.456   -19.567 3.576   1.00 34.47  ? 220 ARG   A NE  1 
ATOM   1509 C  CZ  . ARG   A 1 215 ? 9.739   -19.982 4.803   1.00 47.00  ? 220 ARG   A CZ  1 
ATOM   1510 N  NH1 . ARG   A 1 215 ? 8.819   -19.914 5.767   1.00 34.53  ? 220 ARG   A NH1 1 
ATOM   1511 N  NH2 . ARG   A 1 215 ? 10.945  -20.465 5.084   1.00 33.08  ? 220 ARG   A NH2 1 
ATOM   1512 N  N   . ASP   A 1 216 ? 9.135   -14.689 0.843   1.00 21.02  ? 221 ASP   A N   1 
ATOM   1513 C  CA  . ASP   A 1 216 ? 10.455  -14.165 0.461   1.00 21.53  ? 221 ASP   A CA  1 
ATOM   1514 C  C   . ASP   A 1 216 ? 10.604  -12.695 0.881   1.00 23.80  ? 221 ASP   A C   1 
ATOM   1515 O  O   . ASP   A 1 216 ? 11.668  -12.306 1.319   1.00 22.89  ? 221 ASP   A O   1 
ATOM   1516 C  CB  . ASP   A 1 216 ? 10.693  -14.302 -1.054  1.00 23.03  ? 221 ASP   A CB  1 
ATOM   1517 C  CG  . ASP   A 1 216 ? 10.779  -15.759 -1.467  1.00 29.32  ? 221 ASP   A CG  1 
ATOM   1518 O  OD1 . ASP   A 1 216 ? 11.477  -16.535 -0.761  1.00 32.21  ? 221 ASP   A OD1 1 
ATOM   1519 O  OD2 . ASP   A 1 216 ? 10.059  -16.150 -2.407  1.00 30.05  ? 221 ASP   A OD2 1 
ATOM   1520 N  N   . ILE   A 1 217 ? 9.541   -11.887 0.733   1.00 21.63  ? 222 ILE   A N   1 
ATOM   1521 C  CA  . ILE   A 1 217 ? 9.570   -10.482 1.168   1.00 20.92  ? 222 ILE   A CA  1 
ATOM   1522 C  C   . ILE   A 1 217 ? 9.741   -10.423 2.709   1.00 23.30  ? 222 ILE   A C   1 
ATOM   1523 O  O   . ILE   A 1 217 ? 10.553  -9.634  3.192   1.00 22.79  ? 222 ILE   A O   1 
ATOM   1524 C  CB  . ILE   A 1 217 ? 8.338   -9.682  0.676   1.00 22.44  ? 222 ILE   A CB  1 
ATOM   1525 C  CG1 . ILE   A 1 217 ? 8.211   -9.743  -0.875  1.00 22.38  ? 222 ILE   A CG1 1 
ATOM   1526 C  CG2 . ILE   A 1 217 ? 8.413   -8.221  1.166   1.00 23.60  ? 222 ILE   A CG2 1 
ATOM   1527 C  CD1 . ILE   A 1 217 ? 6.845   -9.234  -1.440  1.00 24.96  ? 222 ILE   A CD1 1 
ATOM   1528 N  N   . ASP   A 1 218 ? 9.041   -11.310 3.470   1.00 22.60  ? 223 ASP   A N   1 
ATOM   1529 C  CA  . ASP   A 1 218 ? 9.181   -11.348 4.943   1.00 22.18  ? 223 ASP   A CA  1 
ATOM   1530 C  C   . ASP   A 1 218 ? 10.639  -11.597 5.361   1.00 25.76  ? 223 ASP   A C   1 
ATOM   1531 O  O   . ASP   A 1 218 ? 11.126  -11.029 6.352   1.00 26.56  ? 223 ASP   A O   1 
ATOM   1532 C  CB  . ASP   A 1 218 ? 8.264   -12.439 5.545   1.00 23.36  ? 223 ASP   A CB  1 
ATOM   1533 C  CG  . ASP   A 1 218 ? 6.769   -12.191 5.365   1.00 25.47  ? 223 ASP   A CG  1 
ATOM   1534 O  OD1 . ASP   A 1 218 ? 6.377   -11.015 5.141   1.00 25.34  ? 223 ASP   A OD1 1 
ATOM   1535 O  OD2 . ASP   A 1 218 ? 6.002   -13.164 5.398   1.00 26.84  ? 223 ASP   A OD2 1 
ATOM   1536 N  N   . ARG   A 1 219 ? 11.326  -12.465 4.599   1.00 21.41  ? 224 ARG   A N   1 
ATOM   1537 C  CA  . ARG   A 1 219 ? 12.708  -12.824 4.869   1.00 22.42  ? 224 ARG   A CA  1 
ATOM   1538 C  C   . ARG   A 1 219 ? 13.721  -11.779 4.408   1.00 26.11  ? 224 ARG   A C   1 
ATOM   1539 O  O   . ARG   A 1 219 ? 14.631  -11.414 5.157   1.00 26.88  ? 224 ARG   A O   1 
ATOM   1540 C  CB  . ARG   A 1 219 ? 13.032  -14.205 4.259   1.00 21.98  ? 224 ARG   A CB  1 
ATOM   1541 C  CG  . ARG   A 1 219 ? 12.197  -15.381 4.815   1.00 27.01  ? 224 ARG   A CG  1 
ATOM   1542 C  CD  . ARG   A 1 219 ? 12.262  -16.641 3.939   1.00 30.38  ? 224 ARG   A CD  1 
ATOM   1543 N  NE  . ARG   A 1 219 ? 13.648  -17.042 3.640   1.00 36.43  ? 224 ARG   A NE  1 
ATOM   1544 C  CZ  . ARG   A 1 219 ? 14.401  -17.804 4.432   1.00 50.69  ? 224 ARG   A CZ  1 
ATOM   1545 N  NH1 . ARG   A 1 219 ? 13.921  -18.255 5.586   1.00 36.40  ? 224 ARG   A NH1 1 
ATOM   1546 N  NH2 . ARG   A 1 219 ? 15.645  -18.108 4.083   1.00 37.59  ? 224 ARG   A NH2 1 
ATOM   1547 N  N   . LEU   A 1 220 ? 13.605  -11.349 3.143   1.00 23.17  ? 225 LEU   A N   1 
ATOM   1548 C  CA  . LEU   A 1 220 ? 14.599  -10.499 2.511   1.00 21.56  ? 225 LEU   A CA  1 
ATOM   1549 C  C   . LEU   A 1 220 ? 14.391  -9.014  2.701   1.00 23.00  ? 225 LEU   A C   1 
ATOM   1550 O  O   . LEU   A 1 220 ? 15.362  -8.270  2.772   1.00 23.09  ? 225 LEU   A O   1 
ATOM   1551 C  CB  . LEU   A 1 220 ? 14.614  -10.782 0.995   1.00 22.32  ? 225 LEU   A CB  1 
ATOM   1552 C  CG  . LEU   A 1 220 ? 15.135  -12.164 0.543   1.00 25.79  ? 225 LEU   A CG  1 
ATOM   1553 C  CD1 . LEU   A 1 220 ? 14.772  -12.435 -0.905  1.00 26.63  ? 225 LEU   A CD1 1 
ATOM   1554 C  CD2 . LEU   A 1 220 ? 16.644  -12.275 0.768   1.00 28.00  ? 225 LEU   A CD2 1 
ATOM   1555 N  N   . GLY   A 1 221 ? 13.140  -8.591  2.714   1.00 21.86  ? 226 GLY   A N   1 
ATOM   1556 C  CA  . GLY   A 1 221 ? 12.831  -7.175  2.706   1.00 22.50  ? 226 GLY   A CA  1 
ATOM   1557 C  C   . GLY   A 1 221 ? 12.653  -6.747  1.259   1.00 25.51  ? 226 GLY   A C   1 
ATOM   1558 O  O   . GLY   A 1 221 ? 13.302  -7.293  0.347   1.00 25.23  ? 226 GLY   A O   1 
ATOM   1559 N  N   . ILE   A 1 222 ? 11.728  -5.802  1.019   1.00 22.82  ? 227 ILE   A N   1 
ATOM   1560 C  CA  . ILE   A 1 222 ? 11.432  -5.365  -0.349  1.00 22.58  ? 227 ILE   A CA  1 
ATOM   1561 C  C   . ILE   A 1 222 ? 12.691  -4.778  -1.108  1.00 23.39  ? 227 ILE   A C   1 
ATOM   1562 O  O   . ILE   A 1 222 ? 12.734  -4.866  -2.352  1.00 23.07  ? 227 ILE   A O   1 
ATOM   1563 C  CB  . ILE   A 1 222 ? 10.214  -4.399  -0.353  1.00 24.23  ? 227 ILE   A CB  1 
ATOM   1564 C  CG1 . ILE   A 1 222 ? 9.568   -4.288  -1.786  1.00 24.50  ? 227 ILE   A CG1 1 
ATOM   1565 C  CG2 . ILE   A 1 222 ? 10.583  -3.029  0.240   1.00 24.65  ? 227 ILE   A CG2 1 
ATOM   1566 C  CD1 . ILE   A 1 222 ? 8.928   -5.573  -2.353  1.00 26.56  ? 227 ILE   A CD1 1 
ATOM   1567 N  N   . GLN   A 1 223 ? 13.655  -4.171  -0.388  1.00 21.98  ? 228 GLN   A N   1 
ATOM   1568 C  CA  . GLN   A 1 223 ? 14.854  -3.615  -1.049  1.00 23.26  ? 228 GLN   A CA  1 
ATOM   1569 C  C   . GLN   A 1 223 ? 15.659  -4.732  -1.749  1.00 24.17  ? 228 GLN   A C   1 
ATOM   1570 O  O   . GLN   A 1 223 ? 15.956  -4.624  -2.955  1.00 22.83  ? 228 GLN   A O   1 
ATOM   1571 C  CB  . GLN   A 1 223 ? 15.767  -2.882  -0.058  1.00 25.29  ? 228 GLN   A CB  1 
ATOM   1572 C  CG  . GLN   A 1 223 ? 17.101  -2.486  -0.723  1.00 26.05  ? 228 GLN   A CG  1 
ATOM   1573 C  CD  . GLN   A 1 223 ? 18.198  -1.984  0.185   1.00 39.70  ? 228 GLN   A CD  1 
ATOM   1574 O  OE1 . GLN   A 1 223 ? 19.376  -1.875  -0.219  1.00 37.96  ? 228 GLN   A OE1 1 
ATOM   1575 N  NE2 . GLN   A 1 223 ? 17.862  -1.641  1.409   1.00 28.96  ? 228 GLN   A NE2 1 
ATOM   1576 N  N   . LYS   A 1 224 ? 15.924  -5.830  -1.015  1.00 22.64  ? 229 LYS   A N   1 
ATOM   1577 C  CA  . LYS   A 1 224 ? 16.667  -6.971  -1.592  1.00 22.71  ? 229 LYS   A CA  1 
ATOM   1578 C  C   . LYS   A 1 224 ? 15.886  -7.668  -2.684  1.00 24.52  ? 229 LYS   A C   1 
ATOM   1579 O  O   . LYS   A 1 224 ? 16.458  -8.048  -3.702  1.00 24.26  ? 229 LYS   A O   1 
ATOM   1580 C  CB  . LYS   A 1 224 ? 17.138  -7.939  -0.497  1.00 24.86  ? 229 LYS   A CB  1 
ATOM   1581 C  CG  . LYS   A 1 224 ? 18.241  -7.336  0.356   1.00 32.88  ? 229 LYS   A CG  1 
ATOM   1582 C  CD  . LYS   A 1 224 ? 18.764  -8.357  1.386   1.00 45.73  ? 229 LYS   A CD  1 
ATOM   1583 C  CE  . LYS   A 1 224 ? 19.782  -7.772  2.348   1.00 54.73  ? 229 LYS   A CE  1 
ATOM   1584 N  NZ  . LYS   A 1 224 ? 21.077  -7.468  1.680   1.00 65.83  ? 229 LYS   A NZ  1 
ATOM   1585 N  N   . VAL   A 1 225 ? 14.546  -7.722  -2.546  1.00 22.15  ? 230 VAL   A N   1 
ATOM   1586 C  CA  . VAL   A 1 225 ? 13.693  -8.308  -3.565  1.00 21.28  ? 230 VAL   A CA  1 
ATOM   1587 C  C   . VAL   A 1 225 ? 13.845  -7.515  -4.872  1.00 25.08  ? 230 VAL   A C   1 
ATOM   1588 O  O   . VAL   A 1 225 ? 14.009  -8.118  -5.938  1.00 23.62  ? 230 VAL   A O   1 
ATOM   1589 C  CB  . VAL   A 1 225 ? 12.220  -8.371  -3.075  1.00 23.79  ? 230 VAL   A CB  1 
ATOM   1590 C  CG1 . VAL   A 1 225 ? 11.246  -8.617  -4.225  1.00 22.93  ? 230 VAL   A CG1 1 
ATOM   1591 C  CG2 . VAL   A 1 225 ? 12.068  -9.465  -2.011  1.00 22.81  ? 230 VAL   A CG2 1 
ATOM   1592 N  N   . MET   A 1 226 ? 13.811  -6.164  -4.788  1.00 21.19  ? 231 MET   A N   1 
ATOM   1593 C  CA  . MET   A 1 226 ? 13.954  -5.361  -6.007  1.00 20.92  ? 231 MET   A CA  1 
ATOM   1594 C  C   . MET   A 1 226 ? 15.338  -5.490  -6.634  1.00 24.10  ? 231 MET   A C   1 
ATOM   1595 O  O   . MET   A 1 226 ? 15.439  -5.651  -7.859  1.00 23.82  ? 231 MET   A O   1 
ATOM   1596 C  CB  . MET   A 1 226 ? 13.549  -3.898  -5.770  1.00 22.52  ? 231 MET   A CB  1 
ATOM   1597 C  CG  . MET   A 1 226 ? 12.038  -3.747  -5.470  1.00 23.43  ? 231 MET   A CG  1 
ATOM   1598 S  SD  . MET   A 1 226 ? 10.865  -4.714  -6.458  1.00 25.38  ? 231 MET   A SD  1 
ATOM   1599 C  CE  . MET   A 1 226 ? 11.158  -4.156  -8.082  1.00 24.19  ? 231 MET   A CE  1 
ATOM   1600 N  N   . GLU   A 1 227 ? 16.383  -5.457  -5.801  1.00 23.42  ? 232 GLU   A N   1 
ATOM   1601 C  CA  . GLU   A 1 227 ? 17.763  -5.620  -6.292  1.00 23.36  ? 232 GLU   A CA  1 
ATOM   1602 C  C   . GLU   A 1 227 ? 17.923  -6.959  -7.016  1.00 26.48  ? 232 GLU   A C   1 
ATOM   1603 O  O   . GLU   A 1 227 ? 18.481  -7.006  -8.127  1.00 27.67  ? 232 GLU   A O   1 
ATOM   1604 C  CB  . GLU   A 1 227 ? 18.770  -5.537  -5.145  1.00 24.73  ? 232 GLU   A CB  1 
ATOM   1605 C  CG  . GLU   A 1 227 ? 18.935  -4.139  -4.583  1.00 31.45  ? 232 GLU   A CG  1 
ATOM   1606 C  CD  . GLU   A 1 227 ? 19.742  -4.078  -3.300  1.00 43.55  ? 232 GLU   A CD  1 
ATOM   1607 O  OE1 . GLU   A 1 227 ? 20.012  -5.146  -2.705  1.00 36.27  ? 232 GLU   A OE1 1 
ATOM   1608 O  OE2 . GLU   A 1 227 ? 20.081  -2.953  -2.873  1.00 35.43  ? 232 GLU   A OE2 1 
ATOM   1609 N  N   . ARG   A 1 228 ? 17.421  -8.047  -6.402  1.00 23.31  ? 233 ARG   A N   1 
ATOM   1610 C  CA  . ARG   A 1 228 ? 17.529  -9.373  -7.029  1.00 23.36  ? 233 ARG   A CA  1 
ATOM   1611 C  C   . ARG   A 1 228 ? 16.713  -9.471  -8.304  1.00 27.13  ? 233 ARG   A C   1 
ATOM   1612 O  O   . ARG   A 1 228 ? 17.160  -10.105 -9.266  1.00 27.14  ? 233 ARG   A O   1 
ATOM   1613 C  CB  . ARG   A 1 228 ? 17.184  -10.490 -6.051  1.00 23.16  ? 233 ARG   A CB  1 
ATOM   1614 C  CG  . ARG   A 1 228 ? 18.191  -10.582 -4.908  1.00 26.67  ? 233 ARG   A CG  1 
ATOM   1615 C  CD  . ARG   A 1 228 ? 17.773  -11.626 -3.899  1.00 36.63  ? 233 ARG   A CD  1 
ATOM   1616 N  NE  . ARG   A 1 228 ? 18.716  -11.695 -2.781  1.00 43.95  ? 233 ARG   A NE  1 
ATOM   1617 C  CZ  . ARG   A 1 228 ? 18.886  -12.767 -2.017  1.00 53.53  ? 233 ARG   A CZ  1 
ATOM   1618 N  NH1 . ARG   A 1 228 ? 18.168  -13.866 -2.231  1.00 41.98  ? 233 ARG   A NH1 1 
ATOM   1619 N  NH2 . ARG   A 1 228 ? 19.764  -12.746 -1.025  1.00 44.33  ? 233 ARG   A NH2 1 
ATOM   1620 N  N   . THR   A 1 229 ? 15.492  -8.870  -8.315  1.00 23.26  ? 234 THR   A N   1 
ATOM   1621 C  CA  . THR   A 1 229 ? 14.618  -8.857  -9.485  1.00 23.00  ? 234 THR   A CA  1 
ATOM   1622 C  C   . THR   A 1 229 ? 15.384  -8.241  -10.672 1.00 26.21  ? 234 THR   A C   1 
ATOM   1623 O  O   . THR   A 1 229 ? 15.413  -8.835  -11.774 1.00 25.20  ? 234 THR   A O   1 
ATOM   1624 C  CB  . THR   A 1 229 ? 13.280  -8.123  -9.182  1.00 24.86  ? 234 THR   A CB  1 
ATOM   1625 O  OG1 . THR   A 1 229 ? 12.527  -8.913  -8.267  1.00 22.89  ? 234 THR   A OG1 1 
ATOM   1626 C  CG2 . THR   A 1 229 ? 12.427  -7.873  -10.448 1.00 25.52  ? 234 THR   A CG2 1 
ATOM   1627 N  N   . PHE   A 1 230 ? 15.984  -7.043  -10.455 1.00 22.28  ? 235 PHE   A N   1 
ATOM   1628 C  CA  . PHE   A 1 230 ? 16.694  -6.369  -11.547 1.00 23.73  ? 235 PHE   A CA  1 
ATOM   1629 C  C   . PHE   A 1 230 ? 17.968  -7.114  -11.918 1.00 28.67  ? 235 PHE   A C   1 
ATOM   1630 O  O   . PHE   A 1 230 ? 18.285  -7.194  -13.098 1.00 27.70  ? 235 PHE   A O   1 
ATOM   1631 C  CB  . PHE   A 1 230 ? 16.950  -4.893  -11.236 1.00 26.03  ? 235 PHE   A CB  1 
ATOM   1632 C  CG  . PHE   A 1 230 ? 15.656  -4.140  -11.072 1.00 26.92  ? 235 PHE   A CG  1 
ATOM   1633 C  CD1 . PHE   A 1 230 ? 14.616  -4.307  -11.983 1.00 30.62  ? 235 PHE   A CD1 1 
ATOM   1634 C  CD2 . PHE   A 1 230 ? 15.480  -3.254  -10.016 1.00 30.67  ? 235 PHE   A CD2 1 
ATOM   1635 C  CE1 . PHE   A 1 230 ? 13.399  -3.629  -11.817 1.00 32.43  ? 235 PHE   A CE1 1 
ATOM   1636 C  CE2 . PHE   A 1 230 ? 14.264  -2.572  -9.857  1.00 33.51  ? 235 PHE   A CE2 1 
ATOM   1637 C  CZ  . PHE   A 1 230 ? 13.234  -2.778  -10.747 1.00 31.63  ? 235 PHE   A CZ  1 
ATOM   1638 N  N   . ASP   A 1 231 ? 18.641  -7.723  -10.941 1.00 26.22  ? 236 ASP   A N   1 
ATOM   1639 C  CA  . ASP   A 1 231 ? 19.853  -8.518  -11.251 1.00 28.35  ? 236 ASP   A CA  1 
ATOM   1640 C  C   . ASP   A 1 231 ? 19.499  -9.679  -12.193 1.00 29.31  ? 236 ASP   A C   1 
ATOM   1641 O  O   . ASP   A 1 231 ? 20.183  -9.908  -13.192 1.00 28.94  ? 236 ASP   A O   1 
ATOM   1642 C  CB  . ASP   A 1 231 ? 20.484  -9.047  -9.966  1.00 31.38  ? 236 ASP   A CB  1 
ATOM   1643 C  CG  . ASP   A 1 231 ? 21.820  -8.408  -9.685  1.00 58.35  ? 236 ASP   A CG  1 
ATOM   1644 O  OD1 . ASP   A 1 231 ? 21.843  -7.355  -9.007  1.00 60.74  ? 236 ASP   A OD1 1 
ATOM   1645 O  OD2 . ASP   A 1 231 ? 22.845  -8.938  -10.175 1.00 70.65  ? 236 ASP   A OD2 1 
ATOM   1646 N  N   . LEU   A 1 232 ? 18.372  -10.341 -11.938 1.00 26.10  ? 237 LEU   A N   1 
ATOM   1647 C  CA  . LEU   A 1 232 ? 17.911  -11.449 -12.777 1.00 26.20  ? 237 LEU   A CA  1 
ATOM   1648 C  C   . LEU   A 1 232 ? 17.518  -10.996 -14.202 1.00 30.28  ? 237 LEU   A C   1 
ATOM   1649 O  O   . LEU   A 1 232 ? 17.853  -11.654 -15.195 1.00 29.40  ? 237 LEU   A O   1 
ATOM   1650 C  CB  . LEU   A 1 232 ? 16.709  -12.127 -12.122 1.00 26.15  ? 237 LEU   A CB  1 
ATOM   1651 C  CG  . LEU   A 1 232 ? 17.013  -12.958 -10.881 1.00 30.87  ? 237 LEU   A CG  1 
ATOM   1652 C  CD1 . LEU   A 1 232 ? 15.748  -13.187 -10.067 1.00 30.07  ? 237 LEU   A CD1 1 
ATOM   1653 C  CD2 . LEU   A 1 232 ? 17.730  -14.276 -11.264 1.00 32.46  ? 237 LEU   A CD2 1 
ATOM   1654 N  N   . LEU   A 1 233 ? 16.836  -9.852  -14.298 1.00 26.50  ? 238 LEU   A N   1 
ATOM   1655 C  CA  . LEU   A 1 233 ? 16.294  -9.405  -15.563 1.00 25.11  ? 238 LEU   A CA  1 
ATOM   1656 C  C   . LEU   A 1 233 ? 17.204  -8.526  -16.405 1.00 28.16  ? 238 LEU   A C   1 
ATOM   1657 O  O   . LEU   A 1 233 ? 17.327  -8.767  -17.607 1.00 27.36  ? 238 LEU   A O   1 
ATOM   1658 C  CB  . LEU   A 1 233 ? 14.949  -8.698  -15.331 1.00 24.67  ? 238 LEU   A CB  1 
ATOM   1659 C  CG  . LEU   A 1 233 ? 13.795  -9.584  -14.801 1.00 26.42  ? 238 LEU   A CG  1 
ATOM   1660 C  CD1 . LEU   A 1 233 ? 12.533  -8.752  -14.601 1.00 26.42  ? 238 LEU   A CD1 1 
ATOM   1661 C  CD2 . LEU   A 1 233 ? 13.522  -10.771 -15.732 1.00 24.61  ? 238 LEU   A CD2 1 
ATOM   1662 N  N   . ILE   A 1 234 ? 17.776  -7.494  -15.802 1.00 26.07  ? 239 ILE   A N   1 
ATOM   1663 C  CA  . ILE   A 1 234 ? 18.555  -6.484  -16.510 1.00 26.48  ? 239 ILE   A CA  1 
ATOM   1664 C  C   . ILE   A 1 234 ? 19.997  -6.396  -16.002 1.00 31.85  ? 239 ILE   A C   1 
ATOM   1665 O  O   . ILE   A 1 234 ? 20.669  -5.378  -16.224 1.00 32.21  ? 239 ILE   A O   1 
ATOM   1666 C  CB  . ILE   A 1 234 ? 17.816  -5.095  -16.481 1.00 28.35  ? 239 ILE   A CB  1 
ATOM   1667 C  CG1 . ILE   A 1 234 ? 17.592  -4.574  -15.018 1.00 27.51  ? 239 ILE   A CG1 1 
ATOM   1668 C  CG2 . ILE   A 1 234 ? 16.493  -5.128  -17.286 1.00 29.22  ? 239 ILE   A CG2 1 
ATOM   1669 C  CD1 . ILE   A 1 234 ? 17.251  -3.029  -14.913 1.00 28.04  ? 239 ILE   A CD1 1 
ATOM   1670 N  N   . GLY   A 1 235 ? 20.470  -7.444  -15.331 1.00 29.95  ? 240 GLY   A N   1 
ATOM   1671 C  CA  . GLY   A 1 235 ? 21.826  -7.436  -14.788 1.00 30.60  ? 240 GLY   A CA  1 
ATOM   1672 C  C   . GLY   A 1 235 ? 22.920  -7.472  -15.847 1.00 36.25  ? 240 GLY   A C   1 
ATOM   1673 O  O   . GLY   A 1 235 ? 23.995  -6.886  -15.657 1.00 36.50  ? 240 GLY   A O   1 
ATOM   1674 N  N   . LYS   A 1 236 ? 22.649  -8.174  -16.953 1.00 33.36  ? 241 LYS   A N   1 
ATOM   1675 C  CA  . LYS   A 1 236 ? 23.590  -8.338  -18.075 1.00 33.23  ? 241 LYS   A CA  1 
ATOM   1676 C  C   . LYS   A 1 236 ? 23.454  -7.256  -19.144 1.00 39.33  ? 241 LYS   A C   1 
ATOM   1677 O  O   . LYS   A 1 236 ? 24.469  -6.840  -19.713 1.00 40.34  ? 241 LYS   A O   1 
ATOM   1678 C  CB  . LYS   A 1 236 ? 23.474  -9.740  -18.684 1.00 34.30  ? 241 LYS   A CB  1 
ATOM   1679 C  CG  . LYS   A 1 236 ? 23.956  -10.840 -17.747 1.00 45.59  ? 241 LYS   A CG  1 
ATOM   1680 C  CD  . LYS   A 1 236 ? 23.805  -12.228 -18.358 1.00 56.97  ? 241 LYS   A CD  1 
ATOM   1681 C  CE  . LYS   A 1 236 ? 24.267  -13.317 -17.416 1.00 72.55  ? 241 LYS   A CE  1 
ATOM   1682 N  NZ  . LYS   A 1 236 ? 25.752  -13.364 -17.289 1.00 83.95  ? 241 LYS   A NZ  1 
ATOM   1683 N  N   . ARG   A 1 237 ? 22.210  -6.798  -19.423 1.00 33.86  ? 242 ARG   A N   1 
ATOM   1684 C  CA  . ARG   A 1 237 ? 21.932  -5.775  -20.439 1.00 33.18  ? 242 ARG   A CA  1 
ATOM   1685 C  C   . ARG   A 1 237 ? 20.631  -5.031  -20.146 1.00 35.59  ? 242 ARG   A C   1 
ATOM   1686 O  O   . ARG   A 1 237 ? 19.746  -5.563  -19.458 1.00 33.85  ? 242 ARG   A O   1 
ATOM   1687 C  CB  . ARG   A 1 237 ? 21.881  -6.419  -21.858 1.00 32.36  ? 242 ARG   A CB  1 
ATOM   1688 C  CG  . ARG   A 1 237 ? 20.584  -7.177  -22.164 1.00 39.96  ? 242 ARG   A CG  1 
ATOM   1689 C  CD  . ARG   A 1 237 ? 20.808  -8.520  -22.826 1.00 46.24  ? 242 ARG   A CD  1 
ATOM   1690 N  NE  . ARG   A 1 237 ? 19.556  -9.276  -22.885 1.00 50.06  ? 242 ARG   A NE  1 
ATOM   1691 C  CZ  . ARG   A 1 237 ? 19.331  -10.435 -22.275 1.00 57.78  ? 242 ARG   A CZ  1 
ATOM   1692 N  NH1 . ARG   A 1 237 ? 20.295  -11.025 -21.577 1.00 50.05  ? 242 ARG   A NH1 1 
ATOM   1693 N  NH2 . ARG   A 1 237 ? 18.150  -11.028 -22.382 1.00 35.95  ? 242 ARG   A NH2 1 
ATOM   1694 N  N   . GLN   A 1 238 ? 20.507  -3.820  -20.717 1.00 32.71  ? 243 GLN   A N   1 
ATOM   1695 C  CA  . GLN   A 1 238 ? 19.313  -2.985  -20.631 1.00 31.87  ? 243 GLN   A CA  1 
ATOM   1696 C  C   . GLN   A 1 238 ? 18.228  -3.604  -21.523 1.00 33.39  ? 243 GLN   A C   1 
ATOM   1697 O  O   . GLN   A 1 238 ? 18.504  -4.075  -22.633 1.00 32.09  ? 243 GLN   A O   1 
ATOM   1698 C  CB  . GLN   A 1 238 ? 19.625  -1.544  -21.058 1.00 33.52  ? 243 GLN   A CB  1 
ATOM   1699 C  CG  . GLN   A 1 238 ? 20.540  -0.810  -20.075 1.00 45.18  ? 243 GLN   A CG  1 
ATOM   1700 C  CD  . GLN   A 1 238 ? 20.357  0.679   -20.148 1.00 73.36  ? 243 GLN   A CD  1 
ATOM   1701 O  OE1 . GLN   A 1 238 ? 19.638  1.278   -19.337 1.00 69.84  ? 243 GLN   A OE1 1 
ATOM   1702 N  NE2 . GLN   A 1 238 ? 20.999  1.309   -21.125 1.00 66.36  ? 243 GLN   A NE2 1 
ATOM   1703 N  N   . ARG   A 1 239 ? 17.000  -3.637  -21.011 1.00 28.00  ? 244 ARG   A N   1 
ATOM   1704 C  CA  . ARG   A 1 239 ? 15.846  -4.217  -21.653 1.00 27.05  ? 244 ARG   A CA  1 
ATOM   1705 C  C   . ARG   A 1 239 ? 14.611  -3.397  -21.315 1.00 29.32  ? 244 ARG   A C   1 
ATOM   1706 O  O   . ARG   A 1 239 ? 14.518  -2.922  -20.174 1.00 29.10  ? 244 ARG   A O   1 
ATOM   1707 C  CB  . ARG   A 1 239 ? 15.599  -5.645  -21.112 1.00 26.23  ? 244 ARG   A CB  1 
ATOM   1708 C  CG  . ARG   A 1 239 ? 16.798  -6.564  -21.187 1.00 26.15  ? 244 ARG   A CG  1 
ATOM   1709 C  CD  . ARG   A 1 239 ? 16.548  -7.856  -20.460 1.00 26.06  ? 244 ARG   A CD  1 
ATOM   1710 N  NE  . ARG   A 1 239 ? 15.630  -8.729  -21.172 1.00 29.11  ? 244 ARG   A NE  1 
ATOM   1711 C  CZ  . ARG   A 1 239 ? 15.311  -9.954  -20.774 1.00 31.32  ? 244 ARG   A CZ  1 
ATOM   1712 N  NH1 . ARG   A 1 239 ? 15.791  -10.437 -19.628 1.00 27.60  ? 244 ARG   A NH1 1 
ATOM   1713 N  NH2 . ARG   A 1 239 ? 14.497  -10.699 -21.502 1.00 28.89  ? 244 ARG   A NH2 1 
ATOM   1714 N  N   . PRO   A 1 240 ? 13.604  -3.335  -22.220 1.00 25.99  ? 245 PRO   A N   1 
ATOM   1715 C  CA  . PRO   A 1 240 ? 12.341  -2.659  -21.867 1.00 25.15  ? 245 PRO   A CA  1 
ATOM   1716 C  C   . PRO   A 1 240 ? 11.577  -3.513  -20.848 1.00 28.19  ? 245 PRO   A C   1 
ATOM   1717 O  O   . PRO   A 1 240 ? 11.544  -4.754  -20.956 1.00 26.31  ? 245 PRO   A O   1 
ATOM   1718 C  CB  . PRO   A 1 240 ? 11.581  -2.553  -23.191 1.00 27.22  ? 245 PRO   A CB  1 
ATOM   1719 C  CG  . PRO   A 1 240 ? 12.188  -3.567  -24.078 1.00 31.22  ? 245 PRO   A CG  1 
ATOM   1720 C  CD  . PRO   A 1 240 ? 13.563  -3.898  -23.592 1.00 26.08  ? 245 PRO   A CD  1 
ATOM   1721 N  N   . ILE   A 1 241 ? 11.003  -2.838  -19.846 1.00 25.17  ? 246 ILE   A N   1 
ATOM   1722 C  CA  . ILE   A 1 241 ? 10.282  -3.489  -18.756 1.00 24.00  ? 246 ILE   A CA  1 
ATOM   1723 C  C   . ILE   A 1 241 ? 8.794   -3.353  -18.951 1.00 25.94  ? 246 ILE   A C   1 
ATOM   1724 O  O   . ILE   A 1 241 ? 8.300   -2.268  -19.254 1.00 26.67  ? 246 ILE   A O   1 
ATOM   1725 C  CB  . ILE   A 1 241 ? 10.746  -2.973  -17.357 1.00 26.58  ? 246 ILE   A CB  1 
ATOM   1726 C  CG1 . ILE   A 1 241 ? 12.259  -3.283  -17.140 1.00 27.63  ? 246 ILE   A CG1 1 
ATOM   1727 C  CG2 . ILE   A 1 241 ? 9.857   -3.586  -16.225 1.00 26.79  ? 246 ILE   A CG2 1 
ATOM   1728 C  CD1 . ILE   A 1 241 ? 12.950  -2.612  -15.860 1.00 26.84  ? 246 ILE   A CD1 1 
ATOM   1729 N  N   . HIS   A 1 242 ? 8.085   -4.471  -18.776 1.00 23.29  ? 247 HIS   A N   1 
ATOM   1730 C  CA  . HIS   A 1 242 ? 6.635   -4.517  -18.780 1.00 22.62  ? 247 HIS   A CA  1 
ATOM   1731 C  C   . HIS   A 1 242 ? 6.253   -4.813  -17.323 1.00 26.20  ? 247 HIS   A C   1 
ATOM   1732 O  O   . HIS   A 1 242 ? 6.547   -5.905  -16.813 1.00 24.53  ? 247 HIS   A O   1 
ATOM   1733 C  CB  . HIS   A 1 242 ? 6.113   -5.635  -19.685 1.00 23.56  ? 247 HIS   A CB  1 
ATOM   1734 C  CG  . HIS   A 1 242 ? 4.630   -5.589  -19.865 1.00 26.39  ? 247 HIS   A CG  1 
ATOM   1735 N  ND1 . HIS   A 1 242 ? 4.067   -5.152  -21.037 1.00 27.84  ? 247 HIS   A ND1 1 
ATOM   1736 C  CD2 . HIS   A 1 242 ? 3.641   -5.857  -18.978 1.00 27.72  ? 247 HIS   A CD2 1 
ATOM   1737 C  CE1 . HIS   A 1 242 ? 2.759   -5.189  -20.844 1.00 27.22  ? 247 HIS   A CE1 1 
ATOM   1738 N  NE2 . HIS   A 1 242 ? 2.458   -5.611  -19.615 1.00 27.09  ? 247 HIS   A NE2 1 
ATOM   1739 N  N   . LEU   A 1 243 ? 5.632   -3.844  -16.652 1.00 24.10  ? 248 LEU   A N   1 
ATOM   1740 C  CA  . LEU   A 1 243 ? 5.193   -4.027  -15.255 1.00 22.06  ? 248 LEU   A CA  1 
ATOM   1741 C  C   . LEU   A 1 243 ? 3.712   -4.412  -15.295 1.00 24.89  ? 248 LEU   A C   1 
ATOM   1742 O  O   . LEU   A 1 243 ? 2.888   -3.590  -15.678 1.00 26.17  ? 248 LEU   A O   1 
ATOM   1743 C  CB  . LEU   A 1 243 ? 5.383   -2.726  -14.424 1.00 21.64  ? 248 LEU   A CB  1 
ATOM   1744 C  CG  . LEU   A 1 243 ? 4.864   -2.780  -12.960 1.00 24.86  ? 248 LEU   A CG  1 
ATOM   1745 C  CD1 . LEU   A 1 243 ? 5.584   -3.876  -12.140 1.00 25.77  ? 248 LEU   A CD1 1 
ATOM   1746 C  CD2 . LEU   A 1 243 ? 5.031   -1.422  -12.287 1.00 27.04  ? 248 LEU   A CD2 1 
ATOM   1747 N  N   . SER   A 1 244 ? 3.382   -5.656  -14.948 1.00 22.11  ? 249 SER   A N   1 
ATOM   1748 C  CA  . SER   A 1 244 ? 1.987   -6.088  -14.932 1.00 22.67  ? 249 SER   A CA  1 
ATOM   1749 C  C   . SER   A 1 244 ? 1.556   -6.118  -13.456 1.00 25.76  ? 249 SER   A C   1 
ATOM   1750 O  O   . SER   A 1 244 ? 1.985   -6.984  -12.695 1.00 24.70  ? 249 SER   A O   1 
ATOM   1751 C  CB  . SER   A 1 244 ? 1.829   -7.448  -15.611 1.00 25.62  ? 249 SER   A CB  1 
ATOM   1752 O  OG  . SER   A 1 244 ? 0.459   -7.570  -15.949 1.00 28.64  ? 249 SER   A OG  1 
ATOM   1753 N  N   . PHE   A 1 245 ? 0.775   -5.104  -13.046 1.00 24.17  ? 250 PHE   A N   1 
ATOM   1754 C  CA  . PHE   A 1 245 ? 0.445   -4.897  -11.637 1.00 23.74  ? 250 PHE   A CA  1 
ATOM   1755 C  C   . PHE   A 1 245 ? -1.015  -5.158  -11.322 1.00 27.78  ? 250 PHE   A C   1 
ATOM   1756 O  O   . PHE   A 1 245 ? -1.875  -4.369  -11.716 1.00 28.04  ? 250 PHE   A O   1 
ATOM   1757 C  CB  . PHE   A 1 245 ? 0.837   -3.468  -11.229 1.00 24.82  ? 250 PHE   A CB  1 
ATOM   1758 C  CG  . PHE   A 1 245 ? 1.120   -3.273  -9.751  1.00 25.79  ? 250 PHE   A CG  1 
ATOM   1759 C  CD1 . PHE   A 1 245 ? 0.113   -3.436  -8.805  1.00 26.77  ? 250 PHE   A CD1 1 
ATOM   1760 C  CD2 . PHE   A 1 245 ? 2.382   -2.876  -9.315  1.00 25.26  ? 250 PHE   A CD2 1 
ATOM   1761 C  CE1 . PHE   A 1 245 ? 0.383   -3.284  -7.438  1.00 27.32  ? 250 PHE   A CE1 1 
ATOM   1762 C  CE2 . PHE   A 1 245 ? 2.633   -2.664  -7.956  1.00 27.51  ? 250 PHE   A CE2 1 
ATOM   1763 C  CZ  . PHE   A 1 245 ? 1.641   -2.892  -7.026  1.00 25.94  ? 250 PHE   A CZ  1 
ATOM   1764 N  N   . ASP   A 1 246 ? -1.276  -6.246  -10.579 1.00 25.22  ? 251 ASP   A N   1 
ATOM   1765 C  CA  . ASP   A 1 246 ? -2.633  -6.607  -10.153 1.00 25.30  ? 251 ASP   A CA  1 
ATOM   1766 C  C   . ASP   A 1 246 ? -2.827  -5.897  -8.798  1.00 28.41  ? 251 ASP   A C   1 
ATOM   1767 O  O   . ASP   A 1 246 ? -2.002  -6.053  -7.879  1.00 27.50  ? 251 ASP   A O   1 
ATOM   1768 C  CB  . ASP   A 1 246 ? -2.765  -8.144  -10.042 1.00 27.17  ? 251 ASP   A CB  1 
ATOM   1769 C  CG  . ASP   A 1 246 ? -4.161  -8.718  -9.733  1.00 32.88  ? 251 ASP   A CG  1 
ATOM   1770 O  OD1 . ASP   A 1 246 ? -4.944  -8.034  -9.056  1.00 31.43  ? 251 ASP   A OD1 1 
ATOM   1771 O  OD2 . ASP   A 1 246 ? -4.396  -9.934  -10.017 1.00 35.48  ? 251 ASP   A OD2 1 
ATOM   1772 N  N   . ILE   A 1 247 ? -3.902  -5.102  -8.673  1.00 25.52  ? 252 ILE   A N   1 
ATOM   1773 C  CA  . ILE   A 1 247 ? -4.189  -4.385  -7.427  1.00 25.80  ? 252 ILE   A CA  1 
ATOM   1774 C  C   . ILE   A 1 247 ? -4.273  -5.317  -6.215  1.00 26.43  ? 252 ILE   A C   1 
ATOM   1775 O  O   . ILE   A 1 247 ? -3.987  -4.870  -5.091  1.00 26.94  ? 252 ILE   A O   1 
ATOM   1776 C  CB  . ILE   A 1 247 ? -5.443  -3.462  -7.537  1.00 28.13  ? 252 ILE   A CB  1 
ATOM   1777 C  CG1 . ILE   A 1 247 ? -5.341  -2.200  -6.593  1.00 28.03  ? 252 ILE   A CG1 1 
ATOM   1778 C  CG2 . ILE   A 1 247 ? -6.741  -4.249  -7.293  1.00 28.68  ? 252 ILE   A CG2 1 
ATOM   1779 C  CD1 . ILE   A 1 247 ? -4.143  -1.217  -6.842  1.00 27.32  ? 252 ILE   A CD1 1 
ATOM   1780 N  N   . ASP   A 1 248 ? -4.613  -6.606  -6.438  1.00 24.87  ? 253 ASP   A N   1 
ATOM   1781 C  CA  . ASP   A 1 248 ? -4.734  -7.562  -5.345  1.00 24.89  ? 253 ASP   A CA  1 
ATOM   1782 C  C   . ASP   A 1 248 ? -3.371  -7.991  -4.774  1.00 25.65  ? 253 ASP   A C   1 
ATOM   1783 O  O   . ASP   A 1 248 ? -3.354  -8.745  -3.808  1.00 26.03  ? 253 ASP   A O   1 
ATOM   1784 C  CB  . ASP   A 1 248 ? -5.637  -8.759  -5.690  1.00 25.93  ? 253 ASP   A CB  1 
ATOM   1785 C  CG  . ASP   A 1 248 ? -5.103  -9.847  -6.603  1.00 32.79  ? 253 ASP   A CG  1 
ATOM   1786 O  OD1 . ASP   A 1 248 ? -3.867  -9.933  -6.774  1.00 30.15  ? 253 ASP   A OD1 1 
ATOM   1787 O  OD2 . ASP   A 1 248 ? -5.915  -10.667 -7.075  1.00 35.77  ? 253 ASP   A OD2 1 
ATOM   1788 N  N   . ALA   A 1 249 ? -2.234  -7.466  -5.330  1.00 24.24  ? 254 ALA   A N   1 
ATOM   1789 C  CA  . ALA   A 1 249 ? -0.922  -7.713  -4.722  1.00 23.64  ? 254 ALA   A CA  1 
ATOM   1790 C  C   . ALA   A 1 249 ? -0.947  -7.060  -3.302  1.00 26.24  ? 254 ALA   A C   1 
ATOM   1791 O  O   . ALA   A 1 249 ? -0.315  -7.555  -2.358  1.00 24.74  ? 254 ALA   A O   1 
ATOM   1792 C  CB  . ALA   A 1 249 ? 0.155   -7.041  -5.558  1.00 24.56  ? 254 ALA   A CB  1 
ATOM   1793 N  N   . PHE   A 1 250 ? -1.635  -5.901  -3.196  1.00 22.52  ? 255 PHE   A N   1 
ATOM   1794 C  CA  . PHE   A 1 250 ? -1.767  -5.187  -1.925  1.00 22.63  ? 255 PHE   A CA  1 
ATOM   1795 C  C   . PHE   A 1 250 ? -2.697  -5.936  -0.967  1.00 26.61  ? 255 PHE   A C   1 
ATOM   1796 O  O   . PHE   A 1 250 ? -3.619  -6.647  -1.384  1.00 25.63  ? 255 PHE   A O   1 
ATOM   1797 C  CB  . PHE   A 1 250 ? -2.347  -3.776  -2.147  1.00 22.93  ? 255 PHE   A CB  1 
ATOM   1798 C  CG  . PHE   A 1 250 ? -1.398  -2.773  -2.750  1.00 23.47  ? 255 PHE   A CG  1 
ATOM   1799 C  CD1 . PHE   A 1 250 ? -0.398  -2.184  -1.977  1.00 24.23  ? 255 PHE   A CD1 1 
ATOM   1800 C  CD2 . PHE   A 1 250 ? -1.501  -2.413  -4.086  1.00 22.99  ? 255 PHE   A CD2 1 
ATOM   1801 C  CE1 . PHE   A 1 250 ? 0.478   -1.242  -2.527  1.00 23.66  ? 255 PHE   A CE1 1 
ATOM   1802 C  CE2 . PHE   A 1 250 ? -0.662  -1.433  -4.624  1.00 25.54  ? 255 PHE   A CE2 1 
ATOM   1803 C  CZ  . PHE   A 1 250 ? 0.354   -0.883  -3.855  1.00 24.41  ? 255 PHE   A CZ  1 
ATOM   1804 N  N   . ASP   A 1 251 ? -2.493  -5.704  0.332   1.00 25.72  ? 256 ASP   A N   1 
ATOM   1805 C  CA  . ASP   A 1 251 ? -3.344  -6.284  1.355   1.00 24.51  ? 256 ASP   A CA  1 
ATOM   1806 C  C   . ASP   A 1 251 ? -4.797  -5.797  1.109   1.00 27.23  ? 256 ASP   A C   1 
ATOM   1807 O  O   . ASP   A 1 251 ? -4.991  -4.637  0.719   1.00 28.42  ? 256 ASP   A O   1 
ATOM   1808 C  CB  . ASP   A 1 251 ? -2.850  -5.874  2.754   1.00 25.50  ? 256 ASP   A CB  1 
ATOM   1809 C  CG  . ASP   A 1 251 ? -3.498  -6.724  3.817   1.00 30.28  ? 256 ASP   A CG  1 
ATOM   1810 O  OD1 . ASP   A 1 251 ? -3.009  -7.850  4.059   1.00 30.25  ? 256 ASP   A OD1 1 
ATOM   1811 O  OD2 . ASP   A 1 251 ? -4.555  -6.321  4.324   1.00 31.17  ? 256 ASP   A OD2 1 
ATOM   1812 N  N   . PRO   A 1 252 ? -5.794  -6.708  1.258   1.00 26.27  ? 257 PRO   A N   1 
ATOM   1813 C  CA  . PRO   A 1 252 ? -7.200  -6.319  1.047   1.00 28.51  ? 257 PRO   A CA  1 
ATOM   1814 C  C   . PRO   A 1 252 ? -7.678  -5.168  1.930   1.00 32.96  ? 257 PRO   A C   1 
ATOM   1815 O  O   . PRO   A 1 252 ? -8.660  -4.535  1.568   1.00 32.43  ? 257 PRO   A O   1 
ATOM   1816 C  CB  . PRO   A 1 252 ? -7.969  -7.601  1.369   1.00 30.65  ? 257 PRO   A CB  1 
ATOM   1817 C  CG  . PRO   A 1 252 ? -6.988  -8.710  1.153   1.00 34.04  ? 257 PRO   A CG  1 
ATOM   1818 C  CD  . PRO   A 1 252 ? -5.691  -8.130  1.631   1.00 28.96  ? 257 PRO   A CD  1 
ATOM   1819 N  N   . THR   A 1 253 ? -6.994  -4.865  3.056   1.00 29.78  ? 258 THR   A N   1 
ATOM   1820 C  CA  . THR   A 1 253 ? -7.351  -3.708  3.889   1.00 29.81  ? 258 THR   A CA  1 
ATOM   1821 C  C   . THR   A 1 253 ? -7.036  -2.380  3.146   1.00 32.66  ? 258 THR   A C   1 
ATOM   1822 O  O   . THR   A 1 253 ? -7.688  -1.364  3.382   1.00 32.40  ? 258 THR   A O   1 
ATOM   1823 C  CB  . THR   A 1 253 ? -6.685  -3.782  5.277   1.00 37.10  ? 258 THR   A CB  1 
ATOM   1824 O  OG1 . THR   A 1 253 ? -5.267  -3.736  5.111   1.00 37.05  ? 258 THR   A OG1 1 
ATOM   1825 C  CG2 . THR   A 1 253 ? -7.107  -5.031  6.073   1.00 35.19  ? 258 THR   A CG2 1 
ATOM   1826 N  N   . LEU   A 1 254 ? -6.029  -2.391  2.244   1.00 27.08  ? 259 LEU   A N   1 
ATOM   1827 C  CA  . LEU   A 1 254 ? -5.634  -1.247  1.428   1.00 27.46  ? 259 LEU   A CA  1 
ATOM   1828 C  C   . LEU   A 1 254 ? -6.316  -1.247  0.056   1.00 33.07  ? 259 LEU   A C   1 
ATOM   1829 O  O   . LEU   A 1 254 ? -6.500  -0.185  -0.536  1.00 33.69  ? 259 LEU   A O   1 
ATOM   1830 C  CB  . LEU   A 1 254 ? -4.118  -1.280  1.189   1.00 27.36  ? 259 LEU   A CB  1 
ATOM   1831 C  CG  . LEU   A 1 254 ? -3.252  -1.298  2.453   1.00 31.61  ? 259 LEU   A CG  1 
ATOM   1832 C  CD1 . LEU   A 1 254 ? -1.818  -1.609  2.100   1.00 31.63  ? 259 LEU   A CD1 1 
ATOM   1833 C  CD2 . LEU   A 1 254 ? -3.348  0.049   3.211   1.00 32.66  ? 259 LEU   A CD2 1 
ATOM   1834 N  N   . ALA   A 1 255 ? -6.604  -2.448  -0.480  1.00 29.61  ? 260 ALA   A N   1 
ATOM   1835 C  CA  . ALA   A 1 255 ? -7.201  -2.597  -1.801  1.00 29.18  ? 260 ALA   A CA  1 
ATOM   1836 C  C   . ALA   A 1 255 ? -8.387  -3.580  -1.726  1.00 31.92  ? 260 ALA   A C   1 
ATOM   1837 O  O   . ALA   A 1 255 ? -8.325  -4.694  -2.259  1.00 31.27  ? 260 ALA   A O   1 
ATOM   1838 C  CB  . ALA   A 1 255 ? -6.139  -3.074  -2.797  1.00 29.39  ? 260 ALA   A CB  1 
ATOM   1839 N  N   . PRO   A 1 256 ? -9.481  -3.197  -1.018  1.00 31.71  ? 261 PRO   A N   1 
ATOM   1840 C  CA  . PRO   A 1 256 ? -10.601 -4.136  -0.846  1.00 31.96  ? 261 PRO   A CA  1 
ATOM   1841 C  C   . PRO   A 1 256 ? -11.444 -4.432  -2.083  1.00 35.06  ? 261 PRO   A C   1 
ATOM   1842 O  O   . PRO   A 1 256 ? -12.020 -5.521  -2.165  1.00 35.68  ? 261 PRO   A O   1 
ATOM   1843 C  CB  . PRO   A 1 256 ? -11.450 -3.472  0.259   1.00 34.09  ? 261 PRO   A CB  1 
ATOM   1844 C  CG  . PRO   A 1 256 ? -11.190 -2.028  0.128   1.00 37.80  ? 261 PRO   A CG  1 
ATOM   1845 C  CD  . PRO   A 1 256 ? -9.726  -1.932  -0.283  1.00 34.00  ? 261 PRO   A CD  1 
ATOM   1846 N  N   . ALA   A 1 257 ? -11.527 -3.476  -3.009  1.00 30.67  ? 262 ALA   A N   1 
ATOM   1847 C  CA  . ALA   A 1 257 ? -12.364 -3.553  -4.220  1.00 30.76  ? 262 ALA   A CA  1 
ATOM   1848 C  C   . ALA   A 1 257 ? -11.694 -4.385  -5.340  1.00 32.54  ? 262 ALA   A C   1 
ATOM   1849 O  O   . ALA   A 1 257 ? -11.174 -3.841  -6.316  1.00 32.99  ? 262 ALA   A O   1 
ATOM   1850 C  CB  . ALA   A 1 257 ? -12.715 -2.142  -4.691  1.00 31.24  ? 262 ALA   A CB  1 
ATOM   1851 N  N   . THR   A 1 258 ? -11.674 -5.709  -5.152  1.00 30.67  ? 263 THR   A N   1 
ATOM   1852 C  CA  . THR   A 1 258 ? -11.041 -6.676  -6.056  1.00 30.51  ? 263 THR   A CA  1 
ATOM   1853 C  C   . THR   A 1 258 ? -11.707 -8.042  -5.886  1.00 34.20  ? 263 THR   A C   1 
ATOM   1854 O  O   . THR   A 1 258 ? -12.177 -8.359  -4.789  1.00 34.65  ? 263 THR   A O   1 
ATOM   1855 C  CB  . THR   A 1 258 ? -9.483  -6.657  -5.852  1.00 35.44  ? 263 THR   A CB  1 
ATOM   1856 O  OG1 . THR   A 1 258 ? -8.817  -7.192  -7.005  1.00 33.28  ? 263 THR   A OG1 1 
ATOM   1857 C  CG2 . THR   A 1 258 ? -9.026  -7.363  -4.577  1.00 32.00  ? 263 THR   A CG2 1 
ATOM   1858 N  N   . GLY   A 1 259 ? -11.718 -8.837  -6.958  1.00 31.66  ? 264 GLY   A N   1 
ATOM   1859 C  CA  . GLY   A 1 259 ? -12.389 -10.136 -6.999  1.00 31.71  ? 264 GLY   A CA  1 
ATOM   1860 C  C   . GLY   A 1 259 ? -11.804 -11.287 -6.220  1.00 36.28  ? 264 GLY   A C   1 
ATOM   1861 O  O   . GLY   A 1 259 ? -12.553 -12.152 -5.742  1.00 38.16  ? 264 GLY   A O   1 
ATOM   1862 N  N   . THR   A 1 260 ? -10.469 -11.359 -6.128  1.00 32.15  ? 265 THR   A N   1 
ATOM   1863 C  CA  . THR   A 1 260 ? -9.842  -12.468 -5.412  1.00 32.09  ? 265 THR   A CA  1 
ATOM   1864 C  C   . THR   A 1 260 ? -8.925  -11.923 -4.313  1.00 35.69  ? 265 THR   A C   1 
ATOM   1865 O  O   . THR   A 1 260 ? -7.703  -12.072 -4.425  1.00 36.14  ? 265 THR   A O   1 
ATOM   1866 C  CB  . THR   A 1 260 ? -9.179  -13.477 -6.372  1.00 40.01  ? 265 THR   A CB  1 
ATOM   1867 O  OG1 . THR   A 1 260 ? -10.050 -13.711 -7.479  1.00 40.92  ? 265 THR   A OG1 1 
ATOM   1868 C  CG2 . THR   A 1 260 ? -8.859  -14.814 -5.684  1.00 40.65  ? 265 THR   A CG2 1 
ATOM   1869 N  N   . PRO   A 1 261 ? -9.475  -11.269 -3.256  1.00 32.36  ? 266 PRO   A N   1 
ATOM   1870 C  CA  . PRO   A 1 261 ? -8.598  -10.762 -2.193  1.00 31.30  ? 266 PRO   A CA  1 
ATOM   1871 C  C   . PRO   A 1 261 ? -7.975  -11.895 -1.396  1.00 33.98  ? 266 PRO   A C   1 
ATOM   1872 O  O   . PRO   A 1 261 ? -8.610  -12.925 -1.150  1.00 33.10  ? 266 PRO   A O   1 
ATOM   1873 C  CB  . PRO   A 1 261 ? -9.532  -9.906  -1.332  1.00 33.37  ? 266 PRO   A CB  1 
ATOM   1874 C  CG  . PRO   A 1 261 ? -10.887 -10.523 -1.533  1.00 37.17  ? 266 PRO   A CG  1 
ATOM   1875 C  CD  . PRO   A 1 261 ? -10.901 -10.975 -2.957  1.00 33.85  ? 266 PRO   A CD  1 
ATOM   1876 N  N   . VAL   A 1 262 ? -6.703  -11.721 -1.040  1.00 27.41  ? 267 VAL   A N   1 
ATOM   1877 C  CA  . VAL   A 1 262 ? -5.963  -12.700 -0.242  1.00 26.96  ? 267 VAL   A CA  1 
ATOM   1878 C  C   . VAL   A 1 262 ? -5.268  -11.891 0.850   1.00 30.55  ? 267 VAL   A C   1 
ATOM   1879 O  O   . VAL   A 1 262 ? -4.479  -10.993 0.550   1.00 29.41  ? 267 VAL   A O   1 
ATOM   1880 C  CB  . VAL   A 1 262 ? -4.930  -13.537 -1.046  1.00 29.43  ? 267 VAL   A CB  1 
ATOM   1881 C  CG1 . VAL   A 1 262 ? -4.348  -14.644 -0.171  1.00 30.05  ? 267 VAL   A CG1 1 
ATOM   1882 C  CG2 . VAL   A 1 262 ? -5.533  -14.118 -2.330  1.00 29.38  ? 267 VAL   A CG2 1 
ATOM   1883 N  N   . VAL   A 1 263 ? -5.575  -12.195 2.103   1.00 28.00  ? 268 VAL   A N   1 
ATOM   1884 C  CA  . VAL   A 1 263 ? -4.989  -11.513 3.259   1.00 27.72  ? 268 VAL   A CA  1 
ATOM   1885 C  C   . VAL   A 1 263 ? -3.440  -11.679 3.279   1.00 29.01  ? 268 VAL   A C   1 
ATOM   1886 O  O   . VAL   A 1 263 ? -2.911  -12.669 2.763   1.00 28.31  ? 268 VAL   A O   1 
ATOM   1887 C  CB  . VAL   A 1 263 ? -5.642  -12.014 4.583   1.00 33.09  ? 268 VAL   A CB  1 
ATOM   1888 C  CG1 . VAL   A 1 263 ? -7.135  -11.653 4.637   1.00 32.80  ? 268 VAL   A CG1 1 
ATOM   1889 C  CG2 . VAL   A 1 263 ? -5.442  -13.515 4.756   1.00 33.45  ? 268 VAL   A CG2 1 
ATOM   1890 N  N   . GLY   A 1 264 ? -2.756  -10.731 3.909   1.00 25.81  ? 269 GLY   A N   1 
ATOM   1891 C  CA  . GLY   A 1 264 ? -1.310  -10.779 4.071   1.00 25.08  ? 269 GLY   A CA  1 
ATOM   1892 C  C   . GLY   A 1 264 ? -0.551  -10.279 2.859   1.00 25.98  ? 269 GLY   A C   1 
ATOM   1893 O  O   . GLY   A 1 264 ? 0.480   -10.854 2.502   1.00 25.53  ? 269 GLY   A O   1 
ATOM   1894 N  N   . GLY   A 1 265 ? -1.032  -9.196  2.266   1.00 24.35  ? 270 GLY   A N   1 
ATOM   1895 C  CA  . GLY   A 1 265 ? -0.435  -8.638  1.056   1.00 23.81  ? 270 GLY   A CA  1 
ATOM   1896 C  C   . GLY   A 1 265 ? 0.587   -7.550  1.292   1.00 25.93  ? 270 GLY   A C   1 
ATOM   1897 O  O   . GLY   A 1 265 ? 1.014   -7.304  2.432   1.00 25.74  ? 270 GLY   A O   1 
ATOM   1898 N  N   . LEU   A 1 266 ? 1.023   -6.915  0.181   1.00 21.89  ? 271 LEU   A N   1 
ATOM   1899 C  CA  . LEU   A 1 266 ? 1.952   -5.788  0.227   1.00 21.58  ? 271 LEU   A CA  1 
ATOM   1900 C  C   . LEU   A 1 266 ? 1.374   -4.640  1.057   1.00 23.73  ? 271 LEU   A C   1 
ATOM   1901 O  O   . LEU   A 1 266 ? 0.176   -4.359  0.993   1.00 23.95  ? 271 LEU   A O   1 
ATOM   1902 C  CB  . LEU   A 1 266 ? 2.225   -5.238  -1.189  1.00 20.82  ? 271 LEU   A CB  1 
ATOM   1903 C  CG  . LEU   A 1 266 ? 2.889   -6.153  -2.205  1.00 22.55  ? 271 LEU   A CG  1 
ATOM   1904 C  CD1 . LEU   A 1 266 ? 2.860   -5.485  -3.562  1.00 22.01  ? 271 LEU   A CD1 1 
ATOM   1905 C  CD2 . LEU   A 1 266 ? 4.374   -6.496  -1.789  1.00 26.63  ? 271 LEU   A CD2 1 
ATOM   1906 N  N   . THR   A 1 267 ? 2.234   -3.940  1.785   1.00 21.80  ? 272 THR   A N   1 
ATOM   1907 C  CA  . THR   A 1 267 ? 1.819   -2.707  2.474   1.00 21.62  ? 272 THR   A CA  1 
ATOM   1908 C  C   . THR   A 1 267 ? 1.824   -1.573  1.424   1.00 24.86  ? 272 THR   A C   1 
ATOM   1909 O  O   . THR   A 1 267 ? 2.369   -1.745  0.307   1.00 23.45  ? 272 THR   A O   1 
ATOM   1910 C  CB  . THR   A 1 267 ? 2.787   -2.355  3.633   1.00 23.75  ? 272 THR   A CB  1 
ATOM   1911 O  OG1 . THR   A 1 267 ? 4.068   -2.061  3.074   1.00 23.04  ? 272 THR   A OG1 1 
ATOM   1912 C  CG2 . THR   A 1 267 ? 2.878   -3.474  4.714   1.00 23.84  ? 272 THR   A CG2 1 
ATOM   1913 N  N   . TYR   A 1 268 ? 1.288   -0.382  1.794   1.00 22.68  ? 273 TYR   A N   1 
ATOM   1914 C  CA  . TYR   A 1 268 ? 1.333   0.763   0.892   1.00 22.25  ? 273 TYR   A CA  1 
ATOM   1915 C  C   . TYR   A 1 268 ? 2.809   1.078   0.566   1.00 24.55  ? 273 TYR   A C   1 
ATOM   1916 O  O   . TYR   A 1 268 ? 3.176   1.294   -0.605  1.00 23.31  ? 273 TYR   A O   1 
ATOM   1917 C  CB  . TYR   A 1 268 ? 0.645   1.973   1.555   1.00 23.25  ? 273 TYR   A CB  1 
ATOM   1918 C  CG  . TYR   A 1 268 ? 0.751   3.248   0.749   1.00 25.39  ? 273 TYR   A CG  1 
ATOM   1919 C  CD1 . TYR   A 1 268 ? -0.194  3.558   -0.226  1.00 27.53  ? 273 TYR   A CD1 1 
ATOM   1920 C  CD2 . TYR   A 1 268 ? 1.819   4.123   0.925   1.00 25.58  ? 273 TYR   A CD2 1 
ATOM   1921 C  CE1 . TYR   A 1 268 ? -0.099  4.724   -0.981  1.00 28.26  ? 273 TYR   A CE1 1 
ATOM   1922 C  CE2 . TYR   A 1 268 ? 1.919   5.305   0.184   1.00 27.13  ? 273 TYR   A CE2 1 
ATOM   1923 C  CZ  . TYR   A 1 268 ? 0.969   5.581   -0.794  1.00 31.95  ? 273 TYR   A CZ  1 
ATOM   1924 O  OH  . TYR   A 1 268 ? 1.061   6.707   -1.572  1.00 34.06  ? 273 TYR   A OH  1 
ATOM   1925 N  N   . ARG   A 1 269 ? 3.643   1.080   1.611   1.00 22.63  ? 274 ARG   A N   1 
ATOM   1926 C  CA  . ARG   A 1 269 ? 5.068   1.393   1.486   1.00 21.51  ? 274 ARG   A CA  1 
ATOM   1927 C  C   . ARG   A 1 269 ? 5.764   0.438   0.555   1.00 22.91  ? 274 ARG   A C   1 
ATOM   1928 O  O   . ARG   A 1 269 ? 6.552   0.878   -0.285  1.00 22.62  ? 274 ARG   A O   1 
ATOM   1929 C  CB  . ARG   A 1 269 ? 5.711   1.383   2.860   1.00 20.08  ? 274 ARG   A CB  1 
ATOM   1930 C  CG  . ARG   A 1 269 ? 5.320   2.650   3.650   1.00 19.67  ? 274 ARG   A CG  1 
ATOM   1931 C  CD  . ARG   A 1 269 ? 5.497   2.477   5.167   1.00 22.48  ? 274 ARG   A CD  1 
ATOM   1932 N  NE  . ARG   A 1 269 ? 6.863   2.113   5.553   1.00 21.58  ? 274 ARG   A NE  1 
ATOM   1933 C  CZ  . ARG   A 1 269 ? 7.250   1.863   6.803   1.00 24.87  ? 274 ARG   A CZ  1 
ATOM   1934 N  NH1 . ARG   A 1 269 ? 6.392   1.988   7.810   1.00 21.56  ? 274 ARG   A NH1 1 
ATOM   1935 N  NH2 . ARG   A 1 269 ? 8.501   1.487   7.056   1.00 20.80  ? 274 ARG   A NH2 1 
ATOM   1936 N  N   . GLU   A 1 270 ? 5.492   -0.875  0.695   1.00 20.11  ? 275 GLU   A N   1 
ATOM   1937 C  CA  . GLU   A 1 270 ? 6.138   -1.845  -0.200  1.00 20.09  ? 275 GLU   A CA  1 
ATOM   1938 C  C   . GLU   A 1 270 ? 5.740   -1.659  -1.656  1.00 23.34  ? 275 GLU   A C   1 
ATOM   1939 O  O   . GLU   A 1 270 ? 6.603   -1.752  -2.535  1.00 23.14  ? 275 GLU   A O   1 
ATOM   1940 C  CB  . GLU   A 1 270 ? 5.872   -3.279  0.236   1.00 20.66  ? 275 GLU   A CB  1 
ATOM   1941 C  CG  . GLU   A 1 270 ? 6.612   -3.658  1.516   1.00 22.66  ? 275 GLU   A CG  1 
ATOM   1942 C  CD  . GLU   A 1 270 ? 6.115   -4.937  2.171   1.00 24.94  ? 275 GLU   A CD  1 
ATOM   1943 O  OE1 . GLU   A 1 270 ? 4.917   -5.276  2.010   1.00 22.75  ? 275 GLU   A OE1 1 
ATOM   1944 O  OE2 . GLU   A 1 270 ? 6.929   -5.603  2.849   1.00 23.92  ? 275 GLU   A OE2 1 
ATOM   1945 N  N   . GLY   A 1 271 ? 4.445   -1.419  -1.911  1.00 19.56  ? 276 GLY   A N   1 
ATOM   1946 C  CA  . GLY   A 1 271 ? 3.960   -1.217  -3.278  1.00 20.22  ? 276 GLY   A CA  1 
ATOM   1947 C  C   . GLY   A 1 271 ? 4.552   0.019   -3.923  1.00 22.85  ? 276 GLY   A C   1 
ATOM   1948 O  O   . GLY   A 1 271 ? 4.924   -0.001  -5.101  1.00 23.00  ? 276 GLY   A O   1 
ATOM   1949 N  N   . MET   A 1 272 ? 4.676   1.110   -3.139  1.00 22.05  ? 277 MET   A N   1 
ATOM   1950 C  CA  . MET   A 1 272 ? 5.283   2.329   -3.643  1.00 22.35  ? 277 MET   A CA  1 
ATOM   1951 C  C   . MET   A 1 272 ? 6.754   2.068   -3.923  1.00 24.90  ? 277 MET   A C   1 
ATOM   1952 O  O   . MET   A 1 272 ? 7.272   2.522   -4.934  1.00 23.01  ? 277 MET   A O   1 
ATOM   1953 C  CB  . MET   A 1 272 ? 5.108   3.496   -2.658  1.00 23.97  ? 277 MET   A CB  1 
ATOM   1954 C  CG  . MET   A 1 272 ? 3.658   3.922   -2.486  1.00 26.05  ? 277 MET   A CG  1 
ATOM   1955 S  SD  . MET   A 1 272 ? 2.839   4.379   -4.054  1.00 27.67  ? 277 MET   A SD  1 
ATOM   1956 C  CE  . MET   A 1 272 ? 1.841   3.026   -4.250  1.00 24.97  ? 277 MET   A CE  1 
ATOM   1957 N  N   . TYR   A 1 273 ? 7.408   1.312   -3.044  1.00 21.61  ? 278 TYR   A N   1 
ATOM   1958 C  CA  . TYR   A 1 273 ? 8.836   1.004   -3.233  1.00 20.41  ? 278 TYR   A CA  1 
ATOM   1959 C  C   . TYR   A 1 273 ? 9.079   0.268   -4.570  1.00 22.64  ? 278 TYR   A C   1 
ATOM   1960 O  O   . TYR   A 1 273 ? 10.015  0.608   -5.315  1.00 21.74  ? 278 TYR   A O   1 
ATOM   1961 C  CB  . TYR   A 1 273 ? 9.373   0.200   -2.055  1.00 20.27  ? 278 TYR   A CB  1 
ATOM   1962 C  CG  . TYR   A 1 273 ? 10.878  0.103   -2.112  1.00 21.75  ? 278 TYR   A CG  1 
ATOM   1963 C  CD1 . TYR   A 1 273 ? 11.681  1.116   -1.595  1.00 24.67  ? 278 TYR   A CD1 1 
ATOM   1964 C  CD2 . TYR   A 1 273 ? 11.499  -0.964  -2.757  1.00 22.45  ? 278 TYR   A CD2 1 
ATOM   1965 C  CE1 . TYR   A 1 273 ? 13.068  1.062   -1.711  1.00 24.86  ? 278 TYR   A CE1 1 
ATOM   1966 C  CE2 . TYR   A 1 273 ? 12.882  -1.025  -2.875  1.00 23.01  ? 278 TYR   A CE2 1 
ATOM   1967 C  CZ  . TYR   A 1 273 ? 13.657  -0.008  -2.367  1.00 25.73  ? 278 TYR   A CZ  1 
ATOM   1968 O  OH  . TYR   A 1 273 ? 15.025  -0.105  -2.465  1.00 27.60  ? 278 TYR   A OH  1 
ATOM   1969 N  N   . ILE   A 1 274 ? 8.255   -0.749  -4.852  1.00 19.87  ? 279 ILE   A N   1 
ATOM   1970 C  CA  . ILE   A 1 274 ? 8.337   -1.511  -6.106  1.00 19.05  ? 279 ILE   A CA  1 
ATOM   1971 C  C   . ILE   A 1 274 ? 8.250   -0.507  -7.284  1.00 22.43  ? 279 ILE   A C   1 
ATOM   1972 O  O   . ILE   A 1 274 ? 9.119   -0.494  -8.157  1.00 21.11  ? 279 ILE   A O   1 
ATOM   1973 C  CB  . ILE   A 1 274 ? 7.194   -2.548  -6.214  1.00 21.43  ? 279 ILE   A CB  1 
ATOM   1974 C  CG1 . ILE   A 1 274 ? 7.357   -3.658  -5.161  1.00 20.79  ? 279 ILE   A CG1 1 
ATOM   1975 C  CG2 . ILE   A 1 274 ? 7.169   -3.172  -7.647  1.00 21.92  ? 279 ILE   A CG2 1 
ATOM   1976 C  CD1 . ILE   A 1 274 ? 6.099   -4.606  -5.101  1.00 23.49  ? 279 ILE   A CD1 1 
ATOM   1977 N  N   . ALA   A 1 275 ? 7.177   0.321   -7.307  1.00 20.76  ? 280 ALA   A N   1 
ATOM   1978 C  CA  . ALA   A 1 275 ? 6.951   1.280   -8.370  1.00 22.32  ? 280 ALA   A CA  1 
ATOM   1979 C  C   . ALA   A 1 275 ? 8.099   2.287   -8.531  1.00 24.37  ? 280 ALA   A C   1 
ATOM   1980 O  O   . ALA   A 1 275 ? 8.563   2.511   -9.662  1.00 23.62  ? 280 ALA   A O   1 
ATOM   1981 C  CB  . ALA   A 1 275 ? 5.595   1.962   -8.174  1.00 23.50  ? 280 ALA   A CB  1 
ATOM   1982 N  N   . GLU   A 1 276 ? 8.619   2.825   -7.403  1.00 22.90  ? 281 GLU   A N   1 
ATOM   1983 C  CA  . GLU   A 1 276 ? 9.759   3.766   -7.398  1.00 22.71  ? 281 GLU   A CA  1 
ATOM   1984 C  C   . GLU   A 1 276 ? 11.009  3.132   -7.983  1.00 25.07  ? 281 GLU   A C   1 
ATOM   1985 O  O   . GLU   A 1 276 ? 11.696  3.777   -8.785  1.00 25.48  ? 281 GLU   A O   1 
ATOM   1986 C  CB  . GLU   A 1 276 ? 10.079  4.188   -5.981  1.00 23.85  ? 281 GLU   A CB  1 
ATOM   1987 C  CG  . GLU   A 1 276 ? 9.039   5.110   -5.399  1.00 26.64  ? 281 GLU   A CG  1 
ATOM   1988 C  CD  . GLU   A 1 276 ? 9.165   5.264   -3.893  1.00 29.33  ? 281 GLU   A CD  1 
ATOM   1989 O  OE1 . GLU   A 1 276 ? 9.989   4.556   -3.252  1.00 26.15  ? 281 GLU   A OE1 1 
ATOM   1990 O  OE2 . GLU   A 1 276 ? 8.422   6.127   -3.365  1.00 28.01  ? 281 GLU   A OE2 1 
ATOM   1991 N  N   . GLU   A 1 277 ? 11.287  1.862   -7.607  1.00 20.69  ? 282 GLU   A N   1 
ATOM   1992 C  CA  . GLU   A 1 277 ? 12.461  1.159   -8.157  1.00 21.65  ? 282 GLU   A CA  1 
ATOM   1993 C  C   . GLU   A 1 277 ? 12.331  0.903   -9.652  1.00 24.74  ? 282 GLU   A C   1 
ATOM   1994 O  O   . GLU   A 1 277 ? 13.321  1.055   -10.377 1.00 25.48  ? 282 GLU   A O   1 
ATOM   1995 C  CB  . GLU   A 1 277 ? 12.775  -0.118  -7.398  1.00 23.56  ? 282 GLU   A CB  1 
ATOM   1996 C  CG  . GLU   A 1 277 ? 13.335  0.173   -6.022  1.00 27.11  ? 282 GLU   A CG  1 
ATOM   1997 C  CD  . GLU   A 1 277 ? 14.525  1.110   -6.032  1.00 33.33  ? 282 GLU   A CD  1 
ATOM   1998 O  OE1 . GLU   A 1 277 ? 15.584  0.730   -6.582  1.00 34.77  ? 282 GLU   A OE1 1 
ATOM   1999 O  OE2 . GLU   A 1 277 ? 14.342  2.277   -5.626  1.00 30.22  ? 282 GLU   A OE2 1 
ATOM   2000 N  N   . ILE   A 1 278 ? 11.121  0.540   -10.109 1.00 21.30  ? 283 ILE   A N   1 
ATOM   2001 C  CA  . ILE   A 1 278 ? 10.833  0.357   -11.546 1.00 22.78  ? 283 ILE   A CA  1 
ATOM   2002 C  C   . ILE   A 1 278 ? 11.089  1.712   -12.273 1.00 26.15  ? 283 ILE   A C   1 
ATOM   2003 O  O   . ILE   A 1 278 ? 11.743  1.737   -13.328 1.00 24.31  ? 283 ILE   A O   1 
ATOM   2004 C  CB  . ILE   A 1 278 ? 9.378   -0.146  -11.761 1.00 26.62  ? 283 ILE   A CB  1 
ATOM   2005 C  CG1 . ILE   A 1 278 ? 9.181   -1.624  -11.259 1.00 27.47  ? 283 ILE   A CG1 1 
ATOM   2006 C  CG2 . ILE   A 1 278 ? 8.935   0.028   -13.241 1.00 28.16  ? 283 ILE   A CG2 1 
ATOM   2007 C  CD1 . ILE   A 1 278 ? 9.672   -2.744  -12.160 1.00 39.02  ? 283 ILE   A CD1 1 
ATOM   2008 N  N   . HIS   A 1 279 ? 10.597  2.833   -11.711 1.00 23.55  ? 284 HIS   A N   1 
ATOM   2009 C  CA  . HIS   A 1 279 ? 10.848  4.159   -12.299 1.00 24.99  ? 284 HIS   A CA  1 
ATOM   2010 C  C   . HIS   A 1 279 ? 12.360  4.419   -12.417 1.00 28.00  ? 284 HIS   A C   1 
ATOM   2011 O  O   . HIS   A 1 279 ? 12.807  4.890   -13.474 1.00 28.22  ? 284 HIS   A O   1 
ATOM   2012 C  CB  . HIS   A 1 279 ? 10.185  5.276   -11.468 1.00 25.56  ? 284 HIS   A CB  1 
ATOM   2013 C  CG  . HIS   A 1 279 ? 10.627  6.648   -11.897 1.00 29.39  ? 284 HIS   A CG  1 
ATOM   2014 N  ND1 . HIS   A 1 279 ? 10.238  7.186   -13.123 1.00 32.14  ? 284 HIS   A ND1 1 
ATOM   2015 C  CD2 . HIS   A 1 279 ? 11.497  7.501   -11.307 1.00 31.98  ? 284 HIS   A CD2 1 
ATOM   2016 C  CE1 . HIS   A 1 279 ? 10.859  8.350   -13.218 1.00 31.49  ? 284 HIS   A CE1 1 
ATOM   2017 N  NE2 . HIS   A 1 279 ? 11.625  8.590   -12.152 1.00 31.94  ? 284 HIS   A NE2 1 
ATOM   2018 N  N   . ASN   A 1 280 ? 13.136  4.134   -11.325 1.00 25.70  ? 285 ASN   A N   1 
ATOM   2019 C  CA  . ASN   A 1 280 ? 14.583  4.392   -11.227 1.00 26.74  ? 285 ASN   A CA  1 
ATOM   2020 C  C   . ASN   A 1 280 ? 15.441  3.670   -12.275 1.00 31.81  ? 285 ASN   A C   1 
ATOM   2021 O  O   . ASN   A 1 280 ? 16.567  4.096   -12.520 1.00 31.09  ? 285 ASN   A O   1 
ATOM   2022 C  CB  . ASN   A 1 280 ? 15.130  4.104   -9.814  1.00 30.05  ? 285 ASN   A CB  1 
ATOM   2023 C  CG  . ASN   A 1 280 ? 14.665  5.090   -8.767  1.00 43.87  ? 285 ASN   A CG  1 
ATOM   2024 O  OD1 . ASN   A 1 280 ? 14.071  6.130   -9.086  1.00 36.70  ? 285 ASN   A OD1 1 
ATOM   2025 N  ND2 . ASN   A 1 280 ? 14.883  4.763   -7.483  1.00 33.96  ? 285 ASN   A ND2 1 
ATOM   2026 N  N   . THR   A 1 281 ? 14.929  2.584   -12.871 1.00 27.55  ? 286 THR   A N   1 
ATOM   2027 C  CA  . THR   A 1 281 ? 15.663  1.854   -13.935 1.00 27.48  ? 286 THR   A CA  1 
ATOM   2028 C  C   . THR   A 1 281 ? 15.756  2.690   -15.207 1.00 30.81  ? 286 THR   A C   1 
ATOM   2029 O  O   . THR   A 1 281 ? 16.718  2.525   -15.969 1.00 31.40  ? 286 THR   A O   1 
ATOM   2030 C  CB  . THR   A 1 281 ? 15.003  0.516   -14.269 1.00 27.38  ? 286 THR   A CB  1 
ATOM   2031 O  OG1 . THR   A 1 281 ? 13.736  0.723   -14.911 1.00 24.93  ? 286 THR   A OG1 1 
ATOM   2032 C  CG2 . THR   A 1 281 ? 14.895  -0.410  -13.054 1.00 28.37  ? 286 THR   A CG2 1 
ATOM   2033 N  N   . GLY   A 1 282 ? 14.741  3.529   -15.436 1.00 26.99  ? 287 GLY   A N   1 
ATOM   2034 C  CA  . GLY   A 1 282 ? 14.597  4.330   -16.647 1.00 27.57  ? 287 GLY   A CA  1 
ATOM   2035 C  C   . GLY   A 1 282 ? 14.188  3.445   -17.822 1.00 30.96  ? 287 GLY   A C   1 
ATOM   2036 O  O   . GLY   A 1 282 ? 14.211  3.903   -18.968 1.00 31.64  ? 287 GLY   A O   1 
ATOM   2037 N  N   . LEU   A 1 283 ? 13.761  2.170   -17.541 1.00 25.71  ? 288 LEU   A N   1 
ATOM   2038 C  CA  . LEU   A 1 283 ? 13.411  1.186   -18.573 1.00 24.99  ? 288 LEU   A CA  1 
ATOM   2039 C  C   . LEU   A 1 283 ? 11.950  0.792   -18.655 1.00 26.75  ? 288 LEU   A C   1 
ATOM   2040 O  O   . LEU   A 1 283 ? 11.615  -0.077  -19.465 1.00 26.90  ? 288 LEU   A O   1 
ATOM   2041 C  CB  . LEU   A 1 283 ? 14.281  -0.080  -18.422 1.00 25.80  ? 288 LEU   A CB  1 
ATOM   2042 C  CG  . LEU   A 1 283 ? 15.769  0.111   -18.674 1.00 29.09  ? 288 LEU   A CG  1 
ATOM   2043 C  CD1 . LEU   A 1 283 ? 16.568  -1.056  -18.135 1.00 28.78  ? 288 LEU   A CD1 1 
ATOM   2044 C  CD2 . LEU   A 1 283 ? 16.060  0.325   -20.173 1.00 29.47  ? 288 LEU   A CD2 1 
ATOM   2045 N  N   . LEU   A 1 284 ? 11.066  1.405   -17.841 1.00 24.44  ? 289 LEU   A N   1 
ATOM   2046 C  CA  . LEU   A 1 284 ? 9.649   1.093   -17.896 1.00 24.30  ? 289 LEU   A CA  1 
ATOM   2047 C  C   . LEU   A 1 284 ? 9.075   1.446   -19.272 1.00 29.15  ? 289 LEU   A C   1 
ATOM   2048 O  O   . LEU   A 1 284 ? 9.163   2.596   -19.711 1.00 28.78  ? 289 LEU   A O   1 
ATOM   2049 C  CB  . LEU   A 1 284 ? 8.848   1.772   -16.774 1.00 24.11  ? 289 LEU   A CB  1 
ATOM   2050 C  CG  . LEU   A 1 284 ? 7.346   1.467   -16.791 1.00 27.31  ? 289 LEU   A CG  1 
ATOM   2051 C  CD1 . LEU   A 1 284 ? 7.054   -0.016  -16.462 1.00 27.66  ? 289 LEU   A CD1 1 
ATOM   2052 C  CD2 . LEU   A 1 284 ? 6.623   2.359   -15.811 1.00 29.14  ? 289 LEU   A CD2 1 
ATOM   2053 N  N   . SER   A 1 285 ? 8.538   0.447   -19.952 1.00 26.50  ? 290 SER   A N   1 
ATOM   2054 C  CA  . SER   A 1 285 ? 8.025   0.583   -21.313 1.00 26.12  ? 290 SER   A CA  1 
ATOM   2055 C  C   . SER   A 1 285 ? 6.508   0.387   -21.411 1.00 29.66  ? 290 SER   A C   1 
ATOM   2056 O  O   . SER   A 1 285 ? 5.852   0.932   -22.306 1.00 29.33  ? 290 SER   A O   1 
ATOM   2057 C  CB  . SER   A 1 285 ? 8.792   -0.363  -22.233 1.00 29.80  ? 290 SER   A CB  1 
ATOM   2058 O  OG  . SER   A 1 285 ? 8.364   -0.257  -23.580 1.00 30.63  ? 290 SER   A OG  1 
ATOM   2059 N  N   . ALA   A 1 286 ? 5.938   -0.415  -20.507 1.00 26.55  ? 291 ALA   A N   1 
ATOM   2060 C  CA  . ALA   A 1 286 ? 4.496   -0.627  -20.446 1.00 25.78  ? 291 ALA   A CA  1 
ATOM   2061 C  C   . ALA   A 1 286 ? 4.142   -1.000  -19.012 1.00 29.52  ? 291 ALA   A C   1 
ATOM   2062 O  O   . ALA   A 1 286 ? 4.961   -1.593  -18.318 1.00 27.70  ? 291 ALA   A O   1 
ATOM   2063 C  CB  . ALA   A 1 286 ? 4.049   -1.727  -21.403 1.00 26.67  ? 291 ALA   A CB  1 
ATOM   2064 N  N   . LEU   A 1 287 ? 2.942   -0.628  -18.592 1.00 26.71  ? 292 LEU   A N   1 
ATOM   2065 C  CA  . LEU   A 1 287 ? 2.409   -0.906  -17.266 1.00 27.64  ? 292 LEU   A CA  1 
ATOM   2066 C  C   . LEU   A 1 287 ? 0.946   -1.302  -17.382 1.00 30.13  ? 292 LEU   A C   1 
ATOM   2067 O  O   . LEU   A 1 287 ? 0.191   -0.612  -18.055 1.00 30.00  ? 292 LEU   A O   1 
ATOM   2068 C  CB  . LEU   A 1 287 ? 2.573   0.337   -16.362 1.00 28.34  ? 292 LEU   A CB  1 
ATOM   2069 C  CG  . LEU   A 1 287 ? 2.056   0.260   -14.917 1.00 34.15  ? 292 LEU   A CG  1 
ATOM   2070 C  CD1 . LEU   A 1 287 ? 2.703   1.321   -14.091 1.00 34.74  ? 292 LEU   A CD1 1 
ATOM   2071 C  CD2 . LEU   A 1 287 ? 0.579   0.512   -14.832 1.00 36.82  ? 292 LEU   A CD2 1 
ATOM   2072 N  N   . ASP   A 1 288 ? 0.539   -2.395  -16.728 1.00 25.88  ? 293 ASP   A N   1 
ATOM   2073 C  CA  . ASP   A 1 288 ? -0.881  -2.786  -16.665 1.00 24.78  ? 293 ASP   A CA  1 
ATOM   2074 C  C   . ASP   A 1 288 ? -1.295  -2.548  -15.208 1.00 28.59  ? 293 ASP   A C   1 
ATOM   2075 O  O   . ASP   A 1 288 ? -0.570  -2.953  -14.285 1.00 28.99  ? 293 ASP   A O   1 
ATOM   2076 C  CB  . ASP   A 1 288 ? -1.080  -4.288  -16.949 1.00 25.66  ? 293 ASP   A CB  1 
ATOM   2077 C  CG  . ASP   A 1 288 ? -0.455  -4.786  -18.235 1.00 30.32  ? 293 ASP   A CG  1 
ATOM   2078 O  OD1 . ASP   A 1 288 ? -0.441  -4.017  -19.218 1.00 30.83  ? 293 ASP   A OD1 1 
ATOM   2079 O  OD2 . ASP   A 1 288 ? 0.022   -5.952  -18.254 1.00 30.46  ? 293 ASP   A OD2 1 
ATOM   2080 N  N   . LEU   A 1 289 ? -2.462  -1.936  -14.990 1.00 27.13  ? 294 LEU   A N   1 
ATOM   2081 C  CA  . LEU   A 1 289 ? -2.990  -1.785  -13.633 1.00 25.95  ? 294 LEU   A CA  1 
ATOM   2082 C  C   . LEU   A 1 289 ? -4.351  -2.420  -13.688 1.00 29.67  ? 294 LEU   A C   1 
ATOM   2083 O  O   . LEU   A 1 289 ? -5.291  -1.829  -14.230 1.00 28.86  ? 294 LEU   A O   1 
ATOM   2084 C  CB  . LEU   A 1 289 ? -3.049  -0.322  -13.164 1.00 25.66  ? 294 LEU   A CB  1 
ATOM   2085 C  CG  . LEU   A 1 289 ? -3.126  -0.088  -11.620 1.00 30.21  ? 294 LEU   A CG  1 
ATOM   2086 C  CD1 . LEU   A 1 289 ? -4.313  -0.791  -10.996 1.00 30.51  ? 294 LEU   A CD1 1 
ATOM   2087 C  CD2 . LEU   A 1 289 ? -1.830  -0.523  -10.904 1.00 32.29  ? 294 LEU   A CD2 1 
ATOM   2088 N  N   . VAL   A 1 290 ? -4.434  -3.662  -13.197 1.00 26.79  ? 295 VAL   A N   1 
ATOM   2089 C  CA  . VAL   A 1 290 ? -5.637  -4.490  -13.327 1.00 27.12  ? 295 VAL   A CA  1 
ATOM   2090 C  C   . VAL   A 1 290 ? -6.337  -4.906  -12.006 1.00 31.97  ? 295 VAL   A C   1 
ATOM   2091 O  O   . VAL   A 1 290 ? -5.813  -4.723  -10.900 1.00 30.05  ? 295 VAL   A O   1 
ATOM   2092 C  CB  . VAL   A 1 290 ? -5.292  -5.757  -14.156 1.00 29.85  ? 295 VAL   A CB  1 
ATOM   2093 C  CG1 . VAL   A 1 290 ? -4.760  -5.398  -15.557 1.00 29.70  ? 295 VAL   A CG1 1 
ATOM   2094 C  CG2 . VAL   A 1 290 ? -4.295  -6.634  -13.408 1.00 29.21  ? 295 VAL   A CG2 1 
ATOM   2095 N  N   . GLU   A 1 291 ? -7.562  -5.480  -12.176 1.00 29.16  ? 296 GLU   A N   1 
ATOM   2096 C  CA  . GLU   A 1 291 ? -8.423  -6.150  -11.202 1.00 28.78  ? 296 GLU   A CA  1 
ATOM   2097 C  C   . GLU   A 1 291 ? -9.064  -5.205  -10.149 1.00 32.57  ? 296 GLU   A C   1 
ATOM   2098 O  O   . GLU   A 1 291 ? -9.558  -5.669  -9.112  1.00 32.91  ? 296 GLU   A O   1 
ATOM   2099 C  CB  . GLU   A 1 291 ? -7.699  -7.352  -10.552 1.00 29.80  ? 296 GLU   A CB  1 
ATOM   2100 C  CG  . GLU   A 1 291 ? -7.385  -8.481  -11.541 1.00 32.22  ? 296 GLU   A CG  1 
ATOM   2101 C  CD  . GLU   A 1 291 ? -8.499  -9.458  -11.880 1.00 43.90  ? 296 GLU   A CD  1 
ATOM   2102 O  OE1 . GLU   A 1 291 ? -9.567  -9.394  -11.230 1.00 42.61  ? 296 GLU   A OE1 1 
ATOM   2103 O  OE2 . GLU   A 1 291 ? -8.287  -10.327 -12.758 1.00 33.90  ? 296 GLU   A OE2 1 
ATOM   2104 N  N   . VAL   A 1 292 ? -9.171  -3.910  -10.472 1.00 28.69  ? 297 VAL   A N   1 
ATOM   2105 C  CA  . VAL   A 1 292 ? -9.874  -2.980  -9.572  1.00 28.79  ? 297 VAL   A CA  1 
ATOM   2106 C  C   . VAL   A 1 292 ? -11.363 -3.184  -9.925  1.00 35.86  ? 297 VAL   A C   1 
ATOM   2107 O  O   . VAL   A 1 292 ? -11.744 -2.959  -11.072 1.00 36.65  ? 297 VAL   A O   1 
ATOM   2108 C  CB  . VAL   A 1 292 ? -9.444  -1.503  -9.787  1.00 31.27  ? 297 VAL   A CB  1 
ATOM   2109 C  CG1 . VAL   A 1 292 ? -10.357 -0.529  -9.018  1.00 32.31  ? 297 VAL   A CG1 1 
ATOM   2110 C  CG2 . VAL   A 1 292 ? -7.981  -1.287  -9.389  1.00 30.33  ? 297 VAL   A CG2 1 
ATOM   2111 N  N   . ASN   A 1 293 ? -12.161 -3.684  -8.966  1.00 34.79  ? 298 ASN   A N   1 
ATOM   2112 C  CA  . ASN   A 1 293 ? -13.591 -3.915  -9.152  1.00 34.31  ? 298 ASN   A CA  1 
ATOM   2113 C  C   . ASN   A 1 293 ? -14.336 -3.090  -8.084  1.00 38.99  ? 298 ASN   A C   1 
ATOM   2114 O  O   . ASN   A 1 293 ? -14.626 -3.596  -6.996  1.00 38.45  ? 298 ASN   A O   1 
ATOM   2115 C  CB  . ASN   A 1 293 ? -13.937 -5.417  -9.100  1.00 36.42  ? 298 ASN   A CB  1 
ATOM   2116 C  CG  . ASN   A 1 293 ? -15.406 -5.692  -9.388  1.00 44.60  ? 298 ASN   A CG  1 
ATOM   2117 O  OD1 . ASN   A 1 293 ? -16.237 -4.791  -9.380  1.00 39.05  ? 298 ASN   A OD1 1 
ATOM   2118 N  ND2 . ASN   A 1 293 ? -15.762 -6.928  -9.632  1.00 36.66  ? 298 ASN   A ND2 1 
ATOM   2119 N  N   . PRO   A 1 294 ? -14.657 -1.815  -8.398  1.00 38.46  ? 299 PRO   A N   1 
ATOM   2120 C  CA  . PRO   A 1 294 ? -15.326 -0.938  -7.409  1.00 39.98  ? 299 PRO   A CA  1 
ATOM   2121 C  C   . PRO   A 1 294 ? -16.677 -1.414  -6.873  1.00 48.64  ? 299 PRO   A C   1 
ATOM   2122 O  O   . PRO   A 1 294 ? -17.055 -1.011  -5.773  1.00 49.59  ? 299 PRO   A O   1 
ATOM   2123 C  CB  . PRO   A 1 294 ? -15.461 0.403   -8.145  1.00 41.22  ? 299 PRO   A CB  1 
ATOM   2124 C  CG  . PRO   A 1 294 ? -15.304 0.087   -9.562  1.00 45.29  ? 299 PRO   A CG  1 
ATOM   2125 C  CD  . PRO   A 1 294 ? -14.379 -1.081  -9.646  1.00 40.57  ? 299 PRO   A CD  1 
ATOM   2126 N  N   . GLN   A 1 295 ? -17.376 -2.289  -7.615  1.00 46.59  ? 300 GLN   A N   1 
ATOM   2127 C  CA  . GLN   A 1 295 ? -18.673 -2.831  -7.209  1.00 47.02  ? 300 GLN   A CA  1 
ATOM   2128 C  C   . GLN   A 1 295 ? -18.554 -3.805  -6.029  1.00 51.44  ? 300 GLN   A C   1 
ATOM   2129 O  O   . GLN   A 1 295 ? -19.541 -4.017  -5.318  1.00 51.81  ? 300 GLN   A O   1 
ATOM   2130 C  CB  . GLN   A 1 295 ? -19.378 -3.510  -8.396  1.00 48.31  ? 300 GLN   A CB  1 
ATOM   2131 C  CG  . GLN   A 1 295 ? -19.735 -2.561  -9.541  1.00 61.95  ? 300 GLN   A CG  1 
ATOM   2132 C  CD  . GLN   A 1 295 ? -20.715 -3.158  -10.527 1.00 77.00  ? 300 GLN   A CD  1 
ATOM   2133 O  OE1 . GLN   A 1 295 ? -20.920 -4.377  -10.599 1.00 70.42  ? 300 GLN   A OE1 1 
ATOM   2134 N  NE2 . GLN   A 1 295 ? -21.348 -2.303  -11.315 1.00 71.18  ? 300 GLN   A NE2 1 
ATOM   2135 N  N   . LEU   A 1 296 ? -17.344 -4.382  -5.808  1.00 46.74  ? 301 LEU   A N   1 
ATOM   2136 C  CA  . LEU   A 1 296 ? -17.098 -5.339  -4.724  1.00 46.08  ? 301 LEU   A CA  1 
ATOM   2137 C  C   . LEU   A 1 296 ? -16.759 -4.689  -3.376  1.00 50.55  ? 301 LEU   A C   1 
ATOM   2138 O  O   . LEU   A 1 296 ? -16.612 -5.398  -2.374  1.00 51.31  ? 301 LEU   A O   1 
ATOM   2139 C  CB  . LEU   A 1 296 ? -16.032 -6.376  -5.123  1.00 45.63  ? 301 LEU   A CB  1 
ATOM   2140 C  CG  . LEU   A 1 296 ? -16.414 -7.328  -6.261  1.00 49.53  ? 301 LEU   A CG  1 
ATOM   2141 C  CD1 . LEU   A 1 296 ? -15.332 -8.321  -6.495  1.00 48.83  ? 301 LEU   A CD1 1 
ATOM   2142 C  CD2 . LEU   A 1 296 ? -17.723 -8.076  -5.975  1.00 51.43  ? 301 LEU   A CD2 1 
ATOM   2143 N  N   . ALA   A 1 297 ? -16.657 -3.355  -3.346  1.00 47.13  ? 302 ALA   A N   1 
ATOM   2144 C  CA  . ALA   A 1 297 ? -16.394 -2.618  -2.118  1.00 48.07  ? 302 ALA   A CA  1 
ATOM   2145 C  C   . ALA   A 1 297 ? -17.705 -2.525  -1.295  1.00 53.97  ? 302 ALA   A C   1 
ATOM   2146 O  O   . ALA   A 1 297 ? -18.781 -2.348  -1.876  1.00 53.83  ? 302 ALA   A O   1 
ATOM   2147 C  CB  . ALA   A 1 297 ? -15.879 -1.230  -2.457  1.00 48.95  ? 302 ALA   A CB  1 
ATOM   2148 N  N   . THR   A 1 298 ? -17.617 -2.664  0.044   1.00 52.45  ? 303 THR   A N   1 
ATOM   2149 C  CA  . THR   A 1 298 ? -18.791 -2.609  0.941   1.00 53.32  ? 303 THR   A CA  1 
ATOM   2150 C  C   . THR   A 1 298 ? -19.336 -1.180  1.132   1.00 58.83  ? 303 THR   A C   1 
ATOM   2151 O  O   . THR   A 1 298 ? -20.465 -1.014  1.610   1.00 59.10  ? 303 THR   A O   1 
ATOM   2152 C  CB  . THR   A 1 298 ? -18.510 -3.297  2.288   1.00 61.56  ? 303 THR   A CB  1 
ATOM   2153 O  OG1 . THR   A 1 298 ? -17.342 -2.729  2.871   1.00 62.18  ? 303 THR   A OG1 1 
ATOM   2154 C  CG2 . THR   A 1 298 ? -18.362 -4.809  2.162   1.00 60.38  ? 303 THR   A CG2 1 
ATOM   2155 N  N   . SER   A 1 299 ? -18.531 -0.165  0.759   1.00 55.38  ? 304 SER   A N   1 
ATOM   2156 C  CA  . SER   A 1 299 ? -18.837 1.266   0.839   1.00 55.23  ? 304 SER   A CA  1 
ATOM   2157 C  C   . SER   A 1 299 ? -18.166 2.031   -0.322  1.00 59.60  ? 304 SER   A C   1 
ATOM   2158 O  O   . SER   A 1 299 ? -17.261 1.494   -0.973  1.00 58.68  ? 304 SER   A O   1 
ATOM   2159 C  CB  . SER   A 1 299 ? -18.368 1.828   2.177   1.00 58.38  ? 304 SER   A CB  1 
ATOM   2160 O  OG  . SER   A 1 299 ? -16.969 1.663   2.345   1.00 64.05  ? 304 SER   A OG  1 
ATOM   2161 N  N   . GLU   A 1 300 ? -18.598 3.287   -0.560  1.00 56.61  ? 305 GLU   A N   1 
ATOM   2162 C  CA  . GLU   A 1 300 ? -18.067 4.154   -1.616  1.00 56.70  ? 305 GLU   A CA  1 
ATOM   2163 C  C   . GLU   A 1 300 ? -16.614 4.540   -1.344  1.00 59.70  ? 305 GLU   A C   1 
ATOM   2164 O  O   . GLU   A 1 300 ? -15.809 4.562   -2.279  1.00 59.15  ? 305 GLU   A O   1 
ATOM   2165 C  CB  . GLU   A 1 300 ? -18.935 5.415   -1.779  1.00 58.56  ? 305 GLU   A CB  1 
ATOM   2166 C  CG  . GLU   A 1 300 ? -18.688 6.169   -3.075  1.00 71.91  ? 305 GLU   A CG  1 
ATOM   2167 C  CD  . GLU   A 1 300 ? -19.384 7.511   -3.156  1.00 97.54  ? 305 GLU   A CD  1 
ATOM   2168 O  OE1 . GLU   A 1 300 ? -20.605 7.534   -3.432  1.00 99.18  ? 305 GLU   A OE1 1 
ATOM   2169 O  OE2 . GLU   A 1 300 ? -18.707 8.543   -2.944  1.00 91.68  ? 305 GLU   A OE2 1 
ATOM   2170 N  N   . GLU   A 1 301 ? -16.284 4.845   -0.071  1.00 55.59  ? 306 GLU   A N   1 
ATOM   2171 C  CA  . GLU   A 1 301 ? -14.931 5.224   0.339   1.00 55.05  ? 306 GLU   A CA  1 
ATOM   2172 C  C   . GLU   A 1 301 ? -13.922 4.084   0.115   1.00 55.28  ? 306 GLU   A C   1 
ATOM   2173 O  O   . GLU   A 1 301 ? -12.790 4.377   -0.251  1.00 54.73  ? 306 GLU   A O   1 
ATOM   2174 C  CB  . GLU   A 1 301 ? -14.879 5.792   1.777   1.00 56.88  ? 306 GLU   A CB  1 
ATOM   2175 C  CG  . GLU   A 1 301 ? -15.223 4.822   2.900   1.00 73.49  ? 306 GLU   A CG  1 
ATOM   2176 C  CD  . GLU   A 1 301 ? -15.095 5.412   4.293   1.00 104.45 ? 306 GLU   A CD  1 
ATOM   2177 O  OE1 . GLU   A 1 301 ? -13.948 5.634   4.745   1.00 101.58 ? 306 GLU   A OE1 1 
ATOM   2178 O  OE2 . GLU   A 1 301 ? -16.145 5.646   4.936   1.00 101.59 ? 306 GLU   A OE2 1 
ATOM   2179 N  N   . GLU   A 1 302 ? -14.346 2.803   0.283   1.00 49.11  ? 307 GLU   A N   1 
ATOM   2180 C  CA  . GLU   A 1 302 ? -13.509 1.622   0.042   1.00 48.21  ? 307 GLU   A CA  1 
ATOM   2181 C  C   . GLU   A 1 302 ? -13.169 1.498   -1.454  1.00 50.32  ? 307 GLU   A C   1 
ATOM   2182 O  O   . GLU   A 1 302 ? -12.022 1.177   -1.795  1.00 49.68  ? 307 GLU   A O   1 
ATOM   2183 C  CB  . GLU   A 1 302 ? -14.187 0.339   0.548   1.00 49.73  ? 307 GLU   A CB  1 
ATOM   2184 C  CG  . GLU   A 1 302 ? -13.992 0.077   2.036   1.00 61.01  ? 307 GLU   A CG  1 
ATOM   2185 C  CD  . GLU   A 1 302 ? -13.966 -1.384  2.453   1.00 88.01  ? 307 GLU   A CD  1 
ATOM   2186 O  OE1 . GLU   A 1 302 ? -14.682 -2.209  1.835   1.00 82.66  ? 307 GLU   A OE1 1 
ATOM   2187 O  OE2 . GLU   A 1 302 ? -13.230 -1.703  3.415   1.00 85.27  ? 307 GLU   A OE2 1 
ATOM   2188 N  N   . ALA   A 1 303 ? -14.160 1.772   -2.345  1.00 44.49  ? 308 ALA   A N   1 
ATOM   2189 C  CA  . ALA   A 1 303 ? -13.971 1.752   -3.804  1.00 43.53  ? 308 ALA   A CA  1 
ATOM   2190 C  C   . ALA   A 1 303 ? -12.981 2.850   -4.189  1.00 45.86  ? 308 ALA   A C   1 
ATOM   2191 O  O   . ALA   A 1 303 ? -12.014 2.579   -4.911  1.00 44.94  ? 308 ALA   A O   1 
ATOM   2192 C  CB  . ALA   A 1 303 ? -15.297 1.966   -4.518  1.00 44.24  ? 308 ALA   A CB  1 
ATOM   2193 N  N   . LYS   A 1 304 ? -13.205 4.081   -3.660  1.00 41.09  ? 309 LYS   A N   1 
ATOM   2194 C  CA  . LYS   A 1 304 ? -12.348 5.247   -3.881  1.00 40.30  ? 309 LYS   A CA  1 
ATOM   2195 C  C   . LYS   A 1 304 ? -10.931 5.046   -3.324  1.00 41.54  ? 309 LYS   A C   1 
ATOM   2196 O  O   . LYS   A 1 304 ? -9.995  5.553   -3.925  1.00 40.62  ? 309 LYS   A O   1 
ATOM   2197 C  CB  . LYS   A 1 304 ? -12.966 6.517   -3.286  1.00 42.63  ? 309 LYS   A CB  1 
ATOM   2198 C  CG  . LYS   A 1 304 ? -14.083 7.128   -4.128  1.00 62.99  ? 309 LYS   A CG  1 
ATOM   2199 C  CD  . LYS   A 1 304 ? -14.529 8.474   -3.559  1.00 75.70  ? 309 LYS   A CD  1 
ATOM   2200 C  CE  . LYS   A 1 304 ? -15.649 9.102   -4.353  1.00 88.88  ? 309 LYS   A CE  1 
ATOM   2201 N  NZ  . LYS   A 1 304 ? -16.079 10.401  -3.768  1.00 97.08  ? 309 LYS   A NZ  1 
ATOM   2202 N  N   . THR   A 1 305 ? -10.771 4.339   -2.183  1.00 37.01  ? 310 THR   A N   1 
ATOM   2203 C  CA  . THR   A 1 305 ? -9.438  4.076   -1.603  1.00 35.93  ? 310 THR   A CA  1 
ATOM   2204 C  C   . THR   A 1 305 ? -8.627  3.190   -2.579  1.00 37.32  ? 310 THR   A C   1 
ATOM   2205 O  O   . THR   A 1 305 ? -7.434  3.442   -2.800  1.00 34.54  ? 310 THR   A O   1 
ATOM   2206 C  CB  . THR   A 1 305 ? -9.561  3.467   -0.191  1.00 43.84  ? 310 THR   A CB  1 
ATOM   2207 O  OG1 . THR   A 1 305 ? -10.231 4.403   0.650   1.00 48.64  ? 310 THR   A OG1 1 
ATOM   2208 C  CG2 . THR   A 1 305 ? -8.219  3.155   0.439   1.00 39.21  ? 310 THR   A CG2 1 
ATOM   2209 N  N   . THR   A 1 306 ? -9.292  2.172   -3.165  1.00 34.12  ? 311 THR   A N   1 
ATOM   2210 C  CA  . THR   A 1 306 ? -8.676  1.230   -4.108  1.00 33.55  ? 311 THR   A CA  1 
ATOM   2211 C  C   . THR   A 1 306 ? -8.221  1.964   -5.379  1.00 36.39  ? 311 THR   A C   1 
ATOM   2212 O  O   . THR   A 1 306 ? -7.076  1.802   -5.818  1.00 33.73  ? 311 THR   A O   1 
ATOM   2213 C  CB  . THR   A 1 306 ? -9.605  0.048   -4.384  1.00 32.41  ? 311 THR   A CB  1 
ATOM   2214 O  OG1 . THR   A 1 306 ? -10.047 -0.516  -3.144  1.00 29.94  ? 311 THR   A OG1 1 
ATOM   2215 C  CG2 . THR   A 1 306 ? -8.927  -1.041  -5.218  1.00 31.45  ? 311 THR   A CG2 1 
ATOM   2216 N  N   . ALA   A 1 307 ? -9.111  2.820   -5.933  1.00 32.84  ? 312 ALA   A N   1 
ATOM   2217 C  CA  . ALA   A 1 307 ? -8.824  3.623   -7.115  1.00 32.58  ? 312 ALA   A CA  1 
ATOM   2218 C  C   . ALA   A 1 307 ? -7.701  4.623   -6.850  1.00 33.50  ? 312 ALA   A C   1 
ATOM   2219 O  O   . ALA   A 1 307 ? -6.856  4.831   -7.721  1.00 32.92  ? 312 ALA   A O   1 
ATOM   2220 C  CB  . ALA   A 1 307 ? -10.092 4.347   -7.565  1.00 34.09  ? 312 ALA   A CB  1 
ATOM   2221 N  N   . ASN   A 1 308 ? -7.673  5.233   -5.644  1.00 30.28  ? 313 ASN   A N   1 
ATOM   2222 C  CA  . ASN   A 1 308 ? -6.618  6.184   -5.273  1.00 29.36  ? 313 ASN   A CA  1 
ATOM   2223 C  C   . ASN   A 1 308 ? -5.250  5.462   -5.216  1.00 30.13  ? 313 ASN   A C   1 
ATOM   2224 O  O   . ASN   A 1 308 ? -4.248  6.022   -5.650  1.00 28.32  ? 313 ASN   A O   1 
ATOM   2225 C  CB  . ASN   A 1 308 ? -6.918  6.842   -3.923  1.00 30.96  ? 313 ASN   A CB  1 
ATOM   2226 C  CG  . ASN   A 1 308 ? -8.072  7.827   -3.943  1.00 49.22  ? 313 ASN   A CG  1 
ATOM   2227 O  OD1 . ASN   A 1 308 ? -8.522  8.297   -4.996  1.00 42.13  ? 313 ASN   A OD1 1 
ATOM   2228 N  ND2 . ASN   A 1 308 ? -8.600  8.132   -2.766  1.00 43.30  ? 313 ASN   A ND2 1 
ATOM   2229 N  N   . LEU   A 1 309 ? -5.236  4.249   -4.655  1.00 28.40  ? 314 LEU   A N   1 
ATOM   2230 C  CA  . LEU   A 1 309 ? -4.024  3.413   -4.557  1.00 27.64  ? 314 LEU   A CA  1 
ATOM   2231 C  C   . LEU   A 1 309 ? -3.525  3.059   -5.955  1.00 29.66  ? 314 LEU   A C   1 
ATOM   2232 O  O   . LEU   A 1 309 ? -2.323  3.170   -6.220  1.00 28.20  ? 314 LEU   A O   1 
ATOM   2233 C  CB  . LEU   A 1 309 ? -4.347  2.158   -3.749  1.00 27.87  ? 314 LEU   A CB  1 
ATOM   2234 C  CG  . LEU   A 1 309 ? -3.232  1.165   -3.484  1.00 31.18  ? 314 LEU   A CG  1 
ATOM   2235 C  CD1 . LEU   A 1 309 ? -2.061  1.835   -2.743  1.00 32.42  ? 314 LEU   A CD1 1 
ATOM   2236 C  CD2 . LEU   A 1 309 ? -3.778  0.002   -2.704  1.00 31.53  ? 314 LEU   A CD2 1 
ATOM   2237 N  N   . ALA   A 1 310 ? -4.460  2.729   -6.875  1.00 27.06  ? 315 ALA   A N   1 
ATOM   2238 C  CA  . ALA   A 1 310 ? -4.119  2.432   -8.269  1.00 27.39  ? 315 ALA   A CA  1 
ATOM   2239 C  C   . ALA   A 1 310 ? -3.377  3.634   -8.897  1.00 30.17  ? 315 ALA   A C   1 
ATOM   2240 O  O   . ALA   A 1 310 ? -2.337  3.463   -9.542  1.00 27.24  ? 315 ALA   A O   1 
ATOM   2241 C  CB  . ALA   A 1 310 ? -5.392  2.108   -9.061  1.00 28.92  ? 315 ALA   A CB  1 
ATOM   2242 N  N   . VAL   A 1 311 ? -3.895  4.866   -8.670  1.00 27.10  ? 316 VAL   A N   1 
ATOM   2243 C  CA  . VAL   A 1 311 ? -3.270  6.077   -9.178  1.00 26.61  ? 316 VAL   A CA  1 
ATOM   2244 C  C   . VAL   A 1 311 ? -1.862  6.264   -8.578  1.00 27.32  ? 316 VAL   A C   1 
ATOM   2245 O  O   . VAL   A 1 311 ? -0.931  6.590   -9.304  1.00 27.56  ? 316 VAL   A O   1 
ATOM   2246 C  CB  . VAL   A 1 311 ? -4.168  7.311   -8.967  1.00 31.27  ? 316 VAL   A CB  1 
ATOM   2247 C  CG1 . VAL   A 1 311 ? -3.447  8.584   -9.387  1.00 30.58  ? 316 VAL   A CG1 1 
ATOM   2248 C  CG2 . VAL   A 1 311 ? -5.487  7.146   -9.724  1.00 31.28  ? 316 VAL   A CG2 1 
ATOM   2249 N  N   . ASP   A 1 312 ? -1.711  6.028   -7.266  1.00 25.82  ? 317 ASP   A N   1 
ATOM   2250 C  CA  . ASP   A 1 312 ? -0.419  6.141   -6.619  1.00 24.57  ? 317 ASP   A CA  1 
ATOM   2251 C  C   . ASP   A 1 312 ? 0.595   5.172   -7.255  1.00 26.52  ? 317 ASP   A C   1 
ATOM   2252 O  O   . ASP   A 1 312 ? 1.744   5.574   -7.447  1.00 25.04  ? 317 ASP   A O   1 
ATOM   2253 C  CB  . ASP   A 1 312 ? -0.558  5.851   -5.122  1.00 25.36  ? 317 ASP   A CB  1 
ATOM   2254 C  CG  . ASP   A 1 312 ? -1.033  7.022   -4.273  1.00 31.13  ? 317 ASP   A CG  1 
ATOM   2255 O  OD1 . ASP   A 1 312 ? -1.099  8.158   -4.798  1.00 31.75  ? 317 ASP   A OD1 1 
ATOM   2256 O  OD2 . ASP   A 1 312 ? -1.356  6.799   -3.108  1.00 32.29  ? 317 ASP   A OD2 1 
ATOM   2257 N  N   . VAL   A 1 313 ? 0.172   3.936   -7.618  1.00 24.95  ? 318 VAL   A N   1 
ATOM   2258 C  CA  . VAL   A 1 313 ? 1.107   2.968   -8.253  1.00 24.76  ? 318 VAL   A CA  1 
ATOM   2259 C  C   . VAL   A 1 313 ? 1.596   3.513   -9.598  1.00 27.38  ? 318 VAL   A C   1 
ATOM   2260 O  O   . VAL   A 1 313 ? 2.804   3.556   -9.880  1.00 26.19  ? 318 VAL   A O   1 
ATOM   2261 C  CB  . VAL   A 1 313 ? 0.456   1.573   -8.407  1.00 27.25  ? 318 VAL   A CB  1 
ATOM   2262 C  CG1 . VAL   A 1 313 ? 1.332   0.643   -9.271  1.00 27.92  ? 318 VAL   A CG1 1 
ATOM   2263 C  CG2 . VAL   A 1 313 ? 0.189   0.942   -7.039  1.00 26.65  ? 318 VAL   A CG2 1 
ATOM   2264 N  N   . ILE   A 1 314 ? 0.640   3.978   -10.417 1.00 25.10  ? 319 ILE   A N   1 
ATOM   2265 C  CA  . ILE   A 1 314 ? 0.945   4.492   -11.750 1.00 25.30  ? 319 ILE   A CA  1 
ATOM   2266 C  C   . ILE   A 1 314 ? 1.814   5.744   -11.668 1.00 27.44  ? 319 ILE   A C   1 
ATOM   2267 O  O   . ILE   A 1 314 ? 2.846   5.790   -12.315 1.00 27.23  ? 319 ILE   A O   1 
ATOM   2268 C  CB  . ILE   A 1 314 ? -0.323  4.669   -12.617 1.00 28.22  ? 319 ILE   A CB  1 
ATOM   2269 C  CG1 . ILE   A 1 314 ? -1.123  3.347   -12.670 1.00 28.46  ? 319 ILE   A CG1 1 
ATOM   2270 C  CG2 . ILE   A 1 314 ? 0.078   5.159   -14.033 1.00 29.26  ? 319 ILE   A CG2 1 
ATOM   2271 C  CD1 . ILE   A 1 314 ? -2.585  3.471   -13.130 1.00 31.55  ? 319 ILE   A CD1 1 
ATOM   2272 N  N   . ALA   A 1 315 ? 1.455   6.705   -10.796 1.00 26.76  ? 320 ALA   A N   1 
ATOM   2273 C  CA  . ALA   A 1 315 ? 2.220   7.935   -10.595 1.00 25.89  ? 320 ALA   A CA  1 
ATOM   2274 C  C   . ALA   A 1 315 ? 3.658   7.628   -10.122 1.00 27.76  ? 320 ALA   A C   1 
ATOM   2275 O  O   . ALA   A 1 315 ? 4.605   8.185   -10.674 1.00 26.15  ? 320 ALA   A O   1 
ATOM   2276 C  CB  . ALA   A 1 315 ? 1.514   8.817   -9.581  1.00 26.98  ? 320 ALA   A CB  1 
ATOM   2277 N  N   . SER   A 1 316 ? 3.823   6.685   -9.157  1.00 24.56  ? 321 SER   A N   1 
ATOM   2278 C  CA  . SER   A 1 316 ? 5.155   6.317   -8.668  1.00 24.07  ? 321 SER   A CA  1 
ATOM   2279 C  C   . SER   A 1 316 ? 5.975   5.633   -9.745  1.00 28.07  ? 321 SER   A C   1 
ATOM   2280 O  O   . SER   A 1 316 ? 7.181   5.839   -9.814  1.00 26.60  ? 321 SER   A O   1 
ATOM   2281 C  CB  . SER   A 1 316 ? 5.079   5.478   -7.393  1.00 26.33  ? 321 SER   A CB  1 
ATOM   2282 O  OG  . SER   A 1 316 ? 4.395   6.207   -6.386  1.00 31.11  ? 321 SER   A OG  1 
ATOM   2283 N  N   . SER   A 1 317 ? 5.315   4.882   -10.637 1.00 27.48  ? 322 SER   A N   1 
ATOM   2284 C  CA  . SER   A 1 317 ? 6.011   4.234   -11.746 1.00 27.37  ? 322 SER   A CA  1 
ATOM   2285 C  C   . SER   A 1 317 ? 6.552   5.254   -12.762 1.00 31.32  ? 322 SER   A C   1 
ATOM   2286 O  O   . SER   A 1 317 ? 7.455   4.918   -13.526 1.00 30.90  ? 322 SER   A O   1 
ATOM   2287 C  CB  . SER   A 1 317 ? 5.095   3.230   -12.432 1.00 28.75  ? 322 SER   A CB  1 
ATOM   2288 O  OG  . SER   A 1 317 ? 4.705   2.196   -11.544 1.00 28.60  ? 322 SER   A OG  1 
ATOM   2289 N  N   . PHE   A 1 318 ? 6.050   6.519   -12.727 1.00 29.37  ? 323 PHE   A N   1 
ATOM   2290 C  CA  . PHE   A 1 318 ? 6.504   7.568   -13.646 1.00 28.59  ? 323 PHE   A CA  1 
ATOM   2291 C  C   . PHE   A 1 318 ? 7.195   8.756   -12.932 1.00 34.12  ? 323 PHE   A C   1 
ATOM   2292 O  O   . PHE   A 1 318 ? 7.364   9.821   -13.533 1.00 33.54  ? 323 PHE   A O   1 
ATOM   2293 C  CB  . PHE   A 1 318 ? 5.352   8.012   -14.581 1.00 29.89  ? 323 PHE   A CB  1 
ATOM   2294 C  CG  . PHE   A 1 318 ? 5.002   6.913   -15.563 1.00 30.39  ? 323 PHE   A CG  1 
ATOM   2295 C  CD1 . PHE   A 1 318 ? 5.799   6.674   -16.681 1.00 34.71  ? 323 PHE   A CD1 1 
ATOM   2296 C  CD2 . PHE   A 1 318 ? 3.890   6.108   -15.362 1.00 31.97  ? 323 PHE   A CD2 1 
ATOM   2297 C  CE1 . PHE   A 1 318 ? 5.494   5.633   -17.569 1.00 34.32  ? 323 PHE   A CE1 1 
ATOM   2298 C  CE2 . PHE   A 1 318 ? 3.596   5.061   -16.238 1.00 34.92  ? 323 PHE   A CE2 1 
ATOM   2299 C  CZ  . PHE   A 1 318 ? 4.398   4.834   -17.340 1.00 33.11  ? 323 PHE   A CZ  1 
ATOM   2300 N  N   . GLY   A 1 319 ? 7.639   8.553   -11.682 1.00 29.64  ? 324 GLY   A N   1 
ATOM   2301 C  CA  . GLY   A 1 319 ? 8.416   9.578   -11.002 1.00 29.56  ? 324 GLY   A CA  1 
ATOM   2302 C  C   . GLY   A 1 319 ? 7.932   10.142  -9.686  1.00 30.80  ? 324 GLY   A C   1 
ATOM   2303 O  O   . GLY   A 1 319 ? 8.681   10.874  -9.045  1.00 31.90  ? 324 GLY   A O   1 
ATOM   2304 N  N   . GLN   A 1 320 ? 6.687   9.867   -9.291  1.00 26.60  ? 325 GLN   A N   1 
ATOM   2305 C  CA  . GLN   A 1 320 ? 6.207   10.350  -7.996  1.00 27.30  ? 325 GLN   A CA  1 
ATOM   2306 C  C   . GLN   A 1 320 ? 7.025   9.653   -6.908  1.00 30.47  ? 325 GLN   A C   1 
ATOM   2307 O  O   . GLN   A 1 320 ? 7.208   8.435   -6.967  1.00 27.76  ? 325 GLN   A O   1 
ATOM   2308 C  CB  . GLN   A 1 320 ? 4.707   10.086  -7.824  1.00 29.20  ? 325 GLN   A CB  1 
ATOM   2309 C  CG  . GLN   A 1 320 ? 4.168   10.456  -6.432  1.00 38.95  ? 325 GLN   A CG  1 
ATOM   2310 C  CD  . GLN   A 1 320 ? 2.691   10.178  -6.329  1.00 57.07  ? 325 GLN   A CD  1 
ATOM   2311 O  OE1 . GLN   A 1 320 ? 2.244   9.199   -5.696  1.00 51.80  ? 325 GLN   A OE1 1 
ATOM   2312 N  NE2 . GLN   A 1 320 ? 1.911   11.001  -7.011  1.00 39.96  ? 325 GLN   A NE2 1 
ATOM   2313 N  N   . THR   A 1 321 ? 7.572   10.440  -5.969  1.00 29.72  ? 326 THR   A N   1 
ATOM   2314 C  CA  . THR   A 1 321 ? 8.361   9.892   -4.875  1.00 30.64  ? 326 THR   A CA  1 
ATOM   2315 C  C   . THR   A 1 321 ? 7.843   10.365  -3.511  1.00 32.63  ? 326 THR   A C   1 
ATOM   2316 O  O   . THR   A 1 321 ? 6.973   11.237  -3.448  1.00 29.98  ? 326 THR   A O   1 
ATOM   2317 C  CB  . THR   A 1 321 ? 9.845   10.178  -5.100  1.00 44.26  ? 326 THR   A CB  1 
ATOM   2318 O  OG1 . THR   A 1 321 ? 10.604  9.232   -4.346  1.00 60.01  ? 326 THR   A OG1 1 
ATOM   2319 C  CG2 . THR   A 1 321 ? 10.231  11.598  -4.740  1.00 39.50  ? 326 THR   A CG2 1 
ATOM   2320 N  N   . ARG   A 1 322 ? 8.371   9.750   -2.442  1.00 29.93  ? 327 ARG   A N   1 
ATOM   2321 C  CA  . ARG   A 1 322 ? 8.076   10.060  -1.040  1.00 28.51  ? 327 ARG   A CA  1 
ATOM   2322 C  C   . ARG   A 1 322 ? 9.039   11.172  -0.563  1.00 34.21  ? 327 ARG   A C   1 
ATOM   2323 O  O   . ARG   A 1 322 ? 9.044   11.474  0.619   1.00 34.49  ? 327 ARG   A O   1 
ATOM   2324 C  CB  . ARG   A 1 322 ? 8.354   8.802   -0.178  1.00 28.27  ? 327 ARG   A CB  1 
ATOM   2325 C  CG  . ARG   A 1 322 ? 7.135   8.073   0.398   1.00 41.75  ? 327 ARG   A CG  1 
ATOM   2326 C  CD  . ARG   A 1 322 ? 6.646   6.872   -0.397  1.00 29.20  ? 327 ARG   A CD  1 
ATOM   2327 N  NE  . ARG   A 1 322 ? 7.703   5.901   -0.731  1.00 25.76  ? 327 ARG   A NE  1 
ATOM   2328 C  CZ  . ARG   A 1 322 ? 8.031   4.835   0.007   1.00 28.08  ? 327 ARG   A CZ  1 
ATOM   2329 N  NH1 . ARG   A 1 322 ? 7.439   4.618   1.185   1.00 22.45  ? 327 ARG   A NH1 1 
ATOM   2330 N  NH2 . ARG   A 1 322 ? 8.986   4.004   -0.405  1.00 22.80  ? 327 ARG   A NH2 1 
ATOM   2331 N  N   . GLU   A 1 323 ? 9.923   11.706  -1.431  1.00 33.51  ? 328 GLU   A N   1 
ATOM   2332 C  CA  . GLU   A 1 323 ? 10.922  12.695  -1.002  1.00 33.23  ? 328 GLU   A CA  1 
ATOM   2333 C  C   . GLU   A 1 323 ? 10.831  14.086  -1.695  1.00 38.65  ? 328 GLU   A C   1 
ATOM   2334 O  O   . GLU   A 1 323 ? 11.661  14.946  -1.415  1.00 37.86  ? 328 GLU   A O   1 
ATOM   2335 C  CB  . GLU   A 1 323 ? 12.349  12.115  -1.133  1.00 34.02  ? 328 GLU   A CB  1 
ATOM   2336 C  CG  . GLU   A 1 323 ? 12.572  10.846  -0.319  1.00 44.10  ? 328 GLU   A CG  1 
ATOM   2337 C  CD  . GLU   A 1 323 ? 13.957  10.226  -0.341  1.00 54.76  ? 328 GLU   A CD  1 
ATOM   2338 O  OE1 . GLU   A 1 323 ? 14.888  10.838  -0.914  1.00 52.55  ? 328 GLU   A OE1 1 
ATOM   2339 O  OE2 . GLU   A 1 323 ? 14.122  9.148   0.274   1.00 30.34  ? 328 GLU   A OE2 1 
ATOM   2340 N  N   . GLY   A 1 324 ? 9.828   14.297  -2.542  1.00 38.24  ? 329 GLY   A N   1 
ATOM   2341 C  CA  . GLY   A 1 324 ? 9.599   15.572  -3.223  1.00 39.81  ? 329 GLY   A CA  1 
ATOM   2342 C  C   . GLY   A 1 324 ? 10.599  15.980  -4.295  1.00 47.29  ? 329 GLY   A C   1 
ATOM   2343 O  O   . GLY   A 1 324 ? 10.728  17.175  -4.585  1.00 47.22  ? 329 GLY   A O   1 
ATOM   2344 N  N   . GLY   A 1 325 ? 11.271  14.999  -4.906  1.00 44.54  ? 330 GLY   A N   1 
ATOM   2345 C  CA  . GLY   A 1 325 ? 12.276  15.235  -5.944  1.00 45.14  ? 330 GLY   A CA  1 
ATOM   2346 C  C   . GLY   A 1 325 ? 11.786  15.259  -7.388  1.00 51.72  ? 330 GLY   A C   1 
ATOM   2347 O  O   . GLY   A 1 325 ? 12.605  15.433  -8.293  1.00 50.95  ? 330 GLY   A O   1 
ATOM   2348 N  N   . HIS   A 1 326 ? 10.461  15.100  -7.625  1.00 50.79  ? 331 HIS   A N   1 
ATOM   2349 C  CA  . HIS   A 1 326 ? 9.876   15.100  -8.983  1.00 52.53  ? 331 HIS   A CA  1 
ATOM   2350 C  C   . HIS   A 1 326 ? 9.875   16.490  -9.638  1.00 59.07  ? 331 HIS   A C   1 
ATOM   2351 O  O   . HIS   A 1 326 ? 10.293  16.614  -10.792 1.00 58.13  ? 331 HIS   A O   1 
ATOM   2352 C  CB  . HIS   A 1 326 ? 8.477   14.451  -9.049  1.00 53.90  ? 331 HIS   A CB  1 
ATOM   2353 C  CG  . HIS   A 1 326 ? 7.716   14.411  -7.757  1.00 58.06  ? 331 HIS   A CG  1 
ATOM   2354 N  ND1 . HIS   A 1 326 ? 8.101   13.577  -6.711  1.00 60.18  ? 331 HIS   A ND1 1 
ATOM   2355 C  CD2 . HIS   A 1 326 ? 6.579   15.057  -7.403  1.00 60.42  ? 331 HIS   A CD2 1 
ATOM   2356 C  CE1 . HIS   A 1 326 ? 7.208   13.766  -5.752  1.00 59.92  ? 331 HIS   A CE1 1 
ATOM   2357 N  NE2 . HIS   A 1 326 ? 6.271   14.648  -6.121  1.00 60.42  ? 331 HIS   A NE2 1 
ATOM   2358 N  N   . ILE   A 1 327 ? 9.409   17.525  -8.918  1.00 58.03  ? 332 ILE   A N   1 
ATOM   2359 C  CA  . ILE   A 1 327 ? 9.427   18.903  -9.420  1.00 58.97  ? 332 ILE   A CA  1 
ATOM   2360 C  C   . ILE   A 1 327 ? 10.767  19.488  -8.969  1.00 64.61  ? 332 ILE   A C   1 
ATOM   2361 O  O   . ILE   A 1 327 ? 11.033  19.577  -7.764  1.00 64.64  ? 332 ILE   A O   1 
ATOM   2362 C  CB  . ILE   A 1 327 ? 8.191   19.751  -8.973  1.00 62.44  ? 332 ILE   A CB  1 
ATOM   2363 C  CG1 . ILE   A 1 327 ? 6.873   19.201  -9.550  1.00 63.02  ? 332 ILE   A CG1 1 
ATOM   2364 C  CG2 . ILE   A 1 327 ? 8.350   21.234  -9.329  1.00 63.49  ? 332 ILE   A CG2 1 
ATOM   2365 C  CD1 . ILE   A 1 327 ? 5.914   18.697  -8.506  1.00 72.14  ? 332 ILE   A CD1 1 
ATOM   2366 N  N   . VAL   A 1 328 ? 11.627  19.822  -9.938  1.00 62.42  ? 333 VAL   A N   1 
ATOM   2367 C  CA  . VAL   A 1 328 ? 12.962  20.363  -9.690  1.00 62.68  ? 333 VAL   A CA  1 
ATOM   2368 C  C   . VAL   A 1 328 ? 12.894  21.882  -9.451  1.00 67.04  ? 333 VAL   A C   1 
ATOM   2369 O  O   . VAL   A 1 328 ? 12.347  22.629  -10.268 1.00 66.93  ? 333 VAL   A O   1 
ATOM   2370 C  CB  . VAL   A 1 328 ? 13.975  19.959  -10.806 1.00 67.07  ? 333 VAL   A CB  1 
ATOM   2371 C  CG1 . VAL   A 1 328 ? 15.360  20.562  -10.564 1.00 67.06  ? 333 VAL   A CG1 1 
ATOM   2372 C  CG2 . VAL   A 1 328 ? 14.073  18.438  -10.940 1.00 66.92  ? 333 VAL   A CG2 1 
ATOM   2373 N  N   . TYR   A 1 329 ? 13.430  22.309  -8.299  1.00 63.13  ? 334 TYR   A N   1 
ATOM   2374 C  CA  . TYR   A 1 329 ? 13.548  23.695  -7.845  1.00 62.37  ? 334 TYR   A CA  1 
ATOM   2375 C  C   . TYR   A 1 329 ? 15.017  24.055  -8.122  1.00 67.37  ? 334 TYR   A C   1 
ATOM   2376 O  O   . TYR   A 1 329 ? 15.903  23.248  -7.825  1.00 67.81  ? 334 TYR   A O   1 
ATOM   2377 C  CB  . TYR   A 1 329 ? 13.236  23.749  -6.336  1.00 62.39  ? 334 TYR   A CB  1 
ATOM   2378 C  CG  . TYR   A 1 329 ? 12.615  25.036  -5.843  1.00 61.99  ? 334 TYR   A CG  1 
ATOM   2379 C  CD1 . TYR   A 1 329 ? 11.263  25.301  -6.040  1.00 63.28  ? 334 TYR   A CD1 1 
ATOM   2380 C  CD2 . TYR   A 1 329 ? 13.354  25.946  -5.094  1.00 62.35  ? 334 TYR   A CD2 1 
ATOM   2381 C  CE1 . TYR   A 1 329 ? 10.676  26.470  -5.559  1.00 62.93  ? 334 TYR   A CE1 1 
ATOM   2382 C  CE2 . TYR   A 1 329 ? 12.776  27.113  -4.597  1.00 63.03  ? 334 TYR   A CE2 1 
ATOM   2383 C  CZ  . TYR   A 1 329 ? 11.437  27.374  -4.835  1.00 68.98  ? 334 TYR   A CZ  1 
ATOM   2384 O  OH  . TYR   A 1 329 ? 10.865  28.524  -4.345  1.00 69.56  ? 334 TYR   A OH  1 
ATOM   2385 N  N   . ASP   A 1 330 ? 15.280  25.210  -8.753  1.00 64.20  ? 335 ASP   A N   1 
ATOM   2386 C  CA  . ASP   A 1 330 ? 16.653  25.577  -9.124  1.00 63.80  ? 335 ASP   A CA  1 
ATOM   2387 C  C   . ASP   A 1 330 ? 17.286  26.666  -8.246  1.00 64.62  ? 335 ASP   A C   1 
ATOM   2388 O  O   . ASP   A 1 330 ? 18.510  26.659  -8.067  1.00 63.24  ? 335 ASP   A O   1 
ATOM   2389 C  CB  . ASP   A 1 330 ? 16.730  25.960  -10.615 1.00 66.65  ? 335 ASP   A CB  1 
ATOM   2390 C  CG  . ASP   A 1 330 ? 16.488  24.816  -11.599 1.00 83.78  ? 335 ASP   A CG  1 
ATOM   2391 O  OD1 . ASP   A 1 330 ? 16.953  23.679  -11.325 1.00 84.99  ? 335 ASP   A OD1 1 
ATOM   2392 O  OD2 . ASP   A 1 330 ? 15.883  25.068  -12.667 1.00 91.76  ? 335 ASP   A OD2 1 
ATOM   2393 N  N   . GLN   A 1 331 ? 16.463  27.594  -7.709  1.00 59.35  ? 336 GLN   A N   1 
ATOM   2394 C  CA  . GLN   A 1 331 ? 16.911  28.704  -6.859  1.00 58.11  ? 336 GLN   A CA  1 
ATOM   2395 C  C   . GLN   A 1 331 ? 15.847  29.067  -5.843  1.00 58.64  ? 336 GLN   A C   1 
ATOM   2396 O  O   . GLN   A 1 331 ? 14.682  29.220  -6.216  1.00 58.69  ? 336 GLN   A O   1 
ATOM   2397 C  CB  . GLN   A 1 331 ? 17.182  29.964  -7.712  1.00 59.54  ? 336 GLN   A CB  1 
ATOM   2398 C  CG  . GLN   A 1 331 ? 18.474  29.953  -8.524  1.00 81.30  ? 336 GLN   A CG  1 
ATOM   2399 C  CD  . GLN   A 1 331 ? 18.424  30.895  -9.707  1.00 99.96  ? 336 GLN   A CD  1 
ATOM   2400 O  OE1 . GLN   A 1 331 ? 17.748  31.933  -9.697  1.00 94.26  ? 336 GLN   A OE1 1 
ATOM   2401 N  NE2 . GLN   A 1 331 ? 19.178  30.570  -10.745 1.00 93.17  ? 336 GLN   A NE2 1 
ATOM   2402 N  N   . LEU   A 1 332 ? 16.241  29.280  -4.575  1.00 52.84  ? 337 LEU   A N   1 
ATOM   2403 C  CA  . LEU   A 1 332 ? 15.279  29.743  -3.570  1.00 51.66  ? 337 LEU   A CA  1 
ATOM   2404 C  C   . LEU   A 1 332 ? 15.178  31.262  -3.719  1.00 54.14  ? 337 LEU   A C   1 
ATOM   2405 O  O   . LEU   A 1 332 ? 16.217  31.914  -3.927  1.00 53.47  ? 337 LEU   A O   1 
ATOM   2406 C  CB  . LEU   A 1 332 ? 15.735  29.465  -2.118  1.00 51.34  ? 337 LEU   A CB  1 
ATOM   2407 C  CG  . LEU   A 1 332 ? 16.027  28.045  -1.677  1.00 54.95  ? 337 LEU   A CG  1 
ATOM   2408 C  CD1 . LEU   A 1 332 ? 16.870  28.042  -0.400  1.00 54.23  ? 337 LEU   A CD1 1 
ATOM   2409 C  CD2 . LEU   A 1 332 ? 14.756  27.243  -1.487  1.00 58.43  ? 337 LEU   A CD2 1 
ATOM   2410 N  N   . PRO   A 1 333 ? 13.979  31.863  -3.537  1.00 49.64  ? 338 PRO   A N   1 
ATOM   2411 C  CA  . PRO   A 1 333 ? 13.903  33.335  -3.558  1.00 49.03  ? 338 PRO   A CA  1 
ATOM   2412 C  C   . PRO   A 1 333 ? 14.679  33.933  -2.378  1.00 52.22  ? 338 PRO   A C   1 
ATOM   2413 O  O   . PRO   A 1 333 ? 14.790  33.303  -1.319  1.00 50.75  ? 338 PRO   A O   1 
ATOM   2414 C  CB  . PRO   A 1 333 ? 12.405  33.641  -3.481  1.00 50.62  ? 338 PRO   A CB  1 
ATOM   2415 C  CG  . PRO   A 1 333 ? 11.743  32.386  -3.101  1.00 55.33  ? 338 PRO   A CG  1 
ATOM   2416 C  CD  . PRO   A 1 333 ? 12.667  31.240  -3.259  1.00 51.02  ? 338 PRO   A CD  1 
ATOM   2417 N  N   . THR   A 1 334 ? 15.268  35.115  -2.589  1.00 49.14  ? 339 THR   A N   1 
ATOM   2418 C  CA  . THR   A 1 334 ? 16.086  35.813  -1.592  1.00 49.51  ? 339 THR   A CA  1 
ATOM   2419 C  C   . THR   A 1 334 ? 15.403  37.080  -1.065  1.00 51.91  ? 339 THR   A C   1 
ATOM   2420 O  O   . THR   A 1 334 ? 14.750  37.780  -1.847  1.00 51.40  ? 339 THR   A O   1 
ATOM   2421 C  CB  . THR   A 1 334 ? 17.473  36.159  -2.161  1.00 63.21  ? 339 THR   A CB  1 
ATOM   2422 O  OG1 . THR   A 1 334 ? 17.313  36.930  -3.353  1.00 66.64  ? 339 THR   A OG1 1 
ATOM   2423 C  CG2 . THR   A 1 334 ? 18.320  34.929  -2.435  1.00 63.51  ? 339 THR   A CG2 1 
ATOM   2424 N  N   . PRO   A 1 335 ? 15.556  37.396  0.248   1.00 47.81  ? 340 PRO   A N   1 
ATOM   2425 C  CA  . PRO   A 1 335 ? 14.927  38.615  0.796   1.00 52.28  ? 340 PRO   A CA  1 
ATOM   2426 C  C   . PRO   A 1 335 ? 15.455  39.915  0.179   1.00 95.80  ? 340 PRO   A C   1 
ATOM   2427 O  O   . PRO   A 1 335 ? 16.607  39.986  -0.253  1.00 62.03  ? 340 PRO   A O   1 
ATOM   2428 C  CB  . PRO   A 1 335 ? 15.260  38.551  2.294   1.00 53.21  ? 340 PRO   A CB  1 
ATOM   2429 C  CG  . PRO   A 1 335 ? 15.638  37.129  2.559   1.00 55.60  ? 340 PRO   A CG  1 
ATOM   2430 C  CD  . PRO   A 1 335 ? 16.278  36.649  1.301   1.00 50.18  ? 340 PRO   A CD  1 
ATOM   2431 N  N   . ASN   B 1 12  ? 4.598   0.845   43.591  1.00 41.31  ? 17  ASN   B N   1 
ATOM   2432 C  CA  . ASN   B 1 12  ? 5.942   0.525   43.114  1.00 40.16  ? 17  ASN   B CA  1 
ATOM   2433 C  C   . ASN   B 1 12  ? 6.948   1.515   43.658  1.00 41.19  ? 17  ASN   B C   1 
ATOM   2434 O  O   . ASN   B 1 12  ? 6.779   2.737   43.531  1.00 41.49  ? 17  ASN   B O   1 
ATOM   2435 C  CB  . ASN   B 1 12  ? 5.988   0.487   41.599  1.00 39.94  ? 17  ASN   B CB  1 
ATOM   2436 C  CG  . ASN   B 1 12  ? 5.148   -0.625  41.020  1.00 54.66  ? 17  ASN   B CG  1 
ATOM   2437 O  OD1 . ASN   B 1 12  ? 5.106   -1.749  41.541  1.00 50.31  ? 17  ASN   B OD1 1 
ATOM   2438 N  ND2 . ASN   B 1 12  ? 4.507   -0.349  39.899  1.00 40.63  ? 17  ASN   B ND2 1 
ATOM   2439 N  N   . LEU   B 1 13  ? 7.993   0.986   44.276  1.00 36.01  ? 18  LEU   B N   1 
ATOM   2440 C  CA  . LEU   B 1 13  ? 8.994   1.825   44.934  1.00 34.74  ? 18  LEU   B CA  1 
ATOM   2441 C  C   . LEU   B 1 13  ? 10.322  1.881   44.219  1.00 34.61  ? 18  LEU   B C   1 
ATOM   2442 O  O   . LEU   B 1 13  ? 11.135  2.745   44.536  1.00 31.10  ? 18  LEU   B O   1 
ATOM   2443 C  CB  . LEU   B 1 13  ? 9.206   1.327   46.381  1.00 35.63  ? 18  LEU   B CB  1 
ATOM   2444 C  CG  . LEU   B 1 13  ? 7.964   1.044   47.251  1.00 41.54  ? 18  LEU   B CG  1 
ATOM   2445 C  CD1 . LEU   B 1 13  ? 8.380   0.542   48.609  1.00 43.07  ? 18  LEU   B CD1 1 
ATOM   2446 C  CD2 . LEU   B 1 13  ? 7.067   2.262   47.384  1.00 45.39  ? 18  LEU   B CD2 1 
ATOM   2447 N  N   . TYR   B 1 14  ? 10.562  0.952   43.263  1.00 31.37  ? 19  TYR   B N   1 
ATOM   2448 C  CA  . TYR   B 1 14  ? 11.830  0.811   42.559  1.00 31.54  ? 19  TYR   B CA  1 
ATOM   2449 C  C   . TYR   B 1 14  ? 11.626  0.909   41.069  1.00 34.59  ? 19  TYR   B C   1 
ATOM   2450 O  O   . TYR   B 1 14  ? 10.688  0.308   40.532  1.00 34.83  ? 19  TYR   B O   1 
ATOM   2451 C  CB  . TYR   B 1 14  ? 12.469  -0.545  42.878  1.00 34.38  ? 19  TYR   B CB  1 
ATOM   2452 C  CG  . TYR   B 1 14  ? 12.707  -0.744  44.351  1.00 35.59  ? 19  TYR   B CG  1 
ATOM   2453 C  CD1 . TYR   B 1 14  ? 11.714  -1.271  45.171  1.00 38.11  ? 19  TYR   B CD1 1 
ATOM   2454 C  CD2 . TYR   B 1 14  ? 13.902  -0.357  44.938  1.00 37.32  ? 19  TYR   B CD2 1 
ATOM   2455 C  CE1 . TYR   B 1 14  ? 11.902  -1.395  46.546  1.00 39.40  ? 19  TYR   B CE1 1 
ATOM   2456 C  CE2 . TYR   B 1 14  ? 14.105  -0.481  46.310  1.00 37.55  ? 19  TYR   B CE2 1 
ATOM   2457 C  CZ  . TYR   B 1 14  ? 13.103  -1.004  47.108  1.00 44.47  ? 19  TYR   B CZ  1 
ATOM   2458 O  OH  . TYR   B 1 14  ? 13.311  -1.162  48.448  1.00 47.56  ? 19  TYR   B OH  1 
ATOM   2459 N  N   . PHE   B 1 15  ? 12.522  1.646   40.409  1.00 29.55  ? 20  PHE   B N   1 
ATOM   2460 C  CA  . PHE   B 1 15  ? 12.467  1.924   38.962  1.00 27.59  ? 20  PHE   B CA  1 
ATOM   2461 C  C   . PHE   B 1 15  ? 13.857  1.826   38.362  1.00 33.49  ? 20  PHE   B C   1 
ATOM   2462 O  O   . PHE   B 1 15  ? 14.829  2.106   39.046  1.00 33.74  ? 20  PHE   B O   1 
ATOM   2463 C  CB  . PHE   B 1 15  ? 11.868  3.346   38.741  1.00 28.90  ? 20  PHE   B CB  1 
ATOM   2464 C  CG  . PHE   B 1 15  ? 10.513  3.529   39.378  1.00 29.61  ? 20  PHE   B CG  1 
ATOM   2465 C  CD1 . PHE   B 1 15  ? 10.399  3.940   40.704  1.00 30.82  ? 20  PHE   B CD1 1 
ATOM   2466 C  CD2 . PHE   B 1 15  ? 9.347   3.243   38.673  1.00 29.96  ? 20  PHE   B CD2 1 
ATOM   2467 C  CE1 . PHE   B 1 15  ? 9.152   4.060   41.310  1.00 31.39  ? 20  PHE   B CE1 1 
ATOM   2468 C  CE2 . PHE   B 1 15  ? 8.096   3.370   39.279  1.00 31.85  ? 20  PHE   B CE2 1 
ATOM   2469 C  CZ  . PHE   B 1 15  ? 8.003   3.814   40.587  1.00 31.03  ? 20  PHE   B CZ  1 
ATOM   2470 N  N   . GLN   B 1 16  ? 13.978  1.425   37.074  1.00 32.48  ? 21  GLN   B N   1 
ATOM   2471 C  CA  . GLN   B 1 16  ? 15.296  1.313   36.445  1.00 32.98  ? 21  GLN   B CA  1 
ATOM   2472 C  C   . GLN   B 1 16  ? 16.050  2.633   36.392  1.00 35.53  ? 21  GLN   B C   1 
ATOM   2473 O  O   . GLN   B 1 16  ? 17.269  2.643   36.508  1.00 34.88  ? 21  GLN   B O   1 
ATOM   2474 C  CB  . GLN   B 1 16  ? 15.215  0.663   35.049  1.00 35.38  ? 21  GLN   B CB  1 
ATOM   2475 C  CG  . GLN   B 1 16  ? 15.683  -0.801  35.022  1.00 60.40  ? 21  GLN   B CG  1 
ATOM   2476 C  CD  . GLN   B 1 16  ? 17.091  -1.041  35.534  1.00 88.90  ? 21  GLN   B CD  1 
ATOM   2477 O  OE1 . GLN   B 1 16  ? 18.060  -0.377  35.136  1.00 89.70  ? 21  GLN   B OE1 1 
ATOM   2478 N  NE2 . GLN   B 1 16  ? 17.234  -2.023  36.412  1.00 80.30  ? 21  GLN   B NE2 1 
ATOM   2479 N  N   . SER   B 1 17  ? 15.316  3.740   36.218  1.00 33.83  ? 22  SER   B N   1 
ATOM   2480 C  CA  . SER   B 1 17  ? 15.858  5.094   36.195  1.00 33.28  ? 22  SER   B CA  1 
ATOM   2481 C  C   . SER   B 1 17  ? 14.794  6.070   36.689  1.00 34.31  ? 22  SER   B C   1 
ATOM   2482 O  O   . SER   B 1 17  ? 13.597  5.771   36.655  1.00 32.66  ? 22  SER   B O   1 
ATOM   2483 C  CB  . SER   B 1 17  ? 16.370  5.479   34.802  1.00 37.77  ? 22  SER   B CB  1 
ATOM   2484 O  OG  . SER   B 1 17  ? 15.347  5.403   33.825  1.00 45.31  ? 22  SER   B OG  1 
ATOM   2485 N  N   . VAL   B 1 18  ? 15.247  7.217   37.208  1.00 31.28  ? 23  VAL   B N   1 
ATOM   2486 C  CA  . VAL   B 1 18  ? 14.376  8.241   37.743  1.00 31.00  ? 23  VAL   B CA  1 
ATOM   2487 C  C   . VAL   B 1 18  ? 14.649  9.513   36.968  1.00 34.77  ? 23  VAL   B C   1 
ATOM   2488 O  O   . VAL   B 1 18  ? 15.748  10.075  37.048  1.00 36.08  ? 23  VAL   B O   1 
ATOM   2489 C  CB  . VAL   B 1 18  ? 14.556  8.402   39.276  1.00 34.46  ? 23  VAL   B CB  1 
ATOM   2490 C  CG1 . VAL   B 1 18  ? 13.762  9.589   39.810  1.00 34.08  ? 23  VAL   B CG1 1 
ATOM   2491 C  CG2 . VAL   B 1 18  ? 14.150  7.117   39.995  1.00 34.71  ? 23  VAL   B CG2 1 
ATOM   2492 N  N   . HIS   B 1 19  ? 13.668  9.938   36.181  1.00 30.45  ? 24  HIS   B N   1 
ATOM   2493 C  CA  . HIS   B 1 19  ? 13.840  11.155  35.392  1.00 30.20  ? 24  HIS   B CA  1 
ATOM   2494 C  C   . HIS   B 1 19  ? 13.115  12.315  36.043  1.00 32.02  ? 24  HIS   B C   1 
ATOM   2495 O  O   . HIS   B 1 19  ? 12.069  12.113  36.652  1.00 33.22  ? 24  HIS   B O   1 
ATOM   2496 C  CB  . HIS   B 1 19  ? 13.258  10.955  33.968  1.00 31.69  ? 24  HIS   B CB  1 
ATOM   2497 C  CG  . HIS   B 1 19  ? 13.855  9.800   33.236  1.00 36.19  ? 24  HIS   B CG  1 
ATOM   2498 N  ND1 . HIS   B 1 19  ? 15.151  9.844   32.753  1.00 38.79  ? 24  HIS   B ND1 1 
ATOM   2499 C  CD2 . HIS   B 1 19  ? 13.336  8.579   32.981  1.00 38.90  ? 24  HIS   B CD2 1 
ATOM   2500 C  CE1 . HIS   B 1 19  ? 15.361  8.666   32.192  1.00 38.66  ? 24  HIS   B CE1 1 
ATOM   2501 N  NE2 . HIS   B 1 19  ? 14.299  7.873   32.314  1.00 39.07  ? 24  HIS   B NE2 1 
ATOM   2502 N  N   . SER   B 1 20  ? 13.626  13.536  35.849  1.00 26.69  ? 25  SER   B N   1 
ATOM   2503 C  CA  . SER   B 1 20  ? 12.967  14.769  36.298  1.00 26.64  ? 25  SER   B CA  1 
ATOM   2504 C  C   . SER   B 1 20  ? 12.349  15.380  35.021  1.00 29.18  ? 25  SER   B C   1 
ATOM   2505 O  O   . SER   B 1 20  ? 13.063  15.734  34.083  1.00 29.11  ? 25  SER   B O   1 
ATOM   2506 C  CB  . SER   B 1 20  ? 13.960  15.725  36.951  1.00 31.68  ? 25  SER   B CB  1 
ATOM   2507 O  OG  . SER   B 1 20  ? 14.370  15.180  38.198  1.00 36.35  ? 25  SER   B OG  1 
ATOM   2508 N  N   . VAL   B 1 21  ? 11.018  15.416  34.977  1.00 24.90  ? 26  VAL   B N   1 
ATOM   2509 C  CA  . VAL   B 1 21  ? 10.280  15.825  33.784  1.00 25.35  ? 26  VAL   B CA  1 
ATOM   2510 C  C   . VAL   B 1 21  ? 9.403   17.040  34.057  1.00 30.26  ? 26  VAL   B C   1 
ATOM   2511 O  O   . VAL   B 1 21  ? 8.592   17.021  34.989  1.00 30.72  ? 26  VAL   B O   1 
ATOM   2512 C  CB  . VAL   B 1 21  ? 9.450   14.626  33.224  1.00 28.28  ? 26  VAL   B CB  1 
ATOM   2513 C  CG1 . VAL   B 1 21  ? 8.645   15.010  31.972  1.00 26.99  ? 26  VAL   B CG1 1 
ATOM   2514 C  CG2 . VAL   B 1 21  ? 10.320  13.401  32.957  1.00 28.12  ? 26  VAL   B CG2 1 
ATOM   2515 N  N   . ALA   B 1 22  ? 9.534   18.082  33.215  1.00 26.82  ? 27  ALA   B N   1 
ATOM   2516 C  CA  . ALA   B 1 22  ? 8.665   19.282  33.259  1.00 26.86  ? 27  ALA   B CA  1 
ATOM   2517 C  C   . ALA   B 1 22  ? 7.663   19.134  32.111  1.00 30.99  ? 27  ALA   B C   1 
ATOM   2518 O  O   . ALA   B 1 22  ? 8.043   18.687  31.028  1.00 29.14  ? 27  ALA   B O   1 
ATOM   2519 C  CB  . ALA   B 1 22  ? 9.471   20.555  33.055  1.00 27.85  ? 27  ALA   B CB  1 
ATOM   2520 N  N   . VAL   B 1 23  ? 6.392   19.469  32.355  1.00 27.26  ? 28  VAL   B N   1 
ATOM   2521 C  CA  . VAL   B 1 23  ? 5.340   19.389  31.336  1.00 27.58  ? 28  VAL   B CA  1 
ATOM   2522 C  C   . VAL   B 1 23  ? 4.763   20.779  31.113  1.00 32.59  ? 28  VAL   B C   1 
ATOM   2523 O  O   . VAL   B 1 23  ? 4.378   21.458  32.073  1.00 31.22  ? 28  VAL   B O   1 
ATOM   2524 C  CB  . VAL   B 1 23  ? 4.258   18.329  31.672  1.00 31.00  ? 28  VAL   B CB  1 
ATOM   2525 C  CG1 . VAL   B 1 23  ? 3.106   18.338  30.661  1.00 31.22  ? 28  VAL   B CG1 1 
ATOM   2526 C  CG2 . VAL   B 1 23  ? 4.874   16.929  31.785  1.00 30.26  ? 28  VAL   B CG2 1 
ATOM   2527 N  N   . ILE   B 1 24  ? 4.736   21.208  29.843  1.00 29.69  ? 29  ILE   B N   1 
ATOM   2528 C  CA  . ILE   B 1 24  ? 4.191   22.502  29.432  1.00 29.76  ? 29  ILE   B CA  1 
ATOM   2529 C  C   . ILE   B 1 24  ? 3.138   22.243  28.371  1.00 32.62  ? 29  ILE   B C   1 
ATOM   2530 O  O   . ILE   B 1 24  ? 3.438   21.610  27.360  1.00 31.95  ? 29  ILE   B O   1 
ATOM   2531 C  CB  . ILE   B 1 24  ? 5.285   23.452  28.863  1.00 33.16  ? 29  ILE   B CB  1 
ATOM   2532 C  CG1 . ILE   B 1 24  ? 6.460   23.677  29.829  1.00 33.95  ? 29  ILE   B CG1 1 
ATOM   2533 C  CG2 . ILE   B 1 24  ? 4.678   24.801  28.396  1.00 34.40  ? 29  ILE   B CG2 1 
ATOM   2534 C  CD1 . ILE   B 1 24  ? 7.657   24.191  29.111  1.00 41.13  ? 29  ILE   B CD1 1 
ATOM   2535 N  N   . GLY   B 1 25  ? 1.928   22.751  28.588  1.00 30.70  ? 30  GLY   B N   1 
ATOM   2536 C  CA  . GLY   B 1 25  ? 0.883   22.718  27.577  1.00 30.73  ? 30  GLY   B CA  1 
ATOM   2537 C  C   . GLY   B 1 25  ? 1.018   23.979  26.742  1.00 34.97  ? 30  GLY   B C   1 
ATOM   2538 O  O   . GLY   B 1 25  ? 1.049   25.095  27.289  1.00 33.69  ? 30  GLY   B O   1 
ATOM   2539 N  N   . ALA   B 1 26  ? 1.098   23.828  25.403  1.00 30.70  ? 31  ALA   B N   1 
ATOM   2540 C  CA  . ALA   B 1 26  ? 1.233   24.971  24.511  1.00 30.16  ? 31  ALA   B CA  1 
ATOM   2541 C  C   . ALA   B 1 26  ? 0.143   24.884  23.432  1.00 35.48  ? 31  ALA   B C   1 
ATOM   2542 O  O   . ALA   B 1 26  ? 0.379   24.370  22.334  1.00 32.85  ? 31  ALA   B O   1 
ATOM   2543 C  CB  . ALA   B 1 26  ? 2.639   25.024  23.910  1.00 30.73  ? 31  ALA   B CB  1 
ATOM   2544 N  N   . PRO   B 1 27  ? -1.088  25.340  23.759  1.00 36.53  ? 32  PRO   B N   1 
ATOM   2545 C  CA  . PRO   B 1 27  ? -2.197  25.227  22.790  1.00 37.30  ? 32  PRO   B CA  1 
ATOM   2546 C  C   . PRO   B 1 27  ? -2.136  26.216  21.607  1.00 43.83  ? 32  PRO   B C   1 
ATOM   2547 O  O   . PRO   B 1 27  ? -3.102  26.927  21.347  1.00 46.54  ? 32  PRO   B O   1 
ATOM   2548 C  CB  . PRO   B 1 27  ? -3.439  25.395  23.665  1.00 39.27  ? 32  PRO   B CB  1 
ATOM   2549 C  CG  . PRO   B 1 27  ? -2.998  26.202  24.823  1.00 43.91  ? 32  PRO   B CG  1 
ATOM   2550 C  CD  . PRO   B 1 27  ? -1.542  25.919  25.044  1.00 39.22  ? 32  PRO   B CD  1 
ATOM   2551 N  N   . PHE   B 1 28  ? -1.002  26.241  20.881  1.00 40.70  ? 33  PHE   B N   1 
ATOM   2552 C  CA  . PHE   B 1 28  ? -0.727  27.091  19.712  1.00 40.60  ? 33  PHE   B CA  1 
ATOM   2553 C  C   . PHE   B 1 28  ? -1.601  26.613  18.552  1.00 39.80  ? 33  PHE   B C   1 
ATOM   2554 O  O   . PHE   B 1 28  ? -1.580  25.424  18.249  1.00 36.42  ? 33  PHE   B O   1 
ATOM   2555 C  CB  . PHE   B 1 28  ? 0.729   26.854  19.247  1.00 43.88  ? 33  PHE   B CB  1 
ATOM   2556 C  CG  . PHE   B 1 28  ? 1.862   27.745  19.690  1.00 46.44  ? 33  PHE   B CG  1 
ATOM   2557 C  CD1 . PHE   B 1 28  ? 2.299   27.737  21.010  1.00 50.21  ? 33  PHE   B CD1 1 
ATOM   2558 C  CD2 . PHE   B 1 28  ? 2.611   28.453  18.757  1.00 49.40  ? 33  PHE   B CD2 1 
ATOM   2559 C  CE1 . PHE   B 1 28  ? 3.404   28.497  21.405  1.00 50.77  ? 33  PHE   B CE1 1 
ATOM   2560 C  CE2 . PHE   B 1 28  ? 3.701   29.229  19.157  1.00 52.21  ? 33  PHE   B CE2 1 
ATOM   2561 C  CZ  . PHE   B 1 28  ? 4.103   29.226  20.476  1.00 50.12  ? 33  PHE   B CZ  1 
ATOM   2562 N  N   . SER   B 1 29  ? -2.342  27.513  17.880  1.00 35.10  ? 34  SER   B N   1 
ATOM   2563 C  CA  . SER   B 1 29  ? -3.114  27.107  16.701  1.00 34.63  ? 34  SER   B CA  1 
ATOM   2564 C  C   . SER   B 1 29  ? -2.849  28.052  15.523  1.00 38.55  ? 34  SER   B C   1 
ATOM   2565 O  O   . SER   B 1 29  ? -3.138  27.702  14.375  1.00 37.43  ? 34  SER   B O   1 
ATOM   2566 C  CB  . SER   B 1 29  ? -4.611  27.025  17.004  1.00 39.79  ? 34  SER   B CB  1 
ATOM   2567 O  OG  . SER   B 1 29  ? -5.198  28.312  17.128  1.00 50.88  ? 34  SER   B OG  1 
ATOM   2568 N  N   . GLN   B 1 30  ? -2.262  29.226  15.808  1.00 35.71  ? 35  GLN   B N   1 
ATOM   2569 C  CA  . GLN   B 1 30  ? -2.037  30.287  14.827  1.00 36.55  ? 35  GLN   B CA  1 
ATOM   2570 C  C   . GLN   B 1 30  ? -0.888  30.025  13.844  1.00 39.68  ? 35  GLN   B C   1 
ATOM   2571 O  O   . GLN   B 1 30  ? -0.646  30.847  12.954  1.00 39.25  ? 35  GLN   B O   1 
ATOM   2572 C  CB  . GLN   B 1 30  ? -1.891  31.650  15.519  1.00 38.27  ? 35  GLN   B CB  1 
ATOM   2573 C  CG  . GLN   B 1 30  ? -3.243  32.194  15.964  1.00 57.85  ? 35  GLN   B CG  1 
ATOM   2574 C  CD  . GLN   B 1 30  ? -3.140  33.564  16.577  1.00 80.84  ? 35  GLN   B CD  1 
ATOM   2575 O  OE1 . GLN   B 1 30  ? -2.759  33.721  17.744  1.00 80.97  ? 35  GLN   B OE1 1 
ATOM   2576 N  NE2 . GLN   B 1 30  ? -3.525  34.580  15.820  1.00 66.61  ? 35  GLN   B NE2 1 
ATOM   2577 N  N   . GLY   B 1 31  ? -0.224  28.871  13.976  1.00 36.71  ? 36  GLY   B N   1 
ATOM   2578 C  CA  . GLY   B 1 31  ? 0.801   28.455  13.028  1.00 35.63  ? 36  GLY   B CA  1 
ATOM   2579 C  C   . GLY   B 1 31  ? 0.155   27.766  11.836  1.00 36.82  ? 36  GLY   B C   1 
ATOM   2580 O  O   . GLY   B 1 31  ? 0.850   27.387  10.894  1.00 34.01  ? 36  GLY   B O   1 
ATOM   2581 N  N   . GLN   B 1 32  ? -1.194  27.588  11.874  1.00 34.85  ? 37  GLN   B N   1 
ATOM   2582 C  CA  . GLN   B 1 32  ? -1.982  26.948  10.809  1.00 35.17  ? 37  GLN   B CA  1 
ATOM   2583 C  C   . GLN   B 1 32  ? -3.467  27.399  10.817  1.00 41.85  ? 37  GLN   B C   1 
ATOM   2584 O  O   . GLN   B 1 32  ? -3.844  28.242  11.634  1.00 41.25  ? 37  GLN   B O   1 
ATOM   2585 C  CB  . GLN   B 1 32  ? -1.836  25.408  10.828  1.00 35.90  ? 37  GLN   B CB  1 
ATOM   2586 C  CG  . GLN   B 1 32  ? -2.100  24.767  12.186  1.00 30.52  ? 37  GLN   B CG  1 
ATOM   2587 C  CD  . GLN   B 1 32  ? -3.550  24.461  12.384  1.00 46.33  ? 37  GLN   B CD  1 
ATOM   2588 O  OE1 . GLN   B 1 32  ? -4.114  23.571  11.738  1.00 40.70  ? 37  GLN   B OE1 1 
ATOM   2589 N  NE2 . GLN   B 1 32  ? -4.193  25.221  13.261  1.00 40.92  ? 37  GLN   B NE2 1 
ATOM   2590 N  N   . LYS   B 1 33  ? -4.298  26.833  9.909   1.00 39.74  ? 38  LYS   B N   1 
ATOM   2591 C  CA  . LYS   B 1 33  ? -5.690  27.268  9.707   1.00 39.31  ? 38  LYS   B CA  1 
ATOM   2592 C  C   . LYS   B 1 33  ? -6.787  26.337  10.233  1.00 45.66  ? 38  LYS   B C   1 
ATOM   2593 O  O   . LYS   B 1 33  ? -7.917  26.798  10.406  1.00 46.31  ? 38  LYS   B O   1 
ATOM   2594 C  CB  . LYS   B 1 33  ? -5.922  27.552  8.209   1.00 39.83  ? 38  LYS   B CB  1 
ATOM   2595 C  CG  . LYS   B 1 33  ? -5.200  28.807  7.737   1.00 40.53  ? 38  LYS   B CG  1 
ATOM   2596 C  CD  . LYS   B 1 33  ? -5.347  29.061  6.246   1.00 51.40  ? 38  LYS   B CD  1 
ATOM   2597 C  CE  . LYS   B 1 33  ? -4.611  30.315  5.830   1.00 57.80  ? 38  LYS   B CE  1 
ATOM   2598 N  NZ  . LYS   B 1 33  ? -3.204  30.034  5.421   1.00 60.66  ? 38  LYS   B NZ  1 
ATOM   2599 N  N   . ARG   B 1 34  ? -6.486  25.054  10.476  1.00 43.24  ? 39  ARG   B N   1 
ATOM   2600 C  CA  . ARG   B 1 34  ? -7.492  24.097  10.951  1.00 43.41  ? 39  ARG   B CA  1 
ATOM   2601 C  C   . ARG   B 1 34  ? -7.756  24.289  12.444  1.00 48.96  ? 39  ARG   B C   1 
ATOM   2602 O  O   . ARG   B 1 34  ? -6.824  24.268  13.261  1.00 49.85  ? 39  ARG   B O   1 
ATOM   2603 C  CB  . ARG   B 1 34  ? -7.082  22.647  10.638  1.00 43.09  ? 39  ARG   B CB  1 
ATOM   2604 C  CG  . ARG   B 1 34  ? -6.832  22.380  9.153   1.00 52.38  ? 39  ARG   B CG  1 
ATOM   2605 C  CD  . ARG   B 1 34  ? -7.842  21.423  8.576   1.00 61.24  ? 39  ARG   B CD  1 
ATOM   2606 N  NE  . ARG   B 1 34  ? -7.226  20.157  8.188   1.00 67.11  ? 39  ARG   B NE  1 
ATOM   2607 C  CZ  . ARG   B 1 34  ? -7.909  19.068  7.850   1.00 84.52  ? 39  ARG   B CZ  1 
ATOM   2608 N  NH1 . ARG   B 1 34  ? -9.237  19.081  7.852   1.00 68.33  ? 39  ARG   B NH1 1 
ATOM   2609 N  NH2 . ARG   B 1 34  ? -7.270  17.955  7.515   1.00 76.79  ? 39  ARG   B NH2 1 
ATOM   2610 N  N   . LYS   B 1 35  ? -9.020  24.524  12.805  1.00 44.46  ? 40  LYS   B N   1 
ATOM   2611 C  CA  . LYS   B 1 35  ? -9.332  24.701  14.221  1.00 43.22  ? 40  LYS   B CA  1 
ATOM   2612 C  C   . LYS   B 1 35  ? -9.351  23.344  14.953  1.00 41.72  ? 40  LYS   B C   1 
ATOM   2613 O  O   . LYS   B 1 35  ? -9.737  22.320  14.360  1.00 39.95  ? 40  LYS   B O   1 
ATOM   2614 C  CB  . LYS   B 1 35  ? -10.643 25.499  14.431  1.00 47.38  ? 40  LYS   B CB  1 
ATOM   2615 C  CG  . LYS   B 1 35  ? -11.882 24.924  13.732  1.00 72.57  ? 40  LYS   B CG  1 
ATOM   2616 C  CD  . LYS   B 1 35  ? -13.138 25.787  13.945  1.00 86.06  ? 40  LYS   B CD  1 
ATOM   2617 C  CE  . LYS   B 1 35  ? -13.343 26.809  12.847  1.00 99.30  ? 40  LYS   B CE  1 
ATOM   2618 N  NZ  . LYS   B 1 35  ? -14.648 27.510  12.978  1.00 108.95 ? 40  LYS   B NZ  1 
ATOM   2619 N  N   . GLY   B 1 36  ? -8.903  23.357  16.212  1.00 35.49  ? 41  GLY   B N   1 
ATOM   2620 C  CA  . GLY   B 1 36  ? -8.934  22.179  17.076  1.00 35.44  ? 41  GLY   B CA  1 
ATOM   2621 C  C   . GLY   B 1 36  ? -7.614  21.725  17.678  1.00 36.48  ? 41  GLY   B C   1 
ATOM   2622 O  O   . GLY   B 1 36  ? -7.619  21.030  18.695  1.00 36.57  ? 41  GLY   B O   1 
ATOM   2623 N  N   . VAL   B 1 37  ? -6.488  22.092  17.052  1.00 31.68  ? 42  VAL   B N   1 
ATOM   2624 C  CA  . VAL   B 1 37  ? -5.134  21.690  17.505  1.00 30.66  ? 42  VAL   B CA  1 
ATOM   2625 C  C   . VAL   B 1 37  ? -4.798  22.325  18.888  1.00 34.25  ? 42  VAL   B C   1 
ATOM   2626 O  O   . VAL   B 1 37  ? -3.972  21.788  19.636  1.00 32.44  ? 42  VAL   B O   1 
ATOM   2627 C  CB  . VAL   B 1 37  ? -4.062  21.950  16.406  1.00 33.54  ? 42  VAL   B CB  1 
ATOM   2628 C  CG1 . VAL   B 1 37  ? -3.740  23.426  16.248  1.00 33.12  ? 42  VAL   B CG1 1 
ATOM   2629 C  CG2 . VAL   B 1 37  ? -2.795  21.127  16.629  1.00 32.81  ? 42  VAL   B CG2 1 
ATOM   2630 N  N   . GLU   B 1 38  ? -5.493  23.441  19.245  1.00 31.29  ? 43  GLU   B N   1 
ATOM   2631 C  CA  . GLU   B 1 38  ? -5.358  24.085  20.556  1.00 31.46  ? 43  GLU   B CA  1 
ATOM   2632 C  C   . GLU   B 1 38  ? -5.855  23.144  21.686  1.00 35.38  ? 43  GLU   B C   1 
ATOM   2633 O  O   . GLU   B 1 38  ? -5.476  23.333  22.841  1.00 36.46  ? 43  GLU   B O   1 
ATOM   2634 C  CB  . GLU   B 1 38  ? -6.107  25.444  20.578  1.00 32.65  ? 43  GLU   B CB  1 
ATOM   2635 C  CG  . GLU   B 1 38  ? -7.621  25.329  20.439  1.00 41.30  ? 43  GLU   B CG  1 
ATOM   2636 C  CD  . GLU   B 1 38  ? -8.199  25.352  19.035  1.00 59.81  ? 43  GLU   B CD  1 
ATOM   2637 O  OE1 . GLU   B 1 38  ? -7.509  24.924  18.080  1.00 39.07  ? 43  GLU   B OE1 1 
ATOM   2638 O  OE2 . GLU   B 1 38  ? -9.369  25.778  18.895  1.00 53.65  ? 43  GLU   B OE2 1 
ATOM   2639 N  N   . HIS   B 1 39  ? -6.668  22.119  21.346  1.00 32.14  ? 44  HIS   B N   1 
ATOM   2640 C  CA  . HIS   B 1 39  ? -7.194  21.123  22.279  1.00 33.24  ? 44  HIS   B CA  1 
ATOM   2641 C  C   . HIS   B 1 39  ? -6.288  19.873  22.452  1.00 33.90  ? 44  HIS   B C   1 
ATOM   2642 O  O   . HIS   B 1 39  ? -6.620  18.970  23.233  1.00 32.05  ? 44  HIS   B O   1 
ATOM   2643 C  CB  . HIS   B 1 39  ? -8.630  20.733  21.876  1.00 35.36  ? 44  HIS   B CB  1 
ATOM   2644 C  CG  . HIS   B 1 39  ? -9.541  21.921  21.835  1.00 40.62  ? 44  HIS   B CG  1 
ATOM   2645 N  ND1 . HIS   B 1 39  ? -9.699  22.746  22.939  1.00 43.52  ? 44  HIS   B ND1 1 
ATOM   2646 C  CD2 . HIS   B 1 39  ? -10.258 22.427  20.804  1.00 43.98  ? 44  HIS   B CD2 1 
ATOM   2647 C  CE1 . HIS   B 1 39  ? -10.520 23.712  22.553  1.00 43.62  ? 44  HIS   B CE1 1 
ATOM   2648 N  NE2 . HIS   B 1 39  ? -10.890 23.560  21.279  1.00 44.06  ? 44  HIS   B NE2 1 
ATOM   2649 N  N   . GLY   B 1 40  ? -5.164  19.842  21.723  1.00 31.24  ? 45  GLY   B N   1 
ATOM   2650 C  CA  . GLY   B 1 40  ? -4.195  18.747  21.790  1.00 29.47  ? 45  GLY   B CA  1 
ATOM   2651 C  C   . GLY   B 1 40  ? -3.662  18.540  23.204  1.00 29.08  ? 45  GLY   B C   1 
ATOM   2652 O  O   . GLY   B 1 40  ? -3.686  17.404  23.701  1.00 27.20  ? 45  GLY   B O   1 
ATOM   2653 N  N   . PRO   B 1 41  ? -3.223  19.614  23.917  1.00 27.54  ? 46  PRO   B N   1 
ATOM   2654 C  CA  . PRO   B 1 41  ? -2.697  19.415  25.285  1.00 27.83  ? 46  PRO   B CA  1 
ATOM   2655 C  C   . PRO   B 1 41  ? -3.715  18.796  26.230  1.00 30.28  ? 46  PRO   B C   1 
ATOM   2656 O  O   . PRO   B 1 41  ? -3.399  17.819  26.894  1.00 27.24  ? 46  PRO   B O   1 
ATOM   2657 C  CB  . PRO   B 1 41  ? -2.248  20.819  25.700  1.00 28.98  ? 46  PRO   B CB  1 
ATOM   2658 C  CG  . PRO   B 1 41  ? -1.955  21.492  24.400  1.00 32.17  ? 46  PRO   B CG  1 
ATOM   2659 C  CD  . PRO   B 1 41  ? -3.053  21.023  23.510  1.00 27.85  ? 46  PRO   B CD  1 
ATOM   2660 N  N   . ALA   B 1 42  ? -4.966  19.300  26.224  1.00 29.95  ? 47  ALA   B N   1 
ATOM   2661 C  CA  . ALA   B 1 42  ? -6.017  18.725  27.066  1.00 30.27  ? 47  ALA   B CA  1 
ATOM   2662 C  C   . ALA   B 1 42  ? -6.314  17.272  26.682  1.00 32.51  ? 47  ALA   B C   1 
ATOM   2663 O  O   . ALA   B 1 42  ? -6.530  16.455  27.568  1.00 31.77  ? 47  ALA   B O   1 
ATOM   2664 C  CB  . ALA   B 1 42  ? -7.281  19.570  26.975  1.00 30.86  ? 47  ALA   B CB  1 
ATOM   2665 N  N   . ALA   B 1 43  ? -6.288  16.932  25.376  1.00 29.13  ? 48  ALA   B N   1 
ATOM   2666 C  CA  . ALA   B 1 43  ? -6.540  15.555  24.939  1.00 29.05  ? 48  ALA   B CA  1 
ATOM   2667 C  C   . ALA   B 1 43  ? -5.435  14.602  25.449  1.00 30.42  ? 48  ALA   B C   1 
ATOM   2668 O  O   . ALA   B 1 43  ? -5.737  13.510  25.922  1.00 31.05  ? 48  ALA   B O   1 
ATOM   2669 C  CB  . ALA   B 1 43  ? -6.641  15.497  23.418  1.00 29.53  ? 48  ALA   B CB  1 
ATOM   2670 N  N   . ILE   B 1 44  ? -4.161  15.023  25.348  1.00 27.15  ? 49  ILE   B N   1 
ATOM   2671 C  CA  . ILE   B 1 44  ? -3.020  14.220  25.811  1.00 26.09  ? 49  ILE   B CA  1 
ATOM   2672 C  C   . ILE   B 1 44  ? -3.097  14.035  27.346  1.00 31.21  ? 49  ILE   B C   1 
ATOM   2673 O  O   . ILE   B 1 44  ? -2.917  12.915  27.843  1.00 31.50  ? 49  ILE   B O   1 
ATOM   2674 C  CB  . ILE   B 1 44  ? -1.665  14.790  25.326  1.00 27.51  ? 49  ILE   B CB  1 
ATOM   2675 C  CG1 . ILE   B 1 44  ? -1.597  14.792  23.762  1.00 27.37  ? 49  ILE   B CG1 1 
ATOM   2676 C  CG2 . ILE   B 1 44  ? -0.481  13.999  25.939  1.00 26.85  ? 49  ILE   B CG2 1 
ATOM   2677 C  CD1 . ILE   B 1 44  ? -0.543  15.713  23.174  1.00 29.06  ? 49  ILE   B CD1 1 
ATOM   2678 N  N   . ARG   B 1 45  ? -3.441  15.120  28.074  1.00 28.20  ? 50  ARG   B N   1 
ATOM   2679 C  CA  . ARG   B 1 45  ? -3.598  15.078  29.534  1.00 28.25  ? 50  ARG   B CA  1 
ATOM   2680 C  C   . ARG   B 1 45  ? -4.725  14.116  29.943  1.00 33.09  ? 50  ARG   B C   1 
ATOM   2681 O  O   . ARG   B 1 45  ? -4.543  13.318  30.858  1.00 32.45  ? 50  ARG   B O   1 
ATOM   2682 C  CB  . ARG   B 1 45  ? -3.857  16.483  30.090  1.00 28.36  ? 50  ARG   B CB  1 
ATOM   2683 C  CG  . ARG   B 1 45  ? -2.638  17.386  30.047  1.00 34.69  ? 50  ARG   B CG  1 
ATOM   2684 C  CD  . ARG   B 1 45  ? -2.974  18.740  30.647  1.00 37.29  ? 50  ARG   B CD  1 
ATOM   2685 N  NE  . ARG   B 1 45  ? -1.840  19.667  30.656  1.00 33.46  ? 50  ARG   B NE  1 
ATOM   2686 C  CZ  . ARG   B 1 45  ? -0.925  19.736  31.619  1.00 43.90  ? 50  ARG   B CZ  1 
ATOM   2687 N  NH1 . ARG   B 1 45  ? -0.943  18.871  32.627  1.00 34.27  ? 50  ARG   B NH1 1 
ATOM   2688 N  NH2 . ARG   B 1 45  ? 0.046   20.639  31.556  1.00 40.33  ? 50  ARG   B NH2 1 
ATOM   2689 N  N   . GLU   B 1 46  ? -5.867  14.162  29.226  1.00 32.72  ? 51  GLU   B N   1 
ATOM   2690 C  CA  . GLU   B 1 46  ? -7.036  13.304  29.481  1.00 33.62  ? 51  GLU   B CA  1 
ATOM   2691 C  C   . GLU   B 1 46  ? -6.733  11.827  29.267  1.00 36.73  ? 51  GLU   B C   1 
ATOM   2692 O  O   . GLU   B 1 46  ? -7.347  10.970  29.907  1.00 36.51  ? 51  GLU   B O   1 
ATOM   2693 C  CB  . GLU   B 1 46  ? -8.232  13.747  28.627  1.00 35.36  ? 51  GLU   B CB  1 
ATOM   2694 C  CG  . GLU   B 1 46  ? -8.942  14.961  29.208  1.00 50.74  ? 51  GLU   B CG  1 
ATOM   2695 C  CD  . GLU   B 1 46  ? -9.669  15.885  28.245  1.00 74.84  ? 51  GLU   B CD  1 
ATOM   2696 O  OE1 . GLU   B 1 46  ? -10.085 15.430  27.154  1.00 70.81  ? 51  GLU   B OE1 1 
ATOM   2697 O  OE2 . GLU   B 1 46  ? -9.846  17.071  28.606  1.00 67.20  ? 51  GLU   B OE2 1 
ATOM   2698 N  N   . ALA   B 1 47  ? -5.771  11.527  28.357  1.00 31.89  ? 52  ALA   B N   1 
ATOM   2699 C  CA  . ALA   B 1 47  ? -5.320  10.173  28.039  1.00 32.25  ? 52  ALA   B CA  1 
ATOM   2700 C  C   . ALA   B 1 47  ? -4.397  9.577   29.140  1.00 35.96  ? 52  ALA   B C   1 
ATOM   2701 O  O   . ALA   B 1 47  ? -3.935  8.435   29.015  1.00 36.47  ? 52  ALA   B O   1 
ATOM   2702 C  CB  . ALA   B 1 47  ? -4.641  10.163  26.676  1.00 32.71  ? 52  ALA   B CB  1 
ATOM   2703 N  N   . GLY   B 1 48  ? -4.193  10.343  30.219  1.00 32.12  ? 53  GLY   B N   1 
ATOM   2704 C  CA  . GLY   B 1 48  ? -3.457  9.939   31.414  1.00 31.80  ? 53  GLY   B CA  1 
ATOM   2705 C  C   . GLY   B 1 48  ? -1.971  10.210  31.429  1.00 31.84  ? 53  GLY   B C   1 
ATOM   2706 O  O   . GLY   B 1 48  ? -1.234  9.479   32.094  1.00 32.89  ? 53  GLY   B O   1 
ATOM   2707 N  N   . LEU   B 1 49  ? -1.515  11.258  30.726  1.00 27.24  ? 54  LEU   B N   1 
ATOM   2708 C  CA  . LEU   B 1 49  ? -0.076  11.559  30.646  1.00 26.23  ? 54  LEU   B CA  1 
ATOM   2709 C  C   . LEU   B 1 49  ? 0.656   11.627  31.993  1.00 29.36  ? 54  LEU   B C   1 
ATOM   2710 O  O   . LEU   B 1 49  ? 1.645   10.918  32.195  1.00 28.19  ? 54  LEU   B O   1 
ATOM   2711 C  CB  . LEU   B 1 49  ? 0.196   12.851  29.853  1.00 25.48  ? 54  LEU   B CB  1 
ATOM   2712 C  CG  . LEU   B 1 49  ? 1.695   13.232  29.733  1.00 29.71  ? 54  LEU   B CG  1 
ATOM   2713 C  CD1 . LEU   B 1 49  ? 2.492   12.171  28.939  1.00 30.48  ? 54  LEU   B CD1 1 
ATOM   2714 C  CD2 . LEU   B 1 49  ? 1.868   14.592  29.141  1.00 29.49  ? 54  LEU   B CD2 1 
ATOM   2715 N  N   . MET   B 1 50  ? 0.160   12.468  32.915  1.00 28.30  ? 55  MET   B N   1 
ATOM   2716 C  CA  . MET   B 1 50  ? 0.812   12.692  34.209  1.00 28.31  ? 55  MET   B CA  1 
ATOM   2717 C  C   . MET   B 1 50  ? 0.883   11.420  35.052  1.00 31.16  ? 55  MET   B C   1 
ATOM   2718 O  O   . MET   B 1 50  ? 1.964   11.092  35.553  1.00 30.00  ? 55  MET   B O   1 
ATOM   2719 C  CB  . MET   B 1 50  ? 0.173   13.882  34.946  1.00 30.02  ? 55  MET   B CB  1 
ATOM   2720 C  CG  . MET   B 1 50  ? 0.192   15.170  34.098  1.00 34.00  ? 55  MET   B CG  1 
ATOM   2721 S  SD  . MET   B 1 50  ? 1.836   15.597  33.409  1.00 37.59  ? 55  MET   B SD  1 
ATOM   2722 C  CE  . MET   B 1 50  ? 2.564   16.395  34.815  1.00 35.51  ? 55  MET   B CE  1 
ATOM   2723 N  N   . LYS   B 1 51  ? -0.209  10.648  35.089  1.00 29.60  ? 56  LYS   B N   1 
ATOM   2724 C  CA  . LYS   B 1 51  ? -0.285  9.373   35.795  1.00 30.35  ? 56  LYS   B CA  1 
ATOM   2725 C  C   . LYS   B 1 51  ? 0.709   8.374   35.214  1.00 33.26  ? 56  LYS   B C   1 
ATOM   2726 O  O   . LYS   B 1 51  ? 1.388   7.669   35.966  1.00 32.59  ? 56  LYS   B O   1 
ATOM   2727 C  CB  . LYS   B 1 51  ? -1.714  8.810   35.744  1.00 35.16  ? 56  LYS   B CB  1 
ATOM   2728 C  CG  . LYS   B 1 51  ? -2.006  7.776   36.825  1.00 57.22  ? 56  LYS   B CG  1 
ATOM   2729 C  CD  . LYS   B 1 51  ? -3.453  7.305   36.794  1.00 72.45  ? 56  LYS   B CD  1 
ATOM   2730 C  CE  . LYS   B 1 51  ? -3.767  6.411   37.970  1.00 87.58  ? 56  LYS   B CE  1 
ATOM   2731 N  NZ  . LYS   B 1 51  ? -5.212  6.072   38.041  1.00 98.48  ? 56  LYS   B NZ  1 
ATOM   2732 N  N   . ARG   B 1 52  ? 0.838   8.351   33.871  1.00 29.33  ? 57  ARG   B N   1 
ATOM   2733 C  CA  . ARG   B 1 52  ? 1.743   7.420   33.222  1.00 27.68  ? 57  ARG   B CA  1 
ATOM   2734 C  C   . ARG   B 1 52  ? 3.190   7.737   33.591  1.00 28.74  ? 57  ARG   B C   1 
ATOM   2735 O  O   . ARG   B 1 52  ? 3.946   6.819   33.908  1.00 29.23  ? 57  ARG   B O   1 
ATOM   2736 C  CB  . ARG   B 1 52  ? 1.542   7.440   31.699  1.00 26.99  ? 57  ARG   B CB  1 
ATOM   2737 C  CG  . ARG   B 1 52  ? 2.433   6.447   30.951  1.00 27.78  ? 57  ARG   B CG  1 
ATOM   2738 C  CD  . ARG   B 1 52  ? 1.937   4.995   30.990  1.00 31.36  ? 57  ARG   B CD  1 
ATOM   2739 N  NE  . ARG   B 1 52  ? 0.618   4.870   30.383  1.00 36.91  ? 57  ARG   B NE  1 
ATOM   2740 C  CZ  . ARG   B 1 52  ? 0.409   4.743   29.075  1.00 47.03  ? 57  ARG   B CZ  1 
ATOM   2741 N  NH1 . ARG   B 1 52  ? -0.821  4.680   28.599  1.00 40.05  ? 57  ARG   B NH1 1 
ATOM   2742 N  NH2 . ARG   B 1 52  ? 1.429   4.662   28.239  1.00 33.03  ? 57  ARG   B NH2 1 
ATOM   2743 N  N   . LEU   B 1 53  ? 3.572   9.026   33.530  1.00 26.53  ? 58  LEU   B N   1 
ATOM   2744 C  CA  . LEU   B 1 53  ? 4.934   9.452   33.850  1.00 26.07  ? 58  LEU   B CA  1 
ATOM   2745 C  C   . LEU   B 1 53  ? 5.238   9.169   35.319  1.00 28.73  ? 58  LEU   B C   1 
ATOM   2746 O  O   . LEU   B 1 53  ? 6.332   8.703   35.610  1.00 28.38  ? 58  LEU   B O   1 
ATOM   2747 C  CB  . LEU   B 1 53  ? 5.185   10.920  33.497  1.00 26.69  ? 58  LEU   B CB  1 
ATOM   2748 C  CG  . LEU   B 1 53  ? 5.209   11.224  31.988  1.00 30.87  ? 58  LEU   B CG  1 
ATOM   2749 C  CD1 . LEU   B 1 53  ? 5.235   12.707  31.731  1.00 30.54  ? 58  LEU   B CD1 1 
ATOM   2750 C  CD2 . LEU   B 1 53  ? 6.369   10.507  31.292  1.00 34.40  ? 58  LEU   B CD2 1 
ATOM   2751 N  N   . SER   B 1 54  ? 4.257   9.379   36.211  1.00 28.88  ? 59  SER   B N   1 
ATOM   2752 C  CA  . SER   B 1 54  ? 4.411   9.098   37.654  1.00 29.82  ? 59  SER   B CA  1 
ATOM   2753 C  C   . SER   B 1 54  ? 4.654   7.616   37.862  1.00 32.97  ? 59  SER   B C   1 
ATOM   2754 O  O   . SER   B 1 54  ? 5.534   7.259   38.643  1.00 32.78  ? 59  SER   B O   1 
ATOM   2755 C  CB  . SER   B 1 54  ? 3.167   9.527   38.425  1.00 36.37  ? 59  SER   B CB  1 
ATOM   2756 O  OG  . SER   B 1 54  ? 3.096   10.941  38.492  1.00 47.36  ? 59  SER   B OG  1 
ATOM   2757 N  N   . SER   B 1 55  ? 3.944   6.755   37.077  1.00 30.08  ? 60  SER   B N   1 
ATOM   2758 C  CA  . SER   B 1 55  ? 4.052   5.301   37.128  1.00 30.25  ? 60  SER   B CA  1 
ATOM   2759 C  C   . SER   B 1 55  ? 5.423   4.812   36.663  1.00 31.36  ? 60  SER   B C   1 
ATOM   2760 O  O   . SER   B 1 55  ? 5.831   3.706   37.006  1.00 31.07  ? 60  SER   B O   1 
ATOM   2761 C  CB  . SER   B 1 55  ? 2.895   4.631   36.389  1.00 34.29  ? 60  SER   B CB  1 
ATOM   2762 O  OG  . SER   B 1 55  ? 3.134   4.519   34.996  1.00 40.80  ? 60  SER   B OG  1 
ATOM   2763 N  N   . LEU   B 1 56  ? 6.166   5.680   35.968  1.00 27.40  ? 61  LEU   B N   1 
ATOM   2764 C  CA  . LEU   B 1 56  ? 7.528   5.414   35.522  1.00 27.38  ? 61  LEU   B CA  1 
ATOM   2765 C  C   . LEU   B 1 56  ? 8.566   5.914   36.524  1.00 31.78  ? 61  LEU   B C   1 
ATOM   2766 O  O   . LEU   B 1 56  ? 9.761   5.783   36.276  1.00 32.19  ? 61  LEU   B O   1 
ATOM   2767 C  CB  . LEU   B 1 56  ? 7.793   6.022   34.127  1.00 27.54  ? 61  LEU   B CB  1 
ATOM   2768 C  CG  . LEU   B 1 56  ? 6.999   5.395   32.987  1.00 31.24  ? 61  LEU   B CG  1 
ATOM   2769 C  CD1 . LEU   B 1 56  ? 7.265   6.144   31.680  1.00 30.46  ? 61  LEU   B CD1 1 
ATOM   2770 C  CD2 . LEU   B 1 56  ? 7.287   3.892   32.845  1.00 33.56  ? 61  LEU   B CD2 1 
ATOM   2771 N  N   . GLY   B 1 57  ? 8.106   6.433   37.655  1.00 31.52  ? 62  GLY   B N   1 
ATOM   2772 C  CA  . GLY   B 1 57  ? 8.996   6.927   38.698  1.00 31.74  ? 62  GLY   B CA  1 
ATOM   2773 C  C   . GLY   B 1 57  ? 9.586   8.295   38.417  1.00 35.45  ? 62  GLY   B C   1 
ATOM   2774 O  O   . GLY   B 1 57  ? 10.632  8.635   38.980  1.00 36.91  ? 62  GLY   B O   1 
ATOM   2775 N  N   . CYS   B 1 58  ? 8.949   9.083   37.524  1.00 29.73  ? 63  CYS   B N   1 
ATOM   2776 C  CA  . CYS   B 1 58  ? 9.411   10.441  37.212  1.00 28.59  ? 63  CYS   B CA  1 
ATOM   2777 C  C   . CYS   B 1 58  ? 9.114   11.399  38.347  1.00 32.99  ? 63  CYS   B C   1 
ATOM   2778 O  O   . CYS   B 1 58  ? 8.061   11.305  38.981  1.00 33.38  ? 63  CYS   B O   1 
ATOM   2779 C  CB  . CYS   B 1 58  ? 8.767   10.966  35.930  1.00 28.07  ? 63  CYS   B CB  1 
ATOM   2780 S  SG  . CYS   B 1 58  ? 9.220   10.066  34.427  1.00 31.34  ? 63  CYS   B SG  1 
ATOM   2781 N  N   . HIS   B 1 59  ? 9.999   12.380  38.532  1.00 29.66  ? 64  HIS   B N   1 
ATOM   2782 C  CA  . HIS   B 1 59  ? 9.767   13.537  39.399  1.00 29.81  ? 64  HIS   B CA  1 
ATOM   2783 C  C   . HIS   B 1 59  ? 9.131   14.522  38.421  1.00 34.46  ? 64  HIS   B C   1 
ATOM   2784 O  O   . HIS   B 1 59  ? 9.732   14.796  37.382  1.00 35.31  ? 64  HIS   B O   1 
ATOM   2785 C  CB  . HIS   B 1 59  ? 11.098  14.116  39.898  1.00 30.50  ? 64  HIS   B CB  1 
ATOM   2786 C  CG  . HIS   B 1 59  ? 11.798  13.268  40.909  1.00 33.02  ? 64  HIS   B CG  1 
ATOM   2787 N  ND1 . HIS   B 1 59  ? 11.181  12.889  42.086  1.00 34.95  ? 64  HIS   B ND1 1 
ATOM   2788 C  CD2 . HIS   B 1 59  ? 13.065  12.799  40.911  1.00 34.98  ? 64  HIS   B CD2 1 
ATOM   2789 C  CE1 . HIS   B 1 59  ? 12.081  12.193  42.756  1.00 33.92  ? 64  HIS   B CE1 1 
ATOM   2790 N  NE2 . HIS   B 1 59  ? 13.225  12.100  42.085  1.00 34.53  ? 64  HIS   B NE2 1 
ATOM   2791 N  N   . LEU   B 1 60  ? 7.910   14.978  38.688  1.00 31.61  ? 65  LEU   B N   1 
ATOM   2792 C  CA  . LEU   B 1 60  ? 7.197   15.874  37.779  1.00 32.62  ? 65  LEU   B CA  1 
ATOM   2793 C  C   . LEU   B 1 60  ? 7.083   17.309  38.243  1.00 38.70  ? 65  LEU   B C   1 
ATOM   2794 O  O   . LEU   B 1 60  ? 6.852   17.572  39.425  1.00 37.62  ? 65  LEU   B O   1 
ATOM   2795 C  CB  . LEU   B 1 60  ? 5.754   15.366  37.550  1.00 33.17  ? 65  LEU   B CB  1 
ATOM   2796 C  CG  . LEU   B 1 60  ? 5.445   14.171  36.615  1.00 38.51  ? 65  LEU   B CG  1 
ATOM   2797 C  CD1 . LEU   B 1 60  ? 6.231   14.208  35.298  1.00 38.57  ? 65  LEU   B CD1 1 
ATOM   2798 C  CD2 . LEU   B 1 60  ? 5.554   12.863  37.326  1.00 45.14  ? 65  LEU   B CD2 1 
ATOM   2799 N  N   . LYS   B 1 61  ? 7.140   18.241  37.283  1.00 35.61  ? 66  LYS   B N   1 
ATOM   2800 C  CA  . LYS   B 1 61  ? 6.836   19.662  37.488  1.00 34.79  ? 66  LYS   B CA  1 
ATOM   2801 C  C   . LYS   B 1 61  ? 5.873   20.042  36.377  1.00 38.33  ? 66  LYS   B C   1 
ATOM   2802 O  O   . LYS   B 1 61  ? 6.264   20.101  35.208  1.00 37.87  ? 66  LYS   B O   1 
ATOM   2803 C  CB  . LYS   B 1 61  ? 8.078   20.561  37.508  1.00 37.71  ? 66  LYS   B CB  1 
ATOM   2804 C  CG  . LYS   B 1 61  ? 7.748   22.013  37.850  1.00 45.23  ? 66  LYS   B CG  1 
ATOM   2805 C  CD  . LYS   B 1 61  ? 8.994   22.851  38.088  1.00 50.42  ? 66  LYS   B CD  1 
ATOM   2806 C  CE  . LYS   B 1 61  ? 8.646   24.243  38.556  1.00 65.17  ? 66  LYS   B CE  1 
ATOM   2807 N  NZ  . LYS   B 1 61  ? 9.864   25.070  38.764  1.00 73.92  ? 66  LYS   B NZ  1 
ATOM   2808 N  N   . ASP   B 1 62  ? 4.599   20.235  36.726  1.00 35.00  ? 67  ASP   B N   1 
ATOM   2809 C  CA  . ASP   B 1 62  ? 3.605   20.616  35.744  1.00 34.65  ? 67  ASP   B CA  1 
ATOM   2810 C  C   . ASP   B 1 62  ? 3.510   22.143  35.683  1.00 39.33  ? 67  ASP   B C   1 
ATOM   2811 O  O   . ASP   B 1 62  ? 3.093   22.779  36.667  1.00 38.36  ? 67  ASP   B O   1 
ATOM   2812 C  CB  . ASP   B 1 62  ? 2.253   19.968  36.063  1.00 36.42  ? 67  ASP   B CB  1 
ATOM   2813 C  CG  . ASP   B 1 62  ? 1.207   20.073  34.968  1.00 39.36  ? 67  ASP   B CG  1 
ATOM   2814 O  OD1 . ASP   B 1 62  ? 1.441   20.817  33.982  1.00 37.56  ? 67  ASP   B OD1 1 
ATOM   2815 O  OD2 . ASP   B 1 62  ? 0.147   19.429  35.105  1.00 44.50  ? 67  ASP   B OD2 1 
ATOM   2816 N  N   . PHE   B 1 63  ? 3.930   22.734  34.542  1.00 34.95  ? 68  PHE   B N   1 
ATOM   2817 C  CA  . PHE   B 1 63  ? 3.868   24.184  34.340  1.00 34.74  ? 68  PHE   B CA  1 
ATOM   2818 C  C   . PHE   B 1 63  ? 2.473   24.629  33.892  1.00 40.10  ? 68  PHE   B C   1 
ATOM   2819 O  O   . PHE   B 1 63  ? 2.254   25.827  33.690  1.00 41.11  ? 68  PHE   B O   1 
ATOM   2820 C  CB  . PHE   B 1 63  ? 4.946   24.655  33.351  1.00 36.92  ? 68  PHE   B CB  1 
ATOM   2821 C  CG  . PHE   B 1 63  ? 6.340   24.769  33.921  1.00 39.49  ? 68  PHE   B CG  1 
ATOM   2822 C  CD1 . PHE   B 1 63  ? 7.170   23.657  34.003  1.00 42.89  ? 68  PHE   B CD1 1 
ATOM   2823 C  CD2 . PHE   B 1 63  ? 6.839   25.996  34.339  1.00 41.99  ? 68  PHE   B CD2 1 
ATOM   2824 C  CE1 . PHE   B 1 63  ? 8.469   23.770  34.506  1.00 44.57  ? 68  PHE   B CE1 1 
ATOM   2825 C  CE2 . PHE   B 1 63  ? 8.139   26.110  34.839  1.00 45.10  ? 68  PHE   B CE2 1 
ATOM   2826 C  CZ  . PHE   B 1 63  ? 8.947   24.997  34.921  1.00 43.80  ? 68  PHE   B CZ  1 
ATOM   2827 N  N   . GLY   B 1 64  ? 1.546   23.672  33.774  1.00 36.83  ? 69  GLY   B N   1 
ATOM   2828 C  CA  . GLY   B 1 64  ? 0.174   23.891  33.334  1.00 37.04  ? 69  GLY   B CA  1 
ATOM   2829 C  C   . GLY   B 1 64  ? 0.105   24.205  31.852  1.00 42.67  ? 69  GLY   B C   1 
ATOM   2830 O  O   . GLY   B 1 64  ? 1.073   23.983  31.115  1.00 40.94  ? 69  GLY   B O   1 
ATOM   2831 N  N   . ASP   B 1 65  ? -1.041  24.714  31.400  1.00 40.45  ? 70  ASP   B N   1 
ATOM   2832 C  CA  . ASP   B 1 65  ? -1.219  25.067  29.997  1.00 41.11  ? 70  ASP   B CA  1 
ATOM   2833 C  C   . ASP   B 1 65  ? -1.071  26.569  29.839  1.00 47.32  ? 70  ASP   B C   1 
ATOM   2834 O  O   . ASP   B 1 65  ? -1.759  27.335  30.529  1.00 47.30  ? 70  ASP   B O   1 
ATOM   2835 C  CB  . ASP   B 1 65  ? -2.569  24.552  29.461  1.00 42.97  ? 70  ASP   B CB  1 
ATOM   2836 C  CG  . ASP   B 1 65  ? -2.769  23.049  29.616  1.00 53.32  ? 70  ASP   B CG  1 
ATOM   2837 O  OD1 . ASP   B 1 65  ? -1.772  22.296  29.493  1.00 50.35  ? 70  ASP   B OD1 1 
ATOM   2838 O  OD2 . ASP   B 1 65  ? -3.928  22.623  29.824  1.00 64.42  ? 70  ASP   B OD2 1 
ATOM   2839 N  N   . LEU   B 1 66  ? -0.128  26.992  28.984  1.00 44.97  ? 71  LEU   B N   1 
ATOM   2840 C  CA  . LEU   B 1 66  ? 0.140   28.407  28.744  1.00 45.98  ? 71  LEU   B CA  1 
ATOM   2841 C  C   . LEU   B 1 66  ? -1.032  29.095  28.048  1.00 53.46  ? 71  LEU   B C   1 
ATOM   2842 O  O   . LEU   B 1 66  ? -1.775  28.451  27.302  1.00 52.37  ? 71  LEU   B O   1 
ATOM   2843 C  CB  . LEU   B 1 66  ? 1.423   28.617  27.933  1.00 46.03  ? 71  LEU   B CB  1 
ATOM   2844 C  CG  . LEU   B 1 66  ? 2.755   28.094  28.489  1.00 51.16  ? 71  LEU   B CG  1 
ATOM   2845 C  CD1 . LEU   B 1 66  ? 3.902   28.473  27.557  1.00 51.28  ? 71  LEU   B CD1 1 
ATOM   2846 C  CD2 . LEU   B 1 66  ? 3.040   28.618  29.903  1.00 53.96  ? 71  LEU   B CD2 1 
ATOM   2847 N  N   . SER   B 1 67  ? -1.197  30.400  28.319  1.00 53.21  ? 72  SER   B N   1 
ATOM   2848 C  CA  . SER   B 1 67  ? -2.255  31.241  27.763  1.00 55.08  ? 72  SER   B CA  1 
ATOM   2849 C  C   . SER   B 1 67  ? -1.655  32.154  26.705  1.00 62.82  ? 72  SER   B C   1 
ATOM   2850 O  O   . SER   B 1 67  ? -0.673  32.854  26.971  1.00 61.77  ? 72  SER   B O   1 
ATOM   2851 C  CB  . SER   B 1 67  ? -2.910  32.076  28.863  1.00 59.23  ? 72  SER   B CB  1 
ATOM   2852 O  OG  . SER   B 1 67  ? -3.424  31.270  29.911  1.00 69.59  ? 72  SER   B OG  1 
ATOM   2853 N  N   . PHE   B 1 68  ? -2.222  32.117  25.493  1.00 62.95  ? 73  PHE   B N   1 
ATOM   2854 C  CA  . PHE   B 1 68  ? -1.748  32.942  24.391  1.00 64.37  ? 73  PHE   B CA  1 
ATOM   2855 C  C   . PHE   B 1 68  ? -2.848  33.875  23.918  1.00 71.04  ? 73  PHE   B C   1 
ATOM   2856 O  O   . PHE   B 1 68  ? -3.886  33.418  23.428  1.00 71.28  ? 73  PHE   B O   1 
ATOM   2857 C  CB  . PHE   B 1 68  ? -1.207  32.081  23.231  1.00 66.29  ? 73  PHE   B CB  1 
ATOM   2858 C  CG  . PHE   B 1 68  ? -0.194  31.031  23.626  1.00 67.88  ? 73  PHE   B CG  1 
ATOM   2859 C  CD1 . PHE   B 1 68  ? 1.078   31.394  24.058  1.00 70.96  ? 73  PHE   B CD1 1 
ATOM   2860 C  CD2 . PHE   B 1 68  ? -0.507  29.679  23.553  1.00 69.89  ? 73  PHE   B CD2 1 
ATOM   2861 C  CE1 . PHE   B 1 68  ? 2.018   30.423  24.410  1.00 71.87  ? 73  PHE   B CE1 1 
ATOM   2862 C  CE2 . PHE   B 1 68  ? 0.435   28.709  23.905  1.00 72.66  ? 73  PHE   B CE2 1 
ATOM   2863 C  CZ  . PHE   B 1 68  ? 1.688   29.087  24.334  1.00 70.83  ? 73  PHE   B CZ  1 
ATOM   2864 N  N   . THR   B 1 69  ? -2.631  35.184  24.107  1.00 68.89  ? 74  THR   B N   1 
ATOM   2865 C  CA  . THR   B 1 69  ? -3.562  36.223  23.671  1.00 69.40  ? 74  THR   B CA  1 
ATOM   2866 C  C   . THR   B 1 69  ? -3.102  36.702  22.290  1.00 73.65  ? 74  THR   B C   1 
ATOM   2867 O  O   . THR   B 1 69  ? -1.958  37.153  22.162  1.00 72.88  ? 74  THR   B O   1 
ATOM   2868 C  CB  . THR   B 1 69  ? -3.680  37.358  24.705  1.00 80.39  ? 74  THR   B CB  1 
ATOM   2869 O  OG1 . THR   B 1 69  ? -2.373  37.801  25.078  1.00 83.15  ? 74  THR   B OG1 1 
ATOM   2870 C  CG2 . THR   B 1 69  ? -4.474  36.948  25.942  1.00 78.38  ? 74  THR   B CG2 1 
ATOM   2871 N  N   . PRO   B 1 70  ? -3.937  36.555  21.231  1.00 70.95  ? 75  PRO   B N   1 
ATOM   2872 C  CA  . PRO   B 1 70  ? -3.497  36.988  19.893  1.00 70.89  ? 75  PRO   B CA  1 
ATOM   2873 C  C   . PRO   B 1 70  ? -3.336  38.502  19.784  1.00 74.52  ? 75  PRO   B C   1 
ATOM   2874 O  O   . PRO   B 1 70  ? -4.093  39.251  20.406  1.00 73.92  ? 75  PRO   B O   1 
ATOM   2875 C  CB  . PRO   B 1 70  ? -4.598  36.462  18.959  1.00 72.67  ? 75  PRO   B CB  1 
ATOM   2876 C  CG  . PRO   B 1 70  ? -5.422  35.519  19.791  1.00 77.04  ? 75  PRO   B CG  1 
ATOM   2877 C  CD  . PRO   B 1 70  ? -5.312  36.022  21.190  1.00 72.57  ? 75  PRO   B CD  1 
ATOM   2878 N  N   . VAL   B 1 71  ? -2.313  38.940  19.026  1.00 71.25  ? 76  VAL   B N   1 
ATOM   2879 C  CA  . VAL   B 1 71  ? -1.997  40.351  18.760  1.00 70.99  ? 76  VAL   B CA  1 
ATOM   2880 C  C   . VAL   B 1 71  ? -3.201  40.940  17.980  1.00 75.46  ? 76  VAL   B C   1 
ATOM   2881 O  O   . VAL   B 1 71  ? -3.656  40.294  17.031  1.00 74.67  ? 76  VAL   B O   1 
ATOM   2882 C  CB  . VAL   B 1 71  ? -0.644  40.491  17.994  1.00 74.61  ? 76  VAL   B CB  1 
ATOM   2883 C  CG1 . VAL   B 1 71  ? -0.316  41.950  17.686  1.00 74.55  ? 76  VAL   B CG1 1 
ATOM   2884 C  CG2 . VAL   B 1 71  ? 0.503   39.842  18.767  1.00 74.21  ? 76  VAL   B CG2 1 
ATOM   2885 N  N   . PRO   B 1 72  ? -3.780  42.100  18.404  1.00 72.95  ? 77  PRO   B N   1 
ATOM   2886 C  CA  . PRO   B 1 72  ? -4.979  42.625  17.717  1.00 72.53  ? 77  PRO   B CA  1 
ATOM   2887 C  C   . PRO   B 1 72  ? -4.790  43.029  16.251  1.00 75.03  ? 77  PRO   B C   1 
ATOM   2888 O  O   . PRO   B 1 72  ? -5.632  42.681  15.419  1.00 75.10  ? 77  PRO   B O   1 
ATOM   2889 C  CB  . PRO   B 1 72  ? -5.403  43.820  18.588  1.00 74.39  ? 77  PRO   B CB  1 
ATOM   2890 C  CG  . PRO   B 1 72  ? -4.705  43.625  19.894  1.00 78.99  ? 77  PRO   B CG  1 
ATOM   2891 C  CD  . PRO   B 1 72  ? -3.411  42.963  19.545  1.00 74.64  ? 77  PRO   B CD  1 
ATOM   2892 N  N   . LYS   B 1 73  ? -3.705  43.762  15.939  1.00 69.84  ? 78  LYS   B N   1 
ATOM   2893 C  CA  . LYS   B 1 73  ? -3.410  44.233  14.581  1.00 68.85  ? 78  LYS   B CA  1 
ATOM   2894 C  C   . LYS   B 1 73  ? -2.261  43.404  13.983  1.00 69.05  ? 78  LYS   B C   1 
ATOM   2895 O  O   . LYS   B 1 73  ? -1.214  43.943  13.602  1.00 68.90  ? 78  LYS   B O   1 
ATOM   2896 C  CB  . LYS   B 1 73  ? -3.100  45.747  14.595  1.00 71.98  ? 78  LYS   B CB  1 
ATOM   2897 C  CG  . LYS   B 1 73  ? -3.409  46.465  13.284  1.00 92.39  ? 78  LYS   B CG  1 
ATOM   2898 C  CD  . LYS   B 1 73  ? -3.238  47.979  13.427  1.00 106.16 ? 78  LYS   B CD  1 
ATOM   2899 C  CE  . LYS   B 1 73  ? -3.578  48.739  12.165  1.00 121.09 ? 78  LYS   B CE  1 
ATOM   2900 N  NZ  . LYS   B 1 73  ? -5.046  48.809  11.926  1.00 131.87 ? 78  LYS   B NZ  1 
ATOM   2901 N  N   . ASP   B 1 74  ? -2.466  42.074  13.923  1.00 62.11  ? 79  ASP   B N   1 
ATOM   2902 C  CA  . ASP   B 1 74  ? -1.473  41.136  13.404  1.00 60.07  ? 79  ASP   B CA  1 
ATOM   2903 C  C   . ASP   B 1 74  ? -1.626  40.940  11.899  1.00 62.29  ? 79  ASP   B C   1 
ATOM   2904 O  O   . ASP   B 1 74  ? -2.041  39.869  11.437  1.00 61.74  ? 79  ASP   B O   1 
ATOM   2905 C  CB  . ASP   B 1 74  ? -1.521  39.798  14.170  1.00 60.69  ? 79  ASP   B CB  1 
ATOM   2906 C  CG  . ASP   B 1 74  ? -0.279  38.932  14.028  1.00 57.53  ? 79  ASP   B CG  1 
ATOM   2907 O  OD1 . ASP   B 1 74  ? 0.658   39.336  13.299  1.00 54.45  ? 79  ASP   B OD1 1 
ATOM   2908 O  OD2 . ASP   B 1 74  ? -0.234  37.868  14.657  1.00 58.82  ? 79  ASP   B OD2 1 
ATOM   2909 N  N   . ASP   B 1 75  ? -1.284  41.988  11.132  1.00 57.69  ? 80  ASP   B N   1 
ATOM   2910 C  CA  . ASP   B 1 75  ? -1.370  41.957  9.673   1.00 57.32  ? 80  ASP   B CA  1 
ATOM   2911 C  C   . ASP   B 1 75  ? -0.400  40.954  9.060   1.00 58.29  ? 80  ASP   B C   1 
ATOM   2912 O  O   . ASP   B 1 75  ? 0.721   40.804  9.539   1.00 56.97  ? 80  ASP   B O   1 
ATOM   2913 C  CB  . ASP   B 1 75  ? -1.217  43.359  9.068   1.00 59.85  ? 80  ASP   B CB  1 
ATOM   2914 C  CG  . ASP   B 1 75  ? -2.546  44.080  8.971   1.00 76.70  ? 80  ASP   B CG  1 
ATOM   2915 O  OD1 . ASP   B 1 75  ? -3.353  43.723  8.078   1.00 78.98  ? 80  ASP   B OD1 1 
ATOM   2916 O  OD2 . ASP   B 1 75  ? -2.805  44.963  9.816   1.00 83.72  ? 80  ASP   B OD2 1 
ATOM   2917 N  N   . LEU   B 1 76  ? -0.854  40.241  8.024   1.00 53.77  ? 81  LEU   B N   1 
ATOM   2918 C  CA  . LEU   B 1 76  ? -0.044  39.221  7.363   1.00 53.24  ? 81  LEU   B CA  1 
ATOM   2919 C  C   . LEU   B 1 76  ? 1.204   39.805  6.679   1.00 54.08  ? 81  LEU   B C   1 
ATOM   2920 O  O   . LEU   B 1 76  ? 1.226   40.987  6.324   1.00 53.19  ? 81  LEU   B O   1 
ATOM   2921 C  CB  . LEU   B 1 76  ? -0.859  38.307  6.406   1.00 53.86  ? 81  LEU   B CB  1 
ATOM   2922 C  CG  . LEU   B 1 76  ? -1.967  38.881  5.515   1.00 59.27  ? 81  LEU   B CG  1 
ATOM   2923 C  CD1 . LEU   B 1 76  ? -2.221  37.958  4.359   1.00 59.40  ? 81  LEU   B CD1 1 
ATOM   2924 C  CD2 . LEU   B 1 76  ? -3.291  39.010  6.278   1.00 62.99  ? 81  LEU   B CD2 1 
ATOM   2925 N  N   . TYR   B 1 77  ? 2.273   38.995  6.597   1.00 47.80  ? 82  TYR   B N   1 
ATOM   2926 C  CA  . TYR   B 1 77  ? 3.538   39.393  5.985   1.00 46.60  ? 82  TYR   B CA  1 
ATOM   2927 C  C   . TYR   B 1 77  ? 3.533   38.973  4.518   1.00 47.21  ? 82  TYR   B C   1 
ATOM   2928 O  O   . TYR   B 1 77  ? 3.260   37.811  4.210   1.00 45.61  ? 82  TYR   B O   1 
ATOM   2929 C  CB  . TYR   B 1 77  ? 4.725   38.765  6.738   1.00 48.20  ? 82  TYR   B CB  1 
ATOM   2930 C  CG  . TYR   B 1 77  ? 6.090   39.192  6.245   1.00 50.59  ? 82  TYR   B CG  1 
ATOM   2931 C  CD1 . TYR   B 1 77  ? 6.707   40.337  6.743   1.00 52.47  ? 82  TYR   B CD1 1 
ATOM   2932 C  CD2 . TYR   B 1 77  ? 6.794   38.420  5.324   1.00 51.88  ? 82  TYR   B CD2 1 
ATOM   2933 C  CE1 . TYR   B 1 77  ? 7.975   40.723  6.310   1.00 53.82  ? 82  TYR   B CE1 1 
ATOM   2934 C  CE2 . TYR   B 1 77  ? 8.065   38.794  4.886   1.00 52.93  ? 82  TYR   B CE2 1 
ATOM   2935 C  CZ  . TYR   B 1 77  ? 8.651   39.948  5.381   1.00 62.01  ? 82  TYR   B CZ  1 
ATOM   2936 O  OH  . TYR   B 1 77  ? 9.906   40.324  4.959   1.00 66.42  ? 82  TYR   B OH  1 
ATOM   2937 N  N   . ASN   B 1 78  ? 3.810   39.935  3.615   1.00 43.10  ? 83  ASN   B N   1 
ATOM   2938 C  CA  . ASN   B 1 78  ? 3.871   39.754  2.157   1.00 42.60  ? 83  ASN   B CA  1 
ATOM   2939 C  C   . ASN   B 1 78  ? 2.612   39.091  1.586   1.00 43.41  ? 83  ASN   B C   1 
ATOM   2940 O  O   . ASN   B 1 78  ? 2.697   38.227  0.705   1.00 42.97  ? 83  ASN   B O   1 
ATOM   2941 C  CB  . ASN   B 1 78  ? 5.159   39.022  1.735   1.00 49.36  ? 83  ASN   B CB  1 
ATOM   2942 C  CG  . ASN   B 1 78  ? 6.302   39.968  1.456   1.00 88.32  ? 83  ASN   B CG  1 
ATOM   2943 O  OD1 . ASN   B 1 78  ? 6.957   40.486  2.370   1.00 84.94  ? 83  ASN   B OD1 1 
ATOM   2944 N  ND2 . ASN   B 1 78  ? 6.542   40.245  0.181   1.00 83.90  ? 83  ASN   B ND2 1 
ATOM   2945 N  N   . ASN   B 1 79  ? 1.434   39.498  2.117   1.00 37.67  ? 84  ASN   B N   1 
ATOM   2946 C  CA  . ASN   B 1 79  ? 0.124   38.991  1.716   1.00 37.08  ? 84  ASN   B CA  1 
ATOM   2947 C  C   . ASN   B 1 79  ? 0.014   37.462  1.748   1.00 41.20  ? 84  ASN   B C   1 
ATOM   2948 O  O   . ASN   B 1 79  ? -0.838  36.886  1.066   1.00 40.52  ? 84  ASN   B O   1 
ATOM   2949 C  CB  . ASN   B 1 79  ? -0.262  39.554  0.344   1.00 37.97  ? 84  ASN   B CB  1 
ATOM   2950 C  CG  . ASN   B 1 79  ? -0.592  41.023  0.395   1.00 53.83  ? 84  ASN   B CG  1 
ATOM   2951 O  OD1 . ASN   B 1 79  ? -0.032  41.831  -0.355  1.00 49.55  ? 84  ASN   B OD1 1 
ATOM   2952 N  ND2 . ASN   B 1 79  ? -1.505  41.394  1.288   1.00 42.56  ? 84  ASN   B ND2 1 
ATOM   2953 N  N   . LEU   B 1 80  ? 0.842   36.802  2.584   1.00 38.90  ? 85  LEU   B N   1 
ATOM   2954 C  CA  . LEU   B 1 80  ? 0.812   35.347  2.650   1.00 39.05  ? 85  LEU   B CA  1 
ATOM   2955 C  C   . LEU   B 1 80  ? 0.983   34.787  4.068   1.00 41.29  ? 85  LEU   B C   1 
ATOM   2956 O  O   . LEU   B 1 80  ? 0.122   34.011  4.486   1.00 41.42  ? 85  LEU   B O   1 
ATOM   2957 C  CB  . LEU   B 1 80  ? 1.836   34.746  1.671   1.00 39.73  ? 85  LEU   B CB  1 
ATOM   2958 C  CG  . LEU   B 1 80  ? 1.771   33.225  1.379   1.00 44.12  ? 85  LEU   B CG  1 
ATOM   2959 C  CD1 . LEU   B 1 80  ? 0.372   32.766  0.960   1.00 44.83  ? 85  LEU   B CD1 1 
ATOM   2960 C  CD2 . LEU   B 1 80  ? 2.772   32.854  0.331   1.00 44.46  ? 85  LEU   B CD2 1 
ATOM   2961 N  N   . ILE   B 1 81  ? 2.063   35.178  4.790   1.00 38.37  ? 86  ILE   B N   1 
ATOM   2962 C  CA  . ILE   B 1 81  ? 2.391   34.695  6.155   1.00 38.56  ? 86  ILE   B CA  1 
ATOM   2963 C  C   . ILE   B 1 81  ? 1.336   35.144  7.163   1.00 42.25  ? 86  ILE   B C   1 
ATOM   2964 O  O   . ILE   B 1 81  ? 1.306   36.318  7.544   1.00 40.46  ? 86  ILE   B O   1 
ATOM   2965 C  CB  . ILE   B 1 81  ? 3.815   35.097  6.638   1.00 42.48  ? 86  ILE   B CB  1 
ATOM   2966 C  CG1 . ILE   B 1 81  ? 4.902   34.981  5.523   1.00 43.25  ? 86  ILE   B CG1 1 
ATOM   2967 C  CG2 . ILE   B 1 81  ? 4.217   34.341  7.918   1.00 43.70  ? 86  ILE   B CG2 1 
ATOM   2968 C  CD1 . ILE   B 1 81  ? 5.137   33.641  4.942   1.00 44.91  ? 86  ILE   B CD1 1 
ATOM   2969 N  N   . VAL   B 1 82  ? 0.508   34.206  7.622   1.00 39.22  ? 87  VAL   B N   1 
ATOM   2970 C  CA  . VAL   B 1 82  ? -0.591  34.496  8.539   1.00 39.50  ? 87  VAL   B CA  1 
ATOM   2971 C  C   . VAL   B 1 82  ? -0.141  34.445  10.022  1.00 40.82  ? 87  VAL   B C   1 
ATOM   2972 O  O   . VAL   B 1 82  ? 0.684   33.607  10.407  1.00 37.99  ? 87  VAL   B O   1 
ATOM   2973 C  CB  . VAL   B 1 82  ? -1.839  33.615  8.231   1.00 44.88  ? 87  VAL   B CB  1 
ATOM   2974 C  CG1 . VAL   B 1 82  ? -1.588  32.128  8.487   1.00 44.90  ? 87  VAL   B CG1 1 
ATOM   2975 C  CG2 . VAL   B 1 82  ? -3.082  34.108  8.965   1.00 45.09  ? 87  VAL   B CG2 1 
ATOM   2976 N  N   . ASN   B 1 83  ? -0.677  35.386  10.831  1.00 37.46  ? 88  ASN   B N   1 
ATOM   2977 C  CA  . ASN   B 1 83  ? -0.434  35.538  12.276  1.00 36.41  ? 88  ASN   B CA  1 
ATOM   2978 C  C   . ASN   B 1 83  ? 1.062   35.603  12.654  1.00 41.05  ? 88  ASN   B C   1 
ATOM   2979 O  O   . ASN   B 1 83  ? 1.442   34.918  13.612  1.00 42.55  ? 88  ASN   B O   1 
ATOM   2980 C  CB  . ASN   B 1 83  ? -1.145  34.412  13.049  1.00 36.64  ? 88  ASN   B CB  1 
ATOM   2981 C  CG  . ASN   B 1 83  ? -2.602  34.216  12.683  1.00 51.76  ? 88  ASN   B CG  1 
ATOM   2982 O  OD1 . ASN   B 1 83  ? -3.397  35.160  12.659  1.00 48.31  ? 88  ASN   B OD1 1 
ATOM   2983 N  ND2 . ASN   B 1 83  ? -2.991  32.977  12.411  1.00 40.47  ? 88  ASN   B ND2 1 
ATOM   2984 N  N   . PRO   B 1 84  ? 1.942   36.386  11.969  1.00 35.97  ? 89  PRO   B N   1 
ATOM   2985 C  CA  . PRO   B 1 84  ? 3.370   36.342  12.326  1.00 35.46  ? 89  PRO   B CA  1 
ATOM   2986 C  C   . PRO   B 1 84  ? 3.731   36.901  13.708  1.00 39.17  ? 89  PRO   B C   1 
ATOM   2987 O  O   . PRO   B 1 84  ? 4.559   36.299  14.382  1.00 36.98  ? 89  PRO   B O   1 
ATOM   2988 C  CB  . PRO   B 1 84  ? 4.042   37.104  11.193  1.00 36.96  ? 89  PRO   B CB  1 
ATOM   2989 C  CG  . PRO   B 1 84  ? 2.992   38.057  10.726  1.00 41.54  ? 89  PRO   B CG  1 
ATOM   2990 C  CD  . PRO   B 1 84  ? 1.721   37.287  10.812  1.00 37.32  ? 89  PRO   B CD  1 
ATOM   2991 N  N   . ARG   B 1 85  ? 3.118   38.027  14.147  1.00 36.59  ? 90  ARG   B N   1 
ATOM   2992 C  CA  . ARG   B 1 85  ? 3.424   38.588  15.473  1.00 36.53  ? 90  ARG   B CA  1 
ATOM   2993 C  C   . ARG   B 1 85  ? 2.953   37.672  16.602  1.00 39.28  ? 90  ARG   B C   1 
ATOM   2994 O  O   . ARG   B 1 85  ? 3.672   37.527  17.584  1.00 39.57  ? 90  ARG   B O   1 
ATOM   2995 C  CB  . ARG   B 1 85  ? 2.836   40.002  15.653  1.00 38.13  ? 90  ARG   B CB  1 
ATOM   2996 C  CG  . ARG   B 1 85  ? 3.488   41.046  14.771  1.00 43.02  ? 90  ARG   B CG  1 
ATOM   2997 C  CD  . ARG   B 1 85  ? 2.577   42.242  14.559  1.00 47.73  ? 90  ARG   B CD  1 
ATOM   2998 N  NE  . ARG   B 1 85  ? 3.018   43.048  13.422  1.00 52.58  ? 90  ARG   B NE  1 
ATOM   2999 C  CZ  . ARG   B 1 85  ? 2.642   42.838  12.165  1.00 65.80  ? 90  ARG   B CZ  1 
ATOM   3000 N  NH1 . ARG   B 1 85  ? 1.813   41.844  11.869  1.00 51.51  ? 90  ARG   B NH1 1 
ATOM   3001 N  NH2 . ARG   B 1 85  ? 3.105   43.610  11.191  1.00 55.00  ? 90  ARG   B NH2 1 
ATOM   3002 N  N   . SER   B 1 86  ? 1.770   37.052  16.456  1.00 34.71  ? 91  SER   B N   1 
ATOM   3003 C  CA  . SER   B 1 86  ? 1.209   36.127  17.442  1.00 35.01  ? 91  SER   B CA  1 
ATOM   3004 C  C   . SER   B 1 86  ? 2.114   34.890  17.586  1.00 37.82  ? 91  SER   B C   1 
ATOM   3005 O  O   . SER   B 1 86  ? 2.420   34.502  18.716  1.00 37.92  ? 91  SER   B O   1 
ATOM   3006 C  CB  . SER   B 1 86  ? -0.185  35.674  17.030  1.00 39.13  ? 91  SER   B CB  1 
ATOM   3007 O  OG  . SER   B 1 86  ? -1.077  36.774  16.971  1.00 52.14  ? 91  SER   B OG  1 
ATOM   3008 N  N   . VAL   B 1 87  ? 2.545   34.294  16.443  1.00 33.13  ? 92  VAL   B N   1 
ATOM   3009 C  CA  . VAL   B 1 87  ? 3.410   33.110  16.457  1.00 32.17  ? 92  VAL   B CA  1 
ATOM   3010 C  C   . VAL   B 1 87  ? 4.785   33.464  17.025  1.00 36.61  ? 92  VAL   B C   1 
ATOM   3011 O  O   . VAL   B 1 87  ? 5.263   32.770  17.925  1.00 34.79  ? 92  VAL   B O   1 
ATOM   3012 C  CB  . VAL   B 1 87  ? 3.488   32.438  15.063  1.00 35.15  ? 92  VAL   B CB  1 
ATOM   3013 C  CG1 . VAL   B 1 87  ? 4.593   31.381  15.015  1.00 34.76  ? 92  VAL   B CG1 1 
ATOM   3014 C  CG2 . VAL   B 1 87  ? 2.137   31.841  14.675  1.00 34.68  ? 92  VAL   B CG2 1 
ATOM   3015 N  N   . GLY   B 1 88  ? 5.375   34.561  16.541  1.00 33.54  ? 93  GLY   B N   1 
ATOM   3016 C  CA  . GLY   B 1 88  ? 6.683   35.009  17.014  1.00 33.93  ? 93  GLY   B CA  1 
ATOM   3017 C  C   . GLY   B 1 88  ? 6.729   35.295  18.508  1.00 38.68  ? 93  GLY   B C   1 
ATOM   3018 O  O   . GLY   B 1 88  ? 7.658   34.857  19.203  1.00 37.57  ? 93  GLY   B O   1 
ATOM   3019 N  N   . LEU   B 1 89  ? 5.714   36.034  19.004  1.00 37.58  ? 94  LEU   B N   1 
ATOM   3020 C  CA  . LEU   B 1 89  ? 5.554   36.447  20.404  1.00 38.85  ? 94  LEU   B CA  1 
ATOM   3021 C  C   . LEU   B 1 89  ? 5.261   35.275  21.324  1.00 41.28  ? 94  LEU   B C   1 
ATOM   3022 O  O   . LEU   B 1 89  ? 5.842   35.218  22.411  1.00 40.33  ? 94  LEU   B O   1 
ATOM   3023 C  CB  . LEU   B 1 89  ? 4.447   37.528  20.544  1.00 40.37  ? 94  LEU   B CB  1 
ATOM   3024 C  CG  . LEU   B 1 89  ? 4.053   37.969  21.965  1.00 48.09  ? 94  LEU   B CG  1 
ATOM   3025 C  CD1 . LEU   B 1 89  ? 4.805   39.226  22.382  1.00 49.78  ? 94  LEU   B CD1 1 
ATOM   3026 C  CD2 . LEU   B 1 89  ? 2.545   38.192  22.072  1.00 52.71  ? 94  LEU   B CD2 1 
ATOM   3027 N  N   . ALA   B 1 90  ? 4.341   34.372  20.928  1.00 37.26  ? 95  ALA   B N   1 
ATOM   3028 C  CA  . ALA   B 1 90  ? 3.982   33.212  21.761  1.00 36.32  ? 95  ALA   B CA  1 
ATOM   3029 C  C   . ALA   B 1 90  ? 5.185   32.283  21.890  1.00 39.29  ? 95  ALA   B C   1 
ATOM   3030 O  O   . ALA   B 1 90  ? 5.419   31.726  22.965  1.00 37.34  ? 95  ALA   B O   1 
ATOM   3031 C  CB  . ALA   B 1 90  ? 2.794   32.471  21.173  1.00 36.64  ? 95  ALA   B CB  1 
ATOM   3032 N  N   . ASN   B 1 91  ? 5.980   32.178  20.810  1.00 36.34  ? 96  ASN   B N   1 
ATOM   3033 C  CA  . ASN   B 1 91  ? 7.207   31.391  20.807  1.00 35.89  ? 96  ASN   B CA  1 
ATOM   3034 C  C   . ASN   B 1 91  ? 8.267   32.034  21.684  1.00 37.87  ? 96  ASN   B C   1 
ATOM   3035 O  O   . ASN   B 1 91  ? 9.013   31.303  22.320  1.00 35.65  ? 96  ASN   B O   1 
ATOM   3036 C  CB  . ASN   B 1 91  ? 7.710   31.146  19.395  1.00 36.89  ? 96  ASN   B CB  1 
ATOM   3037 C  CG  . ASN   B 1 91  ? 7.108   29.895  18.827  1.00 41.51  ? 96  ASN   B CG  1 
ATOM   3038 O  OD1 . ASN   B 1 91  ? 7.212   28.825  19.430  1.00 33.12  ? 96  ASN   B OD1 1 
ATOM   3039 N  ND2 . ASN   B 1 91  ? 6.408   30.004  17.702  1.00 31.66  ? 96  ASN   B ND2 1 
ATOM   3040 N  N   . GLN   B 1 92  ? 8.286   33.398  21.792  1.00 33.27  ? 97  GLN   B N   1 
ATOM   3041 C  CA  . GLN   B 1 92  ? 9.238   34.081  22.673  1.00 33.44  ? 97  GLN   B CA  1 
ATOM   3042 C  C   . GLN   B 1 92  ? 8.939   33.754  24.132  1.00 36.82  ? 97  GLN   B C   1 
ATOM   3043 O  O   . GLN   B 1 92  ? 9.863   33.498  24.895  1.00 38.59  ? 97  GLN   B O   1 
ATOM   3044 C  CB  . GLN   B 1 92  ? 9.236   35.607  22.442  1.00 34.35  ? 97  GLN   B CB  1 
ATOM   3045 C  CG  . GLN   B 1 92  ? 10.408  36.294  23.152  1.00 42.40  ? 97  GLN   B CG  1 
ATOM   3046 C  CD  . GLN   B 1 92  ? 10.467  37.785  22.951  1.00 57.26  ? 97  GLN   B CD  1 
ATOM   3047 O  OE1 . GLN   B 1 92  ? 9.466   38.459  22.677  1.00 55.53  ? 97  GLN   B OE1 1 
ATOM   3048 N  NE2 . GLN   B 1 92  ? 11.652  38.330  23.116  1.00 44.95  ? 97  GLN   B NE2 1 
ATOM   3049 N  N   . GLU   B 1 93  ? 7.658   33.700  24.491  1.00 32.59  ? 98  GLU   B N   1 
ATOM   3050 C  CA  . GLU   B 1 93  ? 7.215   33.386  25.850  1.00 33.11  ? 98  GLU   B CA  1 
ATOM   3051 C  C   . GLU   B 1 93  ? 7.462   31.916  26.185  1.00 37.33  ? 98  GLU   B C   1 
ATOM   3052 O  O   . GLU   B 1 93  ? 7.940   31.609  27.275  1.00 37.41  ? 98  GLU   B O   1 
ATOM   3053 C  CB  . GLU   B 1 93  ? 5.737   33.738  26.044  1.00 34.55  ? 98  GLU   B CB  1 
ATOM   3054 C  CG  . GLU   B 1 93  ? 5.459   35.232  25.983  1.00 45.16  ? 98  GLU   B CG  1 
ATOM   3055 C  CD  . GLU   B 1 93  ? 6.172   36.057  27.041  1.00 66.22  ? 98  GLU   B CD  1 
ATOM   3056 O  OE1 . GLU   B 1 93  ? 5.888   35.859  28.244  1.00 66.73  ? 98  GLU   B OE1 1 
ATOM   3057 O  OE2 . GLU   B 1 93  ? 7.052   36.866  26.668  1.00 50.99  ? 98  GLU   B OE2 1 
ATOM   3058 N  N   . LEU   B 1 94  ? 7.190   31.020  25.215  1.00 32.84  ? 99  LEU   B N   1 
ATOM   3059 C  CA  . LEU   B 1 94  ? 7.408   29.594  25.380  1.00 31.48  ? 99  LEU   B CA  1 
ATOM   3060 C  C   . LEU   B 1 94  ? 8.892   29.306  25.561  1.00 34.01  ? 99  LEU   B C   1 
ATOM   3061 O  O   . LEU   B 1 94  ? 9.236   28.494  26.432  1.00 33.59  ? 99  LEU   B O   1 
ATOM   3062 C  CB  . LEU   B 1 94  ? 6.788   28.817  24.193  1.00 30.62  ? 99  LEU   B CB  1 
ATOM   3063 C  CG  . LEU   B 1 94  ? 7.033   27.288  24.120  1.00 32.29  ? 99  LEU   B CG  1 
ATOM   3064 C  CD1 . LEU   B 1 94  ? 6.614   26.561  25.418  1.00 31.32  ? 99  LEU   B CD1 1 
ATOM   3065 C  CD2 . LEU   B 1 94  ? 6.323   26.714  22.937  1.00 32.63  ? 99  LEU   B CD2 1 
ATOM   3066 N  N   . ALA   B 1 95  ? 9.774   30.011  24.797  1.00 30.48  ? 100 ALA   B N   1 
ATOM   3067 C  CA  . ALA   B 1 95  ? 11.225  29.861  24.900  1.00 30.84  ? 100 ALA   B CA  1 
ATOM   3068 C  C   . ALA   B 1 95  ? 11.714  30.154  26.322  1.00 37.52  ? 100 ALA   B C   1 
ATOM   3069 O  O   . ALA   B 1 95  ? 12.649  29.502  26.793  1.00 35.65  ? 100 ALA   B O   1 
ATOM   3070 C  CB  . ALA   B 1 95  ? 11.937  30.769  23.909  1.00 31.57  ? 100 ALA   B CB  1 
ATOM   3071 N  N   . GLU   B 1 96  ? 11.092  31.150  26.987  1.00 35.93  ? 101 GLU   B N   1 
ATOM   3072 C  CA  . GLU   B 1 96  ? 11.430  31.525  28.363  1.00 37.02  ? 101 GLU   B CA  1 
ATOM   3073 C  C   . GLU   B 1 96  ? 11.142  30.401  29.346  1.00 40.91  ? 101 GLU   B C   1 
ATOM   3074 O  O   . GLU   B 1 96  ? 12.015  30.062  30.143  1.00 40.81  ? 101 GLU   B O   1 
ATOM   3075 C  CB  . GLU   B 1 96  ? 10.713  32.830  28.776  1.00 38.94  ? 101 GLU   B CB  1 
ATOM   3076 C  CG  . GLU   B 1 96  ? 11.554  34.068  28.515  1.00 52.27  ? 101 GLU   B CG  1 
ATOM   3077 C  CD  . GLU   B 1 96  ? 12.845  34.154  29.309  1.00 65.99  ? 101 GLU   B CD  1 
ATOM   3078 O  OE1 . GLU   B 1 96  ? 13.874  34.558  28.722  1.00 56.07  ? 101 GLU   B OE1 1 
ATOM   3079 O  OE2 . GLU   B 1 96  ? 12.837  33.782  30.505  1.00 64.35  ? 101 GLU   B OE2 1 
ATOM   3080 N  N   . VAL   B 1 97  ? 9.938   29.805  29.264  1.00 37.65  ? 102 VAL   B N   1 
ATOM   3081 C  CA  . VAL   B 1 97  ? 9.505   28.689  30.106  1.00 36.89  ? 102 VAL   B CA  1 
ATOM   3082 C  C   . VAL   B 1 97  ? 10.443  27.464  29.906  1.00 38.06  ? 102 VAL   B C   1 
ATOM   3083 O  O   . VAL   B 1 97  ? 10.899  26.879  30.894  1.00 36.86  ? 102 VAL   B O   1 
ATOM   3084 C  CB  . VAL   B 1 97  ? 8.009   28.355  29.886  1.00 40.89  ? 102 VAL   B CB  1 
ATOM   3085 C  CG1 . VAL   B 1 97  ? 7.523   27.309  30.884  1.00 40.55  ? 102 VAL   B CG1 1 
ATOM   3086 C  CG2 . VAL   B 1 97  ? 7.143   29.613  29.980  1.00 41.04  ? 102 VAL   B CG2 1 
ATOM   3087 N  N   . VAL   B 1 98  ? 10.775  27.124  28.631  1.00 32.61  ? 103 VAL   B N   1 
ATOM   3088 C  CA  . VAL   B 1 98  ? 11.649  25.986  28.312  1.00 29.82  ? 103 VAL   B CA  1 
ATOM   3089 C  C   . VAL   B 1 98  ? 13.051  26.182  28.880  1.00 34.15  ? 103 VAL   B C   1 
ATOM   3090 O  O   . VAL   B 1 98  ? 13.565  25.272  29.534  1.00 31.80  ? 103 VAL   B O   1 
ATOM   3091 C  CB  . VAL   B 1 98  ? 11.663  25.654  26.786  1.00 31.57  ? 103 VAL   B CB  1 
ATOM   3092 C  CG1 . VAL   B 1 98  ? 12.695  24.574  26.447  1.00 31.07  ? 103 VAL   B CG1 1 
ATOM   3093 C  CG2 . VAL   B 1 98  ? 10.272  25.252  26.304  1.00 30.77  ? 103 VAL   B CG2 1 
ATOM   3094 N  N   . SER   B 1 99  ? 13.667  27.366  28.643  1.00 32.34  ? 104 SER   B N   1 
ATOM   3095 C  CA  . SER   B 1 99  ? 15.012  27.691  29.135  1.00 33.07  ? 104 SER   B CA  1 
ATOM   3096 C  C   . SER   B 1 99  ? 15.092  27.521  30.663  1.00 36.92  ? 104 SER   B C   1 
ATOM   3097 O  O   . SER   B 1 99  ? 16.043  26.921  31.148  1.00 36.77  ? 104 SER   B O   1 
ATOM   3098 C  CB  . SER   B 1 99  ? 15.391  29.122  28.754  1.00 37.92  ? 104 SER   B CB  1 
ATOM   3099 O  OG  . SER   B 1 99  ? 16.745  29.362  29.108  1.00 46.13  ? 104 SER   B OG  1 
ATOM   3100 N  N   . ARG   B 1 100 ? 14.060  27.983  31.386  1.00 34.79  ? 105 ARG   B N   1 
ATOM   3101 C  CA  . ARG   B 1 100 ? 13.915  27.910  32.846  1.00 36.50  ? 105 ARG   B CA  1 
ATOM   3102 C  C   . ARG   B 1 100 ? 13.832  26.453  33.329  1.00 41.08  ? 105 ARG   B C   1 
ATOM   3103 O  O   . ARG   B 1 100 ? 14.613  26.060  34.200  1.00 41.70  ? 105 ARG   B O   1 
ATOM   3104 C  CB  . ARG   B 1 100 ? 12.663  28.682  33.281  1.00 39.73  ? 105 ARG   B CB  1 
ATOM   3105 C  CG  . ARG   B 1 100 ? 12.678  29.211  34.715  1.00 60.98  ? 105 ARG   B CG  1 
ATOM   3106 C  CD  . ARG   B 1 100 ? 12.034  30.598  34.848  1.00 76.61  ? 105 ARG   B CD  1 
ATOM   3107 N  NE  . ARG   B 1 100 ? 10.723  30.700  34.194  1.00 86.52  ? 105 ARG   B NE  1 
ATOM   3108 C  CZ  . ARG   B 1 100 ? 10.516  31.263  33.005  1.00 100.11 ? 105 ARG   B CZ  1 
ATOM   3109 N  NH1 . ARG   B 1 100 ? 11.531  31.779  32.319  1.00 90.13  ? 105 ARG   B NH1 1 
ATOM   3110 N  NH2 . ARG   B 1 100 ? 9.298   31.295  32.483  1.00 81.03  ? 105 ARG   B NH2 1 
ATOM   3111 N  N   . ALA   B 1 101 ? 12.924  25.649  32.728  1.00 35.94  ? 106 ALA   B N   1 
ATOM   3112 C  CA  . ALA   B 1 101 ? 12.739  24.232  33.059  1.00 34.80  ? 106 ALA   B CA  1 
ATOM   3113 C  C   . ALA   B 1 101 ? 14.046  23.448  32.849  1.00 35.39  ? 106 ALA   B C   1 
ATOM   3114 O  O   . ALA   B 1 101 ? 14.455  22.692  33.736  1.00 33.57  ? 106 ALA   B O   1 
ATOM   3115 C  CB  . ALA   B 1 101 ? 11.612  23.639  32.220  1.00 35.61  ? 106 ALA   B CB  1 
ATOM   3116 N  N   . VAL   B 1 102 ? 14.710  23.654  31.696  1.00 30.29  ? 107 VAL   B N   1 
ATOM   3117 C  CA  . VAL   B 1 102 ? 15.980  22.984  31.376  1.00 31.15  ? 107 VAL   B CA  1 
ATOM   3118 C  C   . VAL   B 1 102 ? 17.094  23.455  32.339  1.00 36.90  ? 107 VAL   B C   1 
ATOM   3119 O  O   . VAL   B 1 102 ? 17.865  22.629  32.843  1.00 35.04  ? 107 VAL   B O   1 
ATOM   3120 C  CB  . VAL   B 1 102 ? 16.321  23.147  29.864  1.00 35.20  ? 107 VAL   B CB  1 
ATOM   3121 C  CG1 . VAL   B 1 102 ? 17.715  22.616  29.530  1.00 35.48  ? 107 VAL   B CG1 1 
ATOM   3122 C  CG2 . VAL   B 1 102 ? 15.272  22.436  29.009  1.00 34.75  ? 107 VAL   B CG2 1 
ATOM   3123 N  N   . SER   B 1 103 ? 17.119  24.771  32.643  1.00 35.15  ? 108 SER   B N   1 
ATOM   3124 C  CA  . SER   B 1 103 ? 18.093  25.370  33.568  1.00 36.47  ? 108 SER   B CA  1 
ATOM   3125 C  C   . SER   B 1 103 ? 17.983  24.756  34.963  1.00 38.81  ? 108 SER   B C   1 
ATOM   3126 O  O   . SER   B 1 103 ? 19.007  24.543  35.615  1.00 39.36  ? 108 SER   B O   1 
ATOM   3127 C  CB  . SER   B 1 103 ? 17.899  26.882  33.656  1.00 40.87  ? 108 SER   B CB  1 
ATOM   3128 O  OG  . SER   B 1 103 ? 19.033  27.488  34.253  1.00 55.93  ? 108 SER   B OG  1 
ATOM   3129 N  N   . ASP   B 1 104 ? 16.738  24.455  35.406  1.00 35.65  ? 109 ASP   B N   1 
ATOM   3130 C  CA  . ASP   B 1 104 ? 16.427  23.836  36.694  1.00 35.68  ? 109 ASP   B CA  1 
ATOM   3131 C  C   . ASP   B 1 104 ? 16.675  22.303  36.711  1.00 39.51  ? 109 ASP   B C   1 
ATOM   3132 O  O   . ASP   B 1 104 ? 16.463  21.671  37.742  1.00 40.30  ? 109 ASP   B O   1 
ATOM   3133 C  CB  . ASP   B 1 104 ? 14.971  24.153  37.110  1.00 38.15  ? 109 ASP   B CB  1 
ATOM   3134 C  CG  . ASP   B 1 104 ? 14.673  25.584  37.533  1.00 56.86  ? 109 ASP   B CG  1 
ATOM   3135 O  OD1 . ASP   B 1 104 ? 15.611  26.421  37.527  1.00 59.24  ? 109 ASP   B OD1 1 
ATOM   3136 O  OD2 . ASP   B 1 104 ? 13.504  25.866  37.886  1.00 65.36  ? 109 ASP   B OD2 1 
ATOM   3137 N  N   . GLY   B 1 105 ? 17.126  21.736  35.591  1.00 35.29  ? 110 GLY   B N   1 
ATOM   3138 C  CA  . GLY   B 1 105 ? 17.441  20.316  35.469  1.00 34.96  ? 110 GLY   B CA  1 
ATOM   3139 C  C   . GLY   B 1 105 ? 16.325  19.386  35.017  1.00 37.12  ? 110 GLY   B C   1 
ATOM   3140 O  O   . GLY   B 1 105 ? 16.442  18.172  35.193  1.00 36.23  ? 110 GLY   B O   1 
ATOM   3141 N  N   . TYR   B 1 106 ? 15.238  19.920  34.442  1.00 32.35  ? 111 TYR   B N   1 
ATOM   3142 C  CA  . TYR   B 1 106 ? 14.130  19.078  33.974  1.00 30.41  ? 111 TYR   B CA  1 
ATOM   3143 C  C   . TYR   B 1 106 ? 14.248  18.798  32.491  1.00 31.43  ? 111 TYR   B C   1 
ATOM   3144 O  O   . TYR   B 1 106 ? 14.626  19.680  31.730  1.00 30.52  ? 111 TYR   B O   1 
ATOM   3145 C  CB  . TYR   B 1 106 ? 12.776  19.770  34.174  1.00 31.12  ? 111 TYR   B CB  1 
ATOM   3146 C  CG  . TYR   B 1 106 ? 12.346  19.914  35.612  1.00 33.77  ? 111 TYR   B CG  1 
ATOM   3147 C  CD1 . TYR   B 1 106 ? 11.686  18.879  36.270  1.00 35.36  ? 111 TYR   B CD1 1 
ATOM   3148 C  CD2 . TYR   B 1 106 ? 12.611  21.080  36.324  1.00 35.91  ? 111 TYR   B CD2 1 
ATOM   3149 C  CE1 . TYR   B 1 106 ? 11.319  18.993  37.609  1.00 34.33  ? 111 TYR   B CE1 1 
ATOM   3150 C  CE2 . TYR   B 1 106 ? 12.258  21.202  37.668  1.00 37.22  ? 111 TYR   B CE2 1 
ATOM   3151 C  CZ  . TYR   B 1 106 ? 11.594  20.164  38.300  1.00 43.03  ? 111 TYR   B CZ  1 
ATOM   3152 O  OH  . TYR   B 1 106 ? 11.226  20.284  39.621  1.00 42.70  ? 111 TYR   B OH  1 
ATOM   3153 N  N   . SER   B 1 107 ? 13.877  17.571  32.085  1.00 28.42  ? 112 SER   B N   1 
ATOM   3154 C  CA  . SER   B 1 107 ? 13.716  17.209  30.680  1.00 26.40  ? 112 SER   B CA  1 
ATOM   3155 C  C   . SER   B 1 107 ? 12.345  17.824  30.348  1.00 28.52  ? 112 SER   B C   1 
ATOM   3156 O  O   . SER   B 1 107 ? 11.362  17.540  31.026  1.00 28.06  ? 112 SER   B O   1 
ATOM   3157 C  CB  . SER   B 1 107 ? 13.695  15.691  30.503  1.00 29.52  ? 112 SER   B CB  1 
ATOM   3158 O  OG  . SER   B 1 107 ? 15.015  15.176  30.594  1.00 38.82  ? 112 SER   B OG  1 
ATOM   3159 N  N   . CYS   B 1 108 ? 12.311  18.752  29.389  1.00 27.26  ? 113 CYS   B N   1 
ATOM   3160 C  CA  . CYS   B 1 108 ? 11.121  19.545  29.125  1.00 28.58  ? 113 CYS   B CA  1 
ATOM   3161 C  C   . CYS   B 1 108 ? 10.201  18.983  28.043  1.00 29.71  ? 113 CYS   B C   1 
ATOM   3162 O  O   . CYS   B 1 108 ? 10.557  19.010  26.864  1.00 28.54  ? 113 CYS   B O   1 
ATOM   3163 C  CB  . CYS   B 1 108 ? 11.532  20.982  28.817  1.00 30.26  ? 113 CYS   B CB  1 
ATOM   3164 S  SG  . CYS   B 1 108 ? 10.167  22.162  28.875  1.00 35.09  ? 113 CYS   B SG  1 
ATOM   3165 N  N   . VAL   B 1 109 ? 8.994   18.545  28.449  1.00 25.02  ? 114 VAL   B N   1 
ATOM   3166 C  CA  . VAL   B 1 109 ? 7.981   18.016  27.547  1.00 25.15  ? 114 VAL   B CA  1 
ATOM   3167 C  C   . VAL   B 1 109 ? 6.990   19.134  27.196  1.00 28.82  ? 114 VAL   B C   1 
ATOM   3168 O  O   . VAL   B 1 109 ? 6.324   19.654  28.098  1.00 28.50  ? 114 VAL   B O   1 
ATOM   3169 C  CB  . VAL   B 1 109 ? 7.249   16.789  28.149  1.00 27.83  ? 114 VAL   B CB  1 
ATOM   3170 C  CG1 . VAL   B 1 109 ? 6.030   16.402  27.304  1.00 28.14  ? 114 VAL   B CG1 1 
ATOM   3171 C  CG2 . VAL   B 1 109 ? 8.196   15.604  28.308  1.00 26.79  ? 114 VAL   B CG2 1 
ATOM   3172 N  N   . THR   B 1 110 ? 6.877   19.480  25.903  1.00 24.85  ? 115 THR   B N   1 
ATOM   3173 C  CA  . THR   B 1 110 ? 5.896   20.468  25.481  1.00 25.30  ? 115 THR   B CA  1 
ATOM   3174 C  C   . THR   B 1 110 ? 4.814   19.786  24.665  1.00 28.45  ? 115 THR   B C   1 
ATOM   3175 O  O   . THR   B 1 110 ? 5.119   19.108  23.669  1.00 27.78  ? 115 THR   B O   1 
ATOM   3176 C  CB  . THR   B 1 110 ? 6.538   21.644  24.716  1.00 31.52  ? 115 THR   B CB  1 
ATOM   3177 O  OG1 . THR   B 1 110 ? 7.592   22.228  25.492  1.00 29.68  ? 115 THR   B OG1 1 
ATOM   3178 C  CG2 . THR   B 1 110 ? 5.513   22.720  24.336  1.00 30.34  ? 115 THR   B CG2 1 
ATOM   3179 N  N   . LEU   B 1 111 ? 3.544   20.003  25.049  1.00 25.05  ? 116 LEU   B N   1 
ATOM   3180 C  CA  . LEU   B 1 111 ? 2.416   19.426  24.320  1.00 24.41  ? 116 LEU   B CA  1 
ATOM   3181 C  C   . LEU   B 1 111 ? 1.825   20.467  23.398  1.00 28.83  ? 116 LEU   B C   1 
ATOM   3182 O  O   . LEU   B 1 111 ? 1.507   21.582  23.834  1.00 28.94  ? 116 LEU   B O   1 
ATOM   3183 C  CB  . LEU   B 1 111 ? 1.313   18.916  25.276  1.00 24.22  ? 116 LEU   B CB  1 
ATOM   3184 C  CG  . LEU   B 1 111 ? 1.766   18.104  26.489  1.00 28.26  ? 116 LEU   B CG  1 
ATOM   3185 C  CD1 . LEU   B 1 111 ? 0.574   17.768  27.386  1.00 26.91  ? 116 LEU   B CD1 1 
ATOM   3186 C  CD2 . LEU   B 1 111 ? 2.478   16.838  26.062  1.00 27.80  ? 116 LEU   B CD2 1 
ATOM   3187 N  N   . GLY   B 1 112 ? 1.684   20.109  22.132  1.00 26.01  ? 117 GLY   B N   1 
ATOM   3188 C  CA  . GLY   B 1 112 ? 1.075   20.995  21.159  1.00 25.71  ? 117 GLY   B CA  1 
ATOM   3189 C  C   . GLY   B 1 112 ? -0.398  20.711  20.932  1.00 27.37  ? 117 GLY   B C   1 
ATOM   3190 O  O   . GLY   B 1 112 ? -0.917  19.723  21.445  1.00 26.75  ? 117 GLY   B O   1 
ATOM   3191 N  N   . GLY   B 1 113 ? -1.088  21.559  20.159  1.00 27.13  ? 118 GLY   B N   1 
ATOM   3192 C  CA  . GLY   B 1 113 ? -0.516  22.727  19.500  1.00 26.78  ? 118 GLY   B CA  1 
ATOM   3193 C  C   . GLY   B 1 113 ? 0.176   22.384  18.193  1.00 29.77  ? 118 GLY   B C   1 
ATOM   3194 O  O   . GLY   B 1 113 ? 0.648   21.245  18.004  1.00 26.53  ? 118 GLY   B O   1 
ATOM   3195 N  N   . ASP   B 1 114 ? 0.202   23.354  17.263  1.00 26.94  ? 119 ASP   B N   1 
ATOM   3196 C  CA  . ASP   B 1 114 ? 0.821   23.120  15.966  1.00 26.29  ? 119 ASP   B CA  1 
ATOM   3197 C  C   . ASP   B 1 114 ? 2.355   23.175  16.052  1.00 27.78  ? 119 ASP   B C   1 
ATOM   3198 O  O   . ASP   B 1 114 ? 2.903   23.673  17.041  1.00 27.05  ? 119 ASP   B O   1 
ATOM   3199 C  CB  . ASP   B 1 114 ? 0.235   24.035  14.883  1.00 28.89  ? 119 ASP   B CB  1 
ATOM   3200 C  CG  . ASP   B 1 114 ? 0.663   25.471  15.025  1.00 33.72  ? 119 ASP   B CG  1 
ATOM   3201 O  OD1 . ASP   B 1 114 ? 1.869   25.741  14.883  1.00 29.26  ? 119 ASP   B OD1 1 
ATOM   3202 O  OD2 . ASP   B 1 114 ? -0.198  26.317  15.330  1.00 40.24  ? 119 ASP   B OD2 1 
ATOM   3203 N  N   . HIS   B 1 115 ? 3.049   22.640  15.012  1.00 24.66  ? 120 HIS   B N   1 
ATOM   3204 C  CA  . HIS   B 1 115 ? 4.507   22.514  15.014  1.00 23.79  ? 120 HIS   B CA  1 
ATOM   3205 C  C   . HIS   B 1 115 ? 5.274   23.849  14.993  1.00 27.61  ? 120 HIS   B C   1 
ATOM   3206 O  O   . HIS   B 1 115 ? 6.490   23.835  15.246  1.00 27.58  ? 120 HIS   B O   1 
ATOM   3207 C  CB  . HIS   B 1 115 ? 4.998   21.558  13.903  1.00 24.07  ? 120 HIS   B CB  1 
ATOM   3208 C  CG  . HIS   B 1 115 ? 6.146   20.694  14.361  1.00 25.01  ? 120 HIS   B CG  1 
ATOM   3209 N  ND1 . HIS   B 1 115 ? 6.398   19.471  13.755  1.00 25.66  ? 120 HIS   B ND1 1 
ATOM   3210 C  CD2 . HIS   B 1 115 ? 7.017   20.858  15.396  1.00 25.48  ? 120 HIS   B CD2 1 
ATOM   3211 C  CE1 . HIS   B 1 115 ? 7.425   18.947  14.404  1.00 24.24  ? 120 HIS   B CE1 1 
ATOM   3212 N  NE2 . HIS   B 1 115 ? 7.815   19.729  15.428  1.00 24.35  ? 120 HIS   B NE2 1 
ATOM   3213 N  N   . SER   B 1 116 ? 4.602   25.019  14.776  1.00 25.58  ? 121 SER   B N   1 
ATOM   3214 C  CA  . SER   B 1 116 ? 5.354   26.293  14.864  1.00 26.31  ? 121 SER   B CA  1 
ATOM   3215 C  C   . SER   B 1 116 ? 5.928   26.497  16.280  1.00 28.22  ? 121 SER   B C   1 
ATOM   3216 O  O   . SER   B 1 116 ? 6.897   27.256  16.428  1.00 28.86  ? 121 SER   B O   1 
ATOM   3217 C  CB  . SER   B 1 116 ? 4.485   27.501  14.479  1.00 29.74  ? 121 SER   B CB  1 
ATOM   3218 O  OG  . SER   B 1 116 ? 3.466   27.728  15.440  1.00 31.35  ? 121 SER   B OG  1 
ATOM   3219 N  N   . LEU   B 1 117 ? 5.373   25.783  17.311  1.00 24.83  ? 122 LEU   B N   1 
ATOM   3220 C  CA  . LEU   B 1 117 ? 5.871   25.877  18.696  1.00 24.72  ? 122 LEU   B CA  1 
ATOM   3221 C  C   . LEU   B 1 117 ? 7.354   25.434  18.853  1.00 28.62  ? 122 LEU   B C   1 
ATOM   3222 O  O   . LEU   B 1 117 ? 7.996   25.789  19.848  1.00 27.42  ? 122 LEU   B O   1 
ATOM   3223 C  CB  . LEU   B 1 117 ? 4.966   25.169  19.716  1.00 26.09  ? 122 LEU   B CB  1 
ATOM   3224 C  CG  . LEU   B 1 117 ? 4.860   23.642  19.683  1.00 29.96  ? 122 LEU   B CG  1 
ATOM   3225 C  CD1 . LEU   B 1 117 ? 5.964   22.974  20.527  1.00 31.82  ? 122 LEU   B CD1 1 
ATOM   3226 C  CD2 . LEU   B 1 117 ? 3.536   23.209  20.230  1.00 32.00  ? 122 LEU   B CD2 1 
ATOM   3227 N  N   . ALA   B 1 118 ? 7.876   24.627  17.897  1.00 25.76  ? 123 ALA   B N   1 
ATOM   3228 C  CA  . ALA   B 1 118 ? 9.286   24.197  17.940  1.00 26.24  ? 123 ALA   B CA  1 
ATOM   3229 C  C   . ALA   B 1 118 ? 10.241  25.372  17.843  1.00 29.25  ? 123 ALA   B C   1 
ATOM   3230 O  O   . ALA   B 1 118 ? 11.387  25.243  18.258  1.00 28.56  ? 123 ALA   B O   1 
ATOM   3231 C  CB  . ALA   B 1 118 ? 9.582   23.210  16.838  1.00 26.84  ? 123 ALA   B CB  1 
ATOM   3232 N  N   . ILE   B 1 119 ? 9.812   26.497  17.238  1.00 26.79  ? 124 ILE   B N   1 
ATOM   3233 C  CA  . ILE   B 1 119 ? 10.654  27.694  17.166  1.00 25.50  ? 124 ILE   B CA  1 
ATOM   3234 C  C   . ILE   B 1 119 ? 10.991  28.110  18.621  1.00 28.50  ? 124 ILE   B C   1 
ATOM   3235 O  O   . ILE   B 1 119 ? 12.154  28.321  18.928  1.00 28.86  ? 124 ILE   B O   1 
ATOM   3236 C  CB  . ILE   B 1 119 ? 9.926   28.840  16.419  1.00 27.42  ? 124 ILE   B CB  1 
ATOM   3237 C  CG1 . ILE   B 1 119 ? 9.654   28.495  14.934  1.00 27.49  ? 124 ILE   B CG1 1 
ATOM   3238 C  CG2 . ILE   B 1 119 ? 10.733  30.162  16.549  1.00 28.14  ? 124 ILE   B CG2 1 
ATOM   3239 C  CD1 . ILE   B 1 119 ? 8.528   29.372  14.220  1.00 31.38  ? 124 ILE   B CD1 1 
ATOM   3240 N  N   . GLY   B 1 120 ? 9.977   28.181  19.487  1.00 27.14  ? 125 GLY   B N   1 
ATOM   3241 C  CA  . GLY   B 1 120 ? 10.177  28.538  20.889  1.00 27.44  ? 125 GLY   B CA  1 
ATOM   3242 C  C   . GLY   B 1 120 ? 10.845  27.467  21.727  1.00 29.81  ? 125 GLY   B C   1 
ATOM   3243 O  O   . GLY   B 1 120 ? 11.779  27.768  22.467  1.00 29.42  ? 125 GLY   B O   1 
ATOM   3244 N  N   . THR   B 1 121 ? 10.416  26.196  21.595  1.00 26.84  ? 126 THR   B N   1 
ATOM   3245 C  CA  . THR   B 1 121 ? 11.033  25.134  22.420  1.00 24.80  ? 126 THR   B CA  1 
ATOM   3246 C  C   . THR   B 1 121 ? 12.510  24.931  22.101  1.00 27.64  ? 126 THR   B C   1 
ATOM   3247 O  O   . THR   B 1 121 ? 13.318  24.810  23.030  1.00 28.36  ? 126 THR   B O   1 
ATOM   3248 C  CB  . THR   B 1 121 ? 10.259  23.824  22.375  1.00 28.00  ? 126 THR   B CB  1 
ATOM   3249 O  OG1 . THR   B 1 121 ? 10.385  23.251  21.070  1.00 27.17  ? 126 THR   B OG1 1 
ATOM   3250 C  CG2 . THR   B 1 121 ? 8.789   23.998  22.762  1.00 27.39  ? 126 THR   B CG2 1 
ATOM   3251 N  N   . ILE   B 1 122 ? 12.870  24.893  20.799  1.00 25.67  ? 127 ILE   B N   1 
ATOM   3252 C  CA  . ILE   B 1 122 ? 14.271  24.688  20.401  1.00 24.69  ? 127 ILE   B CA  1 
ATOM   3253 C  C   . ILE   B 1 122 ? 15.111  25.917  20.783  1.00 29.28  ? 127 ILE   B C   1 
ATOM   3254 O  O   . ILE   B 1 122 ? 16.196  25.749  21.339  1.00 28.85  ? 127 ILE   B O   1 
ATOM   3255 C  CB  . ILE   B 1 122 ? 14.422  24.238  18.910  1.00 26.62  ? 127 ILE   B CB  1 
ATOM   3256 C  CG1 . ILE   B 1 122 ? 13.776  22.844  18.734  1.00 26.60  ? 127 ILE   B CG1 1 
ATOM   3257 C  CG2 . ILE   B 1 122 ? 15.894  24.187  18.474  1.00 26.94  ? 127 ILE   B CG2 1 
ATOM   3258 C  CD1 . ILE   B 1 122 ? 13.675  22.315  17.283  1.00 27.26  ? 127 ILE   B CD1 1 
ATOM   3259 N  N   . SER   B 1 123 ? 14.603  27.136  20.518  1.00 28.61  ? 128 SER   B N   1 
ATOM   3260 C  CA  . SER   B 1 123 ? 15.330  28.372  20.888  1.00 28.75  ? 128 SER   B CA  1 
ATOM   3261 C  C   . SER   B 1 123 ? 15.597  28.426  22.406  1.00 32.07  ? 128 SER   B C   1 
ATOM   3262 O  O   . SER   B 1 123 ? 16.724  28.700  22.810  1.00 33.04  ? 128 SER   B O   1 
ATOM   3263 C  CB  . SER   B 1 123 ? 14.551  29.613  20.461  1.00 30.45  ? 128 SER   B CB  1 
ATOM   3264 O  OG  . SER   B 1 123 ? 14.460  29.687  19.049  1.00 39.58  ? 128 SER   B OG  1 
ATOM   3265 N  N   . GLY   B 1 124 ? 14.573  28.120  23.210  1.00 28.99  ? 129 GLY   B N   1 
ATOM   3266 C  CA  . GLY   B 1 124 ? 14.638  28.095  24.672  1.00 29.57  ? 129 GLY   B CA  1 
ATOM   3267 C  C   . GLY   B 1 124 ? 15.634  27.085  25.202  1.00 33.73  ? 129 GLY   B C   1 
ATOM   3268 O  O   . GLY   B 1 124 ? 16.459  27.384  26.063  1.00 33.22  ? 129 GLY   B O   1 
ATOM   3269 N  N   . HIS   B 1 125 ? 15.583  25.886  24.644  1.00 28.54  ? 130 HIS   B N   1 
ATOM   3270 C  CA  . HIS   B 1 125 ? 16.461  24.787  24.993  1.00 27.01  ? 130 HIS   B CA  1 
ATOM   3271 C  C   . HIS   B 1 125 ? 17.931  25.153  24.710  1.00 31.66  ? 130 HIS   B C   1 
ATOM   3272 O  O   . HIS   B 1 125 ? 18.790  24.894  25.561  1.00 31.49  ? 130 HIS   B O   1 
ATOM   3273 C  CB  . HIS   B 1 125 ? 16.044  23.560  24.152  1.00 26.36  ? 130 HIS   B CB  1 
ATOM   3274 C  CG  . HIS   B 1 125 ? 16.627  22.253  24.593  1.00 29.10  ? 130 HIS   B CG  1 
ATOM   3275 N  ND1 . HIS   B 1 125 ? 16.332  21.088  23.917  1.00 28.94  ? 130 HIS   B ND1 1 
ATOM   3276 C  CD2 . HIS   B 1 125 ? 17.487  21.969  25.602  1.00 30.39  ? 130 HIS   B CD2 1 
ATOM   3277 C  CE1 . HIS   B 1 125 ? 17.019  20.136  24.525  1.00 29.21  ? 130 HIS   B CE1 1 
ATOM   3278 N  NE2 . HIS   B 1 125 ? 17.720  20.615  25.552  1.00 29.73  ? 130 HIS   B NE2 1 
ATOM   3279 N  N   . ALA   B 1 126 ? 18.202  25.791  23.546  1.00 30.23  ? 131 ALA   B N   1 
ATOM   3280 C  CA  . ALA   B 1 126 ? 19.561  26.161  23.098  1.00 31.61  ? 131 ALA   B CA  1 
ATOM   3281 C  C   . ALA   B 1 126 ? 20.199  27.246  23.977  1.00 38.50  ? 131 ALA   B C   1 
ATOM   3282 O  O   . ALA   B 1 126 ? 21.421  27.416  23.944  1.00 39.09  ? 131 ALA   B O   1 
ATOM   3283 C  CB  . ALA   B 1 126 ? 19.527  26.617  21.641  1.00 32.47  ? 131 ALA   B CB  1 
ATOM   3284 N  N   . ARG   B 1 127 ? 19.379  27.975  24.751  1.00 37.29  ? 132 ARG   B N   1 
ATOM   3285 C  CA  . ARG   B 1 127 ? 19.861  29.022  25.664  1.00 38.64  ? 132 ARG   B CA  1 
ATOM   3286 C  C   . ARG   B 1 127 ? 20.660  28.416  26.820  1.00 45.32  ? 132 ARG   B C   1 
ATOM   3287 O  O   . ARG   B 1 127 ? 21.814  28.796  27.032  1.00 46.07  ? 132 ARG   B O   1 
ATOM   3288 C  CB  . ARG   B 1 127 ? 18.693  29.849  26.217  1.00 37.93  ? 132 ARG   B CB  1 
ATOM   3289 C  CG  . ARG   B 1 127 ? 18.149  30.839  25.226  1.00 48.05  ? 132 ARG   B CG  1 
ATOM   3290 C  CD  . ARG   B 1 127 ? 17.218  31.824  25.887  1.00 50.75  ? 132 ARG   B CD  1 
ATOM   3291 N  NE  . ARG   B 1 127 ? 16.416  32.518  24.881  1.00 51.22  ? 132 ARG   B NE  1 
ATOM   3292 C  CZ  . ARG   B 1 127 ? 15.148  32.873  25.046  1.00 56.65  ? 132 ARG   B CZ  1 
ATOM   3293 N  NH1 . ARG   B 1 127 ? 14.521  32.611  26.185  1.00 44.88  ? 132 ARG   B NH1 1 
ATOM   3294 N  NH2 . ARG   B 1 127 ? 14.498  33.498  24.076  1.00 50.61  ? 132 ARG   B NH2 1 
ATOM   3295 N  N   . HIS   B 1 128 ? 20.136  27.339  27.422  1.00 42.40  ? 133 HIS   B N   1 
ATOM   3296 C  C   . HIS   B 1 128 ? 21.958  25.139  27.896  1.00 46.64  ? 133 HIS   B C   1 
ATOM   3297 O  O   . HIS   B 1 128 ? 23.113  25.206  28.317  1.00 47.08  ? 133 HIS   B O   1 
ATOM   3298 N  N   . CYS   B 1 129 ? 21.643  24.842  26.610  1.00 40.49  ? 134 CYS   B N   1 
ATOM   3299 C  CA  . CYS   B 1 129 ? 22.238  23.711  25.908  1.00 39.17  ? 134 CYS   B CA  1 
ATOM   3300 C  C   . CYS   B 1 129 ? 22.633  24.112  24.469  1.00 41.57  ? 134 CYS   B C   1 
ATOM   3301 O  O   . CYS   B 1 129 ? 22.045  23.585  23.520  1.00 39.18  ? 134 CYS   B O   1 
ATOM   3302 C  CB  . CYS   B 1 129 ? 21.297  22.506  25.928  1.00 39.32  ? 134 CYS   B CB  1 
ATOM   3303 S  SG  . CYS   B 1 129 ? 20.797  21.987  27.590  1.00 42.81  ? 134 CYS   B SG  1 
ATOM   3304 N  N   . PRO   B 1 130 ? 23.656  24.991  24.273  1.00 37.61  ? 135 PRO   B N   1 
ATOM   3305 C  CA  . PRO   B 1 130 ? 24.031  25.394  22.902  1.00 36.63  ? 135 PRO   B CA  1 
ATOM   3306 C  C   . PRO   B 1 130 ? 24.516  24.263  21.990  1.00 37.02  ? 135 PRO   B C   1 
ATOM   3307 O  O   . PRO   B 1 130 ? 24.472  24.426  20.769  1.00 37.64  ? 135 PRO   B O   1 
ATOM   3308 C  CB  . PRO   B 1 130 ? 25.140  26.438  23.126  1.00 38.73  ? 135 PRO   B CB  1 
ATOM   3309 C  CG  . PRO   B 1 130 ? 25.678  26.128  24.484  1.00 43.60  ? 135 PRO   B CG  1 
ATOM   3310 C  CD  . PRO   B 1 130 ? 24.482  25.703  25.273  1.00 39.61  ? 135 PRO   B CD  1 
ATOM   3311 N  N   . ASP   B 1 131 ? 24.982  23.133  22.568  1.00 33.24  ? 136 ASP   B N   1 
ATOM   3312 C  CA  . ASP   B 1 131 ? 25.441  21.985  21.789  1.00 31.96  ? 136 ASP   B CA  1 
ATOM   3313 C  C   . ASP   B 1 131 ? 24.343  20.920  21.615  1.00 33.75  ? 136 ASP   B C   1 
ATOM   3314 O  O   . ASP   B 1 131 ? 24.644  19.755  21.345  1.00 32.44  ? 136 ASP   B O   1 
ATOM   3315 C  CB  . ASP   B 1 131 ? 26.746  21.385  22.358  1.00 33.57  ? 136 ASP   B CB  1 
ATOM   3316 C  CG  . ASP   B 1 131 ? 27.487  20.476  21.378  1.00 38.26  ? 136 ASP   B CG  1 
ATOM   3317 O  OD1 . ASP   B 1 131 ? 27.430  20.738  20.157  1.00 37.61  ? 136 ASP   B OD1 1 
ATOM   3318 O  OD2 . ASP   B 1 131 ? 28.147  19.526  21.837  1.00 43.29  ? 136 ASP   B OD2 1 
ATOM   3319 N  N   . LEU   B 1 132 ? 23.073  21.331  21.742  1.00 29.83  ? 137 LEU   B N   1 
ATOM   3320 C  CA  . LEU   B 1 132 ? 21.952  20.396  21.556  1.00 29.84  ? 137 LEU   B CA  1 
ATOM   3321 C  C   . LEU   B 1 132 ? 21.863  19.894  20.089  1.00 31.47  ? 137 LEU   B C   1 
ATOM   3322 O  O   . LEU   B 1 132 ? 22.337  20.550  19.153  1.00 29.36  ? 137 LEU   B O   1 
ATOM   3323 C  CB  . LEU   B 1 132 ? 20.600  21.050  21.990  1.00 30.06  ? 137 LEU   B CB  1 
ATOM   3324 C  CG  . LEU   B 1 132 ? 19.863  21.988  20.985  1.00 35.06  ? 137 LEU   B CG  1 
ATOM   3325 C  CD1 . LEU   B 1 132 ? 18.584  22.523  21.579  1.00 35.43  ? 137 LEU   B CD1 1 
ATOM   3326 C  CD2 . LEU   B 1 132 ? 20.731  23.178  20.528  1.00 38.91  ? 137 LEU   B CD2 1 
ATOM   3327 N  N   . CYS   B 1 133 ? 21.218  18.744  19.900  1.00 26.50  ? 138 CYS   B N   1 
ATOM   3328 C  CA  . CYS   B 1 133 ? 20.957  18.242  18.560  1.00 25.69  ? 138 CYS   B CA  1 
ATOM   3329 C  C   . CYS   B 1 133 ? 19.464  17.955  18.521  1.00 28.56  ? 138 CYS   B C   1 
ATOM   3330 O  O   . CYS   B 1 133 ? 18.827  17.848  19.567  1.00 26.60  ? 138 CYS   B O   1 
ATOM   3331 C  CB  . CYS   B 1 133 ? 21.788  17.010  18.219  1.00 26.40  ? 138 CYS   B CB  1 
ATOM   3332 S  SG  . CYS   B 1 133 ? 21.530  15.604  19.322  1.00 29.07  ? 138 CYS   B SG  1 
ATOM   3333 N  N   . VAL   B 1 134 ? 18.917  17.867  17.311  1.00 25.27  ? 139 VAL   B N   1 
ATOM   3334 C  CA  . VAL   B 1 134 ? 17.486  17.730  17.141  1.00 23.49  ? 139 VAL   B CA  1 
ATOM   3335 C  C   . VAL   B 1 134 ? 17.165  16.477  16.338  1.00 25.21  ? 139 VAL   B C   1 
ATOM   3336 O  O   . VAL   B 1 134 ? 17.726  16.281  15.267  1.00 24.02  ? 139 VAL   B O   1 
ATOM   3337 C  CB  . VAL   B 1 134 ? 16.915  19.010  16.463  1.00 26.29  ? 139 VAL   B CB  1 
ATOM   3338 C  CG1 . VAL   B 1 134 ? 15.418  18.878  16.181  1.00 25.54  ? 139 VAL   B CG1 1 
ATOM   3339 C  CG2 . VAL   B 1 134 ? 17.177  20.265  17.311  1.00 25.71  ? 139 VAL   B CG2 1 
ATOM   3340 N  N   . VAL   B 1 135 ? 16.200  15.682  16.826  1.00 22.57  ? 140 VAL   B N   1 
ATOM   3341 C  CA  . VAL   B 1 135 ? 15.698  14.538  16.055  1.00 22.25  ? 140 VAL   B CA  1 
ATOM   3342 C  C   . VAL   B 1 135 ? 14.264  14.969  15.730  1.00 22.55  ? 140 VAL   B C   1 
ATOM   3343 O  O   . VAL   B 1 135 ? 13.462  15.145  16.642  1.00 22.07  ? 140 VAL   B O   1 
ATOM   3344 C  CB  . VAL   B 1 135 ? 15.749  13.180  16.797  1.00 24.80  ? 140 VAL   B CB  1 
ATOM   3345 C  CG1 . VAL   B 1 135 ? 15.111  12.081  15.941  1.00 24.51  ? 140 VAL   B CG1 1 
ATOM   3346 C  CG2 . VAL   B 1 135 ? 17.198  12.806  17.137  1.00 24.84  ? 140 VAL   B CG2 1 
ATOM   3347 N  N   . TRP   B 1 136 ? 13.976  15.189  14.441  1.00 21.20  ? 141 TRP   B N   1 
ATOM   3348 C  CA  . TRP   B 1 136 ? 12.686  15.703  13.964  1.00 21.38  ? 141 TRP   B CA  1 
ATOM   3349 C  C   . TRP   B 1 136 ? 11.896  14.579  13.303  1.00 23.84  ? 141 TRP   B C   1 
ATOM   3350 O  O   . TRP   B 1 136 ? 12.217  14.171  12.182  1.00 23.26  ? 141 TRP   B O   1 
ATOM   3351 C  CB  . TRP   B 1 136 ? 12.929  16.864  12.992  1.00 21.21  ? 141 TRP   B CB  1 
ATOM   3352 C  CG  . TRP   B 1 136 ? 11.718  17.700  12.725  1.00 22.93  ? 141 TRP   B CG  1 
ATOM   3353 C  CD1 . TRP   B 1 136 ? 10.671  17.398  11.904  1.00 25.77  ? 141 TRP   B CD1 1 
ATOM   3354 C  CD2 . TRP   B 1 136 ? 11.506  19.048  13.172  1.00 22.73  ? 141 TRP   B CD2 1 
ATOM   3355 N  NE1 . TRP   B 1 136 ? 9.754   18.434  11.906  1.00 24.69  ? 141 TRP   B NE1 1 
ATOM   3356 C  CE2 . TRP   B 1 136 ? 10.240  19.456  12.680  1.00 25.31  ? 141 TRP   B CE2 1 
ATOM   3357 C  CE3 . TRP   B 1 136 ? 12.204  19.902  14.055  1.00 23.92  ? 141 TRP   B CE3 1 
ATOM   3358 C  CZ2 . TRP   B 1 136 ? 9.714   20.733  12.938  1.00 25.68  ? 141 TRP   B CZ2 1 
ATOM   3359 C  CZ3 . TRP   B 1 136 ? 11.660  21.151  14.351  1.00 25.40  ? 141 TRP   B CZ3 1 
ATOM   3360 C  CH2 . TRP   B 1 136 ? 10.418  21.545  13.814  1.00 25.70  ? 141 TRP   B CH2 1 
ATOM   3361 N  N   . VAL   B 1 137 ? 10.854  14.082  13.997  1.00 22.53  ? 142 VAL   B N   1 
ATOM   3362 C  CA  . VAL   B 1 137 ? 10.088  12.927  13.551  1.00 21.12  ? 142 VAL   B CA  1 
ATOM   3363 C  C   . VAL   B 1 137 ? 8.773   13.444  13.011  1.00 21.82  ? 142 VAL   B C   1 
ATOM   3364 O  O   . VAL   B 1 137 ? 8.005   14.051  13.755  1.00 21.36  ? 142 VAL   B O   1 
ATOM   3365 C  CB  . VAL   B 1 137 ? 9.896   11.902  14.703  1.00 21.95  ? 142 VAL   B CB  1 
ATOM   3366 C  CG1 . VAL   B 1 137 ? 9.137   10.686  14.191  1.00 22.11  ? 142 VAL   B CG1 1 
ATOM   3367 C  CG2 . VAL   B 1 137 ? 11.251  11.466  15.298  1.00 19.99  ? 142 VAL   B CG2 1 
ATOM   3368 N  N   . ASP   B 1 138 ? 8.568   13.310  11.694  1.00 20.77  ? 143 ASP   B N   1 
ATOM   3369 C  CA  . ASP   B 1 138 ? 7.445   13.943  11.026  1.00 20.86  ? 143 ASP   B CA  1 
ATOM   3370 C  C   . ASP   B 1 138 ? 7.301   13.387  9.611   1.00 23.47  ? 143 ASP   B C   1 
ATOM   3371 O  O   . ASP   B 1 138 ? 8.278   12.928  9.007   1.00 20.76  ? 143 ASP   B O   1 
ATOM   3372 C  CB  . ASP   B 1 138 ? 7.825   15.439  10.922  1.00 21.39  ? 143 ASP   B CB  1 
ATOM   3373 C  CG  . ASP   B 1 138 ? 6.742   16.482  10.787  1.00 27.65  ? 143 ASP   B CG  1 
ATOM   3374 O  OD1 . ASP   B 1 138 ? 5.796   16.251  10.026  1.00 22.81  ? 143 ASP   B OD1 1 
ATOM   3375 O  OD2 . ASP   B 1 138 ? 6.909   17.575  11.359  1.00 24.86  ? 143 ASP   B OD2 1 
ATOM   3376 N  N   . ALA   B 1 139 ? 6.073   13.479  9.056   1.00 20.64  ? 144 ALA   B N   1 
ATOM   3377 C  CA  . ALA   B 1 139 ? 5.820   13.160  7.645   1.00 21.28  ? 144 ALA   B CA  1 
ATOM   3378 C  C   . ALA   B 1 139 ? 6.398   14.308  6.769   1.00 23.46  ? 144 ALA   B C   1 
ATOM   3379 O  O   . ALA   B 1 139 ? 6.612   14.137  5.578   1.00 22.91  ? 144 ALA   B O   1 
ATOM   3380 C  CB  . ALA   B 1 139 ? 4.315   13.073  7.414   1.00 22.24  ? 144 ALA   B CB  1 
ATOM   3381 N  N   . HIS   B 1 140 ? 6.619   15.480  7.392   1.00 21.51  ? 145 HIS   B N   1 
ATOM   3382 C  CA  . HIS   B 1 140 ? 7.008   16.753  6.765   1.00 22.82  ? 145 HIS   B CA  1 
ATOM   3383 C  C   . HIS   B 1 140 ? 8.347   17.320  7.261   1.00 26.30  ? 145 HIS   B C   1 
ATOM   3384 O  O   . HIS   B 1 140 ? 8.743   17.101  8.412   1.00 25.04  ? 145 HIS   B O   1 
ATOM   3385 C  CB  . HIS   B 1 140 ? 5.912   17.796  7.055   1.00 22.65  ? 145 HIS   B CB  1 
ATOM   3386 C  CG  . HIS   B 1 140 ? 4.540   17.303  6.709   1.00 24.92  ? 145 HIS   B CG  1 
ATOM   3387 N  ND1 . HIS   B 1 140 ? 3.636   16.910  7.681   1.00 26.00  ? 145 HIS   B ND1 1 
ATOM   3388 C  CD2 . HIS   B 1 140 ? 3.996   17.081  5.490   1.00 26.55  ? 145 HIS   B CD2 1 
ATOM   3389 C  CE1 . HIS   B 1 140 ? 2.571   16.477  7.025   1.00 25.43  ? 145 HIS   B CE1 1 
ATOM   3390 N  NE2 . HIS   B 1 140 ? 2.737   16.567  5.703   1.00 26.20  ? 145 HIS   B NE2 1 
ATOM   3391 N  N   . ALA   B 1 141 ? 9.029   18.078  6.389   1.00 24.61  ? 146 ALA   B N   1 
ATOM   3392 C  CA  . ALA   B 1 141 ? 10.314  18.666  6.749   1.00 24.05  ? 146 ALA   B CA  1 
ATOM   3393 C  C   . ALA   B 1 141 ? 10.157  20.024  7.483   1.00 25.62  ? 146 ALA   B C   1 
ATOM   3394 O  O   . ALA   B 1 141 ? 11.066  20.450  8.175   1.00 24.22  ? 146 ALA   B O   1 
ATOM   3395 C  CB  . ALA   B 1 141 ? 11.195  18.800  5.514   1.00 24.87  ? 146 ALA   B CB  1 
ATOM   3396 N  N   . ASP   B 1 142 ? 8.982   20.688  7.342   1.00 24.40  ? 147 ASP   B N   1 
ATOM   3397 C  CA  . ASP   B 1 142 ? 8.672   21.961  8.015   1.00 24.04  ? 147 ASP   B CA  1 
ATOM   3398 C  C   . ASP   B 1 142 ? 9.828   22.965  7.823   1.00 27.45  ? 147 ASP   B C   1 
ATOM   3399 O  O   . ASP   B 1 142 ? 10.213  23.661  8.768   1.00 27.76  ? 147 ASP   B O   1 
ATOM   3400 C  CB  . ASP   B 1 142 ? 8.428   21.682  9.524   1.00 25.05  ? 147 ASP   B CB  1 
ATOM   3401 C  CG  . ASP   B 1 142 ? 7.185   20.851  9.802   1.00 27.11  ? 147 ASP   B CG  1 
ATOM   3402 O  OD1 . ASP   B 1 142 ? 6.485   20.510  8.835   1.00 28.30  ? 147 ASP   B OD1 1 
ATOM   3403 O  OD2 . ASP   B 1 142 ? 6.933   20.525  10.997  1.00 28.44  ? 147 ASP   B OD2 1 
ATOM   3404 N  N   . ILE   B 1 143 ? 10.422  22.977  6.605   1.00 25.20  ? 148 ILE   B N   1 
ATOM   3405 C  CA  . ILE   B 1 143 ? 11.619  23.790  6.339   1.00 24.98  ? 148 ILE   B CA  1 
ATOM   3406 C  C   . ILE   B 1 143 ? 11.375  24.805  5.210   1.00 29.26  ? 148 ILE   B C   1 
ATOM   3407 O  O   . ILE   B 1 143 ? 12.326  25.392  4.712   1.00 28.89  ? 148 ILE   B O   1 
ATOM   3408 C  CB  . ILE   B 1 143 ? 12.853  22.877  6.133   1.00 27.57  ? 148 ILE   B CB  1 
ATOM   3409 C  CG1 . ILE   B 1 143 ? 14.187  23.657  6.356   1.00 27.65  ? 148 ILE   B CG1 1 
ATOM   3410 C  CG2 . ILE   B 1 143 ? 12.822  22.114  4.800   1.00 28.22  ? 148 ILE   B CG2 1 
ATOM   3411 C  CD1 . ILE   B 1 143 ? 15.387  22.768  6.587   1.00 29.94  ? 148 ILE   B CD1 1 
ATOM   3412 N  N   . ASN   B 1 144 ? 10.104  25.081  4.876   1.00 25.24  ? 149 ASN   B N   1 
ATOM   3413 C  CA  . ASN   B 1 144 ? 9.822   26.159  3.938   1.00 26.29  ? 149 ASN   B CA  1 
ATOM   3414 C  C   . ASN   B 1 144 ? 10.305  27.449  4.573   1.00 30.72  ? 149 ASN   B C   1 
ATOM   3415 O  O   . ASN   B 1 144 ? 10.329  27.559  5.795   1.00 29.72  ? 149 ASN   B O   1 
ATOM   3416 C  CB  . ASN   B 1 144 ? 8.317   26.259  3.625   1.00 26.59  ? 149 ASN   B CB  1 
ATOM   3417 C  CG  . ASN   B 1 144 ? 7.948   25.411  2.445   1.00 33.85  ? 149 ASN   B CG  1 
ATOM   3418 O  OD1 . ASN   B 1 144 ? 8.483   25.586  1.345   1.00 32.12  ? 149 ASN   B OD1 1 
ATOM   3419 N  ND2 . ASN   B 1 144 ? 7.105   24.410  2.662   1.00 29.79  ? 149 ASN   B ND2 1 
ATOM   3420 N  N   . THR   B 1 145 ? 10.800  28.372  3.761   1.00 29.23  ? 150 THR   B N   1 
ATOM   3421 C  CA  . THR   B 1 145 ? 11.188  29.682  4.276   1.00 28.92  ? 150 THR   B CA  1 
ATOM   3422 C  C   . THR   B 1 145 ? 9.936   30.563  4.119   1.00 33.55  ? 150 THR   B C   1 
ATOM   3423 O  O   . THR   B 1 145 ? 9.030   30.184  3.367   1.00 33.09  ? 150 THR   B O   1 
ATOM   3424 C  CB  . THR   B 1 145 ? 12.387  30.285  3.486   1.00 35.02  ? 150 THR   B CB  1 
ATOM   3425 O  OG1 . THR   B 1 145 ? 11.941  30.765  2.217   1.00 32.70  ? 150 THR   B OG1 1 
ATOM   3426 C  CG2 . THR   B 1 145 ? 13.568  29.329  3.347   1.00 34.36  ? 150 THR   B CG2 1 
ATOM   3427 N  N   . PRO   B 1 146 ? 9.882   31.764  4.750   1.00 31.68  ? 151 PRO   B N   1 
ATOM   3428 C  CA  . PRO   B 1 146 ? 8.739   32.672  4.505   1.00 32.56  ? 151 PRO   B CA  1 
ATOM   3429 C  C   . PRO   B 1 146 ? 8.550   33.038  3.015   1.00 37.95  ? 151 PRO   B C   1 
ATOM   3430 O  O   . PRO   B 1 146 ? 7.445   33.398  2.600   1.00 38.52  ? 151 PRO   B O   1 
ATOM   3431 C  CB  . PRO   B 1 146 ? 9.094   33.899  5.342   1.00 33.78  ? 151 PRO   B CB  1 
ATOM   3432 C  CG  . PRO   B 1 146 ? 10.016  33.372  6.420   1.00 38.26  ? 151 PRO   B CG  1 
ATOM   3433 C  CD  . PRO   B 1 146 ? 10.838  32.350  5.713   1.00 33.86  ? 151 PRO   B CD  1 
ATOM   3434 N  N   . LEU   B 1 147 ? 9.606   32.877  2.202   1.00 34.74  ? 152 LEU   B N   1 
ATOM   3435 C  CA  . LEU   B 1 147 ? 9.558   33.153  0.759   1.00 36.63  ? 152 LEU   B CA  1 
ATOM   3436 C  C   . LEU   B 1 147 ? 9.202   31.933  -0.121  1.00 40.25  ? 152 LEU   B C   1 
ATOM   3437 O  O   . LEU   B 1 147 ? 8.776   32.139  -1.263  1.00 40.42  ? 152 LEU   B O   1 
ATOM   3438 C  CB  . LEU   B 1 147 ? 10.871  33.791  0.279   1.00 36.92  ? 152 LEU   B CB  1 
ATOM   3439 C  CG  . LEU   B 1 147 ? 11.411  34.997  1.064   1.00 42.37  ? 152 LEU   B CG  1 
ATOM   3440 C  CD1 . LEU   B 1 147 ? 12.765  35.374  0.565   1.00 42.69  ? 152 LEU   B CD1 1 
ATOM   3441 C  CD2 . LEU   B 1 147 ? 10.452  36.194  1.030   1.00 46.44  ? 152 LEU   B CD2 1 
ATOM   3442 N  N   . THR   B 1 148 ? 9.377   30.672  0.384   1.00 34.50  ? 153 THR   B N   1 
ATOM   3443 C  CA  . THR   B 1 148 ? 9.066   29.466  -0.401  1.00 33.01  ? 153 THR   B CA  1 
ATOM   3444 C  C   . THR   B 1 148 ? 7.673   28.894  -0.088  1.00 35.39  ? 153 THR   B C   1 
ATOM   3445 O  O   . THR   B 1 148 ? 7.102   28.183  -0.920  1.00 33.87  ? 153 THR   B O   1 
ATOM   3446 C  CB  . THR   B 1 148 ? 10.147  28.384  -0.260  1.00 39.33  ? 153 THR   B CB  1 
ATOM   3447 O  OG1 . THR   B 1 148 ? 10.091  27.811  1.055   1.00 34.91  ? 153 THR   B OG1 1 
ATOM   3448 C  CG2 . THR   B 1 148 ? 11.556  28.890  -0.594  1.00 34.31  ? 153 THR   B CG2 1 
ATOM   3449 N  N   . THR   B 1 149 ? 7.153   29.164  1.122   1.00 30.90  ? 154 THR   B N   1 
ATOM   3450 C  CA  . THR   B 1 149 ? 5.838   28.666  1.536   1.00 31.43  ? 154 THR   B CA  1 
ATOM   3451 C  C   . THR   B 1 149 ? 4.732   29.066  0.538   1.00 36.89  ? 154 THR   B C   1 
ATOM   3452 O  O   . THR   B 1 149 ? 4.731   30.194  0.038   1.00 36.48  ? 154 THR   B O   1 
ATOM   3453 C  CB  . THR   B 1 149 ? 5.486   29.117  2.965   1.00 35.07  ? 154 THR   B CB  1 
ATOM   3454 O  OG1 . THR   B 1 149 ? 4.166   28.661  3.254   1.00 33.10  ? 154 THR   B OG1 1 
ATOM   3455 C  CG2 . THR   B 1 149 ? 5.504   30.641  3.141   1.00 40.31  ? 154 THR   B CG2 1 
ATOM   3456 N  N   . SER   B 1 150 ? 3.796   28.142  0.276   1.00 34.72  ? 155 SER   B N   1 
ATOM   3457 C  CA  . SER   B 1 150 ? 2.650   28.393  -0.602  1.00 35.33  ? 155 SER   B CA  1 
ATOM   3458 C  C   . SER   B 1 150 ? 1.385   28.604  0.222   1.00 38.49  ? 155 SER   B C   1 
ATOM   3459 O  O   . SER   B 1 150 ? 0.432   29.224  -0.264  1.00 38.51  ? 155 SER   B O   1 
ATOM   3460 C  CB  . SER   B 1 150 ? 2.456   27.227  -1.563  1.00 39.90  ? 155 SER   B CB  1 
ATOM   3461 O  OG  . SER   B 1 150 ? 3.594   27.130  -2.404  1.00 54.42  ? 155 SER   B OG  1 
ATOM   3462 N  N   . SER   B 1 151 ? 1.372   28.093  1.477   1.00 32.32  ? 156 SER   B N   1 
ATOM   3463 C  CA  . SER   B 1 151 ? 0.215   28.187  2.365   1.00 31.83  ? 156 SER   B CA  1 
ATOM   3464 C  C   . SER   B 1 151 ? 0.248   29.420  3.252   1.00 36.55  ? 156 SER   B C   1 
ATOM   3465 O  O   . SER   B 1 151 ? -0.809  29.883  3.685   1.00 39.17  ? 156 SER   B O   1 
ATOM   3466 C  CB  . SER   B 1 151 ? 0.143   26.955  3.257   1.00 34.52  ? 156 SER   B CB  1 
ATOM   3467 O  OG  . SER   B 1 151 ? 1.288   26.926  4.095   1.00 35.06  ? 156 SER   B OG  1 
ATOM   3468 N  N   . GLY   B 1 152 ? 1.452   29.871  3.593   1.00 32.45  ? 157 GLY   B N   1 
ATOM   3469 C  CA  . GLY   B 1 152 ? 1.674   30.952  4.550   1.00 32.23  ? 157 GLY   B CA  1 
ATOM   3470 C  C   . GLY   B 1 152 ? 1.540   30.477  5.995   1.00 35.92  ? 157 GLY   B C   1 
ATOM   3471 O  O   . GLY   B 1 152 ? 1.562   31.298  6.920   1.00 36.92  ? 157 GLY   B O   1 
ATOM   3472 N  N   . ASN   B 1 153 ? 1.407   29.142  6.217   1.00 31.13  ? 158 ASN   B N   1 
ATOM   3473 C  CA  . ASN   B 1 153 ? 1.252   28.568  7.570   1.00 29.46  ? 158 ASN   B CA  1 
ATOM   3474 C  C   . ASN   B 1 153 ? 2.613   28.377  8.206   1.00 32.15  ? 158 ASN   B C   1 
ATOM   3475 O  O   . ASN   B 1 153 ? 3.462   27.686  7.647   1.00 30.01  ? 158 ASN   B O   1 
ATOM   3476 C  CB  . ASN   B 1 153 ? 0.458   27.268  7.522   1.00 31.46  ? 158 ASN   B CB  1 
ATOM   3477 C  CG  . ASN   B 1 153 ? -0.958  27.476  7.033   1.00 43.46  ? 158 ASN   B CG  1 
ATOM   3478 O  OD1 . ASN   B 1 153 ? -1.515  28.574  7.140   1.00 34.86  ? 158 ASN   B OD1 1 
ATOM   3479 N  ND2 . ASN   B 1 153 ? -1.559  26.443  6.468   1.00 33.14  ? 158 ASN   B ND2 1 
ATOM   3480 N  N   . LEU   B 1 154 ? 2.836   29.029  9.361   1.00 28.06  ? 159 LEU   B N   1 
ATOM   3481 C  CA  . LEU   B 1 154 ? 4.136   28.997  10.026  1.00 27.11  ? 159 LEU   B CA  1 
ATOM   3482 C  C   . LEU   B 1 154 ? 4.511   27.602  10.556  1.00 29.06  ? 159 LEU   B C   1 
ATOM   3483 O  O   . LEU   B 1 154 ? 5.692   27.343  10.670  1.00 28.33  ? 159 LEU   B O   1 
ATOM   3484 C  CB  . LEU   B 1 154 ? 4.247   30.095  11.108  1.00 27.45  ? 159 LEU   B CB  1 
ATOM   3485 C  CG  . LEU   B 1 154 ? 4.515   31.493  10.487  1.00 30.72  ? 159 LEU   B CG  1 
ATOM   3486 C  CD1 . LEU   B 1 154 ? 4.141   32.624  11.428  1.00 31.20  ? 159 LEU   B CD1 1 
ATOM   3487 C  CD2 . LEU   B 1 154 ? 5.948   31.654  10.005  1.00 30.36  ? 159 LEU   B CD2 1 
ATOM   3488 N  N   . HIS   B 1 155 ? 3.557   26.689  10.754  1.00 26.45  ? 160 HIS   B N   1 
ATOM   3489 C  CA  . HIS   B 1 155 ? 3.919   25.310  11.197  1.00 26.01  ? 160 HIS   B CA  1 
ATOM   3490 C  C   . HIS   B 1 155 ? 4.717   24.539  10.102  1.00 28.98  ? 160 HIS   B C   1 
ATOM   3491 O  O   . HIS   B 1 155 ? 5.332   23.520  10.413  1.00 27.21  ? 160 HIS   B O   1 
ATOM   3492 C  CB  . HIS   B 1 155 ? 2.694   24.502  11.684  1.00 25.80  ? 160 HIS   B CB  1 
ATOM   3493 C  CG  . HIS   B 1 155 ? 1.752   24.021  10.616  1.00 27.58  ? 160 HIS   B CG  1 
ATOM   3494 N  ND1 . HIS   B 1 155 ? 0.879   22.978  10.857  1.00 29.04  ? 160 HIS   B ND1 1 
ATOM   3495 C  CD2 . HIS   B 1 155 ? 1.544   24.472  9.353   1.00 29.01  ? 160 HIS   B CD2 1 
ATOM   3496 C  CE1 . HIS   B 1 155 ? 0.210   22.800  9.728   1.00 28.07  ? 160 HIS   B CE1 1 
ATOM   3497 N  NE2 . HIS   B 1 155 ? 0.547   23.705  8.815   1.00 28.15  ? 160 HIS   B NE2 1 
ATOM   3498 N  N   . GLY   B 1 156 ? 4.698   25.042  8.852   1.00 26.37  ? 161 GLY   B N   1 
ATOM   3499 C  CA  . GLY   B 1 156 ? 5.415   24.455  7.718   1.00 25.84  ? 161 GLY   B CA  1 
ATOM   3500 C  C   . GLY   B 1 156 ? 6.775   25.098  7.503   1.00 27.21  ? 161 GLY   B C   1 
ATOM   3501 O  O   . GLY   B 1 156 ? 7.488   24.750  6.550   1.00 26.18  ? 161 GLY   B O   1 
ATOM   3502 N  N   . GLN   B 1 157 ? 7.145   26.060  8.390   1.00 24.35  ? 162 GLN   B N   1 
ATOM   3503 C  CA  . GLN   B 1 157 ? 8.404   26.817  8.277   1.00 24.63  ? 162 GLN   B CA  1 
ATOM   3504 C  C   . GLN   B 1 157 ? 9.359   26.816  9.501   1.00 29.44  ? 162 GLN   B C   1 
ATOM   3505 O  O   . GLN   B 1 157 ? 10.386  27.512  9.430   1.00 28.82  ? 162 GLN   B O   1 
ATOM   3506 C  CB  . GLN   B 1 157 ? 8.038   28.301  8.001   1.00 26.59  ? 162 GLN   B CB  1 
ATOM   3507 C  CG  . GLN   B 1 157 ? 7.227   28.525  6.732   1.00 25.45  ? 162 GLN   B CG  1 
ATOM   3508 C  CD  . GLN   B 1 157 ? 6.698   29.933  6.669   1.00 36.35  ? 162 GLN   B CD  1 
ATOM   3509 O  OE1 . GLN   B 1 157 ? 7.453   30.900  6.663   1.00 32.33  ? 162 GLN   B OE1 1 
ATOM   3510 N  NE2 . GLN   B 1 157 ? 5.387   30.070  6.626   1.00 30.70  ? 162 GLN   B NE2 1 
ATOM   3511 N  N   . PRO   B 1 158 ? 9.078   26.137  10.643  1.00 26.59  ? 163 PRO   B N   1 
ATOM   3512 C  CA  . PRO   B 1 158 ? 9.890   26.375  11.845  1.00 26.39  ? 163 PRO   B CA  1 
ATOM   3513 C  C   . PRO   B 1 158 ? 11.373  26.153  11.707  1.00 27.78  ? 163 PRO   B C   1 
ATOM   3514 O  O   . PRO   B 1 158 ? 12.146  26.940  12.263  1.00 28.50  ? 163 PRO   B O   1 
ATOM   3515 C  CB  . PRO   B 1 158 ? 9.272   25.446  12.896  1.00 28.28  ? 163 PRO   B CB  1 
ATOM   3516 C  CG  . PRO   B 1 158 ? 8.558   24.390  12.104  1.00 31.34  ? 163 PRO   B CG  1 
ATOM   3517 C  CD  . PRO   B 1 158 ? 7.981   25.206  10.956  1.00 27.73  ? 163 PRO   B CD  1 
ATOM   3518 N  N   . VAL   B 1 159 ? 11.768  25.097  10.982  1.00 23.62  ? 164 VAL   B N   1 
ATOM   3519 C  CA  . VAL   B 1 159 ? 13.187  24.774  10.860  1.00 23.74  ? 164 VAL   B CA  1 
ATOM   3520 C  C   . VAL   B 1 159 ? 13.949  25.898  10.119  1.00 27.65  ? 164 VAL   B C   1 
ATOM   3521 O  O   . VAL   B 1 159 ? 15.123  26.132  10.423  1.00 28.79  ? 164 VAL   B O   1 
ATOM   3522 C  CB  . VAL   B 1 159 ? 13.432  23.357  10.277  1.00 27.48  ? 164 VAL   B CB  1 
ATOM   3523 C  CG1 . VAL   B 1 159 ? 14.924  23.016  10.230  1.00 27.43  ? 164 VAL   B CG1 1 
ATOM   3524 C  CG2 . VAL   B 1 159 ? 12.679  22.296  11.087  1.00 27.57  ? 164 VAL   B CG2 1 
ATOM   3525 N  N   . SER   B 1 160 ? 13.294  26.618  9.198   1.00 25.77  ? 165 SER   B N   1 
ATOM   3526 C  CA  . SER   B 1 160 ? 13.990  27.702  8.467   1.00 27.11  ? 165 SER   B CA  1 
ATOM   3527 C  C   . SER   B 1 160 ? 14.501  28.814  9.371   1.00 31.36  ? 165 SER   B C   1 
ATOM   3528 O  O   . SER   B 1 160 ? 15.541  29.396  9.072   1.00 32.26  ? 165 SER   B O   1 
ATOM   3529 C  CB  . SER   B 1 160 ? 13.113  28.302  7.372   1.00 30.03  ? 165 SER   B CB  1 
ATOM   3530 O  OG  . SER   B 1 160 ? 12.032  29.060  7.892   1.00 33.99  ? 165 SER   B OG  1 
ATOM   3531 N  N   . PHE   B 1 161 ? 13.804  29.076  10.494  1.00 28.55  ? 166 PHE   B N   1 
ATOM   3532 C  CA  . PHE   B 1 161 ? 14.201  30.115  11.455  1.00 28.88  ? 166 PHE   B CA  1 
ATOM   3533 C  C   . PHE   B 1 161 ? 15.316  29.685  12.385  1.00 33.83  ? 166 PHE   B C   1 
ATOM   3534 O  O   . PHE   B 1 161 ? 15.966  30.528  13.007  1.00 34.53  ? 166 PHE   B O   1 
ATOM   3535 C  CB  . PHE   B 1 161 ? 12.986  30.542  12.287  1.00 30.76  ? 166 PHE   B CB  1 
ATOM   3536 C  CG  . PHE   B 1 161 ? 11.829  31.024  11.448  1.00 32.91  ? 166 PHE   B CG  1 
ATOM   3537 C  CD1 . PHE   B 1 161 ? 11.857  32.280  10.849  1.00 36.31  ? 166 PHE   B CD1 1 
ATOM   3538 C  CD2 . PHE   B 1 161 ? 10.690  30.239  11.284  1.00 34.79  ? 166 PHE   B CD2 1 
ATOM   3539 C  CE1 . PHE   B 1 161 ? 10.784  32.721  10.068  1.00 37.38  ? 166 PHE   B CE1 1 
ATOM   3540 C  CE2 . PHE   B 1 161 ? 9.621   30.680  10.506  1.00 37.01  ? 166 PHE   B CE2 1 
ATOM   3541 C  CZ  . PHE   B 1 161 ? 9.676   31.914  9.894   1.00 35.62  ? 166 PHE   B CZ  1 
ATOM   3542 N  N   . LEU   B 1 162 ? 15.508  28.374  12.524  1.00 30.01  ? 167 LEU   B N   1 
ATOM   3543 C  CA  . LEU   B 1 162 ? 16.468  27.819  13.474  1.00 29.26  ? 167 LEU   B CA  1 
ATOM   3544 C  C   . LEU   B 1 162 ? 17.813  27.480  12.892  1.00 32.08  ? 167 LEU   B C   1 
ATOM   3545 O  O   . LEU   B 1 162 ? 18.781  27.484  13.638  1.00 32.06  ? 167 LEU   B O   1 
ATOM   3546 C  CB  . LEU   B 1 162 ? 15.866  26.560  14.146  1.00 29.01  ? 167 LEU   B CB  1 
ATOM   3547 C  CG  . LEU   B 1 162 ? 14.551  26.736  14.914  1.00 33.23  ? 167 LEU   B CG  1 
ATOM   3548 C  CD1 . LEU   B 1 162 ? 13.895  25.389  15.174  1.00 33.49  ? 167 LEU   B CD1 1 
ATOM   3549 C  CD2 . LEU   B 1 162 ? 14.769  27.433  16.263  1.00 36.14  ? 167 LEU   B CD2 1 
ATOM   3550 N  N   . LEU   B 1 163 ? 17.885  27.134  11.597  1.00 29.59  ? 168 LEU   B N   1 
ATOM   3551 C  CA  . LEU   B 1 163 ? 19.161  26.706  11.006  1.00 32.01  ? 168 LEU   B CA  1 
ATOM   3552 C  C   . LEU   B 1 163 ? 20.081  27.849  10.624  1.00 36.83  ? 168 LEU   B C   1 
ATOM   3553 O  O   . LEU   B 1 163 ? 19.699  28.684  9.809   1.00 37.10  ? 168 LEU   B O   1 
ATOM   3554 C  CB  . LEU   B 1 163 ? 18.964  25.759  9.814   1.00 33.41  ? 168 LEU   B CB  1 
ATOM   3555 C  CG  . LEU   B 1 163 ? 18.542  24.316  10.130  1.00 40.04  ? 168 LEU   B CG  1 
ATOM   3556 C  CD1 . LEU   B 1 163 ? 18.477  23.503  8.870   1.00 41.47  ? 168 LEU   B CD1 1 
ATOM   3557 C  CD2 . LEU   B 1 163 ? 19.513  23.632  11.071  1.00 42.79  ? 168 LEU   B CD2 1 
ATOM   3558 N  N   . ARG   B 1 164 ? 21.315  27.847  11.169  1.00 34.04  ? 169 ARG   B N   1 
ATOM   3559 C  CA  . ARG   B 1 164 ? 22.310  28.903  10.912  1.00 34.47  ? 169 ARG   B CA  1 
ATOM   3560 C  C   . ARG   B 1 164 ? 22.579  29.143  9.431   1.00 39.33  ? 169 ARG   B C   1 
ATOM   3561 O  O   . ARG   B 1 164 ? 22.518  30.285  8.976   1.00 39.73  ? 169 ARG   B O   1 
ATOM   3562 C  CB  . ARG   B 1 164 ? 23.630  28.636  11.658  1.00 32.80  ? 169 ARG   B CB  1 
ATOM   3563 C  CG  . ARG   B 1 164 ? 23.522  28.871  13.153  1.00 43.70  ? 169 ARG   B CG  1 
ATOM   3564 C  CD  . ARG   B 1 164 ? 24.883  28.896  13.815  1.00 56.94  ? 169 ARG   B CD  1 
ATOM   3565 N  NE  . ARG   B 1 164 ? 25.202  27.603  14.416  1.00 65.97  ? 169 ARG   B NE  1 
ATOM   3566 C  CZ  . ARG   B 1 164 ? 24.992  27.298  15.692  1.00 75.58  ? 169 ARG   B CZ  1 
ATOM   3567 N  NH1 . ARG   B 1 164 ? 24.476  28.198  16.522  1.00 66.76  ? 169 ARG   B NH1 1 
ATOM   3568 N  NH2 . ARG   B 1 164 ? 25.297  26.091  16.150  1.00 52.86  ? 169 ARG   B NH2 1 
ATOM   3569 N  N   . GLU   B 1 165 ? 22.817  28.062  8.671   1.00 36.19  ? 170 GLU   B N   1 
ATOM   3570 C  CA  . GLU   B 1 165 ? 23.169  28.108  7.248   1.00 35.07  ? 170 GLU   B CA  1 
ATOM   3571 C  C   . GLU   B 1 165 ? 22.089  28.696  6.335   1.00 39.79  ? 170 GLU   B C   1 
ATOM   3572 O  O   . GLU   B 1 165 ? 22.421  29.086  5.218   1.00 40.68  ? 170 GLU   B O   1 
ATOM   3573 C  CB  . GLU   B 1 165 ? 23.600  26.715  6.747   1.00 35.88  ? 170 GLU   B CB  1 
ATOM   3574 C  CG  . GLU   B 1 165 ? 24.898  26.190  7.360   1.00 37.23  ? 170 GLU   B CG  1 
ATOM   3575 C  CD  . GLU   B 1 165 ? 24.758  25.459  8.686   1.00 51.21  ? 170 GLU   B CD  1 
ATOM   3576 O  OE1 . GLU   B 1 165 ? 23.631  25.431  9.234   1.00 37.07  ? 170 GLU   B OE1 1 
ATOM   3577 O  OE2 . GLU   B 1 165 ? 25.777  24.926  9.188   1.00 45.28  ? 170 GLU   B OE2 1 
ATOM   3578 N  N   . LEU   B 1 166 ? 20.818  28.769  6.787   1.00 35.82  ? 171 LEU   B N   1 
ATOM   3579 C  CA  . LEU   B 1 166 ? 19.716  29.300  5.982   1.00 37.02  ? 171 LEU   B CA  1 
ATOM   3580 C  C   . LEU   B 1 166 ? 19.389  30.774  6.226   1.00 41.58  ? 171 LEU   B C   1 
ATOM   3581 O  O   . LEU   B 1 166 ? 18.517  31.300  5.533   1.00 40.74  ? 171 LEU   B O   1 
ATOM   3582 C  CB  . LEU   B 1 166 ? 18.431  28.493  6.234   1.00 37.44  ? 171 LEU   B CB  1 
ATOM   3583 C  CG  . LEU   B 1 166 ? 18.206  27.239  5.431   1.00 42.16  ? 171 LEU   B CG  1 
ATOM   3584 C  CD1 . LEU   B 1 166 ? 17.089  26.417  6.068   1.00 42.50  ? 171 LEU   B CD1 1 
ATOM   3585 C  CD2 . LEU   B 1 166 ? 17.865  27.567  3.962   1.00 42.30  ? 171 LEU   B CD2 1 
ATOM   3586 N  N   . GLN   B 1 167 ? 20.041  31.416  7.221   1.00 39.64  ? 172 GLN   B N   1 
ATOM   3587 C  CA  . GLN   B 1 167 ? 19.792  32.790  7.688   1.00 40.02  ? 172 GLN   B CA  1 
ATOM   3588 C  C   . GLN   B 1 167 ? 19.646  33.829  6.559   1.00 43.58  ? 172 GLN   B C   1 
ATOM   3589 O  O   . GLN   B 1 167 ? 18.703  34.619  6.586   1.00 42.07  ? 172 GLN   B O   1 
ATOM   3590 C  CB  . GLN   B 1 167 ? 20.858  33.235  8.721   1.00 41.53  ? 172 GLN   B CB  1 
ATOM   3591 C  CG  . GLN   B 1 167 ? 20.475  34.528  9.476   1.00 65.79  ? 172 GLN   B CG  1 
ATOM   3592 C  CD  . GLN   B 1 167 ? 21.379  34.919  10.630  1.00 84.38  ? 172 GLN   B CD  1 
ATOM   3593 O  OE1 . GLN   B 1 167 ? 22.547  34.520  10.726  1.00 79.75  ? 172 GLN   B OE1 1 
ATOM   3594 N  NE2 . GLN   B 1 167 ? 20.855  35.749  11.522  1.00 75.56  ? 172 GLN   B NE2 1 
ATOM   3595 N  N   . ASP   B 1 168 ? 20.528  33.781  5.553   1.00 40.36  ? 173 ASP   B N   1 
ATOM   3596 C  CA  . ASP   B 1 168 ? 20.519  34.709  4.405   1.00 40.25  ? 173 ASP   B CA  1 
ATOM   3597 C  C   . ASP   B 1 168 ? 19.319  34.517  3.453   1.00 41.57  ? 173 ASP   B C   1 
ATOM   3598 O  O   . ASP   B 1 168 ? 19.066  35.370  2.597   1.00 40.35  ? 173 ASP   B O   1 
ATOM   3599 C  CB  . ASP   B 1 168 ? 21.857  34.636  3.645   1.00 43.18  ? 173 ASP   B CB  1 
ATOM   3600 C  CG  . ASP   B 1 168 ? 22.294  33.226  3.288   1.00 64.56  ? 173 ASP   B CG  1 
ATOM   3601 O  OD1 . ASP   B 1 168 ? 22.559  32.428  4.223   1.00 68.16  ? 173 ASP   B OD1 1 
ATOM   3602 O  OD2 . ASP   B 1 168 ? 22.402  32.928  2.081   1.00 73.83  ? 173 ASP   B OD2 1 
ATOM   3603 N  N   . LYS   B 1 169 ? 18.591  33.398  3.600   1.00 35.15  ? 174 LYS   B N   1 
ATOM   3604 C  CA  . LYS   B 1 169 ? 17.415  33.085  2.789   1.00 33.63  ? 174 LYS   B CA  1 
ATOM   3605 C  C   . LYS   B 1 169 ? 16.121  33.377  3.530   1.00 36.25  ? 174 LYS   B C   1 
ATOM   3606 O  O   . LYS   B 1 169 ? 15.038  33.231  2.962   1.00 35.97  ? 174 LYS   B O   1 
ATOM   3607 C  CB  . LYS   B 1 169 ? 17.457  31.606  2.345   1.00 35.15  ? 174 LYS   B CB  1 
ATOM   3608 C  CG  . LYS   B 1 169 ? 18.694  31.222  1.525   1.00 43.79  ? 174 LYS   B CG  1 
ATOM   3609 C  CD  . LYS   B 1 169 ? 18.648  31.782  0.097   1.00 51.15  ? 174 LYS   B CD  1 
ATOM   3610 C  CE  . LYS   B 1 169 ? 19.940  32.459  -0.275  1.00 70.35  ? 174 LYS   B CE  1 
ATOM   3611 N  NZ  . LYS   B 1 169 ? 20.995  31.485  -0.645  1.00 76.45  ? 174 LYS   B NZ  1 
ATOM   3612 N  N   . VAL   B 1 170 ? 16.226  33.796  4.795   1.00 33.02  ? 175 VAL   B N   1 
ATOM   3613 C  CA  . VAL   B 1 170 ? 15.072  34.018  5.656   1.00 32.18  ? 175 VAL   B CA  1 
ATOM   3614 C  C   . VAL   B 1 170 ? 14.918  35.512  5.969   1.00 36.73  ? 175 VAL   B C   1 
ATOM   3615 O  O   . VAL   B 1 170 ? 15.804  36.097  6.604   1.00 37.09  ? 175 VAL   B O   1 
ATOM   3616 C  CB  . VAL   B 1 170 ? 15.179  33.133  6.943   1.00 35.56  ? 175 VAL   B CB  1 
ATOM   3617 C  CG1 . VAL   B 1 170 ? 14.035  33.403  7.926   1.00 35.35  ? 175 VAL   B CG1 1 
ATOM   3618 C  CG2 . VAL   B 1 170 ? 15.247  31.645  6.580   1.00 34.92  ? 175 VAL   B CG2 1 
ATOM   3619 N  N   . PRO   B 1 171 ? 13.802  36.144  5.530   1.00 35.31  ? 176 PRO   B N   1 
ATOM   3620 C  CA  . PRO   B 1 171 ? 13.606  37.571  5.845   1.00 36.32  ? 176 PRO   B CA  1 
ATOM   3621 C  C   . PRO   B 1 171 ? 13.226  37.753  7.314   1.00 42.45  ? 176 PRO   B C   1 
ATOM   3622 O  O   . PRO   B 1 171 ? 12.808  36.787  7.959   1.00 41.70  ? 176 PRO   B O   1 
ATOM   3623 C  CB  . PRO   B 1 171 ? 12.482  37.988  4.890   1.00 37.21  ? 176 PRO   B CB  1 
ATOM   3624 C  CG  . PRO   B 1 171 ? 11.684  36.749  4.694   1.00 41.32  ? 176 PRO   B CG  1 
ATOM   3625 C  CD  . PRO   B 1 171 ? 12.652  35.596  4.777   1.00 36.77  ? 176 PRO   B CD  1 
ATOM   3626 N  N   . GLN   B 1 172 ? 13.398  38.967  7.857   1.00 40.77  ? 177 GLN   B N   1 
ATOM   3627 C  CA  . GLN   B 1 172 ? 13.022  39.232  9.243   1.00 41.20  ? 177 GLN   B CA  1 
ATOM   3628 C  C   . GLN   B 1 172 ? 11.504  39.493  9.314   1.00 44.70  ? 177 GLN   B C   1 
ATOM   3629 O  O   . GLN   B 1 172 ? 11.015  40.468  8.741   1.00 45.03  ? 177 GLN   B O   1 
ATOM   3630 C  CB  . GLN   B 1 172 ? 13.832  40.413  9.832   1.00 43.66  ? 177 GLN   B CB  1 
ATOM   3631 C  CG  . GLN   B 1 172 ? 13.965  40.327  11.358  1.00 66.33  ? 177 GLN   B CG  1 
ATOM   3632 C  CD  . GLN   B 1 172 ? 14.273  41.649  12.027  1.00 87.39  ? 177 GLN   B CD  1 
ATOM   3633 O  OE1 . GLN   B 1 172 ? 15.370  41.857  12.567  1.00 79.93  ? 177 GLN   B OE1 1 
ATOM   3634 N  NE2 . GLN   B 1 172 ? 13.289  42.546  12.071  1.00 79.33  ? 177 GLN   B NE2 1 
ATOM   3635 N  N   . LEU   B 1 173 ? 10.762  38.594  9.979   1.00 40.10  ? 178 LEU   B N   1 
ATOM   3636 C  CA  . LEU   B 1 173 ? 9.312   38.696  10.144  1.00 39.77  ? 178 LEU   B CA  1 
ATOM   3637 C  C   . LEU   B 1 173 ? 8.949   39.532  11.381  1.00 43.09  ? 178 LEU   B C   1 
ATOM   3638 O  O   . LEU   B 1 173 ? 9.725   39.553  12.345  1.00 40.78  ? 178 LEU   B O   1 
ATOM   3639 C  CB  . LEU   B 1 173 ? 8.716   37.279  10.291  1.00 40.57  ? 178 LEU   B CB  1 
ATOM   3640 C  CG  . LEU   B 1 173 ? 8.063   36.645  9.046   1.00 45.71  ? 178 LEU   B CG  1 
ATOM   3641 C  CD1 . LEU   B 1 173 ? 8.972   36.716  7.815   1.00 45.58  ? 178 LEU   B CD1 1 
ATOM   3642 C  CD2 . LEU   B 1 173 ? 7.626   35.199  9.335   1.00 45.85  ? 178 LEU   B CD2 1 
ATOM   3643 N  N   . PRO   B 1 174 ? 7.761   40.194  11.409  1.00 41.13  ? 179 PRO   B N   1 
ATOM   3644 C  CA  . PRO   B 1 174 ? 7.378   40.924  12.624  1.00 40.90  ? 179 PRO   B CA  1 
ATOM   3645 C  C   . PRO   B 1 174 ? 7.131   39.924  13.754  1.00 43.55  ? 179 PRO   B C   1 
ATOM   3646 O  O   . PRO   B 1 174 ? 6.535   38.864  13.526  1.00 41.43  ? 179 PRO   B O   1 
ATOM   3647 C  CB  . PRO   B 1 174 ? 6.108   41.668  12.210  1.00 42.62  ? 179 PRO   B CB  1 
ATOM   3648 C  CG  . PRO   B 1 174 ? 5.533   40.853  11.108  1.00 47.54  ? 179 PRO   B CG  1 
ATOM   3649 C  CD  . PRO   B 1 174 ? 6.694   40.252  10.384  1.00 42.68  ? 179 PRO   B CD  1 
ATOM   3650 N  N   . GLY   B 1 175 ? 7.654   40.253  14.930  1.00 40.53  ? 180 GLY   B N   1 
ATOM   3651 C  CA  . GLY   B 1 175 ? 7.578   39.415  16.120  1.00 40.11  ? 180 GLY   B CA  1 
ATOM   3652 C  C   . GLY   B 1 175 ? 8.622   38.314  16.201  1.00 42.02  ? 180 GLY   B C   1 
ATOM   3653 O  O   . GLY   B 1 175 ? 8.585   37.524  17.145  1.00 41.14  ? 180 GLY   B O   1 
ATOM   3654 N  N   . PHE   B 1 176 ? 9.584   38.277  15.252  1.00 38.46  ? 181 PHE   B N   1 
ATOM   3655 C  CA  . PHE   B 1 176 ? 10.637  37.250  15.161  1.00 37.57  ? 181 PHE   B CA  1 
ATOM   3656 C  C   . PHE   B 1 176 ? 12.074  37.772  15.400  1.00 43.74  ? 181 PHE   B C   1 
ATOM   3657 O  O   . PHE   B 1 176 ? 13.012  36.973  15.370  1.00 43.73  ? 181 PHE   B O   1 
ATOM   3658 C  CB  . PHE   B 1 176 ? 10.574  36.570  13.775  1.00 38.20  ? 181 PHE   B CB  1 
ATOM   3659 C  CG  . PHE   B 1 176 ? 9.552   35.467  13.594  1.00 37.90  ? 181 PHE   B CG  1 
ATOM   3660 C  CD1 . PHE   B 1 176 ? 8.195   35.757  13.535  1.00 39.34  ? 181 PHE   B CD1 1 
ATOM   3661 C  CD2 . PHE   B 1 176 ? 9.955   34.153  13.373  1.00 39.73  ? 181 PHE   B CD2 1 
ATOM   3662 C  CE1 . PHE   B 1 176 ? 7.251   34.741  13.341  1.00 40.18  ? 181 PHE   B CE1 1 
ATOM   3663 C  CE2 . PHE   B 1 176 ? 9.014   33.135  13.186  1.00 41.98  ? 181 PHE   B CE2 1 
ATOM   3664 C  CZ  . PHE   B 1 176 ? 7.669   33.432  13.171  1.00 39.44  ? 181 PHE   B CZ  1 
ATOM   3665 N  N   . SER   B 1 177 ? 12.257  39.095  15.625  1.00 41.99  ? 182 SER   B N   1 
ATOM   3666 C  CA  . SER   B 1 177 ? 13.583  39.702  15.814  1.00 42.55  ? 182 SER   B CA  1 
ATOM   3667 C  C   . SER   B 1 177 ? 14.399  39.088  16.959  1.00 46.06  ? 182 SER   B C   1 
ATOM   3668 O  O   . SER   B 1 177 ? 15.627  39.038  16.867  1.00 46.24  ? 182 SER   B O   1 
ATOM   3669 C  CB  . SER   B 1 177 ? 13.478  41.217  15.978  1.00 45.86  ? 182 SER   B CB  1 
ATOM   3670 O  OG  . SER   B 1 177 ? 12.679  41.544  17.100  1.00 53.10  ? 182 SER   B OG  1 
ATOM   3671 N  N   . TRP   B 1 178 ? 13.711  38.575  17.999  1.00 41.79  ? 183 TRP   B N   1 
ATOM   3672 C  CA  . TRP   B 1 178 ? 14.318  37.940  19.169  1.00 41.22  ? 183 TRP   B CA  1 
ATOM   3673 C  C   . TRP   B 1 178 ? 15.095  36.627  18.863  1.00 45.77  ? 183 TRP   B C   1 
ATOM   3674 O  O   . TRP   B 1 178 ? 15.976  36.246  19.642  1.00 43.39  ? 183 TRP   B O   1 
ATOM   3675 C  CB  . TRP   B 1 178 ? 13.251  37.690  20.238  1.00 39.50  ? 183 TRP   B CB  1 
ATOM   3676 C  CG  . TRP   B 1 178 ? 12.191  36.699  19.833  1.00 39.81  ? 183 TRP   B CG  1 
ATOM   3677 C  CD1 . TRP   B 1 178 ? 11.001  36.971  19.222  1.00 42.47  ? 183 TRP   B CD1 1 
ATOM   3678 C  CD2 . TRP   B 1 178 ? 12.226  35.277  20.029  1.00 39.24  ? 183 TRP   B CD2 1 
ATOM   3679 N  NE1 . TRP   B 1 178 ? 10.301  35.806  19.007  1.00 41.43  ? 183 TRP   B NE1 1 
ATOM   3680 C  CE2 . TRP   B 1 178 ? 11.023  34.752  19.506  1.00 42.70  ? 183 TRP   B CE2 1 
ATOM   3681 C  CE3 . TRP   B 1 178 ? 13.159  34.392  20.603  1.00 40.40  ? 183 TRP   B CE3 1 
ATOM   3682 C  CZ2 . TRP   B 1 178 ? 10.741  33.379  19.507  1.00 41.51  ? 183 TRP   B CZ2 1 
ATOM   3683 C  CZ3 . TRP   B 1 178 ? 12.882  33.029  20.594  1.00 41.45  ? 183 TRP   B CZ3 1 
ATOM   3684 C  CH2 . TRP   B 1 178 ? 11.676  32.540  20.075  1.00 41.97  ? 183 TRP   B CH2 1 
ATOM   3685 N  N   . ILE   B 1 179 ? 14.732  35.922  17.768  1.00 44.92  ? 184 ILE   B N   1 
ATOM   3686 C  CA  . ILE   B 1 179 ? 15.337  34.634  17.389  1.00 45.31  ? 184 ILE   B CA  1 
ATOM   3687 C  C   . ILE   B 1 179 ? 16.751  34.767  16.849  1.00 51.67  ? 184 ILE   B C   1 
ATOM   3688 O  O   . ILE   B 1 179 ? 17.022  35.588  15.974  1.00 52.80  ? 184 ILE   B O   1 
ATOM   3689 C  CB  . ILE   B 1 179 ? 14.450  33.818  16.398  1.00 48.41  ? 184 ILE   B CB  1 
ATOM   3690 C  CG1 . ILE   B 1 179 ? 13.004  33.767  16.871  1.00 48.76  ? 184 ILE   B CG1 1 
ATOM   3691 C  CG2 . ILE   B 1 179 ? 15.004  32.384  16.167  1.00 49.16  ? 184 ILE   B CG2 1 
ATOM   3692 C  CD1 . ILE   B 1 179 ? 12.032  33.594  15.840  1.00 56.18  ? 184 ILE   B CD1 1 
ATOM   3693 N  N   . LYS   B 1 180 ? 17.633  33.909  17.350  1.00 49.06  ? 185 LYS   B N   1 
ATOM   3694 C  CA  . LYS   B 1 180 ? 19.003  33.785  16.886  1.00 49.91  ? 185 LYS   B CA  1 
ATOM   3695 C  C   . LYS   B 1 180 ? 19.127  32.338  16.359  1.00 52.94  ? 185 LYS   B C   1 
ATOM   3696 O  O   . LYS   B 1 180 ? 18.899  31.418  17.150  1.00 52.55  ? 185 LYS   B O   1 
ATOM   3697 C  CB  . LYS   B 1 180 ? 19.998  34.056  18.034  1.00 53.71  ? 185 LYS   B CB  1 
ATOM   3698 C  CG  . LYS   B 1 180 ? 20.109  35.537  18.392  1.00 79.95  ? 185 LYS   B CG  1 
ATOM   3699 C  CD  . LYS   B 1 180 ? 20.763  35.749  19.752  1.00 96.09  ? 185 LYS   B CD  1 
ATOM   3700 C  CE  . LYS   B 1 180 ? 20.574  37.157  20.275  1.00 111.04 ? 185 LYS   B CE  1 
ATOM   3701 N  NZ  . LYS   B 1 180 ? 19.206  37.372  20.820  1.00 121.78 ? 185 LYS   B NZ  1 
ATOM   3702 N  N   . PRO   B 1 181 ? 19.399  32.097  15.042  1.00 48.67  ? 186 PRO   B N   1 
ATOM   3703 C  CA  . PRO   B 1 181 ? 19.547  30.700  14.569  1.00 47.49  ? 186 PRO   B CA  1 
ATOM   3704 C  C   . PRO   B 1 181 ? 20.535  29.959  15.473  1.00 48.50  ? 186 PRO   B C   1 
ATOM   3705 O  O   . PRO   B 1 181 ? 21.626  30.459  15.741  1.00 47.61  ? 186 PRO   B O   1 
ATOM   3706 C  CB  . PRO   B 1 181 ? 20.054  30.856  13.135  1.00 49.61  ? 186 PRO   B CB  1 
ATOM   3707 C  CG  . PRO   B 1 181 ? 19.609  32.221  12.722  1.00 54.64  ? 186 PRO   B CG  1 
ATOM   3708 C  CD  . PRO   B 1 181 ? 19.668  33.063  13.955  1.00 50.47  ? 186 PRO   B CD  1 
ATOM   3709 N  N   . CYS   B 1 182 ? 20.098  28.827  16.041  1.00 43.91  ? 187 CYS   B N   1 
ATOM   3710 C  CA  . CYS   B 1 182 ? 20.872  28.111  17.053  1.00 43.32  ? 187 CYS   B CA  1 
ATOM   3711 C  C   . CYS   B 1 182 ? 21.435  26.760  16.612  1.00 48.23  ? 187 CYS   B C   1 
ATOM   3712 O  O   . CYS   B 1 182 ? 22.373  26.271  17.243  1.00 50.66  ? 187 CYS   B O   1 
ATOM   3713 C  CB  . CYS   B 1 182 ? 20.047  27.968  18.332  1.00 42.91  ? 187 CYS   B CB  1 
ATOM   3714 S  SG  . CYS   B 1 182 ? 18.345  27.388  18.059  1.00 46.57  ? 187 CYS   B SG  1 
ATOM   3715 N  N   . ILE   B 1 183 ? 20.868  26.136  15.584  1.00 42.46  ? 188 ILE   B N   1 
ATOM   3716 C  CA  . ILE   B 1 183 ? 21.357  24.813  15.185  1.00 41.96  ? 188 ILE   B CA  1 
ATOM   3717 C  C   . ILE   B 1 183 ? 22.007  24.828  13.835  1.00 40.79  ? 188 ILE   B C   1 
ATOM   3718 O  O   . ILE   B 1 183 ? 21.561  25.558  12.959  1.00 39.42  ? 188 ILE   B O   1 
ATOM   3719 C  CB  . ILE   B 1 183 ? 20.267  23.710  15.283  1.00 46.16  ? 188 ILE   B CB  1 
ATOM   3720 C  CG1 . ILE   B 1 183 ? 18.904  24.201  14.722  1.00 46.50  ? 188 ILE   B CG1 1 
ATOM   3721 C  CG2 . ILE   B 1 183 ? 20.149  23.218  16.740  1.00 48.88  ? 188 ILE   B CG2 1 
ATOM   3722 C  CD1 . ILE   B 1 183 ? 17.840  23.124  14.487  1.00 58.59  ? 188 ILE   B CD1 1 
ATOM   3723 N  N   . SER   B 1 184 ? 23.070  24.025  13.658  1.00 35.98  ? 189 SER   B N   1 
ATOM   3724 C  CA  . SER   B 1 184 ? 23.708  23.923  12.355  1.00 34.77  ? 189 SER   B CA  1 
ATOM   3725 C  C   . SER   B 1 184 ? 22.991  22.821  11.584  1.00 36.71  ? 189 SER   B C   1 
ATOM   3726 O  O   . SER   B 1 184 ? 22.350  21.945  12.192  1.00 35.59  ? 189 SER   B O   1 
ATOM   3727 C  CB  . SER   B 1 184 ? 25.200  23.623  12.495  1.00 39.02  ? 189 SER   B CB  1 
ATOM   3728 O  OG  . SER   B 1 184 ? 25.459  22.377  13.121  1.00 50.86  ? 189 SER   B OG  1 
ATOM   3729 N  N   . SER   B 1 185 ? 23.091  22.855  10.249  1.00 33.07  ? 190 SER   B N   1 
ATOM   3730 C  CA  . SER   B 1 185 ? 22.473  21.843  9.387   1.00 33.12  ? 190 SER   B CA  1 
ATOM   3731 C  C   . SER   B 1 185 ? 22.924  20.413  9.724   1.00 35.31  ? 190 SER   B C   1 
ATOM   3732 O  O   . SER   B 1 185 ? 22.161  19.481  9.475   1.00 33.91  ? 190 SER   B O   1 
ATOM   3733 C  CB  . SER   B 1 185 ? 22.740  22.162  7.919   1.00 37.24  ? 190 SER   B CB  1 
ATOM   3734 O  OG  . SER   B 1 185 ? 24.124  22.063  7.642   1.00 48.99  ? 190 SER   B OG  1 
ATOM   3735 N  N   . ALA   B 1 186 ? 24.137  20.241  10.327  1.00 30.90  ? 191 ALA   B N   1 
ATOM   3736 C  CA  . ALA   B 1 186 ? 24.677  18.931  10.719  1.00 30.41  ? 191 ALA   B CA  1 
ATOM   3737 C  C   . ALA   B 1 186 ? 24.098  18.414  12.054  1.00 31.56  ? 191 ALA   B C   1 
ATOM   3738 O  O   . ALA   B 1 186 ? 24.329  17.256  12.423  1.00 31.07  ? 191 ALA   B O   1 
ATOM   3739 C  CB  . ALA   B 1 186 ? 26.209  18.995  10.792  1.00 31.44  ? 191 ALA   B CB  1 
ATOM   3740 N  N   . SER   B 1 187 ? 23.356  19.272  12.768  1.00 28.04  ? 192 SER   B N   1 
ATOM   3741 C  CA  . SER   B 1 187 ? 22.818  18.971  14.099  1.00 27.19  ? 192 SER   B CA  1 
ATOM   3742 C  C   . SER   B 1 187 ? 21.322  18.628  14.159  1.00 26.59  ? 192 SER   B C   1 
ATOM   3743 O  O   . SER   B 1 187 ? 20.791  18.496  15.260  1.00 25.22  ? 192 SER   B O   1 
ATOM   3744 C  CB  . SER   B 1 187 ? 23.133  20.111  15.061  1.00 31.33  ? 192 SER   B CB  1 
ATOM   3745 O  OG  . SER   B 1 187 ? 24.541  20.245  15.161  1.00 38.43  ? 192 SER   B OG  1 
ATOM   3746 N  N   . ILE   B 1 188 ? 20.689  18.413  13.006  1.00 26.64  ? 193 ILE   B N   1 
ATOM   3747 C  CA  . ILE   B 1 188 ? 19.271  18.004  12.891  1.00 25.26  ? 193 ILE   B CA  1 
ATOM   3748 C  C   . ILE   B 1 188 ? 19.166  16.799  11.961  1.00 25.95  ? 193 ILE   B C   1 
ATOM   3749 O  O   . ILE   B 1 188 ? 19.732  16.818  10.869  1.00 24.62  ? 193 ILE   B O   1 
ATOM   3750 C  CB  . ILE   B 1 188 ? 18.308  19.170  12.448  1.00 27.86  ? 193 ILE   B CB  1 
ATOM   3751 C  CG1 . ILE   B 1 188 ? 16.811  18.700  12.398  1.00 27.53  ? 193 ILE   B CG1 1 
ATOM   3752 C  CG2 . ILE   B 1 188 ? 18.717  19.841  11.104  1.00 27.89  ? 193 ILE   B CG2 1 
ATOM   3753 C  CD1 . ILE   B 1 188 ? 15.745  19.797  12.244  1.00 26.89  ? 193 ILE   B CD1 1 
ATOM   3754 N  N   . VAL   B 1 189 ? 18.439  15.749  12.384  1.00 23.18  ? 194 VAL   B N   1 
ATOM   3755 C  CA  . VAL   B 1 189 ? 18.190  14.595  11.530  1.00 21.57  ? 194 VAL   B CA  1 
ATOM   3756 C  C   . VAL   B 1 189 ? 16.679  14.414  11.507  1.00 22.56  ? 194 VAL   B C   1 
ATOM   3757 O  O   . VAL   B 1 189 ? 16.072  14.445  12.574  1.00 22.25  ? 194 VAL   B O   1 
ATOM   3758 C  CB  . VAL   B 1 189 ? 18.889  13.305  12.019  1.00 24.54  ? 194 VAL   B CB  1 
ATOM   3759 C  CG1 . VAL   B 1 189 ? 18.416  12.090  11.217  1.00 24.46  ? 194 VAL   B CG1 1 
ATOM   3760 C  CG2 . VAL   B 1 189 ? 20.411  13.446  11.902  1.00 24.53  ? 194 VAL   B CG2 1 
ATOM   3761 N  N   . TYR   B 1 190 ? 16.106  14.220  10.308  1.00 21.42  ? 195 TYR   B N   1 
ATOM   3762 C  CA  . TYR   B 1 190 ? 14.668  13.973  10.137  1.00 21.50  ? 195 TYR   B CA  1 
ATOM   3763 C  C   . TYR   B 1 190 ? 14.410  12.462  10.062  1.00 24.12  ? 195 TYR   B C   1 
ATOM   3764 O  O   . TYR   B 1 190 ? 15.191  11.713  9.437   1.00 23.99  ? 195 TYR   B O   1 
ATOM   3765 C  CB  . TYR   B 1 190 ? 14.177  14.563  8.809   1.00 23.09  ? 195 TYR   B CB  1 
ATOM   3766 C  CG  . TYR   B 1 190 ? 14.072  16.070  8.813   1.00 23.06  ? 195 TYR   B CG  1 
ATOM   3767 C  CD1 . TYR   B 1 190 ? 12.941  16.709  9.322   1.00 23.61  ? 195 TYR   B CD1 1 
ATOM   3768 C  CD2 . TYR   B 1 190 ? 15.102  16.861  8.313   1.00 23.70  ? 195 TYR   B CD2 1 
ATOM   3769 C  CE1 . TYR   B 1 190 ? 12.819  18.097  9.289   1.00 23.96  ? 195 TYR   B CE1 1 
ATOM   3770 C  CE2 . TYR   B 1 190 ? 14.995  18.250  8.288   1.00 24.34  ? 195 TYR   B CE2 1 
ATOM   3771 C  CZ  . TYR   B 1 190 ? 13.837  18.860  8.751   1.00 30.23  ? 195 TYR   B CZ  1 
ATOM   3772 O  OH  . TYR   B 1 190 ? 13.692  20.220  8.712   1.00 28.47  ? 195 TYR   B OH  1 
ATOM   3773 N  N   . ILE   B 1 191 ? 13.228  12.027  10.554  1.00 21.21  ? 196 ILE   B N   1 
ATOM   3774 C  CA  . ILE   B 1 191 ? 12.838  10.639  10.420  1.00 20.22  ? 196 ILE   B CA  1 
ATOM   3775 C  C   . ILE   B 1 191 ? 11.365  10.663  10.060  1.00 22.86  ? 196 ILE   B C   1 
ATOM   3776 O  O   . ILE   B 1 191 ? 10.585  11.268  10.794  1.00 23.25  ? 196 ILE   B O   1 
ATOM   3777 C  CB  . ILE   B 1 191 ? 13.066  9.802   11.715  1.00 21.62  ? 196 ILE   B CB  1 
ATOM   3778 C  CG1 . ILE   B 1 191 ? 14.574  9.787   12.123  1.00 22.00  ? 196 ILE   B CG1 1 
ATOM   3779 C  CG2 . ILE   B 1 191 ? 12.510  8.361   11.531  1.00 21.73  ? 196 ILE   B CG2 1 
ATOM   3780 C  CD1 . ILE   B 1 191 ? 14.801  9.137   13.543  1.00 22.44  ? 196 ILE   B CD1 1 
ATOM   3781 N  N   . GLY   B 1 192 ? 11.005  9.939   9.006   1.00 20.49  ? 197 GLY   B N   1 
ATOM   3782 C  CA  . GLY   B 1 192 ? 9.594   9.734   8.652   1.00 20.93  ? 197 GLY   B CA  1 
ATOM   3783 C  C   . GLY   B 1 192 ? 9.088   10.453  7.419   1.00 22.71  ? 197 GLY   B C   1 
ATOM   3784 O  O   . GLY   B 1 192 ? 7.918   10.321  7.079   1.00 22.08  ? 197 GLY   B O   1 
ATOM   3785 N  N   . LEU   B 1 193 ? 9.925   11.279  6.792   1.00 20.55  ? 198 LEU   B N   1 
ATOM   3786 C  CA  . LEU   B 1 193 ? 9.521   12.148  5.684   1.00 22.07  ? 198 LEU   B CA  1 
ATOM   3787 C  C   . LEU   B 1 193 ? 8.827   11.424  4.550   1.00 23.22  ? 198 LEU   B C   1 
ATOM   3788 O  O   . LEU   B 1 193 ? 9.274   10.359  4.103   1.00 23.11  ? 198 LEU   B O   1 
ATOM   3789 C  CB  . LEU   B 1 193 ? 10.703  12.947  5.110   1.00 22.35  ? 198 LEU   B CB  1 
ATOM   3790 C  CG  . LEU   B 1 193 ? 11.501  13.815  6.089   1.00 25.11  ? 198 LEU   B CG  1 
ATOM   3791 C  CD1 . LEU   B 1 193 ? 12.495  14.684  5.320   1.00 26.10  ? 198 LEU   B CD1 1 
ATOM   3792 C  CD2 . LEU   B 1 193 ? 10.564  14.720  6.939   1.00 25.32  ? 198 LEU   B CD2 1 
ATOM   3793 N  N   . ARG   B 1 194 ? 7.729   12.015  4.082   1.00 22.48  ? 199 ARG   B N   1 
ATOM   3794 C  CA  . ARG   B 1 194 ? 6.981   11.468  2.933   1.00 22.59  ? 199 ARG   B CA  1 
ATOM   3795 C  C   . ARG   B 1 194 ? 6.134   12.505  2.171   1.00 27.68  ? 199 ARG   B C   1 
ATOM   3796 O  O   . ARG   B 1 194 ? 5.520   12.147  1.161   1.00 27.32  ? 199 ARG   B O   1 
ATOM   3797 C  CB  . ARG   B 1 194 ? 6.123   10.251  3.311   1.00 22.12  ? 199 ARG   B CB  1 
ATOM   3798 C  CG  . ARG   B 1 194 ? 5.101   10.527  4.408   1.00 23.35  ? 199 ARG   B CG  1 
ATOM   3799 C  CD  . ARG   B 1 194 ? 4.496   9.206   4.846   1.00 23.96  ? 199 ARG   B CD  1 
ATOM   3800 N  NE  . ARG   B 1 194 ? 3.423   9.363   5.838   1.00 25.56  ? 199 ARG   B NE  1 
ATOM   3801 C  CZ  . ARG   B 1 194 ? 3.597   9.501   7.151   1.00 26.13  ? 199 ARG   B CZ  1 
ATOM   3802 N  NH1 . ARG   B 1 194 ? 4.831   9.580   7.670   1.00 21.20  ? 199 ARG   B NH1 1 
ATOM   3803 N  NH2 . ARG   B 1 194 ? 2.544   9.567   7.959   1.00 23.09  ? 199 ARG   B NH2 1 
ATOM   3804 N  N   . ASP   B 1 195 ? 6.106   13.763  2.624   1.00 24.52  ? 200 ASP   B N   1 
ATOM   3805 C  CA  . ASP   B 1 195 ? 5.332   14.813  1.954   1.00 25.22  ? 200 ASP   B CA  1 
ATOM   3806 C  C   . ASP   B 1 195 ? 6.195   16.057  1.990   1.00 28.55  ? 200 ASP   B C   1 
ATOM   3807 O  O   . ASP   B 1 195 ? 6.085   16.866  2.909   1.00 28.78  ? 200 ASP   B O   1 
ATOM   3808 C  CB  . ASP   B 1 195 ? 3.999   15.006  2.698   1.00 27.49  ? 200 ASP   B CB  1 
ATOM   3809 C  CG  . ASP   B 1 195 ? 3.093   16.095  2.145   1.00 37.74  ? 200 ASP   B CG  1 
ATOM   3810 O  OD1 . ASP   B 1 195 ? 3.211   16.408  0.941   1.00 38.34  ? 200 ASP   B OD1 1 
ATOM   3811 O  OD2 . ASP   B 1 195 ? 2.215   16.578  2.903   1.00 33.91  ? 200 ASP   B OD2 1 
ATOM   3812 N  N   . VAL   B 1 196 ? 7.136   16.134  1.051   1.00 25.22  ? 201 VAL   B N   1 
ATOM   3813 C  CA  . VAL   B 1 196 ? 8.149   17.193  1.005   1.00 25.07  ? 201 VAL   B CA  1 
ATOM   3814 C  C   . VAL   B 1 196 ? 7.910   18.081  -0.214  1.00 29.32  ? 201 VAL   B C   1 
ATOM   3815 O  O   . VAL   B 1 196 ? 7.836   17.587  -1.339  1.00 28.81  ? 201 VAL   B O   1 
ATOM   3816 C  CB  . VAL   B 1 196 ? 9.554   16.526  0.992   1.00 27.43  ? 201 VAL   B CB  1 
ATOM   3817 C  CG1 . VAL   B 1 196 ? 10.666  17.564  1.044   1.00 27.59  ? 201 VAL   B CG1 1 
ATOM   3818 C  CG2 . VAL   B 1 196 ? 9.698   15.525  2.153   1.00 26.07  ? 201 VAL   B CG2 1 
ATOM   3819 N  N   . ASP   B 1 197 ? 7.740   19.393  0.020   1.00 26.87  ? 202 ASP   B N   1 
ATOM   3820 C  CA  . ASP   B 1 197 ? 7.522   20.352  -1.063  1.00 26.64  ? 202 ASP   B CA  1 
ATOM   3821 C  C   . ASP   B 1 197 ? 8.793   20.497  -1.900  1.00 30.76  ? 202 ASP   B C   1 
ATOM   3822 O  O   . ASP   B 1 197 ? 9.896   20.342  -1.372  1.00 29.19  ? 202 ASP   B O   1 
ATOM   3823 C  CB  . ASP   B 1 197 ? 7.083   21.727  -0.495  1.00 27.74  ? 202 ASP   B CB  1 
ATOM   3824 C  CG  . ASP   B 1 197 ? 5.756   21.727  0.248   1.00 32.87  ? 202 ASP   B CG  1 
ATOM   3825 O  OD1 . ASP   B 1 197 ? 4.934   20.818  0.004   1.00 34.24  ? 202 ASP   B OD1 1 
ATOM   3826 O  OD2 . ASP   B 1 197 ? 5.514   22.673  1.028   1.00 33.01  ? 202 ASP   B OD2 1 
ATOM   3827 N  N   . PRO   B 1 198 ? 8.674   20.770  -3.228  1.00 29.91  ? 203 PRO   B N   1 
ATOM   3828 C  CA  . PRO   B 1 198 ? 9.891   20.949  -4.045  1.00 29.79  ? 203 PRO   B CA  1 
ATOM   3829 C  C   . PRO   B 1 198 ? 10.931  21.925  -3.451  1.00 31.16  ? 203 PRO   B C   1 
ATOM   3830 O  O   . PRO   B 1 198 ? 12.085  21.500  -3.377  1.00 31.30  ? 203 PRO   B O   1 
ATOM   3831 C  CB  . PRO   B 1 198 ? 9.351   21.388  -5.416  1.00 31.77  ? 203 PRO   B CB  1 
ATOM   3832 C  CG  . PRO   B 1 198 ? 7.933   20.873  -5.444  1.00 36.74  ? 203 PRO   B CG  1 
ATOM   3833 C  CD  . PRO   B 1 198 ? 7.444   20.953  -4.024  1.00 32.11  ? 203 PRO   B CD  1 
ATOM   3834 N  N   . PRO   B 1 199 ? 10.605  23.137  -2.907  1.00 28.78  ? 204 PRO   B N   1 
ATOM   3835 C  CA  . PRO   B 1 199 ? 11.669  23.964  -2.308  1.00 29.49  ? 204 PRO   B CA  1 
ATOM   3836 C  C   . PRO   B 1 199 ? 12.312  23.298  -1.085  1.00 31.13  ? 204 PRO   B C   1 
ATOM   3837 O  O   . PRO   B 1 199 ? 13.489  23.509  -0.834  1.00 29.27  ? 204 PRO   B O   1 
ATOM   3838 C  CB  . PRO   B 1 199 ? 10.952  25.253  -1.914  1.00 31.42  ? 204 PRO   B CB  1 
ATOM   3839 C  CG  . PRO   B 1 199 ? 9.523   24.925  -1.872  1.00 35.46  ? 204 PRO   B CG  1 
ATOM   3840 C  CD  . PRO   B 1 199 ? 9.300   23.825  -2.842  1.00 30.63  ? 204 PRO   B CD  1 
ATOM   3841 N  N   . GLU   B 1 200 ? 11.537  22.495  -0.326  1.00 28.37  ? 205 GLU   B N   1 
ATOM   3842 C  CA  . GLU   B 1 200 ? 12.076  21.801  0.856   1.00 27.76  ? 205 GLU   B CA  1 
ATOM   3843 C  C   . GLU   B 1 200 ? 13.102  20.738  0.448   1.00 28.21  ? 205 GLU   B C   1 
ATOM   3844 O  O   . GLU   B 1 200 ? 14.162  20.619  1.070   1.00 28.70  ? 205 GLU   B O   1 
ATOM   3845 C  CB  . GLU   B 1 200 ? 10.949  21.173  1.674   1.00 29.05  ? 205 GLU   B CB  1 
ATOM   3846 C  CG  . GLU   B 1 200 ? 10.018  22.198  2.296   1.00 30.34  ? 205 GLU   B CG  1 
ATOM   3847 C  CD  . GLU   B 1 200 ? 8.964   21.520  3.140   1.00 30.66  ? 205 GLU   B CD  1 
ATOM   3848 O  OE1 . GLU   B 1 200 ? 8.132   20.796  2.552   1.00 29.70  ? 205 GLU   B OE1 1 
ATOM   3849 O  OE2 . GLU   B 1 200 ? 9.026   21.628  4.386   1.00 27.72  ? 205 GLU   B OE2 1 
ATOM   3850 N  N   . HIS   B 1 201 ? 12.801  20.002  -0.633  1.00 27.30  ? 206 HIS   B N   1 
ATOM   3851 C  CA  . HIS   B 1 201 ? 13.701  18.997  -1.195  1.00 28.30  ? 206 HIS   B CA  1 
ATOM   3852 C  C   . HIS   B 1 201 ? 15.010  19.685  -1.586  1.00 31.42  ? 206 HIS   B C   1 
ATOM   3853 O  O   . HIS   B 1 201 ? 16.090  19.166  -1.279  1.00 29.99  ? 206 HIS   B O   1 
ATOM   3854 C  CB  . HIS   B 1 201 ? 13.063  18.308  -2.416  1.00 30.39  ? 206 HIS   B CB  1 
ATOM   3855 C  CG  . HIS   B 1 201 ? 13.969  17.302  -3.057  1.00 35.10  ? 206 HIS   B CG  1 
ATOM   3856 N  ND1 . HIS   B 1 201 ? 13.945  15.968  -2.682  1.00 37.68  ? 206 HIS   B ND1 1 
ATOM   3857 C  CD2 . HIS   B 1 201 ? 14.930  17.478  -3.996  1.00 37.00  ? 206 HIS   B CD2 1 
ATOM   3858 C  CE1 . HIS   B 1 201 ? 14.886  15.377  -3.403  1.00 37.51  ? 206 HIS   B CE1 1 
ATOM   3859 N  NE2 . HIS   B 1 201 ? 15.508  16.245  -4.205  1.00 37.77  ? 206 HIS   B NE2 1 
ATOM   3860 N  N   . PHE   B 1 202 ? 14.899  20.875  -2.231  1.00 28.53  ? 207 PHE   B N   1 
ATOM   3861 C  CA  . PHE   B 1 202 ? 16.055  21.685  -2.634  1.00 29.07  ? 207 PHE   B CA  1 
ATOM   3862 C  C   . PHE   B 1 202 ? 16.907  22.019  -1.397  1.00 31.93  ? 207 PHE   B C   1 
ATOM   3863 O  O   . PHE   B 1 202 ? 18.123  21.825  -1.425  1.00 33.04  ? 207 PHE   B O   1 
ATOM   3864 C  CB  . PHE   B 1 202 ? 15.601  22.973  -3.346  1.00 31.19  ? 207 PHE   B CB  1 
ATOM   3865 C  CG  . PHE   B 1 202 ? 16.748  23.901  -3.692  1.00 34.43  ? 207 PHE   B CG  1 
ATOM   3866 C  CD1 . PHE   B 1 202 ? 17.222  24.826  -2.768  1.00 36.98  ? 207 PHE   B CD1 1 
ATOM   3867 C  CD2 . PHE   B 1 202 ? 17.351  23.850  -4.945  1.00 39.07  ? 207 PHE   B CD2 1 
ATOM   3868 C  CE1 . PHE   B 1 202 ? 18.301  25.668  -3.082  1.00 39.47  ? 207 PHE   B CE1 1 
ATOM   3869 C  CE2 . PHE   B 1 202 ? 18.419  24.701  -5.262  1.00 42.76  ? 207 PHE   B CE2 1 
ATOM   3870 C  CZ  . PHE   B 1 202 ? 18.886  25.603  -4.329  1.00 40.43  ? 207 PHE   B CZ  1 
ATOM   3871 N  N   . ILE   B 1 203 ? 16.268  22.526  -0.322  1.00 28.79  ? 208 ILE   B N   1 
ATOM   3872 C  CA  . ILE   B 1 203 ? 16.961  22.868  0.920   1.00 29.32  ? 208 ILE   B CA  1 
ATOM   3873 C  C   . ILE   B 1 203 ? 17.649  21.643  1.521   1.00 30.76  ? 208 ILE   B C   1 
ATOM   3874 O  O   . ILE   B 1 203 ? 18.833  21.708  1.846   1.00 29.30  ? 208 ILE   B O   1 
ATOM   3875 C  CB  . ILE   B 1 203 ? 16.052  23.584  1.957   1.00 32.18  ? 208 ILE   B CB  1 
ATOM   3876 C  CG1 . ILE   B 1 203 ? 15.576  24.962  1.423   1.00 32.67  ? 208 ILE   B CG1 1 
ATOM   3877 C  CG2 . ILE   B 1 203 ? 16.778  23.745  3.308   1.00 32.18  ? 208 ILE   B CG2 1 
ATOM   3878 C  CD1 . ILE   B 1 203 ? 14.260  25.501  2.054   1.00 33.14  ? 208 ILE   B CD1 1 
ATOM   3879 N  N   . LEU   B 1 204 ? 16.916  20.530  1.674   1.00 29.01  ? 209 LEU   B N   1 
ATOM   3880 C  CA  . LEU   B 1 204 ? 17.524  19.333  2.261   1.00 29.10  ? 209 LEU   B CA  1 
ATOM   3881 C  C   . LEU   B 1 204 ? 18.748  18.872  1.470   1.00 32.80  ? 209 LEU   B C   1 
ATOM   3882 O  O   . LEU   B 1 204 ? 19.779  18.576  2.062   1.00 30.36  ? 209 LEU   B O   1 
ATOM   3883 C  CB  . LEU   B 1 204 ? 16.513  18.188  2.385   1.00 28.56  ? 209 LEU   B CB  1 
ATOM   3884 C  CG  . LEU   B 1 204 ? 15.294  18.411  3.287   1.00 31.74  ? 209 LEU   B CG  1 
ATOM   3885 C  CD1 . LEU   B 1 204 ? 14.323  17.250  3.114   1.00 31.23  ? 209 LEU   B CD1 1 
ATOM   3886 C  CD2 . LEU   B 1 204 ? 15.692  18.579  4.760   1.00 31.36  ? 209 LEU   B CD2 1 
ATOM   3887 N  N   . LYS   B 1 205 ? 18.641  18.858  0.133   1.00 31.36  ? 210 LYS   B N   1 
ATOM   3888 C  CA  . LYS   B 1 205 ? 19.746  18.410  -0.708  1.00 31.67  ? 210 LYS   B CA  1 
ATOM   3889 C  C   . LYS   B 1 205 ? 20.925  19.393  -0.701  1.00 34.99  ? 210 LYS   B C   1 
ATOM   3890 O  O   . LYS   B 1 205 ? 22.062  18.991  -0.431  1.00 34.49  ? 210 LYS   B O   1 
ATOM   3891 C  CB  . LYS   B 1 205 ? 19.263  18.141  -2.147  1.00 34.11  ? 210 LYS   B CB  1 
ATOM   3892 C  CG  . LYS   B 1 205 ? 18.363  16.909  -2.293  1.00 49.07  ? 210 LYS   B CG  1 
ATOM   3893 C  CD  . LYS   B 1 205 ? 19.144  15.585  -2.262  1.00 60.61  ? 210 LYS   B CD  1 
ATOM   3894 C  CE  . LYS   B 1 205 ? 18.233  14.388  -2.325  1.00 73.75  ? 210 LYS   B CE  1 
ATOM   3895 N  NZ  . LYS   B 1 205 ? 18.993  13.118  -2.194  1.00 87.69  ? 210 LYS   B NZ  1 
ATOM   3896 N  N   . ASN   B 1 206 ? 20.651  20.673  -0.970  1.00 31.92  ? 211 ASN   B N   1 
ATOM   3897 C  CA  . ASN   B 1 206 ? 21.725  21.663  -1.099  1.00 32.21  ? 211 ASN   B CA  1 
ATOM   3898 C  C   . ASN   B 1 206 ? 22.408  22.042  0.214   1.00 35.82  ? 211 ASN   B C   1 
ATOM   3899 O  O   . ASN   B 1 206 ? 23.579  22.434  0.181   1.00 35.56  ? 211 ASN   B O   1 
ATOM   3900 C  CB  . ASN   B 1 206 ? 21.237  22.885  -1.852  1.00 35.32  ? 211 ASN   B CB  1 
ATOM   3901 C  CG  . ASN   B 1 206 ? 21.009  22.568  -3.311  1.00 56.98  ? 211 ASN   B CG  1 
ATOM   3902 O  OD1 . ASN   B 1 206 ? 19.891  22.268  -3.739  1.00 51.35  ? 211 ASN   B OD1 1 
ATOM   3903 N  ND2 . ASN   B 1 206 ? 22.081  22.513  -4.084  1.00 48.74  ? 211 ASN   B ND2 1 
ATOM   3904 N  N   . TYR   B 1 207 ? 21.740  21.854  1.366   1.00 31.82  ? 212 TYR   B N   1 
ATOM   3905 C  CA  . TYR   B 1 207 ? 22.369  22.152  2.651   1.00 31.68  ? 212 TYR   B CA  1 
ATOM   3906 C  C   . TYR   B 1 207 ? 22.849  20.885  3.363   1.00 33.35  ? 212 TYR   B C   1 
ATOM   3907 O  O   . TYR   B 1 207 ? 23.336  20.955  4.490   1.00 33.76  ? 212 TYR   B O   1 
ATOM   3908 C  CB  . TYR   B 1 207 ? 21.484  23.033  3.540   1.00 32.59  ? 212 TYR   B CB  1 
ATOM   3909 C  CG  . TYR   B 1 207 ? 21.265  24.415  2.965   1.00 32.98  ? 212 TYR   B CG  1 
ATOM   3910 C  CD1 . TYR   B 1 207 ? 20.304  24.638  1.979   1.00 34.34  ? 212 TYR   B CD1 1 
ATOM   3911 C  CD2 . TYR   B 1 207 ? 22.039  25.496  3.384   1.00 33.59  ? 212 TYR   B CD2 1 
ATOM   3912 C  CE1 . TYR   B 1 207 ? 20.109  25.904  1.431   1.00 35.44  ? 212 TYR   B CE1 1 
ATOM   3913 C  CE2 . TYR   B 1 207 ? 21.831  26.776  2.865   1.00 34.42  ? 212 TYR   B CE2 1 
ATOM   3914 C  CZ  . TYR   B 1 207 ? 20.871  26.972  1.880   1.00 38.97  ? 212 TYR   B CZ  1 
ATOM   3915 O  OH  . TYR   B 1 207 ? 20.652  28.220  1.345   1.00 38.87  ? 212 TYR   B OH  1 
ATOM   3916 N  N   . ASP   B 1 208 ? 22.767  19.743  2.663   1.00 30.96  ? 213 ASP   B N   1 
ATOM   3917 C  CA  . ASP   B 1 208 ? 23.229  18.430  3.117   1.00 30.88  ? 213 ASP   B CA  1 
ATOM   3918 C  C   . ASP   B 1 208 ? 22.666  18.081  4.501   1.00 32.68  ? 213 ASP   B C   1 
ATOM   3919 O  O   . ASP   B 1 208 ? 23.393  17.655  5.402   1.00 31.19  ? 213 ASP   B O   1 
ATOM   3920 C  CB  . ASP   B 1 208 ? 24.778  18.336  3.063   1.00 34.22  ? 213 ASP   B CB  1 
ATOM   3921 C  CG  . ASP   B 1 208 ? 25.336  16.918  2.965   1.00 53.47  ? 213 ASP   B CG  1 
ATOM   3922 O  OD1 . ASP   B 1 208 ? 24.609  16.018  2.467   1.00 55.63  ? 213 ASP   B OD1 1 
ATOM   3923 O  OD2 . ASP   B 1 208 ? 26.500  16.707  3.382   1.00 61.12  ? 213 ASP   B OD2 1 
ATOM   3924 N  N   . ILE   B 1 209 ? 21.343  18.308  4.666   1.00 28.70  ? 214 ILE   B N   1 
ATOM   3925 C  CA  . ILE   B 1 209 ? 20.658  17.985  5.907   1.00 27.41  ? 214 ILE   B CA  1 
ATOM   3926 C  C   . ILE   B 1 209 ? 20.274  16.518  5.779   1.00 29.23  ? 214 ILE   B C   1 
ATOM   3927 O  O   . ILE   B 1 209 ? 19.624  16.146  4.809   1.00 28.83  ? 214 ILE   B O   1 
ATOM   3928 C  CB  . ILE   B 1 209 ? 19.408  18.879  6.120   1.00 30.11  ? 214 ILE   B CB  1 
ATOM   3929 C  CG1 . ILE   B 1 209 ? 19.824  20.382  6.222   1.00 30.24  ? 214 ILE   B CG1 1 
ATOM   3930 C  CG2 . ILE   B 1 209 ? 18.626  18.419  7.387   1.00 31.45  ? 214 ILE   B CG2 1 
ATOM   3931 C  CD1 . ILE   B 1 209 ? 18.685  21.358  6.035   1.00 33.52  ? 214 ILE   B CD1 1 
ATOM   3932 N  N   . GLN   B 1 210 ? 20.674  15.716  6.758   1.00 25.91  ? 215 GLN   B N   1 
ATOM   3933 C  CA  . GLN   B 1 210 ? 20.437  14.267  6.760   1.00 26.15  ? 215 GLN   B CA  1 
ATOM   3934 C  C   . GLN   B 1 210 ? 19.017  13.929  7.134   1.00 28.51  ? 215 GLN   B C   1 
ATOM   3935 O  O   . GLN   B 1 210 ? 18.463  14.487  8.089   1.00 27.34  ? 215 GLN   B O   1 
ATOM   3936 C  CB  . GLN   B 1 210 ? 21.432  13.549  7.669   1.00 27.90  ? 215 GLN   B CB  1 
ATOM   3937 C  CG  . GLN   B 1 210 ? 22.918  13.828  7.326   1.00 33.72  ? 215 GLN   B CG  1 
ATOM   3938 C  CD  . GLN   B 1 210 ? 23.233  13.620  5.857   1.00 45.33  ? 215 GLN   B CD  1 
ATOM   3939 O  OE1 . GLN   B 1 210 ? 23.151  12.501  5.330   1.00 42.60  ? 215 GLN   B OE1 1 
ATOM   3940 N  NE2 . GLN   B 1 210 ? 23.550  14.707  5.150   1.00 36.90  ? 215 GLN   B NE2 1 
ATOM   3941 N  N   . TYR   B 1 211 ? 18.428  13.019  6.375   1.00 25.15  ? 216 TYR   B N   1 
ATOM   3942 C  CA  . TYR   B 1 211 ? 17.071  12.559  6.651   1.00 23.97  ? 216 TYR   B CA  1 
ATOM   3943 C  C   . TYR   B 1 211 ? 16.919  11.101  6.324   1.00 25.98  ? 216 TYR   B C   1 
ATOM   3944 O  O   . TYR   B 1 211 ? 17.546  10.590  5.388   1.00 26.65  ? 216 TYR   B O   1 
ATOM   3945 C  CB  . TYR   B 1 211 ? 16.017  13.396  5.917   1.00 25.30  ? 216 TYR   B CB  1 
ATOM   3946 C  CG  . TYR   B 1 211 ? 16.083  13.338  4.399   1.00 27.21  ? 216 TYR   B CG  1 
ATOM   3947 C  CD1 . TYR   B 1 211 ? 16.838  14.262  3.678   1.00 29.02  ? 216 TYR   B CD1 1 
ATOM   3948 C  CD2 . TYR   B 1 211 ? 15.320  12.418  3.684   1.00 29.24  ? 216 TYR   B CD2 1 
ATOM   3949 C  CE1 . TYR   B 1 211 ? 16.870  14.238  2.278   1.00 29.95  ? 216 TYR   B CE1 1 
ATOM   3950 C  CE2 . TYR   B 1 211 ? 15.324  12.400  2.288   1.00 30.74  ? 216 TYR   B CE2 1 
ATOM   3951 C  CZ  . TYR   B 1 211 ? 16.096  13.316  1.588   1.00 38.33  ? 216 TYR   B CZ  1 
ATOM   3952 O  OH  . TYR   B 1 211 ? 16.097  13.295  0.209   1.00 39.59  ? 216 TYR   B OH  1 
ATOM   3953 N  N   . PHE   B 1 212 ? 16.019  10.454  7.060   1.00 22.06  ? 217 PHE   B N   1 
ATOM   3954 C  CA  . PHE   B 1 212 ? 15.637  9.078   6.823   1.00 21.59  ? 217 PHE   B CA  1 
ATOM   3955 C  C   . PHE   B 1 212 ? 14.162  9.154   6.471   1.00 24.09  ? 217 PHE   B C   1 
ATOM   3956 O  O   . PHE   B 1 212 ? 13.331  9.271   7.356   1.00 25.02  ? 217 PHE   B O   1 
ATOM   3957 C  CB  . PHE   B 1 212 ? 15.907  8.181   8.043   1.00 23.26  ? 217 PHE   B CB  1 
ATOM   3958 C  CG  . PHE   B 1 212 ? 17.383  8.105   8.326   1.00 23.43  ? 217 PHE   B CG  1 
ATOM   3959 C  CD1 . PHE   B 1 212 ? 18.186  7.178   7.663   1.00 25.63  ? 217 PHE   B CD1 1 
ATOM   3960 C  CD2 . PHE   B 1 212 ? 17.975  8.966   9.245   1.00 24.20  ? 217 PHE   B CD2 1 
ATOM   3961 C  CE1 . PHE   B 1 212 ? 19.565  7.138   7.894   1.00 27.18  ? 217 PHE   B CE1 1 
ATOM   3962 C  CE2 . PHE   B 1 212 ? 19.358  8.955   9.436   1.00 27.40  ? 217 PHE   B CE2 1 
ATOM   3963 C  CZ  . PHE   B 1 212 ? 20.136  8.022   8.775   1.00 25.69  ? 217 PHE   B CZ  1 
ATOM   3964 N  N   . SER   B 1 213 ? 13.862  9.191   5.182   1.00 22.77  ? 218 SER   B N   1 
ATOM   3965 C  CA  . SER   B 1 213 ? 12.473  9.252   4.703   1.00 21.79  ? 218 SER   B CA  1 
ATOM   3966 C  C   . SER   B 1 213 ? 11.805  7.882   4.936   1.00 22.22  ? 218 SER   B C   1 
ATOM   3967 O  O   . SER   B 1 213 ? 12.476  6.905   5.304   1.00 22.44  ? 218 SER   B O   1 
ATOM   3968 C  CB  . SER   B 1 213 ? 12.456  9.562   3.216   1.00 22.62  ? 218 SER   B CB  1 
ATOM   3969 O  OG  . SER   B 1 213 ? 12.936  8.411   2.537   1.00 25.51  ? 218 SER   B OG  1 
ATOM   3970 N  N   . MET   B 1 214 ? 10.485  7.766   4.634   1.00 20.87  ? 219 MET   B N   1 
ATOM   3971 C  CA  . MET   B 1 214 ? 9.853   6.456   4.742   1.00 19.40  ? 219 MET   B CA  1 
ATOM   3972 C  C   . MET   B 1 214 ? 10.564  5.457   3.806   1.00 21.99  ? 219 MET   B C   1 
ATOM   3973 O  O   . MET   B 1 214 ? 10.704  4.277   4.143   1.00 22.24  ? 219 MET   B O   1 
ATOM   3974 C  CB  . MET   B 1 214 ? 8.352   6.508   4.383   1.00 20.58  ? 219 MET   B CB  1 
ATOM   3975 C  CG  . MET   B 1 214 ? 7.535   7.325   5.381   1.00 23.45  ? 219 MET   B CG  1 
ATOM   3976 S  SD  . MET   B 1 214 ? 7.746   6.881   7.131   1.00 24.04  ? 219 MET   B SD  1 
ATOM   3977 C  CE  . MET   B 1 214 ? 7.392   5.130   7.086   1.00 21.04  ? 219 MET   B CE  1 
ATOM   3978 N  N   . ARG   B 1 215 ? 11.049  5.945   2.648   1.00 21.96  ? 220 ARG   B N   1 
ATOM   3979 C  CA  . ARG   B 1 215 ? 11.729  5.040   1.716   1.00 21.86  ? 220 ARG   B CA  1 
ATOM   3980 C  C   . ARG   B 1 215 ? 13.051  4.547   2.353   1.00 25.02  ? 220 ARG   B C   1 
ATOM   3981 O  O   . ARG   B 1 215 ? 13.375  3.360   2.278   1.00 22.35  ? 220 ARG   B O   1 
ATOM   3982 C  CB  . ARG   B 1 215 ? 11.996  5.810   0.435   1.00 22.67  ? 220 ARG   B CB  1 
ATOM   3983 C  CG  . ARG   B 1 215 ? 12.747  4.990   -0.579  1.00 26.99  ? 220 ARG   B CG  1 
ATOM   3984 C  CD  . ARG   B 1 215 ? 13.146  5.828   -1.745  1.00 31.11  ? 220 ARG   B CD  1 
ATOM   3985 N  NE  . ARG   B 1 215 ? 14.341  5.244   -2.318  1.00 31.77  ? 220 ARG   B NE  1 
ATOM   3986 C  CZ  . ARG   B 1 215 ? 14.350  4.317   -3.256  1.00 48.32  ? 220 ARG   B CZ  1 
ATOM   3987 N  NH1 . ARG   B 1 215 ? 13.199  3.877   -3.781  1.00 37.69  ? 220 ARG   B NH1 1 
ATOM   3988 N  NH2 . ARG   B 1 215 ? 15.506  3.820   -3.689  1.00 34.44  ? 220 ARG   B NH2 1 
ATOM   3989 N  N   . ASP   B 1 216 ? 13.756  5.428   3.074   1.00 22.23  ? 221 ASP   B N   1 
ATOM   3990 C  CA  . ASP   B 1 216 ? 14.974  5.001   3.780   1.00 22.40  ? 221 ASP   B CA  1 
ATOM   3991 C  C   . ASP   B 1 216 ? 14.661  3.985   4.859   1.00 23.72  ? 221 ASP   B C   1 
ATOM   3992 O  O   . ASP   B 1 216 ? 15.434  3.065   5.061   1.00 23.30  ? 221 ASP   B O   1 
ATOM   3993 C  CB  . ASP   B 1 216 ? 15.738  6.171   4.392   1.00 23.48  ? 221 ASP   B CB  1 
ATOM   3994 C  CG  . ASP   B 1 216 ? 16.278  7.125   3.351   1.00 28.34  ? 221 ASP   B CG  1 
ATOM   3995 O  OD1 . ASP   B 1 216 ? 16.911  6.648   2.377   1.00 28.44  ? 221 ASP   B OD1 1 
ATOM   3996 O  OD2 . ASP   B 1 216 ? 16.068  8.342   3.501   1.00 27.86  ? 221 ASP   B OD2 1 
ATOM   3997 N  N   . ILE   B 1 217 ? 13.511  4.138   5.560   1.00 22.03  ? 222 ILE   B N   1 
ATOM   3998 C  CA  . ILE   B 1 217 ? 13.117  3.181   6.590   1.00 21.21  ? 222 ILE   B CA  1 
ATOM   3999 C  C   . ILE   B 1 217 ? 12.760  1.839   5.931   1.00 22.72  ? 222 ILE   B C   1 
ATOM   4000 O  O   . ILE   B 1 217 ? 13.110  0.798   6.466   1.00 22.76  ? 222 ILE   B O   1 
ATOM   4001 C  CB  . ILE   B 1 217 ? 11.945  3.732   7.449   1.00 23.38  ? 222 ILE   B CB  1 
ATOM   4002 C  CG1 . ILE   B 1 217 ? 12.368  5.089   8.128   1.00 23.32  ? 222 ILE   B CG1 1 
ATOM   4003 C  CG2 . ILE   B 1 217 ? 11.495  2.682   8.481   1.00 22.37  ? 222 ILE   B CG2 1 
ATOM   4004 C  CD1 . ILE   B 1 217 ? 11.220  5.873   8.799   1.00 25.53  ? 222 ILE   B CD1 1 
ATOM   4005 N  N   . ASP   B 1 218 ? 12.103  1.869   4.747   1.00 21.27  ? 223 ASP   B N   1 
ATOM   4006 C  CA  . ASP   B 1 218 ? 11.714  0.666   3.992   1.00 21.09  ? 223 ASP   B CA  1 
ATOM   4007 C  C   . ASP   B 1 218 ? 12.944  -0.166  3.641   1.00 23.98  ? 223 ASP   B C   1 
ATOM   4008 O  O   . ASP   B 1 218 ? 12.900  -1.397  3.645   1.00 23.02  ? 223 ASP   B O   1 
ATOM   4009 C  CB  . ASP   B 1 218 ? 10.992  1.068   2.712   1.00 21.57  ? 223 ASP   B CB  1 
ATOM   4010 C  CG  . ASP   B 1 218 ? 9.608   1.665   2.920   1.00 22.30  ? 223 ASP   B CG  1 
ATOM   4011 O  OD1 . ASP   B 1 218 ? 9.013   1.423   3.998   1.00 22.20  ? 223 ASP   B OD1 1 
ATOM   4012 O  OD2 . ASP   B 1 218 ? 9.132   2.371   2.016   1.00 25.12  ? 223 ASP   B OD2 1 
ATOM   4013 N  N   . ARG   B 1 219 ? 14.041  0.535   3.334   1.00 23.50  ? 224 ARG   B N   1 
ATOM   4014 C  CA  . ARG   B 1 219 ? 15.313  -0.080  2.942   1.00 24.56  ? 224 ARG   B CA  1 
ATOM   4015 C  C   . ARG   B 1 219 ? 16.135  -0.561  4.145   1.00 27.89  ? 224 ARG   B C   1 
ATOM   4016 O  O   . ARG   B 1 219 ? 16.563  -1.722  4.199   1.00 26.21  ? 224 ARG   B O   1 
ATOM   4017 C  CB  . ARG   B 1 219 ? 16.150  0.951   2.133   1.00 23.27  ? 224 ARG   B CB  1 
ATOM   4018 C  CG  . ARG   B 1 219 ? 15.576  1.270   0.754   1.00 29.08  ? 224 ARG   B CG  1 
ATOM   4019 C  CD  . ARG   B 1 219 ? 16.211  2.476   0.063   1.00 28.02  ? 224 ARG   B CD  1 
ATOM   4020 N  NE  . ARG   B 1 219 ? 17.672  2.356   -0.026  1.00 29.68  ? 224 ARG   B NE  1 
ATOM   4021 C  CZ  . ARG   B 1 219 ? 18.333  1.688   -0.968  1.00 43.66  ? 224 ARG   B CZ  1 
ATOM   4022 N  NH1 . ARG   B 1 219 ? 17.671  1.019   -1.909  1.00 30.32  ? 224 ARG   B NH1 1 
ATOM   4023 N  NH2 . ARG   B 1 219 ? 19.660  1.666   -0.967  1.00 33.59  ? 224 ARG   B NH2 1 
ATOM   4024 N  N   . LEU   B 1 220 ? 16.380  0.335   5.095   1.00 24.26  ? 225 LEU   B N   1 
ATOM   4025 C  CA  . LEU   B 1 220 ? 17.259  0.057   6.237   1.00 24.26  ? 225 LEU   B CA  1 
ATOM   4026 C  C   . LEU   B 1 220 ? 16.627  -0.673  7.401   1.00 26.65  ? 225 LEU   B C   1 
ATOM   4027 O  O   . LEU   B 1 220 ? 17.318  -1.410  8.102   1.00 25.48  ? 225 LEU   B O   1 
ATOM   4028 C  CB  . LEU   B 1 220 ? 17.822  1.388   6.764   1.00 24.70  ? 225 LEU   B CB  1 
ATOM   4029 C  CG  . LEU   B 1 220 ? 18.809  2.153   5.864   1.00 29.51  ? 225 LEU   B CG  1 
ATOM   4030 C  CD1 . LEU   B 1 220 ? 18.999  3.579   6.366   1.00 29.53  ? 225 LEU   B CD1 1 
ATOM   4031 C  CD2 . LEU   B 1 220 ? 20.176  1.431   5.795   1.00 31.08  ? 225 LEU   B CD2 1 
ATOM   4032 N  N   . GLY   B 1 221 ? 15.351  -0.381  7.661   1.00 22.25  ? 226 GLY   B N   1 
ATOM   4033 C  CA  . GLY   B 1 221 ? 14.693  -0.840  8.874   1.00 22.29  ? 226 GLY   B CA  1 
ATOM   4034 C  C   . GLY   B 1 221 ? 14.945  0.166   9.985   1.00 25.47  ? 226 GLY   B C   1 
ATOM   4035 O  O   . GLY   B 1 221 ? 15.996  0.830   10.024  1.00 23.99  ? 226 GLY   B O   1 
ATOM   4036 N  N   . ILE   B 1 222 ? 13.983  0.314   10.908  1.00 21.55  ? 227 ILE   B N   1 
ATOM   4037 C  CA  . ILE   B 1 222 ? 14.093  1.332   11.955  1.00 21.70  ? 227 ILE   B CA  1 
ATOM   4038 C  C   . ILE   B 1 222 ? 15.341  1.168   12.890  1.00 24.74  ? 227 ILE   B C   1 
ATOM   4039 O  O   . ILE   B 1 222 ? 15.875  2.180   13.377  1.00 24.32  ? 227 ILE   B O   1 
ATOM   4040 C  CB  . ILE   B 1 222 ? 12.745  1.420   12.749  1.00 24.23  ? 227 ILE   B CB  1 
ATOM   4041 C  CG1 . ILE   B 1 222 ? 12.617  2.760   13.507  1.00 23.84  ? 227 ILE   B CG1 1 
ATOM   4042 C  CG2 . ILE   B 1 222 ? 12.501  0.208   13.663  1.00 27.34  ? 227 ILE   B CG2 1 
ATOM   4043 C  CD1 . ILE   B 1 222 ? 12.438  3.973   12.589  1.00 24.41  ? 227 ILE   B CD1 1 
ATOM   4044 N  N   . GLN   B 1 223 ? 15.806  -0.083  13.131  1.00 23.87  ? 228 GLN   B N   1 
ATOM   4045 C  CA  . GLN   B 1 223 ? 16.985  -0.263  13.994  1.00 24.15  ? 228 GLN   B CA  1 
ATOM   4046 C  C   . GLN   B 1 223 ? 18.194  0.458   13.379  1.00 25.71  ? 228 GLN   B C   1 
ATOM   4047 O  O   . GLN   B 1 223 ? 18.875  1.218   14.069  1.00 25.69  ? 228 GLN   B O   1 
ATOM   4048 C  CB  . GLN   B 1 223 ? 17.319  -1.747  14.228  1.00 24.78  ? 228 GLN   B CB  1 
ATOM   4049 C  CG  . GLN   B 1 223 ? 18.647  -1.924  15.030  1.00 26.39  ? 228 GLN   B CG  1 
ATOM   4050 C  CD  . GLN   B 1 223 ? 19.252  -3.316  15.033  1.00 40.74  ? 228 GLN   B CD  1 
ATOM   4051 O  OE1 . GLN   B 1 223 ? 20.432  -3.521  15.363  1.00 42.25  ? 228 GLN   B OE1 1 
ATOM   4052 N  NE2 . GLN   B 1 223 ? 18.477  -4.312  14.719  1.00 28.51  ? 228 GLN   B NE2 1 
ATOM   4053 N  N   . LYS   B 1 224 ? 18.457  0.219   12.089  1.00 23.71  ? 229 LYS   B N   1 
ATOM   4054 C  CA  . LYS   B 1 224 ? 19.612  0.847   11.430  1.00 23.47  ? 229 LYS   B CA  1 
ATOM   4055 C  C   . LYS   B 1 224 ? 19.383  2.362   11.284  1.00 27.30  ? 229 LYS   B C   1 
ATOM   4056 O  O   . LYS   B 1 224 ? 20.313  3.152   11.400  1.00 25.47  ? 229 LYS   B O   1 
ATOM   4057 C  CB  . LYS   B 1 224 ? 19.889  0.182   10.082  1.00 25.23  ? 229 LYS   B CB  1 
ATOM   4058 C  CG  . LYS   B 1 224 ? 20.554  -1.189  10.253  1.00 35.18  ? 229 LYS   B CG  1 
ATOM   4059 C  CD  . LYS   B 1 224 ? 21.195  -1.645  8.955   1.00 41.30  ? 229 LYS   B CD  1 
ATOM   4060 C  CE  . LYS   B 1 224 ? 21.825  -3.017  9.078   1.00 50.62  ? 229 LYS   B CE  1 
ATOM   4061 N  NZ  . LYS   B 1 224 ? 20.805  -4.098  9.041   1.00 59.74  ? 229 LYS   B NZ  1 
ATOM   4062 N  N   . VAL   B 1 225 ? 18.118  2.772   11.101  1.00 22.09  ? 230 VAL   B N   1 
ATOM   4063 C  CA  . VAL   B 1 225 ? 17.828  4.210   11.032  1.00 20.80  ? 230 VAL   B CA  1 
ATOM   4064 C  C   . VAL   B 1 225 ? 18.242  4.902   12.352  1.00 24.94  ? 230 VAL   B C   1 
ATOM   4065 O  O   . VAL   B 1 225 ? 18.887  5.965   12.318  1.00 23.93  ? 230 VAL   B O   1 
ATOM   4066 C  CB  . VAL   B 1 225 ? 16.318  4.453   10.705  1.00 22.88  ? 230 VAL   B CB  1 
ATOM   4067 C  CG1 . VAL   B 1 225 ? 15.934  5.906   10.992  1.00 22.56  ? 230 VAL   B CG1 1 
ATOM   4068 C  CG2 . VAL   B 1 225 ? 16.025  4.097   9.247   1.00 22.76  ? 230 VAL   B CG2 1 
ATOM   4069 N  N   . MET   B 1 226 ? 17.885  4.311   13.515  1.00 22.13  ? 231 MET   B N   1 
ATOM   4070 C  CA  . MET   B 1 226 ? 18.236  4.931   14.797  1.00 21.60  ? 231 MET   B CA  1 
ATOM   4071 C  C   . MET   B 1 226 ? 19.743  4.899   15.006  1.00 26.20  ? 231 MET   B C   1 
ATOM   4072 O  O   . MET   B 1 226 ? 20.300  5.906   15.436  1.00 24.18  ? 231 MET   B O   1 
ATOM   4073 C  CB  . MET   B 1 226 ? 17.482  4.321   15.984  1.00 23.14  ? 231 MET   B CB  1 
ATOM   4074 C  CG  . MET   B 1 226 ? 15.955  4.511   15.891  1.00 24.52  ? 231 MET   B CG  1 
ATOM   4075 S  SD  . MET   B 1 226 ? 15.450  6.225   15.524  1.00 25.19  ? 231 MET   B SD  1 
ATOM   4076 C  CE  . MET   B 1 226 ? 15.964  7.051   17.033  1.00 24.13  ? 231 MET   B CE  1 
ATOM   4077 N  N   . GLU   B 1 227 ? 20.394  3.758   14.691  1.00 24.27  ? 232 GLU   B N   1 
ATOM   4078 C  CA  . GLU   B 1 227 ? 21.868  3.671   14.842  1.00 24.23  ? 232 GLU   B CA  1 
ATOM   4079 C  C   . GLU   B 1 227 ? 22.544  4.781   14.037  1.00 27.02  ? 232 GLU   B C   1 
ATOM   4080 O  O   . GLU   B 1 227 ? 23.401  5.507   14.569  1.00 27.78  ? 232 GLU   B O   1 
ATOM   4081 C  CB  . GLU   B 1 227 ? 22.389  2.320   14.371  1.00 25.79  ? 232 GLU   B CB  1 
ATOM   4082 C  CG  . GLU   B 1 227 ? 22.131  1.211   15.372  1.00 31.94  ? 232 GLU   B CG  1 
ATOM   4083 C  CD  . GLU   B 1 227 ? 22.308  -0.186  14.805  1.00 40.85  ? 232 GLU   B CD  1 
ATOM   4084 O  OE1 . GLU   B 1 227 ? 22.596  -0.312  13.591  1.00 37.23  ? 232 GLU   B OE1 1 
ATOM   4085 O  OE2 . GLU   B 1 227 ? 22.104  -1.158  15.566  1.00 39.74  ? 232 GLU   B OE2 1 
ATOM   4086 N  N   . ARG   B 1 228 ? 22.146  4.931   12.763  1.00 23.51  ? 233 ARG   B N   1 
ATOM   4087 C  CA  . ARG   B 1 228 ? 22.727  5.953   11.888  1.00 24.43  ? 233 ARG   B CA  1 
ATOM   4088 C  C   . ARG   B 1 228 ? 22.423  7.359   12.366  1.00 28.13  ? 233 ARG   B C   1 
ATOM   4089 O  O   . ARG   B 1 228 ? 23.297  8.220   12.305  1.00 27.80  ? 233 ARG   B O   1 
ATOM   4090 C  CB  . ARG   B 1 228 ? 22.308  5.750   10.436  1.00 24.26  ? 233 ARG   B CB  1 
ATOM   4091 C  CG  . ARG   B 1 228 ? 22.884  4.453   9.871   1.00 27.90  ? 233 ARG   B CG  1 
ATOM   4092 C  CD  . ARG   B 1 228 ? 22.509  4.266   8.426   1.00 32.73  ? 233 ARG   B CD  1 
ATOM   4093 N  NE  . ARG   B 1 228 ? 23.099  3.046   7.871   1.00 44.04  ? 233 ARG   B NE  1 
ATOM   4094 C  CZ  . ARG   B 1 228 ? 23.350  2.864   6.580   1.00 52.08  ? 233 ARG   B CZ  1 
ATOM   4095 N  NH1 . ARG   B 1 228 ? 23.073  3.820   5.702   1.00 42.22  ? 233 ARG   B NH1 1 
ATOM   4096 N  NH2 . ARG   B 1 228 ? 23.866  1.719   6.154   1.00 45.85  ? 233 ARG   B NH2 1 
ATOM   4097 N  N   . THR   B 1 229 ? 21.197  7.591   12.872  1.00 24.61  ? 234 THR   B N   1 
ATOM   4098 C  CA  . THR   B 1 229 ? 20.811  8.899   13.397  1.00 24.29  ? 234 THR   B CA  1 
ATOM   4099 C  C   . THR   B 1 229 ? 21.751  9.309   14.539  1.00 27.23  ? 234 THR   B C   1 
ATOM   4100 O  O   . THR   B 1 229 ? 22.231  10.454  14.558  1.00 28.55  ? 234 THR   B O   1 
ATOM   4101 C  CB  . THR   B 1 229 ? 19.346  8.883   13.864  1.00 25.93  ? 234 THR   B CB  1 
ATOM   4102 O  OG1 . THR   B 1 229 ? 18.523  8.794   12.702  1.00 23.89  ? 234 THR   B OG1 1 
ATOM   4103 C  CG2 . THR   B 1 229 ? 18.973  10.148  14.646  1.00 27.53  ? 234 THR   B CG2 1 
ATOM   4104 N  N   . PHE   B 1 230 ? 21.999  8.385   15.491  1.00 24.90  ? 235 PHE   B N   1 
ATOM   4105 C  CA  . PHE   B 1 230 ? 22.864  8.645   16.630  1.00 25.76  ? 235 PHE   B CA  1 
ATOM   4106 C  C   . PHE   B 1 230 ? 24.317  8.788   16.198  1.00 30.00  ? 235 PHE   B C   1 
ATOM   4107 O  O   . PHE   B 1 230 ? 24.996  9.654   16.737  1.00 29.07  ? 235 PHE   B O   1 
ATOM   4108 C  CB  . PHE   B 1 230 ? 22.697  7.616   17.741  1.00 27.67  ? 235 PHE   B CB  1 
ATOM   4109 C  CG  . PHE   B 1 230 ? 21.299  7.580   18.320  1.00 29.24  ? 235 PHE   B CG  1 
ATOM   4110 C  CD1 . PHE   B 1 230 ? 20.587  8.755   18.541  1.00 31.88  ? 235 PHE   B CD1 1 
ATOM   4111 C  CD2 . PHE   B 1 230 ? 20.724  6.376   18.704  1.00 32.68  ? 235 PHE   B CD2 1 
ATOM   4112 C  CE1 . PHE   B 1 230 ? 19.283  8.720   19.060  1.00 33.97  ? 235 PHE   B CE1 1 
ATOM   4113 C  CE2 . PHE   B 1 230 ? 19.427  6.344   19.238  1.00 36.31  ? 235 PHE   B CE2 1 
ATOM   4114 C  CZ  . PHE   B 1 230 ? 18.721  7.516   19.412  1.00 33.82  ? 235 PHE   B CZ  1 
ATOM   4115 N  N   . ASP   B 1 231 ? 24.761  8.030   15.192  1.00 27.45  ? 236 ASP   B N   1 
ATOM   4116 C  CA  . ASP   B 1 231 ? 26.135  8.209   14.669  1.00 27.56  ? 236 ASP   B CA  1 
ATOM   4117 C  C   . ASP   B 1 231 ? 26.312  9.650   14.158  1.00 32.33  ? 236 ASP   B C   1 
ATOM   4118 O  O   . ASP   B 1 231 ? 27.365  10.272  14.375  1.00 33.43  ? 236 ASP   B O   1 
ATOM   4119 C  CB  . ASP   B 1 231 ? 26.411  7.249   13.496  1.00 29.30  ? 236 ASP   B CB  1 
ATOM   4120 C  CG  . ASP   B 1 231 ? 26.609  5.793   13.878  1.00 37.53  ? 236 ASP   B CG  1 
ATOM   4121 O  OD1 . ASP   B 1 231 ? 26.836  5.516   15.074  1.00 38.45  ? 236 ASP   B OD1 1 
ATOM   4122 O  OD2 . ASP   B 1 231 ? 26.580  4.935   12.972  1.00 41.21  ? 236 ASP   B OD2 1 
ATOM   4123 N  N   . LEU   B 1 232 ? 25.287  10.177  13.474  1.00 28.35  ? 237 LEU   B N   1 
ATOM   4124 C  CA  . LEU   B 1 232 ? 25.341  11.522  12.897  1.00 28.39  ? 237 LEU   B CA  1 
ATOM   4125 C  C   . LEU   B 1 232 ? 25.291  12.623  13.950  1.00 32.39  ? 237 LEU   B C   1 
ATOM   4126 O  O   . LEU   B 1 232 ? 25.942  13.672  13.788  1.00 33.03  ? 237 LEU   B O   1 
ATOM   4127 C  CB  . LEU   B 1 232 ? 24.177  11.723  11.912  1.00 28.79  ? 237 LEU   B CB  1 
ATOM   4128 C  CG  . LEU   B 1 232 ? 24.238  10.943  10.594  1.00 32.60  ? 237 LEU   B CG  1 
ATOM   4129 C  CD1 . LEU   B 1 232 ? 22.876  10.903  9.940   1.00 31.17  ? 237 LEU   B CD1 1 
ATOM   4130 C  CD2 . LEU   B 1 232 ? 25.280  11.540  9.632   1.00 35.65  ? 237 LEU   B CD2 1 
ATOM   4131 N  N   . LEU   B 1 233 ? 24.511  12.404  15.012  1.00 26.87  ? 238 LEU   B N   1 
ATOM   4132 C  CA  . LEU   B 1 233 ? 24.292  13.449  16.000  1.00 26.85  ? 238 LEU   B CA  1 
ATOM   4133 C  C   . LEU   B 1 233 ? 25.150  13.359  17.249  1.00 30.29  ? 238 LEU   B C   1 
ATOM   4134 O  O   . LEU   B 1 233 ? 25.661  14.391  17.694  1.00 30.66  ? 238 LEU   B O   1 
ATOM   4135 C  CB  . LEU   B 1 233 ? 22.805  13.544  16.395  1.00 26.08  ? 238 LEU   B CB  1 
ATOM   4136 C  CG  . LEU   B 1 233 ? 21.808  13.881  15.273  1.00 28.97  ? 238 LEU   B CG  1 
ATOM   4137 C  CD1 . LEU   B 1 233 ? 20.388  13.858  15.809  1.00 29.23  ? 238 LEU   B CD1 1 
ATOM   4138 C  CD2 . LEU   B 1 233 ? 22.085  15.255  14.634  1.00 28.14  ? 238 LEU   B CD2 1 
ATOM   4139 N  N   . ILE   B 1 234 ? 25.261  12.173  17.848  1.00 28.20  ? 239 ILE   B N   1 
ATOM   4140 C  CA  . ILE   B 1 234 ? 26.001  11.975  19.102  1.00 28.88  ? 239 ILE   B CA  1 
ATOM   4141 C  C   . ILE   B 1 234 ? 27.189  11.003  18.949  1.00 33.45  ? 239 ILE   B C   1 
ATOM   4142 O  O   . ILE   B 1 234 ? 27.680  10.483  19.943  1.00 34.55  ? 239 ILE   B O   1 
ATOM   4143 C  CB  . ILE   B 1 234 ? 25.051  11.572  20.254  1.00 31.68  ? 239 ILE   B CB  1 
ATOM   4144 C  CG1 . ILE   B 1 234 ? 24.312  10.240  19.962  1.00 31.83  ? 239 ILE   B CG1 1 
ATOM   4145 C  CG2 . ILE   B 1 234 ? 24.083  12.722  20.587  1.00 32.53  ? 239 ILE   B CG2 1 
ATOM   4146 C  CD1 . ILE   B 1 234 ? 23.569  9.582   21.205  1.00 30.79  ? 239 ILE   B CD1 1 
ATOM   4147 N  N   . GLY   B 1 235 ? 27.628  10.786  17.718  1.00 32.14  ? 240 GLY   B N   1 
ATOM   4148 C  CA  . GLY   B 1 235 ? 28.746  9.891   17.438  1.00 33.36  ? 240 GLY   B CA  1 
ATOM   4149 C  C   . GLY   B 1 235 ? 30.068  10.437  17.954  1.00 37.64  ? 240 GLY   B C   1 
ATOM   4150 O  O   . GLY   B 1 235 ? 30.884  9.675   18.477  1.00 37.09  ? 240 GLY   B O   1 
ATOM   4151 N  N   . LYS   B 1 236 ? 30.269  11.762  17.823  1.00 34.62  ? 241 LYS   B N   1 
ATOM   4152 C  CA  . LYS   B 1 236 ? 31.517  12.440  18.240  1.00 35.47  ? 241 LYS   B CA  1 
ATOM   4153 C  C   . LYS   B 1 236 ? 31.536  12.742  19.728  1.00 40.86  ? 241 LYS   B C   1 
ATOM   4154 O  O   . LYS   B 1 236 ? 32.569  12.569  20.392  1.00 40.65  ? 241 LYS   B O   1 
ATOM   4155 C  CB  . LYS   B 1 236 ? 31.751  13.733  17.436  1.00 36.93  ? 241 LYS   B CB  1 
ATOM   4156 C  CG  . LYS   B 1 236 ? 32.028  13.493  15.955  1.00 48.16  ? 241 LYS   B CG  1 
ATOM   4157 C  CD  . LYS   B 1 236 ? 32.383  14.784  15.230  1.00 58.83  ? 241 LYS   B CD  1 
ATOM   4158 C  CE  . LYS   B 1 236 ? 32.190  14.653  13.739  1.00 74.69  ? 241 LYS   B CE  1 
ATOM   4159 N  NZ  . LYS   B 1 236 ? 32.909  15.720  12.992  1.00 88.17  ? 241 LYS   B NZ  1 
ATOM   4160 N  N   . ARG   B 1 237 ? 30.399  13.212  20.258  1.00 35.94  ? 242 ARG   B N   1 
ATOM   4161 C  CA  . ARG   B 1 237 ? 30.291  13.570  21.668  1.00 35.24  ? 242 ARG   B CA  1 
ATOM   4162 C  C   . ARG   B 1 237 ? 28.852  13.460  22.168  1.00 37.95  ? 242 ARG   B C   1 
ATOM   4163 O  O   . ARG   B 1 237 ? 27.899  13.529  21.375  1.00 36.08  ? 242 ARG   B O   1 
ATOM   4164 C  CB  . ARG   B 1 237 ? 30.862  14.992  21.908  1.00 36.30  ? 242 ARG   B CB  1 
ATOM   4165 C  CG  . ARG   B 1 237 ? 30.061  16.100  21.235  1.00 43.64  ? 242 ARG   B CG  1 
ATOM   4166 C  CD  . ARG   B 1 237 ? 30.880  17.317  20.845  1.00 46.79  ? 242 ARG   B CD  1 
ATOM   4167 N  NE  . ARG   B 1 237 ? 30.025  18.278  20.144  1.00 43.33  ? 242 ARG   B NE  1 
ATOM   4168 C  CZ  . ARG   B 1 237 ? 29.877  18.346  18.825  1.00 53.77  ? 242 ARG   B CZ  1 
ATOM   4169 N  NH1 . ARG   B 1 237 ? 30.559  17.533  18.030  1.00 49.17  ? 242 ARG   B NH1 1 
ATOM   4170 N  NH2 . ARG   B 1 237 ? 29.053  19.235  18.290  1.00 46.13  ? 242 ARG   B NH2 1 
ATOM   4171 N  N   . GLN   B 1 238 ? 28.707  13.297  23.491  1.00 35.37  ? 243 GLN   B N   1 
ATOM   4172 C  CA  . GLN   B 1 238 ? 27.404  13.241  24.140  1.00 34.64  ? 243 GLN   B CA  1 
ATOM   4173 C  C   . GLN   B 1 238 ? 26.869  14.645  24.049  1.00 38.41  ? 243 GLN   B C   1 
ATOM   4174 O  O   . GLN   B 1 238 ? 27.614  15.612  24.299  1.00 39.78  ? 243 GLN   B O   1 
ATOM   4175 C  CB  . GLN   B 1 238 ? 27.519  12.811  25.609  1.00 35.69  ? 243 GLN   B CB  1 
ATOM   4176 C  CG  . GLN   B 1 238 ? 28.117  11.426  25.799  1.00 40.89  ? 243 GLN   B CG  1 
ATOM   4177 C  CD  . GLN   B 1 238 ? 27.085  10.331  25.723  1.00 60.11  ? 243 GLN   B CD  1 
ATOM   4178 O  OE1 . GLN   B 1 238 ? 26.888  9.704   24.676  1.00 55.28  ? 243 GLN   B OE1 1 
ATOM   4179 N  NE2 . GLN   B 1 238 ? 26.427  10.059  26.844  1.00 51.66  ? 243 GLN   B NE2 1 
ATOM   4180 N  N   . ARG   B 1 239 ? 25.628  14.768  23.580  1.00 32.27  ? 244 ARG   B N   1 
ATOM   4181 C  CA  . ARG   B 1 239 ? 24.954  16.044  23.404  1.00 31.28  ? 244 ARG   B CA  1 
ATOM   4182 C  C   . ARG   B 1 239 ? 23.521  15.931  23.902  1.00 32.98  ? 244 ARG   B C   1 
ATOM   4183 O  O   . ARG   B 1 239 ? 22.903  14.883  23.689  1.00 30.72  ? 244 ARG   B O   1 
ATOM   4184 C  CB  . ARG   B 1 239 ? 24.894  16.438  21.920  1.00 31.09  ? 244 ARG   B CB  1 
ATOM   4185 C  CG  . ARG   B 1 239 ? 26.226  16.589  21.224  1.00 32.35  ? 244 ARG   B CG  1 
ATOM   4186 C  CD  . ARG   B 1 239 ? 26.003  16.698  19.743  1.00 33.40  ? 244 ARG   B CD  1 
ATOM   4187 N  NE  . ARG   B 1 239 ? 25.678  18.063  19.341  1.00 34.16  ? 244 ARG   B NE  1 
ATOM   4188 C  CZ  . ARG   B 1 239 ? 25.538  18.449  18.082  1.00 34.97  ? 244 ARG   B CZ  1 
ATOM   4189 N  NH1 . ARG   B 1 239 ? 25.650  17.567  17.092  1.00 30.70  ? 244 ARG   B NH1 1 
ATOM   4190 N  NH2 . ARG   B 1 239 ? 25.288  19.718  17.798  1.00 33.03  ? 244 ARG   B NH2 1 
ATOM   4191 N  N   . PRO   B 1 240 ? 22.949  17.015  24.471  1.00 29.42  ? 245 PRO   B N   1 
ATOM   4192 C  CA  . PRO   B 1 240 ? 21.529  16.970  24.876  1.00 28.17  ? 245 PRO   B CA  1 
ATOM   4193 C  C   . PRO   B 1 240 ? 20.675  16.799  23.615  1.00 30.58  ? 245 PRO   B C   1 
ATOM   4194 O  O   . PRO   B 1 240 ? 20.961  17.409  22.582  1.00 28.86  ? 245 PRO   B O   1 
ATOM   4195 C  CB  . PRO   B 1 240 ? 21.285  18.352  25.508  1.00 30.44  ? 245 PRO   B CB  1 
ATOM   4196 C  CG  . PRO   B 1 240 ? 22.670  18.907  25.812  1.00 35.48  ? 245 PRO   B CG  1 
ATOM   4197 C  CD  . PRO   B 1 240 ? 23.559  18.337  24.773  1.00 31.08  ? 245 PRO   B CD  1 
ATOM   4198 N  N   . ILE   B 1 241 ? 19.659  15.936  23.692  1.00 26.07  ? 246 ILE   B N   1 
ATOM   4199 C  CA  . ILE   B 1 241 ? 18.802  15.672  22.537  1.00 24.57  ? 246 ILE   B CA  1 
ATOM   4200 C  C   . ILE   B 1 241 ? 17.474  16.387  22.685  1.00 25.69  ? 246 ILE   B C   1 
ATOM   4201 O  O   . ILE   B 1 241 ? 16.831  16.290  23.727  1.00 26.72  ? 246 ILE   B O   1 
ATOM   4202 C  CB  . ILE   B 1 241 ? 18.589  14.141  22.337  1.00 25.89  ? 246 ILE   B CB  1 
ATOM   4203 C  CG1 . ILE   B 1 241 ? 19.935  13.448  21.953  1.00 26.00  ? 246 ILE   B CG1 1 
ATOM   4204 C  CG2 . ILE   B 1 241 ? 17.477  13.850  21.272  1.00 25.21  ? 246 ILE   B CG2 1 
ATOM   4205 C  CD1 . ILE   B 1 241 ? 19.880  11.855  21.962  1.00 29.68  ? 246 ILE   B CD1 1 
ATOM   4206 N  N   . HIS   B 1 242 ? 17.059  17.049  21.617  1.00 22.44  ? 247 HIS   B N   1 
ATOM   4207 C  CA  . HIS   B 1 242 ? 15.743  17.643  21.507  1.00 22.80  ? 247 HIS   B CA  1 
ATOM   4208 C  C   . HIS   B 1 242 ? 14.925  16.774  20.524  1.00 25.43  ? 247 HIS   B C   1 
ATOM   4209 O  O   . HIS   B 1 242 ? 15.208  16.782  19.325  1.00 25.31  ? 247 HIS   B O   1 
ATOM   4210 C  CB  . HIS   B 1 242 ? 15.833  19.078  20.983  1.00 23.53  ? 247 HIS   B CB  1 
ATOM   4211 C  CG  . HIS   B 1 242 ? 14.505  19.777  21.052  1.00 25.76  ? 247 HIS   B CG  1 
ATOM   4212 N  ND1 . HIS   B 1 242 ? 14.283  20.803  21.958  1.00 26.61  ? 247 HIS   B ND1 1 
ATOM   4213 C  CD2 . HIS   B 1 242 ? 13.360  19.546  20.360  1.00 26.57  ? 247 HIS   B CD2 1 
ATOM   4214 C  CE1 . HIS   B 1 242 ? 13.012  21.160  21.792  1.00 25.84  ? 247 HIS   B CE1 1 
ATOM   4215 N  NE2 . HIS   B 1 242 ? 12.425  20.448  20.822  1.00 26.04  ? 247 HIS   B NE2 1 
ATOM   4216 N  N   . LEU   B 1 243 ? 13.939  16.024  21.024  1.00 22.50  ? 248 LEU   B N   1 
ATOM   4217 C  CA  . LEU   B 1 243 ? 13.089  15.216  20.158  1.00 22.03  ? 248 LEU   B CA  1 
ATOM   4218 C  C   . LEU   B 1 243 ? 11.869  16.006  19.785  1.00 23.72  ? 248 LEU   B C   1 
ATOM   4219 O  O   . LEU   B 1 243 ? 11.028  16.239  20.658  1.00 23.74  ? 248 LEU   B O   1 
ATOM   4220 C  CB  . LEU   B 1 243 ? 12.704  13.879  20.824  1.00 20.96  ? 248 LEU   B CB  1 
ATOM   4221 C  CG  . LEU   B 1 243 ? 11.664  12.948  20.078  1.00 22.73  ? 248 LEU   B CG  1 
ATOM   4222 C  CD1 . LEU   B 1 243 ? 12.194  12.531  18.679  1.00 24.22  ? 248 LEU   B CD1 1 
ATOM   4223 C  CD2 . LEU   B 1 243 ? 11.354  11.709  20.913  1.00 24.52  ? 248 LEU   B CD2 1 
ATOM   4224 N  N   . SER   B 1 244 ? 11.739  16.409  18.497  1.00 21.15  ? 249 SER   B N   1 
ATOM   4225 C  CA  . SER   B 1 244 ? 10.501  17.143  18.097  1.00 22.07  ? 249 SER   B CA  1 
ATOM   4226 C  C   . SER   B 1 244 ? 9.657   16.157  17.300  1.00 24.89  ? 249 SER   B C   1 
ATOM   4227 O  O   . SER   B 1 244 ? 9.995   15.805  16.146  1.00 23.59  ? 249 SER   B O   1 
ATOM   4228 C  CB  . SER   B 1 244 ? 10.819  18.401  17.291  1.00 24.94  ? 249 SER   B CB  1 
ATOM   4229 O  OG  . SER   B 1 244 ? 9.688   19.259  17.336  1.00 25.20  ? 249 SER   B OG  1 
ATOM   4230 N  N   . PHE   B 1 245 ? 8.567   15.692  17.923  1.00 21.48  ? 250 PHE   B N   1 
ATOM   4231 C  CA  . PHE   B 1 245 ? 7.769   14.605  17.383  1.00 20.72  ? 250 PHE   B CA  1 
ATOM   4232 C  C   . PHE   B 1 245 ? 6.374   15.039  16.946  1.00 23.23  ? 250 PHE   B C   1 
ATOM   4233 O  O   . PHE   B 1 245 ? 5.538   15.387  17.788  1.00 23.83  ? 250 PHE   B O   1 
ATOM   4234 C  CB  . PHE   B 1 245 ? 7.666   13.496  18.442  1.00 22.00  ? 250 PHE   B CB  1 
ATOM   4235 C  CG  . PHE   B 1 245 ? 7.357   12.119  17.905  1.00 22.35  ? 250 PHE   B CG  1 
ATOM   4236 C  CD1 . PHE   B 1 245 ? 6.166   11.866  17.221  1.00 24.87  ? 250 PHE   B CD1 1 
ATOM   4237 C  CD2 . PHE   B 1 245 ? 8.255   11.077  18.076  1.00 22.62  ? 250 PHE   B CD2 1 
ATOM   4238 C  CE1 . PHE   B 1 245 ? 5.893   10.585  16.707  1.00 25.39  ? 250 PHE   B CE1 1 
ATOM   4239 C  CE2 . PHE   B 1 245 ? 7.969   9.786   17.598  1.00 25.29  ? 250 PHE   B CE2 1 
ATOM   4240 C  CZ  . PHE   B 1 245 ? 6.799   9.553   16.894  1.00 24.15  ? 250 PHE   B CZ  1 
ATOM   4241 N  N   . ASP   B 1 246 ? 6.157   15.066  15.631  1.00 21.91  ? 251 ASP   B N   1 
ATOM   4242 C  CA  . ASP   B 1 246 ? 4.861   15.406  15.053  1.00 21.46  ? 251 ASP   B CA  1 
ATOM   4243 C  C   . ASP   B 1 246 ? 4.094   14.097  14.999  1.00 24.06  ? 251 ASP   B C   1 
ATOM   4244 O  O   . ASP   B 1 246 ? 4.584   13.127  14.411  1.00 24.84  ? 251 ASP   B O   1 
ATOM   4245 C  CB  . ASP   B 1 246 ? 5.064   16.031  13.660  1.00 23.54  ? 251 ASP   B CB  1 
ATOM   4246 C  CG  . ASP   B 1 246 ? 3.822   16.578  12.976  1.00 26.83  ? 251 ASP   B CG  1 
ATOM   4247 O  OD1 . ASP   B 1 246 ? 2.729   16.011  13.188  1.00 25.96  ? 251 ASP   B OD1 1 
ATOM   4248 O  OD2 . ASP   B 1 246 ? 3.965   17.474  12.123  1.00 27.21  ? 251 ASP   B OD2 1 
ATOM   4249 N  N   . ILE   B 1 247 ? 2.853   14.061  15.565  1.00 21.20  ? 252 ILE   B N   1 
ATOM   4250 C  CA  . ILE   B 1 247 ? 2.040   12.838  15.551  1.00 21.97  ? 252 ILE   B CA  1 
ATOM   4251 C  C   . ILE   B 1 247 ? 1.758   12.320  14.132  1.00 21.83  ? 252 ILE   B C   1 
ATOM   4252 O  O   . ILE   B 1 247 ? 1.563   11.106  13.964  1.00 22.80  ? 252 ILE   B O   1 
ATOM   4253 C  CB  . ILE   B 1 247 ? 0.720   13.016  16.364  1.00 24.91  ? 252 ILE   B CB  1 
ATOM   4254 C  CG1 . ILE   B 1 247 ? 0.203   11.652  16.914  1.00 24.80  ? 252 ILE   B CG1 1 
ATOM   4255 C  CG2 . ILE   B 1 247 ? -0.356  13.787  15.582  1.00 27.04  ? 252 ILE   B CG2 1 
ATOM   4256 C  CD1 . ILE   B 1 247 ? 1.169   10.994  18.038  1.00 26.25  ? 252 ILE   B CD1 1 
ATOM   4257 N  N   . ASP   B 1 248 ? 1.765   13.228  13.125  1.00 20.12  ? 253 ASP   B N   1 
ATOM   4258 C  CA  . ASP   B 1 248 ? 1.488   12.828  11.745  1.00 21.30  ? 253 ASP   B CA  1 
ATOM   4259 C  C   . ASP   B 1 248 ? 2.631   12.003  11.142  1.00 23.89  ? 253 ASP   B C   1 
ATOM   4260 O  O   . ASP   B 1 248 ? 2.480   11.525  10.028  1.00 24.05  ? 253 ASP   B O   1 
ATOM   4261 C  CB  . ASP   B 1 248 ? 1.077   14.034  10.863  1.00 22.05  ? 253 ASP   B CB  1 
ATOM   4262 C  CG  . ASP   B 1 248 ? 2.162   15.008  10.474  1.00 25.23  ? 253 ASP   B CG  1 
ATOM   4263 O  OD1 . ASP   B 1 248 ? 3.371   14.626  10.545  1.00 26.07  ? 253 ASP   B OD1 1 
ATOM   4264 O  OD2 . ASP   B 1 248 ? 1.819   16.167  10.078  1.00 24.69  ? 253 ASP   B OD2 1 
ATOM   4265 N  N   . ALA   B 1 249 ? 3.760   11.802  11.880  1.00 22.01  ? 254 ALA   B N   1 
ATOM   4266 C  CA  . ALA   B 1 249 ? 4.811   10.890  11.376  1.00 23.26  ? 254 ALA   B CA  1 
ATOM   4267 C  C   . ALA   B 1 249 ? 4.206   9.450   11.261  1.00 23.81  ? 254 ALA   B C   1 
ATOM   4268 O  O   . ALA   B 1 249 ? 4.596   8.656   10.393  1.00 22.60  ? 254 ALA   B O   1 
ATOM   4269 C  CB  . ALA   B 1 249 ? 5.978   10.858  12.349  1.00 24.48  ? 254 ALA   B CB  1 
ATOM   4270 N  N   . PHE   B 1 250 ? 3.275   9.115   12.188  1.00 20.35  ? 255 PHE   B N   1 
ATOM   4271 C  CA  . PHE   B 1 250 ? 2.615   7.807   12.192  1.00 20.32  ? 255 PHE   B CA  1 
ATOM   4272 C  C   . PHE   B 1 250 ? 1.600   7.720   11.045  1.00 24.50  ? 255 PHE   B C   1 
ATOM   4273 O  O   . PHE   B 1 250 ? 1.026   8.735   10.638  1.00 23.09  ? 255 PHE   B O   1 
ATOM   4274 C  CB  . PHE   B 1 250 ? 1.826   7.646   13.491  1.00 20.37  ? 255 PHE   B CB  1 
ATOM   4275 C  CG  . PHE   B 1 250 ? 2.659   7.327   14.688  1.00 20.33  ? 255 PHE   B CG  1 
ATOM   4276 C  CD1 . PHE   B 1 250 ? 3.177   6.046   14.871  1.00 21.53  ? 255 PHE   B CD1 1 
ATOM   4277 C  CD2 . PHE   B 1 250 ? 2.891   8.290   15.663  1.00 21.50  ? 255 PHE   B CD2 1 
ATOM   4278 C  CE1 . PHE   B 1 250 ? 3.909   5.729   16.026  1.00 20.99  ? 255 PHE   B CE1 1 
ATOM   4279 C  CE2 . PHE   B 1 250 ? 3.607   7.975   16.823  1.00 23.89  ? 255 PHE   B CE2 1 
ATOM   4280 C  CZ  . PHE   B 1 250 ? 4.117   6.690   16.994  1.00 23.20  ? 255 PHE   B CZ  1 
ATOM   4281 N  N   . ASP   B 1 251 ? 1.336   6.497   10.577  1.00 22.50  ? 256 ASP   B N   1 
ATOM   4282 C  CA  . ASP   B 1 251 ? 0.339   6.273   9.548   1.00 22.23  ? 256 ASP   B CA  1 
ATOM   4283 C  C   . ASP   B 1 251 ? -1.025  6.836   10.045  1.00 25.17  ? 256 ASP   B C   1 
ATOM   4284 O  O   . ASP   B 1 251 ? -1.342  6.693   11.229  1.00 25.51  ? 256 ASP   B O   1 
ATOM   4285 C  CB  . ASP   B 1 251 ? 0.194   4.771   9.287   1.00 23.29  ? 256 ASP   B CB  1 
ATOM   4286 C  CG  . ASP   B 1 251 ? -0.540  4.538   7.989   1.00 30.09  ? 256 ASP   B CG  1 
ATOM   4287 O  OD1 . ASP   B 1 251 ? 0.103   4.647   6.919   1.00 29.25  ? 256 ASP   B OD1 1 
ATOM   4288 O  OD2 . ASP   B 1 251 ? -1.785  4.419   8.026   1.00 28.50  ? 256 ASP   B OD2 1 
ATOM   4289 N  N   . PRO   B 1 252 ? -1.819  7.440   9.135   1.00 24.57  ? 257 PRO   B N   1 
ATOM   4290 C  CA  . PRO   B 1 252 ? -3.129  7.995   9.533   1.00 25.55  ? 257 PRO   B CA  1 
ATOM   4291 C  C   . PRO   B 1 252 ? -4.088  6.971   10.128  1.00 29.55  ? 257 PRO   B C   1 
ATOM   4292 O  O   . PRO   B 1 252 ? -4.983  7.376   10.867  1.00 28.86  ? 257 PRO   B O   1 
ATOM   4293 C  CB  . PRO   B 1 252 ? -3.667  8.589   8.229   1.00 27.62  ? 257 PRO   B CB  1 
ATOM   4294 C  CG  . PRO   B 1 252 ? -2.429  8.954   7.466   1.00 30.13  ? 257 PRO   B CG  1 
ATOM   4295 C  CD  . PRO   B 1 252 ? -1.521  7.763   7.731   1.00 24.91  ? 257 PRO   B CD  1 
ATOM   4296 N  N   . THR   B 1 253 ? -3.903  5.652   9.858   1.00 28.00  ? 258 THR   B N   1 
ATOM   4297 C  CA  . THR   B 1 253 ? -4.753  4.612   10.448  1.00 28.78  ? 258 THR   B CA  1 
ATOM   4298 C  C   . THR   B 1 253 ? -4.540  4.566   11.960  1.00 32.60  ? 258 THR   B C   1 
ATOM   4299 O  O   . THR   B 1 253 ? -5.471  4.233   12.692  1.00 35.37  ? 258 THR   B O   1 
ATOM   4300 C  CB  . THR   B 1 253 ? -4.502  3.233   9.815   1.00 37.71  ? 258 THR   B CB  1 
ATOM   4301 O  OG1 . THR   B 1 253 ? -3.135  2.839   10.001  1.00 35.25  ? 258 THR   B OG1 1 
ATOM   4302 C  CG2 . THR   B 1 253 ? -4.911  3.173   8.349   1.00 37.31  ? 258 THR   B CG2 1 
ATOM   4303 N  N   . LEU   B 1 254 ? -3.315  4.930   12.425  1.00 26.74  ? 259 LEU   B N   1 
ATOM   4304 C  CA  . LEU   B 1 254 ? -2.914  4.934   13.834  1.00 26.20  ? 259 LEU   B CA  1 
ATOM   4305 C  C   . LEU   B 1 254 ? -3.084  6.297   14.509  1.00 28.35  ? 259 LEU   B C   1 
ATOM   4306 O  O   . LEU   B 1 254 ? -3.275  6.357   15.731  1.00 27.59  ? 259 LEU   B O   1 
ATOM   4307 C  CB  . LEU   B 1 254 ? -1.433  4.527   13.951  1.00 26.59  ? 259 LEU   B CB  1 
ATOM   4308 C  CG  . LEU   B 1 254 ? -1.077  3.189   13.365  1.00 31.14  ? 259 LEU   B CG  1 
ATOM   4309 C  CD1 . LEU   B 1 254 ? 0.423   3.088   13.137  1.00 29.92  ? 259 LEU   B CD1 1 
ATOM   4310 C  CD2 . LEU   B 1 254 ? -1.567  2.047   14.257  1.00 35.22  ? 259 LEU   B CD2 1 
ATOM   4311 N  N   . ALA   B 1 255 ? -2.898  7.375   13.743  1.00 25.60  ? 260 ALA   B N   1 
ATOM   4312 C  CA  . ALA   B 1 255 ? -2.969  8.737   14.265  1.00 25.96  ? 260 ALA   B CA  1 
ATOM   4313 C  C   . ALA   B 1 255 ? -3.877  9.577   13.362  1.00 27.68  ? 260 ALA   B C   1 
ATOM   4314 O  O   . ALA   B 1 255 ? -3.424  10.504  12.705  1.00 26.08  ? 260 ALA   B O   1 
ATOM   4315 C  CB  . ALA   B 1 255 ? -1.566  9.348   14.348  1.00 26.74  ? 260 ALA   B CB  1 
ATOM   4316 N  N   . PRO   B 1 256 ? -5.187  9.264   13.326  1.00 25.61  ? 261 PRO   B N   1 
ATOM   4317 C  CA  . PRO   B 1 256 ? -6.078  10.014  12.427  1.00 25.77  ? 261 PRO   B CA  1 
ATOM   4318 C  C   . PRO   B 1 256 ? -6.334  11.460  12.855  1.00 28.50  ? 261 PRO   B C   1 
ATOM   4319 O  O   . PRO   B 1 256 ? -6.579  12.307  11.993  1.00 29.55  ? 261 PRO   B O   1 
ATOM   4320 C  CB  . PRO   B 1 256 ? -7.384  9.199   12.466  1.00 27.69  ? 261 PRO   B CB  1 
ATOM   4321 C  CG  . PRO   B 1 256 ? -7.364  8.514   13.783  1.00 30.78  ? 261 PRO   B CG  1 
ATOM   4322 C  CD  . PRO   B 1 256 ? -5.909  8.174   14.018  1.00 26.84  ? 261 PRO   B CD  1 
ATOM   4323 N  N   . ALA   B 1 257 ? -6.282  11.747  14.166  1.00 24.34  ? 262 ALA   B N   1 
ATOM   4324 C  CA  . ALA   B 1 257 ? -6.628  13.080  14.669  1.00 24.56  ? 262 ALA   B CA  1 
ATOM   4325 C  C   . ALA   B 1 257 ? -5.492  14.080  14.502  1.00 26.24  ? 262 ALA   B C   1 
ATOM   4326 O  O   . ALA   B 1 257 ? -4.833  14.441  15.479  1.00 26.95  ? 262 ALA   B O   1 
ATOM   4327 C  CB  . ALA   B 1 257 ? -7.085  12.986  16.125  1.00 25.86  ? 262 ALA   B CB  1 
ATOM   4328 N  N   . THR   B 1 258 ? -5.256  14.530  13.251  1.00 23.86  ? 263 THR   B N   1 
ATOM   4329 C  CA  . THR   B 1 258 ? -4.171  15.463  12.920  1.00 24.07  ? 263 THR   B CA  1 
ATOM   4330 C  C   . THR   B 1 258 ? -4.531  16.207  11.616  1.00 27.98  ? 263 THR   B C   1 
ATOM   4331 O  O   . THR   B 1 258 ? -5.291  15.674  10.802  1.00 28.53  ? 263 THR   B O   1 
ATOM   4332 C  CB  . THR   B 1 258 ? -2.801  14.699  12.852  1.00 24.74  ? 263 THR   B CB  1 
ATOM   4333 O  OG1 . THR   B 1 258 ? -1.710  15.629  12.936  1.00 25.48  ? 263 THR   B OG1 1 
ATOM   4334 C  CG2 . THR   B 1 258 ? -2.667  13.819  11.582  1.00 26.47  ? 263 THR   B CG2 1 
ATOM   4335 N  N   . GLY   B 1 259 ? -3.942  17.381  11.428  1.00 25.83  ? 264 GLY   B N   1 
ATOM   4336 C  CA  . GLY   B 1 259 ? -4.226  18.301  10.328  1.00 26.43  ? 264 GLY   B CA  1 
ATOM   4337 C  C   . GLY   B 1 259 ? -3.796  17.935  8.919   1.00 30.67  ? 264 GLY   B C   1 
ATOM   4338 O  O   . GLY   B 1 259 ? -4.511  18.233  7.951   1.00 29.73  ? 264 GLY   B O   1 
ATOM   4339 N  N   . THR   B 1 260 ? -2.573  17.405  8.775   1.00 27.81  ? 265 THR   B N   1 
ATOM   4340 C  CA  . THR   B 1 260 ? -2.007  17.074  7.455   1.00 27.00  ? 265 THR   B CA  1 
ATOM   4341 C  C   . THR   B 1 260 ? -1.635  15.574  7.389   1.00 28.49  ? 265 THR   B C   1 
ATOM   4342 O  O   . THR   B 1 260 ? -0.438  15.247  7.356   1.00 27.69  ? 265 THR   B O   1 
ATOM   4343 C  CB  . THR   B 1 260 ? -0.837  18.025  7.115   1.00 32.98  ? 265 THR   B CB  1 
ATOM   4344 O  OG1 . THR   B 1 260 ? -1.240  19.375  7.346   1.00 31.05  ? 265 THR   B OG1 1 
ATOM   4345 C  CG2 . THR   B 1 260 ? -0.383  17.914  5.653   1.00 35.63  ? 265 THR   B CG2 1 
ATOM   4346 N  N   . PRO   B 1 261 ? -2.628  14.655  7.432   1.00 25.56  ? 266 PRO   B N   1 
ATOM   4347 C  CA  . PRO   B 1 261 ? -2.298  13.216  7.401   1.00 25.21  ? 266 PRO   B CA  1 
ATOM   4348 C  C   . PRO   B 1 261 ? -1.780  12.800  6.041   1.00 29.19  ? 266 PRO   B C   1 
ATOM   4349 O  O   . PRO   B 1 261 ? -2.241  13.328  5.020   1.00 27.66  ? 266 PRO   B O   1 
ATOM   4350 C  CB  . PRO   B 1 261 ? -3.627  12.530  7.705   1.00 27.47  ? 266 PRO   B CB  1 
ATOM   4351 C  CG  . PRO   B 1 261 ? -4.670  13.500  7.218   1.00 31.45  ? 266 PRO   B CG  1 
ATOM   4352 C  CD  . PRO   B 1 261 ? -4.095  14.873  7.453   1.00 26.77  ? 266 PRO   B CD  1 
ATOM   4353 N  N   . VAL   B 1 262 ? -0.774  11.905  6.028   1.00 24.82  ? 267 VAL   B N   1 
ATOM   4354 C  CA  . VAL   B 1 262 ? -0.186  11.373  4.797   1.00 24.80  ? 267 VAL   B CA  1 
ATOM   4355 C  C   . VAL   B 1 262 ? -0.083  9.849   4.924   1.00 26.89  ? 267 VAL   B C   1 
ATOM   4356 O  O   . VAL   B 1 262 ? 0.556   9.347   5.850   1.00 25.21  ? 267 VAL   B O   1 
ATOM   4357 C  CB  . VAL   B 1 262 ? 1.208   11.994  4.447   1.00 27.62  ? 267 VAL   B CB  1 
ATOM   4358 C  CG1 . VAL   B 1 262 ? 1.692   11.505  3.072   1.00 27.61  ? 267 VAL   B CG1 1 
ATOM   4359 C  CG2 . VAL   B 1 262 ? 1.183   13.533  4.510   1.00 27.30  ? 267 VAL   B CG2 1 
ATOM   4360 N  N   . VAL   B 1 263 ? -0.724  9.112   4.004   1.00 25.55  ? 268 VAL   B N   1 
ATOM   4361 C  CA  . VAL   B 1 263 ? -0.695  7.649   3.982   1.00 25.56  ? 268 VAL   B CA  1 
ATOM   4362 C  C   . VAL   B 1 263 ? 0.756   7.114   3.934   1.00 26.04  ? 268 VAL   B C   1 
ATOM   4363 O  O   . VAL   B 1 263 ? 1.645   7.806   3.437   1.00 26.11  ? 268 VAL   B O   1 
ATOM   4364 C  CB  . VAL   B 1 263 ? -1.531  7.133   2.767   1.00 30.62  ? 268 VAL   B CB  1 
ATOM   4365 C  CG1 . VAL   B 1 263 ? -0.930  7.591   1.436   1.00 29.88  ? 268 VAL   B CG1 1 
ATOM   4366 C  CG2 . VAL   B 1 263 ? -1.725  5.614   2.800   1.00 32.13  ? 268 VAL   B CG2 1 
ATOM   4367 N  N   . GLY   B 1 264 ? 0.958   5.901   4.457   1.00 24.55  ? 269 GLY   B N   1 
ATOM   4368 C  CA  . GLY   B 1 264 ? 2.248   5.216   4.424   1.00 23.67  ? 269 GLY   B CA  1 
ATOM   4369 C  C   . GLY   B 1 264 ? 3.247   5.688   5.454   1.00 23.20  ? 269 GLY   B C   1 
ATOM   4370 O  O   . GLY   B 1 264 ? 4.441   5.809   5.152   1.00 23.03  ? 269 GLY   B O   1 
ATOM   4371 N  N   . GLY   B 1 265 ? 2.790   5.868   6.687   1.00 21.29  ? 270 GLY   B N   1 
ATOM   4372 C  CA  . GLY   B 1 265 ? 3.660   6.355   7.755   1.00 21.00  ? 270 GLY   B CA  1 
ATOM   4373 C  C   . GLY   B 1 265 ? 4.241   5.275   8.634   1.00 21.32  ? 270 GLY   B C   1 
ATOM   4374 O  O   . GLY   B 1 265 ? 4.153   4.065   8.338   1.00 22.18  ? 270 GLY   B O   1 
ATOM   4375 N  N   . LEU   B 1 266 ? 4.814   5.722   9.774   1.00 20.54  ? 271 LEU   B N   1 
ATOM   4376 C  CA  . LEU   B 1 266 ? 5.398   4.803   10.750  1.00 19.91  ? 271 LEU   B CA  1 
ATOM   4377 C  C   . LEU   B 1 266 ? 4.333   3.889   11.318  1.00 21.89  ? 271 LEU   B C   1 
ATOM   4378 O  O   . LEU   B 1 266 ? 3.197   4.315   11.536  1.00 21.95  ? 271 LEU   B O   1 
ATOM   4379 C  CB  . LEU   B 1 266 ? 6.025   5.569   11.939  1.00 20.30  ? 271 LEU   B CB  1 
ATOM   4380 C  CG  . LEU   B 1 266 ? 7.081   6.621   11.640  1.00 22.79  ? 271 LEU   B CG  1 
ATOM   4381 C  CD1 . LEU   B 1 266 ? 7.390   7.389   12.894  1.00 23.27  ? 271 LEU   B CD1 1 
ATOM   4382 C  CD2 . LEU   B 1 266 ? 8.393   5.980   11.155  1.00 25.59  ? 271 LEU   B CD2 1 
ATOM   4383 N  N   . THR   B 1 267 ? 4.712   2.655   11.602  1.00 21.09  ? 272 THR   B N   1 
ATOM   4384 C  CA  . THR   B 1 267 ? 3.807   1.752   12.299  1.00 20.74  ? 272 THR   B CA  1 
ATOM   4385 C  C   . THR   B 1 267 ? 3.915   2.098   13.811  1.00 23.30  ? 272 THR   B C   1 
ATOM   4386 O  O   . THR   B 1 267 ? 4.822   2.852   14.231  1.00 21.66  ? 272 THR   B O   1 
ATOM   4387 C  CB  . THR   B 1 267 ? 4.223   0.284   12.110  1.00 22.66  ? 272 THR   B CB  1 
ATOM   4388 O  OG1 . THR   B 1 267 ? 5.496   0.086   12.759  1.00 21.14  ? 272 THR   B OG1 1 
ATOM   4389 C  CG2 . THR   B 1 267 ? 4.266   -0.151  10.608  1.00 22.25  ? 272 THR   B CG2 1 
ATOM   4390 N  N   . TYR   B 1 268 ? 2.991   1.549   14.630  1.00 21.66  ? 273 TYR   B N   1 
ATOM   4391 C  CA  . TYR   B 1 268 ? 3.047   1.739   16.080  1.00 20.86  ? 273 TYR   B CA  1 
ATOM   4392 C  C   . TYR   B 1 268 ? 4.423   1.275   16.575  1.00 21.41  ? 273 TYR   B C   1 
ATOM   4393 O  O   . TYR   B 1 268 ? 5.094   1.995   17.333  1.00 22.31  ? 273 TYR   B O   1 
ATOM   4394 C  CB  . TYR   B 1 268 ? 1.943   0.927   16.780  1.00 21.39  ? 273 TYR   B CB  1 
ATOM   4395 C  CG  . TYR   B 1 268 ? 1.990   1.045   18.286  1.00 22.29  ? 273 TYR   B CG  1 
ATOM   4396 C  CD1 . TYR   B 1 268 ? 1.322   2.075   18.946  1.00 26.33  ? 273 TYR   B CD1 1 
ATOM   4397 C  CD2 . TYR   B 1 268 ? 2.725   0.142   19.057  1.00 22.82  ? 273 TYR   B CD2 1 
ATOM   4398 C  CE1 . TYR   B 1 268 ? 1.377   2.202   20.332  1.00 25.96  ? 273 TYR   B CE1 1 
ATOM   4399 C  CE2 . TYR   B 1 268 ? 2.762   0.244   20.447  1.00 23.91  ? 273 TYR   B CE2 1 
ATOM   4400 C  CZ  . TYR   B 1 268 ? 2.127   1.311   21.073  1.00 28.52  ? 273 TYR   B CZ  1 
ATOM   4401 O  OH  . TYR   B 1 268 ? 2.186   1.450   22.436  1.00 29.26  ? 273 TYR   B OH  1 
ATOM   4402 N  N   . ARG   B 1 269 ? 4.842   0.058   16.140  1.00 19.62  ? 274 ARG   B N   1 
ATOM   4403 C  CA  . ARG   B 1 269 ? 6.140   -0.505  16.549  1.00 20.23  ? 274 ARG   B CA  1 
ATOM   4404 C  C   . ARG   B 1 269 ? 7.313   0.380   16.183  1.00 21.90  ? 274 ARG   B C   1 
ATOM   4405 O  O   . ARG   B 1 269 ? 8.181   0.595   17.043  1.00 22.01  ? 274 ARG   B O   1 
ATOM   4406 C  CB  . ARG   B 1 269 ? 6.309   -1.903  15.954  1.00 19.90  ? 274 ARG   B CB  1 
ATOM   4407 C  CG  . ARG   B 1 269 ? 5.329   -2.907  16.578  1.00 20.81  ? 274 ARG   B CG  1 
ATOM   4408 C  CD  . ARG   B 1 269 ? 4.994   -4.073  15.652  1.00 22.74  ? 274 ARG   B CD  1 
ATOM   4409 N  NE  . ARG   B 1 269 ? 6.206   -4.794  15.271  1.00 23.40  ? 274 ARG   B NE  1 
ATOM   4410 C  CZ  . ARG   B 1 269 ? 6.225   -5.876  14.496  1.00 25.55  ? 274 ARG   B CZ  1 
ATOM   4411 N  NH1 . ARG   B 1 269 ? 5.091   -6.424  14.083  1.00 22.10  ? 274 ARG   B NH1 1 
ATOM   4412 N  NH2 . ARG   B 1 269 ? 7.381   -6.448  14.172  1.00 23.69  ? 274 ARG   B NH2 1 
ATOM   4413 N  N   . GLU   B 1 270 ? 7.334   0.939   14.938  1.00 19.02  ? 275 GLU   B N   1 
ATOM   4414 C  CA  . GLU   B 1 270 ? 8.455   1.819   14.546  1.00 17.93  ? 275 GLU   B CA  1 
ATOM   4415 C  C   . GLU   B 1 270 ? 8.516   3.075   15.422  1.00 20.08  ? 275 GLU   B C   1 
ATOM   4416 O  O   . GLU   B 1 270 ? 9.590   3.424   15.915  1.00 20.68  ? 275 GLU   B O   1 
ATOM   4417 C  CB  . GLU   B 1 270 ? 8.356   2.216   13.089  1.00 18.46  ? 275 GLU   B CB  1 
ATOM   4418 C  CG  . GLU   B 1 270 ? 8.725   1.071   12.169  1.00 21.44  ? 275 GLU   B CG  1 
ATOM   4419 C  CD  . GLU   B 1 270 ? 8.308   1.288   10.719  1.00 26.50  ? 275 GLU   B CD  1 
ATOM   4420 O  OE1 . GLU   B 1 270 ? 7.328   2.028   10.466  1.00 22.12  ? 275 GLU   B OE1 1 
ATOM   4421 O  OE2 . GLU   B 1 270 ? 8.949   0.678   9.833   1.00 24.31  ? 275 GLU   B OE2 1 
ATOM   4422 N  N   . GLY   B 1 271 ? 7.368   3.696   15.678  1.00 20.04  ? 276 GLY   B N   1 
ATOM   4423 C  CA  . GLY   B 1 271 ? 7.306   4.899   16.519  1.00 20.44  ? 276 GLY   B CA  1 
ATOM   4424 C  C   . GLY   B 1 271 ? 7.779   4.639   17.945  1.00 20.44  ? 276 GLY   B C   1 
ATOM   4425 O  O   . GLY   B 1 271 ? 8.554   5.423   18.501  1.00 21.22  ? 276 GLY   B O   1 
ATOM   4426 N  N   . MET   B 1 272 ? 7.372   3.505   18.534  1.00 19.31  ? 277 MET   B N   1 
ATOM   4427 C  CA  . MET   B 1 272 ? 7.821   3.144   19.900  1.00 19.97  ? 277 MET   B CA  1 
ATOM   4428 C  C   . MET   B 1 272 ? 9.315   2.893   19.879  1.00 21.94  ? 277 MET   B C   1 
ATOM   4429 O  O   . MET   B 1 272 ? 10.024  3.317   20.786  1.00 24.05  ? 277 MET   B O   1 
ATOM   4430 C  CB  . MET   B 1 272 ? 7.081   1.911   20.437  1.00 21.78  ? 277 MET   B CB  1 
ATOM   4431 C  CG  . MET   B 1 272 ? 5.581   2.152   20.606  1.00 24.81  ? 277 MET   B CG  1 
ATOM   4432 S  SD  . MET   B 1 272 ? 5.232   3.543   21.748  1.00 27.94  ? 277 MET   B SD  1 
ATOM   4433 C  CE  . MET   B 1 272 ? 4.703   4.724   20.652  1.00 24.57  ? 277 MET   B CE  1 
ATOM   4434 N  N   . TYR   B 1 273 ? 9.787   2.240   18.824  1.00 20.11  ? 278 TYR   B N   1 
ATOM   4435 C  CA  . TYR   B 1 273 ? 11.220  1.947   18.716  1.00 20.80  ? 278 TYR   B CA  1 
ATOM   4436 C  C   . TYR   B 1 273 ? 12.057  3.241   18.717  1.00 23.20  ? 278 TYR   B C   1 
ATOM   4437 O  O   . TYR   B 1 273 ? 13.082  3.334   19.423  1.00 22.03  ? 278 TYR   B O   1 
ATOM   4438 C  CB  . TYR   B 1 273 ? 11.498  1.050   17.508  1.00 20.73  ? 278 TYR   B CB  1 
ATOM   4439 C  CG  . TYR   B 1 273 ? 12.916  0.550   17.556  1.00 23.29  ? 278 TYR   B CG  1 
ATOM   4440 C  CD1 . TYR   B 1 273 ? 13.251  -0.591  18.287  1.00 25.15  ? 278 TYR   B CD1 1 
ATOM   4441 C  CD2 . TYR   B 1 273 ? 13.940  1.275   16.967  1.00 24.57  ? 278 TYR   B CD2 1 
ATOM   4442 C  CE1 . TYR   B 1 273 ? 14.580  -1.022  18.378  1.00 26.28  ? 278 TYR   B CE1 1 
ATOM   4443 C  CE2 . TYR   B 1 273 ? 15.254  0.837   17.016  1.00 26.18  ? 278 TYR   B CE2 1 
ATOM   4444 C  CZ  . TYR   B 1 273 ? 15.572  -0.307  17.722  1.00 27.62  ? 278 TYR   B CZ  1 
ATOM   4445 O  OH  . TYR   B 1 273 ? 16.889  -0.693  17.752  1.00 28.61  ? 278 TYR   B OH  1 
ATOM   4446 N  N   . ILE   B 1 274 ? 11.623  4.242   17.932  1.00 20.24  ? 279 ILE   B N   1 
ATOM   4447 C  CA  . ILE   B 1 274 ? 12.310  5.542   17.916  1.00 19.40  ? 279 ILE   B CA  1 
ATOM   4448 C  C   . ILE   B 1 274 ? 12.435  6.091   19.354  1.00 23.38  ? 279 ILE   B C   1 
ATOM   4449 O  O   . ILE   B 1 274 ? 13.538  6.427   19.813  1.00 22.47  ? 279 ILE   B O   1 
ATOM   4450 C  CB  . ILE   B 1 274 ? 11.551  6.535   17.021  1.00 21.69  ? 279 ILE   B CB  1 
ATOM   4451 C  CG1 . ILE   B 1 274 ? 11.591  6.068   15.560  1.00 20.75  ? 279 ILE   B CG1 1 
ATOM   4452 C  CG2 . ILE   B 1 274 ? 12.100  7.981   17.207  1.00 22.96  ? 279 ILE   B CG2 1 
ATOM   4453 C  CD1 . ILE   B 1 274 ? 10.720  6.956   14.636  1.00 22.99  ? 279 ILE   B CD1 1 
ATOM   4454 N  N   . ALA   B 1 275 ? 11.306  6.167   20.065  1.00 20.08  ? 280 ALA   B N   1 
ATOM   4455 C  CA  . ALA   B 1 275 ? 11.227  6.705   21.416  1.00 22.08  ? 280 ALA   B CA  1 
ATOM   4456 C  C   . ALA   B 1 275 ? 12.062  5.896   22.404  1.00 23.63  ? 280 ALA   B C   1 
ATOM   4457 O  O   . ALA   B 1 275 ? 12.792  6.487   23.200  1.00 23.82  ? 280 ALA   B O   1 
ATOM   4458 C  CB  . ALA   B 1 275 ? 9.768   6.778   21.853  1.00 23.16  ? 280 ALA   B CB  1 
ATOM   4459 N  N   . GLU   B 1 276 ? 11.992  4.551   22.331  1.00 21.65  ? 281 GLU   B N   1 
ATOM   4460 C  CA  . GLU   B 1 276 ? 12.790  3.654   23.182  1.00 21.25  ? 281 GLU   B CA  1 
ATOM   4461 C  C   . GLU   B 1 276 ? 14.295  3.927   22.973  1.00 24.75  ? 281 GLU   B C   1 
ATOM   4462 O  O   . GLU   B 1 276 ? 15.054  3.997   23.948  1.00 25.14  ? 281 GLU   B O   1 
ATOM   4463 C  CB  . GLU   B 1 276 ? 12.494  2.204   22.819  1.00 22.93  ? 281 GLU   B CB  1 
ATOM   4464 C  CG  . GLU   B 1 276 ? 11.150  1.742   23.346  1.00 22.46  ? 281 GLU   B CG  1 
ATOM   4465 C  CD  . GLU   B 1 276 ? 10.711  0.399   22.802  1.00 29.99  ? 281 GLU   B CD  1 
ATOM   4466 O  OE1 . GLU   B 1 276 ? 11.363  -0.126  21.869  1.00 26.89  ? 281 GLU   B OE1 1 
ATOM   4467 O  OE2 . GLU   B 1 276 ? 9.613   -0.041  23.206  1.00 27.64  ? 281 GLU   B OE2 1 
ATOM   4468 N  N   . GLU   B 1 277 ? 14.719  4.065   21.720  1.00 20.88  ? 282 GLU   B N   1 
ATOM   4469 C  CA  . GLU   B 1 277 ? 16.146  4.298   21.443  1.00 20.81  ? 282 GLU   B CA  1 
ATOM   4470 C  C   . GLU   B 1 277 ? 16.600  5.659   21.976  1.00 25.68  ? 282 GLU   B C   1 
ATOM   4471 O  O   . GLU   B 1 277 ? 17.699  5.753   22.536  1.00 25.95  ? 282 GLU   B O   1 
ATOM   4472 C  CB  . GLU   B 1 277 ? 16.458  4.128   19.962  1.00 22.29  ? 282 GLU   B CB  1 
ATOM   4473 C  CG  . GLU   B 1 277 ? 16.448  2.668   19.540  1.00 27.75  ? 282 GLU   B CG  1 
ATOM   4474 C  CD  . GLU   B 1 277 ? 17.296  1.789   20.449  1.00 38.87  ? 282 GLU   B CD  1 
ATOM   4475 O  OE1 . GLU   B 1 277 ? 18.534  1.965   20.469  1.00 32.65  ? 282 GLU   B OE1 1 
ATOM   4476 O  OE2 . GLU   B 1 277 ? 16.709  1.039   21.254  1.00 34.42  ? 282 GLU   B OE2 1 
ATOM   4477 N  N   . ILE   B 1 278 ? 15.742  6.685   21.856  1.00 22.69  ? 283 ILE   B N   1 
ATOM   4478 C  CA  . ILE   B 1 278 ? 16.003  8.030   22.392  1.00 23.42  ? 283 ILE   B CA  1 
ATOM   4479 C  C   . ILE   B 1 278 ? 16.189  7.901   23.929  1.00 26.00  ? 283 ILE   B C   1 
ATOM   4480 O  O   . ILE   B 1 278 ? 17.177  8.391   24.488  1.00 25.07  ? 283 ILE   B O   1 
ATOM   4481 C  CB  . ILE   B 1 278 ? 14.837  8.997   22.015  1.00 26.53  ? 283 ILE   B CB  1 
ATOM   4482 C  CG1 . ILE   B 1 278 ? 14.870  9.387   20.498  1.00 28.13  ? 283 ILE   B CG1 1 
ATOM   4483 C  CG2 . ILE   B 1 278 ? 14.833  10.258  22.948  1.00 28.44  ? 283 ILE   B CG2 1 
ATOM   4484 C  CD1 . ILE   B 1 278 ? 15.865  10.536  20.082  1.00 32.82  ? 283 ILE   B CD1 1 
ATOM   4485 N  N   . HIS   B 1 279 ? 15.277  7.180   24.595  1.00 23.25  ? 284 HIS   B N   1 
ATOM   4486 C  CA  . HIS   B 1 279 ? 15.421  6.950   26.033  1.00 22.94  ? 284 HIS   B CA  1 
ATOM   4487 C  C   . HIS   B 1 279 ? 16.768  6.256   26.361  1.00 28.39  ? 284 HIS   B C   1 
ATOM   4488 O  O   . HIS   B 1 279 ? 17.433  6.678   27.302  1.00 27.21  ? 284 HIS   B O   1 
ATOM   4489 C  CB  . HIS   B 1 279 ? 14.260  6.112   26.580  1.00 24.27  ? 284 HIS   B CB  1 
ATOM   4490 C  CG  . HIS   B 1 279 ? 14.525  5.657   27.985  1.00 27.65  ? 284 HIS   B CG  1 
ATOM   4491 N  ND1 . HIS   B 1 279 ? 14.473  6.549   29.059  1.00 29.63  ? 284 HIS   B ND1 1 
ATOM   4492 C  CD2 . HIS   B 1 279 ? 14.948  4.457   28.441  1.00 29.15  ? 284 HIS   B CD2 1 
ATOM   4493 C  CE1 . HIS   B 1 279 ? 14.787  5.831   30.131  1.00 28.27  ? 284 HIS   B CE1 1 
ATOM   4494 N  NE2 . HIS   B 1 279 ? 15.094  4.582   29.815  1.00 29.10  ? 284 HIS   B NE2 1 
ATOM   4495 N  N   . ASN   B 1 280 ? 17.145  5.208   25.596  1.00 27.05  ? 285 ASN   B N   1 
ATOM   4496 C  CA  . ASN   B 1 280 ? 18.365  4.415   25.827  1.00 27.14  ? 285 ASN   B CA  1 
ATOM   4497 C  C   . ASN   B 1 280 ? 19.665  5.236   25.742  1.00 30.51  ? 285 ASN   B C   1 
ATOM   4498 O  O   . ASN   B 1 280 ? 20.662  4.829   26.349  1.00 29.62  ? 285 ASN   B O   1 
ATOM   4499 C  CB  . ASN   B 1 280 ? 18.407  3.190   24.895  1.00 27.39  ? 285 ASN   B CB  1 
ATOM   4500 C  CG  . ASN   B 1 280 ? 17.421  2.098   25.248  1.00 41.28  ? 285 ASN   B CG  1 
ATOM   4501 O  OD1 . ASN   B 1 280 ? 16.872  2.057   26.350  1.00 42.97  ? 285 ASN   B OD1 1 
ATOM   4502 N  ND2 . ASN   B 1 280 ? 17.199  1.150   24.333  1.00 32.69  ? 285 ASN   B ND2 1 
ATOM   4503 N  N   . THR   B 1 281 ? 19.653  6.406   25.052  1.00 27.08  ? 286 THR   B N   1 
ATOM   4504 C  CA  . THR   B 1 281 ? 20.852  7.287   25.002  1.00 26.56  ? 286 THR   B CA  1 
ATOM   4505 C  C   . THR   B 1 281 ? 21.132  7.908   26.390  1.00 30.19  ? 286 THR   B C   1 
ATOM   4506 O  O   . THR   B 1 281 ? 22.291  8.223   26.699  1.00 31.63  ? 286 THR   B O   1 
ATOM   4507 C  CB  . THR   B 1 281 ? 20.689  8.444   23.979  1.00 26.86  ? 286 THR   B CB  1 
ATOM   4508 O  OG1 . THR   B 1 281 ? 19.709  9.395   24.432  1.00 26.46  ? 286 THR   B OG1 1 
ATOM   4509 C  CG2 . THR   B 1 281 ? 20.395  7.964   22.556  1.00 28.40  ? 286 THR   B CG2 1 
ATOM   4510 N  N   . GLY   B 1 282 ? 20.067  8.121   27.173  1.00 25.79  ? 287 GLY   B N   1 
ATOM   4511 C  CA  . GLY   B 1 282 ? 20.098  8.842   28.442  1.00 26.16  ? 287 GLY   B CA  1 
ATOM   4512 C  C   . GLY   B 1 282 ? 20.385  10.327  28.227  1.00 29.43  ? 287 GLY   B C   1 
ATOM   4513 O  O   . GLY   B 1 282 ? 20.749  11.034  29.178  1.00 30.07  ? 287 GLY   B O   1 
ATOM   4514 N  N   . LEU   B 1 283 ? 20.200  10.829  26.975  1.00 26.42  ? 288 LEU   B N   1 
ATOM   4515 C  CA  . LEU   B 1 283 ? 20.510  12.222  26.627  1.00 26.13  ? 288 LEU   B CA  1 
ATOM   4516 C  C   . LEU   B 1 283 ? 19.305  13.092  26.334  1.00 28.08  ? 288 LEU   B C   1 
ATOM   4517 O  O   . LEU   B 1 283 ? 19.482  14.274  26.067  1.00 26.51  ? 288 LEU   B O   1 
ATOM   4518 C  CB  . LEU   B 1 283 ? 21.498  12.281  25.451  1.00 26.97  ? 288 LEU   B CB  1 
ATOM   4519 C  CG  . LEU   B 1 283 ? 22.905  11.708  25.706  1.00 30.39  ? 288 LEU   B CG  1 
ATOM   4520 C  CD1 . LEU   B 1 283 ? 23.653  11.517  24.416  1.00 29.97  ? 288 LEU   B CD1 1 
ATOM   4521 C  CD2 . LEU   B 1 283 ? 23.711  12.578  26.694  1.00 32.00  ? 288 LEU   B CD2 1 
ATOM   4522 N  N   . LEU   B 1 284 ? 18.078  12.520  26.365  1.00 24.21  ? 289 LEU   B N   1 
ATOM   4523 C  CA  . LEU   B 1 284 ? 16.877  13.311  26.073  1.00 23.83  ? 289 LEU   B CA  1 
ATOM   4524 C  C   . LEU   B 1 284 ? 16.777  14.486  27.039  1.00 27.67  ? 289 LEU   B C   1 
ATOM   4525 O  O   . LEU   B 1 284 ? 16.801  14.285  28.256  1.00 28.47  ? 289 LEU   B O   1 
ATOM   4526 C  CB  . LEU   B 1 284 ? 15.616  12.462  26.138  1.00 23.41  ? 289 LEU   B CB  1 
ATOM   4527 C  CG  . LEU   B 1 284 ? 14.306  13.209  25.787  1.00 27.18  ? 289 LEU   B CG  1 
ATOM   4528 C  CD1 . LEU   B 1 284 ? 14.306  13.717  24.335  1.00 27.30  ? 289 LEU   B CD1 1 
ATOM   4529 C  CD2 . LEU   B 1 284 ? 13.113  12.323  26.040  1.00 29.06  ? 289 LEU   B CD2 1 
ATOM   4530 N  N   . SER   B 1 285 ? 16.676  15.702  26.490  1.00 24.08  ? 290 SER   B N   1 
ATOM   4531 C  CA  . SER   B 1 285 ? 16.659  16.937  27.265  1.00 23.54  ? 290 SER   B CA  1 
ATOM   4532 C  C   . SER   B 1 285 ? 15.362  17.739  27.092  1.00 27.34  ? 290 SER   B C   1 
ATOM   4533 O  O   . SER   B 1 285 ? 14.959  18.447  28.004  1.00 27.19  ? 290 SER   B O   1 
ATOM   4534 C  CB  . SER   B 1 285 ? 17.910  17.740  26.931  1.00 27.65  ? 290 SER   B CB  1 
ATOM   4535 O  OG  . SER   B 1 285 ? 18.085  18.902  27.721  1.00 30.15  ? 290 SER   B OG  1 
ATOM   4536 N  N   . ALA   B 1 286 ? 14.709  17.629  25.917  1.00 23.87  ? 291 ALA   B N   1 
ATOM   4537 C  CA  . ALA   B 1 286 ? 13.415  18.248  25.666  1.00 22.75  ? 291 ALA   B CA  1 
ATOM   4538 C  C   . ALA   B 1 286 ? 12.701  17.448  24.600  1.00 25.51  ? 291 ALA   B C   1 
ATOM   4539 O  O   . ALA   B 1 286 ? 13.339  16.810  23.759  1.00 24.94  ? 291 ALA   B O   1 
ATOM   4540 C  CB  . ALA   B 1 286 ? 13.561  19.704  25.243  1.00 23.66  ? 291 ALA   B CB  1 
ATOM   4541 N  N   . LEU   B 1 287 ? 11.379  17.414  24.684  1.00 23.67  ? 292 LEU   B N   1 
ATOM   4542 C  CA  . LEU   B 1 287 ? 10.550  16.654  23.752  1.00 24.22  ? 292 LEU   B CA  1 
ATOM   4543 C  C   . LEU   B 1 287 ? 9.334   17.514  23.420  1.00 26.09  ? 292 LEU   B C   1 
ATOM   4544 O  O   . LEU   B 1 287 ? 8.730   18.078  24.331  1.00 24.74  ? 292 LEU   B O   1 
ATOM   4545 C  CB  . LEU   B 1 287 ? 10.098  15.342  24.432  1.00 24.54  ? 292 LEU   B CB  1 
ATOM   4546 C  CG  . LEU   B 1 287 ? 9.228   14.356  23.654  1.00 29.47  ? 292 LEU   B CG  1 
ATOM   4547 C  CD1 . LEU   B 1 287 ? 9.349   12.989  24.262  1.00 31.35  ? 292 LEU   B CD1 1 
ATOM   4548 C  CD2 . LEU   B 1 287 ? 7.745   14.742  23.678  1.00 31.87  ? 292 LEU   B CD2 1 
ATOM   4549 N  N   . ASP   B 1 288 ? 8.964   17.579  22.138  1.00 22.94  ? 293 ASP   B N   1 
ATOM   4550 C  CA  . ASP   B 1 288 ? 7.722   18.245  21.694  1.00 22.17  ? 293 ASP   B CA  1 
ATOM   4551 C  C   . ASP   B 1 288 ? 6.804   17.151  21.165  1.00 24.86  ? 293 ASP   B C   1 
ATOM   4552 O  O   . ASP   B 1 288 ? 7.245   16.298  20.393  1.00 24.26  ? 293 ASP   B O   1 
ATOM   4553 C  CB  . ASP   B 1 288 ? 7.975   19.234  20.545  1.00 23.19  ? 293 ASP   B CB  1 
ATOM   4554 C  CG  . ASP   B 1 288 ? 9.115   20.202  20.741  1.00 25.18  ? 293 ASP   B CG  1 
ATOM   4555 O  OD1 . ASP   B 1 288 ? 9.255   20.739  21.871  1.00 26.89  ? 293 ASP   B OD1 1 
ATOM   4556 O  OD2 . ASP   B 1 288 ? 9.882   20.406  19.780  1.00 27.66  ? 293 ASP   B OD2 1 
ATOM   4557 N  N   . LEU   B 1 289 ? 5.541   17.156  21.564  1.00 23.76  ? 294 LEU   B N   1 
ATOM   4558 C  CA  . LEU   B 1 289 ? 4.571   16.210  21.021  1.00 23.33  ? 294 LEU   B CA  1 
ATOM   4559 C  C   . LEU   B 1 289 ? 3.493   17.086  20.444  1.00 27.12  ? 294 LEU   B C   1 
ATOM   4560 O  O   . LEU   B 1 289 ? 2.679   17.649  21.191  1.00 26.73  ? 294 LEU   B O   1 
ATOM   4561 C  CB  . LEU   B 1 289 ? 4.011   15.224  22.068  1.00 22.79  ? 294 LEU   B CB  1 
ATOM   4562 C  CG  . LEU   B 1 289 ? 3.369   13.932  21.485  1.00 25.19  ? 294 LEU   B CG  1 
ATOM   4563 C  CD1 . LEU   B 1 289 ? 2.207   14.246  20.515  1.00 24.38  ? 294 LEU   B CD1 1 
ATOM   4564 C  CD2 . LEU   B 1 289 ? 4.400   13.016  20.774  1.00 27.51  ? 294 LEU   B CD2 1 
ATOM   4565 N  N   . VAL   B 1 290 ? 3.510   17.222  19.103  1.00 21.68  ? 295 VAL   B N   1 
ATOM   4566 C  CA  . VAL   B 1 290 ? 2.679   18.186  18.387  1.00 22.84  ? 295 VAL   B CA  1 
ATOM   4567 C  C   . VAL   B 1 290 ? 1.680   17.596  17.383  1.00 25.43  ? 295 VAL   B C   1 
ATOM   4568 O  O   . VAL   B 1 290 ? 1.757   16.440  16.932  1.00 24.08  ? 295 VAL   B O   1 
ATOM   4569 C  CB  . VAL   B 1 290 ? 3.582   19.265  17.671  1.00 24.61  ? 295 VAL   B CB  1 
ATOM   4570 C  CG1 . VAL   B 1 290 ? 4.520   19.985  18.650  1.00 24.76  ? 295 VAL   B CG1 1 
ATOM   4571 C  CG2 . VAL   B 1 290 ? 4.391   18.660  16.524  1.00 24.66  ? 295 VAL   B CG2 1 
ATOM   4572 N  N   . GLU   B 1 291 ? 0.775   18.503  16.957  1.00 24.52  ? 296 GLU   B N   1 
ATOM   4573 C  CA  . GLU   B 1 291 ? -0.199  18.351  15.897  1.00 24.49  ? 296 GLU   B CA  1 
ATOM   4574 C  C   . GLU   B 1 291 ? -1.345  17.378  16.209  1.00 26.61  ? 296 GLU   B C   1 
ATOM   4575 O  O   . GLU   B 1 291 ? -2.061  17.000  15.291  1.00 25.57  ? 296 GLU   B O   1 
ATOM   4576 C  CB  . GLU   B 1 291 ? 0.493   18.027  14.537  1.00 25.49  ? 296 GLU   B CB  1 
ATOM   4577 C  CG  . GLU   B 1 291 ? 1.384   19.164  14.021  1.00 27.01  ? 296 GLU   B CG  1 
ATOM   4578 C  CD  . GLU   B 1 291 ? 0.694   20.407  13.466  1.00 31.01  ? 296 GLU   B CD  1 
ATOM   4579 O  OE1 . GLU   B 1 291 ? -0.551  20.392  13.355  1.00 38.85  ? 296 GLU   B OE1 1 
ATOM   4580 O  OE2 . GLU   B 1 291 ? 1.397   21.381  13.115  1.00 29.34  ? 296 GLU   B OE2 1 
ATOM   4581 N  N   . VAL   B 1 292 ? -1.592  17.041  17.498  1.00 24.37  ? 297 VAL   B N   1 
ATOM   4582 C  CA  . VAL   B 1 292 ? -2.769  16.228  17.824  1.00 23.96  ? 297 VAL   B CA  1 
ATOM   4583 C  C   . VAL   B 1 292 ? -3.954  17.223  17.756  1.00 27.94  ? 297 VAL   B C   1 
ATOM   4584 O  O   . VAL   B 1 292 ? -3.936  18.243  18.446  1.00 27.67  ? 297 VAL   B O   1 
ATOM   4585 C  CB  . VAL   B 1 292 ? -2.704  15.568  19.219  1.00 27.26  ? 297 VAL   B CB  1 
ATOM   4586 C  CG1 . VAL   B 1 292 ? -4.047  14.922  19.580  1.00 27.48  ? 297 VAL   B CG1 1 
ATOM   4587 C  CG2 . VAL   B 1 292 ? -1.575  14.520  19.276  1.00 26.55  ? 297 VAL   B CG2 1 
ATOM   4588 N  N   . ASN   B 1 293 ? -4.925  16.937  16.904  1.00 26.63  ? 298 ASN   B N   1 
ATOM   4589 C  CA  . ASN   B 1 293 ? -6.101  17.805  16.744  1.00 27.22  ? 298 ASN   B CA  1 
ATOM   4590 C  C   . ASN   B 1 293 ? -7.307  16.894  16.923  1.00 29.51  ? 298 ASN   B C   1 
ATOM   4591 O  O   . ASN   B 1 293 ? -7.717  16.254  15.958  1.00 27.86  ? 298 ASN   B O   1 
ATOM   4592 C  CB  . ASN   B 1 293 ? -6.091  18.546  15.392  1.00 27.69  ? 298 ASN   B CB  1 
ATOM   4593 C  CG  . ASN   B 1 293 ? -7.294  19.467  15.238  1.00 35.87  ? 298 ASN   B CG  1 
ATOM   4594 O  OD1 . ASN   B 1 293 ? -8.292  19.304  15.948  1.00 30.04  ? 298 ASN   B OD1 1 
ATOM   4595 N  ND2 . ASN   B 1 293 ? -7.229  20.445  14.333  1.00 30.11  ? 298 ASN   B ND2 1 
ATOM   4596 N  N   . PRO   B 1 294 ? -7.866  16.783  18.167  1.00 30.46  ? 299 PRO   B N   1 
ATOM   4597 C  CA  . PRO   B 1 294 ? -8.978  15.841  18.394  1.00 31.04  ? 299 PRO   B CA  1 
ATOM   4598 C  C   . PRO   B 1 294 ? -10.215 16.089  17.545  1.00 36.17  ? 299 PRO   B C   1 
ATOM   4599 O  O   . PRO   B 1 294 ? -10.928 15.130  17.266  1.00 36.14  ? 299 PRO   B O   1 
ATOM   4600 C  CB  . PRO   B 1 294 ? -9.320  16.003  19.876  1.00 32.88  ? 299 PRO   B CB  1 
ATOM   4601 C  CG  . PRO   B 1 294 ? -8.201  16.727  20.467  1.00 37.32  ? 299 PRO   B CG  1 
ATOM   4602 C  CD  . PRO   B 1 294 ? -7.473  17.467  19.411  1.00 33.18  ? 299 PRO   B CD  1 
ATOM   4603 N  N   . GLN   B 1 295 ? -10.436 17.347  17.115  1.00 33.93  ? 300 GLN   B N   1 
ATOM   4604 C  CA  . GLN   B 1 295 ? -11.581 17.756  16.282  1.00 35.18  ? 300 GLN   B CA  1 
ATOM   4605 C  C   . GLN   B 1 295 ? -11.586 17.136  14.881  1.00 39.34  ? 300 GLN   B C   1 
ATOM   4606 O  O   . GLN   B 1 295 ? -12.644 17.070  14.251  1.00 38.56  ? 300 GLN   B O   1 
ATOM   4607 C  CB  . GLN   B 1 295 ? -11.659 19.292  16.174  1.00 36.59  ? 300 GLN   B CB  1 
ATOM   4608 C  CG  . GLN   B 1 295 ? -12.401 19.928  17.347  1.00 58.43  ? 300 GLN   B CG  1 
ATOM   4609 C  CD  . GLN   B 1 295 ? -12.491 21.438  17.281  1.00 80.86  ? 300 GLN   B CD  1 
ATOM   4610 O  OE1 . GLN   B 1 295 ? -12.597 22.055  16.209  1.00 76.44  ? 300 GLN   B OE1 1 
ATOM   4611 N  NE2 . GLN   B 1 295 ? -12.511 22.067  18.445  1.00 74.21  ? 300 GLN   B NE2 1 
ATOM   4612 N  N   . LEU   B 1 296 ? -10.413 16.681  14.387  1.00 34.20  ? 301 LEU   B N   1 
ATOM   4613 C  CA  . LEU   B 1 296 ? -10.304 16.114  13.045  1.00 32.94  ? 301 LEU   B CA  1 
ATOM   4614 C  C   . LEU   B 1 296 ? -10.523 14.617  13.007  1.00 35.73  ? 301 LEU   B C   1 
ATOM   4615 O  O   . LEU   B 1 296 ? -10.578 14.028  11.921  1.00 34.50  ? 301 LEU   B O   1 
ATOM   4616 C  CB  . LEU   B 1 296 ? -8.979  16.523  12.378  1.00 32.93  ? 301 LEU   B CB  1 
ATOM   4617 C  CG  . LEU   B 1 296 ? -8.794  18.047  12.235  1.00 37.05  ? 301 LEU   B CG  1 
ATOM   4618 C  CD1 . LEU   B 1 296 ? -7.506  18.370  11.545  1.00 36.85  ? 301 LEU   B CD1 1 
ATOM   4619 C  CD2 . LEU   B 1 296 ? -9.947  18.686  11.452  1.00 40.19  ? 301 LEU   B CD2 1 
ATOM   4620 N  N   . ALA   B 1 297 ? -10.724 14.003  14.182  1.00 33.54  ? 302 ALA   B N   1 
ATOM   4621 C  CA  . ALA   B 1 297 ? -11.038 12.583  14.254  1.00 35.08  ? 302 ALA   B CA  1 
ATOM   4622 C  C   . ALA   B 1 297 ? -12.492 12.438  13.791  1.00 40.77  ? 302 ALA   B C   1 
ATOM   4623 O  O   . ALA   B 1 297 ? -13.264 13.390  13.951  1.00 40.84  ? 302 ALA   B O   1 
ATOM   4624 C  CB  . ALA   B 1 297 ? -10.923 12.103  15.683  1.00 35.71  ? 302 ALA   B CB  1 
ATOM   4625 N  N   . THR   B 1 298 ? -12.855 11.280  13.205  1.00 37.46  ? 303 THR   B N   1 
ATOM   4626 C  CA  . THR   B 1 298 ? -14.243 11.077  12.763  1.00 37.02  ? 303 THR   B CA  1 
ATOM   4627 C  C   . THR   B 1 298 ? -15.062 10.510  13.913  1.00 39.00  ? 303 THR   B C   1 
ATOM   4628 O  O   . THR   B 1 298 ? -16.293 10.530  13.853  1.00 39.57  ? 303 THR   B O   1 
ATOM   4629 C  CB  . THR   B 1 298 ? -14.328 10.207  11.500  1.00 45.33  ? 303 THR   B CB  1 
ATOM   4630 O  OG1 . THR   B 1 298 ? -13.782 8.919   11.775  1.00 44.01  ? 303 THR   B OG1 1 
ATOM   4631 C  CG2 . THR   B 1 298 ? -13.653 10.848  10.278  1.00 47.40  ? 303 THR   B CG2 1 
ATOM   4632 N  N   . SER   B 1 299 ? -14.384 9.997   14.966  1.00 33.45  ? 304 SER   B N   1 
ATOM   4633 C  CA  . SER   B 1 299 ? -15.040 9.401   16.131  1.00 32.79  ? 304 SER   B CA  1 
ATOM   4634 C  C   . SER   B 1 299 ? -14.223 9.610   17.411  1.00 37.41  ? 304 SER   B C   1 
ATOM   4635 O  O   . SER   B 1 299 ? -13.023 9.898   17.343  1.00 35.28  ? 304 SER   B O   1 
ATOM   4636 C  CB  . SER   B 1 299 ? -15.224 7.904   15.906  1.00 35.49  ? 304 SER   B CB  1 
ATOM   4637 O  OG  . SER   B 1 299 ? -13.982 7.216   15.973  1.00 37.86  ? 304 SER   B OG  1 
ATOM   4638 N  N   . GLU   B 1 300 ? -14.855 9.387   18.574  1.00 35.30  ? 305 GLU   B N   1 
ATOM   4639 C  CA  . GLU   B 1 300 ? -14.188 9.500   19.876  1.00 35.81  ? 305 GLU   B CA  1 
ATOM   4640 C  C   . GLU   B 1 300 ? -13.052 8.482   19.986  1.00 40.76  ? 305 GLU   B C   1 
ATOM   4641 O  O   . GLU   B 1 300 ? -11.995 8.832   20.520  1.00 39.84  ? 305 GLU   B O   1 
ATOM   4642 C  CB  . GLU   B 1 300 ? -15.185 9.306   21.019  1.00 37.50  ? 305 GLU   B CB  1 
ATOM   4643 C  CG  . GLU   B 1 300 ? -14.636 9.662   22.392  1.00 49.02  ? 305 GLU   B CG  1 
ATOM   4644 C  CD  . GLU   B 1 300 ? -15.612 9.424   23.529  1.00 76.05  ? 305 GLU   B CD  1 
ATOM   4645 O  OE1 . GLU   B 1 300 ? -16.672 10.091  23.555  1.00 77.93  ? 305 GLU   B OE1 1 
ATOM   4646 O  OE2 . GLU   B 1 300 ? -15.313 8.574   24.400  1.00 66.79  ? 305 GLU   B OE2 1 
ATOM   4647 N  N   . GLU   B 1 301 ? -13.262 7.240   19.479  1.00 37.94  ? 306 GLU   B N   1 
ATOM   4648 C  CA  . GLU   B 1 301 ? -12.227 6.202   19.522  1.00 39.54  ? 306 GLU   B CA  1 
ATOM   4649 C  C   . GLU   B 1 301 ? -10.999 6.612   18.684  1.00 41.54  ? 306 GLU   B C   1 
ATOM   4650 O  O   . GLU   B 1 301 ? -9.875  6.368   19.123  1.00 40.60  ? 306 GLU   B O   1 
ATOM   4651 C  CB  . GLU   B 1 301 ? -12.767 4.798   19.171  1.00 41.88  ? 306 GLU   B CB  1 
ATOM   4652 C  CG  . GLU   B 1 301 ? -13.179 4.588   17.721  1.00 58.06  ? 306 GLU   B CG  1 
ATOM   4653 C  CD  . GLU   B 1 301 ? -13.282 3.148   17.241  1.00 93.68  ? 306 GLU   B CD  1 
ATOM   4654 O  OE1 . GLU   B 1 301 ? -12.620 2.262   17.831  1.00 92.37  ? 306 GLU   B OE1 1 
ATOM   4655 O  OE2 . GLU   B 1 301 ? -13.996 2.917   16.238  1.00 92.06  ? 306 GLU   B OE2 1 
ATOM   4656 N  N   . GLU   B 1 302 ? -11.220 7.288   17.531  1.00 35.83  ? 307 GLU   B N   1 
ATOM   4657 C  CA  . GLU   B 1 302 ? -10.165 7.829   16.665  1.00 35.12  ? 307 GLU   B CA  1 
ATOM   4658 C  C   . GLU   B 1 302 ? -9.370  8.909   17.420  1.00 37.43  ? 307 GLU   B C   1 
ATOM   4659 O  O   . GLU   B 1 302 ? -8.136  8.888   17.393  1.00 35.86  ? 307 GLU   B O   1 
ATOM   4660 C  CB  . GLU   B 1 302 ? -10.753 8.429   15.370  1.00 36.45  ? 307 GLU   B CB  1 
ATOM   4661 C  CG  . GLU   B 1 302 ? -10.953 7.432   14.241  1.00 46.60  ? 307 GLU   B CG  1 
ATOM   4662 C  CD  . GLU   B 1 302 ? -10.894 7.997   12.828  1.00 58.74  ? 307 GLU   B CD  1 
ATOM   4663 O  OE1 . GLU   B 1 302 ? -10.911 9.240   12.665  1.00 41.84  ? 307 GLU   B OE1 1 
ATOM   4664 O  OE2 . GLU   B 1 302 ? -10.814 7.187   11.875  1.00 54.71  ? 307 GLU   B OE2 1 
ATOM   4665 N  N   . ALA   B 1 303 ? -10.074 9.829   18.124  1.00 33.25  ? 308 ALA   B N   1 
ATOM   4666 C  CA  . ALA   B 1 303 ? -9.440  10.894  18.909  1.00 33.02  ? 308 ALA   B CA  1 
ATOM   4667 C  C   . ALA   B 1 303 ? -8.660  10.323  20.095  1.00 34.49  ? 308 ALA   B C   1 
ATOM   4668 O  O   . ALA   B 1 303 ? -7.511  10.719  20.337  1.00 34.21  ? 308 ALA   B O   1 
ATOM   4669 C  CB  . ALA   B 1 303 ? -10.496 11.889  19.402  1.00 33.98  ? 308 ALA   B CB  1 
ATOM   4670 N  N   . LYS   B 1 304 ? -9.278  9.394   20.829  1.00 30.01  ? 309 LYS   B N   1 
ATOM   4671 C  CA  . LYS   B 1 304 ? -8.659  8.767   22.001  1.00 29.66  ? 309 LYS   B CA  1 
ATOM   4672 C  C   . LYS   B 1 304 ? -7.453  7.936   21.597  1.00 32.88  ? 309 LYS   B C   1 
ATOM   4673 O  O   . LYS   B 1 304 ? -6.440  7.998   22.295  1.00 32.42  ? 309 LYS   B O   1 
ATOM   4674 C  CB  . LYS   B 1 304 ? -9.673  7.945   22.809  1.00 32.08  ? 309 LYS   B CB  1 
ATOM   4675 C  CG  . LYS   B 1 304 ? -10.601 8.854   23.604  1.00 38.86  ? 309 LYS   B CG  1 
ATOM   4676 C  CD  . LYS   B 1 304 ? -11.532 8.073   24.521  1.00 47.49  ? 309 LYS   B CD  1 
ATOM   4677 C  CE  . LYS   B 1 304 ? -12.243 8.989   25.489  1.00 64.44  ? 309 LYS   B CE  1 
ATOM   4678 N  NZ  . LYS   B 1 304 ? -13.255 8.255   26.298  1.00 74.97  ? 309 LYS   B NZ  1 
ATOM   4679 N  N   . THR   B 1 305 ? -7.539  7.223   20.448  1.00 30.35  ? 310 THR   B N   1 
ATOM   4680 C  CA  . THR   B 1 305 ? -6.434  6.419   19.887  1.00 29.58  ? 310 THR   B CA  1 
ATOM   4681 C  C   . THR   B 1 305 ? -5.221  7.331   19.645  1.00 29.91  ? 310 THR   B C   1 
ATOM   4682 O  O   . THR   B 1 305 ? -4.117  6.997   20.087  1.00 29.56  ? 310 THR   B O   1 
ATOM   4683 C  CB  . THR   B 1 305 ? -6.903  5.661   18.634  1.00 40.20  ? 310 THR   B CB  1 
ATOM   4684 O  OG1 . THR   B 1 305 ? -7.776  4.626   19.082  1.00 43.60  ? 310 THR   B OG1 1 
ATOM   4685 C  CG2 . THR   B 1 305 ? -5.750  5.028   17.837  1.00 43.58  ? 310 THR   B CG2 1 
ATOM   4686 N  N   . THR   B 1 306 ? -5.448  8.495   19.016  1.00 26.35  ? 311 THR   B N   1 
ATOM   4687 C  CA  . THR   B 1 306 ? -4.385  9.461   18.712  1.00 25.38  ? 311 THR   B CA  1 
ATOM   4688 C  C   . THR   B 1 306 ? -3.754  10.000  20.001  1.00 28.11  ? 311 THR   B C   1 
ATOM   4689 O  O   . THR   B 1 306 ? -2.534  9.993   20.137  1.00 26.83  ? 311 THR   B O   1 
ATOM   4690 C  CB  . THR   B 1 306 ? -4.885  10.577  17.792  1.00 28.86  ? 311 THR   B CB  1 
ATOM   4691 O  OG1 . THR   B 1 306 ? -5.540  10.011  16.650  1.00 25.16  ? 311 THR   B OG1 1 
ATOM   4692 C  CG2 . THR   B 1 306 ? -3.767  11.491  17.319  1.00 24.15  ? 311 THR   B CG2 1 
ATOM   4693 N  N   . ALA   B 1 307 ? -4.597  10.413  20.975  1.00 26.01  ? 312 ALA   B N   1 
ATOM   4694 C  CA  . ALA   B 1 307 ? -4.141  10.905  22.280  1.00 25.96  ? 312 ALA   B CA  1 
ATOM   4695 C  C   . ALA   B 1 307 ? -3.378  9.804   23.056  1.00 26.52  ? 312 ALA   B C   1 
ATOM   4696 O  O   . ALA   B 1 307 ? -2.316  10.098  23.596  1.00 27.38  ? 312 ALA   B O   1 
ATOM   4697 C  CB  . ALA   B 1 307 ? -5.334  11.408  23.084  1.00 27.34  ? 312 ALA   B CB  1 
ATOM   4698 N  N   . ASN   B 1 308 ? -3.864  8.544   23.052  1.00 26.12  ? 313 ASN   B N   1 
ATOM   4699 C  CA  . ASN   B 1 308 ? -3.209  7.382   23.702  1.00 25.95  ? 313 ASN   B CA  1 
ATOM   4700 C  C   . ASN   B 1 308 ? -1.837  7.138   23.069  1.00 27.74  ? 313 ASN   B C   1 
ATOM   4701 O  O   . ASN   B 1 308 ? -0.876  6.847   23.774  1.00 27.19  ? 313 ASN   B O   1 
ATOM   4702 C  CB  . ASN   B 1 308 ? -4.077  6.115   23.623  1.00 28.51  ? 313 ASN   B CB  1 
ATOM   4703 C  CG  . ASN   B 1 308 ? -5.288  6.176   24.548  1.00 42.14  ? 313 ASN   B CG  1 
ATOM   4704 O  OD1 . ASN   B 1 308 ? -5.358  6.996   25.470  1.00 39.57  ? 313 ASN   B OD1 1 
ATOM   4705 N  ND2 . ASN   B 1 308 ? -6.296  5.362   24.273  1.00 32.36  ? 313 ASN   B ND2 1 
ATOM   4706 N  N   . LEU   B 1 309 ? -1.760  7.266   21.735  1.00 24.40  ? 314 LEU   B N   1 
ATOM   4707 C  CA  . LEU   B 1 309 ? -0.500  7.107   21.015  1.00 23.11  ? 314 LEU   B CA  1 
ATOM   4708 C  C   . LEU   B 1 309 ? 0.492   8.194   21.449  1.00 25.75  ? 314 LEU   B C   1 
ATOM   4709 O  O   . LEU   B 1 309 ? 1.659   7.877   21.718  1.00 23.34  ? 314 LEU   B O   1 
ATOM   4710 C  CB  . LEU   B 1 309 ? -0.789  7.216   19.526  1.00 23.53  ? 314 LEU   B CB  1 
ATOM   4711 C  CG  . LEU   B 1 309 ? 0.391   6.969   18.603  1.00 24.90  ? 314 LEU   B CG  1 
ATOM   4712 C  CD1 . LEU   B 1 309 ? 1.026   5.585   18.881  1.00 24.62  ? 314 LEU   B CD1 1 
ATOM   4713 C  CD2 . LEU   B 1 309 ? -0.084  7.055   17.162  1.00 26.07  ? 314 LEU   B CD2 1 
ATOM   4714 N  N   . ALA   B 1 310 ? 0.022   9.468   21.567  1.00 23.40  ? 315 ALA   B N   1 
ATOM   4715 C  CA  . ALA   B 1 310 ? 0.858   10.580  22.014  1.00 23.77  ? 315 ALA   B CA  1 
ATOM   4716 C  C   . ALA   B 1 310 ? 1.422   10.259  23.415  1.00 25.91  ? 315 ALA   B C   1 
ATOM   4717 O  O   . ALA   B 1 310 ? 2.631   10.381  23.641  1.00 23.58  ? 315 ALA   B O   1 
ATOM   4718 C  CB  . ALA   B 1 310 ? 0.040   11.876  22.039  1.00 23.84  ? 315 ALA   B CB  1 
ATOM   4719 N  N   . VAL   B 1 311 ? 0.573   9.751   24.322  1.00 22.80  ? 316 VAL   B N   1 
ATOM   4720 C  CA  . VAL   B 1 311 ? 1.033   9.356   25.664  1.00 23.39  ? 316 VAL   B CA  1 
ATOM   4721 C  C   . VAL   B 1 311 ? 2.089   8.243   25.564  1.00 23.81  ? 316 VAL   B C   1 
ATOM   4722 O  O   . VAL   B 1 311 ? 3.122   8.336   26.236  1.00 24.57  ? 316 VAL   B O   1 
ATOM   4723 C  CB  . VAL   B 1 311 ? -0.155  8.982   26.592  1.00 26.90  ? 316 VAL   B CB  1 
ATOM   4724 C  CG1 . VAL   B 1 311 ? 0.339   8.366   27.905  1.00 26.39  ? 316 VAL   B CG1 1 
ATOM   4725 C  CG2 . VAL   B 1 311 ? -1.003  10.223  26.863  1.00 26.95  ? 316 VAL   B CG2 1 
ATOM   4726 N  N   . ASP   B 1 312 ? 1.861   7.244   24.687  1.00 21.77  ? 317 ASP   B N   1 
ATOM   4727 C  CA  . ASP   B 1 312 ? 2.813   6.137   24.506  1.00 21.33  ? 317 ASP   B CA  1 
ATOM   4728 C  C   . ASP   B 1 312 ? 4.180   6.640   24.042  1.00 22.89  ? 317 ASP   B C   1 
ATOM   4729 O  O   . ASP   B 1 312 ? 5.197   6.158   24.551  1.00 23.86  ? 317 ASP   B O   1 
ATOM   4730 C  CB  . ASP   B 1 312 ? 2.260   5.080   23.535  1.00 23.45  ? 317 ASP   B CB  1 
ATOM   4731 C  CG  . ASP   B 1 312 ? 1.248   4.134   24.147  1.00 27.69  ? 317 ASP   B CG  1 
ATOM   4732 O  OD1 . ASP   B 1 312 ? 1.100   4.138   25.388  1.00 30.84  ? 317 ASP   B OD1 1 
ATOM   4733 O  OD2 . ASP   B 1 312 ? 0.617   3.366   23.388  1.00 30.03  ? 317 ASP   B OD2 1 
ATOM   4734 N  N   . VAL   B 1 313 ? 4.212   7.577   23.102  1.00 20.23  ? 318 VAL   B N   1 
ATOM   4735 C  CA  . VAL   B 1 313 ? 5.488   8.136   22.633  1.00 20.22  ? 318 VAL   B CA  1 
ATOM   4736 C  C   . VAL   B 1 313 ? 6.243   8.799   23.803  1.00 23.32  ? 318 VAL   B C   1 
ATOM   4737 O  O   . VAL   B 1 313 ? 7.461   8.586   23.967  1.00 23.42  ? 318 VAL   B O   1 
ATOM   4738 C  CB  . VAL   B 1 313 ? 5.277   9.152   21.472  1.00 23.02  ? 318 VAL   B CB  1 
ATOM   4739 C  CG1 . VAL   B 1 313 ? 6.599   9.886   21.166  1.00 23.53  ? 318 VAL   B CG1 1 
ATOM   4740 C  CG2 . VAL   B 1 313 ? 4.735   8.463   20.217  1.00 22.86  ? 318 VAL   B CG2 1 
ATOM   4741 N  N   . ILE   B 1 314 ? 5.532   9.657   24.573  1.00 20.78  ? 319 ILE   B N   1 
ATOM   4742 C  CA  . ILE   B 1 314 ? 6.149   10.388  25.684  1.00 21.18  ? 319 ILE   B CA  1 
ATOM   4743 C  C   . ILE   B 1 314 ? 6.642   9.413   26.758  1.00 23.55  ? 319 ILE   B C   1 
ATOM   4744 O  O   . ILE   B 1 314 ? 7.811   9.483   27.158  1.00 23.60  ? 319 ILE   B O   1 
ATOM   4745 C  CB  . ILE   B 1 314 ? 5.232   11.494  26.236  1.00 24.71  ? 319 ILE   B CB  1 
ATOM   4746 C  CG1 . ILE   B 1 314 ? 4.905   12.518  25.120  1.00 25.00  ? 319 ILE   B CG1 1 
ATOM   4747 C  CG2 . ILE   B 1 314 ? 5.907   12.186  27.445  1.00 26.21  ? 319 ILE   B CG2 1 
ATOM   4748 C  CD1 . ILE   B 1 314 ? 3.625   13.343  25.403  1.00 28.31  ? 319 ILE   B CD1 1 
ATOM   4749 N  N   . ALA   B 1 315 ? 5.795   8.453   27.133  1.00 23.10  ? 320 ALA   B N   1 
ATOM   4750 C  CA  . ALA   B 1 315 ? 6.131   7.425   28.123  1.00 23.52  ? 320 ALA   B CA  1 
ATOM   4751 C  C   . ALA   B 1 315 ? 7.349   6.614   27.681  1.00 24.81  ? 320 ALA   B C   1 
ATOM   4752 O  O   . ALA   B 1 315 ? 8.245   6.368   28.489  1.00 24.20  ? 320 ALA   B O   1 
ATOM   4753 C  CB  . ALA   B 1 315 ? 4.948   6.507   28.362  1.00 24.99  ? 320 ALA   B CB  1 
ATOM   4754 N  N   . SER   B 1 316 ? 7.433   6.282   26.361  1.00 21.51  ? 321 SER   B N   1 
ATOM   4755 C  CA  . SER   B 1 316 ? 8.542   5.469   25.847  1.00 20.92  ? 321 SER   B CA  1 
ATOM   4756 C  C   . SER   B 1 316 ? 9.821   6.263   25.832  1.00 25.02  ? 321 SER   B C   1 
ATOM   4757 O  O   . SER   B 1 316 ? 10.898  5.697   25.973  1.00 25.61  ? 321 SER   B O   1 
ATOM   4758 C  CB  . SER   B 1 316 ? 8.209   4.914   24.464  1.00 23.79  ? 321 SER   B CB  1 
ATOM   4759 O  OG  . SER   B 1 316 ? 7.163   3.965   24.617  1.00 26.36  ? 321 SER   B OG  1 
ATOM   4760 N  N   . SER   B 1 317 ? 9.699   7.588   25.746  1.00 22.64  ? 322 SER   B N   1 
ATOM   4761 C  CA  . SER   B 1 317 ? 10.866  8.451   25.744  1.00 22.85  ? 322 SER   B CA  1 
ATOM   4762 C  C   . SER   B 1 317 ? 11.472  8.550   27.161  1.00 26.33  ? 322 SER   B C   1 
ATOM   4763 O  O   . SER   B 1 317 ? 12.646  8.932   27.297  1.00 27.37  ? 322 SER   B O   1 
ATOM   4764 C  CB  . SER   B 1 317 ? 10.490  9.821   25.196  1.00 24.84  ? 322 SER   B CB  1 
ATOM   4765 O  OG  . SER   B 1 317 ? 10.075  9.700   23.842  1.00 26.76  ? 322 SER   B OG  1 
ATOM   4766 N  N   . PHE   B 1 318 ? 10.690  8.148   28.195  1.00 23.10  ? 323 PHE   B N   1 
ATOM   4767 C  CA  . PHE   B 1 318 ? 11.131  8.160   29.593  1.00 23.82  ? 323 PHE   B CA  1 
ATOM   4768 C  C   . PHE   B 1 318 ? 11.197  6.767   30.257  1.00 27.41  ? 323 PHE   B C   1 
ATOM   4769 O  O   . PHE   B 1 318 ? 11.241  6.690   31.489  1.00 28.37  ? 323 PHE   B O   1 
ATOM   4770 C  CB  . PHE   B 1 318 ? 10.307  9.157   30.422  1.00 25.93  ? 323 PHE   B CB  1 
ATOM   4771 C  CG  . PHE   B 1 318 ? 10.616  10.566  29.969  1.00 25.90  ? 323 PHE   B CG  1 
ATOM   4772 C  CD1 . PHE   B 1 318 ? 11.830  11.175  30.306  1.00 28.35  ? 323 PHE   B CD1 1 
ATOM   4773 C  CD2 . PHE   B 1 318 ? 9.745   11.253  29.135  1.00 26.54  ? 323 PHE   B CD2 1 
ATOM   4774 C  CE1 . PHE   B 1 318 ? 12.139  12.464  29.853  1.00 28.19  ? 323 PHE   B CE1 1 
ATOM   4775 C  CE2 . PHE   B 1 318 ? 10.051  12.547  28.686  1.00 28.23  ? 323 PHE   B CE2 1 
ATOM   4776 C  CZ  . PHE   B 1 318 ? 11.240  13.149  29.060  1.00 27.41  ? 323 PHE   B CZ  1 
ATOM   4777 N  N   . GLY   B 1 319 ? 11.255  5.688   29.462  1.00 26.02  ? 324 GLY   B N   1 
ATOM   4778 C  CA  . GLY   B 1 319 ? 11.448  4.359   30.032  1.00 26.13  ? 324 GLY   B CA  1 
ATOM   4779 C  C   . GLY   B 1 319 ? 10.422  3.285   29.763  1.00 28.77  ? 324 GLY   B C   1 
ATOM   4780 O  O   . GLY   B 1 319 ? 10.726  2.108   29.989  1.00 28.57  ? 324 GLY   B O   1 
ATOM   4781 N  N   . GLN   B 1 320 ? 9.198   3.646   29.321  1.00 23.82  ? 325 GLN   B N   1 
ATOM   4782 C  CA  . GLN   B 1 320 ? 8.238   2.591   28.977  1.00 26.02  ? 325 GLN   B CA  1 
ATOM   4783 C  C   . GLN   B 1 320 ? 8.812   1.756   27.794  1.00 29.88  ? 325 GLN   B C   1 
ATOM   4784 O  O   . GLN   B 1 320 ? 9.359   2.313   26.846  1.00 28.51  ? 325 GLN   B O   1 
ATOM   4785 C  CB  . GLN   B 1 320 ? 6.881   3.188   28.590  1.00 28.60  ? 325 GLN   B CB  1 
ATOM   4786 C  CG  . GLN   B 1 320 ? 5.894   2.206   27.950  1.00 36.89  ? 325 GLN   B CG  1 
ATOM   4787 C  CD  . GLN   B 1 320 ? 4.551   2.852   27.736  1.00 52.46  ? 325 GLN   B CD  1 
ATOM   4788 O  OE1 . GLN   B 1 320 ? 4.044   2.973   26.597  1.00 45.50  ? 325 GLN   B OE1 1 
ATOM   4789 N  NE2 . GLN   B 1 320 ? 3.982   3.336   28.832  1.00 34.59  ? 325 GLN   B NE2 1 
ATOM   4790 N  N   . THR   B 1 321 ? 8.719   0.433   27.892  1.00 32.12  ? 326 THR   B N   1 
ATOM   4791 C  CA  . THR   B 1 321 ? 9.180   -0.449  26.822  1.00 33.09  ? 326 THR   B CA  1 
ATOM   4792 C  C   . THR   B 1 321 ? 8.177   -1.577  26.630  1.00 36.74  ? 326 THR   B C   1 
ATOM   4793 O  O   . THR   B 1 321 ? 7.283   -1.745  27.458  1.00 37.13  ? 326 THR   B O   1 
ATOM   4794 C  CB  . THR   B 1 321 ? 10.590  -0.973  27.100  1.00 48.77  ? 326 THR   B CB  1 
ATOM   4795 O  OG1 . THR   B 1 321 ? 11.050  -1.672  25.932  1.00 60.27  ? 326 THR   B OG1 1 
ATOM   4796 C  CG2 . THR   B 1 321 ? 10.631  -1.890  28.292  1.00 42.85  ? 326 THR   B CG2 1 
ATOM   4797 N  N   . ARG   B 1 322 ? 8.343   -2.335  25.549  1.00 34.28  ? 327 ARG   B N   1 
ATOM   4798 C  CA  . ARG   B 1 322 ? 7.494   -3.481  25.205  1.00 32.32  ? 327 ARG   B CA  1 
ATOM   4799 C  C   . ARG   B 1 322 ? 7.718   -4.661  26.162  1.00 35.69  ? 327 ARG   B C   1 
ATOM   4800 O  O   . ARG   B 1 322 ? 6.789   -5.407  26.391  1.00 36.50  ? 327 ARG   B O   1 
ATOM   4801 C  CB  . ARG   B 1 322 ? 7.764   -3.933  23.758  1.00 30.95  ? 327 ARG   B CB  1 
ATOM   4802 C  CG  . ARG   B 1 322 ? 6.680   -3.535  22.721  1.00 37.14  ? 327 ARG   B CG  1 
ATOM   4803 C  CD  . ARG   B 1 322 ? 6.762   -2.081  22.273  1.00 26.83  ? 327 ARG   B CD  1 
ATOM   4804 N  NE  . ARG   B 1 322 ? 8.068   -1.758  21.696  1.00 22.58  ? 327 ARG   B NE  1 
ATOM   4805 C  CZ  . ARG   B 1 322 ? 8.412   -1.975  20.424  1.00 24.29  ? 327 ARG   B CZ  1 
ATOM   4806 N  NH1 . ARG   B 1 322 ? 7.539   -2.505  19.568  1.00 25.37  ? 327 ARG   B NH1 1 
ATOM   4807 N  NH2 . ARG   B 1 322 ? 9.628   -1.661  19.998  1.00 21.54  ? 327 ARG   B NH2 1 
ATOM   4808 N  N   . GLU   B 1 323 ? 8.915   -4.824  26.726  1.00 33.66  ? 328 GLU   B N   1 
ATOM   4809 C  CA  . GLU   B 1 323 ? 9.243   -5.955  27.611  1.00 34.99  ? 328 GLU   B CA  1 
ATOM   4810 C  C   . GLU   B 1 323 ? 8.997   -5.721  29.092  1.00 40.41  ? 328 GLU   B C   1 
ATOM   4811 O  O   . GLU   B 1 323 ? 9.148   -6.650  29.895  1.00 38.04  ? 328 GLU   B O   1 
ATOM   4812 C  CB  . GLU   B 1 323 ? 10.721  -6.352  27.446  1.00 36.55  ? 328 GLU   B CB  1 
ATOM   4813 C  CG  . GLU   B 1 323 ? 11.401  -5.775  26.218  1.00 50.00  ? 328 GLU   B CG  1 
ATOM   4814 C  CD  . GLU   B 1 323 ? 12.630  -6.514  25.736  1.00 57.25  ? 328 GLU   B CD  1 
ATOM   4815 O  OE1 . GLU   B 1 323 ? 13.434  -6.968  26.583  1.00 58.15  ? 328 GLU   B OE1 1 
ATOM   4816 O  OE2 . GLU   B 1 323 ? 12.804  -6.604  24.500  1.00 35.54  ? 328 GLU   B OE2 1 
ATOM   4817 N  N   . GLY   B 1 324 ? 8.714   -4.477  29.460  1.00 40.19  ? 329 GLY   B N   1 
ATOM   4818 C  CA  . GLY   B 1 324 ? 8.621   -4.117  30.864  1.00 41.50  ? 329 GLY   B CA  1 
ATOM   4819 C  C   . GLY   B 1 324 ? 10.050  -3.961  31.343  1.00 46.92  ? 329 GLY   B C   1 
ATOM   4820 O  O   . GLY   B 1 324 ? 10.982  -3.851  30.536  1.00 49.63  ? 329 GLY   B O   1 
ATOM   4821 N  N   . GLY   B 1 325 ? 10.260  -4.010  32.627  1.00 42.28  ? 330 GLY   B N   1 
ATOM   4822 C  CA  . GLY   B 1 325 ? 11.618  -3.831  33.110  1.00 41.01  ? 330 GLY   B CA  1 
ATOM   4823 C  C   . GLY   B 1 325 ? 11.887  -2.404  33.531  1.00 42.73  ? 330 GLY   B C   1 
ATOM   4824 O  O   . GLY   B 1 325 ? 12.926  -2.144  34.126  1.00 41.80  ? 330 GLY   B O   1 
ATOM   4825 N  N   . HIS   B 1 326 ? 10.940  -1.473  33.253  1.00 38.45  ? 331 HIS   B N   1 
ATOM   4826 C  CA  . HIS   B 1 326 ? 11.043  -0.072  33.686  1.00 40.02  ? 331 HIS   B CA  1 
ATOM   4827 C  C   . HIS   B 1 326 ? 10.831  -0.019  35.204  1.00 42.89  ? 331 HIS   B C   1 
ATOM   4828 O  O   . HIS   B 1 326 ? 11.591  0.634   35.915  1.00 41.43  ? 331 HIS   B O   1 
ATOM   4829 C  CB  . HIS   B 1 326 ? 10.066  0.855   32.942  1.00 41.93  ? 331 HIS   B CB  1 
ATOM   4830 C  CG  . HIS   B 1 326 ? 8.738   0.251   32.578  1.00 46.56  ? 331 HIS   B CG  1 
ATOM   4831 N  ND1 . HIS   B 1 326 ? 8.561   -0.442  31.383  1.00 48.78  ? 331 HIS   B ND1 1 
ATOM   4832 C  CD2 . HIS   B 1 326 ? 7.547   0.331   33.217  1.00 49.20  ? 331 HIS   B CD2 1 
ATOM   4833 C  CE1 . HIS   B 1 326 ? 7.281   -0.784  31.353  1.00 48.69  ? 331 HIS   B CE1 1 
ATOM   4834 N  NE2 . HIS   B 1 326 ? 6.627   -0.335  32.433  1.00 49.17  ? 331 HIS   B NE2 1 
ATOM   4835 N  N   . ILE   B 1 327 ? 9.847   -0.778  35.689  1.00 39.84  ? 332 ILE   B N   1 
ATOM   4836 C  CA  . ILE   B 1 327 ? 9.544   -0.919  37.106  1.00 40.11  ? 332 ILE   B CA  1 
ATOM   4837 C  C   . ILE   B 1 327 ? 10.389  -2.093  37.607  1.00 45.76  ? 332 ILE   B C   1 
ATOM   4838 O  O   . ILE   B 1 327 ? 10.312  -3.183  37.034  1.00 46.04  ? 332 ILE   B O   1 
ATOM   4839 C  CB  . ILE   B 1 327 ? 8.013   -1.106  37.330  1.00 43.08  ? 332 ILE   B CB  1 
ATOM   4840 C  CG1 . ILE   B 1 327 ? 7.243   0.167   36.888  1.00 44.19  ? 332 ILE   B CG1 1 
ATOM   4841 C  CG2 . ILE   B 1 327 ? 7.709   -1.460  38.793  1.00 44.37  ? 332 ILE   B CG2 1 
ATOM   4842 C  CD1 . ILE   B 1 327 ? 5.811   -0.052  36.399  1.00 56.05  ? 332 ILE   B CD1 1 
ATOM   4843 N  N   . VAL   B 1 328 ? 11.243  -1.847  38.622  1.00 42.52  ? 333 VAL   B N   1 
ATOM   4844 C  CA  . VAL   B 1 328 ? 12.141  -2.840  39.223  1.00 43.05  ? 333 VAL   B CA  1 
ATOM   4845 C  C   . VAL   B 1 328 ? 11.405  -3.652  40.312  1.00 48.65  ? 333 VAL   B C   1 
ATOM   4846 O  O   . VAL   B 1 328 ? 10.748  -3.087  41.188  1.00 47.62  ? 333 VAL   B O   1 
ATOM   4847 C  CB  . VAL   B 1 328 ? 13.475  -2.197  39.703  1.00 48.23  ? 333 VAL   B CB  1 
ATOM   4848 C  CG1 . VAL   B 1 328 ? 14.258  -3.102  40.658  1.00 48.44  ? 333 VAL   B CG1 1 
ATOM   4849 C  CG2 . VAL   B 1 328 ? 14.343  -1.797  38.516  1.00 48.31  ? 333 VAL   B CG2 1 
ATOM   4850 N  N   . TYR   B 1 329 ? 11.473  -4.981  40.201  1.00 46.37  ? 334 TYR   B N   1 
ATOM   4851 C  CA  . TYR   B 1 329 ? 10.850  -5.917  41.133  1.00 46.47  ? 334 TYR   B CA  1 
ATOM   4852 C  C   . TYR   B 1 329 ? 11.970  -6.513  41.988  1.00 54.51  ? 334 TYR   B C   1 
ATOM   4853 O  O   . TYR   B 1 329 ? 12.953  -7.031  41.450  1.00 54.47  ? 334 TYR   B O   1 
ATOM   4854 C  CB  . TYR   B 1 329 ? 10.065  -6.978  40.350  1.00 46.67  ? 334 TYR   B CB  1 
ATOM   4855 C  CG  . TYR   B 1 329 ? 9.073   -7.765  41.170  1.00 47.24  ? 334 TYR   B CG  1 
ATOM   4856 C  CD1 . TYR   B 1 329 ? 7.784   -7.288  41.386  1.00 48.66  ? 334 TYR   B CD1 1 
ATOM   4857 C  CD2 . TYR   B 1 329 ? 9.398   -9.020  41.675  1.00 48.23  ? 334 TYR   B CD2 1 
ATOM   4858 C  CE1 . TYR   B 1 329 ? 6.857   -8.020  42.126  1.00 50.31  ? 334 TYR   B CE1 1 
ATOM   4859 C  CE2 . TYR   B 1 329 ? 8.473   -9.772  42.395  1.00 49.03  ? 334 TYR   B CE2 1 
ATOM   4860 C  CZ  . TYR   B 1 329 ? 7.207   -9.265  42.628  1.00 56.40  ? 334 TYR   B CZ  1 
ATOM   4861 O  OH  . TYR   B 1 329 ? 6.298   -10.014 43.339  1.00 59.56  ? 334 TYR   B OH  1 
ATOM   4862 N  N   . ASP   B 1 330 ? 11.859  -6.353  43.321  1.00 53.90  ? 335 ASP   B N   1 
ATOM   4863 C  CA  . ASP   B 1 330 ? 12.878  -6.766  44.293  1.00 54.83  ? 335 ASP   B CA  1 
ATOM   4864 C  C   . ASP   B 1 330 ? 13.063  -8.292  44.435  1.00 58.18  ? 335 ASP   B C   1 
ATOM   4865 O  O   . ASP   B 1 330 ? 14.149  -8.802  44.147  1.00 57.52  ? 335 ASP   B O   1 
ATOM   4866 C  CB  . ASP   B 1 330 ? 12.625  -6.112  45.674  1.00 57.50  ? 335 ASP   B CB  1 
ATOM   4867 C  CG  . ASP   B 1 330 ? 11.162  -6.031  46.092  1.00 72.56  ? 335 ASP   B CG  1 
ATOM   4868 O  OD1 . ASP   B 1 330 ? 10.529  -7.100  46.259  1.00 73.89  ? 335 ASP   B OD1 1 
ATOM   4869 O  OD2 . ASP   B 1 330 ? 10.657  -4.900  46.275  1.00 78.64  ? 335 ASP   B OD2 1 
ATOM   4870 N  N   . GLN   B 1 331 ? 12.025  -9.001  44.915  1.00 54.26  ? 336 GLN   B N   1 
ATOM   4871 C  CA  . GLN   B 1 331 ? 12.031  -10.440 45.176  1.00 53.36  ? 336 GLN   B CA  1 
ATOM   4872 C  C   . GLN   B 1 331 ? 10.629  -11.009 45.021  1.00 54.07  ? 336 GLN   B C   1 
ATOM   4873 O  O   . GLN   B 1 331 ? 9.641   -10.312 45.272  1.00 53.17  ? 336 GLN   B O   1 
ATOM   4874 C  CB  . GLN   B 1 331 ? 12.499  -10.720 46.623  1.00 55.26  ? 336 GLN   B CB  1 
ATOM   4875 C  CG  . GLN   B 1 331 ? 14.006  -10.887 46.810  1.00 79.66  ? 336 GLN   B CG  1 
ATOM   4876 C  CD  . GLN   B 1 331 ? 14.368  -11.501 48.152  1.00 100.91 ? 336 GLN   B CD  1 
ATOM   4877 O  OE1 . GLN   B 1 331 ? 15.176  -12.437 48.232  1.00 94.59  ? 336 GLN   B OE1 1 
ATOM   4878 N  NE2 . GLN   B 1 331 ? 13.803  -10.982 49.241  1.00 93.41  ? 336 GLN   B NE2 1 
ATOM   4879 N  N   . LEU   B 1 332 ? 10.548  -12.296 44.665  1.00 49.08  ? 337 LEU   B N   1 
ATOM   4880 C  CA  . LEU   B 1 332 ? 9.277   -12.996 44.526  1.00 48.60  ? 337 LEU   B CA  1 
ATOM   4881 C  C   . LEU   B 1 332 ? 8.748   -13.385 45.915  1.00 54.46  ? 337 LEU   B C   1 
ATOM   4882 O  O   . LEU   B 1 332 ? 9.551   -13.778 46.767  1.00 53.05  ? 337 LEU   B O   1 
ATOM   4883 C  CB  . LEU   B 1 332 ? 9.447   -14.259 43.655  1.00 48.43  ? 337 LEU   B CB  1 
ATOM   4884 C  CG  . LEU   B 1 332 ? 9.664   -14.005 42.153  1.00 52.31  ? 337 LEU   B CG  1 
ATOM   4885 C  CD1 . LEU   B 1 332 ? 10.265  -15.215 41.477  1.00 51.95  ? 337 LEU   B CD1 1 
ATOM   4886 C  CD2 . LEU   B 1 332 ? 8.374   -13.576 41.465  1.00 53.89  ? 337 LEU   B CD2 1 
ATOM   4887 N  N   . PRO   B 1 333 ? 7.420   -13.271 46.172  1.00 52.71  ? 338 PRO   B N   1 
ATOM   4888 C  CA  . PRO   B 1 333 ? 6.893   -13.692 47.479  1.00 53.54  ? 338 PRO   B CA  1 
ATOM   4889 C  C   . PRO   B 1 333 ? 6.878   -15.219 47.576  1.00 60.31  ? 338 PRO   B C   1 
ATOM   4890 O  O   . PRO   B 1 333 ? 6.626   -15.895 46.575  1.00 60.27  ? 338 PRO   B O   1 
ATOM   4891 C  CB  . PRO   B 1 333 ? 5.467   -13.116 47.503  1.00 55.05  ? 338 PRO   B CB  1 
ATOM   4892 C  CG  . PRO   B 1 333 ? 5.309   -12.325 46.233  1.00 59.37  ? 338 PRO   B CG  1 
ATOM   4893 C  CD  . PRO   B 1 333 ? 6.330   -12.836 45.278  1.00 54.53  ? 338 PRO   B CD  1 
ATOM   4894 N  N   . THR   B 1 334 ? 7.177   -15.758 48.768  1.00 58.17  ? 339 THR   B N   1 
ATOM   4895 C  CA  . THR   B 1 334 ? 7.217   -17.205 49.014  1.00 58.43  ? 339 THR   B CA  1 
ATOM   4896 C  C   . THR   B 1 334 ? 5.917   -17.706 49.659  1.00 62.74  ? 339 THR   B C   1 
ATOM   4897 O  O   . THR   B 1 334 ? 5.316   -16.967 50.447  1.00 62.14  ? 339 THR   B O   1 
ATOM   4898 C  CB  . THR   B 1 334 ? 8.452   -17.594 49.845  1.00 69.67  ? 339 THR   B CB  1 
ATOM   4899 O  OG1 . THR   B 1 334 ? 8.487   -16.803 51.036  1.00 73.21  ? 339 THR   B OG1 1 
ATOM   4900 C  CG2 . THR   B 1 334 ? 9.759   -17.453 49.063  1.00 68.15  ? 339 THR   B CG2 1 
ATOM   4901 N  N   . PRO   B 1 335 ? 5.457   -18.947 49.339  1.00 59.92  ? 340 PRO   B N   1 
ATOM   4902 C  CA  . PRO   B 1 335 ? 4.216   -19.461 49.956  1.00 63.61  ? 340 PRO   B CA  1 
ATOM   4903 C  C   . PRO   B 1 335 ? 4.336   -19.656 51.466  1.00 83.88  ? 340 PRO   B C   1 
ATOM   4904 O  O   . PRO   B 1 335 ? 5.429   -19.917 51.963  1.00 53.10  ? 340 PRO   B O   1 
ATOM   4905 C  CB  . PRO   B 1 335 ? 4.003   -20.809 49.253  1.00 64.70  ? 340 PRO   B CB  1 
ATOM   4906 C  CG  . PRO   B 1 335 ? 4.840   -20.745 48.009  1.00 67.77  ? 340 PRO   B CG  1 
ATOM   4907 C  CD  . PRO   B 1 335 ? 6.030   -19.941 48.409  1.00 62.47  ? 340 PRO   B CD  1 
ATOM   4908 N  N   . VAL   C 1 18  ? 1.720   -36.613 5.129   1.00 59.87  ? 23  VAL   C N   1 
ATOM   4909 C  CA  . VAL   C 1 18  ? 0.479   -36.983 5.812   1.00 59.54  ? 23  VAL   C CA  1 
ATOM   4910 C  C   . VAL   C 1 18  ? 0.639   -36.803 7.338   1.00 62.48  ? 23  VAL   C C   1 
ATOM   4911 O  O   . VAL   C 1 18  ? 1.500   -37.442 7.956   1.00 62.58  ? 23  VAL   C O   1 
ATOM   4912 C  CB  . VAL   C 1 18  ? -0.018  -38.411 5.415   1.00 63.86  ? 23  VAL   C CB  1 
ATOM   4913 C  CG1 . VAL   C 1 18  ? -1.228  -38.840 6.245   1.00 63.66  ? 23  VAL   C CG1 1 
ATOM   4914 C  CG2 . VAL   C 1 18  ? -0.343  -38.495 3.923   1.00 63.70  ? 23  VAL   C CG2 1 
ATOM   4915 N  N   . HIS   C 1 19  ? -0.192  -35.927 7.928   1.00 56.96  ? 24  HIS   C N   1 
ATOM   4916 C  CA  . HIS   C 1 19  ? -0.196  -35.651 9.369   1.00 55.52  ? 24  HIS   C CA  1 
ATOM   4917 C  C   . HIS   C 1 19  ? -1.484  -36.182 9.982   1.00 55.08  ? 24  HIS   C C   1 
ATOM   4918 O  O   . HIS   C 1 19  ? -2.563  -35.868 9.486   1.00 54.00  ? 24  HIS   C O   1 
ATOM   4919 C  CB  . HIS   C 1 19  ? -0.127  -34.130 9.659   1.00 56.40  ? 24  HIS   C CB  1 
ATOM   4920 C  CG  . HIS   C 1 19  ? 0.973   -33.394 8.963   1.00 60.08  ? 24  HIS   C CG  1 
ATOM   4921 N  ND1 . HIS   C 1 19  ? 2.292   -33.519 9.360   1.00 62.07  ? 24  HIS   C ND1 1 
ATOM   4922 C  CD2 . HIS   C 1 19  ? 0.906   -32.505 7.946   1.00 61.79  ? 24  HIS   C CD2 1 
ATOM   4923 C  CE1 . HIS   C 1 19  ? 2.986   -32.729 8.556   1.00 61.34  ? 24  HIS   C CE1 1 
ATOM   4924 N  NE2 . HIS   C 1 19  ? 2.194   -32.097 7.691   1.00 61.52  ? 24  HIS   C NE2 1 
ATOM   4925 N  N   . SER   C 1 20  ? -1.389  -36.939 11.075  1.00 49.89  ? 25  SER   C N   1 
ATOM   4926 C  CA  . SER   C 1 20  ? -2.586  -37.401 11.787  1.00 49.18  ? 25  SER   C CA  1 
ATOM   4927 C  C   . SER   C 1 20  ? -2.901  -36.307 12.817  1.00 50.16  ? 25  SER   C C   1 
ATOM   4928 O  O   . SER   C 1 20  ? -2.054  -36.002 13.643  1.00 48.58  ? 25  SER   C O   1 
ATOM   4929 C  CB  . SER   C 1 20  ? -2.344  -38.756 12.444  1.00 52.74  ? 25  SER   C CB  1 
ATOM   4930 O  OG  . SER   C 1 20  ? -2.346  -39.769 11.450  1.00 60.16  ? 25  SER   C OG  1 
ATOM   4931 N  N   . VAL   C 1 21  ? -4.064  -35.643 12.690  1.00 46.61  ? 26  VAL   C N   1 
ATOM   4932 C  CA  . VAL   C 1 21  ? -4.425  -34.505 13.552  1.00 46.35  ? 26  VAL   C CA  1 
ATOM   4933 C  C   . VAL   C 1 21  ? -5.730  -34.722 14.342  1.00 47.93  ? 26  VAL   C C   1 
ATOM   4934 O  O   . VAL   C 1 21  ? -6.790  -34.918 13.742  1.00 46.63  ? 26  VAL   C O   1 
ATOM   4935 C  CB  . VAL   C 1 21  ? -4.475  -33.187 12.716  1.00 50.28  ? 26  VAL   C CB  1 
ATOM   4936 C  CG1 . VAL   C 1 21  ? -4.898  -31.991 13.565  1.00 50.07  ? 26  VAL   C CG1 1 
ATOM   4937 C  CG2 . VAL   C 1 21  ? -3.146  -32.911 12.011  1.00 50.07  ? 26  VAL   C CG2 1 
ATOM   4938 N  N   . ALA   C 1 22  ? -5.645  -34.627 15.681  1.00 44.04  ? 27  ALA   C N   1 
ATOM   4939 C  CA  . ALA   C 1 22  ? -6.782  -34.728 16.597  1.00 43.66  ? 27  ALA   C CA  1 
ATOM   4940 C  C   . ALA   C 1 22  ? -7.182  -33.319 17.017  1.00 46.57  ? 27  ALA   C C   1 
ATOM   4941 O  O   . ALA   C 1 22  ? -6.323  -32.558 17.474  1.00 47.23  ? 27  ALA   C O   1 
ATOM   4942 C  CB  . ALA   C 1 22  ? -6.411  -35.550 17.824  1.00 44.31  ? 27  ALA   C CB  1 
ATOM   4943 N  N   . VAL   C 1 23  ? -8.463  -32.954 16.798  1.00 41.22  ? 28  VAL   C N   1 
ATOM   4944 C  CA  . VAL   C 1 23  ? -9.023  -31.651 17.153  1.00 40.25  ? 28  VAL   C CA  1 
ATOM   4945 C  C   . VAL   C 1 23  ? -9.867  -31.818 18.428  1.00 44.15  ? 28  VAL   C C   1 
ATOM   4946 O  O   . VAL   C 1 23  ? -10.811 -32.621 18.456  1.00 41.55  ? 28  VAL   C O   1 
ATOM   4947 C  CB  . VAL   C 1 23  ? -9.796  -30.993 15.975  1.00 43.92  ? 28  VAL   C CB  1 
ATOM   4948 C  CG1 . VAL   C 1 23  ? -10.526 -29.717 16.409  1.00 43.55  ? 28  VAL   C CG1 1 
ATOM   4949 C  CG2 . VAL   C 1 23  ? -8.855  -30.700 14.804  1.00 43.71  ? 28  VAL   C CG2 1 
ATOM   4950 N  N   . ILE   C 1 24  ? -9.500  -31.070 19.485  1.00 40.56  ? 29  ILE   C N   1 
ATOM   4951 C  CA  . ILE   C 1 24  ? -10.194 -31.088 20.780  1.00 40.70  ? 29  ILE   C CA  1 
ATOM   4952 C  C   . ILE   C 1 24  ? -10.751 -29.702 21.061  1.00 45.75  ? 29  ILE   C C   1 
ATOM   4953 O  O   . ILE   C 1 24  ? -10.012 -28.717 21.038  1.00 44.45  ? 29  ILE   C O   1 
ATOM   4954 C  CB  . ILE   C 1 24  ? -9.268  -31.582 21.936  1.00 43.82  ? 29  ILE   C CB  1 
ATOM   4955 C  CG1 . ILE   C 1 24  ? -8.834  -33.036 21.727  1.00 44.02  ? 29  ILE   C CG1 1 
ATOM   4956 C  CG2 . ILE   C 1 24  ? -9.948  -31.413 23.319  1.00 45.85  ? 29  ILE   C CG2 1 
ATOM   4957 C  CD1 . ILE   C 1 24  ? -7.640  -33.454 22.562  1.00 51.25  ? 29  ILE   C CD1 1 
ATOM   4958 N  N   . GLY   C 1 25  ? -12.053 -29.643 21.285  1.00 43.97  ? 30  GLY   C N   1 
ATOM   4959 C  CA  . GLY   C 1 25  ? -12.731 -28.418 21.672  1.00 44.60  ? 30  GLY   C CA  1 
ATOM   4960 C  C   . GLY   C 1 25  ? -12.672 -28.343 23.184  1.00 49.85  ? 30  GLY   C C   1 
ATOM   4961 O  O   . GLY   C 1 25  ? -13.279 -29.183 23.857  1.00 48.83  ? 30  GLY   C O   1 
ATOM   4962 N  N   . ALA   C 1 26  ? -11.872 -27.404 23.732  1.00 46.64  ? 31  ALA   C N   1 
ATOM   4963 C  CA  . ALA   C 1 26  ? -11.755 -27.209 25.180  1.00 46.98  ? 31  ALA   C CA  1 
ATOM   4964 C  C   . ALA   C 1 26  ? -12.409 -25.859 25.531  1.00 52.81  ? 31  ALA   C C   1 
ATOM   4965 O  O   . ALA   C 1 26  ? -11.730 -24.828 25.543  1.00 51.60  ? 31  ALA   C O   1 
ATOM   4966 C  CB  . ALA   C 1 26  ? -10.298 -27.248 25.618  1.00 47.69  ? 31  ALA   C CB  1 
ATOM   4967 N  N   . PRO   C 1 27  ? -13.743 -25.833 25.769  1.00 52.05  ? 32  PRO   C N   1 
ATOM   4968 C  CA  . PRO   C 1 27  ? -14.422 -24.550 26.012  1.00 53.30  ? 32  PRO   C CA  1 
ATOM   4969 C  C   . PRO   C 1 27  ? -14.211 -23.956 27.413  1.00 59.53  ? 32  PRO   C C   1 
ATOM   4970 O  O   . PRO   C 1 27  ? -15.177 -23.707 28.132  1.00 59.70  ? 32  PRO   C O   1 
ATOM   4971 C  CB  . PRO   C 1 27  ? -15.899 -24.865 25.705  1.00 55.01  ? 32  PRO   C CB  1 
ATOM   4972 C  CG  . PRO   C 1 27  ? -15.924 -26.287 25.169  1.00 58.82  ? 32  PRO   C CG  1 
ATOM   4973 C  CD  . PRO   C 1 27  ? -14.718 -26.939 25.752  1.00 53.90  ? 32  PRO   C CD  1 
ATOM   4974 N  N   . PHE   C 1 28  ? -12.938 -23.714 27.783  1.00 57.90  ? 33  PHE   C N   1 
ATOM   4975 C  CA  . PHE   C 1 28  ? -12.506 -23.122 29.056  1.00 58.80  ? 33  PHE   C CA  1 
ATOM   4976 C  C   . PHE   C 1 28  ? -12.888 -21.632 29.099  1.00 60.73  ? 33  PHE   C C   1 
ATOM   4977 O  O   . PHE   C 1 28  ? -12.737 -20.931 28.098  1.00 59.87  ? 33  PHE   C O   1 
ATOM   4978 C  CB  . PHE   C 1 28  ? -10.971 -23.202 29.163  1.00 61.85  ? 33  PHE   C CB  1 
ATOM   4979 C  CG  . PHE   C 1 28  ? -10.344 -24.393 29.847  1.00 64.55  ? 33  PHE   C CG  1 
ATOM   4980 C  CD1 . PHE   C 1 28  ? -10.332 -25.642 29.235  1.00 68.42  ? 33  PHE   C CD1 1 
ATOM   4981 C  CD2 . PHE   C 1 28  ? -9.646  -24.239 31.040  1.00 67.57  ? 33  PHE   C CD2 1 
ATOM   4982 C  CE1 . PHE   C 1 28  ? -9.693  -26.730 29.840  1.00 69.67  ? 33  PHE   C CE1 1 
ATOM   4983 C  CE2 . PHE   C 1 28  ? -9.005  -25.327 31.642  1.00 70.93  ? 33  PHE   C CE2 1 
ATOM   4984 C  CZ  . PHE   C 1 28  ? -9.031  -26.565 31.035  1.00 69.15  ? 33  PHE   C CZ  1 
ATOM   4985 N  N   . SER   C 1 29  ? -13.339 -21.136 30.262  1.00 55.41  ? 34  SER   C N   1 
ATOM   4986 C  CA  . SER   C 1 29  ? -13.661 -19.714 30.425  1.00 54.22  ? 34  SER   C CA  1 
ATOM   4987 C  C   . SER   C 1 29  ? -13.342 -19.239 31.832  1.00 56.02  ? 34  SER   C C   1 
ATOM   4988 O  O   . SER   C 1 29  ? -13.139 -18.045 32.038  1.00 55.17  ? 34  SER   C O   1 
ATOM   4989 C  CB  . SER   C 1 29  ? -15.115 -19.418 30.064  1.00 58.49  ? 34  SER   C CB  1 
ATOM   4990 O  OG  . SER   C 1 29  ? -16.008 -19.808 31.094  1.00 70.27  ? 34  SER   C OG  1 
ATOM   4991 N  N   . GLN   C 1 30  ? -13.263 -20.184 32.791  1.00 51.36  ? 35  GLN   C N   1 
ATOM   4992 C  CA  . GLN   C 1 30  ? -13.026 -19.914 34.213  1.00 50.13  ? 35  GLN   C CA  1 
ATOM   4993 C  C   . GLN   C 1 30  ? -11.598 -19.468 34.559  1.00 50.48  ? 35  GLN   C C   1 
ATOM   4994 O  O   . GLN   C 1 30  ? -11.340 -19.133 35.715  1.00 49.67  ? 35  GLN   C O   1 
ATOM   4995 C  CB  . GLN   C 1 30  ? -13.452 -21.114 35.081  1.00 51.57  ? 35  GLN   C CB  1 
ATOM   4996 C  CG  . GLN   C 1 30  ? -14.952 -21.132 35.387  1.00 73.50  ? 35  GLN   C CG  1 
ATOM   4997 C  CD  . GLN   C 1 30  ? -15.776 -21.968 34.432  1.00 99.72  ? 35  GLN   C CD  1 
ATOM   4998 O  OE1 . GLN   C 1 30  ? -15.486 -22.091 33.230  1.00 96.82  ? 35  GLN   C OE1 1 
ATOM   4999 N  NE2 . GLN   C 1 30  ? -16.856 -22.540 34.948  1.00 92.26  ? 35  GLN   C NE2 1 
ATOM   5000 N  N   . GLY   C 1 31  ? -10.698 -19.431 33.573  1.00 44.63  ? 36  GLY   C N   1 
ATOM   5001 C  CA  . GLY   C 1 31  ? -9.329  -18.964 33.783  1.00 43.17  ? 36  GLY   C CA  1 
ATOM   5002 C  C   . GLY   C 1 31  ? -9.239  -17.445 33.784  1.00 44.85  ? 36  GLY   C C   1 
ATOM   5003 O  O   . GLY   C 1 31  ? -8.186  -16.885 34.091  1.00 42.69  ? 36  GLY   C O   1 
ATOM   5004 N  N   . GLN   C 1 32  ? -10.345 -16.775 33.397  1.00 41.54  ? 37  GLN   C N   1 
ATOM   5005 C  CA  . GLN   C 1 32  ? -10.504 -15.313 33.340  1.00 42.11  ? 37  GLN   C CA  1 
ATOM   5006 C  C   . GLN   C 1 32  ? -11.963 -14.877 33.608  1.00 49.39  ? 37  GLN   C C   1 
ATOM   5007 O  O   . GLN   C 1 32  ? -12.834 -15.736 33.781  1.00 49.13  ? 37  GLN   C O   1 
ATOM   5008 C  CB  . GLN   C 1 32  ? -9.941  -14.724 32.029  1.00 42.25  ? 37  GLN   C CB  1 
ATOM   5009 C  CG  . GLN   C 1 32  ? -10.316 -15.482 30.771  1.00 40.24  ? 37  GLN   C CG  1 
ATOM   5010 C  CD  . GLN   C 1 32  ? -11.627 -15.025 30.225  1.00 53.45  ? 37  GLN   C CD  1 
ATOM   5011 O  OE1 . GLN   C 1 32  ? -11.760 -13.912 29.706  1.00 47.82  ? 37  GLN   C OE1 1 
ATOM   5012 N  NE2 . GLN   C 1 32  ? -12.633 -15.869 30.361  1.00 53.62  ? 37  GLN   C NE2 1 
ATOM   5013 N  N   . LYS   C 1 33  ? -12.232 -13.555 33.661  1.00 48.23  ? 38  LYS   C N   1 
ATOM   5014 C  CA  . LYS   C 1 33  ? -13.573 -13.044 33.997  1.00 49.28  ? 38  LYS   C CA  1 
ATOM   5015 C  C   . LYS   C 1 33  ? -14.489 -12.714 32.810  1.00 56.29  ? 38  LYS   C C   1 
ATOM   5016 O  O   . LYS   C 1 33  ? -15.705 -12.609 33.009  1.00 56.23  ? 38  LYS   C O   1 
ATOM   5017 C  CB  . LYS   C 1 33  ? -13.473 -11.825 34.931  1.00 51.36  ? 38  LYS   C CB  1 
ATOM   5018 C  CG  . LYS   C 1 33  ? -12.919 -12.174 36.311  1.00 63.57  ? 38  LYS   C CG  1 
ATOM   5019 C  CD  . LYS   C 1 33  ? -12.924 -10.983 37.252  1.00 69.78  ? 38  LYS   C CD  1 
ATOM   5020 C  CE  . LYS   C 1 33  ? -12.240 -11.297 38.561  1.00 72.69  ? 38  LYS   C CE  1 
ATOM   5021 N  NZ  . LYS   C 1 33  ? -10.759 -11.238 38.444  1.00 78.67  ? 38  LYS   C NZ  1 
ATOM   5022 N  N   . ARG   C 1 34  ? -13.933 -12.528 31.596  1.00 54.89  ? 39  ARG   C N   1 
ATOM   5023 C  CA  . ARG   C 1 34  ? -14.744 -12.189 30.425  1.00 55.39  ? 39  ARG   C CA  1 
ATOM   5024 C  C   . ARG   C 1 34  ? -15.395 -13.422 29.803  1.00 60.58  ? 39  ARG   C C   1 
ATOM   5025 O  O   . ARG   C 1 34  ? -14.710 -14.375 29.445  1.00 61.20  ? 39  ARG   C O   1 
ATOM   5026 C  CB  . ARG   C 1 34  ? -13.954 -11.361 29.392  1.00 56.75  ? 39  ARG   C CB  1 
ATOM   5027 C  CG  . ARG   C 1 34  ? -13.549 -9.977  29.896  1.00 69.50  ? 39  ARG   C CG  1 
ATOM   5028 C  CD  . ARG   C 1 34  ? -13.845 -8.891  28.880  1.00 84.83  ? 39  ARG   C CD  1 
ATOM   5029 N  NE  . ARG   C 1 34  ? -12.635 -8.166  28.479  1.00 95.44  ? 39  ARG   C NE  1 
ATOM   5030 C  CZ  . ARG   C 1 34  ? -12.625 -7.106  27.675  1.00 110.68 ? 39  ARG   C CZ  1 
ATOM   5031 N  NH1 . ARG   C 1 34  ? -13.760 -6.626  27.180  1.00 97.20  ? 39  ARG   C NH1 1 
ATOM   5032 N  NH2 . ARG   C 1 34  ? -11.479 -6.515  27.363  1.00 99.21  ? 39  ARG   C NH2 1 
ATOM   5033 N  N   . LYS   C 1 35  ? -16.723 -13.412 29.702  1.00 56.99  ? 40  LYS   C N   1 
ATOM   5034 C  CA  . LYS   C 1 35  ? -17.491 -14.524 29.137  1.00 56.00  ? 40  LYS   C CA  1 
ATOM   5035 C  C   . LYS   C 1 35  ? -17.541 -14.465 27.613  1.00 56.62  ? 40  LYS   C C   1 
ATOM   5036 O  O   . LYS   C 1 35  ? -17.517 -13.371 27.034  1.00 55.68  ? 40  LYS   C O   1 
ATOM   5037 C  CB  . LYS   C 1 35  ? -18.911 -14.588 29.743  1.00 59.18  ? 40  LYS   C CB  1 
ATOM   5038 C  CG  . LYS   C 1 35  ? -19.712 -13.281 29.673  1.00 78.02  ? 40  LYS   C CG  1 
ATOM   5039 C  CD  . LYS   C 1 35  ? -20.908 -13.277 30.632  1.00 90.99  ? 40  LYS   C CD  1 
ATOM   5040 C  CE  . LYS   C 1 35  ? -20.583 -12.691 31.989  1.00 102.31 ? 40  LYS   C CE  1 
ATOM   5041 N  NZ  . LYS   C 1 35  ? -21.785 -12.621 32.860  1.00 110.66 ? 40  LYS   C NZ  1 
ATOM   5042 N  N   . GLY   C 1 36  ? -17.626 -15.642 26.989  1.00 50.88  ? 41  GLY   C N   1 
ATOM   5043 C  CA  . GLY   C 1 36  ? -17.725 -15.776 25.539  1.00 49.87  ? 41  GLY   C CA  1 
ATOM   5044 C  C   . GLY   C 1 36  ? -16.640 -16.608 24.887  1.00 51.02  ? 41  GLY   C C   1 
ATOM   5045 O  O   . GLY   C 1 36  ? -16.858 -17.150 23.799  1.00 50.40  ? 41  GLY   C O   1 
ATOM   5046 N  N   . VAL   C 1 37  ? -15.465 -16.705 25.552  1.00 45.91  ? 42  VAL   C N   1 
ATOM   5047 C  CA  . VAL   C 1 37  ? -14.267 -17.423 25.097  1.00 45.67  ? 42  VAL   C CA  1 
ATOM   5048 C  C   . VAL   C 1 37  ? -14.526 -18.956 24.984  1.00 50.35  ? 42  VAL   C C   1 
ATOM   5049 O  O   . VAL   C 1 37  ? -13.783 -19.653 24.291  1.00 49.25  ? 42  VAL   C O   1 
ATOM   5050 C  CB  . VAL   C 1 37  ? -13.018 -17.048 25.950  1.00 48.67  ? 42  VAL   C CB  1 
ATOM   5051 C  CG1 . VAL   C 1 37  ? -13.072 -17.635 27.360  1.00 48.43  ? 42  VAL   C CG1 1 
ATOM   5052 C  CG2 . VAL   C 1 37  ? -11.710 -17.408 25.248  1.00 48.05  ? 42  VAL   C CG2 1 
ATOM   5053 N  N   . GLU   C 1 38  ? -15.611 -19.454 25.627  1.00 47.52  ? 43  GLU   C N   1 
ATOM   5054 C  CA  . GLU   C 1 38  ? -16.026 -20.858 25.571  1.00 47.37  ? 43  GLU   C CA  1 
ATOM   5055 C  C   . GLU   C 1 38  ? -16.602 -21.197 24.188  1.00 52.30  ? 43  GLU   C C   1 
ATOM   5056 O  O   . GLU   C 1 38  ? -16.673 -22.371 23.833  1.00 52.94  ? 43  GLU   C O   1 
ATOM   5057 C  CB  . GLU   C 1 38  ? -17.037 -21.199 26.708  1.00 48.43  ? 43  GLU   C CB  1 
ATOM   5058 C  CG  . GLU   C 1 38  ? -18.406 -20.540 26.588  1.00 54.31  ? 43  GLU   C CG  1 
ATOM   5059 C  CD  . GLU   C 1 38  ? -18.562 -19.137 27.152  1.00 72.96  ? 43  GLU   C CD  1 
ATOM   5060 O  OE1 . GLU   C 1 38  ? -17.534 -18.479 27.437  1.00 54.65  ? 43  GLU   C OE1 1 
ATOM   5061 O  OE2 . GLU   C 1 38  ? -19.725 -18.695 27.310  1.00 64.17  ? 43  GLU   C OE2 1 
ATOM   5062 N  N   . HIS   C 1 39  ? -17.025 -20.174 23.424  1.00 49.27  ? 44  HIS   C N   1 
ATOM   5063 C  CA  . HIS   C 1 39  ? -17.589 -20.325 22.078  1.00 50.04  ? 44  HIS   C CA  1 
ATOM   5064 C  C   . HIS   C 1 39  ? -16.498 -20.245 20.989  1.00 51.95  ? 44  HIS   C C   1 
ATOM   5065 O  O   . HIS   C 1 39  ? -16.803 -20.298 19.793  1.00 49.86  ? 44  HIS   C O   1 
ATOM   5066 C  CB  . HIS   C 1 39  ? -18.719 -19.307 21.846  1.00 52.05  ? 44  HIS   C CB  1 
ATOM   5067 C  CG  . HIS   C 1 39  ? -19.807 -19.396 22.873  1.00 56.65  ? 44  HIS   C CG  1 
ATOM   5068 N  ND1 . HIS   C 1 39  ? -20.616 -20.521 22.976  1.00 58.87  ? 44  HIS   C ND1 1 
ATOM   5069 C  CD2 . HIS   C 1 39  ? -20.166 -18.510 23.832  1.00 59.13  ? 44  HIS   C CD2 1 
ATOM   5070 C  CE1 . HIS   C 1 39  ? -21.442 -20.277 23.982  1.00 58.67  ? 44  HIS   C CE1 1 
ATOM   5071 N  NE2 . HIS   C 1 39  ? -21.211 -19.080 24.527  1.00 59.09  ? 44  HIS   C NE2 1 
ATOM   5072 N  N   . GLY   C 1 40  ? -15.247 -20.140 21.439  1.00 48.52  ? 45  GLY   C N   1 
ATOM   5073 C  CA  . GLY   C 1 40  ? -14.050 -20.099 20.605  1.00 48.58  ? 45  GLY   C CA  1 
ATOM   5074 C  C   . GLY   C 1 40  ? -13.835 -21.368 19.793  1.00 51.38  ? 45  GLY   C C   1 
ATOM   5075 O  O   . GLY   C 1 40  ? -13.678 -21.260 18.575  1.00 49.91  ? 45  GLY   C O   1 
ATOM   5076 N  N   . PRO   C 1 41  ? -13.896 -22.599 20.396  1.00 47.89  ? 46  PRO   C N   1 
ATOM   5077 C  CA  . PRO   C 1 41  ? -13.704 -23.826 19.591  1.00 47.30  ? 46  PRO   C CA  1 
ATOM   5078 C  C   . PRO   C 1 41  ? -14.707 -23.996 18.459  1.00 50.26  ? 46  PRO   C C   1 
ATOM   5079 O  O   . PRO   C 1 41  ? -14.313 -24.418 17.376  1.00 48.42  ? 46  PRO   C O   1 
ATOM   5080 C  CB  . PRO   C 1 41  ? -13.808 -24.952 20.629  1.00 49.03  ? 46  PRO   C CB  1 
ATOM   5081 C  CG  . PRO   C 1 41  ? -13.441 -24.309 21.909  1.00 53.28  ? 46  PRO   C CG  1 
ATOM   5082 C  CD  . PRO   C 1 41  ? -14.070 -22.949 21.821  1.00 48.92  ? 46  PRO   C CD  1 
ATOM   5083 N  N   . ALA   C 1 42  ? -15.982 -23.628 18.693  1.00 47.81  ? 47  ALA   C N   1 
ATOM   5084 C  CA  . ALA   C 1 42  ? -17.043 -23.706 17.692  1.00 48.12  ? 47  ALA   C CA  1 
ATOM   5085 C  C   . ALA   C 1 42  ? -16.835 -22.660 16.602  1.00 51.08  ? 47  ALA   C C   1 
ATOM   5086 O  O   . ALA   C 1 42  ? -17.064 -22.968 15.431  1.00 50.86  ? 47  ALA   C O   1 
ATOM   5087 C  CB  . ALA   C 1 42  ? -18.404 -23.511 18.347  1.00 49.02  ? 47  ALA   C CB  1 
ATOM   5088 N  N   . ALA   C 1 43  ? -16.412 -21.417 16.985  1.00 46.88  ? 48  ALA   C N   1 
ATOM   5089 C  CA  . ALA   C 1 43  ? -16.159 -20.309 16.042  1.00 45.66  ? 48  ALA   C CA  1 
ATOM   5090 C  C   . ALA   C 1 43  ? -15.069 -20.692 15.044  1.00 46.06  ? 48  ALA   C C   1 
ATOM   5091 O  O   . ALA   C 1 43  ? -15.176 -20.361 13.863  1.00 46.55  ? 48  ALA   C O   1 
ATOM   5092 C  CB  . ALA   C 1 43  ? -15.762 -19.043 16.792  1.00 46.36  ? 48  ALA   C CB  1 
ATOM   5093 N  N   . ILE   C 1 44  ? -14.054 -21.425 15.519  1.00 40.97  ? 49  ILE   C N   1 
ATOM   5094 C  CA  . ILE   C 1 44  ? -12.930 -21.906 14.717  1.00 40.94  ? 49  ILE   C CA  1 
ATOM   5095 C  C   . ILE   C 1 44  ? -13.419 -23.009 13.750  1.00 46.29  ? 49  ILE   C C   1 
ATOM   5096 O  O   . ILE   C 1 44  ? -13.037 -22.998 12.574  1.00 45.75  ? 49  ILE   C O   1 
ATOM   5097 C  CB  . ILE   C 1 44  ? -11.728 -22.309 15.612  1.00 43.10  ? 49  ILE   C CB  1 
ATOM   5098 C  CG1 . ILE   C 1 44  ? -11.202 -21.067 16.385  1.00 42.47  ? 49  ILE   C CG1 1 
ATOM   5099 C  CG2 . ILE   C 1 44  ? -10.600 -22.982 14.793  1.00 44.27  ? 49  ILE   C CG2 1 
ATOM   5100 C  CD1 . ILE   C 1 44  ? -10.328 -21.328 17.572  1.00 36.81  ? 49  ILE   C CD1 1 
ATOM   5101 N  N   . ARG   C 1 45  ? -14.326 -23.901 14.228  1.00 42.74  ? 50  ARG   C N   1 
ATOM   5102 C  CA  . ARG   C 1 45  ? -14.927 -24.963 13.409  1.00 41.93  ? 50  ARG   C CA  1 
ATOM   5103 C  C   . ARG   C 1 45  ? -15.819 -24.378 12.321  1.00 46.64  ? 50  ARG   C C   1 
ATOM   5104 O  O   . ARG   C 1 45  ? -15.701 -24.785 11.162  1.00 45.89  ? 50  ARG   C O   1 
ATOM   5105 C  CB  . ARG   C 1 45  ? -15.702 -25.966 14.280  1.00 40.65  ? 50  ARG   C CB  1 
ATOM   5106 C  CG  . ARG   C 1 45  ? -14.810 -27.038 14.870  1.00 44.06  ? 50  ARG   C CG  1 
ATOM   5107 C  CD  . ARG   C 1 45  ? -15.634 -28.247 15.289  1.00 47.57  ? 50  ARG   C CD  1 
ATOM   5108 N  NE  . ARG   C 1 45  ? -14.886 -29.123 16.189  1.00 49.39  ? 50  ARG   C NE  1 
ATOM   5109 C  CZ  . ARG   C 1 45  ? -14.712 -28.885 17.483  1.00 59.15  ? 50  ARG   C CZ  1 
ATOM   5110 N  NH1 . ARG   C 1 45  ? -15.232 -27.799 18.040  1.00 46.48  ? 50  ARG   C NH1 1 
ATOM   5111 N  NH2 . ARG   C 1 45  ? -14.004 -29.723 18.228  1.00 52.45  ? 50  ARG   C NH2 1 
ATOM   5112 N  N   . GLU   C 1 46  ? -16.660 -23.384 12.676  1.00 44.40  ? 51  GLU   C N   1 
ATOM   5113 C  CA  . GLU   C 1 46  ? -17.557 -22.694 11.746  1.00 45.85  ? 51  GLU   C CA  1 
ATOM   5114 C  C   . GLU   C 1 46  ? -16.794 -21.932 10.671  1.00 51.06  ? 51  GLU   C C   1 
ATOM   5115 O  O   . GLU   C 1 46  ? -17.336 -21.702 9.590   1.00 51.25  ? 51  GLU   C O   1 
ATOM   5116 C  CB  . GLU   C 1 46  ? -18.532 -21.767 12.484  1.00 47.82  ? 51  GLU   C CB  1 
ATOM   5117 C  CG  . GLU   C 1 46  ? -19.829 -22.456 12.875  1.00 63.42  ? 51  GLU   C CG  1 
ATOM   5118 C  CD  . GLU   C 1 46  ? -20.130 -22.458 14.360  1.00 86.57  ? 51  GLU   C CD  1 
ATOM   5119 O  OE1 . GLU   C 1 46  ? -20.373 -21.364 14.921  1.00 84.62  ? 51  GLU   C OE1 1 
ATOM   5120 O  OE2 . GLU   C 1 46  ? -20.153 -23.558 14.959  1.00 78.37  ? 51  GLU   C OE2 1 
ATOM   5121 N  N   . ALA   C 1 47  ? -15.522 -21.566 10.965  1.00 48.25  ? 52  ALA   C N   1 
ATOM   5122 C  CA  . ALA   C 1 47  ? -14.620 -20.885 10.041  1.00 47.83  ? 52  ALA   C CA  1 
ATOM   5123 C  C   . ALA   C 1 47  ? -13.975 -21.885 9.051   1.00 51.21  ? 52  ALA   C C   1 
ATOM   5124 O  O   . ALA   C 1 47  ? -13.095 -21.507 8.275   1.00 50.99  ? 52  ALA   C O   1 
ATOM   5125 C  CB  . ALA   C 1 47  ? -13.555 -20.120 10.819  1.00 48.24  ? 52  ALA   C CB  1 
ATOM   5126 N  N   . GLY   C 1 48  ? -14.438 -23.143 9.092   1.00 47.00  ? 53  GLY   C N   1 
ATOM   5127 C  CA  . GLY   C 1 48  ? -14.034 -24.227 8.200   1.00 45.60  ? 53  GLY   C CA  1 
ATOM   5128 C  C   . GLY   C 1 48  ? -12.705 -24.900 8.459   1.00 45.32  ? 53  GLY   C C   1 
ATOM   5129 O  O   . GLY   C 1 48  ? -12.039 -25.300 7.499   1.00 45.59  ? 53  GLY   C O   1 
ATOM   5130 N  N   . LEU   C 1 49  ? -12.328 -25.078 9.750   1.00 38.89  ? 54  LEU   C N   1 
ATOM   5131 C  CA  . LEU   C 1 49  ? -11.078 -25.715 10.183  1.00 37.64  ? 54  LEU   C CA  1 
ATOM   5132 C  C   . LEU   C 1 49  ? -10.882 -27.135 9.638   1.00 44.33  ? 54  LEU   C C   1 
ATOM   5133 O  O   . LEU   C 1 49  ? -9.767  -27.493 9.224   1.00 43.30  ? 54  LEU   C O   1 
ATOM   5134 C  CB  . LEU   C 1 49  ? -10.950 -25.725 11.735  1.00 36.90  ? 54  LEU   C CB  1 
ATOM   5135 C  CG  . LEU   C 1 49  ? -9.717  -26.449 12.328  1.00 41.19  ? 54  LEU   C CG  1 
ATOM   5136 C  CD1 . LEU   C 1 49  ? -8.401  -25.729 11.976  1.00 42.17  ? 54  LEU   C CD1 1 
ATOM   5137 C  CD2 . LEU   C 1 49  ? -9.839  -26.651 13.829  1.00 42.36  ? 54  LEU   C CD2 1 
ATOM   5138 N  N   . MET   C 1 50  ? -11.942 -27.969 9.729   1.00 42.39  ? 55  MET   C N   1 
ATOM   5139 C  CA  . MET   C 1 50  ? -11.892 -29.368 9.300   1.00 41.52  ? 55  MET   C CA  1 
ATOM   5140 C  C   . MET   C 1 50  ? -11.715 -29.482 7.791   1.00 42.84  ? 55  MET   C C   1 
ATOM   5141 O  O   . MET   C 1 50  ? -10.781 -30.150 7.362   1.00 43.00  ? 55  MET   C O   1 
ATOM   5142 C  CB  . MET   C 1 50  ? -13.098 -30.171 9.839   1.00 43.56  ? 55  MET   C CB  1 
ATOM   5143 C  CG  . MET   C 1 50  ? -13.166 -30.224 11.378  1.00 46.54  ? 55  MET   C CG  1 
ATOM   5144 S  SD  . MET   C 1 50  ? -11.576 -30.463 12.237  1.00 49.55  ? 55  MET   C SD  1 
ATOM   5145 C  CE  . MET   C 1 50  ? -11.477 -32.248 12.275  1.00 46.48  ? 55  MET   C CE  1 
ATOM   5146 N  N   . LYS   C 1 51  ? -12.538 -28.762 6.997   1.00 41.24  ? 56  LYS   C N   1 
ATOM   5147 C  CA  . LYS   C 1 51  ? -12.440 -28.694 5.525   1.00 42.20  ? 56  LYS   C CA  1 
ATOM   5148 C  C   . LYS   C 1 51  ? -11.005 -28.291 5.122   1.00 46.38  ? 56  LYS   C C   1 
ATOM   5149 O  O   . LYS   C 1 51  ? -10.435 -28.886 4.205   1.00 46.41  ? 56  LYS   C O   1 
ATOM   5150 C  CB  . LYS   C 1 51  ? -13.460 -27.673 4.976   1.00 45.15  ? 56  LYS   C CB  1 
ATOM   5151 C  CG  . LYS   C 1 51  ? -13.623 -27.663 3.458   1.00 62.32  ? 56  LYS   C CG  1 
ATOM   5152 C  CD  . LYS   C 1 51  ? -14.774 -26.744 3.034   1.00 73.98  ? 56  LYS   C CD  1 
ATOM   5153 C  CE  . LYS   C 1 51  ? -14.925 -26.621 1.533   1.00 88.04  ? 56  LYS   C CE  1 
ATOM   5154 N  NZ  . LYS   C 1 51  ? -15.561 -27.823 0.925   1.00 98.24  ? 56  LYS   C NZ  1 
ATOM   5155 N  N   . ARG   C 1 52  ? -10.399 -27.339 5.875   1.00 41.78  ? 57  ARG   C N   1 
ATOM   5156 C  CA  . ARG   C 1 52  ? -9.042  -26.866 5.614   1.00 41.17  ? 57  ARG   C CA  1 
ATOM   5157 C  C   . ARG   C 1 52  ? -7.956  -27.908 5.904   1.00 41.82  ? 57  ARG   C C   1 
ATOM   5158 O  O   . ARG   C 1 52  ? -7.070  -28.102 5.067   1.00 41.24  ? 57  ARG   C O   1 
ATOM   5159 C  CB  . ARG   C 1 52  ? -8.764  -25.549 6.365   1.00 41.66  ? 57  ARG   C CB  1 
ATOM   5160 C  CG  . ARG   C 1 52  ? -7.424  -24.926 5.985   1.00 50.29  ? 57  ARG   C CG  1 
ATOM   5161 C  CD  . ARG   C 1 52  ? -7.482  -24.144 4.686   1.00 52.61  ? 57  ARG   C CD  1 
ATOM   5162 N  NE  . ARG   C 1 52  ? -8.392  -23.009 4.806   1.00 52.23  ? 57  ARG   C NE  1 
ATOM   5163 C  CZ  . ARG   C 1 52  ? -8.085  -21.854 5.388   1.00 56.14  ? 57  ARG   C CZ  1 
ATOM   5164 N  NH1 . ARG   C 1 52  ? -8.991  -20.897 5.485   1.00 45.23  ? 57  ARG   C NH1 1 
ATOM   5165 N  NH2 . ARG   C 1 52  ? -6.869  -21.653 5.884   1.00 42.86  ? 57  ARG   C NH2 1 
ATOM   5166 N  N   . LEU   C 1 53  ? -7.995  -28.555 7.081   1.00 36.46  ? 58  LEU   C N   1 
ATOM   5167 C  CA  . LEU   C 1 53  ? -6.985  -29.553 7.427   1.00 36.94  ? 58  LEU   C CA  1 
ATOM   5168 C  C   . LEU   C 1 53  ? -7.085  -30.801 6.533   1.00 41.83  ? 58  LEU   C C   1 
ATOM   5169 O  O   . LEU   C 1 53  ? -6.062  -31.412 6.252   1.00 40.41  ? 58  LEU   C O   1 
ATOM   5170 C  CB  . LEU   C 1 53  ? -7.021  -29.935 8.913   1.00 37.41  ? 58  LEU   C CB  1 
ATOM   5171 C  CG  . LEU   C 1 53  ? -6.637  -28.836 9.928   1.00 41.36  ? 58  LEU   C CG  1 
ATOM   5172 C  CD1 . LEU   C 1 53  ? -6.963  -29.278 11.343  1.00 41.07  ? 58  LEU   C CD1 1 
ATOM   5173 C  CD2 . LEU   C 1 53  ? -5.143  -28.475 9.838   1.00 41.62  ? 58  LEU   C CD2 1 
ATOM   5174 N  N   . SER   C 1 54  ? -8.305  -31.133 6.050   1.00 41.57  ? 59  SER   C N   1 
ATOM   5175 C  CA  . SER   C 1 54  ? -8.547  -32.269 5.151   1.00 43.58  ? 59  SER   C CA  1 
ATOM   5176 C  C   . SER   C 1 54  ? -7.889  -32.022 3.788   1.00 49.42  ? 59  SER   C C   1 
ATOM   5177 O  O   . SER   C 1 54  ? -7.195  -32.905 3.271   1.00 48.97  ? 59  SER   C O   1 
ATOM   5178 C  CB  . SER   C 1 54  ? -10.043 -32.508 4.979   1.00 49.26  ? 59  SER   C CB  1 
ATOM   5179 O  OG  . SER   C 1 54  ? -10.618 -32.949 6.198   1.00 63.36  ? 59  SER   C OG  1 
ATOM   5180 N  N   . SER   C 1 55  ? -8.051  -30.790 3.257   1.00 46.55  ? 60  SER   C N   1 
ATOM   5181 C  CA  . SER   C 1 55  ? -7.484  -30.333 1.987   1.00 46.45  ? 60  SER   C CA  1 
ATOM   5182 C  C   . SER   C 1 55  ? -5.947  -30.417 1.988   1.00 47.49  ? 60  SER   C C   1 
ATOM   5183 O  O   . SER   C 1 55  ? -5.336  -30.468 0.923   1.00 46.02  ? 60  SER   C O   1 
ATOM   5184 C  CB  . SER   C 1 55  ? -7.963  -28.920 1.664   1.00 50.97  ? 60  SER   C CB  1 
ATOM   5185 O  OG  . SER   C 1 55  ? -7.208  -27.934 2.351   1.00 65.50  ? 60  SER   C OG  1 
ATOM   5186 N  N   . LEU   C 1 56  ? -5.342  -30.464 3.185   1.00 44.00  ? 61  LEU   C N   1 
ATOM   5187 C  CA  . LEU   C 1 56  ? -3.897  -30.557 3.415   1.00 44.26  ? 61  LEU   C CA  1 
ATOM   5188 C  C   . LEU   C 1 56  ? -3.421  -32.016 3.506   1.00 51.42  ? 61  LEU   C C   1 
ATOM   5189 O  O   . LEU   C 1 56  ? -2.230  -32.276 3.717   1.00 51.21  ? 61  LEU   C O   1 
ATOM   5190 C  CB  . LEU   C 1 56  ? -3.543  -29.784 4.703   1.00 43.99  ? 61  LEU   C CB  1 
ATOM   5191 C  CG  . LEU   C 1 56  ? -2.937  -28.362 4.614   1.00 48.30  ? 61  LEU   C CG  1 
ATOM   5192 C  CD1 . LEU   C 1 56  ? -3.405  -27.568 3.395   1.00 47.35  ? 61  LEU   C CD1 1 
ATOM   5193 C  CD2 . LEU   C 1 56  ? -3.205  -27.591 5.900   1.00 50.29  ? 61  LEU   C CD2 1 
ATOM   5194 N  N   . GLY   C 1 57  ? -4.358  -32.949 3.338   1.00 49.37  ? 62  GLY   C N   1 
ATOM   5195 C  CA  . GLY   C 1 57  ? -4.084  -34.377 3.379   1.00 49.37  ? 62  GLY   C CA  1 
ATOM   5196 C  C   . GLY   C 1 57  ? -3.937  -34.961 4.768   1.00 52.73  ? 62  GLY   C C   1 
ATOM   5197 O  O   . GLY   C 1 57  ? -3.409  -36.067 4.906   1.00 53.47  ? 62  GLY   C O   1 
ATOM   5198 N  N   . CYS   C 1 58  ? -4.396  -34.227 5.812   1.00 46.72  ? 63  CYS   C N   1 
ATOM   5199 C  CA  . CYS   C 1 58  ? -4.333  -34.694 7.197   1.00 45.18  ? 63  CYS   C CA  1 
ATOM   5200 C  C   . CYS   C 1 58  ? -5.334  -35.822 7.430   1.00 46.28  ? 63  CYS   C C   1 
ATOM   5201 O  O   . CYS   C 1 58  ? -6.429  -35.803 6.860   1.00 45.18  ? 63  CYS   C O   1 
ATOM   5202 C  CB  . CYS   C 1 58  ? -4.589  -33.550 8.178   1.00 45.15  ? 63  CYS   C CB  1 
ATOM   5203 S  SG  . CYS   C 1 58  ? -3.407  -32.179 8.061   1.00 48.66  ? 63  CYS   C SG  1 
ATOM   5204 N  N   . HIS   C 1 59  ? -4.984  -36.758 8.313   1.00 42.88  ? 64  HIS   C N   1 
ATOM   5205 C  CA  . HIS   C 1 59  ? -5.903  -37.818 8.747   1.00 43.17  ? 64  HIS   C CA  1 
ATOM   5206 C  C   . HIS   C 1 59  ? -6.528  -37.249 10.030  1.00 44.52  ? 64  HIS   C C   1 
ATOM   5207 O  O   . HIS   C 1 59  ? -5.825  -37.086 11.025  1.00 42.57  ? 64  HIS   C O   1 
ATOM   5208 C  CB  . HIS   C 1 59  ? -5.160  -39.140 9.018   1.00 44.70  ? 64  HIS   C CB  1 
ATOM   5209 C  CG  . HIS   C 1 59  ? -6.048  -40.201 9.601   1.00 48.67  ? 64  HIS   C CG  1 
ATOM   5210 N  ND1 . HIS   C 1 59  ? -7.071  -40.779 8.860   1.00 50.73  ? 64  HIS   C ND1 1 
ATOM   5211 C  CD2 . HIS   C 1 59  ? -6.063  -40.726 10.848  1.00 50.56  ? 64  HIS   C CD2 1 
ATOM   5212 C  CE1 . HIS   C 1 59  ? -7.658  -41.641 9.674   1.00 49.82  ? 64  HIS   C CE1 1 
ATOM   5213 N  NE2 . HIS   C 1 59  ? -7.083  -41.647 10.877  1.00 50.20  ? 64  HIS   C NE2 1 
ATOM   5214 N  N   . LEU   C 1 60  ? -7.823  -36.882 9.976   1.00 41.79  ? 65  LEU   C N   1 
ATOM   5215 C  CA  . LEU   C 1 60  ? -8.497  -36.189 11.073  1.00 42.13  ? 65  LEU   C CA  1 
ATOM   5216 C  C   . LEU   C 1 60  ? -9.337  -37.004 12.039  1.00 43.75  ? 65  LEU   C C   1 
ATOM   5217 O  O   . LEU   C 1 60  ? -10.137 -37.851 11.629  1.00 42.39  ? 65  LEU   C O   1 
ATOM   5218 C  CB  . LEU   C 1 60  ? -9.419  -35.078 10.513  1.00 42.97  ? 65  LEU   C CB  1 
ATOM   5219 C  CG  . LEU   C 1 60  ? -8.836  -33.738 10.002  1.00 48.63  ? 65  LEU   C CG  1 
ATOM   5220 C  CD1 . LEU   C 1 60  ? -7.771  -33.161 10.930  1.00 49.01  ? 65  LEU   C CD1 1 
ATOM   5221 C  CD2 . LEU   C 1 60  ? -8.392  -33.825 8.575   1.00 52.87  ? 65  LEU   C CD2 1 
ATOM   5222 N  N   . LYS   C 1 61  ? -9.269  -36.603 13.321  1.00 37.41  ? 66  LYS   C N   1 
ATOM   5223 C  CA  . LYS   C 1 61  ? -10.149 -37.079 14.373  1.00 36.86  ? 66  LYS   C CA  1 
ATOM   5224 C  C   . LYS   C 1 61  ? -10.630 -35.854 15.126  1.00 41.36  ? 66  LYS   C C   1 
ATOM   5225 O  O   . LYS   C 1 61  ? -9.809  -35.107 15.652  1.00 44.05  ? 66  LYS   C O   1 
ATOM   5226 C  CB  . LYS   C 1 61  ? -9.484  -38.055 15.343  1.00 37.78  ? 66  LYS   C CB  1 
ATOM   5227 C  CG  . LYS   C 1 61  ? -10.509 -38.659 16.322  1.00 42.41  ? 66  LYS   C CG  1 
ATOM   5228 C  CD  . LYS   C 1 61  ? -9.894  -39.682 17.260  1.00 49.25  ? 66  LYS   C CD  1 
ATOM   5229 C  CE  . LYS   C 1 61  ? -10.914 -40.573 17.932  1.00 63.20  ? 66  LYS   C CE  1 
ATOM   5230 N  NZ  . LYS   C 1 61  ? -11.741 -39.846 18.932  1.00 73.54  ? 66  LYS   C NZ  1 
ATOM   5231 N  N   . ASP   C 1 62  ? -11.939 -35.644 15.167  1.00 35.18  ? 67  ASP   C N   1 
ATOM   5232 C  CA  . ASP   C 1 62  ? -12.528 -34.551 15.929  1.00 34.92  ? 67  ASP   C CA  1 
ATOM   5233 C  C   . ASP   C 1 62  ? -13.178 -35.175 17.156  1.00 39.73  ? 67  ASP   C C   1 
ATOM   5234 O  O   . ASP   C 1 62  ? -14.048 -36.048 17.029  1.00 38.08  ? 67  ASP   C O   1 
ATOM   5235 C  CB  . ASP   C 1 62  ? -13.578 -33.786 15.106  1.00 35.94  ? 67  ASP   C CB  1 
ATOM   5236 C  CG  . ASP   C 1 62  ? -14.056 -32.473 15.725  1.00 43.13  ? 67  ASP   C CG  1 
ATOM   5237 O  OD1 . ASP   C 1 62  ? -13.672 -32.177 16.888  1.00 41.03  ? 67  ASP   C OD1 1 
ATOM   5238 O  OD2 . ASP   C 1 62  ? -14.787 -31.726 15.036  1.00 47.67  ? 67  ASP   C OD2 1 
ATOM   5239 N  N   . PHE   C 1 63  ? -12.742 -34.746 18.347  1.00 37.32  ? 68  PHE   C N   1 
ATOM   5240 C  CA  . PHE   C 1 63  ? -13.312 -35.247 19.604  1.00 37.49  ? 68  PHE   C CA  1 
ATOM   5241 C  C   . PHE   C 1 63  ? -14.569 -34.435 19.982  1.00 44.13  ? 68  PHE   C C   1 
ATOM   5242 O  O   . PHE   C 1 63  ? -15.242 -34.754 20.969  1.00 45.52  ? 68  PHE   C O   1 
ATOM   5243 C  CB  . PHE   C 1 63  ? -12.279 -35.146 20.734  1.00 38.15  ? 68  PHE   C CB  1 
ATOM   5244 C  CG  . PHE   C 1 63  ? -11.201 -36.196 20.726  1.00 39.37  ? 68  PHE   C CG  1 
ATOM   5245 C  CD1 . PHE   C 1 63  ? -10.098 -36.080 19.886  1.00 41.61  ? 68  PHE   C CD1 1 
ATOM   5246 C  CD2 . PHE   C 1 63  ? -11.280 -37.302 21.564  1.00 41.00  ? 68  PHE   C CD2 1 
ATOM   5247 C  CE1 . PHE   C 1 63  ? -9.091  -37.046 19.892  1.00 42.76  ? 68  PHE   C CE1 1 
ATOM   5248 C  CE2 . PHE   C 1 63  ? -10.275 -38.274 21.563  1.00 44.22  ? 68  PHE   C CE2 1 
ATOM   5249 C  CZ  . PHE   C 1 63  ? -9.190  -38.147 20.720  1.00 42.83  ? 68  PHE   C CZ  1 
ATOM   5250 N  N   . GLY   C 1 64  ? -14.871 -33.410 19.188  1.00 40.40  ? 69  GLY   C N   1 
ATOM   5251 C  CA  . GLY   C 1 64  ? -15.963 -32.479 19.441  1.00 41.01  ? 69  GLY   C CA  1 
ATOM   5252 C  C   . GLY   C 1 64  ? -15.568 -31.599 20.615  1.00 46.17  ? 69  GLY   C C   1 
ATOM   5253 O  O   . GLY   C 1 64  ? -14.377 -31.520 20.950  1.00 43.70  ? 69  GLY   C O   1 
ATOM   5254 N  N   . ASP   C 1 65  ? -16.557 -30.976 21.284  1.00 44.94  ? 70  ASP   C N   1 
ATOM   5255 C  CA  . ASP   C 1 65  ? -16.273 -30.135 22.450  1.00 46.35  ? 70  ASP   C CA  1 
ATOM   5256 C  C   . ASP   C 1 65  ? -16.407 -30.936 23.747  1.00 53.84  ? 70  ASP   C C   1 
ATOM   5257 O  O   . ASP   C 1 65  ? -17.463 -31.528 23.999  1.00 53.24  ? 70  ASP   C O   1 
ATOM   5258 C  CB  . ASP   C 1 65  ? -17.182 -28.887 22.478  1.00 48.34  ? 70  ASP   C CB  1 
ATOM   5259 C  CG  . ASP   C 1 65  ? -17.017 -27.956 21.292  1.00 58.56  ? 70  ASP   C CG  1 
ATOM   5260 O  OD1 . ASP   C 1 65  ? -15.931 -27.961 20.680  1.00 56.05  ? 70  ASP   C OD1 1 
ATOM   5261 O  OD2 . ASP   C 1 65  ? -17.977 -27.210 20.983  1.00 68.63  ? 70  ASP   C OD2 1 
ATOM   5262 N  N   . LEU   C 1 66  ? -15.328 -30.968 24.554  1.00 52.87  ? 71  LEU   C N   1 
ATOM   5263 C  CA  . LEU   C 1 66  ? -15.302 -31.652 25.848  1.00 54.26  ? 71  LEU   C CA  1 
ATOM   5264 C  C   . LEU   C 1 66  ? -16.261 -30.973 26.824  1.00 62.31  ? 71  LEU   C C   1 
ATOM   5265 O  O   . LEU   C 1 66  ? -16.353 -29.742 26.852  1.00 61.16  ? 71  LEU   C O   1 
ATOM   5266 C  CB  . LEU   C 1 66  ? -13.894 -31.649 26.474  1.00 53.86  ? 71  LEU   C CB  1 
ATOM   5267 C  CG  . LEU   C 1 66  ? -12.758 -32.411 25.792  1.00 58.39  ? 71  LEU   C CG  1 
ATOM   5268 C  CD1 . LEU   C 1 66  ? -11.518 -32.379 26.662  1.00 58.22  ? 71  LEU   C CD1 1 
ATOM   5269 C  CD2 . LEU   C 1 66  ? -13.129 -33.869 25.501  1.00 61.65  ? 71  LEU   C CD2 1 
ATOM   5270 N  N   . SER   C 1 67  ? -16.981 -31.781 27.614  1.00 62.31  ? 72  SER   C N   1 
ATOM   5271 C  CA  . SER   C 1 67  ? -17.903 -31.272 28.622  1.00 63.48  ? 72  SER   C CA  1 
ATOM   5272 C  C   . SER   C 1 67  ? -17.266 -31.530 29.983  1.00 69.97  ? 72  SER   C C   1 
ATOM   5273 O  O   . SER   C 1 67  ? -17.300 -32.659 30.484  1.00 69.24  ? 72  SER   C O   1 
ATOM   5274 C  CB  . SER   C 1 67  ? -19.276 -31.930 28.500  1.00 66.93  ? 72  SER   C CB  1 
ATOM   5275 O  OG  . SER   C 1 67  ? -20.244 -31.202 29.239  1.00 75.74  ? 72  SER   C OG  1 
ATOM   5276 N  N   . PHE   C 1 68  ? -16.603 -30.493 30.531  1.00 69.04  ? 73  PHE   C N   1 
ATOM   5277 C  CA  . PHE   C 1 68  ? -15.917 -30.552 31.822  1.00 70.07  ? 73  PHE   C CA  1 
ATOM   5278 C  C   . PHE   C 1 68  ? -16.925 -30.563 32.969  1.00 77.02  ? 73  PHE   C C   1 
ATOM   5279 O  O   . PHE   C 1 68  ? -17.996 -29.953 32.861  1.00 76.39  ? 73  PHE   C O   1 
ATOM   5280 C  CB  . PHE   C 1 68  ? -14.914 -29.388 31.981  1.00 71.87  ? 73  PHE   C CB  1 
ATOM   5281 C  CG  . PHE   C 1 68  ? -13.913 -29.253 30.855  1.00 73.32  ? 73  PHE   C CG  1 
ATOM   5282 C  CD1 . PHE   C 1 68  ? -12.854 -30.146 30.731  1.00 76.22  ? 73  PHE   C CD1 1 
ATOM   5283 C  CD2 . PHE   C 1 68  ? -14.037 -28.240 29.911  1.00 75.27  ? 73  PHE   C CD2 1 
ATOM   5284 C  CE1 . PHE   C 1 68  ? -11.938 -30.029 29.681  1.00 76.89  ? 73  PHE   C CE1 1 
ATOM   5285 C  CE2 . PHE   C 1 68  ? -13.116 -28.121 28.865  1.00 77.85  ? 73  PHE   C CE2 1 
ATOM   5286 C  CZ  . PHE   C 1 68  ? -12.077 -29.020 28.755  1.00 75.90  ? 73  PHE   C CZ  1 
ATOM   5287 N  N   . THR   C 1 69  ? -16.580 -31.273 34.058  1.00 76.18  ? 74  THR   C N   1 
ATOM   5288 C  CA  . THR   C 1 69  ? -17.411 -31.416 35.257  1.00 77.26  ? 74  THR   C CA  1 
ATOM   5289 C  C   . THR   C 1 69  ? -17.495 -30.066 36.003  1.00 83.59  ? 74  THR   C C   1 
ATOM   5290 O  O   . THR   C 1 69  ? -16.462 -29.558 36.456  1.00 83.13  ? 74  THR   C O   1 
ATOM   5291 C  CB  . THR   C 1 69  ? -16.902 -32.585 36.126  1.00 86.36  ? 74  THR   C CB  1 
ATOM   5292 O  OG1 . THR   C 1 69  ? -16.688 -33.733 35.300  1.00 85.57  ? 74  THR   C OG1 1 
ATOM   5293 C  CG2 . THR   C 1 69  ? -17.857 -32.934 37.264  1.00 85.21  ? 74  THR   C CG2 1 
ATOM   5294 N  N   . PRO   C 1 70  ? -18.701 -29.456 36.113  1.00 82.00  ? 75  PRO   C N   1 
ATOM   5295 C  CA  . PRO   C 1 70  ? -18.801 -28.158 36.797  1.00 82.46  ? 75  PRO   C CA  1 
ATOM   5296 C  C   . PRO   C 1 70  ? -18.737 -28.279 38.316  1.00 88.22  ? 75  PRO   C C   1 
ATOM   5297 O  O   . PRO   C 1 70  ? -19.385 -29.156 38.896  1.00 87.89  ? 75  PRO   C O   1 
ATOM   5298 C  CB  . PRO   C 1 70  ? -20.150 -27.593 36.317  1.00 84.10  ? 75  PRO   C CB  1 
ATOM   5299 C  CG  . PRO   C 1 70  ? -20.708 -28.605 35.341  1.00 88.26  ? 75  PRO   C CG  1 
ATOM   5300 C  CD  . PRO   C 1 70  ? -20.021 -29.897 35.625  1.00 83.70  ? 75  PRO   C CD  1 
ATOM   5301 N  N   . VAL   C 1 71  ? -17.938 -27.401 38.953  1.00 85.98  ? 76  VAL   C N   1 
ATOM   5302 C  CA  . VAL   C 1 71  ? -17.771 -27.355 40.407  1.00 86.37  ? 76  VAL   C CA  1 
ATOM   5303 C  C   . VAL   C 1 71  ? -18.744 -26.286 40.951  1.00 92.02  ? 76  VAL   C C   1 
ATOM   5304 O  O   . VAL   C 1 71  ? -18.557 -25.100 40.657  1.00 91.64  ? 76  VAL   C O   1 
ATOM   5305 C  CB  . VAL   C 1 71  ? -16.294 -27.116 40.842  1.00 90.14  ? 76  VAL   C CB  1 
ATOM   5306 C  CG1 . VAL   C 1 71  ? -16.150 -27.140 42.361  1.00 89.93  ? 76  VAL   C CG1 1 
ATOM   5307 C  CG2 . VAL   C 1 71  ? -15.356 -28.140 40.209  1.00 89.94  ? 76  VAL   C CG2 1 
ATOM   5308 N  N   . PRO   C 1 72  ? -19.816 -26.680 41.688  1.00 89.76  ? 77  PRO   C N   1 
ATOM   5309 C  CA  . PRO   C 1 72  ? -20.767 -25.672 42.194  1.00 89.75  ? 77  PRO   C CA  1 
ATOM   5310 C  C   . PRO   C 1 72  ? -20.194 -24.823 43.328  1.00 93.26  ? 77  PRO   C C   1 
ATOM   5311 O  O   . PRO   C 1 72  ? -20.375 -23.604 43.316  1.00 93.13  ? 77  PRO   C O   1 
ATOM   5312 C  CB  . PRO   C 1 72  ? -21.985 -26.502 42.638  1.00 91.67  ? 77  PRO   C CB  1 
ATOM   5313 C  CG  . PRO   C 1 72  ? -21.690 -27.927 42.238  1.00 96.13  ? 77  PRO   C CG  1 
ATOM   5314 C  CD  . PRO   C 1 72  ? -20.207 -28.038 42.114  1.00 91.56  ? 77  PRO   C CD  1 
ATOM   5315 N  N   . LYS   C 1 73  ? -19.496 -25.458 44.292  1.00 89.19  ? 78  LYS   C N   1 
ATOM   5316 C  CA  . LYS   C 1 73  ? -18.872 -24.771 45.422  1.00 88.76  ? 78  LYS   C CA  1 
ATOM   5317 C  C   . LYS   C 1 73  ? -17.372 -24.617 45.153  1.00 91.52  ? 78  LYS   C C   1 
ATOM   5318 O  O   . LYS   C 1 73  ? -16.598 -25.558 45.352  1.00 91.12  ? 78  LYS   C O   1 
ATOM   5319 C  CB  . LYS   C 1 73  ? -19.161 -25.497 46.756  1.00 91.39  ? 78  LYS   C CB  1 
ATOM   5320 C  CG  . LYS   C 1 73  ? -18.750 -24.700 47.992  1.00 109.26 ? 78  LYS   C CG  1 
ATOM   5321 C  CD  . LYS   C 1 73  ? -19.008 -25.462 49.290  1.00 120.84 ? 78  LYS   C CD  1 
ATOM   5322 C  CE  . LYS   C 1 73  ? -18.441 -24.757 50.504  1.00 132.55 ? 78  LYS   C CE  1 
ATOM   5323 N  NZ  . LYS   C 1 73  ? -19.193 -23.518 50.850  1.00 141.97 ? 78  LYS   C NZ  1 
ATOM   5324 N  N   . ASP   C 1 74  ? -16.980 -23.428 44.662  1.00 87.09  ? 79  ASP   C N   1 
ATOM   5325 C  CA  . ASP   C 1 74  ? -15.595 -23.093 44.332  1.00 86.39  ? 79  ASP   C CA  1 
ATOM   5326 C  C   . ASP   C 1 74  ? -15.318 -21.619 44.650  1.00 88.75  ? 79  ASP   C C   1 
ATOM   5327 O  O   . ASP   C 1 74  ? -15.306 -20.769 43.751  1.00 88.48  ? 79  ASP   C O   1 
ATOM   5328 C  CB  . ASP   C 1 74  ? -15.288 -23.439 42.855  1.00 88.22  ? 79  ASP   C CB  1 
ATOM   5329 C  CG  . ASP   C 1 74  ? -13.832 -23.328 42.421  1.00 97.67  ? 79  ASP   C CG  1 
ATOM   5330 O  OD1 . ASP   C 1 74  ? -12.946 -23.273 43.304  1.00 97.99  ? 79  ASP   C OD1 1 
ATOM   5331 O  OD2 . ASP   C 1 74  ? -13.575 -23.351 41.202  1.00 102.88 ? 79  ASP   C OD2 1 
ATOM   5332 N  N   . ASP   C 1 75  ? -15.120 -21.319 45.947  1.00 83.79  ? 80  ASP   C N   1 
ATOM   5333 C  CA  . ASP   C 1 75  ? -14.833 -19.962 46.414  1.00 82.81  ? 80  ASP   C CA  1 
ATOM   5334 C  C   . ASP   C 1 75  ? -13.388 -19.563 46.105  1.00 83.71  ? 80  ASP   C C   1 
ATOM   5335 O  O   . ASP   C 1 75  ? -12.547 -20.435 45.862  1.00 83.35  ? 80  ASP   C O   1 
ATOM   5336 C  CB  . ASP   C 1 75  ? -15.179 -19.792 47.902  1.00 84.91  ? 80  ASP   C CB  1 
ATOM   5337 C  CG  . ASP   C 1 75  ? -16.346 -18.849 48.129  1.00 96.81  ? 80  ASP   C CG  1 
ATOM   5338 O  OD1 . ASP   C 1 75  ? -16.104 -17.630 48.279  1.00 97.80  ? 80  ASP   C OD1 1 
ATOM   5339 O  OD2 . ASP   C 1 75  ? -17.504 -19.326 48.132  1.00 102.37 ? 80  ASP   C OD2 1 
ATOM   5340 N  N   . LEU   C 1 76  ? -13.114 -18.244 46.085  1.00 77.79  ? 81  LEU   C N   1 
ATOM   5341 C  CA  . LEU   C 1 76  ? -11.802 -17.681 45.756  1.00 76.34  ? 81  LEU   C CA  1 
ATOM   5342 C  C   . LEU   C 1 76  ? -10.716 -18.017 46.787  1.00 76.99  ? 81  LEU   C C   1 
ATOM   5343 O  O   . LEU   C 1 76  ? -10.971 -18.000 47.992  1.00 77.16  ? 81  LEU   C O   1 
ATOM   5344 C  CB  . LEU   C 1 76  ? -11.843 -16.160 45.447  1.00 76.39  ? 81  LEU   C CB  1 
ATOM   5345 C  CG  . LEU   C 1 76  ? -12.753 -15.214 46.257  1.00 81.11  ? 81  LEU   C CG  1 
ATOM   5346 C  CD1 . LEU   C 1 76  ? -12.298 -13.781 46.097  1.00 81.20  ? 81  LEU   C CD1 1 
ATOM   5347 C  CD2 . LEU   C 1 76  ? -14.210 -15.282 45.789  1.00 83.86  ? 81  LEU   C CD2 1 
ATOM   5348 N  N   . TYR   C 1 77  ? -9.518  -18.377 46.282  1.00 70.33  ? 82  TYR   C N   1 
ATOM   5349 C  CA  . TYR   C 1 77  ? -8.325  -18.749 47.049  1.00 68.67  ? 82  TYR   C CA  1 
ATOM   5350 C  C   . TYR   C 1 77  ? -7.570  -17.490 47.481  1.00 70.37  ? 82  TYR   C C   1 
ATOM   5351 O  O   . TYR   C 1 77  ? -7.154  -16.698 46.626  1.00 69.37  ? 82  TYR   C O   1 
ATOM   5352 C  CB  . TYR   C 1 77  ? -7.423  -19.674 46.201  1.00 69.25  ? 82  TYR   C CB  1 
ATOM   5353 C  CG  . TYR   C 1 77  ? -6.123  -20.094 46.857  1.00 69.97  ? 82  TYR   C CG  1 
ATOM   5354 C  CD1 . TYR   C 1 77  ? -6.073  -21.189 47.714  1.00 71.63  ? 82  TYR   C CD1 1 
ATOM   5355 C  CD2 . TYR   C 1 77  ? -4.929  -19.440 46.564  1.00 70.58  ? 82  TYR   C CD2 1 
ATOM   5356 C  CE1 . TYR   C 1 77  ? -4.874  -21.601 48.295  1.00 72.24  ? 82  TYR   C CE1 1 
ATOM   5357 C  CE2 . TYR   C 1 77  ? -3.725  -19.834 47.150  1.00 71.32  ? 82  TYR   C CE2 1 
ATOM   5358 C  CZ  . TYR   C 1 77  ? -3.702  -20.919 48.011  1.00 77.76  ? 82  TYR   C CZ  1 
ATOM   5359 O  OH  . TYR   C 1 77  ? -2.521  -21.322 48.587  1.00 77.64  ? 82  TYR   C OH  1 
ATOM   5360 N  N   . ASN   C 1 78  ? -7.393  -17.319 48.816  1.00 65.38  ? 83  ASN   C N   1 
ATOM   5361 C  CA  . ASN   C 1 78  ? -6.730  -16.179 49.478  1.00 64.30  ? 83  ASN   C CA  1 
ATOM   5362 C  C   . ASN   C 1 78  ? -7.313  -14.823 49.044  1.00 65.16  ? 83  ASN   C C   1 
ATOM   5363 O  O   . ASN   C 1 78  ? -6.568  -13.860 48.837  1.00 64.85  ? 83  ASN   C O   1 
ATOM   5364 C  CB  . ASN   C 1 78  ? -5.195  -16.228 49.321  1.00 66.74  ? 83  ASN   C CB  1 
ATOM   5365 C  CG  . ASN   C 1 78  ? -4.489  -17.166 50.274  1.00 96.58  ? 83  ASN   C CG  1 
ATOM   5366 O  OD1 . ASN   C 1 78  ? -4.862  -17.323 51.447  1.00 93.32  ? 83  ASN   C OD1 1 
ATOM   5367 N  ND2 . ASN   C 1 78  ? -3.411  -17.773 49.803  1.00 89.10  ? 83  ASN   C ND2 1 
ATOM   5368 N  N   . ASN   C 1 79  ? -8.659  -14.774 48.884  1.00 59.59  ? 84  ASN   C N   1 
ATOM   5369 C  CA  . ASN   C 1 79  ? -9.452  -13.607 48.479  1.00 59.06  ? 84  ASN   C CA  1 
ATOM   5370 C  C   . ASN   C 1 79  ? -8.933  -12.937 47.180  1.00 60.73  ? 84  ASN   C C   1 
ATOM   5371 O  O   . ASN   C 1 79  ? -9.028  -11.715 47.030  1.00 60.39  ? 84  ASN   C O   1 
ATOM   5372 C  CB  . ASN   C 1 79  ? -9.580  -12.599 49.644  1.00 62.81  ? 84  ASN   C CB  1 
ATOM   5373 C  CG  . ASN   C 1 79  ? -10.883 -11.840 49.656  1.00 94.26  ? 84  ASN   C CG  1 
ATOM   5374 O  OD1 . ASN   C 1 79  ? -11.957 -12.397 49.917  1.00 92.22  ? 84  ASN   C OD1 1 
ATOM   5375 N  ND2 . ASN   C 1 79  ? -10.816 -10.543 49.388  1.00 87.62  ? 84  ASN   C ND2 1 
ATOM   5376 N  N   . LEU   C 1 80  ? -8.408  -13.748 46.231  1.00 55.42  ? 85  LEU   C N   1 
ATOM   5377 C  CA  . LEU   C 1 80  ? -7.848  -13.252 44.973  1.00 54.36  ? 85  LEU   C CA  1 
ATOM   5378 C  C   . LEU   C 1 80  ? -8.043  -14.214 43.783  1.00 56.74  ? 85  LEU   C C   1 
ATOM   5379 O  O   . LEU   C 1 80  ? -8.653  -13.803 42.796  1.00 56.17  ? 85  LEU   C O   1 
ATOM   5380 C  CB  . LEU   C 1 80  ? -6.353  -12.880 45.172  1.00 54.27  ? 85  LEU   C CB  1 
ATOM   5381 C  CG  . LEU   C 1 80  ? -5.546  -12.349 43.968  1.00 58.71  ? 85  LEU   C CG  1 
ATOM   5382 C  CD1 . LEU   C 1 80  ? -5.941  -10.927 43.600  1.00 59.01  ? 85  LEU   C CD1 1 
ATOM   5383 C  CD2 . LEU   C 1 80  ? -4.070  -12.372 44.276  1.00 61.23  ? 85  LEU   C CD2 1 
ATOM   5384 N  N   . ILE   C 1 81  ? -7.516  -15.468 43.867  1.00 52.97  ? 86  ILE   C N   1 
ATOM   5385 C  CA  . ILE   C 1 81  ? -7.581  -16.483 42.792  1.00 52.69  ? 86  ILE   C CA  1 
ATOM   5386 C  C   . ILE   C 1 81  ? -9.018  -16.950 42.530  1.00 57.98  ? 86  ILE   C C   1 
ATOM   5387 O  O   . ILE   C 1 81  ? -9.602  -17.653 43.358  1.00 57.41  ? 86  ILE   C O   1 
ATOM   5388 C  CB  . ILE   C 1 81  ? -6.609  -17.692 43.015  1.00 55.51  ? 86  ILE   C CB  1 
ATOM   5389 C  CG1 . ILE   C 1 81  ? -5.206  -17.264 43.539  1.00 55.75  ? 86  ILE   C CG1 1 
ATOM   5390 C  CG2 . ILE   C 1 81  ? -6.495  -18.584 41.761  1.00 55.54  ? 86  ILE   C CG2 1 
ATOM   5391 C  CD1 . ILE   C 1 81  ? -4.341  -16.458 42.627  1.00 60.22  ? 86  ILE   C CD1 1 
ATOM   5392 N  N   . VAL   C 1 82  ? -9.571  -16.572 41.365  1.00 55.47  ? 87  VAL   C N   1 
ATOM   5393 C  CA  . VAL   C 1 82  ? -10.935 -16.913 40.958  1.00 55.88  ? 87  VAL   C CA  1 
ATOM   5394 C  C   . VAL   C 1 82  ? -10.990 -18.314 40.287  1.00 59.44  ? 87  VAL   C C   1 
ATOM   5395 O  O   . VAL   C 1 82  ? -10.099 -18.681 39.514  1.00 57.42  ? 87  VAL   C O   1 
ATOM   5396 C  CB  . VAL   C 1 82  ? -11.600 -15.779 40.116  1.00 60.88  ? 87  VAL   C CB  1 
ATOM   5397 C  CG1 . VAL   C 1 82  ? -10.931 -15.584 38.755  1.00 60.99  ? 87  VAL   C CG1 1 
ATOM   5398 C  CG2 . VAL   C 1 82  ? -13.108 -15.980 39.971  1.00 61.04  ? 87  VAL   C CG2 1 
ATOM   5399 N  N   . ASN   C 1 83  ? -12.039 -19.092 40.640  1.00 56.93  ? 88  ASN   C N   1 
ATOM   5400 C  CA  . ASN   C 1 83  ? -12.350 -20.447 40.165  1.00 56.79  ? 88  ASN   C CA  1 
ATOM   5401 C  C   . ASN   C 1 83  ? -11.132 -21.412 40.178  1.00 61.37  ? 88  ASN   C C   1 
ATOM   5402 O  O   . ASN   C 1 83  ? -10.843 -21.986 39.129  1.00 61.86  ? 88  ASN   C O   1 
ATOM   5403 C  CB  . ASN   C 1 83  ? -12.993 -20.390 38.762  1.00 57.49  ? 88  ASN   C CB  1 
ATOM   5404 C  CG  . ASN   C 1 83  ? -14.053 -19.332 38.570  1.00 78.16  ? 88  ASN   C CG  1 
ATOM   5405 O  OD1 . ASN   C 1 83  ? -15.088 -19.308 39.247  1.00 73.59  ? 88  ASN   C OD1 1 
ATOM   5406 N  ND2 . ASN   C 1 83  ? -13.835 -18.461 37.600  1.00 68.83  ? 88  ASN   C ND2 1 
ATOM   5407 N  N   . PRO   C 1 84  ? -10.381 -21.616 41.296  1.00 57.67  ? 89  PRO   C N   1 
ATOM   5408 C  CA  . PRO   C 1 84  ? -9.209  -22.511 41.221  1.00 57.51  ? 89  PRO   C CA  1 
ATOM   5409 C  C   . PRO   C 1 84  ? -9.547  -23.973 40.932  1.00 61.76  ? 89  PRO   C C   1 
ATOM   5410 O  O   . PRO   C 1 84  ? -9.026  -24.516 39.959  1.00 61.43  ? 89  PRO   C O   1 
ATOM   5411 C  CB  . PRO   C 1 84  ? -8.497  -22.314 42.567  1.00 59.23  ? 89  PRO   C CB  1 
ATOM   5412 C  CG  . PRO   C 1 84  ? -9.135  -21.112 43.189  1.00 63.81  ? 89  PRO   C CG  1 
ATOM   5413 C  CD  . PRO   C 1 84  ? -10.525 -21.049 42.651  1.00 59.44  ? 89  PRO   C CD  1 
ATOM   5414 N  N   . ARG   C 1 85  ? -10.450 -24.589 41.730  1.00 57.81  ? 90  ARG   C N   1 
ATOM   5415 C  CA  . ARG   C 1 85  ? -10.876 -25.987 41.562  1.00 56.88  ? 90  ARG   C CA  1 
ATOM   5416 C  C   . ARG   C 1 85  ? -11.421 -26.276 40.164  1.00 56.94  ? 90  ARG   C C   1 
ATOM   5417 O  O   . ARG   C 1 85  ? -11.052 -27.294 39.580  1.00 55.87  ? 90  ARG   C O   1 
ATOM   5418 C  CB  . ARG   C 1 85  ? -11.896 -26.402 42.641  1.00 58.72  ? 90  ARG   C CB  1 
ATOM   5419 C  CG  . ARG   C 1 85  ? -11.295 -26.543 44.030  1.00 73.87  ? 90  ARG   C CG  1 
ATOM   5420 C  CD  . ARG   C 1 85  ? -12.359 -26.584 45.113  1.00 87.67  ? 90  ARG   C CD  1 
ATOM   5421 N  NE  . ARG   C 1 85  ? -11.834 -26.124 46.402  1.00 99.77  ? 90  ARG   C NE  1 
ATOM   5422 C  CZ  . ARG   C 1 85  ? -11.971 -24.887 46.874  1.00 114.83 ? 90  ARG   C CZ  1 
ATOM   5423 N  NH1 . ARG   C 1 85  ? -12.630 -23.970 46.175  1.00 100.73 ? 90  ARG   C NH1 1 
ATOM   5424 N  NH2 . ARG   C 1 85  ? -11.457 -24.560 48.051  1.00 103.23 ? 90  ARG   C NH2 1 
ATOM   5425 N  N   . SER   C 1 86  ? -12.273 -25.372 39.627  1.00 52.05  ? 91  SER   C N   1 
ATOM   5426 C  CA  . SER   C 1 86  ? -12.875 -25.484 38.296  1.00 51.50  ? 91  SER   C CA  1 
ATOM   5427 C  C   . SER   C 1 86  ? -11.817 -25.542 37.186  1.00 53.78  ? 91  SER   C C   1 
ATOM   5428 O  O   . SER   C 1 86  ? -11.903 -26.412 36.316  1.00 53.35  ? 91  SER   C O   1 
ATOM   5429 C  CB  . SER   C 1 86  ? -13.856 -24.341 38.044  1.00 55.54  ? 91  SER   C CB  1 
ATOM   5430 O  OG  . SER   C 1 86  ? -14.956 -24.400 38.939  1.00 64.58  ? 91  SER   C OG  1 
ATOM   5431 N  N   . VAL   C 1 87  ? -10.806 -24.649 37.246  1.00 48.91  ? 92  VAL   C N   1 
ATOM   5432 C  CA  . VAL   C 1 87  ? -9.701  -24.571 36.280  1.00 48.75  ? 92  VAL   C CA  1 
ATOM   5433 C  C   . VAL   C 1 87  ? -8.791  -25.796 36.409  1.00 52.99  ? 92  VAL   C C   1 
ATOM   5434 O  O   . VAL   C 1 87  ? -8.398  -26.369 35.394  1.00 52.22  ? 92  VAL   C O   1 
ATOM   5435 C  CB  . VAL   C 1 87  ? -8.914  -23.237 36.422  1.00 51.76  ? 92  VAL   C CB  1 
ATOM   5436 C  CG1 . VAL   C 1 87  ? -7.626  -23.234 35.595  1.00 51.51  ? 92  VAL   C CG1 1 
ATOM   5437 C  CG2 . VAL   C 1 87  ? -9.789  -22.053 36.053  1.00 51.08  ? 92  VAL   C CG2 1 
ATOM   5438 N  N   . GLY   C 1 88  ? -8.472  -26.174 37.649  1.00 49.75  ? 93  GLY   C N   1 
ATOM   5439 C  CA  . GLY   C 1 88  ? -7.605  -27.308 37.947  1.00 49.65  ? 93  GLY   C CA  1 
ATOM   5440 C  C   . GLY   C 1 88  ? -8.158  -28.656 37.520  1.00 53.72  ? 93  GLY   C C   1 
ATOM   5441 O  O   . GLY   C 1 88  ? -7.404  -29.504 37.033  1.00 52.35  ? 93  GLY   C O   1 
ATOM   5442 N  N   . LEU   C 1 89  ? -9.478  -28.860 37.712  1.00 51.41  ? 94  LEU   C N   1 
ATOM   5443 C  CA  . LEU   C 1 89  ? -10.180 -30.106 37.380  1.00 51.75  ? 94  LEU   C CA  1 
ATOM   5444 C  C   . LEU   C 1 89  ? -10.382 -30.249 35.873  1.00 55.05  ? 94  LEU   C C   1 
ATOM   5445 O  O   . LEU   C 1 89  ? -10.201 -31.344 35.343  1.00 53.90  ? 94  LEU   C O   1 
ATOM   5446 C  CB  . LEU   C 1 89  ? -11.525 -30.214 38.147  1.00 52.05  ? 94  LEU   C CB  1 
ATOM   5447 C  CG  . LEU   C 1 89  ? -12.496 -31.375 37.798  1.00 57.22  ? 94  LEU   C CG  1 
ATOM   5448 C  CD1 . LEU   C 1 89  ? -11.911 -32.722 38.158  1.00 57.83  ? 94  LEU   C CD1 1 
ATOM   5449 C  CD2 . LEU   C 1 89  ? -13.823 -31.205 38.508  1.00 58.56  ? 94  LEU   C CD2 1 
ATOM   5450 N  N   . ALA   C 1 90  ? -10.779 -29.151 35.193  1.00 51.60  ? 95  ALA   C N   1 
ATOM   5451 C  CA  . ALA   C 1 90  ? -10.985 -29.135 33.747  1.00 50.94  ? 95  ALA   C CA  1 
ATOM   5452 C  C   . ALA   C 1 90  ? -9.662  -29.421 33.024  1.00 52.42  ? 95  ALA   C C   1 
ATOM   5453 O  O   . ALA   C 1 90  ? -9.663  -30.142 32.023  1.00 51.41  ? 95  ALA   C O   1 
ATOM   5454 C  CB  . ALA   C 1 90  ? -11.571 -27.801 33.302  1.00 51.58  ? 95  ALA   C CB  1 
ATOM   5455 N  N   . ASN   C 1 91  ? -8.538  -28.916 33.568  1.00 47.35  ? 96  ASN   C N   1 
ATOM   5456 C  CA  . ASN   C 1 91  ? -7.204  -29.168 33.024  1.00 46.21  ? 96  ASN   C CA  1 
ATOM   5457 C  C   . ASN   C 1 91  ? -6.809  -30.631 33.226  1.00 48.96  ? 96  ASN   C C   1 
ATOM   5458 O  O   . ASN   C 1 91  ? -6.139  -31.202 32.367  1.00 47.14  ? 96  ASN   C O   1 
ATOM   5459 C  CB  . ASN   C 1 91  ? -6.151  -28.229 33.638  1.00 42.94  ? 96  ASN   C CB  1 
ATOM   5460 C  CG  . ASN   C 1 91  ? -6.017  -26.913 32.916  1.00 61.77  ? 96  ASN   C CG  1 
ATOM   5461 O  OD1 . ASN   C 1 91  ? -5.715  -26.862 31.718  1.00 55.29  ? 96  ASN   C OD1 1 
ATOM   5462 N  ND2 . ASN   C 1 91  ? -6.237  -25.818 33.625  1.00 47.23  ? 96  ASN   C ND2 1 
ATOM   5463 N  N   . GLN   C 1 92  ? -7.229  -31.238 34.354  1.00 44.89  ? 97  GLN   C N   1 
ATOM   5464 C  CA  . GLN   C 1 92  ? -6.935  -32.645 34.660  1.00 43.33  ? 97  GLN   C CA  1 
ATOM   5465 C  C   . GLN   C 1 92  ? -7.618  -33.562 33.663  1.00 45.29  ? 97  GLN   C C   1 
ATOM   5466 O  O   . GLN   C 1 92  ? -6.990  -34.500 33.180  1.00 45.72  ? 97  GLN   C O   1 
ATOM   5467 C  CB  . GLN   C 1 92  ? -7.333  -33.000 36.104  1.00 44.68  ? 97  GLN   C CB  1 
ATOM   5468 C  CG  . GLN   C 1 92  ? -6.458  -34.117 36.689  1.00 59.62  ? 97  GLN   C CG  1 
ATOM   5469 C  CD  . GLN   C 1 92  ? -6.983  -34.685 37.986  1.00 81.74  ? 97  GLN   C CD  1 
ATOM   5470 O  OE1 . GLN   C 1 92  ? -7.618  -33.998 38.795  1.00 76.49  ? 97  GLN   C OE1 1 
ATOM   5471 N  NE2 . GLN   C 1 92  ? -6.710  -35.961 38.221  1.00 77.87  ? 97  GLN   C NE2 1 
ATOM   5472 N  N   . GLU   C 1 93  ? -8.882  -33.253 33.318  1.00 41.54  ? 98  GLU   C N   1 
ATOM   5473 C  CA  . GLU   C 1 93  ? -9.702  -33.975 32.351  1.00 42.10  ? 98  GLU   C CA  1 
ATOM   5474 C  C   . GLU   C 1 93  ? -9.103  -33.796 30.952  1.00 46.27  ? 98  GLU   C C   1 
ATOM   5475 O  O   . GLU   C 1 93  ? -8.977  -34.768 30.204  1.00 46.25  ? 98  GLU   C O   1 
ATOM   5476 C  CB  . GLU   C 1 93  ? -11.148 -33.451 32.365  1.00 44.07  ? 98  GLU   C CB  1 
ATOM   5477 C  CG  . GLU   C 1 93  ? -11.930 -33.797 33.623  1.00 56.66  ? 98  GLU   C CG  1 
ATOM   5478 C  CD  . GLU   C 1 93  ? -13.377 -33.354 33.569  1.00 81.38  ? 98  GLU   C CD  1 
ATOM   5479 O  OE1 . GLU   C 1 93  ? -14.185 -34.040 32.901  1.00 88.56  ? 98  GLU   C OE1 1 
ATOM   5480 O  OE2 . GLU   C 1 93  ? -13.702 -32.311 34.179  1.00 73.15  ? 98  GLU   C OE2 1 
ATOM   5481 N  N   . LEU   C 1 94  ? -8.715  -32.546 30.617  1.00 42.08  ? 99  LEU   C N   1 
ATOM   5482 C  CA  . LEU   C 1 94  ? -8.099  -32.216 29.336  1.00 40.49  ? 99  LEU   C CA  1 
ATOM   5483 C  C   . LEU   C 1 94  ? -6.762  -32.934 29.145  1.00 41.87  ? 99  LEU   C C   1 
ATOM   5484 O  O   . LEU   C 1 94  ? -6.549  -33.474 28.062  1.00 41.86  ? 99  LEU   C O   1 
ATOM   5485 C  CB  . LEU   C 1 94  ? -7.963  -30.685 29.152  1.00 40.60  ? 99  LEU   C CB  1 
ATOM   5486 C  CG  . LEU   C 1 94  ? -7.247  -30.172 27.877  1.00 44.22  ? 99  LEU   C CG  1 
ATOM   5487 C  CD1 . LEU   C 1 94  ? -7.945  -30.633 26.608  1.00 42.98  ? 99  LEU   C CD1 1 
ATOM   5488 C  CD2 . LEU   C 1 94  ? -7.150  -28.663 27.905  1.00 44.82  ? 99  LEU   C CD2 1 
ATOM   5489 N  N   . ALA   C 1 95  ? -5.893  -32.970 30.185  1.00 37.33  ? 100 ALA   C N   1 
ATOM   5490 C  CA  . ALA   C 1 95  ? -4.586  -33.629 30.144  1.00 37.72  ? 100 ALA   C CA  1 
ATOM   5491 C  C   . ALA   C 1 95  ? -4.686  -35.133 29.813  1.00 45.67  ? 100 ALA   C C   1 
ATOM   5492 O  O   . ALA   C 1 95  ? -3.778  -35.677 29.170  1.00 44.48  ? 100 ALA   C O   1 
ATOM   5493 C  CB  . ALA   C 1 95  ? -3.839  -33.427 31.450  1.00 38.25  ? 100 ALA   C CB  1 
ATOM   5494 N  N   . GLU   C 1 96  ? -5.780  -35.789 30.268  1.00 44.52  ? 101 GLU   C N   1 
ATOM   5495 C  CA  . GLU   C 1 96  ? -6.087  -37.202 30.019  1.00 45.20  ? 101 GLU   C CA  1 
ATOM   5496 C  C   . GLU   C 1 96  ? -6.460  -37.402 28.543  1.00 49.79  ? 101 GLU   C C   1 
ATOM   5497 O  O   . GLU   C 1 96  ? -5.893  -38.296 27.908  1.00 49.24  ? 101 GLU   C O   1 
ATOM   5498 C  CB  . GLU   C 1 96  ? -7.245  -37.689 30.922  1.00 46.64  ? 101 GLU   C CB  1 
ATOM   5499 C  CG  . GLU   C 1 96  ? -6.860  -37.897 32.376  1.00 61.77  ? 101 GLU   C CG  1 
ATOM   5500 C  CD  . GLU   C 1 96  ? -6.199  -39.228 32.678  1.00 93.95  ? 101 GLU   C CD  1 
ATOM   5501 O  OE1 . GLU   C 1 96  ? -4.974  -39.238 32.935  1.00 93.71  ? 101 GLU   C OE1 1 
ATOM   5502 O  OE2 . GLU   C 1 96  ? -6.907  -40.262 32.657  1.00 94.36  ? 101 GLU   C OE2 1 
ATOM   5503 N  N   . VAL   C 1 97  ? -7.413  -36.573 28.009  1.00 46.44  ? 102 VAL   C N   1 
ATOM   5504 C  CA  . VAL   C 1 97  ? -7.884  -36.606 26.608  1.00 46.91  ? 102 VAL   C CA  1 
ATOM   5505 C  C   . VAL   C 1 97  ? -6.697  -36.353 25.649  1.00 52.07  ? 102 VAL   C C   1 
ATOM   5506 O  O   . VAL   C 1 97  ? -6.567  -37.036 24.628  1.00 50.86  ? 102 VAL   C O   1 
ATOM   5507 C  CB  . VAL   C 1 97  ? -9.085  -35.650 26.338  1.00 50.56  ? 102 VAL   C CB  1 
ATOM   5508 C  CG1 . VAL   C 1 97  ? -9.537  -35.706 24.877  1.00 50.47  ? 102 VAL   C CG1 1 
ATOM   5509 C  CG2 . VAL   C 1 97  ? -10.264 -35.969 27.254  1.00 50.56  ? 102 VAL   C CG2 1 
ATOM   5510 N  N   . VAL   C 1 98  ? -5.825  -35.389 26.014  1.00 49.09  ? 103 VAL   C N   1 
ATOM   5511 C  CA  . VAL   C 1 98  ? -4.615  -35.022 25.284  1.00 48.99  ? 103 VAL   C CA  1 
ATOM   5512 C  C   . VAL   C 1 98  ? -3.629  -36.190 25.318  1.00 55.97  ? 103 VAL   C C   1 
ATOM   5513 O  O   . VAL   C 1 98  ? -3.090  -36.544 24.268  1.00 55.19  ? 103 VAL   C O   1 
ATOM   5514 C  CB  . VAL   C 1 98  ? -4.010  -33.686 25.822  1.00 51.83  ? 103 VAL   C CB  1 
ATOM   5515 C  CG1 . VAL   C 1 98  ? -2.525  -33.539 25.487  1.00 50.94  ? 103 VAL   C CG1 1 
ATOM   5516 C  CG2 . VAL   C 1 98  ? -4.807  -32.487 25.315  1.00 51.26  ? 103 VAL   C CG2 1 
ATOM   5517 N  N   . SER   C 1 99  ? -3.421  -36.812 26.504  1.00 53.93  ? 104 SER   C N   1 
ATOM   5518 C  CA  . SER   C 1 99  ? -2.499  -37.947 26.642  1.00 54.32  ? 104 SER   C CA  1 
ATOM   5519 C  C   . SER   C 1 99  ? -2.948  -39.137 25.783  1.00 57.65  ? 104 SER   C C   1 
ATOM   5520 O  O   . SER   C 1 99  ? -2.112  -39.761 25.136  1.00 57.11  ? 104 SER   C O   1 
ATOM   5521 C  CB  . SER   C 1 99  ? -2.340  -38.358 28.103  1.00 58.35  ? 104 SER   C CB  1 
ATOM   5522 O  OG  . SER   C 1 99  ? -1.084  -38.982 28.323  1.00 68.89  ? 104 SER   C OG  1 
ATOM   5523 N  N   . ARG   C 1 100 ? -4.271  -39.391 25.728  1.00 54.93  ? 105 ARG   C N   1 
ATOM   5524 C  CA  . ARG   C 1 100 ? -4.893  -40.472 24.955  1.00 55.36  ? 105 ARG   C CA  1 
ATOM   5525 C  C   . ARG   C 1 100 ? -4.804  -40.190 23.440  1.00 58.70  ? 105 ARG   C C   1 
ATOM   5526 O  O   . ARG   C 1 100 ? -4.462  -41.098 22.683  1.00 58.87  ? 105 ARG   C O   1 
ATOM   5527 C  CB  . ARG   C 1 100 ? -6.349  -40.676 25.408  1.00 58.42  ? 105 ARG   C CB  1 
ATOM   5528 C  CG  . ARG   C 1 100 ? -6.941  -42.045 25.085  1.00 75.91  ? 105 ARG   C CG  1 
ATOM   5529 C  CD  . ARG   C 1 100 ? -7.111  -42.870 26.351  1.00 94.08  ? 105 ARG   C CD  1 
ATOM   5530 N  NE  . ARG   C 1 100 ? -8.517  -43.085 26.710  1.00 106.78 ? 105 ARG   C NE  1 
ATOM   5531 C  CZ  . ARG   C 1 100 ? -9.245  -42.262 27.463  1.00 121.17 ? 105 ARG   C CZ  1 
ATOM   5532 N  NH1 . ARG   C 1 100 ? -8.719  -41.134 27.928  1.00 108.48 ? 105 ARG   C NH1 1 
ATOM   5533 N  NH2 . ARG   C 1 100 ? -10.507 -42.554 27.745  1.00 106.61 ? 105 ARG   C NH2 1 
ATOM   5534 N  N   . ALA   C 1 101 ? -5.082  -38.936 23.006  1.00 53.93  ? 106 ALA   C N   1 
ATOM   5535 C  CA  . ALA   C 1 101 ? -4.990  -38.523 21.595  1.00 53.24  ? 106 ALA   C CA  1 
ATOM   5536 C  C   . ALA   C 1 101 ? -3.548  -38.642 21.082  1.00 55.04  ? 106 ALA   C C   1 
ATOM   5537 O  O   . ALA   C 1 101 ? -3.344  -39.140 19.971  1.00 54.26  ? 106 ALA   C O   1 
ATOM   5538 C  CB  . ALA   C 1 101 ? -5.506  -37.103 21.413  1.00 53.84  ? 106 ALA   C CB  1 
ATOM   5539 N  N   . VAL   C 1 102 ? -2.555  -38.248 21.916  1.00 50.30  ? 107 VAL   C N   1 
ATOM   5540 C  CA  . VAL   C 1 102 ? -1.126  -38.342 21.587  1.00 49.96  ? 107 VAL   C CA  1 
ATOM   5541 C  C   . VAL   C 1 102 ? -0.770  -39.808 21.411  1.00 55.56  ? 107 VAL   C C   1 
ATOM   5542 O  O   . VAL   C 1 102 ? -0.224  -40.170 20.370  1.00 55.41  ? 107 VAL   C O   1 
ATOM   5543 C  CB  . VAL   C 1 102 ? -0.200  -37.611 22.613  1.00 53.26  ? 107 VAL   C CB  1 
ATOM   5544 C  CG1 . VAL   C 1 102 ? 1.267   -37.994 22.429  1.00 52.60  ? 107 VAL   C CG1 1 
ATOM   5545 C  CG2 . VAL   C 1 102 ? -0.361  -36.095 22.521  1.00 53.16  ? 107 VAL   C CG2 1 
ATOM   5546 N  N   . SER   C 1 103 ? -1.138  -40.649 22.414  1.00 53.21  ? 108 SER   C N   1 
ATOM   5547 C  CA  . SER   C 1 103 ? -0.944  -42.103 22.477  1.00 53.24  ? 108 SER   C CA  1 
ATOM   5548 C  C   . SER   C 1 103 ? -1.458  -42.808 21.209  1.00 57.27  ? 108 SER   C C   1 
ATOM   5549 O  O   . SER   C 1 103 ? -0.769  -43.676 20.673  1.00 57.52  ? 108 SER   C O   1 
ATOM   5550 C  CB  . SER   C 1 103 ? -1.641  -42.664 23.718  1.00 57.09  ? 108 SER   C CB  1 
ATOM   5551 O  OG  . SER   C 1 103 ? -1.389  -44.044 23.921  1.00 70.84  ? 108 SER   C OG  1 
ATOM   5552 N  N   . ASP   C 1 104 ? -2.644  -42.396 20.713  1.00 53.69  ? 109 ASP   C N   1 
ATOM   5553 C  CA  . ASP   C 1 104 ? -3.295  -42.927 19.511  1.00 53.43  ? 109 ASP   C CA  1 
ATOM   5554 C  C   . ASP   C 1 104 ? -2.583  -42.531 18.195  1.00 57.35  ? 109 ASP   C C   1 
ATOM   5555 O  O   . ASP   C 1 104 ? -3.030  -42.931 17.116  1.00 57.39  ? 109 ASP   C O   1 
ATOM   5556 C  CB  . ASP   C 1 104 ? -4.790  -42.512 19.477  1.00 55.66  ? 109 ASP   C CB  1 
ATOM   5557 C  CG  . ASP   C 1 104 ? -5.676  -43.080 20.584  1.00 68.13  ? 109 ASP   C CG  1 
ATOM   5558 O  OD1 . ASP   C 1 104 ? -5.236  -44.031 21.278  1.00 68.85  ? 109 ASP   C OD1 1 
ATOM   5559 O  OD2 . ASP   C 1 104 ? -6.811  -42.578 20.753  1.00 74.53  ? 109 ASP   C OD2 1 
ATOM   5560 N  N   . GLY   C 1 105 ? -1.497  -41.760 18.302  1.00 52.86  ? 110 GLY   C N   1 
ATOM   5561 C  CA  . GLY   C 1 105 ? -0.690  -41.302 17.173  1.00 52.11  ? 110 GLY   C CA  1 
ATOM   5562 C  C   . GLY   C 1 105 ? -1.133  -40.007 16.510  1.00 53.50  ? 110 GLY   C C   1 
ATOM   5563 O  O   . GLY   C 1 105 ? -0.746  -39.742 15.366  1.00 52.84  ? 110 GLY   C O   1 
ATOM   5564 N  N   . TYR   C 1 106 ? -1.932  -39.179 17.211  1.00 48.00  ? 111 TYR   C N   1 
ATOM   5565 C  CA  . TYR   C 1 106 ? -2.405  -37.918 16.640  1.00 46.85  ? 111 TYR   C CA  1 
ATOM   5566 C  C   . TYR   C 1 106 ? -1.664  -36.680 17.162  1.00 48.74  ? 111 TYR   C C   1 
ATOM   5567 O  O   . TYR   C 1 106 ? -1.370  -36.594 18.356  1.00 49.09  ? 111 TYR   C O   1 
ATOM   5568 C  CB  . TYR   C 1 106 ? -3.897  -37.725 16.931  1.00 47.84  ? 111 TYR   C CB  1 
ATOM   5569 C  CG  . TYR   C 1 106 ? -4.859  -38.516 16.075  1.00 49.14  ? 111 TYR   C CG  1 
ATOM   5570 C  CD1 . TYR   C 1 106 ? -5.180  -38.100 14.784  1.00 50.93  ? 111 TYR   C CD1 1 
ATOM   5571 C  CD2 . TYR   C 1 106 ? -5.549  -39.607 16.596  1.00 49.75  ? 111 TYR   C CD2 1 
ATOM   5572 C  CE1 . TYR   C 1 106 ? -6.108  -38.794 14.008  1.00 51.32  ? 111 TYR   C CE1 1 
ATOM   5573 C  CE2 . TYR   C 1 106 ? -6.480  -40.310 15.831  1.00 50.15  ? 111 TYR   C CE2 1 
ATOM   5574 C  CZ  . TYR   C 1 106 ? -6.756  -39.901 14.536  1.00 56.90  ? 111 TYR   C CZ  1 
ATOM   5575 O  OH  . TYR   C 1 106 ? -7.688  -40.582 13.784  1.00 55.06  ? 111 TYR   C OH  1 
ATOM   5576 N  N   . SER   C 1 107 ? -1.430  -35.692 16.271  1.00 43.19  ? 112 SER   C N   1 
ATOM   5577 C  CA  . SER   C 1 107 ? -0.863  -34.377 16.621  1.00 42.73  ? 112 SER   C CA  1 
ATOM   5578 C  C   . SER   C 1 107 ? -2.047  -33.664 17.212  1.00 44.42  ? 112 SER   C C   1 
ATOM   5579 O  O   . SER   C 1 107 ? -3.102  -33.596 16.571  1.00 43.10  ? 112 SER   C O   1 
ATOM   5580 C  CB  . SER   C 1 107 ? -0.339  -33.648 15.386  1.00 46.00  ? 112 SER   C CB  1 
ATOM   5581 O  OG  . SER   C 1 107 ? 1.024   -33.983 15.186  1.00 55.29  ? 112 SER   C OG  1 
ATOM   5582 N  N   . CYS   C 1 108 ? -1.932  -33.254 18.480  1.00 43.31  ? 113 CYS   C N   1 
ATOM   5583 C  CA  . CYS   C 1 108 ? -3.076  -32.712 19.190  1.00 43.67  ? 113 CYS   C CA  1 
ATOM   5584 C  C   . CYS   C 1 108 ? -3.253  -31.210 19.054  1.00 42.14  ? 113 CYS   C C   1 
ATOM   5585 O  O   . CYS   C 1 108 ? -2.416  -30.454 19.517  1.00 40.85  ? 113 CYS   C O   1 
ATOM   5586 C  CB  . CYS   C 1 108 ? -3.050  -33.138 20.653  1.00 45.81  ? 113 CYS   C CB  1 
ATOM   5587 S  SG  . CYS   C 1 108 ? -4.642  -32.953 21.481  1.00 50.92  ? 113 CYS   C SG  1 
ATOM   5588 N  N   . VAL   C 1 109 ? -4.395  -30.807 18.482  1.00 37.64  ? 114 VAL   C N   1 
ATOM   5589 C  CA  . VAL   C 1 109 ? -4.831  -29.427 18.281  1.00 36.70  ? 114 VAL   C CA  1 
ATOM   5590 C  C   . VAL   C 1 109 ? -5.960  -29.158 19.278  1.00 40.42  ? 114 VAL   C C   1 
ATOM   5591 O  O   . VAL   C 1 109 ? -7.082  -29.671 19.117  1.00 39.06  ? 114 VAL   C O   1 
ATOM   5592 C  CB  . VAL   C 1 109 ? -5.260  -29.141 16.807  1.00 40.22  ? 114 VAL   C CB  1 
ATOM   5593 C  CG1 . VAL   C 1 109 ? -5.923  -27.772 16.659  1.00 39.97  ? 114 VAL   C CG1 1 
ATOM   5594 C  CG2 . VAL   C 1 109 ? -4.071  -29.255 15.866  1.00 39.54  ? 114 VAL   C CG2 1 
ATOM   5595 N  N   . THR   C 1 110 ? -5.650  -28.365 20.321  1.00 37.04  ? 115 THR   C N   1 
ATOM   5596 C  CA  . THR   C 1 110 ? -6.641  -27.974 21.312  1.00 36.53  ? 115 THR   C CA  1 
ATOM   5597 C  C   . THR   C 1 110 ? -7.132  -26.561 21.033  1.00 39.25  ? 115 THR   C C   1 
ATOM   5598 O  O   . THR   C 1 110 ? -6.338  -25.614 20.942  1.00 38.56  ? 115 THR   C O   1 
ATOM   5599 C  CB  . THR   C 1 110 ? -6.116  -28.148 22.741  1.00 41.80  ? 115 THR   C CB  1 
ATOM   5600 O  OG1 . THR   C 1 110 ? -5.602  -29.472 22.926  1.00 42.78  ? 115 THR   C OG1 1 
ATOM   5601 C  CG2 . THR   C 1 110 ? -7.194  -27.853 23.794  1.00 39.57  ? 115 THR   C CG2 1 
ATOM   5602 N  N   . LEU   C 1 111 ? -8.439  -26.435 20.846  1.00 35.77  ? 116 LEU   C N   1 
ATOM   5603 C  CA  . LEU   C 1 111 ? -9.085  -25.165 20.590  1.00 35.81  ? 116 LEU   C CA  1 
ATOM   5604 C  C   . LEU   C 1 111 ? -9.606  -24.601 21.895  1.00 41.89  ? 116 LEU   C C   1 
ATOM   5605 O  O   . LEU   C 1 111 ? -10.295 -25.303 22.647  1.00 42.04  ? 116 LEU   C O   1 
ATOM   5606 C  CB  . LEU   C 1 111 ? -10.232 -25.279 19.577  1.00 35.71  ? 116 LEU   C CB  1 
ATOM   5607 C  CG  . LEU   C 1 111 ? -9.949  -26.023 18.264  1.00 39.39  ? 116 LEU   C CG  1 
ATOM   5608 C  CD1 . LEU   C 1 111 ? -11.193 -26.060 17.397  1.00 39.17  ? 116 LEU   C CD1 1 
ATOM   5609 C  CD2 . LEU   C 1 111 ? -8.748  -25.405 17.511  1.00 39.95  ? 116 LEU   C CD2 1 
ATOM   5610 N  N   . GLY   C 1 112 ? -9.239  -23.348 22.154  1.00 37.92  ? 117 GLY   C N   1 
ATOM   5611 C  CA  . GLY   C 1 112 ? -9.644  -22.605 23.339  1.00 36.77  ? 117 GLY   C CA  1 
ATOM   5612 C  C   . GLY   C 1 112 ? -10.835 -21.698 23.116  1.00 40.15  ? 117 GLY   C C   1 
ATOM   5613 O  O   . GLY   C 1 112 ? -11.221 -21.449 21.973  1.00 40.04  ? 117 GLY   C O   1 
ATOM   5614 N  N   . GLY   C 1 113 ? -11.434 -21.188 24.199  1.00 37.25  ? 118 GLY   C N   1 
ATOM   5615 C  CA  . GLY   C 1 113 ? -10.996 -21.413 25.576  1.00 36.32  ? 118 GLY   C CA  1 
ATOM   5616 C  C   . GLY   C 1 113 ? -9.909  -20.430 25.978  1.00 39.64  ? 118 GLY   C C   1 
ATOM   5617 O  O   . GLY   C 1 113 ? -9.202  -19.911 25.105  1.00 37.76  ? 118 GLY   C O   1 
ATOM   5618 N  N   . ASP   C 1 114 ? -9.769  -20.139 27.290  1.00 35.01  ? 119 ASP   C N   1 
ATOM   5619 C  CA  . ASP   C 1 114 ? -8.732  -19.207 27.743  1.00 34.19  ? 119 ASP   C CA  1 
ATOM   5620 C  C   . ASP   C 1 114 ? -7.397  -19.920 27.857  1.00 36.39  ? 119 ASP   C C   1 
ATOM   5621 O  O   . ASP   C 1 114 ? -7.378  -21.150 27.900  1.00 36.38  ? 119 ASP   C O   1 
ATOM   5622 C  CB  . ASP   C 1 114 ? -9.126  -18.523 29.063  1.00 35.39  ? 119 ASP   C CB  1 
ATOM   5623 C  CG  . ASP   C 1 114 ? -9.215  -19.469 30.232  1.00 39.98  ? 119 ASP   C CG  1 
ATOM   5624 O  OD1 . ASP   C 1 114 ? -8.158  -19.870 30.748  1.00 37.25  ? 119 ASP   C OD1 1 
ATOM   5625 O  OD2 . ASP   C 1 114 ? -10.341 -19.789 30.644  1.00 50.18  ? 119 ASP   C OD2 1 
ATOM   5626 N  N   . HIS   C 1 115 ? -6.281  -19.172 27.992  1.00 32.40  ? 120 HIS   C N   1 
ATOM   5627 C  CA  . HIS   C 1 115 ? -4.946  -19.768 28.014  1.00 32.65  ? 120 HIS   C CA  1 
ATOM   5628 C  C   . HIS   C 1 115 ? -4.626  -20.629 29.253  1.00 36.67  ? 120 HIS   C C   1 
ATOM   5629 O  O   . HIS   C 1 115 ? -3.574  -21.274 29.258  1.00 35.21  ? 120 HIS   C O   1 
ATOM   5630 C  CB  . HIS   C 1 115 ? -3.823  -18.718 27.774  1.00 33.43  ? 120 HIS   C CB  1 
ATOM   5631 C  CG  . HIS   C 1 115 ? -2.702  -19.232 26.910  1.00 35.71  ? 120 HIS   C CG  1 
ATOM   5632 N  ND1 . HIS   C 1 115 ? -1.872  -18.361 26.210  1.00 35.60  ? 120 HIS   C ND1 1 
ATOM   5633 C  CD2 . HIS   C 1 115 ? -2.343  -20.508 26.609  1.00 36.66  ? 120 HIS   C CD2 1 
ATOM   5634 C  CE1 . HIS   C 1 115 ? -1.052  -19.127 25.508  1.00 35.56  ? 120 HIS   C CE1 1 
ATOM   5635 N  NE2 . HIS   C 1 115 ? -1.288  -20.428 25.720  1.00 36.38  ? 120 HIS   C NE2 1 
ATOM   5636 N  N   . SER   C 1 116 ? -5.507  -20.689 30.292  1.00 35.45  ? 121 SER   C N   1 
ATOM   5637 C  CA  . SER   C 1 116 ? -5.156  -21.573 31.424  1.00 35.33  ? 121 SER   C CA  1 
ATOM   5638 C  C   . SER   C 1 116 ? -5.175  -23.045 30.974  1.00 39.45  ? 121 SER   C C   1 
ATOM   5639 O  O   . SER   C 1 116 ? -4.533  -23.867 31.617  1.00 38.75  ? 121 SER   C O   1 
ATOM   5640 C  CB  . SER   C 1 116 ? -6.097  -21.393 32.615  1.00 35.90  ? 121 SER   C CB  1 
ATOM   5641 O  OG  . SER   C 1 116 ? -7.378  -21.909 32.303  1.00 37.62  ? 121 SER   C OG  1 
ATOM   5642 N  N   . LEU   C 1 117 ? -5.862  -23.350 29.841  1.00 38.23  ? 122 LEU   C N   1 
ATOM   5643 C  CA  . LEU   C 1 117 ? -5.928  -24.708 29.290  1.00 38.63  ? 122 LEU   C CA  1 
ATOM   5644 C  C   . LEU   C 1 117 ? -4.556  -25.278 28.886  1.00 41.33  ? 122 LEU   C C   1 
ATOM   5645 O  O   . LEU   C 1 117 ? -4.427  -26.505 28.767  1.00 39.24  ? 122 LEU   C O   1 
ATOM   5646 C  CB  . LEU   C 1 117 ? -6.957  -24.852 28.164  1.00 39.67  ? 122 LEU   C CB  1 
ATOM   5647 C  CG  . LEU   C 1 117 ? -6.774  -24.118 26.842  1.00 47.46  ? 122 LEU   C CG  1 
ATOM   5648 C  CD1 . LEU   C 1 117 ? -5.880  -24.907 25.871  1.00 49.22  ? 122 LEU   C CD1 1 
ATOM   5649 C  CD2 . LEU   C 1 117 ? -8.123  -23.929 26.188  1.00 51.94  ? 122 LEU   C CD2 1 
ATOM   5650 N  N   . ALA   C 1 118 ? -3.520  -24.412 28.736  1.00 37.06  ? 123 ALA   C N   1 
ATOM   5651 C  CA  . ALA   C 1 118 ? -2.164  -24.868 28.443  1.00 37.78  ? 123 ALA   C CA  1 
ATOM   5652 C  C   . ALA   C 1 118 ? -1.637  -25.718 29.597  1.00 38.93  ? 123 ALA   C C   1 
ATOM   5653 O  O   . ALA   C 1 118 ? -0.761  -26.560 29.392  1.00 36.49  ? 123 ALA   C O   1 
ATOM   5654 C  CB  . ALA   C 1 118 ? -1.235  -23.695 28.185  1.00 38.69  ? 123 ALA   C CB  1 
ATOM   5655 N  N   . ILE   C 1 119 ? -2.200  -25.541 30.810  1.00 35.53  ? 124 ILE   C N   1 
ATOM   5656 C  CA  . ILE   C 1 119 ? -1.791  -26.371 31.936  1.00 34.65  ? 124 ILE   C CA  1 
ATOM   5657 C  C   . ILE   C 1 119 ? -2.094  -27.839 31.581  1.00 35.24  ? 124 ILE   C C   1 
ATOM   5658 O  O   . ILE   C 1 119 ? -1.227  -28.675 31.737  1.00 35.30  ? 124 ILE   C O   1 
ATOM   5659 C  CB  . ILE   C 1 119 ? -2.437  -25.933 33.286  1.00 37.59  ? 124 ILE   C CB  1 
ATOM   5660 C  CG1 . ILE   C 1 119 ? -2.042  -24.480 33.652  1.00 38.02  ? 124 ILE   C CG1 1 
ATOM   5661 C  CG2 . ILE   C 1 119 ? -2.037  -26.899 34.425  1.00 37.98  ? 124 ILE   C CG2 1 
ATOM   5662 C  CD1 . ILE   C 1 119 ? -2.970  -23.804 34.673  1.00 44.58  ? 124 ILE   C CD1 1 
ATOM   5663 N  N   . GLY   C 1 120 ? -3.300  -28.092 31.080  1.00 33.62  ? 125 GLY   C N   1 
ATOM   5664 C  CA  . GLY   C 1 120 ? -3.786  -29.415 30.688  1.00 34.44  ? 125 GLY   C CA  1 
ATOM   5665 C  C   . GLY   C 1 120 ? -3.082  -29.978 29.469  1.00 40.76  ? 125 GLY   C C   1 
ATOM   5666 O  O   . GLY   C 1 120 ? -2.517  -31.080 29.529  1.00 39.94  ? 125 GLY   C O   1 
ATOM   5667 N  N   . THR   C 1 121 ? -3.043  -29.189 28.374  1.00 37.32  ? 126 THR   C N   1 
ATOM   5668 C  CA  . THR   C 1 121 ? -2.402  -29.629 27.115  1.00 35.45  ? 126 THR   C CA  1 
ATOM   5669 C  C   . THR   C 1 121 ? -0.925  -29.935 27.271  1.00 36.57  ? 126 THR   C C   1 
ATOM   5670 O  O   . THR   C 1 121 ? -0.465  -30.963 26.758  1.00 36.87  ? 126 THR   C O   1 
ATOM   5671 C  CB  . THR   C 1 121 ? -2.649  -28.636 25.980  1.00 37.36  ? 126 THR   C CB  1 
ATOM   5672 O  OG1 . THR   C 1 121 ? -1.904  -27.442 26.218  1.00 38.89  ? 126 THR   C OG1 1 
ATOM   5673 C  CG2 . THR   C 1 121 ? -4.102  -28.323 25.796  1.00 33.83  ? 126 THR   C CG2 1 
ATOM   5674 N  N   . ILE   C 1 122 ? -0.176  -29.065 27.976  1.00 30.97  ? 127 ILE   C N   1 
ATOM   5675 C  CA  . ILE   C 1 122 ? 1.261   -29.270 28.157  1.00 31.18  ? 127 ILE   C CA  1 
ATOM   5676 C  C   . ILE   C 1 122 ? 1.517   -30.468 29.094  1.00 38.09  ? 127 ILE   C C   1 
ATOM   5677 O  O   . ILE   C 1 122 ? 2.417   -31.279 28.822  1.00 37.60  ? 127 ILE   C O   1 
ATOM   5678 C  CB  . ILE   C 1 122 ? 2.048   -27.989 28.549  1.00 33.84  ? 127 ILE   C CB  1 
ATOM   5679 C  CG1 . ILE   C 1 122 ? 1.943   -26.923 27.403  1.00 34.40  ? 127 ILE   C CG1 1 
ATOM   5680 C  CG2 . ILE   C 1 122 ? 3.523   -28.294 28.864  1.00 34.24  ? 127 ILE   C CG2 1 
ATOM   5681 C  CD1 . ILE   C 1 122 ? 2.751   -25.546 27.631  1.00 36.28  ? 127 ILE   C CD1 1 
ATOM   5682 N  N   . SER   C 1 123 ? 0.743   -30.561 30.196  1.00 36.06  ? 128 SER   C N   1 
ATOM   5683 C  CA  . SER   C 1 123 ? 0.892   -31.670 31.147  1.00 36.43  ? 128 SER   C CA  1 
ATOM   5684 C  C   . SER   C 1 123 ? 0.680   -33.025 30.494  1.00 41.22  ? 128 SER   C C   1 
ATOM   5685 O  O   . SER   C 1 123 ? 1.532   -33.896 30.647  1.00 42.92  ? 128 SER   C O   1 
ATOM   5686 C  CB  . SER   C 1 123 ? -0.029  -31.492 32.348  1.00 38.51  ? 128 SER   C CB  1 
ATOM   5687 O  OG  . SER   C 1 123 ? 0.408   -30.376 33.100  1.00 43.72  ? 128 SER   C OG  1 
ATOM   5688 N  N   . GLY   C 1 124 ? -0.406  -33.160 29.729  1.00 39.13  ? 129 GLY   C N   1 
ATOM   5689 C  CA  . GLY   C 1 124 ? -0.751  -34.373 28.993  1.00 38.94  ? 129 GLY   C CA  1 
ATOM   5690 C  C   . GLY   C 1 124 ? 0.306   -34.777 27.982  1.00 43.15  ? 129 GLY   C C   1 
ATOM   5691 O  O   . GLY   C 1 124 ? 0.723   -35.937 27.937  1.00 41.68  ? 129 GLY   C O   1 
ATOM   5692 N  N   . HIS   C 1 125 ? 0.791   -33.799 27.207  1.00 39.66  ? 130 HIS   C N   1 
ATOM   5693 C  CA  . HIS   C 1 125 ? 1.830   -33.975 26.194  1.00 39.13  ? 130 HIS   C CA  1 
ATOM   5694 C  C   . HIS   C 1 125 ? 3.167   -34.440 26.793  1.00 42.24  ? 130 HIS   C C   1 
ATOM   5695 O  O   . HIS   C 1 125 ? 3.791   -35.347 26.244  1.00 43.15  ? 130 HIS   C O   1 
ATOM   5696 C  CB  . HIS   C 1 125 ? 2.005   -32.631 25.447  1.00 40.49  ? 130 HIS   C CB  1 
ATOM   5697 C  CG  . HIS   C 1 125 ? 2.809   -32.680 24.185  1.00 44.25  ? 130 HIS   C CG  1 
ATOM   5698 N  ND1 . HIS   C 1 125 ? 3.225   -31.513 23.559  1.00 46.27  ? 130 HIS   C ND1 1 
ATOM   5699 C  CD2 . HIS   C 1 125 ? 3.245   -33.740 23.466  1.00 45.79  ? 130 HIS   C CD2 1 
ATOM   5700 C  CE1 . HIS   C 1 125 ? 3.913   -31.899 22.499  1.00 45.59  ? 130 HIS   C CE1 1 
ATOM   5701 N  NE2 . HIS   C 1 125 ? 3.950   -33.231 22.400  1.00 45.79  ? 130 HIS   C NE2 1 
ATOM   5702 N  N   . ALA   C 1 126 ? 3.603   -33.838 27.920  1.00 37.08  ? 131 ALA   C N   1 
ATOM   5703 C  CA  . ALA   C 1 126 ? 4.885   -34.140 28.580  1.00 36.68  ? 131 ALA   C CA  1 
ATOM   5704 C  C   . ALA   C 1 126 ? 4.964   -35.553 29.204  1.00 41.48  ? 131 ALA   C C   1 
ATOM   5705 O  O   . ALA   C 1 126 ? 6.067   -36.044 29.448  1.00 41.24  ? 131 ALA   C O   1 
ATOM   5706 C  CB  . ALA   C 1 126 ? 5.207   -33.089 29.625  1.00 37.21  ? 131 ALA   C CB  1 
ATOM   5707 N  N   . ARG   C 1 127 ? 3.802   -36.177 29.463  1.00 40.38  ? 132 ARG   C N   1 
ATOM   5708 C  CA  . ARG   C 1 127 ? 3.705   -37.551 30.002  1.00 42.00  ? 132 ARG   C CA  1 
ATOM   5709 C  C   . ARG   C 1 127 ? 4.354   -38.555 29.019  1.00 49.02  ? 132 ARG   C C   1 
ATOM   5710 O  O   . ARG   C 1 127 ? 5.110   -39.428 29.451  1.00 48.98  ? 132 ARG   C O   1 
ATOM   5711 C  CB  . ARG   C 1 127 ? 2.242   -37.933 30.276  1.00 41.14  ? 132 ARG   C CB  1 
ATOM   5712 C  CG  . ARG   C 1 127 ? 1.685   -37.322 31.564  1.00 48.62  ? 132 ARG   C CG  1 
ATOM   5713 C  CD  . ARG   C 1 127 ? 0.178   -37.461 31.627  1.00 52.57  ? 132 ARG   C CD  1 
ATOM   5714 N  NE  . ARG   C 1 127 ? -0.394  -36.680 32.723  1.00 62.15  ? 132 ARG   C NE  1 
ATOM   5715 C  CZ  . ARG   C 1 127 ? -1.697  -36.512 32.921  1.00 76.15  ? 132 ARG   C CZ  1 
ATOM   5716 N  NH1 . ARG   C 1 127 ? -2.578  -37.073 32.101  1.00 62.46  ? 132 ARG   C NH1 1 
ATOM   5717 N  NH2 . ARG   C 1 127 ? -2.130  -35.778 33.937  1.00 66.16  ? 132 ARG   C NH2 1 
ATOM   5718 N  N   . HIS   C 1 128 ? 4.108   -38.378 27.701  1.00 47.38  ? 133 HIS   C N   1 
ATOM   5719 C  CA  . HIS   C 1 128 ? 4.688   -39.211 26.636  1.00 47.76  ? 133 HIS   C CA  1 
ATOM   5720 C  C   . HIS   C 1 128 ? 5.938   -38.565 26.003  1.00 49.43  ? 133 HIS   C C   1 
ATOM   5721 O  O   . HIS   C 1 128 ? 6.789   -39.286 25.480  1.00 47.30  ? 133 HIS   C O   1 
ATOM   5722 C  CB  . HIS   C 1 128 ? 3.638   -39.557 25.572  1.00 49.92  ? 133 HIS   C CB  1 
ATOM   5723 C  CG  . HIS   C 1 128 ? 2.413   -40.224 26.125  1.00 54.65  ? 133 HIS   C CG  1 
ATOM   5724 N  ND1 . HIS   C 1 128 ? 2.504   -41.275 27.033  1.00 56.82  ? 133 HIS   C ND1 1 
ATOM   5725 C  CD2 . HIS   C 1 128 ? 1.105   -39.963 25.886  1.00 57.17  ? 133 HIS   C CD2 1 
ATOM   5726 C  CE1 . HIS   C 1 128 ? 1.255   -41.607 27.319  1.00 56.72  ? 133 HIS   C CE1 1 
ATOM   5727 N  NE2 . HIS   C 1 128 ? 0.378   -40.853 26.644  1.00 57.15  ? 133 HIS   C NE2 1 
ATOM   5728 N  N   . CYS   C 1 129 ? 6.065   -37.209 26.084  1.00 44.63  ? 134 CYS   C N   1 
ATOM   5729 C  CA  . CYS   C 1 129 ? 7.208   -36.461 25.539  1.00 42.93  ? 134 CYS   C CA  1 
ATOM   5730 C  C   . CYS   C 1 129 ? 7.981   -35.661 26.603  1.00 47.55  ? 134 CYS   C C   1 
ATOM   5731 O  O   . CYS   C 1 129 ? 7.897   -34.431 26.589  1.00 46.53  ? 134 CYS   C O   1 
ATOM   5732 C  CB  . CYS   C 1 129 ? 6.764   -35.569 24.380  1.00 41.88  ? 134 CYS   C CB  1 
ATOM   5733 S  SG  . CYS   C 1 129 ? 6.072   -36.463 22.978  1.00 44.87  ? 134 CYS   C SG  1 
ATOM   5734 N  N   . PRO   C 1 130 ? 8.761   -36.300 27.514  1.00 44.43  ? 135 PRO   C N   1 
ATOM   5735 C  CA  . PRO   C 1 130 ? 9.475   -35.518 28.542  1.00 43.79  ? 135 PRO   C CA  1 
ATOM   5736 C  C   . PRO   C 1 130 ? 10.518  -34.528 28.028  1.00 46.33  ? 135 PRO   C C   1 
ATOM   5737 O  O   . PRO   C 1 130 ? 10.814  -33.570 28.739  1.00 45.88  ? 135 PRO   C O   1 
ATOM   5738 C  CB  . PRO   C 1 130 ? 10.111  -36.595 29.437  1.00 45.84  ? 135 PRO   C CB  1 
ATOM   5739 C  CG  . PRO   C 1 130 ? 10.205  -37.807 28.564  1.00 50.05  ? 135 PRO   C CG  1 
ATOM   5740 C  CD  . PRO   C 1 130 ? 8.973   -37.752 27.713  1.00 45.70  ? 135 PRO   C CD  1 
ATOM   5741 N  N   . ASP   C 1 131 ? 11.084  -34.749 26.815  1.00 40.52  ? 136 ASP   C N   1 
ATOM   5742 C  CA  . ASP   C 1 131 ? 12.079  -33.839 26.249  1.00 39.39  ? 136 ASP   C CA  1 
ATOM   5743 C  C   . ASP   C 1 131 ? 11.418  -32.746 25.383  1.00 40.58  ? 136 ASP   C C   1 
ATOM   5744 O  O   . ASP   C 1 131 ? 12.129  -32.080 24.629  1.00 39.28  ? 136 ASP   C O   1 
ATOM   5745 C  CB  . ASP   C 1 131 ? 13.154  -34.613 25.452  1.00 40.74  ? 136 ASP   C CB  1 
ATOM   5746 C  CG  . ASP   C 1 131 ? 14.465  -33.882 25.200  1.00 43.37  ? 136 ASP   C CG  1 
ATOM   5747 O  OD1 . ASP   C 1 131 ? 14.856  -33.040 26.041  1.00 43.82  ? 136 ASP   C OD1 1 
ATOM   5748 O  OD2 . ASP   C 1 131 ? 15.110  -34.162 24.163  1.00 44.58  ? 136 ASP   C OD2 1 
ATOM   5749 N  N   . LEU   C 1 132 ? 10.075  -32.557 25.490  1.00 36.57  ? 137 LEU   C N   1 
ATOM   5750 C  CA  . LEU   C 1 132 ? 9.382   -31.530 24.697  1.00 36.27  ? 137 LEU   C CA  1 
ATOM   5751 C  C   . LEU   C 1 132 ? 9.928   -30.125 24.960  1.00 40.62  ? 137 LEU   C C   1 
ATOM   5752 O  O   . LEU   C 1 132 ? 10.536  -29.846 26.003  1.00 38.01  ? 137 LEU   C O   1 
ATOM   5753 C  CB  . LEU   C 1 132 ? 7.821   -31.568 24.796  1.00 36.21  ? 137 LEU   C CB  1 
ATOM   5754 C  CG  . LEU   C 1 132 ? 7.081   -31.093 26.095  1.00 40.96  ? 137 LEU   C CG  1 
ATOM   5755 C  CD1 . LEU   C 1 132 ? 7.118   -29.607 26.242  1.00 41.67  ? 137 LEU   C CD1 1 
ATOM   5756 C  CD2 . LEU   C 1 132 ? 5.605   -31.397 26.019  1.00 40.78  ? 137 LEU   C CD2 1 
ATOM   5757 N  N   . CYS   C 1 133 ? 9.752   -29.255 23.962  1.00 36.18  ? 138 CYS   C N   1 
ATOM   5758 C  CA  . CYS   C 1 133 ? 10.112  -27.857 24.104  1.00 34.48  ? 138 CYS   C CA  1 
ATOM   5759 C  C   . CYS   C 1 133 ? 8.893   -27.047 23.728  1.00 33.30  ? 138 CYS   C C   1 
ATOM   5760 O  O   . CYS   C 1 133 ? 7.982   -27.551 23.051  1.00 31.24  ? 138 CYS   C O   1 
ATOM   5761 C  CB  . CYS   C 1 133 ? 11.346  -27.488 23.292  1.00 34.59  ? 138 CYS   C CB  1 
ATOM   5762 S  SG  . CYS   C 1 133 ? 11.147  -27.714 21.508  1.00 37.72  ? 138 CYS   C SG  1 
ATOM   5763 N  N   . VAL   C 1 134 ? 8.794   -25.827 24.282  1.00 29.94  ? 139 VAL   C N   1 
ATOM   5764 C  CA  . VAL   C 1 134 ? 7.597   -25.019 24.084  1.00 28.96  ? 139 VAL   C CA  1 
ATOM   5765 C  C   . VAL   C 1 134 ? 7.906   -23.713 23.385  1.00 30.49  ? 139 VAL   C C   1 
ATOM   5766 O  O   . VAL   C 1 134 ? 8.832   -23.013 23.787  1.00 32.21  ? 139 VAL   C O   1 
ATOM   5767 C  CB  . VAL   C 1 134 ? 6.828   -24.749 25.420  1.00 32.78  ? 139 VAL   C CB  1 
ATOM   5768 C  CG1 . VAL   C 1 134 ? 5.506   -24.021 25.170  1.00 32.77  ? 139 VAL   C CG1 1 
ATOM   5769 C  CG2 . VAL   C 1 134 ? 6.557   -26.052 26.180  1.00 32.32  ? 139 VAL   C CG2 1 
ATOM   5770 N  N   . VAL   C 1 135 ? 7.109   -23.406 22.365  1.00 29.47  ? 140 VAL   C N   1 
ATOM   5771 C  CA  . VAL   C 1 135 ? 7.122   -22.116 21.669  1.00 28.03  ? 140 VAL   C CA  1 
ATOM   5772 C  C   . VAL   C 1 135 ? 5.808   -21.458 22.056  1.00 28.19  ? 140 VAL   C C   1 
ATOM   5773 O  O   . VAL   C 1 135 ? 4.723   -21.891 21.650  1.00 28.06  ? 140 VAL   C O   1 
ATOM   5774 C  CB  . VAL   C 1 135 ? 7.333   -22.211 20.139  1.00 30.03  ? 140 VAL   C CB  1 
ATOM   5775 C  CG1 . VAL   C 1 135 ? 7.324   -20.805 19.510  1.00 30.21  ? 140 VAL   C CG1 1 
ATOM   5776 C  CG2 . VAL   C 1 135 ? 8.641   -22.923 19.819  1.00 29.71  ? 140 VAL   C CG2 1 
ATOM   5777 N  N   . TRP   C 1 136 ? 5.912   -20.405 22.901  1.00 26.70  ? 141 TRP   C N   1 
ATOM   5778 C  CA  . TRP   C 1 136 ? 4.751   -19.708 23.434  1.00 27.66  ? 141 TRP   C CA  1 
ATOM   5779 C  C   . TRP   C 1 136 ? 4.580   -18.388 22.701  1.00 28.78  ? 141 TRP   C C   1 
ATOM   5780 O  O   . TRP   C 1 136 ? 5.414   -17.508 22.868  1.00 27.67  ? 141 TRP   C O   1 
ATOM   5781 C  CB  . TRP   C 1 136 ? 4.959   -19.481 24.933  1.00 27.79  ? 141 TRP   C CB  1 
ATOM   5782 C  CG  . TRP   C 1 136 ? 3.724   -19.081 25.663  1.00 29.38  ? 141 TRP   C CG  1 
ATOM   5783 C  CD1 . TRP   C 1 136 ? 3.163   -17.837 25.717  1.00 32.09  ? 141 TRP   C CD1 1 
ATOM   5784 C  CD2 . TRP   C 1 136 ? 2.940   -19.915 26.529  1.00 29.87  ? 141 TRP   C CD2 1 
ATOM   5785 N  NE1 . TRP   C 1 136 ? 2.073   -17.844 26.559  1.00 32.15  ? 141 TRP   C NE1 1 
ATOM   5786 C  CE2 . TRP   C 1 136 ? 1.915   -19.108 27.075  1.00 33.48  ? 141 TRP   C CE2 1 
ATOM   5787 C  CE3 . TRP   C 1 136 ? 3.002   -21.271 26.893  1.00 31.83  ? 141 TRP   C CE3 1 
ATOM   5788 C  CZ2 . TRP   C 1 136 ? 0.968   -19.608 27.983  1.00 32.86  ? 141 TRP   C CZ2 1 
ATOM   5789 C  CZ3 . TRP   C 1 136 ? 2.046   -21.769 27.770  1.00 33.18  ? 141 TRP   C CZ3 1 
ATOM   5790 C  CH2 . TRP   C 1 136 ? 1.037   -20.946 28.294  1.00 33.66  ? 141 TRP   C CH2 1 
ATOM   5791 N  N   . VAL   C 1 137 ? 3.536   -18.292 21.865  1.00 25.81  ? 142 VAL   C N   1 
ATOM   5792 C  CA  . VAL   C 1 137 ? 3.290   -17.114 21.012  1.00 25.00  ? 142 VAL   C CA  1 
ATOM   5793 C  C   . VAL   C 1 137 ? 2.169   -16.303 21.611  1.00 26.93  ? 142 VAL   C C   1 
ATOM   5794 O  O   . VAL   C 1 137 ? 1.000   -16.714 21.623  1.00 26.20  ? 142 VAL   C O   1 
ATOM   5795 C  CB  . VAL   C 1 137 ? 3.108   -17.486 19.516  1.00 28.21  ? 142 VAL   C CB  1 
ATOM   5796 C  CG1 . VAL   C 1 137 ? 2.999   -16.215 18.665  1.00 28.49  ? 142 VAL   C CG1 1 
ATOM   5797 C  CG2 . VAL   C 1 137 ? 4.284   -18.346 19.030  1.00 27.50  ? 142 VAL   C CG2 1 
ATOM   5798 N  N   . ASP   C 1 138 ? 2.525   -15.108 22.119  1.00 25.10  ? 143 ASP   C N   1 
ATOM   5799 C  CA  . ASP   C 1 138 ? 1.565   -14.341 22.889  1.00 24.41  ? 143 ASP   C CA  1 
ATOM   5800 C  C   . ASP   C 1 138 ? 2.071   -12.921 23.135  1.00 26.94  ? 143 ASP   C C   1 
ATOM   5801 O  O   . ASP   C 1 138 ? 3.278   -12.673 23.159  1.00 25.78  ? 143 ASP   C O   1 
ATOM   5802 C  CB  . ASP   C 1 138 ? 1.520   -15.063 24.255  1.00 25.48  ? 143 ASP   C CB  1 
ATOM   5803 C  CG  . ASP   C 1 138 ? 0.316   -14.855 25.149  1.00 30.66  ? 143 ASP   C CG  1 
ATOM   5804 O  OD1 . ASP   C 1 138 ? -0.213  -13.738 25.180  1.00 30.33  ? 143 ASP   C OD1 1 
ATOM   5805 O  OD2 . ASP   C 1 138 ? -0.072  -15.817 25.838  1.00 34.16  ? 143 ASP   C OD2 1 
ATOM   5806 N  N   . ALA   C 1 139 ? 1.146   -12.011 23.382  1.00 25.58  ? 144 ALA   C N   1 
ATOM   5807 C  CA  . ALA   C 1 139 ? 1.489   -10.630 23.786  1.00 25.35  ? 144 ALA   C CA  1 
ATOM   5808 C  C   . ALA   C 1 139 ? 1.986   -10.642 25.259  1.00 29.55  ? 144 ALA   C C   1 
ATOM   5809 O  O   . ALA   C 1 139 ? 2.709   -9.743  25.718  1.00 26.97  ? 144 ALA   C O   1 
ATOM   5810 C  CB  . ALA   C 1 139 ? 0.250   -9.768  23.682  1.00 25.69  ? 144 ALA   C CB  1 
ATOM   5811 N  N   . HIS   C 1 140 ? 1.612   -11.717 25.971  1.00 27.01  ? 145 HIS   C N   1 
ATOM   5812 C  CA  . HIS   C 1 140 ? 1.815   -11.908 27.406  1.00 27.54  ? 145 HIS   C CA  1 
ATOM   5813 C  C   . HIS   C 1 140 ? 2.666   -13.100 27.749  1.00 31.61  ? 145 HIS   C C   1 
ATOM   5814 O  O   . HIS   C 1 140 ? 2.696   -14.075 26.992  1.00 29.77  ? 145 HIS   C O   1 
ATOM   5815 C  CB  . HIS   C 1 140 ? 0.440   -12.047 28.070  1.00 27.23  ? 145 HIS   C CB  1 
ATOM   5816 C  CG  . HIS   C 1 140 ? -0.501  -10.947 27.716  1.00 29.04  ? 145 HIS   C CG  1 
ATOM   5817 N  ND1 . HIS   C 1 140 ? -1.512  -11.131 26.794  1.00 29.70  ? 145 HIS   C ND1 1 
ATOM   5818 C  CD2 . HIS   C 1 140 ? -0.503  -9.652  28.120  1.00 29.86  ? 145 HIS   C CD2 1 
ATOM   5819 C  CE1 . HIS   C 1 140 ? -2.112  -9.960  26.691  1.00 30.00  ? 145 HIS   C CE1 1 
ATOM   5820 N  NE2 . HIS   C 1 140 ? -1.534  -9.041  27.470  1.00 30.09  ? 145 HIS   C NE2 1 
ATOM   5821 N  N   . ALA   C 1 141 ? 3.395   -13.022 28.876  1.00 28.45  ? 146 ALA   C N   1 
ATOM   5822 C  CA  . ALA   C 1 141 ? 4.232   -14.140 29.304  1.00 28.56  ? 146 ALA   C CA  1 
ATOM   5823 C  C   . ALA   C 1 141 ? 3.459   -15.174 30.124  1.00 32.97  ? 146 ALA   C C   1 
ATOM   5824 O  O   . ALA   C 1 141 ? 3.960   -16.288 30.275  1.00 31.78  ? 146 ALA   C O   1 
ATOM   5825 C  CB  . ALA   C 1 141 ? 5.471   -13.658 30.038  1.00 29.36  ? 146 ALA   C CB  1 
ATOM   5826 N  N   . ASP   C 1 142 ? 2.225   -14.831 30.627  1.00 30.79  ? 147 ASP   C N   1 
ATOM   5827 C  CA  . ASP   C 1 142 ? 1.354   -15.771 31.358  1.00 31.65  ? 147 ASP   C CA  1 
ATOM   5828 C  C   . ASP   C 1 142 ? 2.182   -16.542 32.424  1.00 35.34  ? 147 ASP   C C   1 
ATOM   5829 O  O   . ASP   C 1 142 ? 2.010   -17.755 32.603  1.00 35.37  ? 147 ASP   C O   1 
ATOM   5830 C  CB  . ASP   C 1 142 ? 0.690   -16.746 30.351  1.00 30.79  ? 147 ASP   C CB  1 
ATOM   5831 C  CG  . ASP   C 1 142 ? -0.214  -16.064 29.342  1.00 34.83  ? 147 ASP   C CG  1 
ATOM   5832 O  OD1 . ASP   C 1 142 ? -0.475  -14.842 29.505  1.00 33.58  ? 147 ASP   C OD1 1 
ATOM   5833 O  OD2 . ASP   C 1 142 ? -0.709  -16.755 28.409  1.00 37.20  ? 147 ASP   C OD2 1 
ATOM   5834 N  N   . ILE   C 1 143 ? 3.103   -15.825 33.095  1.00 32.07  ? 148 ILE   C N   1 
ATOM   5835 C  CA  . ILE   C 1 143 ? 4.022   -16.434 34.025  1.00 31.68  ? 148 ILE   C CA  1 
ATOM   5836 C  C   . ILE   C 1 143 ? 3.881   -15.828 35.453  1.00 36.10  ? 148 ILE   C C   1 
ATOM   5837 O  O   . ILE   C 1 143 ? 4.769   -16.018 36.283  1.00 35.61  ? 148 ILE   C O   1 
ATOM   5838 C  CB  . ILE   C 1 143 ? 5.466   -16.449 33.460  1.00 35.51  ? 148 ILE   C CB  1 
ATOM   5839 C  CG1 . ILE   C 1 143 ? 6.324   -17.554 34.127  1.00 35.93  ? 148 ILE   C CG1 1 
ATOM   5840 C  CG2 . ILE   C 1 143 ? 6.160   -15.077 33.478  1.00 35.69  ? 148 ILE   C CG2 1 
ATOM   5841 C  CD1 . ILE   C 1 143 ? 7.517   -17.993 33.359  1.00 40.11  ? 148 ILE   C CD1 1 
ATOM   5842 N  N   . ASN   C 1 144 ? 2.736   -15.183 35.747  1.00 32.28  ? 149 ASN   C N   1 
ATOM   5843 C  CA  . ASN   C 1 144 ? 2.511   -14.699 37.125  1.00 33.73  ? 149 ASN   C CA  1 
ATOM   5844 C  C   . ASN   C 1 144 ? 2.345   -15.941 38.002  1.00 39.95  ? 149 ASN   C C   1 
ATOM   5845 O  O   . ASN   C 1 144 ? 1.855   -16.958 37.519  1.00 38.46  ? 149 ASN   C O   1 
ATOM   5846 C  CB  . ASN   C 1 144 ? 1.236   -13.855 37.221  1.00 34.09  ? 149 ASN   C CB  1 
ATOM   5847 C  CG  . ASN   C 1 144 ? 1.458   -12.383 36.975  1.00 44.35  ? 149 ASN   C CG  1 
ATOM   5848 O  OD1 . ASN   C 1 144 ? 2.308   -11.747 37.605  1.00 34.87  ? 149 ASN   C OD1 1 
ATOM   5849 N  ND2 . ASN   C 1 144 ? 0.698   -11.818 36.046  1.00 36.69  ? 149 ASN   C ND2 1 
ATOM   5850 N  N   . THR   C 1 145 ? 2.802   -15.875 39.257  1.00 38.58  ? 150 THR   C N   1 
ATOM   5851 C  CA  . THR   C 1 145 ? 2.597   -16.976 40.208  1.00 39.34  ? 150 THR   C CA  1 
ATOM   5852 C  C   . THR   C 1 145 ? 1.266   -16.641 40.922  1.00 43.90  ? 150 THR   C C   1 
ATOM   5853 O  O   . THR   C 1 145 ? 0.846   -15.482 40.850  1.00 42.50  ? 150 THR   C O   1 
ATOM   5854 C  CB  . THR   C 1 145 ? 3.759   -17.071 41.221  1.00 45.59  ? 150 THR   C CB  1 
ATOM   5855 O  OG1 . THR   C 1 145 ? 3.709   -15.939 42.089  1.00 41.82  ? 150 THR   C OG1 1 
ATOM   5856 C  CG2 . THR   C 1 145 ? 5.136   -17.215 40.561  1.00 42.77  ? 150 THR   C CG2 1 
ATOM   5857 N  N   . PRO   C 1 146 ? 0.607   -17.571 41.660  1.00 43.20  ? 151 PRO   C N   1 
ATOM   5858 C  CA  . PRO   C 1 146 ? -0.634  -17.198 42.383  1.00 43.50  ? 151 PRO   C CA  1 
ATOM   5859 C  C   . PRO   C 1 146 ? -0.455  -16.087 43.436  1.00 46.38  ? 151 PRO   C C   1 
ATOM   5860 O  O   . PRO   C 1 146 ? -1.440  -15.501 43.895  1.00 45.46  ? 151 PRO   C O   1 
ATOM   5861 C  CB  . PRO   C 1 146 ? -1.075  -18.518 43.029  1.00 45.67  ? 151 PRO   C CB  1 
ATOM   5862 C  CG  . PRO   C 1 146 ? -0.429  -19.584 42.183  1.00 50.42  ? 151 PRO   C CG  1 
ATOM   5863 C  CD  . PRO   C 1 146 ? 0.914   -19.000 41.850  1.00 45.76  ? 151 PRO   C CD  1 
ATOM   5864 N  N   . LEU   C 1 147 ? 0.803   -15.795 43.802  1.00 42.45  ? 152 LEU   C N   1 
ATOM   5865 C  CA  . LEU   C 1 147 ? 1.149   -14.745 44.759  1.00 42.37  ? 152 LEU   C CA  1 
ATOM   5866 C  C   . LEU   C 1 147 ? 1.468   -13.400 44.068  1.00 44.81  ? 152 LEU   C C   1 
ATOM   5867 O  O   . LEU   C 1 147 ? 1.285   -12.357 44.707  1.00 43.97  ? 152 LEU   C O   1 
ATOM   5868 C  CB  . LEU   C 1 147 ? 2.307   -15.181 45.688  1.00 42.82  ? 152 LEU   C CB  1 
ATOM   5869 C  CG  . LEU   C 1 147 ? 2.073   -16.422 46.584  1.00 47.60  ? 152 LEU   C CG  1 
ATOM   5870 C  CD1 . LEU   C 1 147 ? 3.361   -16.892 47.216  1.00 47.22  ? 152 LEU   C CD1 1 
ATOM   5871 C  CD2 . LEU   C 1 147 ? 1.024   -16.163 47.644  1.00 50.72  ? 152 LEU   C CD2 1 
ATOM   5872 N  N   . THR   C 1 148 ? 1.908   -13.410 42.766  1.00 39.07  ? 153 THR   C N   1 
ATOM   5873 C  CA  . THR   C 1 148 ? 2.246   -12.166 42.027  1.00 37.72  ? 153 THR   C CA  1 
ATOM   5874 C  C   . THR   C 1 148 ? 1.068   -11.574 41.248  1.00 40.40  ? 153 THR   C C   1 
ATOM   5875 O  O   . THR   C 1 148 ? 1.084   -10.385 40.937  1.00 40.96  ? 153 THR   C O   1 
ATOM   5876 C  CB  . THR   C 1 148 ? 3.480   -12.306 41.121  1.00 44.38  ? 153 THR   C CB  1 
ATOM   5877 O  OG1 . THR   C 1 148 ? 3.209   -13.173 40.025  1.00 40.63  ? 153 THR   C OG1 1 
ATOM   5878 C  CG2 . THR   C 1 148 ? 4.733   -12.731 41.861  1.00 41.99  ? 153 THR   C CG2 1 
ATOM   5879 N  N   . THR   C 1 149 ? 0.064   -12.387 40.921  1.00 36.64  ? 154 THR   C N   1 
ATOM   5880 C  CA  . THR   C 1 149 ? -1.122  -11.949 40.187  1.00 37.60  ? 154 THR   C CA  1 
ATOM   5881 C  C   . THR   C 1 149 ? -1.879  -10.830 40.918  1.00 46.12  ? 154 THR   C C   1 
ATOM   5882 O  O   . THR   C 1 149 ? -1.992  -10.859 42.146  1.00 45.55  ? 154 THR   C O   1 
ATOM   5883 C  CB  . THR   C 1 149 ? -2.011  -13.146 39.841  1.00 40.96  ? 154 THR   C CB  1 
ATOM   5884 O  OG1 . THR   C 1 149 ? -3.166  -12.694 39.125  1.00 38.05  ? 154 THR   C OG1 1 
ATOM   5885 C  CG2 . THR   C 1 149 ? -2.438  -13.936 41.072  1.00 41.67  ? 154 THR   C CG2 1 
ATOM   5886 N  N   . SER   C 1 150 ? -2.375  -9.847  40.157  1.00 44.61  ? 155 SER   C N   1 
ATOM   5887 C  CA  . SER   C 1 150 ? -3.153  -8.726  40.683  1.00 45.63  ? 155 SER   C CA  1 
ATOM   5888 C  C   . SER   C 1 150 ? -4.616  -8.964  40.337  1.00 50.52  ? 155 SER   C C   1 
ATOM   5889 O  O   . SER   C 1 150 ? -5.508  -8.572  41.095  1.00 51.21  ? 155 SER   C O   1 
ATOM   5890 C  CB  . SER   C 1 150 ? -2.678  -7.412  40.066  1.00 50.17  ? 155 SER   C CB  1 
ATOM   5891 O  OG  . SER   C 1 150 ? -1.299  -7.193  40.320  1.00 58.05  ? 155 SER   C OG  1 
ATOM   5892 N  N   . SER   C 1 151 ? -4.857  -9.652  39.209  1.00 45.24  ? 156 SER   C N   1 
ATOM   5893 C  CA  . SER   C 1 151 ? -6.195  -9.937  38.712  1.00 44.04  ? 156 SER   C CA  1 
ATOM   5894 C  C   . SER   C 1 151 ? -6.818  -11.196 39.319  1.00 46.88  ? 156 SER   C C   1 
ATOM   5895 O  O   . SER   C 1 151 ? -8.041  -11.323 39.318  1.00 46.83  ? 156 SER   C O   1 
ATOM   5896 C  CB  . SER   C 1 151 ? -6.156  -10.096 37.193  1.00 46.48  ? 156 SER   C CB  1 
ATOM   5897 O  OG  . SER   C 1 151 ? -5.482  -11.304 36.870  1.00 49.17  ? 156 SER   C OG  1 
ATOM   5898 N  N   . GLY   C 1 152 ? -5.981  -12.147 39.717  1.00 43.79  ? 157 GLY   C N   1 
ATOM   5899 C  CA  . GLY   C 1 152 ? -6.433  -13.447 40.202  1.00 43.84  ? 157 GLY   C CA  1 
ATOM   5900 C  C   . GLY   C 1 152 ? -6.896  -14.386 39.094  1.00 48.43  ? 157 GLY   C C   1 
ATOM   5901 O  O   . GLY   C 1 152 ? -7.342  -15.499 39.388  1.00 48.81  ? 157 GLY   C O   1 
ATOM   5902 N  N   . ASN   C 1 153 ? -6.802  -13.948 37.805  1.00 44.04  ? 158 ASN   C N   1 
ATOM   5903 C  CA  . ASN   C 1 153 ? -7.200  -14.729 36.618  1.00 42.62  ? 158 ASN   C CA  1 
ATOM   5904 C  C   . ASN   C 1 153 ? -6.127  -15.759 36.286  1.00 44.07  ? 158 ASN   C C   1 
ATOM   5905 O  O   . ASN   C 1 153 ? -4.966  -15.409 36.060  1.00 43.51  ? 158 ASN   C O   1 
ATOM   5906 C  CB  . ASN   C 1 153 ? -7.516  -13.819 35.423  1.00 41.27  ? 158 ASN   C CB  1 
ATOM   5907 C  CG  . ASN   C 1 153 ? -8.624  -12.808 35.672  1.00 56.40  ? 158 ASN   C CG  1 
ATOM   5908 O  OD1 . ASN   C 1 153 ? -9.554  -13.024 36.467  1.00 49.09  ? 158 ASN   C OD1 1 
ATOM   5909 N  ND2 . ASN   C 1 153 ? -8.581  -11.699 34.953  1.00 41.26  ? 158 ASN   C ND2 1 
ATOM   5910 N  N   . LEU   C 1 154 ? -6.502  -17.044 36.317  1.00 37.77  ? 159 LEU   C N   1 
ATOM   5911 C  CA  . LEU   C 1 154 ? -5.548  -18.136 36.111  1.00 36.52  ? 159 LEU   C CA  1 
ATOM   5912 C  C   . LEU   C 1 154 ? -4.939  -18.206 34.696  1.00 35.97  ? 159 LEU   C C   1 
ATOM   5913 O  O   . LEU   C 1 154 ? -3.870  -18.779 34.579  1.00 33.35  ? 159 LEU   C O   1 
ATOM   5914 C  CB  . LEU   C 1 154 ? -6.138  -19.488 36.530  1.00 37.13  ? 159 LEU   C CB  1 
ATOM   5915 C  CG  . LEU   C 1 154 ? -6.176  -19.654 38.057  1.00 42.25  ? 159 LEU   C CG  1 
ATOM   5916 C  CD1 . LEU   C 1 154 ? -7.275  -20.597 38.496  1.00 43.02  ? 159 LEU   C CD1 1 
ATOM   5917 C  CD2 . LEU   C 1 154 ? -4.825  -20.071 38.610  1.00 43.58  ? 159 LEU   C CD2 1 
ATOM   5918 N  N   . HIS   C 1 155 ? -5.548  -17.564 33.678  1.00 34.56  ? 160 HIS   C N   1 
ATOM   5919 C  CA  . HIS   C 1 155 ? -4.966  -17.536 32.311  1.00 33.43  ? 160 HIS   C CA  1 
ATOM   5920 C  C   . HIS   C 1 155 ? -3.687  -16.677 32.244  1.00 37.13  ? 160 HIS   C C   1 
ATOM   5921 O  O   . HIS   C 1 155 ? -2.973  -16.709 31.235  1.00 36.12  ? 160 HIS   C O   1 
ATOM   5922 C  CB  . HIS   C 1 155 ? -6.004  -17.100 31.255  1.00 34.00  ? 160 HIS   C CB  1 
ATOM   5923 C  CG  . HIS   C 1 155 ? -6.314  -15.620 31.204  1.00 37.03  ? 160 HIS   C CG  1 
ATOM   5924 N  ND1 . HIS   C 1 155 ? -6.958  -15.064 30.115  1.00 38.69  ? 160 HIS   C ND1 1 
ATOM   5925 C  CD2 . HIS   C 1 155 ? -6.117  -14.645 32.130  1.00 38.43  ? 160 HIS   C CD2 1 
ATOM   5926 C  CE1 . HIS   C 1 155 ? -7.087  -13.777 30.387  1.00 37.91  ? 160 HIS   C CE1 1 
ATOM   5927 N  NE2 . HIS   C 1 155 ? -6.606  -13.483 31.595  1.00 37.95  ? 160 HIS   C NE2 1 
ATOM   5928 N  N   . GLY   C 1 156 ? -3.415  -15.918 33.318  1.00 33.48  ? 161 GLY   C N   1 
ATOM   5929 C  CA  . GLY   C 1 156 ? -2.235  -15.068 33.410  1.00 33.20  ? 161 GLY   C CA  1 
ATOM   5930 C  C   . GLY   C 1 156 ? -1.124  -15.724 34.191  1.00 34.96  ? 161 GLY   C C   1 
ATOM   5931 O  O   . GLY   C 1 156 ? -0.060  -15.130 34.416  1.00 35.60  ? 161 GLY   C O   1 
ATOM   5932 N  N   . GLN   C 1 157 ? -1.371  -16.976 34.624  1.00 32.34  ? 162 GLN   C N   1 
ATOM   5933 C  CA  . GLN   C 1 157 ? -0.457  -17.753 35.441  1.00 32.28  ? 162 GLN   C CA  1 
ATOM   5934 C  C   . GLN   C 1 157 ? -0.078  -19.171 34.901  1.00 37.20  ? 162 GLN   C C   1 
ATOM   5935 O  O   . GLN   C 1 157 ? 0.687   -19.828 35.607  1.00 36.34  ? 162 GLN   C O   1 
ATOM   5936 C  CB  . GLN   C 1 157 ? -1.083  -17.941 36.857  1.00 33.79  ? 162 GLN   C CB  1 
ATOM   5937 C  CG  . GLN   C 1 157 ? -1.530  -16.651 37.571  1.00 40.66  ? 162 GLN   C CG  1 
ATOM   5938 C  CD  . GLN   C 1 157 ? -2.462  -16.957 38.725  1.00 47.39  ? 162 GLN   C CD  1 
ATOM   5939 O  OE1 . GLN   C 1 157 ? -2.129  -17.729 39.626  1.00 38.86  ? 162 GLN   C OE1 1 
ATOM   5940 N  NE2 . GLN   C 1 157 ? -3.676  -16.419 38.683  1.00 40.45  ? 162 GLN   C NE2 1 
ATOM   5941 N  N   . PRO   C 1 158 ? -0.549  -19.695 33.725  1.00 35.25  ? 163 PRO   C N   1 
ATOM   5942 C  CA  . PRO   C 1 158 ? -0.275  -21.118 33.401  1.00 35.37  ? 163 PRO   C CA  1 
ATOM   5943 C  C   . PRO   C 1 158 ? 1.165   -21.576 33.456  1.00 38.31  ? 163 PRO   C C   1 
ATOM   5944 O  O   . PRO   C 1 158 ? 1.426   -22.662 33.975  1.00 39.37  ? 163 PRO   C O   1 
ATOM   5945 C  CB  . PRO   C 1 158 ? -0.863  -21.302 31.997  1.00 37.00  ? 163 PRO   C CB  1 
ATOM   5946 C  CG  . PRO   C 1 158 ? -1.095  -19.910 31.473  1.00 40.35  ? 163 PRO   C CG  1 
ATOM   5947 C  CD  . PRO   C 1 158 ? -1.427  -19.105 32.702  1.00 36.22  ? 163 PRO   C CD  1 
ATOM   5948 N  N   . VAL   C 1 159 ? 2.095   -20.756 32.972  1.00 32.34  ? 164 VAL   C N   1 
ATOM   5949 C  CA  . VAL   C 1 159 ? 3.500   -21.125 32.918  1.00 31.87  ? 164 VAL   C CA  1 
ATOM   5950 C  C   . VAL   C 1 159 ? 4.121   -21.292 34.331  1.00 38.53  ? 164 VAL   C C   1 
ATOM   5951 O  O   . VAL   C 1 159 ? 5.025   -22.125 34.466  1.00 37.68  ? 164 VAL   C O   1 
ATOM   5952 C  CB  . VAL   C 1 159 ? 4.316   -20.198 31.983  1.00 33.64  ? 164 VAL   C CB  1 
ATOM   5953 C  CG1 . VAL   C 1 159 ? 5.744   -20.705 31.804  1.00 33.36  ? 164 VAL   C CG1 1 
ATOM   5954 C  CG2 . VAL   C 1 159 ? 3.627   -20.077 30.633  1.00 33.01  ? 164 VAL   C CG2 1 
ATOM   5955 N  N   . SER   C 1 160 ? 3.612   -20.582 35.385  1.00 35.24  ? 165 SER   C N   1 
ATOM   5956 C  CA  . SER   C 1 160 ? 4.174   -20.748 36.735  1.00 35.93  ? 165 SER   C CA  1 
ATOM   5957 C  C   . SER   C 1 160 ? 4.037   -22.192 37.244  1.00 40.94  ? 165 SER   C C   1 
ATOM   5958 O  O   . SER   C 1 160 ? 4.986   -22.710 37.825  1.00 40.54  ? 165 SER   C O   1 
ATOM   5959 C  CB  . SER   C 1 160 ? 3.563   -19.771 37.744  1.00 37.72  ? 165 SER   C CB  1 
ATOM   5960 O  OG  . SER   C 1 160 ? 2.162   -19.943 37.885  1.00 42.09  ? 165 SER   C OG  1 
ATOM   5961 N  N   . PHE   C 1 161 ? 2.883   -22.838 36.980  1.00 39.76  ? 166 PHE   C N   1 
ATOM   5962 C  CA  . PHE   C 1 161 ? 2.592   -24.221 37.403  1.00 39.84  ? 166 PHE   C CA  1 
ATOM   5963 C  C   . PHE   C 1 161 ? 3.382   -25.281 36.617  1.00 45.66  ? 166 PHE   C C   1 
ATOM   5964 O  O   . PHE   C 1 161 ? 3.510   -26.420 37.080  1.00 45.11  ? 166 PHE   C O   1 
ATOM   5965 C  CB  . PHE   C 1 161 ? 1.087   -24.517 37.293  1.00 41.65  ? 166 PHE   C CB  1 
ATOM   5966 C  CG  . PHE   C 1 161 ? 0.190   -23.503 37.954  1.00 43.66  ? 166 PHE   C CG  1 
ATOM   5967 C  CD1 . PHE   C 1 161 ? 0.036   -23.483 39.338  1.00 47.47  ? 166 PHE   C CD1 1 
ATOM   5968 C  CD2 . PHE   C 1 161 ? -0.505  -22.565 37.196  1.00 45.52  ? 166 PHE   C CD2 1 
ATOM   5969 C  CE1 . PHE   C 1 161 ? -0.772  -22.518 39.953  1.00 48.32  ? 166 PHE   C CE1 1 
ATOM   5970 C  CE2 . PHE   C 1 161 ? -1.328  -21.613 37.812  1.00 48.53  ? 166 PHE   C CE2 1 
ATOM   5971 C  CZ  . PHE   C 1 161 ? -1.448  -21.591 39.186  1.00 46.88  ? 166 PHE   C CZ  1 
ATOM   5972 N  N   . LEU   C 1 162 ? 3.894   -24.920 35.423  1.00 41.75  ? 167 LEU   C N   1 
ATOM   5973 C  CA  . LEU   C 1 162 ? 4.618   -25.863 34.567  1.00 40.60  ? 167 LEU   C CA  1 
ATOM   5974 C  C   . LEU   C 1 162 ? 6.122   -25.787 34.676  1.00 46.10  ? 167 LEU   C C   1 
ATOM   5975 O  O   . LEU   C 1 162 ? 6.801   -26.767 34.360  1.00 45.93  ? 167 LEU   C O   1 
ATOM   5976 C  CB  . LEU   C 1 162 ? 4.188   -25.691 33.091  1.00 40.12  ? 167 LEU   C CB  1 
ATOM   5977 C  CG  . LEU   C 1 162 ? 2.712   -25.931 32.774  1.00 43.75  ? 167 LEU   C CG  1 
ATOM   5978 C  CD1 . LEU   C 1 162 ? 2.368   -25.404 31.392  1.00 43.61  ? 167 LEU   C CD1 1 
ATOM   5979 C  CD2 . LEU   C 1 162 ? 2.352   -27.403 32.873  1.00 44.04  ? 167 LEU   C CD2 1 
ATOM   5980 N  N   . LEU   C 1 163 ? 6.652   -24.633 35.098  1.00 44.64  ? 168 LEU   C N   1 
ATOM   5981 C  CA  . LEU   C 1 163 ? 8.089   -24.391 35.173  1.00 45.76  ? 168 LEU   C CA  1 
ATOM   5982 C  C   . LEU   C 1 163 ? 8.767   -25.041 36.378  1.00 51.96  ? 168 LEU   C C   1 
ATOM   5983 O  O   . LEU   C 1 163 ? 8.415   -24.727 37.516  1.00 51.19  ? 168 LEU   C O   1 
ATOM   5984 C  CB  . LEU   C 1 163 ? 8.366   -22.877 35.118  1.00 46.24  ? 168 LEU   C CB  1 
ATOM   5985 C  CG  . LEU   C 1 163 ? 9.521   -22.374 34.239  1.00 52.09  ? 168 LEU   C CG  1 
ATOM   5986 C  CD1 . LEU   C 1 163 ? 10.874  -22.546 34.913  1.00 53.00  ? 168 LEU   C CD1 1 
ATOM   5987 C  CD2 . LEU   C 1 163 ? 9.469   -22.935 32.815  1.00 54.21  ? 168 LEU   C CD2 1 
ATOM   5988 N  N   . ARG   C 1 164 ? 9.769   -25.915 36.115  1.00 49.59  ? 169 ARG   C N   1 
ATOM   5989 C  CA  . ARG   C 1 164 ? 10.534  -26.661 37.128  1.00 50.25  ? 169 ARG   C CA  1 
ATOM   5990 C  C   . ARG   C 1 164 ? 11.246  -25.776 38.141  1.00 53.93  ? 169 ARG   C C   1 
ATOM   5991 O  O   . ARG   C 1 164 ? 11.080  -25.981 39.346  1.00 53.47  ? 169 ARG   C O   1 
ATOM   5992 C  CB  . ARG   C 1 164 ? 11.541  -27.636 36.483  1.00 52.32  ? 169 ARG   C CB  1 
ATOM   5993 C  CG  . ARG   C 1 164 ? 10.923  -28.909 35.923  1.00 66.54  ? 169 ARG   C CG  1 
ATOM   5994 C  CD  . ARG   C 1 164 ? 11.995  -29.872 35.440  1.00 79.12  ? 169 ARG   C CD  1 
ATOM   5995 N  NE  . ARG   C 1 164 ? 11.461  -30.851 34.492  1.00 88.23  ? 169 ARG   C NE  1 
ATOM   5996 C  CZ  . ARG   C 1 164 ? 10.985  -32.045 34.829  1.00 104.94 ? 169 ARG   C CZ  1 
ATOM   5997 N  NH1 . ARG   C 1 164 ? 10.974  -32.430 36.100  1.00 93.20  ? 169 ARG   C NH1 1 
ATOM   5998 N  NH2 . ARG   C 1 164 ? 10.516  -32.865 33.897  1.00 93.34  ? 169 ARG   C NH2 1 
ATOM   5999 N  N   . GLU   C 1 165 ? 12.022  -24.786 37.652  1.00 50.18  ? 170 GLU   C N   1 
ATOM   6000 C  CA  . GLU   C 1 165 ? 12.808  -23.854 38.459  1.00 49.88  ? 170 GLU   C CA  1 
ATOM   6001 C  C   . GLU   C 1 165 ? 11.981  -22.932 39.375  1.00 54.05  ? 170 GLU   C C   1 
ATOM   6002 O  O   . GLU   C 1 165 ? 12.545  -22.371 40.318  1.00 54.66  ? 170 GLU   C O   1 
ATOM   6003 C  CB  . GLU   C 1 165 ? 13.749  -23.025 37.566  1.00 50.98  ? 170 GLU   C CB  1 
ATOM   6004 C  CG  . GLU   C 1 165 ? 14.954  -23.797 37.046  1.00 55.58  ? 170 GLU   C CG  1 
ATOM   6005 C  CD  . GLU   C 1 165 ? 14.832  -24.451 35.680  1.00 65.46  ? 170 GLU   C CD  1 
ATOM   6006 O  OE1 . GLU   C 1 165 ? 13.696  -24.615 35.176  1.00 44.51  ? 170 GLU   C OE1 1 
ATOM   6007 O  OE2 . GLU   C 1 165 ? 15.888  -24.823 35.120  1.00 61.82  ? 170 GLU   C OE2 1 
ATOM   6008 N  N   . LEU   C 1 166 ? 10.665  -22.794 39.109  1.00 49.46  ? 171 LEU   C N   1 
ATOM   6009 C  CA  . LEU   C 1 166 ? 9.724   -21.936 39.843  1.00 49.35  ? 171 LEU   C CA  1 
ATOM   6010 C  C   . LEU   C 1 166 ? 8.910   -22.629 40.956  1.00 52.39  ? 171 LEU   C C   1 
ATOM   6011 O  O   . LEU   C 1 166 ? 8.129   -21.947 41.628  1.00 50.53  ? 171 LEU   C O   1 
ATOM   6012 C  CB  . LEU   C 1 166 ? 8.731   -21.290 38.854  1.00 49.52  ? 171 LEU   C CB  1 
ATOM   6013 C  CG  . LEU   C 1 166 ? 9.026   -19.886 38.307  1.00 54.16  ? 171 LEU   C CG  1 
ATOM   6014 C  CD1 . LEU   C 1 166 ? 7.876   -19.417 37.424  1.00 54.18  ? 171 LEU   C CD1 1 
ATOM   6015 C  CD2 . LEU   C 1 166 ? 9.214   -18.862 39.427  1.00 56.13  ? 171 LEU   C CD2 1 
ATOM   6016 N  N   . GLN   C 1 167 ? 9.049   -23.967 41.119  1.00 49.84  ? 172 GLN   C N   1 
ATOM   6017 C  CA  . GLN   C 1 167 ? 8.278   -24.784 42.075  1.00 50.02  ? 172 GLN   C CA  1 
ATOM   6018 C  C   . GLN   C 1 167 ? 8.197   -24.216 43.507  1.00 52.25  ? 172 GLN   C C   1 
ATOM   6019 O  O   . GLN   C 1 167 ? 7.099   -24.162 44.067  1.00 52.10  ? 172 GLN   C O   1 
ATOM   6020 C  CB  . GLN   C 1 167 ? 8.788   -26.239 42.109  1.00 51.87  ? 172 GLN   C CB  1 
ATOM   6021 C  CG  . GLN   C 1 167 ? 7.728   -27.231 42.607  1.00 69.02  ? 172 GLN   C CG  1 
ATOM   6022 C  CD  . GLN   C 1 167 ? 8.204   -28.661 42.777  1.00 87.68  ? 172 GLN   C CD  1 
ATOM   6023 O  OE1 . GLN   C 1 167 ? 9.354   -29.020 42.493  1.00 80.07  ? 172 GLN   C OE1 1 
ATOM   6024 N  NE2 . GLN   C 1 167 ? 7.309   -29.517 43.254  1.00 82.19  ? 172 GLN   C NE2 1 
ATOM   6025 N  N   . ASP   C 1 168 ? 9.331   -23.769 44.076  1.00 48.72  ? 173 ASP   C N   1 
ATOM   6026 C  CA  . ASP   C 1 168 ? 9.375   -23.236 45.449  1.00 48.53  ? 173 ASP   C CA  1 
ATOM   6027 C  C   . ASP   C 1 168 ? 8.640   -21.882 45.643  1.00 49.72  ? 173 ASP   C C   1 
ATOM   6028 O  O   . ASP   C 1 168 ? 8.373   -21.496 46.789  1.00 48.72  ? 173 ASP   C O   1 
ATOM   6029 C  CB  . ASP   C 1 168 ? 10.826  -23.159 45.967  1.00 51.16  ? 173 ASP   C CB  1 
ATOM   6030 C  CG  . ASP   C 1 168 ? 11.799  -22.339 45.135  1.00 68.17  ? 173 ASP   C CG  1 
ATOM   6031 O  OD1 . ASP   C 1 168 ? 11.423  -21.921 44.010  1.00 70.51  ? 173 ASP   C OD1 1 
ATOM   6032 O  OD2 . ASP   C 1 168 ? 12.948  -22.138 45.594  1.00 74.04  ? 173 ASP   C OD2 1 
ATOM   6033 N  N   . LYS   C 1 169 ? 8.294   -21.177 44.539  1.00 43.07  ? 174 LYS   C N   1 
ATOM   6034 C  CA  . LYS   C 1 169 ? 7.590   -19.892 44.604  1.00 41.38  ? 174 LYS   C CA  1 
ATOM   6035 C  C   . LYS   C 1 169 ? 6.097   -20.062 44.304  1.00 44.15  ? 174 LYS   C C   1 
ATOM   6036 O  O   . LYS   C 1 169 ? 5.344   -19.093 44.377  1.00 42.29  ? 174 LYS   C O   1 
ATOM   6037 C  CB  . LYS   C 1 169 ? 8.228   -18.844 43.652  1.00 42.78  ? 174 LYS   C CB  1 
ATOM   6038 C  CG  . LYS   C 1 169 ? 9.761   -18.780 43.638  1.00 49.72  ? 174 LYS   C CG  1 
ATOM   6039 C  CD  . LYS   C 1 169 ? 10.348  -18.106 44.877  1.00 57.64  ? 174 LYS   C CD  1 
ATOM   6040 C  CE  . LYS   C 1 169 ? 11.840  -18.289 44.978  1.00 56.53  ? 174 LYS   C CE  1 
ATOM   6041 N  NZ  . LYS   C 1 169 ? 12.394  -17.587 46.167  1.00 69.76  ? 174 LYS   C NZ  1 
ATOM   6042 N  N   . VAL   C 1 170 ? 5.665   -21.292 43.972  1.00 42.68  ? 175 VAL   C N   1 
ATOM   6043 C  CA  . VAL   C 1 170 ? 4.262   -21.578 43.644  1.00 44.23  ? 175 VAL   C CA  1 
ATOM   6044 C  C   . VAL   C 1 170 ? 3.560   -22.314 44.801  1.00 51.65  ? 175 VAL   C C   1 
ATOM   6045 O  O   . VAL   C 1 170 ? 3.961   -23.436 45.126  1.00 49.72  ? 175 VAL   C O   1 
ATOM   6046 C  CB  . VAL   C 1 170 ? 4.091   -22.326 42.280  1.00 47.98  ? 175 VAL   C CB  1 
ATOM   6047 C  CG1 . VAL   C 1 170 ? 2.621   -22.626 41.988  1.00 47.89  ? 175 VAL   C CG1 1 
ATOM   6048 C  CG2 . VAL   C 1 170 ? 4.709   -21.538 41.132  1.00 47.76  ? 175 VAL   C CG2 1 
ATOM   6049 N  N   . PRO   C 1 171 ? 2.506   -21.712 45.412  1.00 51.83  ? 176 PRO   C N   1 
ATOM   6050 C  CA  . PRO   C 1 171 ? 1.790   -22.414 46.489  1.00 53.01  ? 176 PRO   C CA  1 
ATOM   6051 C  C   . PRO   C 1 171 ? 0.863   -23.479 45.905  1.00 59.93  ? 176 PRO   C C   1 
ATOM   6052 O  O   . PRO   C 1 171 ? 0.442   -23.340 44.755  1.00 59.74  ? 176 PRO   C O   1 
ATOM   6053 C  CB  . PRO   C 1 171 ? 1.003   -21.294 47.173  1.00 54.74  ? 176 PRO   C CB  1 
ATOM   6054 C  CG  . PRO   C 1 171 ? 0.753   -20.298 46.098  1.00 58.83  ? 176 PRO   C CG  1 
ATOM   6055 C  CD  . PRO   C 1 171 ? 1.909   -20.386 45.139  1.00 54.19  ? 176 PRO   C CD  1 
ATOM   6056 N  N   . GLN   C 1 172 ? 0.543   -24.540 46.676  1.00 57.59  ? 177 GLN   C N   1 
ATOM   6057 C  CA  . GLN   C 1 172 ? -0.343  -25.586 46.169  1.00 57.84  ? 177 GLN   C CA  1 
ATOM   6058 C  C   . GLN   C 1 172 ? -1.802  -25.163 46.260  1.00 60.89  ? 177 GLN   C C   1 
ATOM   6059 O  O   . GLN   C 1 172 ? -2.333  -24.965 47.355  1.00 61.12  ? 177 GLN   C O   1 
ATOM   6060 C  CB  . GLN   C 1 172 ? -0.082  -26.944 46.835  1.00 59.63  ? 177 GLN   C CB  1 
ATOM   6061 C  CG  . GLN   C 1 172 ? -0.346  -28.113 45.893  1.00 83.19  ? 177 GLN   C CG  1 
ATOM   6062 C  CD  . GLN   C 1 172 ? -1.280  -29.119 46.511  1.00 111.69 ? 177 GLN   C CD  1 
ATOM   6063 O  OE1 . GLN   C 1 172 ? -0.860  -30.027 47.240  1.00 109.19 ? 177 GLN   C OE1 1 
ATOM   6064 N  NE2 . GLN   C 1 172 ? -2.573  -28.972 46.243  1.00 104.87 ? 177 GLN   C NE2 1 
ATOM   6065 N  N   . LEU   C 1 173 ? -2.434  -24.988 45.094  1.00 56.20  ? 178 LEU   C N   1 
ATOM   6066 C  CA  . LEU   C 1 173 ? -3.821  -24.545 44.958  1.00 55.74  ? 178 LEU   C CA  1 
ATOM   6067 C  C   . LEU   C 1 173 ? -4.805  -25.723 44.968  1.00 59.42  ? 178 LEU   C C   1 
ATOM   6068 O  O   . LEU   C 1 173 ? -4.417  -26.826 44.566  1.00 58.54  ? 178 LEU   C O   1 
ATOM   6069 C  CB  . LEU   C 1 173 ? -3.970  -23.743 43.650  1.00 55.69  ? 178 LEU   C CB  1 
ATOM   6070 C  CG  . LEU   C 1 173 ? -3.880  -22.215 43.731  1.00 60.46  ? 178 LEU   C CG  1 
ATOM   6071 C  CD1 . LEU   C 1 173 ? -2.541  -21.761 44.269  1.00 60.81  ? 178 LEU   C CD1 1 
ATOM   6072 C  CD2 . LEU   C 1 173 ? -4.087  -21.594 42.356  1.00 63.01  ? 178 LEU   C CD2 1 
ATOM   6073 N  N   . PRO   C 1 174 ? -6.082  -25.520 45.392  1.00 55.70  ? 179 PRO   C N   1 
ATOM   6074 C  CA  . PRO   C 1 174 ? -7.039  -26.641 45.380  1.00 55.11  ? 179 PRO   C CA  1 
ATOM   6075 C  C   . PRO   C 1 174 ? -7.375  -27.090 43.956  1.00 57.36  ? 179 PRO   C C   1 
ATOM   6076 O  O   . PRO   C 1 174 ? -7.848  -26.290 43.141  1.00 57.30  ? 179 PRO   C O   1 
ATOM   6077 C  CB  . PRO   C 1 174 ? -8.257  -26.082 46.123  1.00 57.02  ? 179 PRO   C CB  1 
ATOM   6078 C  CG  . PRO   C 1 174 ? -8.175  -24.602 45.936  1.00 61.34  ? 179 PRO   C CG  1 
ATOM   6079 C  CD  . PRO   C 1 174 ? -6.711  -24.280 45.904  1.00 57.22  ? 179 PRO   C CD  1 
ATOM   6080 N  N   . GLY   C 1 175 ? -7.100  -28.363 43.674  1.00 52.35  ? 180 GLY   C N   1 
ATOM   6081 C  CA  . GLY   C 1 175 ? -7.325  -28.976 42.368  1.00 51.61  ? 180 GLY   C CA  1 
ATOM   6082 C  C   . GLY   C 1 175 ? -6.116  -28.891 41.453  1.00 54.09  ? 180 GLY   C C   1 
ATOM   6083 O  O   . GLY   C 1 175 ? -6.211  -29.231 40.273  1.00 54.01  ? 180 GLY   C O   1 
ATOM   6084 N  N   . PHE   C 1 176 ? -4.965  -28.477 42.005  1.00 48.84  ? 181 PHE   C N   1 
ATOM   6085 C  CA  . PHE   C 1 176 ? -3.710  -28.283 41.276  1.00 48.59  ? 181 PHE   C CA  1 
ATOM   6086 C  C   . PHE   C 1 176 ? -2.579  -29.228 41.722  1.00 53.95  ? 181 PHE   C C   1 
ATOM   6087 O  O   . PHE   C 1 176 ? -1.465  -29.121 41.205  1.00 53.41  ? 181 PHE   C O   1 
ATOM   6088 C  CB  . PHE   C 1 176 ? -3.260  -26.800 41.382  1.00 49.75  ? 181 PHE   C CB  1 
ATOM   6089 C  CG  . PHE   C 1 176 ? -3.903  -25.823 40.421  1.00 51.18  ? 181 PHE   C CG  1 
ATOM   6090 C  CD1 . PHE   C 1 176 ? -5.260  -25.524 40.506  1.00 54.10  ? 181 PHE   C CD1 1 
ATOM   6091 C  CD2 . PHE   C 1 176 ? -3.140  -25.154 39.469  1.00 52.94  ? 181 PHE   C CD2 1 
ATOM   6092 C  CE1 . PHE   C 1 176 ? -5.849  -24.611 39.625  1.00 55.16  ? 181 PHE   C CE1 1 
ATOM   6093 C  CE2 . PHE   C 1 176 ? -3.732  -24.243 38.587  1.00 55.53  ? 181 PHE   C CE2 1 
ATOM   6094 C  CZ  . PHE   C 1 176 ? -5.081  -23.976 38.672  1.00 53.73  ? 181 PHE   C CZ  1 
ATOM   6095 N  N   . SER   C 1 177 ? -2.856  -30.148 42.674  1.00 51.96  ? 182 SER   C N   1 
ATOM   6096 C  CA  . SER   C 1 177 ? -1.862  -31.099 43.205  1.00 52.33  ? 182 SER   C CA  1 
ATOM   6097 C  C   . SER   C 1 177 ? -1.331  -32.092 42.164  1.00 56.44  ? 182 SER   C C   1 
ATOM   6098 O  O   . SER   C 1 177 ? -0.160  -32.476 42.240  1.00 55.02  ? 182 SER   C O   1 
ATOM   6099 C  CB  . SER   C 1 177 ? -2.436  -31.872 44.387  1.00 56.40  ? 182 SER   C CB  1 
ATOM   6100 O  OG  . SER   C 1 177 ? -3.548  -32.647 43.969  1.00 67.54  ? 182 SER   C OG  1 
ATOM   6101 N  N   . TRP   C 1 178 ? -2.190  -32.502 41.204  1.00 55.01  ? 183 TRP   C N   1 
ATOM   6102 C  CA  . TRP   C 1 178 ? -1.857  -33.451 40.128  1.00 55.96  ? 183 TRP   C CA  1 
ATOM   6103 C  C   . TRP   C 1 178 ? -0.718  -32.991 39.204  1.00 60.45  ? 183 TRP   C C   1 
ATOM   6104 O  O   . TRP   C 1 178 ? -0.023  -33.832 38.627  1.00 59.64  ? 183 TRP   C O   1 
ATOM   6105 C  CB  . TRP   C 1 178 ? -3.106  -33.798 39.303  1.00 55.29  ? 183 TRP   C CB  1 
ATOM   6106 C  CG  . TRP   C 1 178 ? -3.687  -32.647 38.530  1.00 56.62  ? 183 TRP   C CG  1 
ATOM   6107 C  CD1 . TRP   C 1 178 ? -4.628  -31.760 38.963  1.00 59.58  ? 183 TRP   C CD1 1 
ATOM   6108 C  CD2 . TRP   C 1 178 ? -3.400  -32.296 37.168  1.00 56.53  ? 183 TRP   C CD2 1 
ATOM   6109 N  NE1 . TRP   C 1 178 ? -4.937  -30.868 37.960  1.00 59.14  ? 183 TRP   C NE1 1 
ATOM   6110 C  CE2 . TRP   C 1 178 ? -4.201  -31.177 36.845  1.00 60.48  ? 183 TRP   C CE2 1 
ATOM   6111 C  CE3 . TRP   C 1 178 ? -2.540  -32.818 36.186  1.00 57.67  ? 183 TRP   C CE3 1 
ATOM   6112 C  CZ2 . TRP   C 1 178 ? -4.143  -30.551 35.593  1.00 59.70  ? 183 TRP   C CZ2 1 
ATOM   6113 C  CZ3 . TRP   C 1 178 ? -2.494  -32.203 34.943  1.00 58.82  ? 183 TRP   C CZ3 1 
ATOM   6114 C  CH2 . TRP   C 1 178 ? -3.293  -31.090 34.653  1.00 59.36  ? 183 TRP   C CH2 1 
ATOM   6115 N  N   . ILE   C 1 179 ? -0.536  -31.656 39.069  1.00 57.77  ? 184 ILE   C N   1 
ATOM   6116 C  CA  . ILE   C 1 179 ? 0.470   -31.026 38.212  1.00 57.09  ? 184 ILE   C CA  1 
ATOM   6117 C  C   . ILE   C 1 179 ? 1.889   -31.255 38.712  1.00 61.94  ? 184 ILE   C C   1 
ATOM   6118 O  O   . ILE   C 1 179 ? 2.237   -30.832 39.815  1.00 62.34  ? 184 ILE   C O   1 
ATOM   6119 C  CB  . ILE   C 1 179 ? 0.170   -29.511 37.988  1.00 60.01  ? 184 ILE   C CB  1 
ATOM   6120 C  CG1 . ILE   C 1 179 ? -1.255  -29.295 37.453  1.00 60.23  ? 184 ILE   C CG1 1 
ATOM   6121 C  CG2 . ILE   C 1 179 ? 1.210   -28.858 37.051  1.00 60.25  ? 184 ILE   C CG2 1 
ATOM   6122 C  CD1 . ILE   C 1 179 ? -1.924  -28.091 37.959  1.00 67.69  ? 184 ILE   C CD1 1 
ATOM   6123 N  N   . LYS   C 1 180 ? 2.709   -31.903 37.876  1.00 58.41  ? 185 LYS   C N   1 
ATOM   6124 C  CA  . LYS   C 1 180 ? 4.126   -32.146 38.136  1.00 58.08  ? 185 LYS   C CA  1 
ATOM   6125 C  C   . LYS   C 1 180 ? 4.897   -31.173 37.225  1.00 61.39  ? 185 LYS   C C   1 
ATOM   6126 O  O   . LYS   C 1 180 ? 4.714   -31.250 36.004  1.00 61.18  ? 185 LYS   C O   1 
ATOM   6127 C  CB  . LYS   C 1 180 ? 4.507   -33.609 37.806  1.00 60.70  ? 185 LYS   C CB  1 
ATOM   6128 C  CG  . LYS   C 1 180 ? 3.903   -34.652 38.744  1.00 81.72  ? 185 LYS   C CG  1 
ATOM   6129 C  CD  . LYS   C 1 180 ? 4.160   -36.079 38.254  1.00 93.45  ? 185 LYS   C CD  1 
ATOM   6130 C  CE  . LYS   C 1 180 ? 3.726   -37.136 39.247  1.00 105.31 ? 185 LYS   C CE  1 
ATOM   6131 N  NZ  . LYS   C 1 180 ? 2.247   -37.312 39.279  1.00 114.42 ? 185 LYS   C NZ  1 
ATOM   6132 N  N   . PRO   C 1 181 ? 5.716   -30.230 37.766  1.00 57.77  ? 186 PRO   C N   1 
ATOM   6133 C  CA  . PRO   C 1 181 ? 6.464   -29.309 36.881  1.00 57.36  ? 186 PRO   C CA  1 
ATOM   6134 C  C   . PRO   C 1 181 ? 7.298   -30.098 35.872  1.00 60.21  ? 186 PRO   C C   1 
ATOM   6135 O  O   . PRO   C 1 181 ? 8.160   -30.891 36.265  1.00 59.97  ? 186 PRO   C O   1 
ATOM   6136 C  CB  . PRO   C 1 181 ? 7.327   -28.497 37.853  1.00 59.08  ? 186 PRO   C CB  1 
ATOM   6137 C  CG  . PRO   C 1 181 ? 6.647   -28.626 39.173  1.00 63.13  ? 186 PRO   C CG  1 
ATOM   6138 C  CD  . PRO   C 1 181 ? 6.044   -29.988 39.187  1.00 58.91  ? 186 PRO   C CD  1 
ATOM   6139 N  N   . CYS   C 1 182 ? 6.960   -29.953 34.582  1.00 55.77  ? 187 CYS   C N   1 
ATOM   6140 C  CA  . CYS   C 1 182 ? 7.567   -30.723 33.493  1.00 55.43  ? 187 CYS   C CA  1 
ATOM   6141 C  C   . CYS   C 1 182 ? 8.569   -29.942 32.632  1.00 59.98  ? 187 CYS   C C   1 
ATOM   6142 O  O   . CYS   C 1 182 ? 9.585   -30.517 32.232  1.00 61.04  ? 187 CYS   C O   1 
ATOM   6143 C  CB  . CYS   C 1 182 ? 6.485   -31.371 32.634  1.00 55.63  ? 187 CYS   C CB  1 
ATOM   6144 S  SG  . CYS   C 1 182 ? 5.158   -30.246 32.113  1.00 59.38  ? 187 CYS   C SG  1 
ATOM   6145 N  N   . ILE   C 1 183 ? 8.298   -28.661 32.337  1.00 55.18  ? 188 ILE   C N   1 
ATOM   6146 C  CA  . ILE   C 1 183 ? 9.197   -27.868 31.483  1.00 54.41  ? 188 ILE   C CA  1 
ATOM   6147 C  C   . ILE   C 1 183 ? 10.240  -27.102 32.281  1.00 54.88  ? 188 ILE   C C   1 
ATOM   6148 O  O   . ILE   C 1 183 ? 9.911   -26.507 33.307  1.00 54.30  ? 188 ILE   C O   1 
ATOM   6149 C  CB  . ILE   C 1 183 ? 8.443   -26.940 30.476  1.00 58.00  ? 188 ILE   C CB  1 
ATOM   6150 C  CG1 . ILE   C 1 183 ? 7.441   -25.987 31.177  1.00 58.89  ? 188 ILE   C CG1 1 
ATOM   6151 C  CG2 . ILE   C 1 183 ? 7.763   -27.773 29.384  1.00 58.95  ? 188 ILE   C CG2 1 
ATOM   6152 C  CD1 . ILE   C 1 183 ? 6.970   -24.757 30.346  1.00 68.63  ? 188 ILE   C CD1 1 
ATOM   6153 N  N   . SER   C 1 184 ? 11.504  -27.140 31.812  1.00 49.65  ? 189 SER   C N   1 
ATOM   6154 C  CA  . SER   C 1 184 ? 12.625  -26.399 32.400  1.00 48.72  ? 189 SER   C CA  1 
ATOM   6155 C  C   . SER   C 1 184 ? 12.707  -25.018 31.727  1.00 50.57  ? 189 SER   C C   1 
ATOM   6156 O  O   . SER   C 1 184 ? 12.141  -24.834 30.641  1.00 47.82  ? 189 SER   C O   1 
ATOM   6157 C  CB  . SER   C 1 184 ? 13.941  -27.154 32.229  1.00 53.58  ? 189 SER   C CB  1 
ATOM   6158 O  OG  . SER   C 1 184 ? 14.350  -27.237 30.872  1.00 67.47  ? 189 SER   C OG  1 
ATOM   6159 N  N   . SER   C 1 185 ? 13.410  -24.061 32.367  1.00 47.07  ? 190 SER   C N   1 
ATOM   6160 C  CA  . SER   C 1 185 ? 13.557  -22.687 31.876  1.00 46.52  ? 190 SER   C CA  1 
ATOM   6161 C  C   . SER   C 1 185 ? 14.240  -22.576 30.493  1.00 46.79  ? 190 SER   C C   1 
ATOM   6162 O  O   . SER   C 1 185 ? 13.883  -21.685 29.714  1.00 43.99  ? 190 SER   C O   1 
ATOM   6163 C  CB  . SER   C 1 185 ? 14.260  -21.817 32.911  1.00 51.35  ? 190 SER   C CB  1 
ATOM   6164 O  OG  . SER   C 1 185 ? 15.603  -22.231 33.102  1.00 63.66  ? 190 SER   C OG  1 
ATOM   6165 N  N   . ALA   C 1 186 ? 15.191  -23.485 30.183  1.00 41.57  ? 191 ALA   C N   1 
ATOM   6166 C  CA  . ALA   C 1 186 ? 15.884  -23.492 28.885  1.00 40.52  ? 191 ALA   C CA  1 
ATOM   6167 C  C   . ALA   C 1 186 ? 15.050  -24.124 27.748  1.00 41.24  ? 191 ALA   C C   1 
ATOM   6168 O  O   . ALA   C 1 186 ? 15.476  -24.058 26.592  1.00 42.02  ? 191 ALA   C O   1 
ATOM   6169 C  CB  . ALA   C 1 186 ? 17.232  -24.190 29.011  1.00 41.00  ? 191 ALA   C CB  1 
ATOM   6170 N  N   . SER   C 1 187 ? 13.866  -24.701 28.061  1.00 35.87  ? 192 SER   C N   1 
ATOM   6171 C  CA  . SER   C 1 187 ? 12.996  -25.410 27.109  1.00 35.01  ? 192 SER   C CA  1 
ATOM   6172 C  C   . SER   C 1 187 ? 11.730  -24.667 26.708  1.00 35.30  ? 192 SER   C C   1 
ATOM   6173 O  O   . SER   C 1 187 ? 10.851  -25.248 26.075  1.00 33.75  ? 192 SER   C O   1 
ATOM   6174 C  CB  . SER   C 1 187 ? 12.652  -26.805 27.633  1.00 38.99  ? 192 SER   C CB  1 
ATOM   6175 O  OG  . SER   C 1 187 ? 13.848  -27.523 27.890  1.00 45.35  ? 192 SER   C OG  1 
ATOM   6176 N  N   . ILE   C 1 188 ? 11.634  -23.368 27.055  1.00 31.90  ? 193 ILE   C N   1 
ATOM   6177 C  CA  . ILE   C 1 188 ? 10.493  -22.544 26.655  1.00 31.31  ? 193 ILE   C CA  1 
ATOM   6178 C  C   . ILE   C 1 188 ? 11.035  -21.255 26.045  1.00 32.96  ? 193 ILE   C C   1 
ATOM   6179 O  O   . ILE   C 1 188 ? 11.940  -20.657 26.618  1.00 32.52  ? 193 ILE   C O   1 
ATOM   6180 C  CB  . ILE   C 1 188 ? 9.442   -22.292 27.793  1.00 34.25  ? 193 ILE   C CB  1 
ATOM   6181 C  CG1 . ILE   C 1 188 ? 8.215   -21.481 27.252  1.00 34.35  ? 193 ILE   C CG1 1 
ATOM   6182 C  CG2 . ILE   C 1 188 ? 10.088  -21.653 29.048  1.00 34.16  ? 193 ILE   C CG2 1 
ATOM   6183 C  CD1 . ILE   C 1 188 ? 6.956   -21.405 28.114  1.00 41.42  ? 193 ILE   C CD1 1 
ATOM   6184 N  N   . VAL   C 1 189 ? 10.541  -20.883 24.850  1.00 29.61  ? 194 VAL   C N   1 
ATOM   6185 C  CA  . VAL   C 1 189 ? 10.897  -19.607 24.194  1.00 28.15  ? 194 VAL   C CA  1 
ATOM   6186 C  C   . VAL   C 1 189 ? 9.597   -18.852 23.907  1.00 29.28  ? 194 VAL   C C   1 
ATOM   6187 O  O   . VAL   C 1 189 ? 8.645   -19.423 23.349  1.00 28.40  ? 194 VAL   C O   1 
ATOM   6188 C  CB  . VAL   C 1 189 ? 11.813  -19.767 22.928  1.00 31.63  ? 194 VAL   C CB  1 
ATOM   6189 C  CG1 . VAL   C 1 189 ? 11.897  -18.459 22.126  1.00 30.64  ? 194 VAL   C CG1 1 
ATOM   6190 C  CG2 . VAL   C 1 189 ? 13.222  -20.218 23.317  1.00 31.35  ? 194 VAL   C CG2 1 
ATOM   6191 N  N   . TYR   C 1 190 ? 9.534   -17.546 24.331  1.00 25.75  ? 195 TYR   C N   1 
ATOM   6192 C  CA  . TYR   C 1 190 ? 8.353   -16.735 24.028  1.00 25.50  ? 195 TYR   C CA  1 
ATOM   6193 C  C   . TYR   C 1 190 ? 8.620   -15.914 22.762  1.00 25.48  ? 195 TYR   C C   1 
ATOM   6194 O  O   . TYR   C 1 190 ? 9.745   -15.475 22.535  1.00 25.73  ? 195 TYR   C O   1 
ATOM   6195 C  CB  . TYR   C 1 190 ? 8.056   -15.705 25.136  1.00 27.18  ? 195 TYR   C CB  1 
ATOM   6196 C  CG  . TYR   C 1 190 ? 7.535   -16.290 26.422  1.00 27.20  ? 195 TYR   C CG  1 
ATOM   6197 C  CD1 . TYR   C 1 190 ? 8.404   -16.687 27.427  1.00 30.78  ? 195 TYR   C CD1 1 
ATOM   6198 C  CD2 . TYR   C 1 190 ? 6.171   -16.474 26.623  1.00 27.25  ? 195 TYR   C CD2 1 
ATOM   6199 C  CE1 . TYR   C 1 190 ? 7.927   -17.212 28.630  1.00 30.09  ? 195 TYR   C CE1 1 
ATOM   6200 C  CE2 . TYR   C 1 190 ? 5.683   -17.037 27.807  1.00 28.23  ? 195 TYR   C CE2 1 
ATOM   6201 C  CZ  . TYR   C 1 190 ? 6.565   -17.368 28.817  1.00 33.51  ? 195 TYR   C CZ  1 
ATOM   6202 O  OH  . TYR   C 1 190 ? 6.101   -17.872 30.004  1.00 35.38  ? 195 TYR   C OH  1 
ATOM   6203 N  N   . ILE   C 1 191 ? 7.562   -15.654 22.017  1.00 23.50  ? 196 ILE   C N   1 
ATOM   6204 C  CA  . ILE   C 1 191 ? 7.574   -14.795 20.832  1.00 23.03  ? 196 ILE   C CA  1 
ATOM   6205 C  C   . ILE   C 1 191 ? 6.368   -13.891 20.872  1.00 25.67  ? 196 ILE   C C   1 
ATOM   6206 O  O   . ILE   C 1 191 ? 5.248   -14.392 20.921  1.00 24.37  ? 196 ILE   C O   1 
ATOM   6207 C  CB  . ILE   C 1 191 ? 7.651   -15.599 19.489  1.00 24.75  ? 196 ILE   C CB  1 
ATOM   6208 C  CG1 . ILE   C 1 191 ? 8.892   -16.517 19.447  1.00 25.20  ? 196 ILE   C CG1 1 
ATOM   6209 C  CG2 . ILE   C 1 191 ? 7.673   -14.617 18.271  1.00 23.53  ? 196 ILE   C CG2 1 
ATOM   6210 C  CD1 . ILE   C 1 191 ? 8.889   -17.496 18.277  1.00 25.30  ? 196 ILE   C CD1 1 
ATOM   6211 N  N   . GLY   C 1 192 ? 6.591   -12.576 20.712  1.00 24.33  ? 197 GLY   C N   1 
ATOM   6212 C  CA  . GLY   C 1 192 ? 5.492   -11.620 20.596  1.00 23.40  ? 197 GLY   C CA  1 
ATOM   6213 C  C   . GLY   C 1 192 ? 5.212   -10.729 21.791  1.00 26.30  ? 197 GLY   C C   1 
ATOM   6214 O  O   . GLY   C 1 192 ? 4.321   -9.878  21.702  1.00 25.92  ? 197 GLY   C O   1 
ATOM   6215 N  N   . LEU   C 1 193 ? 5.986   -10.874 22.876  1.00 24.10  ? 198 LEU   C N   1 
ATOM   6216 C  CA  . LEU   C 1 193 ? 5.773   -10.163 24.148  1.00 24.27  ? 198 LEU   C CA  1 
ATOM   6217 C  C   . LEU   C 1 193 ? 5.728   -8.661  24.011  1.00 27.69  ? 198 LEU   C C   1 
ATOM   6218 O  O   . LEU   C 1 193 ? 6.586   -8.067  23.362  1.00 25.16  ? 198 LEU   C O   1 
ATOM   6219 C  CB  . LEU   C 1 193 ? 6.816   -10.532 25.211  1.00 24.07  ? 198 LEU   C CB  1 
ATOM   6220 C  CG  . LEU   C 1 193 ? 6.955   -12.011 25.579  1.00 27.69  ? 198 LEU   C CG  1 
ATOM   6221 C  CD1 . LEU   C 1 193 ? 7.886   -12.172 26.757  1.00 28.87  ? 198 LEU   C CD1 1 
ATOM   6222 C  CD2 . LEU   C 1 193 ? 5.582   -12.627 25.897  1.00 29.65  ? 198 LEU   C CD2 1 
ATOM   6223 N  N   . ARG   C 1 194 ? 4.710   -8.056  24.641  1.00 26.27  ? 199 ARG   C N   1 
ATOM   6224 C  CA  . ARG   C 1 194 ? 4.555   -6.597  24.641  1.00 24.79  ? 199 ARG   C CA  1 
ATOM   6225 C  C   . ARG   C 1 194 ? 3.778   -6.060  25.851  1.00 29.95  ? 199 ARG   C C   1 
ATOM   6226 O  O   . ARG   C 1 194 ? 3.683   -4.839  25.998  1.00 30.28  ? 199 ARG   C O   1 
ATOM   6227 C  CB  . ARG   C 1 194 ? 3.966   -6.083  23.333  1.00 24.11  ? 199 ARG   C CB  1 
ATOM   6228 C  CG  . ARG   C 1 194 ? 2.616   -6.660  22.959  1.00 24.52  ? 199 ARG   C CG  1 
ATOM   6229 C  CD  . ARG   C 1 194 ? 2.254   -6.177  21.579  1.00 24.47  ? 199 ARG   C CD  1 
ATOM   6230 N  NE  . ARG   C 1 194 ? 0.921   -6.571  21.121  1.00 26.38  ? 199 ARG   C NE  1 
ATOM   6231 C  CZ  . ARG   C 1 194 ? 0.605   -7.780  20.661  1.00 26.99  ? 199 ARG   C CZ  1 
ATOM   6232 N  NH1 . ARG   C 1 194 ? 1.519   -8.750  20.629  1.00 25.79  ? 199 ARG   C NH1 1 
ATOM   6233 N  NH2 . ARG   C 1 194 ? -0.611  -8.021  20.205  1.00 25.91  ? 199 ARG   C NH2 1 
ATOM   6234 N  N   . ASP   C 1 195 ? 3.241   -6.940  26.707  1.00 27.50  ? 200 ASP   C N   1 
ATOM   6235 C  CA  . ASP   C 1 195 ? 2.507   -6.497  27.905  1.00 27.18  ? 200 ASP   C CA  1 
ATOM   6236 C  C   . ASP   C 1 195 ? 2.910   -7.422  29.069  1.00 31.25  ? 200 ASP   C C   1 
ATOM   6237 O  O   . ASP   C 1 195 ? 2.204   -8.382  29.387  1.00 31.99  ? 200 ASP   C O   1 
ATOM   6238 C  CB  . ASP   C 1 195 ? 1.004   -6.513  27.602  1.00 29.09  ? 200 ASP   C CB  1 
ATOM   6239 C  CG  . ASP   C 1 195 ? 0.079   -6.099  28.736  1.00 39.50  ? 200 ASP   C CG  1 
ATOM   6240 O  OD1 . ASP   C 1 195 ? 0.541   -5.383  29.646  1.00 40.89  ? 200 ASP   C OD1 1 
ATOM   6241 O  OD2 . ASP   C 1 195 ? -1.115  -6.497  28.705  1.00 39.37  ? 200 ASP   C OD2 1 
ATOM   6242 N  N   . VAL   C 1 196 ? 4.105   -7.172  29.626  1.00 28.86  ? 201 VAL   C N   1 
ATOM   6243 C  CA  . VAL   C 1 196 ? 4.756   -7.997  30.652  1.00 28.97  ? 201 VAL   C CA  1 
ATOM   6244 C  C   . VAL   C 1 196 ? 4.718   -7.272  32.014  1.00 33.44  ? 201 VAL   C C   1 
ATOM   6245 O  O   . VAL   C 1 196 ? 5.249   -6.168  32.143  1.00 32.11  ? 201 VAL   C O   1 
ATOM   6246 C  CB  . VAL   C 1 196 ? 6.216   -8.373  30.242  1.00 32.87  ? 201 VAL   C CB  1 
ATOM   6247 C  CG1 . VAL   C 1 196 ? 6.838   -9.357  31.225  1.00 32.41  ? 201 VAL   C CG1 1 
ATOM   6248 C  CG2 . VAL   C 1 196 ? 6.286   -8.949  28.822  1.00 32.98  ? 201 VAL   C CG2 1 
ATOM   6249 N  N   . ASP   C 1 197 ? 4.087   -7.902  33.020  1.00 31.29  ? 202 ASP   C N   1 
ATOM   6250 C  CA  . ASP   C 1 197 ? 3.987   -7.313  34.370  1.00 30.80  ? 202 ASP   C CA  1 
ATOM   6251 C  C   . ASP   C 1 197 ? 5.363   -7.282  35.034  1.00 33.97  ? 202 ASP   C C   1 
ATOM   6252 O  O   . ASP   C 1 197 ? 6.173   -8.153  34.743  1.00 32.88  ? 202 ASP   C O   1 
ATOM   6253 C  CB  . ASP   C 1 197 ? 3.027   -8.131  35.259  1.00 31.35  ? 202 ASP   C CB  1 
ATOM   6254 C  CG  . ASP   C 1 197 ? 1.589   -8.211  34.815  1.00 36.98  ? 202 ASP   C CG  1 
ATOM   6255 O  OD1 . ASP   C 1 197 ? 1.125   -7.285  34.096  1.00 38.25  ? 202 ASP   C OD1 1 
ATOM   6256 O  OD2 . ASP   C 1 197 ? 0.899   -9.164  35.231  1.00 39.37  ? 202 ASP   C OD2 1 
ATOM   6257 N  N   . PRO   C 1 198 ? 5.654   -6.330  35.962  1.00 31.96  ? 203 PRO   C N   1 
ATOM   6258 C  CA  . PRO   C 1 198 ? 6.989   -6.307  36.604  1.00 31.61  ? 203 PRO   C CA  1 
ATOM   6259 C  C   . PRO   C 1 198 ? 7.460   -7.641  37.237  1.00 34.67  ? 203 PRO   C C   1 
ATOM   6260 O  O   . PRO   C 1 198 ? 8.632   -8.004  37.004  1.00 33.99  ? 203 PRO   C O   1 
ATOM   6261 C  CB  . PRO   C 1 198 ? 6.877   -5.174  37.637  1.00 33.36  ? 203 PRO   C CB  1 
ATOM   6262 C  CG  . PRO   C 1 198 ? 5.783   -4.319  37.147  1.00 38.25  ? 203 PRO   C CG  1 
ATOM   6263 C  CD  . PRO   C 1 198 ? 4.821   -5.189  36.402  1.00 34.44  ? 203 PRO   C CD  1 
ATOM   6264 N  N   . PRO   C 1 199 ? 6.622   -8.419  37.985  1.00 33.12  ? 204 PRO   C N   1 
ATOM   6265 C  CA  . PRO   C 1 199 ? 7.114   -9.714  38.506  1.00 33.39  ? 204 PRO   C CA  1 
ATOM   6266 C  C   . PRO   C 1 199 ? 7.440   -10.718 37.394  1.00 36.31  ? 204 PRO   C C   1 
ATOM   6267 O  O   . PRO   C 1 199 ? 8.345   -11.531 37.556  1.00 35.70  ? 204 PRO   C O   1 
ATOM   6268 C  CB  . PRO   C 1 199 ? 5.962   -10.205 39.387  1.00 35.13  ? 204 PRO   C CB  1 
ATOM   6269 C  CG  . PRO   C 1 199 ? 4.767   -9.511  38.907  1.00 39.23  ? 204 PRO   C CG  1 
ATOM   6270 C  CD  . PRO   C 1 199 ? 5.222   -8.183  38.401  1.00 35.14  ? 204 PRO   C CD  1 
ATOM   6271 N  N   . GLU   C 1 200 ? 6.732   -10.626 36.251  1.00 32.83  ? 205 GLU   C N   1 
ATOM   6272 C  CA  . GLU   C 1 200 ? 6.977   -11.482 35.075  1.00 32.14  ? 205 GLU   C CA  1 
ATOM   6273 C  C   . GLU   C 1 200 ? 8.316   -11.142 34.455  1.00 35.77  ? 205 GLU   C C   1 
ATOM   6274 O  O   . GLU   C 1 200 ? 9.080   -12.060 34.157  1.00 35.00  ? 205 GLU   C O   1 
ATOM   6275 C  CB  . GLU   C 1 200 ? 5.869   -11.339 34.043  1.00 33.28  ? 205 GLU   C CB  1 
ATOM   6276 C  CG  . GLU   C 1 200 ? 4.528   -11.848 34.503  1.00 36.21  ? 205 GLU   C CG  1 
ATOM   6277 C  CD  . GLU   C 1 200 ? 3.468   -11.775 33.427  1.00 41.05  ? 205 GLU   C CD  1 
ATOM   6278 O  OE1 . GLU   C 1 200 ? 3.090   -10.646 33.036  1.00 37.40  ? 205 GLU   C OE1 1 
ATOM   6279 O  OE2 . GLU   C 1 200 ? 3.021   -12.849 32.966  1.00 33.79  ? 205 GLU   C OE2 1 
ATOM   6280 N  N   . HIS   C 1 201 ? 8.646   -9.828  34.309  1.00 30.99  ? 206 HIS   C N   1 
ATOM   6281 C  CA  . HIS   C 1 201 ? 9.948   -9.441  33.777  1.00 31.36  ? 206 HIS   C CA  1 
ATOM   6282 C  C   . HIS   C 1 201 ? 11.041  -9.960  34.700  1.00 36.31  ? 206 HIS   C C   1 
ATOM   6283 O  O   . HIS   C 1 201 ? 12.045  -10.494 34.220  1.00 35.65  ? 206 HIS   C O   1 
ATOM   6284 C  CB  . HIS   C 1 201 ? 10.056  -7.914  33.581  1.00 31.62  ? 206 HIS   C CB  1 
ATOM   6285 C  CG  . HIS   C 1 201 ? 11.346  -7.485  32.949  1.00 34.72  ? 206 HIS   C CG  1 
ATOM   6286 N  ND1 . HIS   C 1 201 ? 12.469  -7.212  33.705  1.00 36.29  ? 206 HIS   C ND1 1 
ATOM   6287 C  CD2 . HIS   C 1 201 ? 11.647  -7.314  31.641  1.00 35.60  ? 206 HIS   C CD2 1 
ATOM   6288 C  CE1 . HIS   C 1 201 ? 13.413  -6.877  32.840  1.00 35.28  ? 206 HIS   C CE1 1 
ATOM   6289 N  NE2 . HIS   C 1 201 ? 12.967  -6.927  31.588  1.00 35.80  ? 206 HIS   C NE2 1 
ATOM   6290 N  N   . PHE   C 1 202 ? 10.826  -9.841  36.042  1.00 34.38  ? 207 PHE   C N   1 
ATOM   6291 C  CA  . PHE   C 1 202 ? 11.769  -10.331 37.043  1.00 36.09  ? 207 PHE   C CA  1 
ATOM   6292 C  C   . PHE   C 1 202 ? 12.037  -11.830 36.835  1.00 37.30  ? 207 PHE   C C   1 
ATOM   6293 O  O   . PHE   C 1 202 ? 13.199  -12.226 36.827  1.00 37.95  ? 207 PHE   C O   1 
ATOM   6294 C  CB  . PHE   C 1 202 ? 11.245  -10.073 38.476  1.00 39.39  ? 207 PHE   C CB  1 
ATOM   6295 C  CG  . PHE   C 1 202 ? 12.148  -10.657 39.541  1.00 42.52  ? 207 PHE   C CG  1 
ATOM   6296 C  CD1 . PHE   C 1 202 ? 13.218  -9.926  40.045  1.00 46.41  ? 207 PHE   C CD1 1 
ATOM   6297 C  CD2 . PHE   C 1 202 ? 11.946  -11.949 40.018  1.00 45.29  ? 207 PHE   C CD2 1 
ATOM   6298 C  CE1 . PHE   C 1 202 ? 14.058  -10.469 41.023  1.00 47.61  ? 207 PHE   C CE1 1 
ATOM   6299 C  CE2 . PHE   C 1 202 ? 12.808  -12.502 40.971  1.00 48.52  ? 207 PHE   C CE2 1 
ATOM   6300 C  CZ  . PHE   C 1 202 ? 13.853  -11.756 41.470  1.00 46.49  ? 207 PHE   C CZ  1 
ATOM   6301 N  N   . ILE   C 1 203 ? 10.962  -12.635 36.662  1.00 33.98  ? 208 ILE   C N   1 
ATOM   6302 C  CA  . ILE   C 1 203 ? 10.987  -14.098 36.449  1.00 33.11  ? 208 ILE   C CA  1 
ATOM   6303 C  C   . ILE   C 1 203 ? 11.769  -14.434 35.183  1.00 38.42  ? 208 ILE   C C   1 
ATOM   6304 O  O   . ILE   C 1 203 ? 12.741  -15.193 35.242  1.00 38.39  ? 208 ILE   C O   1 
ATOM   6305 C  CB  . ILE   C 1 203 ? 9.565   -14.738 36.472  1.00 36.37  ? 208 ILE   C CB  1 
ATOM   6306 C  CG1 . ILE   C 1 203 ? 8.986   -14.740 37.907  1.00 36.21  ? 208 ILE   C CG1 1 
ATOM   6307 C  CG2 . ILE   C 1 203 ? 9.574   -16.177 35.897  1.00 36.33  ? 208 ILE   C CG2 1 
ATOM   6308 C  CD1 . ILE   C 1 203 ? 7.439   -14.833 37.993  1.00 39.72  ? 208 ILE   C CD1 1 
ATOM   6309 N  N   . LEU   C 1 204 ? 11.388  -13.815 34.049  1.00 34.73  ? 209 LEU   C N   1 
ATOM   6310 C  CA  . LEU   C 1 204 ? 12.081  -14.036 32.774  1.00 33.71  ? 209 LEU   C CA  1 
ATOM   6311 C  C   . LEU   C 1 204 ? 13.576  -13.798 32.888  1.00 38.79  ? 209 LEU   C C   1 
ATOM   6312 O  O   . LEU   C 1 204 ? 14.353  -14.664 32.488  1.00 38.37  ? 209 LEU   C O   1 
ATOM   6313 C  CB  . LEU   C 1 204 ? 11.478  -13.167 31.642  1.00 32.53  ? 209 LEU   C CB  1 
ATOM   6314 C  CG  . LEU   C 1 204 ? 10.017  -13.450 31.255  1.00 35.11  ? 209 LEU   C CG  1 
ATOM   6315 C  CD1 . LEU   C 1 204 ? 9.503   -12.427 30.222  1.00 35.01  ? 209 LEU   C CD1 1 
ATOM   6316 C  CD2 . LEU   C 1 204 ? 9.844   -14.868 30.705  1.00 34.44  ? 209 LEU   C CD2 1 
ATOM   6317 N  N   . LYS   C 1 205 ? 13.978  -12.659 33.478  1.00 37.54  ? 210 LYS   C N   1 
ATOM   6318 C  CA  . LYS   C 1 205 ? 15.386  -12.272 33.636  1.00 38.66  ? 210 LYS   C CA  1 
ATOM   6319 C  C   . LYS   C 1 205 ? 16.172  -13.087 34.659  1.00 43.62  ? 210 LYS   C C   1 
ATOM   6320 O  O   . LYS   C 1 205 ? 17.335  -13.405 34.403  1.00 41.87  ? 210 LYS   C O   1 
ATOM   6321 C  CB  . LYS   C 1 205 ? 15.520  -10.770 33.951  1.00 41.97  ? 210 LYS   C CB  1 
ATOM   6322 C  CG  . LYS   C 1 205 ? 15.237  -9.868  32.751  1.00 62.80  ? 210 LYS   C CG  1 
ATOM   6323 C  CD  . LYS   C 1 205 ? 16.408  -9.807  31.757  1.00 74.57  ? 210 LYS   C CD  1 
ATOM   6324 C  CE  . LYS   C 1 205 ? 16.007  -9.165  30.453  1.00 87.14  ? 210 LYS   C CE  1 
ATOM   6325 N  NZ  . LYS   C 1 205 ? 17.112  -9.199  29.457  1.00 98.43  ? 210 LYS   C NZ  1 
ATOM   6326 N  N   . ASN   C 1 206 ? 15.571  -13.389 35.824  1.00 41.79  ? 211 ASN   C N   1 
ATOM   6327 C  CA  . ASN   C 1 206 ? 16.307  -14.102 36.868  1.00 42.44  ? 211 ASN   C CA  1 
ATOM   6328 C  C   . ASN   C 1 206 ? 16.364  -15.616 36.636  1.00 47.15  ? 211 ASN   C C   1 
ATOM   6329 O  O   . ASN   C 1 206 ? 17.324  -16.246 37.083  1.00 48.11  ? 211 ASN   C O   1 
ATOM   6330 C  CB  . ASN   C 1 206 ? 15.798  -13.744 38.267  1.00 44.87  ? 211 ASN   C CB  1 
ATOM   6331 C  CG  . ASN   C 1 206 ? 16.295  -12.387 38.720  1.00 74.86  ? 211 ASN   C CG  1 
ATOM   6332 O  OD1 . ASN   C 1 206 ? 15.734  -11.337 38.371  1.00 70.17  ? 211 ASN   C OD1 1 
ATOM   6333 N  ND2 . ASN   C 1 206 ? 17.402  -12.371 39.451  1.00 66.41  ? 211 ASN   C ND2 1 
ATOM   6334 N  N   . TYR   C 1 207 ? 15.377  -16.188 35.918  1.00 42.84  ? 212 TYR   C N   1 
ATOM   6335 C  CA  . TYR   C 1 207 ? 15.339  -17.623 35.599  1.00 42.27  ? 212 TYR   C CA  1 
ATOM   6336 C  C   . TYR   C 1 207 ? 15.906  -17.950 34.192  1.00 46.24  ? 212 TYR   C C   1 
ATOM   6337 O  O   . TYR   C 1 207 ? 15.829  -19.104 33.763  1.00 44.95  ? 212 TYR   C O   1 
ATOM   6338 C  CB  . TYR   C 1 207 ? 13.925  -18.208 35.801  1.00 43.61  ? 212 TYR   C CB  1 
ATOM   6339 C  CG  . TYR   C 1 207 ? 13.481  -18.214 37.250  1.00 47.10  ? 212 TYR   C CG  1 
ATOM   6340 C  CD1 . TYR   C 1 207 ? 12.904  -17.086 37.829  1.00 49.55  ? 212 TYR   C CD1 1 
ATOM   6341 C  CD2 . TYR   C 1 207 ? 13.655  -19.341 38.049  1.00 48.46  ? 212 TYR   C CD2 1 
ATOM   6342 C  CE1 . TYR   C 1 207 ? 12.536  -17.069 39.174  1.00 52.42  ? 212 TYR   C CE1 1 
ATOM   6343 C  CE2 . TYR   C 1 207 ? 13.265  -19.346 39.389  1.00 49.30  ? 212 TYR   C CE2 1 
ATOM   6344 C  CZ  . TYR   C 1 207 ? 12.714  -18.205 39.950  1.00 57.32  ? 212 TYR   C CZ  1 
ATOM   6345 O  OH  . TYR   C 1 207 ? 12.326  -18.202 41.270  1.00 54.42  ? 212 TYR   C OH  1 
ATOM   6346 N  N   . ASP   C 1 208 ? 16.515  -16.944 33.502  1.00 43.53  ? 213 ASP   C N   1 
ATOM   6347 C  CA  . ASP   C 1 208 ? 17.135  -17.070 32.167  1.00 43.19  ? 213 ASP   C CA  1 
ATOM   6348 C  C   . ASP   C 1 208 ? 16.186  -17.578 31.063  1.00 43.02  ? 213 ASP   C C   1 
ATOM   6349 O  O   . ASP   C 1 208 ? 16.637  -18.305 30.173  1.00 44.35  ? 213 ASP   C O   1 
ATOM   6350 C  CB  . ASP   C 1 208 ? 18.398  -17.954 32.232  1.00 46.38  ? 213 ASP   C CB  1 
ATOM   6351 C  CG  . ASP   C 1 208 ? 19.649  -17.236 32.676  1.00 65.48  ? 213 ASP   C CG  1 
ATOM   6352 O  OD1 . ASP   C 1 208 ? 19.825  -17.057 33.901  1.00 67.45  ? 213 ASP   C OD1 1 
ATOM   6353 O  OD2 . ASP   C 1 208 ? 20.483  -16.906 31.803  1.00 75.75  ? 213 ASP   C OD2 1 
ATOM   6354 N  N   . ILE   C 1 209 ? 14.883  -17.227 31.123  1.00 35.67  ? 214 ILE   C N   1 
ATOM   6355 C  CA  . ILE   C 1 209 ? 13.908  -17.652 30.115  1.00 34.38  ? 214 ILE   C CA  1 
ATOM   6356 C  C   . ILE   C 1 209 ? 14.062  -16.742 28.901  1.00 38.02  ? 214 ILE   C C   1 
ATOM   6357 O  O   . ILE   C 1 209 ? 13.859  -15.534 29.012  1.00 36.40  ? 214 ILE   C O   1 
ATOM   6358 C  CB  . ILE   C 1 209 ? 12.443  -17.714 30.636  1.00 37.17  ? 214 ILE   C CB  1 
ATOM   6359 C  CG1 . ILE   C 1 209 ? 12.307  -18.705 31.826  1.00 37.15  ? 214 ILE   C CG1 1 
ATOM   6360 C  CG2 . ILE   C 1 209 ? 11.452  -18.070 29.507  1.00 38.48  ? 214 ILE   C CG2 1 
ATOM   6361 C  CD1 . ILE   C 1 209 ? 11.136  -18.435 32.731  1.00 35.40  ? 214 ILE   C CD1 1 
ATOM   6362 N  N   . GLN   C 1 210 ? 14.449  -17.324 27.761  1.00 34.88  ? 215 GLN   C N   1 
ATOM   6363 C  CA  . GLN   C 1 210 ? 14.689  -16.576 26.526  1.00 34.19  ? 215 GLN   C CA  1 
ATOM   6364 C  C   . GLN   C 1 210 ? 13.393  -16.149 25.884  1.00 33.11  ? 215 GLN   C C   1 
ATOM   6365 O  O   . GLN   C 1 210 ? 12.422  -16.904 25.869  1.00 32.98  ? 215 GLN   C O   1 
ATOM   6366 C  CB  . GLN   C 1 210 ? 15.573  -17.367 25.534  1.00 35.82  ? 215 GLN   C CB  1 
ATOM   6367 C  CG  . GLN   C 1 210 ? 16.912  -17.887 26.096  1.00 36.86  ? 215 GLN   C CG  1 
ATOM   6368 C  CD  . GLN   C 1 210 ? 17.795  -16.811 26.684  1.00 55.94  ? 215 GLN   C CD  1 
ATOM   6369 O  OE1 . GLN   C 1 210 ? 18.331  -15.950 25.977  1.00 47.86  ? 215 GLN   C OE1 1 
ATOM   6370 N  NE2 . GLN   C 1 210 ? 17.976  -16.843 28.002  1.00 51.33  ? 215 GLN   C NE2 1 
ATOM   6371 N  N   . TYR   C 1 211 ? 13.366  -14.914 25.354  1.00 29.36  ? 216 TYR   C N   1 
ATOM   6372 C  CA  . TYR   C 1 211 ? 12.161  -14.408 24.708  1.00 28.77  ? 216 TYR   C CA  1 
ATOM   6373 C  C   . TYR   C 1 211 ? 12.510  -13.440 23.599  1.00 29.10  ? 216 TYR   C C   1 
ATOM   6374 O  O   . TYR   C 1 211 ? 13.554  -12.793 23.647  1.00 30.02  ? 216 TYR   C O   1 
ATOM   6375 C  CB  . TYR   C 1 211 ? 11.227  -13.743 25.741  1.00 30.30  ? 216 TYR   C CB  1 
ATOM   6376 C  CG  . TYR   C 1 211 ? 11.822  -12.525 26.416  1.00 31.88  ? 216 TYR   C CG  1 
ATOM   6377 C  CD1 . TYR   C 1 211 ? 12.574  -12.646 27.584  1.00 33.38  ? 216 TYR   C CD1 1 
ATOM   6378 C  CD2 . TYR   C 1 211 ? 11.604  -11.245 25.910  1.00 33.34  ? 216 TYR   C CD2 1 
ATOM   6379 C  CE1 . TYR   C 1 211 ? 13.121  -11.530 28.214  1.00 35.16  ? 216 TYR   C CE1 1 
ATOM   6380 C  CE2 . TYR   C 1 211 ? 12.151  -10.118 26.532  1.00 34.61  ? 216 TYR   C CE2 1 
ATOM   6381 C  CZ  . TYR   C 1 211 ? 12.908  -10.267 27.684  1.00 40.67  ? 216 TYR   C CZ  1 
ATOM   6382 O  OH  . TYR   C 1 211 ? 13.438  -9.165  28.318  1.00 42.45  ? 216 TYR   C OH  1 
ATOM   6383 N  N   . PHE   C 1 212 ? 11.621  -13.335 22.620  1.00 25.98  ? 217 PHE   C N   1 
ATOM   6384 C  CA  . PHE   C 1 212 ? 11.734  -12.396 21.510  1.00 24.57  ? 217 PHE   C CA  1 
ATOM   6385 C  C   . PHE   C 1 212 ? 10.510  -11.512 21.607  1.00 26.67  ? 217 PHE   C C   1 
ATOM   6386 O  O   . PHE   C 1 212 ? 9.419   -11.900 21.172  1.00 25.27  ? 217 PHE   C O   1 
ATOM   6387 C  CB  . PHE   C 1 212 ? 11.788  -13.150 20.175  1.00 25.67  ? 217 PHE   C CB  1 
ATOM   6388 C  CG  . PHE   C 1 212 ? 13.040  -13.964 20.075  1.00 26.10  ? 217 PHE   C CG  1 
ATOM   6389 C  CD1 . PHE   C 1 212 ? 14.236  -13.379 19.682  1.00 28.76  ? 217 PHE   C CD1 1 
ATOM   6390 C  CD2 . PHE   C 1 212 ? 13.036  -15.319 20.403  1.00 27.40  ? 217 PHE   C CD2 1 
ATOM   6391 C  CE1 . PHE   C 1 212 ? 15.410  -14.128 19.612  1.00 29.60  ? 217 PHE   C CE1 1 
ATOM   6392 C  CE2 . PHE   C 1 212 ? 14.221  -16.061 20.380  1.00 30.15  ? 217 PHE   C CE2 1 
ATOM   6393 C  CZ  . PHE   C 1 212 ? 15.399  -15.461 19.985  1.00 29.86  ? 217 PHE   C CZ  1 
ATOM   6394 N  N   . SER   C 1 213 ? 10.673  -10.356 22.265  1.00 26.04  ? 218 SER   C N   1 
ATOM   6395 C  CA  . SER   C 1 213 ? 9.571   -9.404  22.403  1.00 24.46  ? 218 SER   C CA  1 
ATOM   6396 C  C   . SER   C 1 213 ? 9.285   -8.779  21.015  1.00 26.66  ? 218 SER   C C   1 
ATOM   6397 O  O   . SER   C 1 213 ? 10.055  -8.978  20.065  1.00 24.81  ? 218 SER   C O   1 
ATOM   6398 C  CB  . SER   C 1 213 ? 9.979   -8.276  23.352  1.00 25.99  ? 218 SER   C CB  1 
ATOM   6399 O  OG  . SER   C 1 213 ? 10.917  -7.410  22.725  1.00 26.17  ? 218 SER   C OG  1 
ATOM   6400 N  N   . MET   C 1 214 ? 8.237   -7.945  20.922  1.00 23.40  ? 219 MET   C N   1 
ATOM   6401 C  CA  . MET   C 1 214 ? 7.975   -7.206  19.677  1.00 21.81  ? 219 MET   C CA  1 
ATOM   6402 C  C   . MET   C 1 214 ? 9.168   -6.342  19.293  1.00 25.75  ? 219 MET   C C   1 
ATOM   6403 O  O   . MET   C 1 214 ? 9.410   -6.164  18.102  1.00 25.33  ? 219 MET   C O   1 
ATOM   6404 C  CB  . MET   C 1 214 ? 6.735   -6.303  19.793  1.00 23.06  ? 219 MET   C CB  1 
ATOM   6405 C  CG  . MET   C 1 214 ? 5.407   -7.046  19.912  1.00 24.65  ? 219 MET   C CG  1 
ATOM   6406 S  SD  . MET   C 1 214 ? 5.110   -8.421  18.731  1.00 25.48  ? 219 MET   C SD  1 
ATOM   6407 C  CE  . MET   C 1 214 ? 5.370   -7.566  17.145  1.00 23.70  ? 219 MET   C CE  1 
ATOM   6408 N  N   . ARG   C 1 215 ? 9.917   -5.823  20.296  1.00 23.43  ? 220 ARG   C N   1 
ATOM   6409 C  CA  . ARG   C 1 215 ? 11.088  -4.991  20.042  1.00 23.45  ? 220 ARG   C CA  1 
ATOM   6410 C  C   . ARG   C 1 215 ? 12.235  -5.846  19.417  1.00 25.50  ? 220 ARG   C C   1 
ATOM   6411 O  O   . ARG   C 1 215 ? 12.879  -5.394  18.462  1.00 23.05  ? 220 ARG   C O   1 
ATOM   6412 C  CB  . ARG   C 1 215 ? 11.519  -4.294  21.326  1.00 24.37  ? 220 ARG   C CB  1 
ATOM   6413 C  CG  . ARG   C 1 215 ? 12.806  -3.540  21.145  1.00 24.78  ? 220 ARG   C CG  1 
ATOM   6414 C  CD  . ARG   C 1 215 ? 13.331  -3.038  22.449  1.00 32.41  ? 220 ARG   C CD  1 
ATOM   6415 N  NE  . ARG   C 1 215 ? 14.758  -2.808  22.305  1.00 33.23  ? 220 ARG   C NE  1 
ATOM   6416 C  CZ  . ARG   C 1 215 ? 15.307  -1.658  21.946  1.00 50.38  ? 220 ARG   C CZ  1 
ATOM   6417 N  NH1 . ARG   C 1 215 ? 14.539  -0.593  21.685  1.00 32.42  ? 220 ARG   C NH1 1 
ATOM   6418 N  NH2 . ARG   C 1 215 ? 16.627  -1.558  21.837  1.00 39.05  ? 220 ARG   C NH2 1 
ATOM   6419 N  N   . ASP   C 1 216 ? 12.405  -7.119  19.883  1.00 23.42  ? 221 ASP   C N   1 
ATOM   6420 C  CA  . ASP   C 1 216 ? 13.384  -8.025  19.287  1.00 23.14  ? 221 ASP   C CA  1 
ATOM   6421 C  C   . ASP   C 1 216 ? 12.994  -8.326  17.839  1.00 25.11  ? 221 ASP   C C   1 
ATOM   6422 O  O   . ASP   C 1 216 ? 13.872  -8.432  17.005  1.00 25.30  ? 221 ASP   C O   1 
ATOM   6423 C  CB  . ASP   C 1 216 ? 13.501  -9.336  20.067  1.00 24.50  ? 221 ASP   C CB  1 
ATOM   6424 C  CG  . ASP   C 1 216 ? 14.060  -9.108  21.445  1.00 28.73  ? 221 ASP   C CG  1 
ATOM   6425 O  OD1 . ASP   C 1 216 ? 15.132  -8.499  21.543  1.00 31.50  ? 221 ASP   C OD1 1 
ATOM   6426 O  OD2 . ASP   C 1 216 ? 13.409  -9.528  22.430  1.00 32.30  ? 221 ASP   C OD2 1 
ATOM   6427 N  N   . ILE   C 1 217 ? 11.676  -8.496  17.552  1.00 21.70  ? 222 ILE   C N   1 
ATOM   6428 C  CA  . ILE   C 1 217 ? 11.184  -8.735  16.190  1.00 21.71  ? 222 ILE   C CA  1 
ATOM   6429 C  C   . ILE   C 1 217 ? 11.474  -7.493  15.311  1.00 24.24  ? 222 ILE   C C   1 
ATOM   6430 O  O   . ILE   C 1 217 ? 11.936  -7.646  14.178  1.00 23.85  ? 222 ILE   C O   1 
ATOM   6431 C  CB  . ILE   C 1 217 ? 9.678   -9.150  16.170  1.00 23.69  ? 222 ILE   C CB  1 
ATOM   6432 C  CG1 . ILE   C 1 217 ? 9.449   -10.415 17.073  1.00 23.49  ? 222 ILE   C CG1 1 
ATOM   6433 C  CG2 . ILE   C 1 217 ? 9.173   -9.398  14.739  1.00 23.39  ? 222 ILE   C CG2 1 
ATOM   6434 C  CD1 . ILE   C 1 217 ? 7.916   -10.797 17.234  1.00 26.15  ? 222 ILE   C CD1 1 
ATOM   6435 N  N   . ASP   C 1 218 ? 11.238  -6.273  15.848  1.00 22.67  ? 223 ASP   C N   1 
ATOM   6436 C  CA  . ASP   C 1 218 ? 11.504  -5.019  15.125  1.00 21.90  ? 223 ASP   C CA  1 
ATOM   6437 C  C   . ASP   C 1 218 ? 12.969  -4.938  14.734  1.00 25.23  ? 223 ASP   C C   1 
ATOM   6438 O  O   . ASP   C 1 218 ? 13.276  -4.424  13.668  1.00 26.89  ? 223 ASP   C O   1 
ATOM   6439 C  CB  . ASP   C 1 218 ? 11.163  -3.785  15.979  1.00 22.41  ? 223 ASP   C CB  1 
ATOM   6440 C  CG  . ASP   C 1 218 ? 9.691   -3.624  16.291  1.00 23.75  ? 223 ASP   C CG  1 
ATOM   6441 O  OD1 . ASP   C 1 218 ? 8.867   -4.171  15.542  1.00 23.92  ? 223 ASP   C OD1 1 
ATOM   6442 O  OD2 . ASP   C 1 218 ? 9.366   -2.965  17.320  1.00 25.36  ? 223 ASP   C OD2 1 
ATOM   6443 N  N   . ARG   C 1 219 ? 13.859  -5.450  15.589  1.00 23.30  ? 224 ARG   C N   1 
ATOM   6444 C  CA  . ARG   C 1 219 ? 15.311  -5.398  15.350  1.00 24.05  ? 224 ARG   C CA  1 
ATOM   6445 C  C   . ARG   C 1 219 ? 15.813  -6.473  14.382  1.00 27.53  ? 224 ARG   C C   1 
ATOM   6446 O  O   . ARG   C 1 219 ? 16.469  -6.172  13.374  1.00 27.82  ? 224 ARG   C O   1 
ATOM   6447 C  CB  . ARG   C 1 219 ? 16.060  -5.488  16.681  1.00 24.19  ? 224 ARG   C CB  1 
ATOM   6448 C  CG  . ARG   C 1 219 ? 15.912  -4.236  17.552  1.00 27.22  ? 224 ARG   C CG  1 
ATOM   6449 C  CD  . ARG   C 1 219 ? 16.487  -4.386  18.960  1.00 32.98  ? 224 ARG   C CD  1 
ATOM   6450 N  NE  . ARG   C 1 219 ? 17.869  -4.886  18.950  1.00 32.20  ? 224 ARG   C NE  1 
ATOM   6451 C  CZ  . ARG   C 1 219 ? 18.956  -4.129  18.807  1.00 45.34  ? 224 ARG   C CZ  1 
ATOM   6452 N  NH1 . ARG   C 1 219 ? 18.846  -2.814  18.647  1.00 31.08  ? 224 ARG   C NH1 1 
ATOM   6453 N  NH2 . ARG   C 1 219 ? 20.159  -4.683  18.808  1.00 34.34  ? 224 ARG   C NH2 1 
ATOM   6454 N  N   . LEU   C 1 220 ? 15.521  -7.734  14.715  1.00 24.11  ? 225 LEU   C N   1 
ATOM   6455 C  CA  . LEU   C 1 220 ? 15.974  -8.897  13.969  1.00 24.23  ? 225 LEU   C CA  1 
ATOM   6456 C  C   . LEU   C 1 220 ? 15.207  -9.269  12.736  1.00 27.56  ? 225 LEU   C C   1 
ATOM   6457 O  O   . LEU   C 1 220 ? 15.788  -9.830  11.808  1.00 27.99  ? 225 LEU   C O   1 
ATOM   6458 C  CB  . LEU   C 1 220 ? 15.942  -10.096 14.931  1.00 24.73  ? 225 LEU   C CB  1 
ATOM   6459 C  CG  . LEU   C 1 220 ? 16.941  -10.092 16.067  1.00 28.93  ? 225 LEU   C CG  1 
ATOM   6460 C  CD1 . LEU   C 1 220 ? 16.538  -11.128 17.131  1.00 29.00  ? 225 LEU   C CD1 1 
ATOM   6461 C  CD2 . LEU   C 1 220 ? 18.357  -10.377 15.548  1.00 34.50  ? 225 LEU   C CD2 1 
ATOM   6462 N  N   . GLY   C 1 221 ? 13.894  -9.084  12.783  1.00 24.24  ? 226 GLY   C N   1 
ATOM   6463 C  CA  . GLY   C 1 221 ? 12.987  -9.590  11.768  1.00 23.99  ? 226 GLY   C CA  1 
ATOM   6464 C  C   . GLY   C 1 221 ? 12.572  -11.003 12.146  1.00 26.73  ? 226 GLY   C C   1 
ATOM   6465 O  O   . GLY   C 1 221 ? 13.342  -11.724 12.803  1.00 25.67  ? 226 GLY   C O   1 
ATOM   6466 N  N   . ILE   C 1 222 ? 11.345  -11.404 11.767  1.00 23.87  ? 227 ILE   C N   1 
ATOM   6467 C  CA  . ILE   C 1 222 ? 10.813  -12.710 12.148  1.00 23.24  ? 227 ILE   C CA  1 
ATOM   6468 C  C   . ILE   C 1 222 ? 11.682  -13.917 11.659  1.00 27.66  ? 227 ILE   C C   1 
ATOM   6469 O  O   . ILE   C 1 222 ? 11.732  -14.928 12.368  1.00 25.91  ? 227 ILE   C O   1 
ATOM   6470 C  CB  . ILE   C 1 222 ? 9.326   -12.843 11.732  1.00 25.36  ? 227 ILE   C CB  1 
ATOM   6471 C  CG1 . ILE   C 1 222 ? 8.611   -13.967 12.536  1.00 24.71  ? 227 ILE   C CG1 1 
ATOM   6472 C  CG2 . ILE   C 1 222 ? 9.156   -13.012 10.197  1.00 26.81  ? 227 ILE   C CG2 1 
ATOM   6473 C  CD1 . ILE   C 1 222 ? 8.502   -13.672 14.096  1.00 29.54  ? 227 ILE   C CD1 1 
ATOM   6474 N  N   . GLN   C 1 223 ? 12.364  -13.811 10.487  1.00 23.89  ? 228 GLN   C N   1 
ATOM   6475 C  CA  . GLN   C 1 223 ? 13.203  -14.944 10.005  1.00 24.33  ? 228 GLN   C CA  1 
ATOM   6476 C  C   . GLN   C 1 223 ? 14.308  -15.257 11.036  1.00 27.93  ? 228 GLN   C C   1 
ATOM   6477 O  O   . GLN   C 1 223 ? 14.416  -16.406 11.505  1.00 26.98  ? 228 GLN   C O   1 
ATOM   6478 C  CB  . GLN   C 1 223 ? 13.825  -14.659 8.610   1.00 25.77  ? 228 GLN   C CB  1 
ATOM   6479 C  CG  . GLN   C 1 223 ? 14.951  -15.694 8.238   1.00 31.88  ? 228 GLN   C CG  1 
ATOM   6480 C  CD  . GLN   C 1 223 ? 15.832  -15.354 7.043   1.00 44.68  ? 228 GLN   C CD  1 
ATOM   6481 O  OE1 . GLN   C 1 223 ? 16.851  -16.018 6.769   1.00 40.69  ? 228 GLN   C OE1 1 
ATOM   6482 N  NE2 . GLN   C 1 223 ? 15.477  -14.341 6.286   1.00 32.40  ? 228 GLN   C NE2 1 
ATOM   6483 N  N   . LYS   C 1 224 ? 15.064  -14.222 11.442  1.00 24.28  ? 229 LYS   C N   1 
ATOM   6484 C  CA  . LYS   C 1 224 ? 16.115  -14.382 12.447  1.00 25.32  ? 229 LYS   C CA  1 
ATOM   6485 C  C   . LYS   C 1 224 ? 15.576  -14.816 13.814  1.00 28.74  ? 229 LYS   C C   1 
ATOM   6486 O  O   . LYS   C 1 224 ? 16.259  -15.559 14.530  1.00 29.50  ? 229 LYS   C O   1 
ATOM   6487 C  CB  . LYS   C 1 224 ? 16.972  -13.134 12.583  1.00 28.14  ? 229 LYS   C CB  1 
ATOM   6488 C  CG  . LYS   C 1 224 ? 17.952  -12.968 11.423  1.00 36.92  ? 229 LYS   C CG  1 
ATOM   6489 C  CD  . LYS   C 1 224 ? 18.928  -11.836 11.715  1.00 55.61  ? 229 LYS   C CD  1 
ATOM   6490 C  CE  . LYS   C 1 224 ? 20.176  -11.913 10.873  1.00 71.96  ? 229 LYS   C CE  1 
ATOM   6491 N  NZ  . LYS   C 1 224 ? 21.318  -11.234 11.542  1.00 85.65  ? 229 LYS   C NZ  1 
ATOM   6492 N  N   . VAL   C 1 225 ? 14.362  -14.342 14.188  1.00 24.14  ? 230 VAL   C N   1 
ATOM   6493 C  CA  . VAL   C 1 225 ? 13.736  -14.727 15.465  1.00 23.62  ? 230 VAL   C CA  1 
ATOM   6494 C  C   . VAL   C 1 225 ? 13.499  -16.260 15.482  1.00 26.74  ? 230 VAL   C C   1 
ATOM   6495 O  O   . VAL   C 1 225 ? 13.831  -16.933 16.474  1.00 27.23  ? 230 VAL   C O   1 
ATOM   6496 C  CB  . VAL   C 1 225 ? 12.444  -13.920 15.735  1.00 26.84  ? 230 VAL   C CB  1 
ATOM   6497 C  CG1 . VAL   C 1 225 ? 11.574  -14.589 16.800  1.00 26.67  ? 230 VAL   C CG1 1 
ATOM   6498 C  CG2 . VAL   C 1 225 ? 12.806  -12.490 16.143  1.00 26.28  ? 230 VAL   C CG2 1 
ATOM   6499 N  N   . MET   C 1 226 ? 12.974  -16.799 14.373  1.00 23.96  ? 231 MET   C N   1 
ATOM   6500 C  CA  . MET   C 1 226 ? 12.722  -18.240 14.259  1.00 23.92  ? 231 MET   C CA  1 
ATOM   6501 C  C   . MET   C 1 226 ? 14.010  -19.050 14.272  1.00 29.51  ? 231 MET   C C   1 
ATOM   6502 O  O   . MET   C 1 226 ? 14.052  -20.095 14.931  1.00 28.39  ? 231 MET   C O   1 
ATOM   6503 C  CB  . MET   C 1 226 ? 11.847  -18.584 13.054  1.00 25.19  ? 231 MET   C CB  1 
ATOM   6504 C  CG  . MET   C 1 226 ? 10.416  -18.059 13.160  1.00 27.36  ? 231 MET   C CG  1 
ATOM   6505 S  SD  . MET   C 1 226 ? 9.603   -18.220 14.787  1.00 29.13  ? 231 MET   C SD  1 
ATOM   6506 C  CE  . MET   C 1 226 ? 9.402   -20.061 14.890  1.00 27.19  ? 231 MET   C CE  1 
ATOM   6507 N  N   . GLU   C 1 227 ? 15.049  -18.572 13.573  1.00 27.70  ? 232 GLU   C N   1 
ATOM   6508 C  CA  . GLU   C 1 227 ? 16.350  -19.255 13.526  1.00 28.24  ? 232 GLU   C CA  1 
ATOM   6509 C  C   . GLU   C 1 227 ? 16.930  -19.363 14.925  1.00 33.96  ? 232 GLU   C C   1 
ATOM   6510 O  O   . GLU   C 1 227 ? 17.324  -20.457 15.351  1.00 33.00  ? 232 GLU   C O   1 
ATOM   6511 C  CB  . GLU   C 1 227 ? 17.342  -18.539 12.599  1.00 29.40  ? 232 GLU   C CB  1 
ATOM   6512 C  CG  . GLU   C 1 227 ? 17.027  -18.679 11.117  1.00 34.59  ? 232 GLU   C CG  1 
ATOM   6513 C  CD  . GLU   C 1 227 ? 17.799  -17.755 10.185  1.00 45.34  ? 232 GLU   C CD  1 
ATOM   6514 O  OE1 . GLU   C 1 227 ? 18.524  -16.859 10.680  1.00 40.01  ? 232 GLU   C OE1 1 
ATOM   6515 O  OE2 . GLU   C 1 227 ? 17.672  -17.922 8.950   1.00 38.79  ? 232 GLU   C OE2 1 
ATOM   6516 N  N   . ARG   C 1 228 ? 16.905  -18.237 15.669  1.00 29.18  ? 233 ARG   C N   1 
ATOM   6517 C  CA  . ARG   C 1 228 ? 17.413  -18.175 17.035  1.00 29.70  ? 233 ARG   C CA  1 
ATOM   6518 C  C   . ARG   C 1 228 ? 16.564  -19.000 18.018  1.00 33.18  ? 233 ARG   C C   1 
ATOM   6519 O  O   . ARG   C 1 228 ? 17.139  -19.632 18.905  1.00 33.77  ? 233 ARG   C O   1 
ATOM   6520 C  CB  . ARG   C 1 228 ? 17.591  -16.722 17.478  1.00 31.47  ? 233 ARG   C CB  1 
ATOM   6521 C  CG  . ARG   C 1 228 ? 18.731  -16.037 16.730  1.00 34.00  ? 233 ARG   C CG  1 
ATOM   6522 C  CD  . ARG   C 1 228 ? 18.926  -14.614 17.193  1.00 40.00  ? 233 ARG   C CD  1 
ATOM   6523 N  NE  . ARG   C 1 228 ? 19.955  -13.931 16.418  1.00 53.36  ? 233 ARG   C NE  1 
ATOM   6524 C  CZ  . ARG   C 1 228 ? 20.619  -12.860 16.837  1.00 66.00  ? 233 ARG   C CZ  1 
ATOM   6525 N  NH1 . ARG   C 1 228 ? 20.362  -12.335 18.029  1.00 47.92  ? 233 ARG   C NH1 1 
ATOM   6526 N  NH2 . ARG   C 1 228 ? 21.540  -12.301 16.065  1.00 61.05  ? 233 ARG   C NH2 1 
ATOM   6527 N  N   . THR   C 1 229 ? 15.225  -19.020 17.848  1.00 29.44  ? 234 THR   C N   1 
ATOM   6528 C  CA  . THR   C 1 229 ? 14.284  -19.813 18.654  1.00 28.22  ? 234 THR   C CA  1 
ATOM   6529 C  C   . THR   C 1 229 ? 14.660  -21.317 18.528  1.00 33.80  ? 234 THR   C C   1 
ATOM   6530 O  O   . THR   C 1 229 ? 14.845  -21.988 19.546  1.00 34.23  ? 234 THR   C O   1 
ATOM   6531 C  CB  . THR   C 1 229 ? 12.829  -19.551 18.208  1.00 33.44  ? 234 THR   C CB  1 
ATOM   6532 O  OG1 . THR   C 1 229 ? 12.490  -18.207 18.568  1.00 28.59  ? 234 THR   C OG1 1 
ATOM   6533 C  CG2 . THR   C 1 229 ? 11.816  -20.498 18.862  1.00 30.51  ? 234 THR   C CG2 1 
ATOM   6534 N  N   . PHE   C 1 230 ? 14.817  -21.804 17.284  1.00 28.86  ? 235 PHE   C N   1 
ATOM   6535 C  CA  . PHE   C 1 230 ? 15.182  -23.204 17.028  1.00 28.82  ? 235 PHE   C CA  1 
ATOM   6536 C  C   . PHE   C 1 230 ? 16.606  -23.507 17.478  1.00 34.19  ? 235 PHE   C C   1 
ATOM   6537 O  O   . PHE   C 1 230 ? 16.844  -24.597 17.995  1.00 35.89  ? 235 PHE   C O   1 
ATOM   6538 C  CB  . PHE   C 1 230 ? 14.914  -23.613 15.573  1.00 29.90  ? 235 PHE   C CB  1 
ATOM   6539 C  CG  . PHE   C 1 230 ? 13.478  -23.492 15.106  1.00 31.42  ? 235 PHE   C CG  1 
ATOM   6540 C  CD1 . PHE   C 1 230 ? 12.422  -23.867 15.930  1.00 34.35  ? 235 PHE   C CD1 1 
ATOM   6541 C  CD2 . PHE   C 1 230 ? 13.184  -23.051 13.819  1.00 33.97  ? 235 PHE   C CD2 1 
ATOM   6542 C  CE1 . PHE   C 1 230 ? 11.099  -23.779 15.484  1.00 35.91  ? 235 PHE   C CE1 1 
ATOM   6543 C  CE2 . PHE   C 1 230 ? 11.862  -22.960 13.379  1.00 36.83  ? 235 PHE   C CE2 1 
ATOM   6544 C  CZ  . PHE   C 1 230 ? 10.827  -23.315 14.213  1.00 34.99  ? 235 PHE   C CZ  1 
ATOM   6545 N  N   . ASP   C 1 231 ? 17.529  -22.543 17.378  1.00 31.93  ? 236 ASP   C N   1 
ATOM   6546 C  CA  . ASP   C 1 231 ? 18.895  -22.699 17.883  1.00 32.31  ? 236 ASP   C CA  1 
ATOM   6547 C  C   . ASP   C 1 231 ? 18.862  -22.986 19.398  1.00 38.81  ? 236 ASP   C C   1 
ATOM   6548 O  O   . ASP   C 1 231 ? 19.595  -23.848 19.888  1.00 38.95  ? 236 ASP   C O   1 
ATOM   6549 C  CB  . ASP   C 1 231 ? 19.737  -21.438 17.637  1.00 34.48  ? 236 ASP   C CB  1 
ATOM   6550 C  CG  . ASP   C 1 231 ? 20.260  -21.222 16.223  1.00 45.40  ? 236 ASP   C CG  1 
ATOM   6551 O  OD1 . ASP   C 1 231 ? 20.325  -22.205 15.452  1.00 46.34  ? 236 ASP   C OD1 1 
ATOM   6552 O  OD2 . ASP   C 1 231 ? 20.666  -20.082 15.912  1.00 54.35  ? 236 ASP   C OD2 1 
ATOM   6553 N  N   . LEU   C 1 232 ? 18.013  -22.249 20.131  1.00 34.47  ? 237 LEU   C N   1 
ATOM   6554 C  CA  . LEU   C 1 232 ? 17.892  -22.381 21.581  1.00 33.38  ? 237 LEU   C CA  1 
ATOM   6555 C  C   . LEU   C 1 232 ? 17.258  -23.684 22.012  1.00 37.58  ? 237 LEU   C C   1 
ATOM   6556 O  O   . LEU   C 1 232 ? 17.724  -24.297 22.982  1.00 38.31  ? 237 LEU   C O   1 
ATOM   6557 C  CB  . LEU   C 1 232 ? 17.095  -21.201 22.157  1.00 32.65  ? 237 LEU   C CB  1 
ATOM   6558 C  CG  . LEU   C 1 232 ? 17.780  -19.833 22.095  1.00 35.96  ? 237 LEU   C CG  1 
ATOM   6559 C  CD1 . LEU   C 1 232 ? 16.757  -18.718 22.241  1.00 34.93  ? 237 LEU   C CD1 1 
ATOM   6560 C  CD2 . LEU   C 1 232 ? 18.916  -19.704 23.124  1.00 36.86  ? 237 LEU   C CD2 1 
ATOM   6561 N  N   . LEU   C 1 233 ? 16.180  -24.092 21.317  1.00 32.59  ? 238 LEU   C N   1 
ATOM   6562 C  CA  . LEU   C 1 233 ? 15.397  -25.265 21.667  1.00 31.81  ? 238 LEU   C CA  1 
ATOM   6563 C  C   . LEU   C 1 233 ? 15.928  -26.564 21.084  1.00 38.47  ? 238 LEU   C C   1 
ATOM   6564 O  O   . LEU   C 1 233 ? 16.074  -27.527 21.832  1.00 37.82  ? 238 LEU   C O   1 
ATOM   6565 C  CB  . LEU   C 1 233 ? 13.914  -25.066 21.310  1.00 31.04  ? 238 LEU   C CB  1 
ATOM   6566 C  CG  . LEU   C 1 233 ? 13.197  -23.866 22.001  1.00 33.25  ? 238 LEU   C CG  1 
ATOM   6567 C  CD1 . LEU   C 1 233 ? 11.779  -23.781 21.578  1.00 31.97  ? 238 LEU   C CD1 1 
ATOM   6568 C  CD2 . LEU   C 1 233 ? 13.194  -24.032 23.525  1.00 34.78  ? 238 LEU   C CD2 1 
ATOM   6569 N  N   . ILE   C 1 234 ? 16.218  -26.592 19.762  1.00 34.55  ? 239 ILE   C N   1 
ATOM   6570 C  CA  . ILE   C 1 234 ? 16.632  -27.803 19.040  1.00 33.34  ? 239 ILE   C CA  1 
ATOM   6571 C  C   . ILE   C 1 234 ? 18.022  -27.697 18.375  1.00 37.69  ? 239 ILE   C C   1 
ATOM   6572 O  O   . ILE   C 1 234 ? 18.322  -28.460 17.442  1.00 37.69  ? 239 ILE   C O   1 
ATOM   6573 C  CB  . ILE   C 1 234 ? 15.508  -28.226 18.037  1.00 35.17  ? 239 ILE   C CB  1 
ATOM   6574 C  CG1 . ILE   C 1 234 ? 15.252  -27.144 16.927  1.00 34.15  ? 239 ILE   C CG1 1 
ATOM   6575 C  CG2 . ILE   C 1 234 ? 14.210  -28.609 18.772  1.00 34.04  ? 239 ILE   C CG2 1 
ATOM   6576 C  CD1 . ILE   C 1 234 ? 14.212  -27.508 15.861  1.00 38.80  ? 239 ILE   C CD1 1 
ATOM   6577 N  N   . GLY   C 1 235 ? 18.891  -26.849 18.923  1.00 33.86  ? 240 GLY   C N   1 
ATOM   6578 C  CA  . GLY   C 1 235 ? 20.254  -26.669 18.425  1.00 34.67  ? 240 GLY   C CA  1 
ATOM   6579 C  C   . GLY   C 1 235 ? 21.184  -27.845 18.697  1.00 42.41  ? 240 GLY   C C   1 
ATOM   6580 O  O   . GLY   C 1 235 ? 22.146  -28.075 17.952  1.00 43.05  ? 240 GLY   C O   1 
ATOM   6581 N  N   . LYS   C 1 236 ? 20.895  -28.594 19.768  1.00 39.09  ? 241 LYS   C N   1 
ATOM   6582 C  CA  . LYS   C 1 236 ? 21.703  -29.732 20.198  1.00 39.23  ? 241 LYS   C CA  1 
ATOM   6583 C  C   . LYS   C 1 236 ? 21.137  -31.067 19.736  1.00 41.84  ? 241 LYS   C C   1 
ATOM   6584 O  O   . LYS   C 1 236 ? 21.918  -31.991 19.504  1.00 41.49  ? 241 LYS   C O   1 
ATOM   6585 C  CB  . LYS   C 1 236 ? 21.916  -29.701 21.721  1.00 43.38  ? 241 LYS   C CB  1 
ATOM   6586 C  CG  . LYS   C 1 236 ? 22.972  -28.681 22.147  1.00 55.90  ? 241 LYS   C CG  1 
ATOM   6587 C  CD  . LYS   C 1 236 ? 23.105  -28.598 23.663  1.00 70.47  ? 241 LYS   C CD  1 
ATOM   6588 C  CE  . LYS   C 1 236 ? 24.084  -27.534 24.109  1.00 84.52  ? 241 LYS   C CE  1 
ATOM   6589 N  NZ  . LYS   C 1 236 ? 25.493  -27.895 23.789  1.00 92.62  ? 241 LYS   C NZ  1 
ATOM   6590 N  N   . ARG   C 1 237 ? 19.799  -31.168 19.593  1.00 37.72  ? 242 ARG   C N   1 
ATOM   6591 C  CA  . ARG   C 1 237 ? 19.089  -32.379 19.161  1.00 37.82  ? 242 ARG   C CA  1 
ATOM   6592 C  C   . ARG   C 1 237 ? 17.652  -32.068 18.773  1.00 40.82  ? 242 ARG   C C   1 
ATOM   6593 O  O   . ARG   C 1 237 ? 17.119  -31.034 19.186  1.00 40.20  ? 242 ARG   C O   1 
ATOM   6594 C  CB  . ARG   C 1 237 ? 19.115  -33.449 20.284  1.00 37.21  ? 242 ARG   C CB  1 
ATOM   6595 C  CG  . ARG   C 1 237 ? 18.079  -33.213 21.381  1.00 41.16  ? 242 ARG   C CG  1 
ATOM   6596 C  CD  . ARG   C 1 237 ? 18.419  -33.891 22.684  1.00 43.09  ? 242 ARG   C CD  1 
ATOM   6597 N  NE  . ARG   C 1 237 ? 17.651  -33.270 23.759  1.00 43.17  ? 242 ARG   C NE  1 
ATOM   6598 C  CZ  . ARG   C 1 237 ? 18.137  -32.387 24.619  1.00 43.14  ? 242 ARG   C CZ  1 
ATOM   6599 N  NH1 . ARG   C 1 237 ? 19.423  -32.066 24.594  1.00 36.10  ? 242 ARG   C NH1 1 
ATOM   6600 N  NH2 . ARG   C 1 237 ? 17.348  -31.840 25.534  1.00 39.66  ? 242 ARG   C NH2 1 
ATOM   6601 N  N   . GLN   C 1 238 ? 17.008  -32.987 18.026  1.00 37.14  ? 243 GLN   C N   1 
ATOM   6602 C  CA  . GLN   C 1 238 ? 15.601  -32.889 17.639  1.00 37.38  ? 243 GLN   C CA  1 
ATOM   6603 C  C   . GLN   C 1 238 ? 14.743  -33.225 18.864  1.00 41.68  ? 243 GLN   C C   1 
ATOM   6604 O  O   . GLN   C 1 238 ? 15.100  -34.117 19.650  1.00 41.96  ? 243 GLN   C O   1 
ATOM   6605 C  CB  . GLN   C 1 238 ? 15.250  -33.818 16.455  1.00 38.87  ? 243 GLN   C CB  1 
ATOM   6606 C  CG  . GLN   C 1 238 ? 16.007  -33.491 15.164  1.00 62.87  ? 243 GLN   C CG  1 
ATOM   6607 C  CD  . GLN   C 1 238 ? 15.160  -33.627 13.917  1.00 90.75  ? 243 GLN   C CD  1 
ATOM   6608 O  OE1 . GLN   C 1 238 ? 14.932  -32.653 13.188  1.00 86.96  ? 243 GLN   C OE1 1 
ATOM   6609 N  NE2 . GLN   C 1 238 ? 14.702  -34.841 13.623  1.00 84.27  ? 243 GLN   C NE2 1 
ATOM   6610 N  N   . ARG   C 1 239 ? 13.646  -32.478 19.049  1.00 37.93  ? 244 ARG   C N   1 
ATOM   6611 C  CA  . ARG   C 1 239 ? 12.739  -32.603 20.190  1.00 36.57  ? 244 ARG   C CA  1 
ATOM   6612 C  C   . ARG   C 1 239 ? 11.291  -32.422 19.769  1.00 38.64  ? 244 ARG   C C   1 
ATOM   6613 O  O   . ARG   C 1 239 ? 11.033  -31.671 18.825  1.00 38.48  ? 244 ARG   C O   1 
ATOM   6614 C  CB  . ARG   C 1 239 ? 13.072  -31.538 21.267  1.00 34.85  ? 244 ARG   C CB  1 
ATOM   6615 C  CG  . ARG   C 1 239 ? 14.484  -31.573 21.811  1.00 39.96  ? 244 ARG   C CG  1 
ATOM   6616 C  CD  . ARG   C 1 239 ? 14.781  -30.335 22.623  1.00 43.65  ? 244 ARG   C CD  1 
ATOM   6617 N  NE  . ARG   C 1 239 ? 14.279  -30.431 23.994  1.00 40.65  ? 244 ARG   C NE  1 
ATOM   6618 C  CZ  . ARG   C 1 239 ? 14.531  -29.541 24.945  1.00 52.72  ? 244 ARG   C CZ  1 
ATOM   6619 N  NH1 . ARG   C 1 239 ? 15.259  -28.460 24.678  1.00 37.32  ? 244 ARG   C NH1 1 
ATOM   6620 N  NH2 . ARG   C 1 239 ? 14.060  -29.726 26.177  1.00 35.66  ? 244 ARG   C NH2 1 
ATOM   6621 N  N   . PRO   C 1 240 ? 10.304  -33.009 20.483  1.00 34.80  ? 245 PRO   C N   1 
ATOM   6622 C  CA  . PRO   C 1 240 ? 8.905   -32.742 20.132  1.00 34.40  ? 245 PRO   C CA  1 
ATOM   6623 C  C   . PRO   C 1 240 ? 8.598   -31.273 20.445  1.00 36.62  ? 245 PRO   C C   1 
ATOM   6624 O  O   . PRO   C 1 240 ? 9.095   -30.753 21.448  1.00 36.02  ? 245 PRO   C O   1 
ATOM   6625 C  CB  . PRO   C 1 240 ? 8.117   -33.662 21.073  1.00 36.92  ? 245 PRO   C CB  1 
ATOM   6626 C  CG  . PRO   C 1 240 ? 9.123   -34.645 21.586  1.00 40.76  ? 245 PRO   C CG  1 
ATOM   6627 C  CD  . PRO   C 1 240 ? 10.384  -33.901 21.664  1.00 37.06  ? 245 PRO   C CD  1 
ATOM   6628 N  N   . ILE   C 1 241 ? 7.857   -30.604 19.552  1.00 30.69  ? 246 ILE   C N   1 
ATOM   6629 C  CA  . ILE   C 1 241 ? 7.494   -29.190 19.736  1.00 28.18  ? 246 ILE   C CA  1 
ATOM   6630 C  C   . ILE   C 1 241 ? 6.052   -29.033 20.141  1.00 30.29  ? 246 ILE   C C   1 
ATOM   6631 O  O   . ILE   C 1 241 ? 5.158   -29.582 19.496  1.00 32.99  ? 246 ILE   C O   1 
ATOM   6632 C  CB  . ILE   C 1 241 ? 7.860   -28.320 18.471  1.00 30.11  ? 246 ILE   C CB  1 
ATOM   6633 C  CG1 . ILE   C 1 241 ? 9.386   -28.271 18.293  1.00 30.64  ? 246 ILE   C CG1 1 
ATOM   6634 C  CG2 . ILE   C 1 241 ? 7.290   -26.871 18.598  1.00 31.00  ? 246 ILE   C CG2 1 
ATOM   6635 C  CD1 . ILE   C 1 241 ? 9.883   -27.615 16.871  1.00 36.14  ? 246 ILE   C CD1 1 
ATOM   6636 N  N   . HIS   C 1 242 ? 5.814   -28.191 21.180  1.00 28.65  ? 247 HIS   C N   1 
ATOM   6637 C  CA  . HIS   C 1 242 ? 4.485   -27.826 21.616  1.00 27.62  ? 247 HIS   C CA  1 
ATOM   6638 C  C   . HIS   C 1 242 ? 4.355   -26.338 21.276  1.00 31.89  ? 247 HIS   C C   1 
ATOM   6639 O  O   . HIS   C 1 242 ? 5.120   -25.532 21.815  1.00 31.51  ? 247 HIS   C O   1 
ATOM   6640 C  CB  . HIS   C 1 242 ? 4.306   -28.018 23.156  1.00 29.12  ? 247 HIS   C CB  1 
ATOM   6641 C  CG  . HIS   C 1 242 ? 2.882   -27.835 23.592  1.00 32.86  ? 247 HIS   C CG  1 
ATOM   6642 N  ND1 . HIS   C 1 242 ? 2.103   -28.917 23.968  1.00 34.88  ? 247 HIS   C ND1 1 
ATOM   6643 C  CD2 . HIS   C 1 242 ? 2.128   -26.709 23.664  1.00 34.13  ? 247 HIS   C CD2 1 
ATOM   6644 C  CE1 . HIS   C 1 242 ? 0.900   -28.426 24.220  1.00 34.08  ? 247 HIS   C CE1 1 
ATOM   6645 N  NE2 . HIS   C 1 242 ? 0.869   -27.099 24.054  1.00 34.37  ? 247 HIS   C NE2 1 
ATOM   6646 N  N   . LEU   C 1 243 ? 3.408   -26.000 20.403  1.00 29.64  ? 248 LEU   C N   1 
ATOM   6647 C  CA  . LEU   C 1 243 ? 3.179   -24.606 20.012  1.00 29.47  ? 248 LEU   C CA  1 
ATOM   6648 C  C   . LEU   C 1 243 ? 1.939   -24.104 20.716  1.00 32.16  ? 248 LEU   C C   1 
ATOM   6649 O  O   . LEU   C 1 243 ? 0.811   -24.485 20.382  1.00 31.70  ? 248 LEU   C O   1 
ATOM   6650 C  CB  . LEU   C 1 243 ? 3.081   -24.474 18.473  1.00 28.84  ? 248 LEU   C CB  1 
ATOM   6651 C  CG  . LEU   C 1 243 ? 2.849   -23.052 17.884  1.00 32.11  ? 248 LEU   C CG  1 
ATOM   6652 C  CD1 . LEU   C 1 243 ? 3.957   -22.103 18.274  1.00 32.02  ? 248 LEU   C CD1 1 
ATOM   6653 C  CD2 . LEU   C 1 243 ? 2.745   -23.104 16.340  1.00 32.78  ? 248 LEU   C CD2 1 
ATOM   6654 N  N   . SER   C 1 244 ? 2.155   -23.251 21.721  1.00 30.29  ? 249 SER   C N   1 
ATOM   6655 C  CA  . SER   C 1 244 ? 1.053   -22.664 22.451  1.00 29.39  ? 249 SER   C CA  1 
ATOM   6656 C  C   . SER   C 1 244 ? 0.844   -21.259 21.945  1.00 32.40  ? 249 SER   C C   1 
ATOM   6657 O  O   . SER   C 1 244 ? 1.655   -20.374 22.225  1.00 31.35  ? 249 SER   C O   1 
ATOM   6658 C  CB  . SER   C 1 244 ? 1.307   -22.691 23.952  1.00 29.94  ? 249 SER   C CB  1 
ATOM   6659 O  OG  . SER   C 1 244 ? 0.016   -22.604 24.531  1.00 31.05  ? 249 SER   C OG  1 
ATOM   6660 N  N   . PHE   C 1 245 ? -0.217  -21.087 21.163  1.00 29.23  ? 250 PHE   C N   1 
ATOM   6661 C  CA  . PHE   C 1 245 ? -0.514  -19.869 20.409  1.00 28.04  ? 250 PHE   C CA  1 
ATOM   6662 C  C   . PHE   C 1 245 ? -1.756  -19.132 20.889  1.00 31.62  ? 250 PHE   C C   1 
ATOM   6663 O  O   . PHE   C 1 245 ? -2.912  -19.526 20.618  1.00 30.49  ? 250 PHE   C O   1 
ATOM   6664 C  CB  . PHE   C 1 245 ? -0.598  -20.199 18.893  1.00 28.55  ? 250 PHE   C CB  1 
ATOM   6665 C  CG  . PHE   C 1 245 ? -0.287  -19.060 17.939  1.00 29.11  ? 250 PHE   C CG  1 
ATOM   6666 C  CD1 . PHE   C 1 245 ? -1.067  -17.907 17.927  1.00 30.34  ? 250 PHE   C CD1 1 
ATOM   6667 C  CD2 . PHE   C 1 245 ? 0.756   -19.168 17.019  1.00 30.60  ? 250 PHE   C CD2 1 
ATOM   6668 C  CE1 . PHE   C 1 245 ? -0.771  -16.847 17.056  1.00 30.54  ? 250 PHE   C CE1 1 
ATOM   6669 C  CE2 . PHE   C 1 245 ? 1.031   -18.115 16.120  1.00 32.29  ? 250 PHE   C CE2 1 
ATOM   6670 C  CZ  . PHE   C 1 245 ? 0.254   -16.974 16.138  1.00 29.30  ? 250 PHE   C CZ  1 
ATOM   6671 N  N   . ASP   C 1 246 ? -1.504  -17.963 21.504  1.00 29.15  ? 251 ASP   C N   1 
ATOM   6672 C  CA  . ASP   C 1 246 ? -2.568  -17.078 21.954  1.00 28.97  ? 251 ASP   C CA  1 
ATOM   6673 C  C   . ASP   C 1 246 ? -2.868  -16.144 20.786  1.00 32.29  ? 251 ASP   C C   1 
ATOM   6674 O  O   . ASP   C 1 246 ? -1.945  -15.491 20.296  1.00 32.43  ? 251 ASP   C O   1 
ATOM   6675 C  CB  . ASP   C 1 246 ? -2.109  -16.276 23.195  1.00 30.47  ? 251 ASP   C CB  1 
ATOM   6676 C  CG  . ASP   C 1 246 ? -3.182  -15.439 23.890  1.00 32.83  ? 251 ASP   C CG  1 
ATOM   6677 O  OD1 . ASP   C 1 246 ? -4.067  -14.899 23.191  1.00 32.80  ? 251 ASP   C OD1 1 
ATOM   6678 O  OD2 . ASP   C 1 246 ? -3.062  -15.221 25.125  1.00 36.15  ? 251 ASP   C OD2 1 
ATOM   6679 N  N   . ILE   C 1 247 ? -4.136  -16.065 20.346  1.00 27.79  ? 252 ILE   C N   1 
ATOM   6680 C  CA  . ILE   C 1 247 ? -4.558  -15.233 19.212  1.00 27.05  ? 252 ILE   C CA  1 
ATOM   6681 C  C   . ILE   C 1 247 ? -4.191  -13.742 19.441  1.00 29.74  ? 252 ILE   C C   1 
ATOM   6682 O  O   . ILE   C 1 247 ? -3.974  -13.006 18.472  1.00 28.90  ? 252 ILE   C O   1 
ATOM   6683 C  CB  . ILE   C 1 247 ? -6.060  -15.458 18.840  1.00 30.77  ? 252 ILE   C CB  1 
ATOM   6684 C  CG1 . ILE   C 1 247 ? -6.373  -15.087 17.367  1.00 31.65  ? 252 ILE   C CG1 1 
ATOM   6685 C  CG2 . ILE   C 1 247 ? -7.020  -14.735 19.817  1.00 32.73  ? 252 ILE   C CG2 1 
ATOM   6686 C  CD1 . ILE   C 1 247 ? -5.718  -16.009 16.257  1.00 29.45  ? 252 ILE   C CD1 1 
ATOM   6687 N  N   . ASP   C 1 248 ? -4.108  -13.317 20.725  1.00 28.21  ? 253 ASP   C N   1 
ATOM   6688 C  CA  . ASP   C 1 248 ? -3.760  -11.926 21.048  1.00 28.59  ? 253 ASP   C CA  1 
ATOM   6689 C  C   . ASP   C 1 248 ? -2.299  -11.586 20.705  1.00 30.54  ? 253 ASP   C C   1 
ATOM   6690 O  O   . ASP   C 1 248 ? -1.917  -10.423 20.835  1.00 28.86  ? 253 ASP   C O   1 
ATOM   6691 C  CB  . ASP   C 1 248 ? -4.120  -11.562 22.504  1.00 30.12  ? 253 ASP   C CB  1 
ATOM   6692 C  CG  . ASP   C 1 248 ? -3.236  -12.106 23.608  1.00 30.62  ? 253 ASP   C CG  1 
ATOM   6693 O  OD1 . ASP   C 1 248 ? -2.085  -12.480 23.325  1.00 31.48  ? 253 ASP   C OD1 1 
ATOM   6694 O  OD2 . ASP   C 1 248 ? -3.702  -12.167 24.776  1.00 35.53  ? 253 ASP   C OD2 1 
ATOM   6695 N  N   . ALA   C 1 249 ? -1.475  -12.578 20.256  1.00 26.74  ? 254 ALA   C N   1 
ATOM   6696 C  CA  . ALA   C 1 249 ? -0.105  -12.265 19.790  1.00 25.31  ? 254 ALA   C CA  1 
ATOM   6697 C  C   . ALA   C 1 249 ? -0.211  -11.316 18.581  1.00 28.30  ? 254 ALA   C C   1 
ATOM   6698 O  O   . ALA   C 1 249 ? 0.662   -10.457 18.395  1.00 27.01  ? 254 ALA   C O   1 
ATOM   6699 C  CB  . ALA   C 1 249 ? 0.627   -13.532 19.382  1.00 25.84  ? 254 ALA   C CB  1 
ATOM   6700 N  N   . PHE   C 1 250 ? -1.286  -11.486 17.758  1.00 24.50  ? 255 PHE   C N   1 
ATOM   6701 C  CA  . PHE   C 1 250 ? -1.523  -10.676 16.568  1.00 24.79  ? 255 PHE   C CA  1 
ATOM   6702 C  C   . PHE   C 1 250 ? -1.996  -9.299  16.963  1.00 27.50  ? 255 PHE   C C   1 
ATOM   6703 O  O   . PHE   C 1 250 ? -2.667  -9.139  17.993  1.00 27.70  ? 255 PHE   C O   1 
ATOM   6704 C  CB  . PHE   C 1 250 ? -2.602  -11.313 15.665  1.00 26.77  ? 255 PHE   C CB  1 
ATOM   6705 C  CG  . PHE   C 1 250 ? -2.127  -12.512 14.880  1.00 27.62  ? 255 PHE   C CG  1 
ATOM   6706 C  CD1 . PHE   C 1 250 ? -1.321  -12.351 13.754  1.00 27.59  ? 255 PHE   C CD1 1 
ATOM   6707 C  CD2 . PHE   C 1 250 ? -2.503  -13.798 15.246  1.00 28.82  ? 255 PHE   C CD2 1 
ATOM   6708 C  CE1 . PHE   C 1 250 ? -0.892  -13.447 13.017  1.00 27.73  ? 255 PHE   C CE1 1 
ATOM   6709 C  CE2 . PHE   C 1 250 ? -2.091  -14.901 14.496  1.00 30.60  ? 255 PHE   C CE2 1 
ATOM   6710 C  CZ  . PHE   C 1 250 ? -1.280  -14.722 13.382  1.00 28.60  ? 255 PHE   C CZ  1 
ATOM   6711 N  N   . ASP   C 1 251 ? -1.726  -8.317  16.106  1.00 25.22  ? 256 ASP   C N   1 
ATOM   6712 C  CA  . ASP   C 1 251 ? -2.230  -6.969  16.362  1.00 24.46  ? 256 ASP   C CA  1 
ATOM   6713 C  C   . ASP   C 1 251 ? -3.759  -7.017  16.498  1.00 29.33  ? 256 ASP   C C   1 
ATOM   6714 O  O   . ASP   C 1 251 ? -4.410  -7.746  15.730  1.00 29.54  ? 256 ASP   C O   1 
ATOM   6715 C  CB  . ASP   C 1 251 ? -1.873  -6.031  15.218  1.00 25.78  ? 256 ASP   C CB  1 
ATOM   6716 C  CG  . ASP   C 1 251 ? -2.074  -4.582  15.616  1.00 28.87  ? 256 ASP   C CG  1 
ATOM   6717 O  OD1 . ASP   C 1 251 ? -1.191  -4.032  16.303  1.00 31.24  ? 256 ASP   C OD1 1 
ATOM   6718 O  OD2 . ASP   C 1 251 ? -3.150  -4.026  15.307  1.00 30.90  ? 256 ASP   C OD2 1 
ATOM   6719 N  N   . PRO   C 1 252 ? -4.342  -6.220  17.426  1.00 28.45  ? 257 PRO   C N   1 
ATOM   6720 C  CA  . PRO   C 1 252 ? -5.817  -6.207  17.580  1.00 29.28  ? 257 PRO   C CA  1 
ATOM   6721 C  C   . PRO   C 1 252 ? -6.599  -5.845  16.326  1.00 33.79  ? 257 PRO   C C   1 
ATOM   6722 O  O   . PRO   C 1 252 ? -7.774  -6.207  16.237  1.00 34.37  ? 257 PRO   C O   1 
ATOM   6723 C  CB  . PRO   C 1 252 ? -6.042  -5.199  18.719  1.00 31.60  ? 257 PRO   C CB  1 
ATOM   6724 C  CG  . PRO   C 1 252 ? -4.781  -5.175  19.474  1.00 35.33  ? 257 PRO   C CG  1 
ATOM   6725 C  CD  . PRO   C 1 252 ? -3.706  -5.333  18.418  1.00 31.25  ? 257 PRO   C CD  1 
ATOM   6726 N  N   . THR   C 1 253 ? -5.977  -5.167  15.328  1.00 28.97  ? 258 THR   C N   1 
ATOM   6727 C  CA  . THR   C 1 253 ? -6.682  -4.873  14.074  1.00 29.75  ? 258 THR   C CA  1 
ATOM   6728 C  C   . THR   C 1 253 ? -6.984  -6.179  13.298  1.00 34.91  ? 258 THR   C C   1 
ATOM   6729 O  O   . THR   C 1 253 ? -7.939  -6.235  12.522  1.00 36.42  ? 258 THR   C O   1 
ATOM   6730 C  CB  . THR   C 1 253 ? -5.886  -3.902  13.190  1.00 37.77  ? 258 THR   C CB  1 
ATOM   6731 O  OG1 . THR   C 1 253 ? -4.616  -4.494  12.891  1.00 40.99  ? 258 THR   C OG1 1 
ATOM   6732 C  CG2 . THR   C 1 253 ? -5.706  -2.534  13.836  1.00 36.85  ? 258 THR   C CG2 1 
ATOM   6733 N  N   . LEU   C 1 254 ? -6.142  -7.207  13.493  1.00 30.99  ? 259 LEU   C N   1 
ATOM   6734 C  CA  . LEU   C 1 254 ? -6.247  -8.513  12.838  1.00 30.83  ? 259 LEU   C CA  1 
ATOM   6735 C  C   . LEU   C 1 254 ? -7.019  -9.523  13.677  1.00 35.29  ? 259 LEU   C C   1 
ATOM   6736 O  O   . LEU   C 1 254 ? -7.726  -10.368 13.103  1.00 35.57  ? 259 LEU   C O   1 
ATOM   6737 C  CB  . LEU   C 1 254 ? -4.845  -9.079  12.546  1.00 30.69  ? 259 LEU   C CB  1 
ATOM   6738 C  CG  . LEU   C 1 254 ? -3.870  -8.145  11.838  1.00 33.92  ? 259 LEU   C CG  1 
ATOM   6739 C  CD1 . LEU   C 1 254 ? -2.472  -8.704  11.916  1.00 33.69  ? 259 LEU   C CD1 1 
ATOM   6740 C  CD2 . LEU   C 1 254 ? -4.285  -7.896  10.366  1.00 36.85  ? 259 LEU   C CD2 1 
ATOM   6741 N  N   . ALA   C 1 255 ? -6.848  -9.467  15.021  1.00 30.42  ? 260 ALA   C N   1 
ATOM   6742 C  CA  . ALA   C 1 255 ? -7.480  -10.372 15.981  1.00 30.03  ? 260 ALA   C CA  1 
ATOM   6743 C  C   . ALA   C 1 255 ? -8.235  -9.559  17.073  1.00 34.49  ? 260 ALA   C C   1 
ATOM   6744 O  O   . ALA   C 1 255 ? -7.799  -9.556  18.226  1.00 34.44  ? 260 ALA   C O   1 
ATOM   6745 C  CB  . ALA   C 1 255 ? -6.431  -11.292 16.605  1.00 30.76  ? 260 ALA   C CB  1 
ATOM   6746 N  N   . PRO   C 1 256 ? -9.341  -8.844  16.721  1.00 33.55  ? 261 PRO   C N   1 
ATOM   6747 C  CA  . PRO   C 1 256 ? -10.046 -8.041  17.738  1.00 34.46  ? 261 PRO   C CA  1 
ATOM   6748 C  C   . PRO   C 1 256 ? -10.874 -8.855  18.735  1.00 39.16  ? 261 PRO   C C   1 
ATOM   6749 O  O   . PRO   C 1 256 ? -11.067 -8.393  19.857  1.00 40.16  ? 261 PRO   C O   1 
ATOM   6750 C  CB  . PRO   C 1 256 ? -10.951 -7.131  16.907  1.00 36.48  ? 261 PRO   C CB  1 
ATOM   6751 C  CG  . PRO   C 1 256 ? -11.209 -7.891  15.659  1.00 41.17  ? 261 PRO   C CG  1 
ATOM   6752 C  CD  . PRO   C 1 256 ? -9.972  -8.694  15.390  1.00 35.96  ? 261 PRO   C CD  1 
ATOM   6753 N  N   . ALA   C 1 257 ? -11.380 -10.044 18.335  1.00 35.58  ? 262 ALA   C N   1 
ATOM   6754 C  CA  . ALA   C 1 257 ? -12.229 -10.872 19.216  1.00 35.50  ? 262 ALA   C CA  1 
ATOM   6755 C  C   . ALA   C 1 257 ? -11.397 -11.665 20.229  1.00 36.88  ? 262 ALA   C C   1 
ATOM   6756 O  O   . ALA   C 1 257 ? -11.203 -12.881 20.103  1.00 35.99  ? 262 ALA   C O   1 
ATOM   6757 C  CB  . ALA   C 1 257 ? -13.124 -11.786 18.386  1.00 36.62  ? 262 ALA   C CB  1 
ATOM   6758 N  N   . THR   C 1 258 ? -10.868 -10.939 21.231  1.00 33.30  ? 263 THR   C N   1 
ATOM   6759 C  CA  . THR   C 1 258 ? -10.001 -11.442 22.284  1.00 31.52  ? 263 THR   C CA  1 
ATOM   6760 C  C   . THR   C 1 258 ? -10.101 -10.557 23.551  1.00 35.64  ? 263 THR   C C   1 
ATOM   6761 O  O   . THR   C 1 258 ? -10.375 -9.357  23.452  1.00 35.96  ? 263 THR   C O   1 
ATOM   6762 C  CB  . THR   C 1 258 ? -8.559  -11.612 21.747  1.00 36.37  ? 263 THR   C CB  1 
ATOM   6763 O  OG1 . THR   C 1 258 ? -7.895  -12.579 22.537  1.00 29.35  ? 263 THR   C OG1 1 
ATOM   6764 C  CG2 . THR   C 1 258 ? -7.762  -10.288 21.693  1.00 37.03  ? 263 THR   C CG2 1 
ATOM   6765 N  N   . GLY   C 1 259 ? -9.846  -11.159 24.699  1.00 33.97  ? 264 GLY   C N   1 
ATOM   6766 C  CA  . GLY   C 1 259 ? -10.004 -10.539 26.016  1.00 33.94  ? 264 GLY   C CA  1 
ATOM   6767 C  C   . GLY   C 1 259 ? -9.050  -9.443  26.429  1.00 38.56  ? 264 GLY   C C   1 
ATOM   6768 O  O   . GLY   C 1 259 ? -9.468  -8.464  27.067  1.00 36.79  ? 264 GLY   C O   1 
ATOM   6769 N  N   . THR   C 1 260 ? -7.745  -9.627  26.137  1.00 34.30  ? 265 THR   C N   1 
ATOM   6770 C  CA  . THR   C 1 260 ? -6.723  -8.641  26.538  1.00 34.17  ? 265 THR   C CA  1 
ATOM   6771 C  C   . THR   C 1 260 ? -5.923  -8.141  25.309  1.00 34.52  ? 265 THR   C C   1 
ATOM   6772 O  O   . THR   C 1 260 ? -4.736  -8.491  25.186  1.00 34.09  ? 265 THR   C O   1 
ATOM   6773 C  CB  . THR   C 1 260 ? -5.847  -9.181  27.681  1.00 47.36  ? 265 THR   C CB  1 
ATOM   6774 O  OG1 . THR   C 1 260 ? -5.135  -10.317 27.209  1.00 57.94  ? 265 THR   C OG1 1 
ATOM   6775 C  CG2 . THR   C 1 260 ? -6.657  -9.573  28.915  1.00 47.18  ? 265 THR   C CG2 1 
ATOM   6776 N  N   . PRO   C 1 261 ? -6.563  -7.359  24.396  1.00 29.89  ? 266 PRO   C N   1 
ATOM   6777 C  CA  . PRO   C 1 261 ? -5.838  -6.878  23.206  1.00 29.49  ? 266 PRO   C CA  1 
ATOM   6778 C  C   . PRO   C 1 261 ? -4.766  -5.857  23.578  1.00 32.24  ? 266 PRO   C C   1 
ATOM   6779 O  O   . PRO   C 1 261 ? -4.912  -5.116  24.567  1.00 30.71  ? 266 PRO   C O   1 
ATOM   6780 C  CB  . PRO   C 1 261 ? -6.931  -6.268  22.329  1.00 31.43  ? 266 PRO   C CB  1 
ATOM   6781 C  CG  . PRO   C 1 261 ? -8.001  -5.839  23.290  1.00 35.61  ? 266 PRO   C CG  1 
ATOM   6782 C  CD  . PRO   C 1 261 ? -7.967  -6.884  24.386  1.00 31.26  ? 266 PRO   C CD  1 
ATOM   6783 N  N   . VAL   C 1 262 ? -3.642  -5.883  22.842  1.00 27.97  ? 267 VAL   C N   1 
ATOM   6784 C  CA  . VAL   C 1 262 ? -2.508  -4.978  23.098  1.00 27.26  ? 267 VAL   C CA  1 
ATOM   6785 C  C   . VAL   C 1 262 ? -2.026  -4.510  21.728  1.00 29.23  ? 267 VAL   C C   1 
ATOM   6786 O  O   . VAL   C 1 262 ? -1.663  -5.349  20.904  1.00 27.26  ? 267 VAL   C O   1 
ATOM   6787 C  CB  . VAL   C 1 262 ? -1.356  -5.638  23.911  1.00 30.04  ? 267 VAL   C CB  1 
ATOM   6788 C  CG1 . VAL   C 1 262 ? -0.210  -4.656  24.128  1.00 29.94  ? 267 VAL   C CG1 1 
ATOM   6789 C  CG2 . VAL   C 1 262 ? -1.839  -6.195  25.265  1.00 29.01  ? 267 VAL   C CG2 1 
ATOM   6790 N  N   . VAL   C 1 263 ? -2.017  -3.183  21.488  1.00 26.94  ? 268 VAL   C N   1 
ATOM   6791 C  CA  . VAL   C 1 263 ? -1.622  -2.596  20.204  1.00 25.98  ? 268 VAL   C CA  1 
ATOM   6792 C  C   . VAL   C 1 263 ? -0.143  -2.930  19.889  1.00 26.53  ? 268 VAL   C C   1 
ATOM   6793 O  O   . VAL   C 1 263 ? 0.622   -3.179  20.820  1.00 26.44  ? 268 VAL   C O   1 
ATOM   6794 C  CB  . VAL   C 1 263 ? -1.899  -1.050  20.185  1.00 31.89  ? 268 VAL   C CB  1 
ATOM   6795 C  CG1 . VAL   C 1 263 ? -1.610  -0.431  18.820  1.00 32.04  ? 268 VAL   C CG1 1 
ATOM   6796 C  CG2 . VAL   C 1 263 ? -3.348  -0.749  20.583  1.00 32.88  ? 268 VAL   C CG2 1 
ATOM   6797 N  N   . GLY   C 1 264 ? 0.198   -2.989  18.597  1.00 24.39  ? 269 GLY   C N   1 
ATOM   6798 C  CA  . GLY   C 1 264 ? 1.562   -3.215  18.115  1.00 24.09  ? 269 GLY   C CA  1 
ATOM   6799 C  C   . GLY   C 1 264 ? 1.986   -4.674  18.108  1.00 24.40  ? 269 GLY   C C   1 
ATOM   6800 O  O   . GLY   C 1 264 ? 3.114   -5.004  18.478  1.00 23.29  ? 269 GLY   C O   1 
ATOM   6801 N  N   . GLY   C 1 265 ? 1.095   -5.552  17.673  1.00 25.02  ? 270 GLY   C N   1 
ATOM   6802 C  CA  . GLY   C 1 265 ? 1.408   -6.976  17.684  1.00 24.19  ? 270 GLY   C CA  1 
ATOM   6803 C  C   . GLY   C 1 265 ? 1.936   -7.494  16.363  1.00 25.29  ? 270 GLY   C C   1 
ATOM   6804 O  O   . GLY   C 1 265 ? 2.264   -6.726  15.436  1.00 24.10  ? 270 GLY   C O   1 
ATOM   6805 N  N   . LEU   C 1 266 ? 1.953   -8.825  16.256  1.00 22.93  ? 271 LEU   C N   1 
ATOM   6806 C  CA  . LEU   C 1 266 ? 2.398   -9.490  15.029  1.00 22.66  ? 271 LEU   C CA  1 
ATOM   6807 C  C   . LEU   C 1 266 ? 1.502   -9.120  13.850  1.00 25.87  ? 271 LEU   C C   1 
ATOM   6808 O  O   . LEU   C 1 266 ? 0.292   -8.990  14.001  1.00 24.54  ? 271 LEU   C O   1 
ATOM   6809 C  CB  . LEU   C 1 266 ? 2.327   -11.019 15.183  1.00 22.38  ? 271 LEU   C CB  1 
ATOM   6810 C  CG  . LEU   C 1 266 ? 3.159   -11.697 16.257  1.00 24.74  ? 271 LEU   C CG  1 
ATOM   6811 C  CD1 . LEU   C 1 266 ? 2.807   -13.191 16.346  1.00 26.02  ? 271 LEU   C CD1 1 
ATOM   6812 C  CD2 . LEU   C 1 266 ? 4.646   -11.565 15.969  1.00 25.29  ? 271 LEU   C CD2 1 
ATOM   6813 N  N   . THR   C 1 267 ? 2.087   -9.008  12.659  1.00 24.53  ? 272 THR   C N   1 
ATOM   6814 C  CA  . THR   C 1 267 ? 1.292   -8.843  11.444  1.00 23.17  ? 272 THR   C CA  1 
ATOM   6815 C  C   . THR   C 1 267 ? 0.818   -10.272 11.032  1.00 24.27  ? 272 THR   C C   1 
ATOM   6816 O  O   . THR   C 1 267 ? 1.340   -11.270 11.556  1.00 22.69  ? 272 THR   C O   1 
ATOM   6817 C  CB  . THR   C 1 267 ? 2.137   -8.266  10.318  1.00 24.98  ? 272 THR   C CB  1 
ATOM   6818 O  OG1 . THR   C 1 267 ? 3.186   -9.204  10.012  1.00 23.84  ? 272 THR   C OG1 1 
ATOM   6819 C  CG2 . THR   C 1 267 ? 2.683   -6.860  10.670  1.00 25.05  ? 272 THR   C CG2 1 
ATOM   6820 N  N   . TYR   C 1 268 ? -0.105  -10.346 10.077  1.00 23.98  ? 273 TYR   C N   1 
ATOM   6821 C  CA  . TYR   C 1 268 ? -0.591  -11.619 9.531   1.00 24.17  ? 273 TYR   C CA  1 
ATOM   6822 C  C   . TYR   C 1 268 ? 0.609   -12.402 8.975   1.00 25.79  ? 273 TYR   C C   1 
ATOM   6823 O  O   . TYR   C 1 268 ? 0.800   -13.575 9.305   1.00 23.35  ? 273 TYR   C O   1 
ATOM   6824 C  CB  . TYR   C 1 268 ? -1.621  -11.361 8.424   1.00 26.00  ? 273 TYR   C CB  1 
ATOM   6825 C  CG  . TYR   C 1 268 ? -2.097  -12.638 7.764   1.00 29.80  ? 273 TYR   C CG  1 
ATOM   6826 C  CD1 . TYR   C 1 268 ? -1.427  -13.172 6.663   1.00 32.48  ? 273 TYR   C CD1 1 
ATOM   6827 C  CD2 . TYR   C 1 268 ? -3.212  -13.322 8.246   1.00 31.64  ? 273 TYR   C CD2 1 
ATOM   6828 C  CE1 . TYR   C 1 268 ? -1.848  -14.364 6.066   1.00 34.28  ? 273 TYR   C CE1 1 
ATOM   6829 C  CE2 . TYR   C 1 268 ? -3.633  -14.515 7.666   1.00 33.10  ? 273 TYR   C CE2 1 
ATOM   6830 C  CZ  . TYR   C 1 268 ? -2.934  -15.045 6.592   1.00 39.76  ? 273 TYR   C CZ  1 
ATOM   6831 O  OH  . TYR   C 1 268 ? -3.348  -16.226 6.017   1.00 40.32  ? 273 TYR   C OH  1 
ATOM   6832 N  N   . ARG   C 1 269 ? 1.471   -11.697 8.209   1.00 24.25  ? 274 ARG   C N   1 
ATOM   6833 C  CA  . ARG   C 1 269 ? 2.660   -12.287 7.608   1.00 24.06  ? 274 ARG   C CA  1 
ATOM   6834 C  C   . ARG   C 1 269 ? 3.616   -12.865 8.632   1.00 25.20  ? 274 ARG   C C   1 
ATOM   6835 O  O   . ARG   C 1 269 ? 4.077   -14.000 8.477   1.00 23.84  ? 274 ARG   C O   1 
ATOM   6836 C  CB  . ARG   C 1 269 ? 3.352   -11.248 6.708   1.00 23.87  ? 274 ARG   C CB  1 
ATOM   6837 C  CG  . ARG   C 1 269 ? 2.514   -10.978 5.454   1.00 25.23  ? 274 ARG   C CG  1 
ATOM   6838 C  CD  . ARG   C 1 269 ? 2.781   -9.626  4.794   1.00 22.22  ? 274 ARG   C CD  1 
ATOM   6839 N  NE  . ARG   C 1 269 ? 4.210   -9.456  4.518   1.00 26.08  ? 274 ARG   C NE  1 
ATOM   6840 C  CZ  . ARG   C 1 269 ? 4.742   -8.345  4.020   1.00 27.08  ? 274 ARG   C CZ  1 
ATOM   6841 N  NH1 . ARG   C 1 269 ? 3.966   -7.318  3.686   1.00 22.92  ? 274 ARG   C NH1 1 
ATOM   6842 N  NH2 . ARG   C 1 269 ? 6.046   -8.265  3.814   1.00 24.94  ? 274 ARG   C NH2 1 
ATOM   6843 N  N   . GLU   C 1 270 ? 3.862   -12.127 9.740   1.00 22.03  ? 275 GLU   C N   1 
ATOM   6844 C  CA  . GLU   C 1 270 ? 4.754   -12.626 10.781  1.00 22.12  ? 275 GLU   C CA  1 
ATOM   6845 C  C   . GLU   C 1 270 ? 4.214   -13.893 11.449  1.00 23.99  ? 275 GLU   C C   1 
ATOM   6846 O  O   . GLU   C 1 270 ? 4.977   -14.825 11.678  1.00 23.36  ? 275 GLU   C O   1 
ATOM   6847 C  CB  . GLU   C 1 270 ? 5.028   -11.552 11.837  1.00 23.14  ? 275 GLU   C CB  1 
ATOM   6848 C  CG  . GLU   C 1 270 ? 6.006   -10.510 11.324  1.00 24.04  ? 275 GLU   C CG  1 
ATOM   6849 C  CD  . GLU   C 1 270 ? 6.055   -9.248  12.168  1.00 26.73  ? 275 GLU   C CD  1 
ATOM   6850 O  OE1 . GLU   C 1 270 ? 5.041   -8.932  12.825  1.00 25.88  ? 275 GLU   C OE1 1 
ATOM   6851 O  OE2 . GLU   C 1 270 ? 7.100   -8.564  12.149  1.00 23.34  ? 275 GLU   C OE2 1 
ATOM   6852 N  N   . GLY   C 1 271 ? 2.921   -13.900 11.754  1.00 23.24  ? 276 GLY   C N   1 
ATOM   6853 C  CA  . GLY   C 1 271 ? 2.277   -15.054 12.393  1.00 24.19  ? 276 GLY   C CA  1 
ATOM   6854 C  C   . GLY   C 1 271 ? 2.305   -16.282 11.503  1.00 27.21  ? 276 GLY   C C   1 
ATOM   6855 O  O   . GLY   C 1 271 ? 2.583   -17.388 11.971  1.00 27.20  ? 276 GLY   C O   1 
ATOM   6856 N  N   . MET   C 1 272 ? 2.057   -16.094 10.201  1.00 25.30  ? 277 MET   C N   1 
ATOM   6857 C  CA  . MET   C 1 272 ? 2.116   -17.203 9.238   1.00 24.99  ? 277 MET   C CA  1 
ATOM   6858 C  C   . MET   C 1 272 ? 3.528   -17.739 9.159   1.00 27.90  ? 277 MET   C C   1 
ATOM   6859 O  O   . MET   C 1 272 ? 3.721   -18.952 9.171   1.00 27.76  ? 277 MET   C O   1 
ATOM   6860 C  CB  . MET   C 1 272 ? 1.612   -16.769 7.854   1.00 27.25  ? 277 MET   C CB  1 
ATOM   6861 C  CG  . MET   C 1 272 ? 0.140   -16.480 7.798   1.00 30.27  ? 277 MET   C CG  1 
ATOM   6862 S  SD  . MET   C 1 272 ? -0.952  -17.808 8.453   1.00 34.20  ? 277 MET   C SD  1 
ATOM   6863 C  CE  . MET   C 1 272 ? -1.515  -17.023 9.954   1.00 30.59  ? 277 MET   C CE  1 
ATOM   6864 N  N   . TYR   C 1 273 ? 4.522   -16.851 9.153   1.00 23.96  ? 278 TYR   C N   1 
ATOM   6865 C  CA  . TYR   C 1 273 ? 5.922   -17.237 9.111   1.00 24.52  ? 278 TYR   C CA  1 
ATOM   6866 C  C   . TYR   C 1 273 ? 6.309   -18.111 10.303  1.00 28.59  ? 278 TYR   C C   1 
ATOM   6867 O  O   . TYR   C 1 273 ? 7.009   -19.117 10.128  1.00 27.20  ? 278 TYR   C O   1 
ATOM   6868 C  CB  . TYR   C 1 273 ? 6.841   -16.022 8.988   1.00 24.97  ? 278 TYR   C CB  1 
ATOM   6869 C  CG  . TYR   C 1 273 ? 8.264   -16.406 8.654   1.00 26.40  ? 278 TYR   C CG  1 
ATOM   6870 C  CD1 . TYR   C 1 273 ? 8.669   -16.574 7.332   1.00 29.00  ? 278 TYR   C CD1 1 
ATOM   6871 C  CD2 . TYR   C 1 273 ? 9.188   -16.676 9.660   1.00 28.52  ? 278 TYR   C CD2 1 
ATOM   6872 C  CE1 . TYR   C 1 273 ? 9.966   -16.987 7.021   1.00 30.35  ? 278 TYR   C CE1 1 
ATOM   6873 C  CE2 . TYR   C 1 273 ? 10.495  -17.046 9.359   1.00 29.56  ? 278 TYR   C CE2 1 
ATOM   6874 C  CZ  . TYR   C 1 273 ? 10.863  -17.253 8.041   1.00 31.32  ? 278 TYR   C CZ  1 
ATOM   6875 O  OH  . TYR   C 1 273 ? 12.150  -17.630 7.753   1.00 32.49  ? 278 TYR   C OH  1 
ATOM   6876 N  N   . ILE   C 1 274 ? 5.846   -17.735 11.524  1.00 23.39  ? 279 ILE   C N   1 
ATOM   6877 C  CA  . ILE   C 1 274 ? 6.140   -18.563 12.709  1.00 23.04  ? 279 ILE   C CA  1 
ATOM   6878 C  C   . ILE   C 1 274 ? 5.609   -19.995 12.475  1.00 25.85  ? 279 ILE   C C   1 
ATOM   6879 O  O   . ILE   C 1 274 ? 6.351   -20.949 12.671  1.00 27.19  ? 279 ILE   C O   1 
ATOM   6880 C  CB  . ILE   C 1 274 ? 5.460   -17.934 13.946  1.00 26.12  ? 279 ILE   C CB  1 
ATOM   6881 C  CG1 . ILE   C 1 274 ? 6.147   -16.608 14.321  1.00 26.66  ? 279 ILE   C CG1 1 
ATOM   6882 C  CG2 . ILE   C 1 274 ? 5.453   -18.941 15.135  1.00 27.30  ? 279 ILE   C CG2 1 
ATOM   6883 C  CD1 . ILE   C 1 274 ? 5.325   -15.763 15.384  1.00 26.69  ? 279 ILE   C CD1 1 
ATOM   6884 N  N   . ALA   C 1 275 ? 4.333   -20.110 12.085  1.00 24.89  ? 280 ALA   C N   1 
ATOM   6885 C  CA  . ALA   C 1 275 ? 3.661   -21.389 11.869  1.00 26.12  ? 280 ALA   C CA  1 
ATOM   6886 C  C   . ALA   C 1 275 ? 4.346   -22.212 10.771  1.00 29.69  ? 280 ALA   C C   1 
ATOM   6887 O  O   . ALA   C 1 275 ? 4.601   -23.412 10.961  1.00 27.63  ? 280 ALA   C O   1 
ATOM   6888 C  CB  . ALA   C 1 275 ? 2.201   -21.161 11.542  1.00 26.76  ? 280 ALA   C CB  1 
ATOM   6889 N  N   . GLU   C 1 276 ? 4.754   -21.529 9.674   1.00 27.33  ? 281 GLU   C N   1 
ATOM   6890 C  CA  . GLU   C 1 276 ? 5.465   -22.186 8.560   1.00 26.50  ? 281 GLU   C CA  1 
ATOM   6891 C  C   . GLU   C 1 276 ? 6.795   -22.765 9.001   1.00 29.36  ? 281 GLU   C C   1 
ATOM   6892 O  O   . GLU   C 1 276 ? 7.115   -23.909 8.634   1.00 30.78  ? 281 GLU   C O   1 
ATOM   6893 C  CB  . GLU   C 1 276 ? 5.688   -21.193 7.405   1.00 26.82  ? 281 GLU   C CB  1 
ATOM   6894 C  CG  . GLU   C 1 276 ? 4.409   -20.791 6.696   1.00 25.16  ? 281 GLU   C CG  1 
ATOM   6895 C  CD  . GLU   C 1 276 ? 4.593   -19.600 5.774   1.00 28.48  ? 281 GLU   C CD  1 
ATOM   6896 O  OE1 . GLU   C 1 276 ? 5.665   -18.948 5.826   1.00 28.73  ? 281 GLU   C OE1 1 
ATOM   6897 O  OE2 . GLU   C 1 276 ? 3.651   -19.312 5.005   1.00 29.57  ? 281 GLU   C OE2 1 
ATOM   6898 N  N   . GLU   C 1 277 ? 7.563   -22.014 9.790   1.00 24.75  ? 282 GLU   C N   1 
ATOM   6899 C  CA  . GLU   C 1 277 ? 8.835   -22.458 10.319  1.00 25.45  ? 282 GLU   C CA  1 
ATOM   6900 C  C   . GLU   C 1 277 ? 8.662   -23.646 11.246  1.00 30.58  ? 282 GLU   C C   1 
ATOM   6901 O  O   . GLU   C 1 277 ? 9.431   -24.599 11.144  1.00 31.06  ? 282 GLU   C O   1 
ATOM   6902 C  CB  . GLU   C 1 277 ? 9.604   -21.333 10.985  1.00 26.76  ? 282 GLU   C CB  1 
ATOM   6903 C  CG  . GLU   C 1 277 ? 10.238  -20.403 9.965   1.00 33.75  ? 282 GLU   C CG  1 
ATOM   6904 C  CD  . GLU   C 1 277 ? 10.973  -21.124 8.845   1.00 44.70  ? 282 GLU   C CD  1 
ATOM   6905 O  OE1 . GLU   C 1 277 ? 12.018  -21.756 9.123   1.00 38.41  ? 282 GLU   C OE1 1 
ATOM   6906 O  OE2 . GLU   C 1 277 ? 10.455  -21.122 7.707   1.00 36.14  ? 282 GLU   C OE2 1 
ATOM   6907 N  N   . ILE   C 1 278 ? 7.629   -23.599 12.122  1.00 28.23  ? 283 ILE   C N   1 
ATOM   6908 C  CA  . ILE   C 1 278 ? 7.270   -24.720 13.008  1.00 28.88  ? 283 ILE   C CA  1 
ATOM   6909 C  C   . ILE   C 1 278 ? 6.951   -25.961 12.130  1.00 31.85  ? 283 ILE   C C   1 
ATOM   6910 O  O   . ILE   C 1 278 ? 7.468   -27.044 12.412  1.00 32.33  ? 283 ILE   C O   1 
ATOM   6911 C  CB  . ILE   C 1 278 ? 6.072   -24.332 13.940  1.00 32.09  ? 283 ILE   C CB  1 
ATOM   6912 C  CG1 . ILE   C 1 278 ? 6.464   -23.240 14.987  1.00 32.38  ? 283 ILE   C CG1 1 
ATOM   6913 C  CG2 . ILE   C 1 278 ? 5.433   -25.583 14.616  1.00 33.05  ? 283 ILE   C CG2 1 
ATOM   6914 C  CD1 . ILE   C 1 278 ? 7.424   -23.622 16.152  1.00 45.99  ? 283 ILE   C CD1 1 
ATOM   6915 N  N   . HIS   C 1 279 ? 6.117   -25.811 11.087  1.00 28.89  ? 284 HIS   C N   1 
ATOM   6916 C  CA  . HIS   C 1 279 ? 5.804   -26.922 10.163  1.00 29.91  ? 284 HIS   C CA  1 
ATOM   6917 C  C   . HIS   C 1 279 ? 7.091   -27.491 9.524   1.00 35.01  ? 284 HIS   C C   1 
ATOM   6918 O  O   . HIS   C 1 279 ? 7.282   -28.716 9.520   1.00 34.42  ? 284 HIS   C O   1 
ATOM   6919 C  CB  . HIS   C 1 279 ? 4.799   -26.511 9.078   1.00 30.57  ? 284 HIS   C CB  1 
ATOM   6920 C  CG  . HIS   C 1 279 ? 4.635   -27.576 8.032   1.00 34.27  ? 284 HIS   C CG  1 
ATOM   6921 N  ND1 . HIS   C 1 279 ? 4.043   -28.793 8.335   1.00 36.15  ? 284 HIS   C ND1 1 
ATOM   6922 C  CD2 . HIS   C 1 279 ? 5.104   -27.624 6.761   1.00 36.09  ? 284 HIS   C CD2 1 
ATOM   6923 C  CE1 . HIS   C 1 279 ? 4.117   -29.516 7.229   1.00 35.03  ? 284 HIS   C CE1 1 
ATOM   6924 N  NE2 . HIS   C 1 279 ? 4.752   -28.863 6.255   1.00 35.66  ? 284 HIS   C NE2 1 
ATOM   6925 N  N   . ASN   C 1 280 ? 7.981   -26.605 9.034   1.00 31.67  ? 285 ASN   C N   1 
ATOM   6926 C  CA  . ASN   C 1 280 ? 9.234   -26.960 8.368   1.00 31.49  ? 285 ASN   C CA  1 
ATOM   6927 C  C   . ASN   C 1 280 ? 10.187  -27.802 9.225   1.00 34.94  ? 285 ASN   C C   1 
ATOM   6928 O  O   . ASN   C 1 280 ? 11.010  -28.521 8.663   1.00 33.59  ? 285 ASN   C O   1 
ATOM   6929 C  CB  . ASN   C 1 280 ? 9.944   -25.719 7.809   1.00 32.41  ? 285 ASN   C CB  1 
ATOM   6930 C  CG  . ASN   C 1 280 ? 9.236   -25.124 6.606   1.00 40.85  ? 285 ASN   C CG  1 
ATOM   6931 O  OD1 . ASN   C 1 280 ? 8.243   -25.668 6.100   1.00 36.53  ? 285 ASN   C OD1 1 
ATOM   6932 N  ND2 . ASN   C 1 280 ? 9.675   -23.938 6.176   1.00 38.51  ? 285 ASN   C ND2 1 
ATOM   6933 N  N   . THR   C 1 281 ? 10.074  -27.752 10.572  1.00 31.22  ? 286 THR   C N   1 
ATOM   6934 C  CA  . THR   C 1 281 ? 10.955  -28.589 11.413  1.00 30.10  ? 286 THR   C CA  1 
ATOM   6935 C  C   . THR   C 1 281 ? 10.570  -30.060 11.304  1.00 33.03  ? 286 THR   C C   1 
ATOM   6936 O  O   . THR   C 1 281 ? 11.412  -30.915 11.549  1.00 35.14  ? 286 THR   C O   1 
ATOM   6937 C  CB  . THR   C 1 281 ? 10.860  -28.201 12.903  1.00 31.04  ? 286 THR   C CB  1 
ATOM   6938 O  OG1 . THR   C 1 281 ? 9.532   -28.463 13.339  1.00 27.46  ? 286 THR   C OG1 1 
ATOM   6939 C  CG2 . THR   C 1 281 ? 11.252  -26.743 13.173  1.00 31.72  ? 286 THR   C CG2 1 
ATOM   6940 N  N   . GLY   C 1 282 ? 9.296   -30.321 11.029  1.00 30.36  ? 287 GLY   C N   1 
ATOM   6941 C  CA  . GLY   C 1 282 ? 8.687   -31.652 11.017  1.00 31.60  ? 287 GLY   C CA  1 
ATOM   6942 C  C   . GLY   C 1 282 ? 8.567   -32.223 12.425  1.00 37.54  ? 287 GLY   C C   1 
ATOM   6943 O  O   . GLY   C 1 282 ? 8.326   -33.427 12.594  1.00 36.94  ? 287 GLY   C O   1 
ATOM   6944 N  N   . LEU   C 1 283 ? 8.762   -31.357 13.458  1.00 33.80  ? 288 LEU   C N   1 
ATOM   6945 C  CA  . LEU   C 1 283 ? 8.773   -31.771 14.873  1.00 33.06  ? 288 LEU   C CA  1 
ATOM   6946 C  C   . LEU   C 1 283 ? 7.536   -31.380 15.689  1.00 38.98  ? 288 LEU   C C   1 
ATOM   6947 O  O   . LEU   C 1 283 ? 7.480   -31.733 16.879  1.00 40.27  ? 288 LEU   C O   1 
ATOM   6948 C  CB  . LEU   C 1 283 ? 10.045  -31.291 15.580  1.00 31.97  ? 288 LEU   C CB  1 
ATOM   6949 C  CG  . LEU   C 1 283 ? 11.378  -31.790 15.038  1.00 35.29  ? 288 LEU   C CG  1 
ATOM   6950 C  CD1 . LEU   C 1 283 ? 12.512  -30.973 15.571  1.00 34.76  ? 288 LEU   C CD1 1 
ATOM   6951 C  CD2 . LEU   C 1 283 ? 11.620  -33.278 15.381  1.00 37.71  ? 288 LEU   C CD2 1 
ATOM   6952 N  N   . LEU   C 1 284 ? 6.525   -30.741 15.071  1.00 35.80  ? 289 LEU   C N   1 
ATOM   6953 C  CA  . LEU   C 1 284 ? 5.303   -30.345 15.778  1.00 35.88  ? 289 LEU   C CA  1 
ATOM   6954 C  C   . LEU   C 1 284 ? 4.506   -31.546 16.307  1.00 42.16  ? 289 LEU   C C   1 
ATOM   6955 O  O   . LEU   C 1 284 ? 4.070   -32.391 15.518  1.00 41.45  ? 289 LEU   C O   1 
ATOM   6956 C  CB  . LEU   C 1 284 ? 4.401   -29.432 14.945  1.00 35.30  ? 289 LEU   C CB  1 
ATOM   6957 C  CG  . LEU   C 1 284 ? 3.127   -28.918 15.656  1.00 38.30  ? 289 LEU   C CG  1 
ATOM   6958 C  CD1 . LEU   C 1 284 ? 3.469   -28.010 16.832  1.00 38.82  ? 289 LEU   C CD1 1 
ATOM   6959 C  CD2 . LEU   C 1 284 ? 2.194   -28.233 14.695  1.00 38.68  ? 289 LEU   C CD2 1 
ATOM   6960 N  N   . SER   C 1 285 ? 4.263   -31.570 17.640  1.00 38.08  ? 290 SER   C N   1 
ATOM   6961 C  CA  . SER   C 1 285 ? 3.549   -32.670 18.294  1.00 38.24  ? 290 SER   C CA  1 
ATOM   6962 C  C   . SER   C 1 285 ? 2.193   -32.259 18.903  1.00 40.66  ? 290 SER   C C   1 
ATOM   6963 O  O   . SER   C 1 285 ? 1.259   -33.066 18.963  1.00 40.05  ? 290 SER   C O   1 
ATOM   6964 C  CB  . SER   C 1 285 ? 4.451   -33.333 19.320  1.00 42.45  ? 290 SER   C CB  1 
ATOM   6965 O  OG  . SER   C 1 285 ? 3.804   -34.462 19.884  1.00 52.34  ? 290 SER   C OG  1 
ATOM   6966 N  N   . ALA   C 1 286 ? 2.070   -30.993 19.329  1.00 35.25  ? 291 ALA   C N   1 
ATOM   6967 C  CA  . ALA   C 1 286 ? 0.819   -30.482 19.873  1.00 34.00  ? 291 ALA   C CA  1 
ATOM   6968 C  C   . ALA   C 1 286 ? 0.769   -28.981 19.668  1.00 34.16  ? 291 ALA   C C   1 
ATOM   6969 O  O   . ALA   C 1 286 ? 1.821   -28.336 19.638  1.00 31.80  ? 291 ALA   C O   1 
ATOM   6970 C  CB  . ALA   C 1 286 ? 0.688   -30.807 21.356  1.00 34.97  ? 291 ALA   C CB  1 
ATOM   6971 N  N   . LEU   C 1 287 ? -0.450  -28.469 19.499  1.00 31.47  ? 292 LEU   C N   1 
ATOM   6972 C  CA  . LEU   C 1 287 ? -0.763  -27.068 19.236  1.00 32.86  ? 292 LEU   C CA  1 
ATOM   6973 C  C   . LEU   C 1 287 ? -1.987  -26.617 20.016  1.00 36.92  ? 292 LEU   C C   1 
ATOM   6974 O  O   . LEU   C 1 287 ? -3.028  -27.265 19.958  1.00 36.16  ? 292 LEU   C O   1 
ATOM   6975 C  CB  . LEU   C 1 287 ? -1.039  -26.893 17.732  1.00 33.15  ? 292 LEU   C CB  1 
ATOM   6976 C  CG  . LEU   C 1 287 ? -1.224  -25.465 17.224  1.00 37.04  ? 292 LEU   C CG  1 
ATOM   6977 C  CD1 . LEU   C 1 287 ? -0.645  -25.331 15.848  1.00 37.89  ? 292 LEU   C CD1 1 
ATOM   6978 C  CD2 . LEU   C 1 287 ? -2.703  -25.056 17.185  1.00 35.44  ? 292 LEU   C CD2 1 
ATOM   6979 N  N   . ASP   C 1 288 ? -1.889  -25.441 20.657  1.00 33.08  ? 293 ASP   C N   1 
ATOM   6980 C  CA  . ASP   C 1 288 ? -3.009  -24.800 21.318  1.00 31.87  ? 293 ASP   C CA  1 
ATOM   6981 C  C   . ASP   C 1 288 ? -3.310  -23.530 20.569  1.00 34.74  ? 293 ASP   C C   1 
ATOM   6982 O  O   . ASP   C 1 288 ? -2.383  -22.751 20.274  1.00 32.83  ? 293 ASP   C O   1 
ATOM   6983 C  CB  . ASP   C 1 288 ? -2.655  -24.397 22.771  1.00 33.43  ? 293 ASP   C CB  1 
ATOM   6984 C  CG  . ASP   C 1 288 ? -1.968  -25.460 23.584  1.00 34.75  ? 293 ASP   C CG  1 
ATOM   6985 O  OD1 . ASP   C 1 288 ? -2.341  -26.648 23.444  1.00 36.56  ? 293 ASP   C OD1 1 
ATOM   6986 O  OD2 . ASP   C 1 288 ? -1.044  -25.117 24.333  1.00 35.29  ? 293 ASP   C OD2 1 
ATOM   6987 N  N   . LEU   C 1 289 ? -4.575  -23.314 20.255  1.00 31.52  ? 294 LEU   C N   1 
ATOM   6988 C  CA  . LEU   C 1 289 ? -5.027  -22.069 19.646  1.00 31.67  ? 294 LEU   C CA  1 
ATOM   6989 C  C   . LEU   C 1 289 ? -6.052  -21.500 20.631  1.00 35.84  ? 294 LEU   C C   1 
ATOM   6990 O  O   . LEU   C 1 289 ? -7.209  -21.938 20.672  1.00 33.08  ? 294 LEU   C O   1 
ATOM   6991 C  CB  . LEU   C 1 289 ? -5.602  -22.238 18.223  1.00 31.80  ? 294 LEU   C CB  1 
ATOM   6992 C  CG  . LEU   C 1 289 ? -5.626  -20.959 17.330  1.00 35.80  ? 294 LEU   C CG  1 
ATOM   6993 C  CD1 . LEU   C 1 289 ? -6.538  -19.850 17.907  1.00 35.58  ? 294 LEU   C CD1 1 
ATOM   6994 C  CD2 . LEU   C 1 289 ? -4.221  -20.442 17.037  1.00 37.41  ? 294 LEU   C CD2 1 
ATOM   6995 N  N   . VAL   C 1 290 ? -5.612  -20.509 21.432  1.00 32.97  ? 295 VAL   C N   1 
ATOM   6996 C  CA  . VAL   C 1 290 ? -6.458  -19.992 22.510  1.00 32.63  ? 295 VAL   C CA  1 
ATOM   6997 C  C   . VAL   C 1 290 ? -6.864  -18.523 22.400  1.00 35.03  ? 295 VAL   C C   1 
ATOM   6998 O  O   . VAL   C 1 290 ? -6.300  -17.761 21.628  1.00 33.60  ? 295 VAL   C O   1 
ATOM   6999 C  CB  . VAL   C 1 290 ? -5.781  -20.252 23.881  1.00 35.18  ? 295 VAL   C CB  1 
ATOM   7000 C  CG1 . VAL   C 1 290 ? -5.608  -21.746 24.144  1.00 35.00  ? 295 VAL   C CG1 1 
ATOM   7001 C  CG2 . VAL   C 1 290 ? -4.441  -19.535 23.981  1.00 34.54  ? 295 VAL   C CG2 1 
ATOM   7002 N  N   . GLU   C 1 291 ? -7.852  -18.145 23.236  1.00 31.89  ? 296 GLU   C N   1 
ATOM   7003 C  CA  . GLU   C 1 291 ? -8.337  -16.791 23.521  1.00 31.19  ? 296 GLU   C CA  1 
ATOM   7004 C  C   . GLU   C 1 291 ? -9.188  -16.139 22.434  1.00 34.71  ? 296 GLU   C C   1 
ATOM   7005 O  O   . GLU   C 1 291 ? -9.432  -14.924 22.498  1.00 34.17  ? 296 GLU   C O   1 
ATOM   7006 C  CB  . GLU   C 1 291 ? -7.182  -15.860 23.957  1.00 32.66  ? 296 GLU   C CB  1 
ATOM   7007 C  CG  . GLU   C 1 291 ? -6.551  -16.255 25.288  1.00 34.25  ? 296 GLU   C CG  1 
ATOM   7008 C  CD  . GLU   C 1 291 ? -7.349  -15.882 26.534  1.00 47.33  ? 296 GLU   C CD  1 
ATOM   7009 O  OE1 . GLU   C 1 291 ? -8.362  -15.156 26.413  1.00 42.94  ? 296 GLU   C OE1 1 
ATOM   7010 O  OE2 . GLU   C 1 291 ? -6.954  -16.320 27.636  1.00 35.39  ? 296 GLU   C OE2 1 
ATOM   7011 N  N   . VAL   C 1 292 ? -9.747  -16.935 21.504  1.00 31.65  ? 297 VAL   C N   1 
ATOM   7012 C  CA  . VAL   C 1 292 ? -10.709 -16.416 20.536  1.00 32.54  ? 297 VAL   C CA  1 
ATOM   7013 C  C   . VAL   C 1 292 ? -12.033 -16.301 21.304  1.00 39.77  ? 297 VAL   C C   1 
ATOM   7014 O  O   . VAL   C 1 292 ? -12.509 -17.303 21.868  1.00 38.95  ? 297 VAL   C O   1 
ATOM   7015 C  CB  . VAL   C 1 292 ? -10.871 -17.285 19.268  1.00 36.59  ? 297 VAL   C CB  1 
ATOM   7016 C  CG1 . VAL   C 1 292 ? -11.943 -16.708 18.354  1.00 36.87  ? 297 VAL   C CG1 1 
ATOM   7017 C  CG2 . VAL   C 1 292 ? -9.544  -17.426 18.514  1.00 36.22  ? 297 VAL   C CG2 1 
ATOM   7018 N  N   . ASN   C 1 293 ? -12.582 -15.077 21.362  1.00 37.54  ? 298 ASN   C N   1 
ATOM   7019 C  CA  . ASN   C 1 293 ? -13.824 -14.773 22.061  1.00 38.19  ? 298 ASN   C CA  1 
ATOM   7020 C  C   . ASN   C 1 293 ? -14.740 -14.009 21.106  1.00 43.23  ? 298 ASN   C C   1 
ATOM   7021 O  O   . ASN   C 1 293 ? -14.669 -12.780 21.048  1.00 41.99  ? 298 ASN   C O   1 
ATOM   7022 C  CB  . ASN   C 1 293 ? -13.551 -13.994 23.351  1.00 40.41  ? 298 ASN   C CB  1 
ATOM   7023 C  CG  . ASN   C 1 293 ? -14.794 -13.793 24.182  1.00 48.84  ? 298 ASN   C CG  1 
ATOM   7024 O  OD1 . ASN   C 1 293 ? -15.922 -13.799 23.672  1.00 36.36  ? 298 ASN   C OD1 1 
ATOM   7025 N  ND2 . ASN   C 1 293 ? -14.616 -13.638 25.473  1.00 40.50  ? 298 ASN   C ND2 1 
ATOM   7026 N  N   . PRO   C 1 294 ? -15.617 -14.724 20.364  1.00 41.85  ? 299 PRO   C N   1 
ATOM   7027 C  CA  . PRO   C 1 294 ? -16.466 -14.042 19.361  1.00 43.19  ? 299 PRO   C CA  1 
ATOM   7028 C  C   . PRO   C 1 294 ? -17.443 -12.997 19.904  1.00 50.50  ? 299 PRO   C C   1 
ATOM   7029 O  O   . PRO   C 1 294 ? -17.881 -12.138 19.140  1.00 51.19  ? 299 PRO   C O   1 
ATOM   7030 C  CB  . PRO   C 1 294 ? -17.195 -15.182 18.632  1.00 44.71  ? 299 PRO   C CB  1 
ATOM   7031 C  CG  . PRO   C 1 294 ? -16.884 -16.414 19.357  1.00 47.91  ? 299 PRO   C CG  1 
ATOM   7032 C  CD  . PRO   C 1 294 ? -15.780 -16.194 20.326  1.00 43.49  ? 299 PRO   C CD  1 
ATOM   7033 N  N   . GLN   C 1 295 ? -17.750 -13.045 21.213  1.00 49.34  ? 300 GLN   C N   1 
ATOM   7034 C  CA  . GLN   C 1 295 ? -18.652 -12.107 21.885  1.00 50.40  ? 300 GLN   C CA  1 
ATOM   7035 C  C   . GLN   C 1 295 ? -18.045 -10.710 22.043  1.00 55.41  ? 300 GLN   C C   1 
ATOM   7036 O  O   . GLN   C 1 295 ? -18.786 -9.723  22.045  1.00 54.93  ? 300 GLN   C O   1 
ATOM   7037 C  CB  . GLN   C 1 295 ? -19.075 -12.657 23.256  1.00 52.09  ? 300 GLN   C CB  1 
ATOM   7038 C  CG  . GLN   C 1 295 ? -20.161 -13.731 23.174  1.00 69.67  ? 300 GLN   C CG  1 
ATOM   7039 C  CD  . GLN   C 1 295 ? -20.778 -14.079 24.512  1.00 91.67  ? 300 GLN   C CD  1 
ATOM   7040 O  OE1 . GLN   C 1 295 ? -20.734 -13.310 25.481  1.00 85.86  ? 300 GLN   C OE1 1 
ATOM   7041 N  NE2 . GLN   C 1 295 ? -21.405 -15.245 24.580  1.00 86.83  ? 300 GLN   C NE2 1 
ATOM   7042 N  N   . LEU   C 1 296 ? -16.701 -10.623 22.158  1.00 52.57  ? 301 LEU   C N   1 
ATOM   7043 C  CA  . LEU   C 1 296 ? -15.999 -9.347  22.342  1.00 52.03  ? 301 LEU   C CA  1 
ATOM   7044 C  C   . LEU   C 1 296 ? -15.836 -8.544  21.048  1.00 57.69  ? 301 LEU   C C   1 
ATOM   7045 O  O   . LEU   C 1 296 ? -15.369 -7.403  21.087  1.00 57.45  ? 301 LEU   C O   1 
ATOM   7046 C  CB  . LEU   C 1 296 ? -14.658 -9.540  23.060  1.00 51.56  ? 301 LEU   C CB  1 
ATOM   7047 C  CG  . LEU   C 1 296 ? -14.736 -10.090 24.483  1.00 55.66  ? 301 LEU   C CG  1 
ATOM   7048 C  CD1 . LEU   C 1 296 ? -13.380 -10.385 25.012  1.00 55.08  ? 301 LEU   C CD1 1 
ATOM   7049 C  CD2 . LEU   C 1 296 ? -15.458 -9.133  25.427  1.00 59.00  ? 301 LEU   C CD2 1 
ATOM   7050 N  N   . ALA   C 1 297 ? -16.264 -9.120  19.914  1.00 55.47  ? 302 ALA   C N   1 
ATOM   7051 C  CA  . ALA   C 1 297 ? -16.245 -8.460  18.615  1.00 55.74  ? 302 ALA   C CA  1 
ATOM   7052 C  C   . ALA   C 1 297 ? -17.394 -7.456  18.545  1.00 60.08  ? 302 ALA   C C   1 
ATOM   7053 O  O   . ALA   C 1 297 ? -18.481 -7.717  19.058  1.00 59.89  ? 302 ALA   C O   1 
ATOM   7054 C  CB  . ALA   C 1 297 ? -16.382 -9.489  17.509  1.00 56.46  ? 302 ALA   C CB  1 
ATOM   7055 N  N   . THR   C 1 298 ? -17.141 -6.303  17.933  1.00 57.25  ? 303 THR   C N   1 
ATOM   7056 C  CA  . THR   C 1 298 ? -18.124 -5.228  17.789  1.00 57.50  ? 303 THR   C CA  1 
ATOM   7057 C  C   . THR   C 1 298 ? -19.116 -5.524  16.653  1.00 63.35  ? 303 THR   C C   1 
ATOM   7058 O  O   . THR   C 1 298 ? -20.206 -4.948  16.623  1.00 63.09  ? 303 THR   C O   1 
ATOM   7059 C  CB  . THR   C 1 298 ? -17.413 -3.875  17.612  1.00 60.86  ? 303 THR   C CB  1 
ATOM   7060 O  OG1 . THR   C 1 298 ? -16.629 -3.916  16.423  1.00 57.51  ? 303 THR   C OG1 1 
ATOM   7061 C  CG2 . THR   C 1 298 ? -16.539 -3.504  18.810  1.00 56.68  ? 303 THR   C CG2 1 
ATOM   7062 N  N   . SER   C 1 299 ? -18.729 -6.423  15.724  1.00 60.73  ? 304 SER   C N   1 
ATOM   7063 C  CA  . SER   C 1 299 ? -19.540 -6.830  14.578  1.00 60.94  ? 304 SER   C CA  1 
ATOM   7064 C  C   . SER   C 1 299 ? -19.385 -8.321  14.278  1.00 65.58  ? 304 SER   C C   1 
ATOM   7065 O  O   . SER   C 1 299 ? -18.544 -8.994  14.885  1.00 65.30  ? 304 SER   C O   1 
ATOM   7066 C  CB  . SER   C 1 299 ? -19.172 -6.003  13.348  1.00 64.56  ? 304 SER   C CB  1 
ATOM   7067 O  OG  . SER   C 1 299 ? -17.830 -6.229  12.947  1.00 73.35  ? 304 SER   C OG  1 
ATOM   7068 N  N   . GLU   C 1 300 ? -20.193 -8.829  13.326  1.00 62.27  ? 305 GLU   C N   1 
ATOM   7069 C  CA  . GLU   C 1 300 ? -20.163 -10.217 12.871  1.00 61.94  ? 305 GLU   C CA  1 
ATOM   7070 C  C   . GLU   C 1 300 ? -18.857 -10.495 12.107  1.00 62.74  ? 305 GLU   C C   1 
ATOM   7071 O  O   . GLU   C 1 300 ? -18.231 -11.532 12.341  1.00 61.15  ? 305 GLU   C O   1 
ATOM   7072 C  CB  . GLU   C 1 300 ? -21.389 -10.512 11.985  1.00 63.74  ? 305 GLU   C CB  1 
ATOM   7073 C  CG  . GLU   C 1 300 ? -21.703 -11.990 11.842  1.00 78.60  ? 305 GLU   C CG  1 
ATOM   7074 C  CD  . GLU   C 1 300 ? -23.019 -12.277 11.147  1.00 108.44 ? 305 GLU   C CD  1 
ATOM   7075 O  OE1 . GLU   C 1 300 ? -24.072 -12.197 11.818  1.00 108.52 ? 305 GLU   C OE1 1 
ATOM   7076 O  OE2 . GLU   C 1 300 ? -22.997 -12.582 9.932   1.00 106.15 ? 305 GLU   C OE2 1 
ATOM   7077 N  N   . GLU   C 1 301 ? -18.439 -9.555  11.223  1.00 58.18  ? 306 GLU   C N   1 
ATOM   7078 C  CA  . GLU   C 1 301 ? -17.223 -9.682  10.418  1.00 57.58  ? 306 GLU   C CA  1 
ATOM   7079 C  C   . GLU   C 1 301 ? -15.953 -9.679  11.281  1.00 58.41  ? 306 GLU   C C   1 
ATOM   7080 O  O   . GLU   C 1 301 ? -15.020 -10.407 10.957  1.00 58.16  ? 306 GLU   C O   1 
ATOM   7081 C  CB  . GLU   C 1 301 ? -17.158 -8.656  9.262   1.00 59.33  ? 306 GLU   C CB  1 
ATOM   7082 C  CG  . GLU   C 1 301 ? -16.993 -7.192  9.651   1.00 73.56  ? 306 GLU   C CG  1 
ATOM   7083 C  CD  . GLU   C 1 301 ? -15.997 -6.417  8.805   1.00 104.09 ? 306 GLU   C CD  1 
ATOM   7084 O  OE1 . GLU   C 1 301 ? -16.000 -6.588  7.564   1.00 107.28 ? 306 GLU   C OE1 1 
ATOM   7085 O  OE2 . GLU   C 1 301 ? -15.218 -5.625  9.385   1.00 99.72  ? 306 GLU   C OE2 1 
ATOM   7086 N  N   . GLU   C 1 302 ? -15.949 -8.923  12.399  1.00 52.66  ? 307 GLU   C N   1 
ATOM   7087 C  CA  . GLU   C 1 302 ? -14.843 -8.855  13.358  1.00 51.54  ? 307 GLU   C CA  1 
ATOM   7088 C  C   . GLU   C 1 302 ? -14.631 -10.208 14.052  1.00 52.75  ? 307 GLU   C C   1 
ATOM   7089 O  O   . GLU   C 1 302 ? -13.486 -10.588 14.305  1.00 50.84  ? 307 GLU   C O   1 
ATOM   7090 C  CB  . GLU   C 1 302 ? -15.105 -7.771  14.412  1.00 53.05  ? 307 GLU   C CB  1 
ATOM   7091 C  CG  . GLU   C 1 302 ? -14.397 -6.449  14.150  1.00 63.04  ? 307 GLU   C CG  1 
ATOM   7092 C  CD  . GLU   C 1 302 ? -14.123 -5.597  15.378  1.00 75.42  ? 307 GLU   C CD  1 
ATOM   7093 O  OE1 . GLU   C 1 302 ? -14.231 -6.117  16.512  1.00 63.54  ? 307 GLU   C OE1 1 
ATOM   7094 O  OE2 . GLU   C 1 302 ? -13.783 -4.406  15.205  1.00 67.86  ? 307 GLU   C OE2 1 
ATOM   7095 N  N   . ALA   C 1 303 ? -15.734 -10.934 14.357  1.00 48.37  ? 308 ALA   C N   1 
ATOM   7096 C  CA  . ALA   C 1 303 ? -15.669 -12.258 14.991  1.00 47.72  ? 308 ALA   C CA  1 
ATOM   7097 C  C   . ALA   C 1 303 ? -15.166 -13.273 13.968  1.00 49.10  ? 308 ALA   C C   1 
ATOM   7098 O  O   . ALA   C 1 303 ? -14.259 -14.054 14.272  1.00 47.05  ? 308 ALA   C O   1 
ATOM   7099 C  CB  . ALA   C 1 303 ? -17.041 -12.668 15.523  1.00 48.58  ? 308 ALA   C CB  1 
ATOM   7100 N  N   . LYS   C 1 304 ? -15.726 -13.212 12.740  1.00 45.89  ? 309 LYS   C N   1 
ATOM   7101 C  CA  . LYS   C 1 304 ? -15.365 -14.062 11.605  1.00 45.45  ? 309 LYS   C CA  1 
ATOM   7102 C  C   . LYS   C 1 304 ? -13.890 -13.899 11.213  1.00 46.95  ? 309 LYS   C C   1 
ATOM   7103 O  O   . LYS   C 1 304 ? -13.225 -14.903 10.980  1.00 45.50  ? 309 LYS   C O   1 
ATOM   7104 C  CB  . LYS   C 1 304 ? -16.293 -13.819 10.401  1.00 48.33  ? 309 LYS   C CB  1 
ATOM   7105 C  CG  . LYS   C 1 304 ? -17.687 -14.421 10.594  1.00 67.84  ? 309 LYS   C CG  1 
ATOM   7106 C  CD  . LYS   C 1 304 ? -18.495 -14.479 9.303   1.00 79.54  ? 309 LYS   C CD  1 
ATOM   7107 C  CE  . LYS   C 1 304 ? -19.790 -15.236 9.492   1.00 91.52  ? 309 LYS   C CE  1 
ATOM   7108 N  NZ  . LYS   C 1 304 ? -20.537 -15.388 8.215   1.00 101.81 ? 309 LYS   C NZ  1 
ATOM   7109 N  N   . THR   C 1 305 ? -13.382 -12.646 11.187  1.00 42.71  ? 310 THR   C N   1 
ATOM   7110 C  CA  . THR   C 1 305 ? -11.978 -12.322 10.871  1.00 41.37  ? 310 THR   C CA  1 
ATOM   7111 C  C   . THR   C 1 305 ? -11.037 -13.044 11.845  1.00 40.48  ? 310 THR   C C   1 
ATOM   7112 O  O   . THR   C 1 305 ? -10.075 -13.687 11.401  1.00 38.15  ? 310 THR   C O   1 
ATOM   7113 C  CB  . THR   C 1 305 ? -11.760 -10.791 10.875  1.00 49.90  ? 310 THR   C CB  1 
ATOM   7114 O  OG1 . THR   C 1 305 ? -12.534 -10.195 9.832   1.00 52.96  ? 310 THR   C OG1 1 
ATOM   7115 C  CG2 . THR   C 1 305 ? -10.295 -10.392 10.711  1.00 51.88  ? 310 THR   C CG2 1 
ATOM   7116 N  N   . THR   C 1 306 ? -11.333 -12.960 13.163  1.00 36.03  ? 311 THR   C N   1 
ATOM   7117 C  CA  . THR   C 1 306 ? -10.510 -13.583 14.202  1.00 35.05  ? 311 THR   C CA  1 
ATOM   7118 C  C   . THR   C 1 306 ? -10.478 -15.104 14.045  1.00 38.17  ? 311 THR   C C   1 
ATOM   7119 O  O   . THR   C 1 306 ? -9.406  -15.712 14.144  1.00 34.95  ? 311 THR   C O   1 
ATOM   7120 C  CB  . THR   C 1 306 ? -10.937 -13.136 15.621  1.00 36.97  ? 311 THR   C CB  1 
ATOM   7121 O  OG1 . THR   C 1 306 ? -11.048 -11.709 15.678  1.00 36.49  ? 311 THR   C OG1 1 
ATOM   7122 C  CG2 . THR   C 1 306 ? -9.980  -13.627 16.703  1.00 35.96  ? 311 THR   C CG2 1 
ATOM   7123 N  N   . ALA   C 1 307 ? -11.665 -15.715 13.823  1.00 36.99  ? 312 ALA   C N   1 
ATOM   7124 C  CA  . ALA   C 1 307 ? -11.824 -17.155 13.631  1.00 36.59  ? 312 ALA   C CA  1 
ATOM   7125 C  C   . ALA   C 1 307 ? -11.093 -17.612 12.357  1.00 36.51  ? 312 ALA   C C   1 
ATOM   7126 O  O   . ALA   C 1 307 ? -10.415 -18.636 12.380  1.00 36.52  ? 312 ALA   C O   1 
ATOM   7127 C  CB  . ALA   C 1 307 ? -13.308 -17.504 13.550  1.00 37.48  ? 312 ALA   C CB  1 
ATOM   7128 N  N   . ASN   C 1 308 ? -11.194 -16.825 11.267  1.00 34.34  ? 313 ASN   C N   1 
ATOM   7129 C  CA  . ASN   C 1 308 ? -10.507 -17.109 10.007  1.00 33.67  ? 313 ASN   C CA  1 
ATOM   7130 C  C   . ASN   C 1 308 ? -8.994  -17.080 10.229  1.00 35.53  ? 313 ASN   C C   1 
ATOM   7131 O  O   . ASN   C 1 308 ? -8.288  -17.965 9.750   1.00 34.31  ? 313 ASN   C O   1 
ATOM   7132 C  CB  . ASN   C 1 308 ? -10.924 -16.127 8.920   1.00 36.10  ? 313 ASN   C CB  1 
ATOM   7133 C  CG  . ASN   C 1 308 ? -12.291 -16.386 8.339   1.00 58.75  ? 313 ASN   C CG  1 
ATOM   7134 O  OD1 . ASN   C 1 308 ? -12.735 -17.528 8.194   1.00 59.12  ? 313 ASN   C OD1 1 
ATOM   7135 N  ND2 . ASN   C 1 308 ? -12.975 -15.327 7.959   1.00 52.23  ? 313 ASN   C ND2 1 
ATOM   7136 N  N   . LEU   C 1 309 ? -8.511  -16.108 11.033  1.00 31.62  ? 314 LEU   C N   1 
ATOM   7137 C  CA  . LEU   C 1 309 ? -7.089  -16.003 11.383  1.00 30.28  ? 314 LEU   C CA  1 
ATOM   7138 C  C   . LEU   C 1 309 ? -6.632  -17.235 12.196  1.00 33.82  ? 314 LEU   C C   1 
ATOM   7139 O  O   . LEU   C 1 309 ? -5.559  -17.780 11.936  1.00 32.85  ? 314 LEU   C O   1 
ATOM   7140 C  CB  . LEU   C 1 309 ? -6.822  -14.689 12.159  1.00 28.93  ? 314 LEU   C CB  1 
ATOM   7141 C  CG  . LEU   C 1 309 ? -5.379  -14.395 12.562  1.00 32.08  ? 314 LEU   C CG  1 
ATOM   7142 C  CD1 . LEU   C 1 309 ? -4.446  -14.418 11.353  1.00 32.23  ? 314 LEU   C CD1 1 
ATOM   7143 C  CD2 . LEU   C 1 309 ? -5.289  -13.041 13.266  1.00 31.89  ? 314 LEU   C CD2 1 
ATOM   7144 N  N   . ALA   C 1 310 ? -7.471  -17.695 13.158  1.00 31.34  ? 315 ALA   C N   1 
ATOM   7145 C  CA  . ALA   C 1 310 ? -7.181  -18.873 13.974  1.00 31.81  ? 315 ALA   C CA  1 
ATOM   7146 C  C   . ALA   C 1 310 ? -6.971  -20.116 13.071  1.00 32.93  ? 315 ALA   C C   1 
ATOM   7147 O  O   . ALA   C 1 310 ? -5.981  -20.827 13.252  1.00 31.56  ? 315 ALA   C O   1 
ATOM   7148 C  CB  . ALA   C 1 310 ? -8.334  -19.113 14.950  1.00 33.20  ? 315 ALA   C CB  1 
ATOM   7149 N  N   . VAL   C 1 311 ? -7.851  -20.302 12.056  1.00 32.16  ? 316 VAL   C N   1 
ATOM   7150 C  CA  . VAL   C 1 311 ? -7.781  -21.400 11.068  1.00 32.78  ? 316 VAL   C CA  1 
ATOM   7151 C  C   . VAL   C 1 311 ? -6.461  -21.307 10.286  1.00 34.07  ? 316 VAL   C C   1 
ATOM   7152 O  O   . VAL   C 1 311 ? -5.745  -22.296 10.208  1.00 33.65  ? 316 VAL   C O   1 
ATOM   7153 C  CB  . VAL   C 1 311 ? -9.027  -21.437 10.134  1.00 37.81  ? 316 VAL   C CB  1 
ATOM   7154 C  CG1 . VAL   C 1 311 ? -8.850  -22.446 8.991   1.00 38.08  ? 316 VAL   C CG1 1 
ATOM   7155 C  CG2 . VAL   C 1 311 ? -10.293 -21.754 10.931  1.00 37.50  ? 316 VAL   C CG2 1 
ATOM   7156 N  N   . ASP   C 1 312 ? -6.096  -20.098 9.806   1.00 30.42  ? 317 ASP   C N   1 
ATOM   7157 C  CA  . ASP   C 1 312 ? -4.831  -19.915 9.073   1.00 29.53  ? 317 ASP   C CA  1 
ATOM   7158 C  C   . ASP   C 1 312 ? -3.623  -20.329 9.884   1.00 30.71  ? 317 ASP   C C   1 
ATOM   7159 O  O   . ASP   C 1 312 ? -2.724  -20.968 9.354   1.00 30.70  ? 317 ASP   C O   1 
ATOM   7160 C  CB  . ASP   C 1 312 ? -4.695  -18.484 8.535   1.00 31.07  ? 317 ASP   C CB  1 
ATOM   7161 C  CG  . ASP   C 1 312 ? -5.678  -18.103 7.447   1.00 37.96  ? 317 ASP   C CG  1 
ATOM   7162 O  OD1 . ASP   C 1 312 ? -6.260  -19.021 6.816   1.00 38.50  ? 317 ASP   C OD1 1 
ATOM   7163 O  OD2 . ASP   C 1 312 ? -5.827  -16.894 7.182   1.00 42.47  ? 317 ASP   C OD2 1 
ATOM   7164 N  N   . VAL   C 1 313 ? -3.602  -20.007 11.189  1.00 26.55  ? 318 VAL   C N   1 
ATOM   7165 C  CA  . VAL   C 1 313 ? -2.493  -20.426 12.039  1.00 26.02  ? 318 VAL   C CA  1 
ATOM   7166 C  C   . VAL   C 1 313 ? -2.383  -21.948 12.102  1.00 28.54  ? 318 VAL   C C   1 
ATOM   7167 O  O   . VAL   C 1 313 ? -1.306  -22.484 11.910  1.00 27.97  ? 318 VAL   C O   1 
ATOM   7168 C  CB  . VAL   C 1 313 ? -2.556  -19.795 13.456  1.00 30.05  ? 318 VAL   C CB  1 
ATOM   7169 C  CG1 . VAL   C 1 313 ? -1.458  -20.344 14.366  1.00 29.33  ? 318 VAL   C CG1 1 
ATOM   7170 C  CG2 . VAL   C 1 313 ? -2.477  -18.272 13.366  1.00 29.84  ? 318 VAL   C CG2 1 
ATOM   7171 N  N   . ILE   C 1 314 ? -3.489  -22.630 12.395  1.00 29.94  ? 319 ILE   C N   1 
ATOM   7172 C  CA  . ILE   C 1 314 ? -3.476  -24.087 12.559  1.00 30.21  ? 319 ILE   C CA  1 
ATOM   7173 C  C   . ILE   C 1 314 ? -3.070  -24.764 11.248  1.00 30.79  ? 319 ILE   C C   1 
ATOM   7174 O  O   . ILE   C 1 314 ? -2.141  -25.564 11.276  1.00 31.31  ? 319 ILE   C O   1 
ATOM   7175 C  CB  . ILE   C 1 314 ? -4.803  -24.639 13.155  1.00 33.78  ? 319 ILE   C CB  1 
ATOM   7176 C  CG1 . ILE   C 1 314 ? -5.142  -23.940 14.504  1.00 34.20  ? 319 ILE   C CG1 1 
ATOM   7177 C  CG2 . ILE   C 1 314 ? -4.700  -26.170 13.359  1.00 34.27  ? 319 ILE   C CG2 1 
ATOM   7178 C  CD1 . ILE   C 1 314 ? -6.649  -23.886 14.826  1.00 37.74  ? 319 ILE   C CD1 1 
ATOM   7179 N  N   . ALA   C 1 315 ? -3.675  -24.348 10.140  1.00 29.75  ? 320 ALA   C N   1 
ATOM   7180 C  CA  . ALA   C 1 315 ? -3.412  -24.854 8.776   1.00 29.57  ? 320 ALA   C CA  1 
ATOM   7181 C  C   . ALA   C 1 315 ? -1.942  -24.676 8.376   1.00 33.93  ? 320 ALA   C C   1 
ATOM   7182 O  O   . ALA   C 1 315 ? -1.318  -25.620 7.882   1.00 34.11  ? 320 ALA   C O   1 
ATOM   7183 C  CB  . ALA   C 1 315 ? -4.327  -24.183 7.780   1.00 30.75  ? 320 ALA   C CB  1 
ATOM   7184 N  N   . SER   C 1 316 ? -1.357  -23.486 8.653   1.00 29.36  ? 321 SER   C N   1 
ATOM   7185 C  CA  . SER   C 1 316 ? 0.057   -23.235 8.358   1.00 27.63  ? 321 SER   C CA  1 
ATOM   7186 C  C   . SER   C 1 316 ? 0.993   -24.070 9.203   1.00 32.27  ? 321 SER   C C   1 
ATOM   7187 O  O   . SER   C 1 316 ? 2.074   -24.446 8.750   1.00 31.47  ? 321 SER   C O   1 
ATOM   7188 C  CB  . SER   C 1 316 ? 0.375   -21.739 8.464   1.00 28.16  ? 321 SER   C CB  1 
ATOM   7189 O  OG  . SER   C 1 316 ? -0.477  -21.025 7.583   1.00 34.35  ? 321 SER   C OG  1 
ATOM   7190 N  N   . SER   C 1 317 ? 0.572   -24.418 10.445  1.00 29.63  ? 322 SER   C N   1 
ATOM   7191 C  CA  . SER   C 1 317 ? 1.373   -25.264 11.315  1.00 29.41  ? 322 SER   C CA  1 
ATOM   7192 C  C   . SER   C 1 317 ? 1.390   -26.721 10.795  1.00 32.89  ? 322 SER   C C   1 
ATOM   7193 O  O   . SER   C 1 317 ? 2.300   -27.463 11.148  1.00 32.83  ? 322 SER   C O   1 
ATOM   7194 C  CB  . SER   C 1 317 ? 0.849   -25.207 12.750  1.00 31.23  ? 322 SER   C CB  1 
ATOM   7195 O  OG  . SER   C 1 317 ? 0.683   -23.857 13.161  1.00 35.91  ? 322 SER   C OG  1 
ATOM   7196 N  N   . PHE   C 1 318 ? 0.419   -27.086 9.938   1.00 31.09  ? 323 PHE   C N   1 
ATOM   7197 C  CA  . PHE   C 1 318 ? 0.318   -28.428 9.342   1.00 31.50  ? 323 PHE   C CA  1 
ATOM   7198 C  C   . PHE   C 1 318 ? 0.586   -28.469 7.824   1.00 36.37  ? 323 PHE   C C   1 
ATOM   7199 O  O   . PHE   C 1 318 ? 0.324   -29.492 7.194   1.00 35.61  ? 323 PHE   C O   1 
ATOM   7200 C  CB  . PHE   C 1 318 ? -1.015  -29.112 9.693   1.00 33.28  ? 323 PHE   C CB  1 
ATOM   7201 C  CG  . PHE   C 1 318 ? -1.026  -29.454 11.162  1.00 34.99  ? 323 PHE   C CG  1 
ATOM   7202 C  CD1 . PHE   C 1 318 ? -0.294  -30.534 11.646  1.00 38.24  ? 323 PHE   C CD1 1 
ATOM   7203 C  CD2 . PHE   C 1 318 ? -1.687  -28.640 12.075  1.00 37.12  ? 323 PHE   C CD2 1 
ATOM   7204 C  CE1 . PHE   C 1 318 ? -0.243  -30.806 13.014  1.00 39.74  ? 323 PHE   C CE1 1 
ATOM   7205 C  CE2 . PHE   C 1 318 ? -1.624  -28.906 13.442  1.00 39.59  ? 323 PHE   C CE2 1 
ATOM   7206 C  CZ  . PHE   C 1 318 ? -0.909  -29.987 13.904  1.00 38.52  ? 323 PHE   C CZ  1 
ATOM   7207 N  N   . GLY   C 1 319 ? 1.164   -27.407 7.258   1.00 32.66  ? 324 GLY   C N   1 
ATOM   7208 C  CA  . GLY   C 1 319 ? 1.535   -27.468 5.849   1.00 32.10  ? 324 GLY   C CA  1 
ATOM   7209 C  C   . GLY   C 1 319 ? 1.040   -26.408 4.905   1.00 36.29  ? 324 GLY   C C   1 
ATOM   7210 O  O   . GLY   C 1 319 ? 1.586   -26.316 3.803   1.00 35.72  ? 324 GLY   C O   1 
ATOM   7211 N  N   . GLN   C 1 320 ? -0.013  -25.636 5.274   1.00 31.92  ? 325 GLN   C N   1 
ATOM   7212 C  CA  . GLN   C 1 320 ? -0.469  -24.559 4.398   1.00 32.28  ? 325 GLN   C CA  1 
ATOM   7213 C  C   . GLN   C 1 320 ? 0.711   -23.584 4.163   1.00 34.95  ? 325 GLN   C C   1 
ATOM   7214 O  O   . GLN   C 1 320 ? 1.407   -23.203 5.109   1.00 32.33  ? 325 GLN   C O   1 
ATOM   7215 C  CB  . GLN   C 1 320 ? -1.670  -23.820 4.982   1.00 34.17  ? 325 GLN   C CB  1 
ATOM   7216 C  CG  . GLN   C 1 320 ? -2.162  -22.663 4.123   1.00 45.75  ? 325 GLN   C CG  1 
ATOM   7217 C  CD  . GLN   C 1 320 ? -3.468  -22.136 4.629   1.00 69.48  ? 325 GLN   C CD  1 
ATOM   7218 O  OE1 . GLN   C 1 320 ? -3.525  -21.287 5.534   1.00 65.91  ? 325 GLN   C OE1 1 
ATOM   7219 N  NE2 . GLN   C 1 320 ? -4.543  -22.638 4.054   1.00 62.77  ? 325 GLN   C NE2 1 
ATOM   7220 N  N   . THR   C 1 321 ? 0.964   -23.252 2.881   1.00 35.39  ? 326 THR   C N   1 
ATOM   7221 C  CA  . THR   C 1 321 ? 2.046   -22.347 2.507   1.00 35.76  ? 326 THR   C CA  1 
ATOM   7222 C  C   . THR   C 1 321 ? 1.442   -21.194 1.720   1.00 38.66  ? 326 THR   C C   1 
ATOM   7223 O  O   . THR   C 1 321 ? 0.283   -21.242 1.315   1.00 39.75  ? 326 THR   C O   1 
ATOM   7224 C  CB  . THR   C 1 321 ? 3.078   -23.057 1.583   1.00 42.41  ? 326 THR   C CB  1 
ATOM   7225 O  OG1 . THR   C 1 321 ? 2.437   -23.363 0.342   1.00 47.11  ? 326 THR   C OG1 1 
ATOM   7226 C  CG2 . THR   C 1 321 ? 3.674   -24.324 2.193   1.00 43.79  ? 326 THR   C CG2 1 
ATOM   7227 N  N   . ARG   C 1 322 ? 2.255   -20.195 1.451   1.00 33.60  ? 327 ARG   C N   1 
ATOM   7228 C  CA  . ARG   C 1 322 ? 1.878   -19.046 0.635   1.00 32.34  ? 327 ARG   C CA  1 
ATOM   7229 C  C   . ARG   C 1 322 ? 2.544   -19.189 -0.753  1.00 35.11  ? 327 ARG   C C   1 
ATOM   7230 O  O   . ARG   C 1 322 ? 2.666   -18.221 -1.488  1.00 33.22  ? 327 ARG   C O   1 
ATOM   7231 C  CB  . ARG   C 1 322 ? 2.285   -17.759 1.348   1.00 32.39  ? 327 ARG   C CB  1 
ATOM   7232 C  CG  . ARG   C 1 322 ? 1.526   -17.647 2.675   1.00 36.45  ? 327 ARG   C CG  1 
ATOM   7233 C  CD  . ARG   C 1 322 ? 1.942   -16.458 3.488   1.00 27.85  ? 327 ARG   C CD  1 
ATOM   7234 N  NE  . ARG   C 1 322 ? 3.201   -16.696 4.180   1.00 25.87  ? 327 ARG   C NE  1 
ATOM   7235 C  CZ  . ARG   C 1 322 ? 3.978   -15.718 4.636   1.00 27.37  ? 327 ARG   C CZ  1 
ATOM   7236 N  NH1 . ARG   C 1 322 ? 3.643   -14.448 4.437   1.00 25.16  ? 327 ARG   C NH1 1 
ATOM   7237 N  NH2 . ARG   C 1 322 ? 5.101   -16.002 5.285   1.00 24.11  ? 327 ARG   C NH2 1 
ATOM   7238 N  N   . GLU   C 1 323 ? 2.955   -20.422 -1.109  1.00 35.83  ? 328 GLU   C N   1 
ATOM   7239 C  CA  . GLU   C 1 323 ? 3.611   -20.732 -2.391  1.00 36.53  ? 328 GLU   C CA  1 
ATOM   7240 C  C   . GLU   C 1 323 ? 2.969   -21.954 -3.063  1.00 42.74  ? 328 GLU   C C   1 
ATOM   7241 O  O   . GLU   C 1 323 ? 3.308   -22.284 -4.196  1.00 42.92  ? 328 GLU   C O   1 
ATOM   7242 C  CB  . GLU   C 1 323 ? 5.124   -20.926 -2.201  1.00 37.96  ? 328 GLU   C CB  1 
ATOM   7243 C  CG  . GLU   C 1 323 ? 5.856   -19.652 -1.811  1.00 50.20  ? 328 GLU   C CG  1 
ATOM   7244 C  CD  . GLU   C 1 323 ? 7.341   -19.762 -1.527  1.00 63.20  ? 328 GLU   C CD  1 
ATOM   7245 O  OE1 . GLU   C 1 323 ? 7.973   -20.729 -2.020  1.00 49.98  ? 328 GLU   C OE1 1 
ATOM   7246 O  OE2 . GLU   C 1 323 ? 7.884   -18.841 -0.866  1.00 35.97  ? 328 GLU   C OE2 1 
ATOM   7247 N  N   . GLY   C 1 324 ? 1.990   -22.549 -2.388  1.00 42.04  ? 329 GLY   C N   1 
ATOM   7248 C  CA  . GLY   C 1 324 ? 1.239   -23.706 -2.860  1.00 43.38  ? 329 GLY   C CA  1 
ATOM   7249 C  C   . GLY   C 1 324 ? 2.020   -24.999 -2.996  1.00 49.27  ? 329 GLY   C C   1 
ATOM   7250 O  O   . GLY   C 1 324 ? 1.672   -25.827 -3.841  1.00 49.80  ? 329 GLY   C O   1 
ATOM   7251 N  N   . GLY   C 1 325 ? 3.054   -25.182 -2.169  1.00 46.40  ? 330 GLY   C N   1 
ATOM   7252 C  CA  . GLY   C 1 325 ? 3.894   -26.379 -2.216  1.00 46.95  ? 330 GLY   C CA  1 
ATOM   7253 C  C   . GLY   C 1 325 ? 3.492   -27.521 -1.297  1.00 53.45  ? 330 GLY   C C   1 
ATOM   7254 O  O   . GLY   C 1 325 ? 4.275   -28.458 -1.106  1.00 53.78  ? 330 GLY   C O   1 
ATOM   7255 N  N   . HIS   C 1 326 ? 2.271   -27.465 -0.733  1.00 51.55  ? 331 HIS   C N   1 
ATOM   7256 C  CA  . HIS   C 1 326 ? 1.756   -28.473 0.201   1.00 52.91  ? 331 HIS   C CA  1 
ATOM   7257 C  C   . HIS   C 1 326 ? 1.480   -29.846 -0.459  1.00 57.46  ? 331 HIS   C C   1 
ATOM   7258 O  O   . HIS   C 1 326 ? 1.844   -30.880 0.109   1.00 57.70  ? 331 HIS   C O   1 
ATOM   7259 C  CB  . HIS   C 1 326 ? 0.514   -27.935 0.947   1.00 54.44  ? 331 HIS   C CB  1 
ATOM   7260 C  CG  . HIS   C 1 326 ? -0.646  -27.596 0.058   1.00 58.89  ? 331 HIS   C CG  1 
ATOM   7261 N  ND1 . HIS   C 1 326 ? -0.510  -26.727 -1.018  1.00 61.11  ? 331 HIS   C ND1 1 
ATOM   7262 C  CD2 . HIS   C 1 326 ? -1.924  -28.038 0.102   1.00 61.51  ? 331 HIS   C CD2 1 
ATOM   7263 C  CE1 . HIS   C 1 326 ? -1.705  -26.666 -1.586  1.00 60.90  ? 331 HIS   C CE1 1 
ATOM   7264 N  NE2 . HIS   C 1 326 ? -2.588  -27.444 -0.954  1.00 61.45  ? 331 HIS   C NE2 1 
ATOM   7265 N  N   . ILE   C 1 327 ? 0.855   -29.838 -1.652  1.00 53.66  ? 332 ILE   C N   1 
ATOM   7266 C  CA  . ILE   C 1 327 ? 0.474   -31.017 -2.446  1.00 53.56  ? 332 ILE   C CA  1 
ATOM   7267 C  C   . ILE   C 1 327 ? 1.611   -31.461 -3.388  1.00 56.13  ? 332 ILE   C C   1 
ATOM   7268 O  O   . ILE   C 1 327 ? 2.249   -30.621 -4.035  1.00 55.56  ? 332 ILE   C O   1 
ATOM   7269 C  CB  . ILE   C 1 327 ? -0.867  -30.728 -3.210  1.00 57.06  ? 332 ILE   C CB  1 
ATOM   7270 C  CG1 . ILE   C 1 327 ? -2.072  -30.734 -2.241  1.00 58.06  ? 332 ILE   C CG1 1 
ATOM   7271 C  CG2 . ILE   C 1 327 ? -1.107  -31.685 -4.393  1.00 58.02  ? 332 ILE   C CG2 1 
ATOM   7272 C  CD1 . ILE   C 1 327 ? -3.404  -30.168 -2.808  1.00 66.72  ? 332 ILE   C CD1 1 
ATOM   7273 N  N   . VAL   C 1 328 ? 1.850   -32.785 -3.462  1.00 51.44  ? 333 VAL   C N   1 
ATOM   7274 C  CA  . VAL   C 1 328 ? 2.839   -33.373 -4.364  1.00 51.00  ? 333 VAL   C CA  1 
ATOM   7275 C  C   . VAL   C 1 328 ? 2.262   -33.271 -5.789  1.00 50.77  ? 333 VAL   C C   1 
ATOM   7276 O  O   . VAL   C 1 328 ? 1.124   -33.687 -6.031  1.00 50.67  ? 333 VAL   C O   1 
ATOM   7277 C  CB  . VAL   C 1 328 ? 3.232   -34.833 -3.964  1.00 56.10  ? 333 VAL   C CB  1 
ATOM   7278 C  CG1 . VAL   C 1 328 ? 4.025   -35.534 -5.072  1.00 56.11  ? 333 VAL   C CG1 1 
ATOM   7279 C  CG2 . VAL   C 1 328 ? 4.029   -34.847 -2.656  1.00 56.20  ? 333 VAL   C CG2 1 
ATOM   7280 N  N   . TYR   C 1 329 ? 3.022   -32.642 -6.693  1.00 43.32  ? 334 TYR   C N   1 
ATOM   7281 C  CA  . TYR   C 1 329 ? 2.655   -32.471 -8.103  1.00 41.64  ? 334 TYR   C CA  1 
ATOM   7282 C  C   . TYR   C 1 329 ? 3.952   -32.650 -8.893  1.00 45.52  ? 334 TYR   C C   1 
ATOM   7283 O  O   . TYR   C 1 329 ? 4.927   -31.939 -8.635  1.00 44.78  ? 334 TYR   C O   1 
ATOM   7284 C  CB  . TYR   C 1 329 ? 2.019   -31.083 -8.329  1.00 40.57  ? 334 TYR   C CB  1 
ATOM   7285 C  CG  . TYR   C 1 329 ? 1.294   -30.931 -9.649  1.00 37.95  ? 334 TYR   C CG  1 
ATOM   7286 C  CD1 . TYR   C 1 329 ? 1.999   -30.778 -10.841 1.00 38.92  ? 334 TYR   C CD1 1 
ATOM   7287 C  CD2 . TYR   C 1 329 ? -0.094  -30.873 -9.700  1.00 37.16  ? 334 TYR   C CD2 1 
ATOM   7288 C  CE1 . TYR   C 1 329 ? 1.338   -30.612 -12.057 1.00 37.16  ? 334 TYR   C CE1 1 
ATOM   7289 C  CE2 . TYR   C 1 329 ? -0.767  -30.720 -10.914 1.00 37.32  ? 334 TYR   C CE2 1 
ATOM   7290 C  CZ  . TYR   C 1 329 ? -0.042  -30.584 -12.087 1.00 40.16  ? 334 TYR   C CZ  1 
ATOM   7291 O  OH  . TYR   C 1 329 ? -0.677  -30.413 -13.285 1.00 37.98  ? 334 TYR   C OH  1 
ATOM   7292 N  N   . ASP   C 1 330 ? 4.001   -33.639 -9.801  1.00 42.39  ? 335 ASP   C N   1 
ATOM   7293 C  CA  . ASP   C 1 330 ? 5.258   -33.884 -10.508 1.00 42.64  ? 335 ASP   C CA  1 
ATOM   7294 C  C   . ASP   C 1 330 ? 5.118   -34.088 -12.015 1.00 43.45  ? 335 ASP   C C   1 
ATOM   7295 O  O   . ASP   C 1 330 ? 6.144   -34.302 -12.672 1.00 42.70  ? 335 ASP   C O   1 
ATOM   7296 C  CB  . ASP   C 1 330 ? 6.047   -35.056 -9.869  1.00 45.22  ? 335 ASP   C CB  1 
ATOM   7297 C  CG  . ASP   C 1 330 ? 5.299   -36.371 -9.696  1.00 60.18  ? 335 ASP   C CG  1 
ATOM   7298 O  OD1 . ASP   C 1 330 ? 4.325   -36.614 -10.454 1.00 60.53  ? 335 ASP   C OD1 1 
ATOM   7299 O  OD2 . ASP   C 1 330 ? 5.712   -37.177 -8.829  1.00 67.23  ? 335 ASP   C OD2 1 
ATOM   7300 N  N   . GLN   C 1 331 ? 3.885   -33.970 -12.573 1.00 38.13  ? 336 GLN   C N   1 
ATOM   7301 C  CA  . GLN   C 1 331 ? 3.701   -34.099 -14.027 1.00 38.04  ? 336 GLN   C CA  1 
ATOM   7302 C  C   . GLN   C 1 331 ? 2.593   -33.198 -14.575 1.00 38.89  ? 336 GLN   C C   1 
ATOM   7303 O  O   . GLN   C 1 331 ? 1.471   -33.210 -14.076 1.00 38.26  ? 336 GLN   C O   1 
ATOM   7304 C  CB  . GLN   C 1 331 ? 3.504   -35.566 -14.478 1.00 39.75  ? 336 GLN   C CB  1 
ATOM   7305 C  CG  . GLN   C 1 331 ? 2.244   -36.257 -13.941 1.00 60.76  ? 336 GLN   C CG  1 
ATOM   7306 C  CD  . GLN   C 1 331 ? 2.092   -37.679 -14.429 1.00 85.49  ? 336 GLN   C CD  1 
ATOM   7307 O  OE1 . GLN   C 1 331 ? 2.018   -38.620 -13.633 1.00 82.55  ? 336 GLN   C OE1 1 
ATOM   7308 N  NE2 . GLN   C 1 331 ? 2.002   -37.867 -15.744 1.00 78.81  ? 336 GLN   C NE2 1 
ATOM   7309 N  N   . LEU   C 1 332 ? 2.904   -32.436 -15.620 1.00 34.35  ? 337 LEU   C N   1 
ATOM   7310 C  CA  . LEU   C 1 332 ? 1.899   -31.574 -16.214 1.00 32.88  ? 337 LEU   C CA  1 
ATOM   7311 C  C   . LEU   C 1 332 ? 1.027   -32.334 -17.228 1.00 35.72  ? 337 LEU   C C   1 
ATOM   7312 O  O   . LEU   C 1 332 ? 1.551   -33.157 -17.990 1.00 36.66  ? 337 LEU   C O   1 
ATOM   7313 C  CB  . LEU   C 1 332 ? 2.567   -30.385 -16.932 1.00 32.79  ? 337 LEU   C CB  1 
ATOM   7314 C  CG  . LEU   C 1 332 ? 3.019   -29.197 -16.089 1.00 37.06  ? 337 LEU   C CG  1 
ATOM   7315 C  CD1 . LEU   C 1 332 ? 3.772   -28.205 -16.952 1.00 36.68  ? 337 LEU   C CD1 1 
ATOM   7316 C  CD2 . LEU   C 1 332 ? 1.827   -28.504 -15.398 1.00 36.19  ? 337 LEU   C CD2 1 
ATOM   7317 N  N   . PRO   C 1 333 ? -0.284  -32.038 -17.285 1.00 32.73  ? 338 PRO   C N   1 
ATOM   7318 C  CA  . PRO   C 1 333 ? -1.112  -32.642 -18.330 1.00 32.95  ? 338 PRO   C CA  1 
ATOM   7319 C  C   . PRO   C 1 333 ? -0.689  -32.098 -19.697 1.00 37.59  ? 338 PRO   C C   1 
ATOM   7320 O  O   . PRO   C 1 333 ? -0.271  -30.940 -19.785 1.00 35.10  ? 338 PRO   C O   1 
ATOM   7321 C  CB  . PRO   C 1 333 ? -2.534  -32.215 -17.964 1.00 34.62  ? 338 PRO   C CB  1 
ATOM   7322 C  CG  . PRO   C 1 333 ? -2.381  -30.998 -17.142 1.00 38.89  ? 338 PRO   C CG  1 
ATOM   7323 C  CD  . PRO   C 1 333 ? -1.052  -31.077 -16.464 1.00 34.44  ? 338 PRO   C CD  1 
ATOM   7324 N  N   . THR   C 1 334 ? -0.775  -32.943 -20.748 1.00 33.91  ? 339 THR   C N   1 
ATOM   7325 C  CA  . THR   C 1 334 ? -0.389  -32.624 -22.128 1.00 33.48  ? 339 THR   C CA  1 
ATOM   7326 C  C   . THR   C 1 334 ? -1.628  -32.620 -23.062 1.00 38.70  ? 339 THR   C C   1 
ATOM   7327 O  O   . THR   C 1 334 ? -2.522  -33.461 -22.903 1.00 39.01  ? 339 THR   C O   1 
ATOM   7328 C  CB  . THR   C 1 334 ? 0.713   -33.560 -22.617 1.00 42.72  ? 339 THR   C CB  1 
ATOM   7329 O  OG1 . THR   C 1 334 ? 0.258   -34.908 -22.503 1.00 44.57  ? 339 THR   C OG1 1 
ATOM   7330 C  CG2 . THR   C 1 334 ? 2.014   -33.392 -21.845 1.00 41.30  ? 339 THR   C CG2 1 
ATOM   7331 N  N   . PRO   C 1 335 ? -1.710  -31.659 -24.018 1.00 36.02  ? 340 PRO   C N   1 
ATOM   7332 C  CA  . PRO   C 1 335 ? -2.898  -31.566 -24.889 1.00 37.07  ? 340 PRO   C CA  1 
ATOM   7333 C  C   . PRO   C 1 335 ? -3.028  -32.664 -25.947 1.00 47.59  ? 340 PRO   C C   1 
ATOM   7334 O  O   . PRO   C 1 335 ? -2.051  -33.344 -26.239 1.00 41.63  ? 340 PRO   C O   1 
ATOM   7335 C  CB  . PRO   C 1 335 ? -2.734  -30.184 -25.539 1.00 38.72  ? 340 PRO   C CB  1 
ATOM   7336 C  CG  . PRO   C 1 335 ? -1.291  -29.974 -25.587 1.00 42.12  ? 340 PRO   C CG  1 
ATOM   7337 C  CD  . PRO   C 1 335 ? -0.766  -30.558 -24.302 1.00 37.90  ? 340 PRO   C CD  1 
HETATM 7338 MN MN  . MN    D 2 .   ? -3.660  -11.364 -11.720 1.00 29.95  ? 401 MN    A MN  1 
HETATM 7339 MN MN  . MN    E 2 .   ? -4.402  -11.685 -8.520  1.00 31.00  ? 402 MN    A MN  1 
HETATM 7340 C  C7  . A1H0B F 3 .   ? -7.242  -17.922 -9.054  1.00 34.36  ? 403 A1H0B A C7  1 
HETATM 7341 C  C9  . A1H0B F 3 .   ? -6.335  -17.921 -7.800  1.00 33.64  ? 403 A1H0B A C9  1 
HETATM 7342 C  C10 . A1H0B F 3 .   ? -5.179  -18.911 -8.136  1.00 34.58  ? 403 A1H0B A C10 1 
HETATM 7343 C  C12 . A1H0B F 3 .   ? -7.117  -19.410 -9.447  1.00 34.42  ? 403 A1H0B A C12 1 
HETATM 7344 C  C14 . A1H0B F 3 .   ? -7.623  -19.695 -10.839 1.00 33.27  ? 403 A1H0B A C14 1 
HETATM 7345 O  O1  . A1H0B F 3 .   ? -6.857  -12.185 -9.670  1.00 37.43  ? 403 A1H0B A O1  1 
HETATM 7346 B  B2  . A1H0B F 3 .   ? -6.044  -13.129 -10.349 1.00 36.37  ? 403 A1H0B A B2  1 
HETATM 7347 O  O3  . A1H0B F 3 .   ? -4.668  -12.845 -10.479 1.00 33.50  ? 403 A1H0B A O3  1 
HETATM 7348 C  C4  . A1H0B F 3 .   ? -6.632  -14.478 -10.922 1.00 36.48  ? 403 A1H0B A C4  1 
HETATM 7349 C  C5  . A1H0B F 3 .   ? -7.033  -15.429 -9.776  1.00 36.04  ? 403 A1H0B A C5  1 
HETATM 7350 C  C6  . A1H0B F 3 .   ? -6.769  -16.909 -10.131 1.00 35.35  ? 403 A1H0B A C6  1 
HETATM 7351 N  N11 . A1H0B F 3 .   ? -5.677  -19.733 -9.279  1.00 35.36  ? 403 A1H0B A N11 1 
HETATM 7352 O  O15 . A1H0B F 3 .   ? -6.923  -20.219 -11.664 1.00 33.26  ? 403 A1H0B A O15 1 
HETATM 7353 O  O16 . A1H0B F 3 .   ? -8.867  -19.332 -11.141 1.00 34.74  ? 403 A1H0B A O16 1 
HETATM 7354 H  H8  . A1H0B F 3 .   ? -8.273  -17.711 -8.770  1.00 34.35  ? 403 A1H0B A H8  1 
HETATM 7355 H  H13 . A1H0B F 3 .   ? -7.700  -20.019 -8.752  1.00 34.18  ? 403 A1H0B A H13 1 
HETATM 7356 MN MN  . MN    G 2 .   ? 5.507   19.146  11.780  1.00 26.13  ? 401 MN    B MN  1 
HETATM 7357 MN MN  . MN    H 2 .   ? 3.780   17.033  9.875   1.00 25.81  ? 402 MN    B MN  1 
HETATM 7358 C  C7  . A1H0B I 3 .   ? 2.506   21.485  4.861   1.00 31.37  ? 403 A1H0B B C7  1 
HETATM 7359 C  C9  . A1H0B I 3 .   ? 2.925   20.111  4.280   1.00 31.03  ? 403 A1H0B B C9  1 
HETATM 7360 C  C10 . A1H0B I 3 .   ? 4.302   20.349  3.604   1.00 30.18  ? 403 A1H0B B C10 1 
HETATM 7361 C  C12 . A1H0B I 3 .   ? 3.105   22.397  3.761   1.00 32.32  ? 403 A1H0B B C12 1 
HETATM 7362 C  C14 . A1H0B I 3 .   ? 3.194   23.853  4.152   1.00 31.73  ? 403 A1H0B B C14 1 
HETATM 7363 O  O1  . A1H0B I 3 .   ? 2.141   19.119  10.065  1.00 28.48  ? 403 A1H0B B O1  1 
HETATM 7364 B  B2  . A1H0B I 3 .   ? 3.280   19.785  9.576   1.00 28.98  ? 403 A1H0B B B2  1 
HETATM 7365 O  O3  . A1H0B I 3 .   ? 4.516   19.130  9.704   1.00 25.98  ? 403 A1H0B B O3  1 
HETATM 7366 C  C4  . A1H0B I 3 .   ? 3.181   21.121  8.750   1.00 26.80  ? 403 A1H0B B C4  1 
HETATM 7367 C  C5  . A1H0B I 3 .   ? 2.683   20.727  7.349   1.00 26.82  ? 403 A1H0B B C5  1 
HETATM 7368 C  C6  . A1H0B I 3 .   ? 3.093   21.752  6.277   1.00 28.99  ? 403 A1H0B B C6  1 
HETATM 7369 N  N11 . A1H0B I 3 .   ? 4.449   21.839  3.467   1.00 31.98  ? 403 A1H0B B N11 1 
HETATM 7370 O  O15 . A1H0B I 3 .   ? 4.233   24.465  4.114   1.00 29.87  ? 403 A1H0B B O15 1 
HETATM 7371 O  O16 . A1H0B I 3 .   ? 2.086   24.454  4.539   1.00 31.83  ? 403 A1H0B B O16 1 
HETATM 7372 H  H8  . A1H0B I 3 .   ? 1.419   21.567  4.871   1.00 30.82  ? 403 A1H0B B H8  1 
HETATM 7373 H  H13 . A1H0B I 3 .   ? 2.487   22.333  2.863   1.00 32.08  ? 403 A1H0B B H13 1 
HETATM 7374 MN MN  . MN    J 2 .   ? -1.973  -16.261 26.825  1.00 32.45  ? 401 MN    C MN  1 
HETATM 7375 MN MN  . MN    K 2 .   ? -2.245  -13.098 25.792  1.00 31.47  ? 402 MN    C MN  1 
HETATM 7376 C  C7  . A1H0B L 3 .   ? -2.818  -10.368 31.968  1.00 34.71  ? 403 A1H0B C C7  1 
HETATM 7377 C  C9  . A1H0B L 3 .   ? -1.854  -9.469  31.152  1.00 31.33  ? 403 A1H0B C C9  1 
HETATM 7378 C  C10 . A1H0B L 3 .   ? -0.465  -9.692  31.816  1.00 31.16  ? 403 A1H0B C C10 1 
HETATM 7379 C  C12 . A1H0B L 3 .   ? -2.227  -10.109 33.374  1.00 33.88  ? 403 A1H0B C C12 1 
HETATM 7380 C  C14 . A1H0B L 3 .   ? -2.735  -11.071 34.430  1.00 33.69  ? 403 A1H0B C C14 1 
HETATM 7381 O  O1  . A1H0B L 3 .   ? -4.473  -13.439 27.404  1.00 35.22  ? 403 A1H0B C O1  1 
HETATM 7382 B  B2  . A1H0B L 3 .   ? -3.397  -13.756 28.258  1.00 33.61  ? 403 A1H0B C B2  1 
HETATM 7383 O  O3  . A1H0B L 3 .   ? -2.201  -14.211 27.699  1.00 32.77  ? 403 A1H0B C O3  1 
HETATM 7384 C  C4  . A1H0B L 3 .   ? -3.452  -13.579 29.823  1.00 35.11  ? 403 A1H0B C C4  1 
HETATM 7385 C  C5  . A1H0B L 3 .   ? -3.344  -12.080 30.134  1.00 35.37  ? 403 A1H0B C C5  1 
HETATM 7386 C  C6  . A1H0B L 3 .   ? -2.793  -11.864 31.550  1.00 33.72  ? 403 A1H0B C C6  1 
HETATM 7387 N  N11 . A1H0B L 3 .   ? -0.756  -10.185 33.201  1.00 33.51  ? 403 A1H0B C N11 1 
HETATM 7388 O  O15 . A1H0B L 3 .   ? -4.055  -11.166 34.614  1.00 36.43  ? 403 A1H0B C O15 1 
HETATM 7389 O  O16 . A1H0B L 3 .   ? -1.976  -11.745 35.086  1.00 31.09  ? 403 A1H0B C O16 1 
HETATM 7390 H  H8  . A1H0B L 3 .   ? -3.833  -9.975  31.909  1.00 34.81  ? 403 A1H0B C H8  1 
HETATM 7391 H  H13 . A1H0B L 3 .   ? -2.490  -9.097  33.689  1.00 34.29  ? 403 A1H0B C H13 1 
HETATM 7392 O  O   . HOH   M 4 .   ? -7.619  -20.407 -14.198 1.00 34.71  ? 501 HOH   A O   1 
HETATM 7393 O  O   . HOH   M 4 .   ? 16.002  -2.016  -4.012  1.00 24.33  ? 502 HOH   A O   1 
HETATM 7394 O  O   . HOH   M 4 .   ? 7.043   -27.820 -21.550 1.00 51.13  ? 503 HOH   A O   1 
HETATM 7395 O  O   . HOH   M 4 .   ? 14.895  12.024  -3.307  1.00 49.47  ? 504 HOH   A O   1 
HETATM 7396 O  O   . HOH   M 4 .   ? 16.407  -1.808  -6.762  1.00 33.93  ? 505 HOH   A O   1 
HETATM 7397 O  O   . HOH   M 4 .   ? 9.853   -11.311 -27.258 1.00 43.21  ? 506 HOH   A O   1 
HETATM 7398 O  O   . HOH   M 4 .   ? -11.040 -7.889  -9.575  1.00 32.82  ? 507 HOH   A O   1 
HETATM 7399 O  O   . HOH   M 4 .   ? -15.707 -23.800 -15.506 1.00 48.80  ? 508 HOH   A O   1 
HETATM 7400 O  O   . HOH   M 4 .   ? -8.430  -9.836  -7.520  1.00 36.41  ? 509 HOH   A O   1 
HETATM 7401 O  O   . HOH   M 4 .   ? -2.374  -17.363 1.339   1.00 41.65  ? 510 HOH   A O   1 
HETATM 7402 O  O   . HOH   M 4 .   ? -9.635  -14.069 -31.491 1.00 40.80  ? 511 HOH   A O   1 
HETATM 7403 O  O   . HOH   M 4 .   ? -4.044  -18.767 -11.347 1.00 32.06  ? 512 HOH   A O   1 
HETATM 7404 O  O   . HOH   M 4 .   ? 2.797   -20.997 -24.293 1.00 36.17  ? 513 HOH   A O   1 
HETATM 7405 O  O   . HOH   M 4 .   ? 9.094   7.260   -8.546  1.00 32.33  ? 514 HOH   A O   1 
HETATM 7406 O  O   . HOH   M 4 .   ? -3.657  7.499   -1.880  1.00 52.15  ? 515 HOH   A O   1 
HETATM 7407 O  O   . HOH   M 4 .   ? 8.645   -10.621 -29.575 1.00 39.58  ? 516 HOH   A O   1 
HETATM 7408 O  O   . HOH   M 4 .   ? 16.330  7.631   -0.088  1.00 35.37  ? 517 HOH   A O   1 
HETATM 7409 O  O   . HOH   M 4 .   ? -16.592 -15.056 -17.390 1.00 53.90  ? 518 HOH   A O   1 
HETATM 7410 O  O   . HOH   M 4 .   ? 8.243   2.847   -27.356 1.00 45.70  ? 519 HOH   A O   1 
HETATM 7411 O  O   . HOH   M 4 .   ? 9.273   5.386   -15.477 1.00 36.25  ? 520 HOH   A O   1 
HETATM 7412 O  O   . HOH   M 4 .   ? 6.872   -9.696  7.455   1.00 30.82  ? 521 HOH   A O   1 
HETATM 7413 O  O   . HOH   M 4 .   ? -14.683 -16.643 -16.246 1.00 43.02  ? 522 HOH   A O   1 
HETATM 7414 O  O   . HOH   M 4 .   ? -0.904  -28.308 -19.402 1.00 34.51  ? 523 HOH   A O   1 
HETATM 7415 O  O   . HOH   M 4 .   ? 9.623   -5.322  3.075   1.00 22.19  ? 524 HOH   A O   1 
HETATM 7416 O  O   . HOH   M 4 .   ? -18.642 -11.372 -25.741 1.00 46.10  ? 525 HOH   A O   1 
HETATM 7417 O  O   . HOH   M 4 .   ? -1.850  -18.211 -8.429  1.00 29.72  ? 526 HOH   A O   1 
HETATM 7418 O  O   . HOH   M 4 .   ? 1.773   -12.985 -28.850 1.00 43.50  ? 527 HOH   A O   1 
HETATM 7419 O  O   . HOH   M 4 .   ? -7.806  -3.036  -32.046 1.00 44.06  ? 528 HOH   A O   1 
HETATM 7420 O  O   . HOH   M 4 .   ? 11.282  11.440  -9.615  1.00 48.29  ? 529 HOH   A O   1 
HETATM 7421 O  O   . HOH   M 4 .   ? 11.697  6.841   -7.957  1.00 38.26  ? 530 HOH   A O   1 
HETATM 7422 O  O   . HOH   M 4 .   ? 14.130  -26.629 -12.192 1.00 41.67  ? 531 HOH   A O   1 
HETATM 7423 O  O   . HOH   M 4 .   ? -10.677 -17.344 -10.702 1.00 37.12  ? 532 HOH   A O   1 
HETATM 7424 O  O   . HOH   M 4 .   ? 19.099  -0.619  -3.879  1.00 37.13  ? 533 HOH   A O   1 
HETATM 7425 O  O   . HOH   M 4 .   ? -9.863  -11.385 -9.393  1.00 45.92  ? 534 HOH   A O   1 
HETATM 7426 O  O   . HOH   M 4 .   ? -14.720 1.495   -17.055 1.00 44.35  ? 535 HOH   A O   1 
HETATM 7427 O  O   . HOH   M 4 .   ? 7.221   1.918   -24.765 1.00 35.70  ? 536 HOH   A O   1 
HETATM 7428 O  O   . HOH   M 4 .   ? 11.418  -21.175 -9.066  1.00 36.68  ? 537 HOH   A O   1 
HETATM 7429 O  O   . HOH   M 4 .   ? 12.374  -16.024 -13.992 1.00 26.79  ? 538 HOH   A O   1 
HETATM 7430 O  O   . HOH   M 4 .   ? 21.231  -5.194  -0.260  1.00 44.44  ? 539 HOH   A O   1 
HETATM 7431 O  O   . HOH   M 4 .   ? 12.371  -11.444 8.750   1.00 27.19  ? 540 HOH   A O   1 
HETATM 7432 O  O   . HOH   M 4 .   ? 12.692  -23.227 -18.158 1.00 42.20  ? 541 HOH   A O   1 
HETATM 7433 O  O   . HOH   M 4 .   ? 1.084   -13.409 3.273   1.00 27.72  ? 542 HOH   A O   1 
HETATM 7434 O  O   . HOH   M 4 .   ? 13.674  -16.395 0.865   1.00 40.34  ? 543 HOH   A O   1 
HETATM 7435 O  O   . HOH   M 4 .   ? -4.314  8.791   -5.207  1.00 32.59  ? 544 HOH   A O   1 
HETATM 7436 O  O   . HOH   M 4 .   ? 12.273  -11.206 -24.278 1.00 45.37  ? 545 HOH   A O   1 
HETATM 7437 O  O   . HOH   M 4 .   ? -8.100  11.012  -15.087 1.00 41.49  ? 546 HOH   A O   1 
HETATM 7438 O  O   . HOH   M 4 .   ? -4.812  -21.602 -26.660 1.00 35.96  ? 547 HOH   A O   1 
HETATM 7439 O  O   . HOH   M 4 .   ? 0.103   -1.924  -20.999 1.00 30.88  ? 548 HOH   A O   1 
HETATM 7440 O  O   . HOH   M 4 .   ? -3.535  -8.389  -32.606 1.00 44.74  ? 549 HOH   A O   1 
HETATM 7441 O  O   . HOH   M 4 .   ? 7.442   -30.606 -17.656 1.00 43.03  ? 550 HOH   A O   1 
HETATM 7442 O  O   . HOH   M 4 .   ? 0.665   -4.887  -34.387 1.00 43.68  ? 551 HOH   A O   1 
HETATM 7443 O  O   . HOH   M 4 .   ? 6.382   -4.968  5.465   1.00 23.88  ? 552 HOH   A O   1 
HETATM 7444 O  O   . HOH   M 4 .   ? 5.985   -2.194  5.040   1.00 23.25  ? 553 HOH   A O   1 
HETATM 7445 O  O   . HOH   M 4 .   ? 16.630  -12.620 -17.702 1.00 37.88  ? 554 HOH   A O   1 
HETATM 7446 O  O   . HOH   M 4 .   ? -7.859  -2.133  -12.661 1.00 30.02  ? 555 HOH   A O   1 
HETATM 7447 O  O   . HOH   M 4 .   ? -14.638 -9.892  -26.556 1.00 52.26  ? 556 HOH   A O   1 
HETATM 7448 O  O   . HOH   M 4 .   ? -13.988 -9.068  -2.832  1.00 44.96  ? 557 HOH   A O   1 
HETATM 7449 O  O   . HOH   M 4 .   ? -12.496 -16.683 -18.617 1.00 34.46  ? 558 HOH   A O   1 
HETATM 7450 O  O   . HOH   M 4 .   ? -12.613 6.711   -8.107  1.00 41.93  ? 559 HOH   A O   1 
HETATM 7451 O  O   . HOH   M 4 .   ? 19.791  -0.456  2.995   1.00 37.12  ? 560 HOH   A O   1 
HETATM 7452 O  O   . HOH   M 4 .   ? 6.065   7.155   -4.387  1.00 36.06  ? 561 HOH   A O   1 
HETATM 7453 O  O   . HOH   M 4 .   ? 18.071  -5.571  -24.923 1.00 38.73  ? 562 HOH   A O   1 
HETATM 7454 O  O   . HOH   M 4 .   ? -18.598 -27.545 -22.539 1.00 44.14  ? 563 HOH   A O   1 
HETATM 7455 O  O   . HOH   M 4 .   ? -0.071  -6.205  4.742   1.00 37.24  ? 564 HOH   A O   1 
HETATM 7456 O  O   . HOH   M 4 .   ? -5.556  -9.269  -2.196  1.00 28.37  ? 565 HOH   A O   1 
HETATM 7457 O  O   . HOH   M 4 .   ? -2.068  18.432  -13.517 1.00 47.47  ? 566 HOH   A O   1 
HETATM 7458 O  O   . HOH   M 4 .   ? 19.972  -4.743  -8.774  1.00 35.14  ? 567 HOH   A O   1 
HETATM 7459 O  O   . HOH   M 4 .   ? 21.203  -2.959  -17.502 1.00 47.99  ? 568 HOH   A O   1 
HETATM 7460 O  O   . HOH   M 4 .   ? -12.802 -12.548 -9.721  1.00 45.99  ? 569 HOH   A O   1 
HETATM 7461 O  O   . HOH   M 4 .   ? -18.295 -19.634 -21.507 1.00 59.73  ? 570 HOH   A O   1 
HETATM 7462 O  O   . HOH   M 4 .   ? 11.962  -19.895 2.376   1.00 52.42  ? 571 HOH   A O   1 
HETATM 7463 O  O   . HOH   M 4 .   ? 15.640  -5.606  1.936   1.00 25.21  ? 572 HOH   A O   1 
HETATM 7464 O  O   . HOH   M 4 .   ? -16.135 -7.663  -20.727 1.00 49.11  ? 573 HOH   A O   1 
HETATM 7465 O  O   . HOH   M 4 .   ? -13.711 -8.806  -10.074 1.00 36.52  ? 574 HOH   A O   1 
HETATM 7466 O  O   . HOH   M 4 .   ? 17.401  -8.839  4.636   1.00 42.92  ? 575 HOH   A O   1 
HETATM 7467 O  O   . HOH   M 4 .   ? -1.251  -14.957 2.722   1.00 29.10  ? 576 HOH   A O   1 
HETATM 7468 O  O   . HOH   M 4 .   ? -6.319  -6.687  -2.259  1.00 30.36  ? 577 HOH   A O   1 
HETATM 7469 O  O   . HOH   M 4 .   ? 5.988   -7.338  -34.926 1.00 38.35  ? 578 HOH   A O   1 
HETATM 7470 O  O   . HOH   M 4 .   ? -3.092  -7.950  6.895   1.00 47.28  ? 579 HOH   A O   1 
HETATM 7471 O  O   . HOH   M 4 .   ? 20.626  -7.827  -3.410  1.00 40.09  ? 580 HOH   A O   1 
HETATM 7472 O  O   . HOH   M 4 .   ? 9.853   -7.420  4.837   1.00 31.28  ? 581 HOH   A O   1 
HETATM 7473 O  O   . HOH   M 4 .   ? 3.704   -10.819 -29.819 1.00 38.25  ? 582 HOH   A O   1 
HETATM 7474 O  O   . HOH   M 4 .   ? -8.701  -29.258 -15.378 1.00 45.88  ? 583 HOH   A O   1 
HETATM 7475 O  O   . HOH   M 4 .   ? 16.056  0.773   -9.613  1.00 34.16  ? 584 HOH   A O   1 
HETATM 7476 O  O   . HOH   M 4 .   ? 9.474   -9.562  8.167   1.00 28.85  ? 585 HOH   A O   1 
HETATM 7477 O  O   . HOH   M 4 .   ? 14.893  -14.874 -14.112 1.00 33.59  ? 586 HOH   A O   1 
HETATM 7478 O  O   . HOH   M 4 .   ? -7.723  -22.980 -10.970 1.00 39.96  ? 587 HOH   A O   1 
HETATM 7479 O  O   . HOH   M 4 .   ? -0.494  -20.639 -1.946  1.00 39.32  ? 588 HOH   A O   1 
HETATM 7480 O  O   . HOH   M 4 .   ? 11.214  20.549  -12.687 1.00 52.31  ? 589 HOH   A O   1 
HETATM 7481 O  O   . HOH   M 4 .   ? 18.827  29.172  -3.321  1.00 48.78  ? 590 HOH   A O   1 
HETATM 7482 O  O   . HOH   M 4 .   ? 0.390   -23.858 -27.645 1.00 52.43  ? 591 HOH   A O   1 
HETATM 7483 O  O   . HOH   M 4 .   ? 20.135  -9.155  -18.124 1.00 38.33  ? 592 HOH   A O   1 
HETATM 7484 O  O   . HOH   M 4 .   ? -6.243  -8.477  5.227   1.00 40.17  ? 593 HOH   A O   1 
HETATM 7485 O  O   . HOH   M 4 .   ? -5.542  -25.223 -10.693 1.00 43.33  ? 594 HOH   A O   1 
HETATM 7486 O  O   . HOH   M 4 .   ? -12.975 0.628   -29.431 1.00 55.24  ? 595 HOH   A O   1 
HETATM 7487 O  O   . HOH   M 4 .   ? -19.512 -8.210  -16.151 1.00 61.96  ? 596 HOH   A O   1 
HETATM 7488 O  O   . HOH   M 4 .   ? 9.310   5.296   -18.653 1.00 42.93  ? 597 HOH   A O   1 
HETATM 7489 O  O   . HOH   M 4 .   ? 17.729  10.630  -0.346  1.00 49.60  ? 598 HOH   A O   1 
HETATM 7490 O  O   . HOH   M 4 .   ? 0.012   0.115   4.369   1.00 32.80  ? 599 HOH   A O   1 
HETATM 7491 O  O   . HOH   M 4 .   ? 13.280  -23.238 -9.569  1.00 42.72  ? 600 HOH   A O   1 
HETATM 7492 O  O   . HOH   M 4 .   ? 12.227  -13.708 -23.255 1.00 30.40  ? 601 HOH   A O   1 
HETATM 7493 O  O   . HOH   M 4 .   ? 11.490  3.526   -15.831 1.00 28.73  ? 602 HOH   A O   1 
HETATM 7494 O  O   . HOH   M 4 .   ? 15.625  -22.043 -10.377 1.00 45.14  ? 603 HOH   A O   1 
HETATM 7495 O  O   . HOH   M 4 .   ? 19.058  0.734   -15.457 1.00 48.48  ? 604 HOH   A O   1 
HETATM 7496 O  O   . HOH   M 4 .   ? -6.629  -20.610 -5.368  1.00 69.19  ? 605 HOH   A O   1 
HETATM 7497 O  O   . HOH   M 4 .   ? 2.531   1.098   4.397   1.00 26.33  ? 606 HOH   A O   1 
HETATM 7498 O  O   . HOH   M 4 .   ? -4.979  2.269   0.325   1.00 41.80  ? 607 HOH   A O   1 
HETATM 7499 O  O   . HOH   M 4 .   ? -7.759  -14.237 2.548   1.00 40.78  ? 608 HOH   A O   1 
HETATM 7500 O  O   . HOH   M 4 .   ? 3.786   8.235   -3.278  1.00 35.63  ? 609 HOH   A O   1 
HETATM 7501 O  O   . HOH   M 4 .   ? -0.032  -27.565 -28.269 1.00 66.15  ? 610 HOH   A O   1 
HETATM 7502 O  O   . HOH   M 4 .   ? -17.962 -11.459 -15.612 1.00 50.83  ? 611 HOH   A O   1 
HETATM 7503 O  O   . HOH   M 4 .   ? -0.406  10.454  -2.901  1.00 48.00  ? 612 HOH   A O   1 
HETATM 7504 O  O   . HOH   M 4 .   ? 12.399  -18.146 -7.050  1.00 40.64  ? 613 HOH   A O   1 
HETATM 7505 O  O   . HOH   M 4 .   ? -7.592  13.515  -14.120 1.00 45.80  ? 614 HOH   A O   1 
HETATM 7506 O  O   . HOH   M 4 .   ? 11.202  -18.354 -4.212  1.00 43.29  ? 615 HOH   A O   1 
HETATM 7507 O  O   . HOH   M 4 .   ? -5.238  4.822   -1.086  1.00 45.67  ? 616 HOH   A O   1 
HETATM 7508 O  O   . HOH   M 4 .   ? 16.252  -16.194 1.644   1.00 48.14  ? 617 HOH   A O   1 
HETATM 7509 O  O   . HOH   M 4 .   ? 21.612  -8.213  -5.931  1.00 53.58  ? 618 HOH   A O   1 
HETATM 7510 O  O   . HOH   M 4 .   ? -2.486  -19.896 -27.754 1.00 38.81  ? 619 HOH   A O   1 
HETATM 7511 O  O   . HOH   M 4 .   ? 14.981  -14.406 -23.846 1.00 45.49  ? 620 HOH   A O   1 
HETATM 7512 O  O   . HOH   M 4 .   ? 5.195   -1.506  7.542   1.00 23.24  ? 621 HOH   A O   1 
HETATM 7513 O  O   . HOH   M 4 .   ? 12.706  -7.175  6.288   1.00 40.52  ? 622 HOH   A O   1 
HETATM 7514 O  O   . HOH   M 4 .   ? 3.025   0.071   6.989   1.00 31.95  ? 623 HOH   A O   1 
HETATM 7515 O  O   . HOH   M 4 .   ? 2.046   -25.840 -30.096 1.00 64.96  ? 624 HOH   A O   1 
HETATM 7516 O  O   . HOH   M 4 .   ? 1.187   -21.496 -26.450 1.00 44.68  ? 625 HOH   A O   1 
HETATM 7517 O  O   . HOH   M 4 .   ? -10.627 -1.919  -30.483 1.00 57.38  ? 626 HOH   A O   1 
HETATM 7518 O  O   . HOH   M 4 .   ? 0.446   -1.732  7.044   1.00 39.83  ? 627 HOH   A O   1 
HETATM 7519 O  O   . HOH   N 4 .   ? 22.938  -2.785  12.726  1.00 40.09  ? 501 HOH   B O   1 
HETATM 7520 O  O   . HOH   N 4 .   ? 20.965  -0.991  17.958  1.00 44.53  ? 502 HOH   B O   1 
HETATM 7521 O  O   . HOH   N 4 .   ? -7.609  12.078  9.551   1.00 37.83  ? 503 HOH   B O   1 
HETATM 7522 O  O   . HOH   N 4 .   ? 7.329   18.814  4.231   1.00 26.14  ? 504 HOH   B O   1 
HETATM 7523 O  O   . HOH   N 4 .   ? 3.703   10.609  -0.037  1.00 33.23  ? 505 HOH   B O   1 
HETATM 7524 O  O   . HOH   N 4 .   ? 6.586   22.370  5.187   1.00 29.15  ? 506 HOH   B O   1 
HETATM 7525 O  O   . HOH   N 4 .   ? 17.085  18.996  30.210  1.00 33.53  ? 507 HOH   B O   1 
HETATM 7526 O  O   . HOH   N 4 .   ? 4.514   26.913  5.267   1.00 29.78  ? 508 HOH   B O   1 
HETATM 7527 O  O   . HOH   N 4 .   ? -1.955  3.488   22.611  1.00 36.92  ? 509 HOH   B O   1 
HETATM 7528 O  O   . HOH   N 4 .   ? 11.856  3.318   26.809  1.00 27.43  ? 510 HOH   B O   1 
HETATM 7529 O  O   . HOH   N 4 .   ? -3.610  30.789  10.788  1.00 60.63  ? 511 HOH   B O   1 
HETATM 7530 O  O   . HOH   N 4 .   ? 1.009   41.816  3.769   1.00 54.31  ? 512 HOH   B O   1 
HETATM 7531 O  O   . HOH   N 4 .   ? 28.002  18.379  24.272  1.00 44.42  ? 513 HOH   B O   1 
HETATM 7532 O  O   . HOH   N 4 .   ? 14.178  1.974   26.309  1.00 34.18  ? 514 HOH   B O   1 
HETATM 7533 O  O   . HOH   N 4 .   ? 17.888  30.676  9.669   1.00 37.18  ? 515 HOH   B O   1 
HETATM 7534 O  O   . HOH   N 4 .   ? 23.104  26.623  19.814  1.00 42.83  ? 516 HOH   B O   1 
HETATM 7535 O  O   . HOH   N 4 .   ? 4.372   18.262  -0.648  1.00 47.23  ? 517 HOH   B O   1 
HETATM 7536 O  O   . HOH   N 4 .   ? 18.775  1.026   16.874  1.00 28.78  ? 518 HOH   B O   1 
HETATM 7537 O  O   . HOH   N 4 .   ? 16.849  15.963  33.697  1.00 51.95  ? 519 HOH   B O   1 
HETATM 7538 O  O   . HOH   N 4 .   ? 21.832  16.788  9.174   1.00 28.11  ? 520 HOH   B O   1 
HETATM 7539 O  O   . HOH   N 4 .   ? 24.618  23.390  5.341   1.00 48.84  ? 521 HOH   B O   1 
HETATM 7540 O  O   . HOH   N 4 .   ? 14.046  31.840  0.867   1.00 35.27  ? 522 HOH   B O   1 
HETATM 7541 O  O   . HOH   N 4 .   ? 18.433  4.426   2.137   1.00 34.32  ? 523 HOH   B O   1 
HETATM 7542 O  O   . HOH   N 4 .   ? 7.489   1.306   24.227  1.00 34.59  ? 524 HOH   B O   1 
HETATM 7543 O  O   . HOH   N 4 .   ? -3.222  15.690  4.122   1.00 46.29  ? 525 HOH   B O   1 
HETATM 7544 O  O   . HOH   N 4 .   ? 18.756  20.120  32.320  1.00 40.32  ? 526 HOH   B O   1 
HETATM 7545 O  O   . HOH   N 4 .   ? 28.693  10.206  22.449  1.00 51.25  ? 527 HOH   B O   1 
HETATM 7546 O  O   . HOH   N 4 .   ? 6.671   -2.172  11.799  1.00 21.56  ? 528 HOH   B O   1 
HETATM 7547 O  O   . HOH   N 4 .   ? -4.740  39.881  11.778  1.00 75.55  ? 529 HOH   B O   1 
HETATM 7548 O  O   . HOH   N 4 .   ? 4.400   2.218   38.780  1.00 39.60  ? 530 HOH   B O   1 
HETATM 7549 O  O   . HOH   N 4 .   ? 0.823   30.893  10.573  1.00 35.49  ? 531 HOH   B O   1 
HETATM 7550 O  O   . HOH   N 4 .   ? -2.840  18.923  13.497  1.00 29.48  ? 532 HOH   B O   1 
HETATM 7551 O  O   . HOH   N 4 .   ? 16.973  5.498   -1.659  1.00 47.15  ? 533 HOH   B O   1 
HETATM 7552 O  O   . HOH   N 4 .   ? 11.272  -0.715  10.150  1.00 23.58  ? 534 HOH   B O   1 
HETATM 7553 O  O   . HOH   N 4 .   ? -0.684  16.994  10.780  1.00 27.90  ? 535 HOH   B O   1 
HETATM 7554 O  O   . HOH   N 4 .   ? -0.531  19.665  10.136  1.00 35.21  ? 536 HOH   B O   1 
HETATM 7555 O  O   . HOH   N 4 .   ? 24.040  22.633  18.698  1.00 35.47  ? 537 HOH   B O   1 
HETATM 7556 O  O   . HOH   N 4 .   ? 7.192   37.751  24.090  1.00 67.13  ? 538 HOH   B O   1 
HETATM 7557 O  O   . HOH   N 4 .   ? 2.095   2.317   7.920   1.00 37.82  ? 539 HOH   B O   1 
HETATM 7558 O  O   . HOH   N 4 .   ? 0.108   11.325  8.685   1.00 23.31  ? 540 HOH   B O   1 
HETATM 7559 O  O   . HOH   N 4 .   ? 8.957   -1.361  42.325  1.00 38.09  ? 541 HOH   B O   1 
HETATM 7560 O  O   . HOH   N 4 .   ? 22.261  30.088  2.530   1.00 50.94  ? 542 HOH   B O   1 
HETATM 7561 O  O   . HOH   N 4 .   ? 13.650  -3.767  2.501   1.00 25.58  ? 543 HOH   B O   1 
HETATM 7562 O  O   . HOH   N 4 .   ? 26.264  16.744  14.290  1.00 44.48  ? 544 HOH   B O   1 
HETATM 7563 O  O   . HOH   N 4 .   ? 7.491   -1.524  9.110   1.00 24.76  ? 545 HOH   B O   1 
HETATM 7564 O  O   . HOH   N 4 .   ? -2.541  13.853  32.648  1.00 33.37  ? 546 HOH   B O   1 
HETATM 7565 O  O   . HOH   N 4 .   ? 11.239  -0.957  7.425   1.00 35.39  ? 547 HOH   B O   1 
HETATM 7566 O  O   . HOH   N 4 .   ? 20.273  15.488  2.230   1.00 41.60  ? 548 HOH   B O   1 
HETATM 7567 O  O   . HOH   N 4 .   ? 19.875  3.045   18.336  1.00 35.57  ? 549 HOH   B O   1 
HETATM 7568 O  O   . HOH   N 4 .   ? -1.689  5.233   26.057  1.00 33.73  ? 550 HOH   B O   1 
HETATM 7569 O  O   . HOH   N 4 .   ? -7.415  15.053  9.180   1.00 33.69  ? 551 HOH   B O   1 
HETATM 7570 O  O   . HOH   N 4 .   ? 13.452  20.332  -5.452  1.00 48.71  ? 552 HOH   B O   1 
HETATM 7571 O  O   . HOH   N 4 .   ? 17.418  16.401  31.116  1.00 42.91  ? 553 HOH   B O   1 
HETATM 7572 O  O   . HOH   N 4 .   ? 10.445  -5.917  36.768  1.00 40.95  ? 554 HOH   B O   1 
HETATM 7573 O  O   . HOH   N 4 .   ? 15.786  33.212  12.425  1.00 43.01  ? 555 HOH   B O   1 
HETATM 7574 O  O   . HOH   N 4 .   ? 5.346   6.042   2.556   1.00 24.86  ? 556 HOH   B O   1 
HETATM 7575 O  O   . HOH   N 4 .   ? -0.082  17.441  20.129  1.00 26.89  ? 557 HOH   B O   1 
HETATM 7576 O  O   . HOH   N 4 .   ? 3.573   25.706  1.568   1.00 39.94  ? 558 HOH   B O   1 
HETATM 7577 O  O   . HOH   N 4 .   ? 17.246  -2.089  10.787  1.00 27.89  ? 559 HOH   B O   1 
HETATM 7578 O  O   . HOH   N 4 .   ? -0.125  23.852  6.098   1.00 33.94  ? 560 HOH   B O   1 
HETATM 7579 O  O   . HOH   N 4 .   ? 18.027  10.092  2.614   1.00 35.87  ? 561 HOH   B O   1 
HETATM 7580 O  O   . HOH   N 4 .   ? 2.213   21.022  0.500   1.00 43.36  ? 562 HOH   B O   1 
HETATM 7581 O  O   . HOH   N 4 .   ? 19.884  4.113   22.015  1.00 33.49  ? 563 HOH   B O   1 
HETATM 7582 O  O   . HOH   N 4 .   ? -3.184  5.319   5.795   1.00 43.00  ? 564 HOH   B O   1 
HETATM 7583 O  O   . HOH   N 4 .   ? -10.179 11.722  10.411  1.00 50.62  ? 565 HOH   B O   1 
HETATM 7584 O  O   . HOH   N 4 .   ? -5.751  22.091  25.322  1.00 32.62  ? 566 HOH   B O   1 
HETATM 7585 O  O   . HOH   N 4 .   ? 8.263   -1.267  3.967   1.00 28.11  ? 567 HOH   B O   1 
HETATM 7586 O  O   . HOH   N 4 .   ? 23.782  15.355  10.439  1.00 37.62  ? 568 HOH   B O   1 
HETATM 7587 O  O   . HOH   N 4 .   ? 17.587  -4.054  3.027   1.00 34.70  ? 569 HOH   B O   1 
HETATM 7588 O  O   . HOH   N 4 .   ? 28.452  14.196  17.921  1.00 39.73  ? 570 HOH   B O   1 
HETATM 7589 O  O   . HOH   N 4 .   ? 14.910  9.777   28.727  1.00 31.40  ? 571 HOH   B O   1 
HETATM 7590 O  O   . HOH   N 4 .   ? 12.172  36.065  10.598  1.00 40.39  ? 572 HOH   B O   1 
HETATM 7591 O  O   . HOH   N 4 .   ? -1.163  10.479  10.962  1.00 23.12  ? 573 HOH   B O   1 
HETATM 7592 O  O   . HOH   N 4 .   ? 20.165  13.522  0.339   1.00 71.71  ? 574 HOH   B O   1 
HETATM 7593 O  O   . HOH   N 4 .   ? -4.055  11.925  3.377   1.00 43.68  ? 575 HOH   B O   1 
HETATM 7594 O  O   . HOH   N 4 .   ? -4.826  20.788  12.868  1.00 32.20  ? 576 HOH   B O   1 
HETATM 7595 O  O   . HOH   N 4 .   ? -8.514  22.524  25.506  1.00 42.85  ? 577 HOH   B O   1 
HETATM 7596 O  O   . HOH   N 4 .   ? 24.524  4.456   16.967  1.00 38.20  ? 578 HOH   B O   1 
HETATM 7597 O  O   . HOH   N 4 .   ? 3.660   8.033   1.433   1.00 24.59  ? 579 HOH   B O   1 
HETATM 7598 O  O   . HOH   N 4 .   ? 9.999   20.958  24.638  1.00 28.68  ? 580 HOH   B O   1 
HETATM 7599 O  O   . HOH   N 4 .   ? 25.181  18.796  7.314   1.00 55.82  ? 581 HOH   B O   1 
HETATM 7600 O  O   . HOH   N 4 .   ? 26.306  22.168  9.715   1.00 45.84  ? 582 HOH   B O   1 
HETATM 7601 O  O   . HOH   N 4 .   ? 10.453  -2.803  4.108   1.00 26.80  ? 583 HOH   B O   1 
HETATM 7602 O  O   . HOH   N 4 .   ? 19.045  -3.362  6.910   1.00 43.63  ? 584 HOH   B O   1 
HETATM 7603 O  O   . HOH   N 4 .   ? 30.085  16.425  25.488  1.00 53.47  ? 585 HOH   B O   1 
HETATM 7604 O  O   . HOH   N 4 .   ? 7.208   14.092  -0.952  1.00 31.80  ? 586 HOH   B O   1 
HETATM 7605 O  O   . HOH   N 4 .   ? 10.311  5.276   45.586  1.00 28.29  ? 587 HOH   B O   1 
HETATM 7606 O  O   . HOH   N 4 .   ? 24.622  28.654  27.569  1.00 58.05  ? 588 HOH   B O   1 
HETATM 7607 O  O   . HOH   N 4 .   ? 31.045  13.274  25.146  1.00 47.34  ? 589 HOH   B O   1 
HETATM 7608 O  O   . HOH   N 4 .   ? 4.844   1.007   24.654  1.00 41.78  ? 590 HOH   B O   1 
HETATM 7609 O  O   . HOH   N 4 .   ? 29.901  8.905   14.467  1.00 50.91  ? 591 HOH   B O   1 
HETATM 7610 O  O   . HOH   N 4 .   ? -8.003  11.820  25.329  1.00 33.92  ? 592 HOH   B O   1 
HETATM 7611 O  O   . HOH   N 4 .   ? -3.110  4.288   20.152  1.00 33.36  ? 593 HOH   B O   1 
HETATM 7612 O  O   . HOH   N 4 .   ? 11.661  7.932   35.607  1.00 37.78  ? 594 HOH   B O   1 
HETATM 7613 O  O   . HOH   N 4 .   ? 20.931  15.567  28.215  1.00 41.78  ? 595 HOH   B O   1 
HETATM 7614 O  O   . HOH   N 4 .   ? 5.758   25.593  -1.028  1.00 47.77  ? 596 HOH   B O   1 
HETATM 7615 O  O   . HOH   N 4 .   ? 20.636  27.834  -1.551  1.00 41.66  ? 597 HOH   B O   1 
HETATM 7616 O  O   . HOH   N 4 .   ? -15.930 6.049   19.257  1.00 46.80  ? 598 HOH   B O   1 
HETATM 7617 O  O   . HOH   N 4 .   ? 16.203  12.896  38.339  1.00 40.87  ? 599 HOH   B O   1 
HETATM 7618 O  O   . HOH   N 4 .   ? 19.927  26.038  30.044  1.00 75.79  ? 600 HOH   B O   1 
HETATM 7619 O  O   . HOH   N 4 .   ? 0.912   -0.248  13.589  1.00 31.00  ? 601 HOH   B O   1 
HETATM 7620 O  O   . HOH   N 4 .   ? 17.973  38.947  18.636  1.00 61.40  ? 602 HOH   B O   1 
HETATM 7621 O  O   . HOH   N 4 .   ? 24.484  23.065  16.067  1.00 39.36  ? 603 HOH   B O   1 
HETATM 7622 O  O   . HOH   N 4 .   ? -3.297  0.094   11.090  1.00 43.35  ? 604 HOH   B O   1 
HETATM 7623 O  O   . HOH   N 4 .   ? -1.002  2.506   5.193   1.00 38.52  ? 605 HOH   B O   1 
HETATM 7624 O  O   . HOH   N 4 .   ? -3.935  24.566  8.008   1.00 42.49  ? 606 HOH   B O   1 
HETATM 7625 O  O   . HOH   N 4 .   ? 17.182  9.797   27.182  1.00 29.58  ? 607 HOH   B O   1 
HETATM 7626 O  O   . HOH   N 4 .   ? -2.425  37.455  9.561   1.00 46.65  ? 608 HOH   B O   1 
HETATM 7627 O  O   . HOH   N 4 .   ? 10.285  41.681  15.040  1.00 64.39  ? 609 HOH   B O   1 
HETATM 7628 O  O   . HOH   N 4 .   ? -2.919  11.858  34.550  1.00 34.48  ? 610 HOH   B O   1 
HETATM 7629 O  O   . HOH   N 4 .   ? 28.870  12.841  14.859  1.00 50.47  ? 611 HOH   B O   1 
HETATM 7630 O  O   . HOH   N 4 .   ? 20.084  9.062   4.819   1.00 45.24  ? 612 HOH   B O   1 
HETATM 7631 O  O   . HOH   N 4 .   ? -2.204  10.653  1.870   1.00 33.40  ? 613 HOH   B O   1 
HETATM 7632 O  O   . HOH   N 4 .   ? 8.208   -1.942  45.004  1.00 43.09  ? 614 HOH   B O   1 
HETATM 7633 O  O   . HOH   N 4 .   ? -2.414  4.024   17.479  1.00 41.02  ? 615 HOH   B O   1 
HETATM 7634 O  O   . HOH   N 4 .   ? 11.462  4.011   34.478  1.00 50.46  ? 616 HOH   B O   1 
HETATM 7635 O  O   . HOH   N 4 .   ? 7.663   5.316   44.893  1.00 37.29  ? 617 HOH   B O   1 
HETATM 7636 O  O   . HOH   N 4 .   ? 25.198  22.011  25.397  1.00 41.49  ? 618 HOH   B O   1 
HETATM 7637 O  O   . HOH   N 4 .   ? 2.776   -1.713  14.748  1.00 25.00  ? 619 HOH   B O   1 
HETATM 7638 O  O   . HOH   N 4 .   ? 19.866  12.258  3.785   1.00 39.45  ? 620 HOH   B O   1 
HETATM 7639 O  O   . HOH   N 4 .   ? -6.111  29.167  13.511  1.00 52.64  ? 621 HOH   B O   1 
HETATM 7640 O  O   . HOH   N 4 .   ? 25.335  7.665   10.055  1.00 43.33  ? 622 HOH   B O   1 
HETATM 7641 O  O   . HOH   N 4 .   ? 20.337  2.529   2.024   1.00 46.60  ? 623 HOH   B O   1 
HETATM 7642 O  O   . HOH   N 4 .   ? 5.380   16.030  -2.792  1.00 52.49  ? 624 HOH   B O   1 
HETATM 7643 O  O   . HOH   N 4 .   ? -2.889  16.442  33.580  1.00 38.06  ? 625 HOH   B O   1 
HETATM 7644 O  O   . HOH   N 4 .   ? 12.698  6.809   -5.235  1.00 44.42  ? 626 HOH   B O   1 
HETATM 7645 O  O   . HOH   N 4 .   ? 13.878  -3.654  7.117   1.00 49.52  ? 627 HOH   B O   1 
HETATM 7646 O  O   . HOH   N 4 .   ? 28.621  15.470  15.531  1.00 57.23  ? 628 HOH   B O   1 
HETATM 7647 O  O   . HOH   N 4 .   ? 4.985   -4.225  11.150  1.00 23.34  ? 629 HOH   B O   1 
HETATM 7648 O  O   . HOH   N 4 .   ? 19.864  5.609   -0.901  1.00 58.98  ? 630 HOH   B O   1 
HETATM 7649 O  O   . HOH   N 4 .   ? 2.774   -3.533  12.577  1.00 30.94  ? 631 HOH   B O   1 
HETATM 7650 O  O   . HOH   N 4 .   ? 17.459  33.257  10.260  1.00 41.80  ? 632 HOH   B O   1 
HETATM 7651 O  O   . HOH   N 4 .   ? 10.959  -3.519  6.693   1.00 41.52  ? 633 HOH   B O   1 
HETATM 7652 O  O   . HOH   N 4 .   ? -5.215  9.976   5.378   1.00 42.78  ? 634 HOH   B O   1 
HETATM 7653 O  O   . HOH   N 4 .   ? 22.699  3.247   18.622  1.00 34.37  ? 635 HOH   B O   1 
HETATM 7654 O  O   . HOH   N 4 .   ? 0.633   0.346   10.811  1.00 44.91  ? 636 HOH   B O   1 
HETATM 7655 O  O   . HOH   N 4 .   ? 3.814   -3.564  8.675   1.00 23.35  ? 637 HOH   B O   1 
HETATM 7656 O  O   . HOH   O 4 .   ? -3.292  -30.614 -13.494 1.00 41.88  ? 501 HOH   C O   1 
HETATM 7657 O  O   . HOH   O 4 .   ? 2.450   -10.894 30.466  1.00 31.86  ? 502 HOH   C O   1 
HETATM 7658 O  O   . HOH   O 4 .   ? 6.342   -24.652 39.182  1.00 51.83  ? 503 HOH   C O   1 
HETATM 7659 O  O   . HOH   O 4 .   ? -3.037  -13.661 36.612  1.00 37.27  ? 504 HOH   C O   1 
HETATM 7660 O  O   . HOH   O 4 .   ? 5.423   -16.386 44.096  1.00 38.36  ? 505 HOH   C O   1 
HETATM 7661 O  O   . HOH   O 4 .   ? 15.233  -6.513  23.347  1.00 39.88  ? 506 HOH   C O   1 
HETATM 7662 O  O   . HOH   O 4 .   ? 15.969  -21.574 25.698  1.00 39.64  ? 507 HOH   C O   1 
HETATM 7663 O  O   . HOH   O 4 .   ? 3.432   -24.424 6.390   1.00 32.82  ? 508 HOH   C O   1 
HETATM 7664 O  O   . HOH   O 4 .   ? 1.112   -20.088 5.445   1.00 38.45  ? 509 HOH   C O   1 
HETATM 7665 O  O   . HOH   O 4 .   ? -0.188  -24.673 42.500  1.00 52.34  ? 510 HOH   C O   1 
HETATM 7666 O  O   . HOH   O 4 .   ? -6.338  -11.176 33.177  1.00 39.80  ? 511 HOH   C O   1 
HETATM 7667 O  O   . HOH   O 4 .   ? 11.961  -24.450 10.204  1.00 40.95  ? 512 HOH   C O   1 
HETATM 7668 O  O   . HOH   O 4 .   ? -2.947  -29.324 22.417  1.00 41.15  ? 513 HOH   C O   1 
HETATM 7669 O  O   . HOH   O 4 .   ? 10.511  -6.923  11.991  1.00 34.44  ? 514 HOH   C O   1 
HETATM 7670 O  O   . HOH   O 4 .   ? 14.464  -20.204 27.491  1.00 35.04  ? 515 HOH   C O   1 
HETATM 7671 O  O   . HOH   O 4 .   ? 8.860   -2.797  13.207  1.00 28.64  ? 516 HOH   C O   1 
HETATM 7672 O  O   . HOH   O 4 .   ? 1.504   -5.394  32.185  1.00 46.76  ? 517 HOH   C O   1 
HETATM 7673 O  O   . HOH   O 4 .   ? 3.715   -29.779 11.282  1.00 37.67  ? 518 HOH   C O   1 
HETATM 7674 O  O   . HOH   O 4 .   ? 18.526  -28.698 21.807  1.00 40.99  ? 519 HOH   C O   1 
HETATM 7675 O  O   . HOH   O 4 .   ? 10.453  -28.591 40.045  1.00 60.96  ? 520 HOH   C O   1 
HETATM 7676 O  O   . HOH   O 4 .   ? 5.907   -24.494 5.358   1.00 38.88  ? 521 HOH   C O   1 
HETATM 7677 O  O   . HOH   O 4 .   ? -6.624  -11.908 24.849  1.00 33.23  ? 522 HOH   C O   1 
HETATM 7678 O  O   . HOH   O 4 .   ? -2.481  -5.550  30.861  1.00 53.44  ? 523 HOH   C O   1 
HETATM 7679 O  O   . HOH   O 4 .   ? 6.554   -6.448  10.525  1.00 24.10  ? 524 HOH   C O   1 
HETATM 7680 O  O   . HOH   O 4 .   ? -9.289  -17.886 37.039  1.00 44.03  ? 525 HOH   C O   1 
HETATM 7681 O  O   . HOH   O 4 .   ? 16.913  -25.831 25.101  1.00 47.42  ? 526 HOH   C O   1 
HETATM 7682 O  O   . HOH   O 4 .   ? -14.480 -27.192 10.772  1.00 51.14  ? 527 HOH   C O   1 
HETATM 7683 O  O   . HOH   O 4 .   ? -3.515  -8.231  21.115  1.00 27.35  ? 528 HOH   C O   1 
HETATM 7684 O  O   . HOH   O 4 .   ? 14.503  -35.637 21.946  1.00 43.60  ? 529 HOH   C O   1 
HETATM 7685 O  O   . HOH   O 4 .   ? -9.292  -19.891 20.822  1.00 33.86  ? 530 HOH   C O   1 
HETATM 7686 O  O   . HOH   O 4 .   ? 0.289   -12.750 32.970  1.00 36.80  ? 531 HOH   C O   1 
HETATM 7687 O  O   . HOH   O 4 .   ? 15.014  -11.727 9.996   1.00 29.43  ? 532 HOH   C O   1 
HETATM 7688 O  O   . HOH   O 4 .   ? 14.075  -30.284 11.513  1.00 57.67  ? 533 HOH   C O   1 
HETATM 7689 O  O   . HOH   O 4 .   ? 19.685  -15.009 9.029   1.00 48.61  ? 534 HOH   C O   1 
HETATM 7690 O  O   . HOH   O 4 .   ? 13.599  -18.481 9.916   1.00 30.80  ? 535 HOH   C O   1 
HETATM 7691 O  O   . HOH   O 4 .   ? -5.228  -9.274  19.141  1.00 29.66  ? 536 HOH   C O   1 
HETATM 7692 O  O   . HOH   O 4 .   ? 18.509  -22.306 13.398  1.00 48.45  ? 537 HOH   C O   1 
HETATM 7693 O  O   . HOH   O 4 .   ? 1.066   -9.088  38.512  1.00 44.94  ? 538 HOH   C O   1 
HETATM 7694 O  O   . HOH   O 4 .   ? -2.692  -33.822 -28.873 1.00 64.54  ? 539 HOH   C O   1 
HETATM 7695 O  O   . HOH   O 4 .   ? -9.473  -18.727 7.127   1.00 40.25  ? 540 HOH   C O   1 
HETATM 7696 O  O   . HOH   O 4 .   ? -17.363 -23.801 21.571  1.00 51.66  ? 541 HOH   C O   1 
HETATM 7697 O  O   . HOH   O 4 .   ? -12.156 -13.428 26.725  1.00 38.34  ? 542 HOH   C O   1 
HETATM 7698 O  O   . HOH   O 4 .   ? 17.176  -7.656  19.872  1.00 36.44  ? 543 HOH   C O   1 
HETATM 7699 O  O   . HOH   O 4 .   ? 4.160   -33.429 -18.890 1.00 38.65  ? 544 HOH   C O   1 
HETATM 7700 O  O   . HOH   O 4 .   ? 4.734   -3.326  19.980  1.00 27.19  ? 545 HOH   C O   1 
HETATM 7701 O  O   . HOH   O 4 .   ? 16.909  -24.689 32.542  1.00 52.53  ? 546 HOH   C O   1 
HETATM 7702 O  O   . HOH   O 4 .   ? 11.850  -31.022 28.155  1.00 40.32  ? 547 HOH   C O   1 
HETATM 7703 O  O   . HOH   O 4 .   ? 5.172   -7.933  8.529   1.00 20.80  ? 548 HOH   C O   1 
HETATM 7704 O  O   . HOH   O 4 .   ? 16.174  -11.919 7.477   1.00 31.97  ? 549 HOH   C O   1 
HETATM 7705 O  O   . HOH   O 4 .   ? -0.323  -24.280 0.304   1.00 44.72  ? 550 HOH   C O   1 
HETATM 7706 O  O   . HOH   O 4 .   ? 9.522   -9.239  10.924  1.00 25.71  ? 551 HOH   C O   1 
HETATM 7707 O  O   . HOH   O 4 .   ? 0.924   -5.191  13.520  1.00 41.02  ? 552 HOH   C O   1 
HETATM 7708 O  O   . HOH   O 4 .   ? 16.974  -4.508  22.562  1.00 43.20  ? 553 HOH   C O   1 
HETATM 7709 O  O   . HOH   O 4 .   ? 15.596  -19.434 7.808   1.00 45.68  ? 554 HOH   C O   1 
HETATM 7710 O  O   . HOH   O 4 .   ? 14.720  -2.561  12.134  1.00 26.91  ? 555 HOH   C O   1 
HETATM 7711 O  O   . HOH   O 4 .   ? 18.565  -35.046 16.902  1.00 37.16  ? 556 HOH   C O   1 
HETATM 7712 O  O   . HOH   O 4 .   ? -4.503  -2.123  16.883  1.00 46.85  ? 557 HOH   C O   1 
HETATM 7713 O  O   . HOH   O 4 .   ? 5.362   -4.789  28.801  1.00 34.85  ? 558 HOH   C O   1 
HETATM 7714 O  O   . HOH   O 4 .   ? -0.264  -35.675 -25.166 1.00 54.12  ? 559 HOH   C O   1 
HETATM 7715 O  O   . HOH   O 4 .   ? -1.224  -1.473  15.108  1.00 37.11  ? 560 HOH   C O   1 
HETATM 7716 O  O   . HOH   O 4 .   ? 14.979  -10.405 24.615  1.00 43.06  ? 561 HOH   C O   1 
HETATM 7717 O  O   . HOH   O 4 .   ? -11.646 -6.821  23.649  1.00 42.76  ? 562 HOH   C O   1 
HETATM 7718 O  O   . HOH   O 4 .   ? 18.124  -8.616  10.728  1.00 44.95  ? 563 HOH   C O   1 
HETATM 7719 O  O   . HOH   O 4 .   ? 18.225  -4.522  11.844  1.00 33.59  ? 564 HOH   C O   1 
HETATM 7720 O  O   . HOH   O 4 .   ? -7.906  -39.256 23.276  1.00 66.17  ? 565 HOH   C O   1 
HETATM 7721 O  O   . HOH   O 4 .   ? 12.494  -29.285 30.120  1.00 41.93  ? 566 HOH   C O   1 
HETATM 7722 O  O   . HOH   O 4 .   ? 5.043   -20.260 2.614   1.00 39.08  ? 567 HOH   C O   1 
HETATM 7723 O  O   . HOH   O 4 .   ? -1.671  -9.847  37.312  1.00 45.29  ? 568 HOH   C O   1 
HETATM 7724 O  O   . HOH   O 4 .   ? 3.192   -2.738  22.183  1.00 26.53  ? 569 HOH   C O   1 
HETATM 7725 O  O   . HOH   O 4 .   ? 6.235   -29.766 12.310  1.00 33.14  ? 570 HOH   C O   1 
HETATM 7726 O  O   . HOH   O 4 .   ? -8.402  -13.132 9.001   1.00 40.16  ? 571 HOH   C O   1 
HETATM 7727 O  O   . HOH   O 4 .   ? -1.251  -7.861  8.896   1.00 37.63  ? 572 HOH   C O   1 
HETATM 7728 O  O   . HOH   O 4 .   ? -3.006  -1.470  23.726  1.00 37.50  ? 573 HOH   C O   1 
HETATM 7729 O  O   . HOH   O 4 .   ? -7.309  -12.442 27.504  1.00 36.40  ? 574 HOH   C O   1 
HETATM 7730 O  O   . HOH   O 4 .   ? 11.318  -2.982  11.887  1.00 29.87  ? 575 HOH   C O   1 
HETATM 7731 O  O   . HOH   O 4 .   ? 5.733   -32.714 -16.666 1.00 39.64  ? 576 HOH   C O   1 
HETATM 7732 O  O   . HOH   O 4 .   ? 0.513   -8.957  7.234   1.00 28.47  ? 577 HOH   C O   1 
HETATM 7733 O  O   . HOH   O 4 .   ? 19.580  -7.687  18.643  1.00 56.68  ? 578 HOH   C O   1 
HETATM 7734 O  O   . HOH   O 4 .   ? 0.424   -30.762 3.460   1.00 53.38  ? 579 HOH   C O   1 
HETATM 7735 O  O   . HOH   O 4 .   ? -6.981  -10.888 10.158  1.00 54.41  ? 580 HOH   C O   1 
HETATM 7736 O  O   . HOH   O 4 .   ? 2.864   -32.431 12.622  1.00 63.25  ? 581 HOH   C O   1 
HETATM 7737 O  O   . HOH   O 4 .   ? -1.344  -19.131 4.845   1.00 55.25  ? 582 HOH   C O   1 
HETATM 7738 O  O   . HOH   O 4 .   ? 18.503  -30.890 15.390  1.00 62.96  ? 583 HOH   C O   1 
HETATM 7739 O  O   . HOH   O 4 .   ? -10.506 -11.342 32.146  1.00 50.96  ? 584 HOH   C O   1 
HETATM 7740 O  O   . HOH   O 4 .   ? 15.824  -13.082 26.250  1.00 45.34  ? 585 HOH   C O   1 
HETATM 7741 O  O   . HOH   O 4 .   ? 14.115  -0.449  24.952  1.00 39.53  ? 586 HOH   C O   1 
HETATM 7742 O  O   . HOH   O 4 .   ? 16.828  -12.767 23.158  1.00 54.53  ? 587 HOH   C O   1 
HETATM 7743 O  O   . HOH   O 4 .   ? -11.080 -9.239  34.271  1.00 59.89  ? 588 HOH   C O   1 
HETATM 7744 O  O   . HOH   O 4 .   ? 21.631  -31.619 15.937  1.00 51.22  ? 589 HOH   C O   1 
HETATM 7745 O  O   . HOH   O 4 .   ? 19.863  -8.092  12.766  1.00 48.05  ? 590 HOH   C O   1 
HETATM 7746 O  O   . HOH   O 4 .   ? 4.224   -5.865  7.051   1.00 22.29  ? 591 HOH   C O   1 
HETATM 7747 O  O   . HOH   O 4 .   ? 1.640   -6.493  6.718   1.00 29.38  ? 592 HOH   C O   1 
HETATM 7748 O  O   . HOH   O 4 .   ? 4.833   -26.044 40.901  1.00 47.67  ? 593 HOH   C O   1 
HETATM 7749 O  O   . HOH   O 4 .   ? 17.963  -25.197 13.845  1.00 51.95  ? 594 HOH   C O   1 
HETATM 7750 O  O   . HOH   O 4 .   ? 10.131  -4.825  10.341  1.00 52.31  ? 595 HOH   C O   1 
HETATM 7751 O  O   . HOH   O 4 .   ? -7.284  -8.691  8.585   1.00 47.54  ? 596 HOH   C O   1 
# 
