data_7I1E
# 
_entry.id   7I1E 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_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   7I1E         pdb_00007i1e 10.2210/pdb7i1e/pdb 
WWPDB D_1001408193 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-05-21 
_pdbx_audit_revision_history.part_number         ? 
# 
_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_database_status.entry_id                        7I1E 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2025-02-03 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 3 
_pdbx_contact_author.name_last          Weiss 
_pdbx_contact_author.name_first         Manfred 
_pdbx_contact_author.name_mi            S. 
_pdbx_contact_author.email              manfred.weiss@helmholtz-berlin.de 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-2362-7047 
# 
loop_
_audit_author.pdbx_ordinal 
_audit_author.name 
1 'Barthel, T.'     
2 'Benz, L.S.'      
3 'Wollenhaupt, J.' 
4 'Weiss, M.S.'     
# 
_citation.id                        primary 
_citation.title                     
'Orthorhombic SARS-CoV-2 main protease crystals provide higher success rate in fragment screening' 
_citation.journal_abbrev            'To be published' 
_citation.journal_volume            ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.year                      ? 
_citation.journal_id_ASTM           ? 
_citation.country                   ? 
_citation.journal_id_ISSN           ? 
_citation.journal_id_CSD            0353 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_DOI      ? 
# 
loop_
_citation_author.ordinal 
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
1  primary 'Barthel, T.'     ? 
2  primary 'Wollenhaupt, J.' ? 
3  primary 'Benz, L.S.'      ? 
4  primary 'Reincke, P.'     ? 
5  primary 'Zhang, L.'       ? 
6  primary 'Lennartz, F.'    ? 
7  primary 'Tabermann, H.'   ? 
8  primary 'Mueller, U.'     ? 
9  primary 'Meente, A.'      ? 
10 primary 'Hilgenfeld, R.'  ? 
11 primary 'Weiss, M.S.'     ? 
# 
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 '3C-like proteinase nsp5'         33825.547 2   3.4.22.69 ? ? ? 
2 non-polymer syn 'CHLORIDE ION'                    35.453    2   ?         ? ? ? 
3 non-polymer syn 3-ethoxybenzene-1-carboximidamide 164.204   1   ?         ? ? ? 
4 non-polymer syn 'SODIUM ION'                      22.990    1   ?         ? ? ? 
5 water       nat water                             18.015    100 ?         ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        '3CL-PRO,3CLp,Main protease,Mpro,Non-structural protein 5,nsp5,SARS coronavirus main proteinase' 
# 
_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       
;SGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGH
SMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFC
YMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYE
PLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCSGVTFQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGH
SMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFC
YMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYE
PLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCSGVTFQ
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'CHLORIDE ION'                    CL  
3 3-ethoxybenzene-1-carboximidamide RD4 
4 'SODIUM ION'                      NA  
5 water                             HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   GLY n 
1 3   PHE n 
1 4   ARG n 
1 5   LYS n 
1 6   MET n 
1 7   ALA n 
1 8   PHE n 
1 9   PRO n 
1 10  SER n 
1 11  GLY n 
1 12  LYS n 
1 13  VAL n 
1 14  GLU n 
1 15  GLY n 
1 16  CYS n 
1 17  MET n 
1 18  VAL n 
1 19  GLN n 
1 20  VAL n 
1 21  THR n 
1 22  CYS n 
1 23  GLY n 
1 24  THR n 
1 25  THR n 
1 26  THR n 
1 27  LEU n 
1 28  ASN n 
1 29  GLY n 
1 30  LEU n 
1 31  TRP n 
1 32  LEU n 
1 33  ASP n 
1 34  ASP n 
1 35  VAL n 
1 36  VAL n 
1 37  TYR n 
1 38  CYS n 
1 39  PRO n 
1 40  ARG n 
1 41  HIS n 
1 42  VAL n 
1 43  ILE n 
1 44  CYS n 
1 45  THR n 
1 46  SER n 
1 47  GLU n 
1 48  ASP n 
1 49  MET n 
1 50  LEU n 
1 51  ASN n 
1 52  PRO n 
1 53  ASN n 
1 54  TYR n 
1 55  GLU n 
1 56  ASP n 
1 57  LEU n 
1 58  LEU n 
1 59  ILE n 
1 60  ARG n 
1 61  LYS n 
1 62  SER n 
1 63  ASN n 
1 64  HIS n 
1 65  ASN n 
1 66  PHE n 
1 67  LEU n 
1 68  VAL n 
1 69  GLN n 
1 70  ALA n 
1 71  GLY n 
1 72  ASN n 
1 73  VAL n 
1 74  GLN n 
1 75  LEU n 
1 76  ARG n 
1 77  VAL n 
1 78  ILE n 
1 79  GLY n 
1 80  HIS n 
1 81  SER n 
1 82  MET n 
1 83  GLN n 
1 84  ASN n 
1 85  CYS n 
1 86  VAL n 
1 87  LEU n 
1 88  LYS n 
1 89  LEU n 
1 90  LYS n 
1 91  VAL n 
1 92  ASP n 
1 93  THR n 
1 94  ALA n 
1 95  ASN n 
1 96  PRO n 
1 97  LYS n 
1 98  THR n 
1 99  PRO n 
1 100 LYS n 
1 101 TYR n 
1 102 LYS n 
1 103 PHE n 
1 104 VAL n 
1 105 ARG n 
1 106 ILE n 
1 107 GLN n 
1 108 PRO n 
1 109 GLY n 
1 110 GLN n 
1 111 THR n 
1 112 PHE n 
1 113 SER n 
1 114 VAL n 
1 115 LEU n 
1 116 ALA n 
1 117 CYS n 
1 118 TYR n 
1 119 ASN n 
1 120 GLY n 
1 121 SER n 
1 122 PRO n 
1 123 SER n 
1 124 GLY n 
1 125 VAL n 
1 126 TYR n 
1 127 GLN n 
1 128 CYS n 
1 129 ALA n 
1 130 MET n 
1 131 ARG n 
1 132 PRO n 
1 133 ASN n 
1 134 PHE n 
1 135 THR n 
1 136 ILE n 
1 137 LYS n 
1 138 GLY n 
1 139 SER n 
1 140 PHE n 
1 141 LEU n 
1 142 ASN n 
1 143 GLY n 
1 144 SER n 
1 145 CYS n 
1 146 GLY n 
1 147 SER n 
1 148 VAL n 
1 149 GLY n 
1 150 PHE n 
1 151 ASN n 
1 152 ILE n 
1 153 ASP n 
1 154 TYR n 
1 155 ASP n 
1 156 CYS n 
1 157 VAL n 
1 158 SER n 
1 159 PHE n 
1 160 CYS n 
1 161 TYR n 
1 162 MET n 
1 163 HIS n 
1 164 HIS n 
1 165 MET n 
1 166 GLU n 
1 167 LEU n 
1 168 PRO n 
1 169 THR n 
1 170 GLY n 
1 171 VAL n 
1 172 HIS n 
1 173 ALA n 
1 174 GLY n 
1 175 THR n 
1 176 ASP n 
1 177 LEU n 
1 178 GLU n 
1 179 GLY n 
1 180 ASN n 
1 181 PHE n 
1 182 TYR n 
1 183 GLY n 
1 184 PRO n 
1 185 PHE n 
1 186 VAL n 
1 187 ASP n 
1 188 ARG n 
1 189 GLN n 
1 190 THR n 
1 191 ALA n 
1 192 GLN n 
1 193 ALA n 
1 194 ALA n 
1 195 GLY n 
1 196 THR n 
1 197 ASP n 
1 198 THR n 
1 199 THR n 
1 200 ILE n 
1 201 THR n 
1 202 VAL n 
1 203 ASN n 
1 204 VAL n 
1 205 LEU n 
1 206 ALA n 
1 207 TRP n 
1 208 LEU n 
1 209 TYR n 
1 210 ALA n 
1 211 ALA n 
1 212 VAL n 
1 213 ILE n 
1 214 ASN n 
1 215 GLY n 
1 216 ASP n 
1 217 ARG n 
1 218 TRP n 
1 219 PHE n 
1 220 LEU n 
1 221 ASN n 
1 222 ARG n 
1 223 PHE n 
1 224 THR n 
1 225 THR n 
1 226 THR n 
1 227 LEU n 
1 228 ASN n 
1 229 ASP n 
1 230 PHE n 
1 231 ASN n 
1 232 LEU n 
1 233 VAL n 
1 234 ALA n 
1 235 MET n 
1 236 LYS n 
1 237 TYR n 
1 238 ASN n 
1 239 TYR n 
1 240 GLU n 
1 241 PRO n 
1 242 LEU n 
1 243 THR n 
1 244 GLN n 
1 245 ASP n 
1 246 HIS n 
1 247 VAL n 
1 248 ASP n 
1 249 ILE n 
1 250 LEU n 
1 251 GLY n 
1 252 PRO n 
1 253 LEU n 
1 254 SER n 
1 255 ALA n 
1 256 GLN n 
1 257 THR n 
1 258 GLY n 
1 259 ILE n 
1 260 ALA n 
1 261 VAL n 
1 262 LEU n 
1 263 ASP n 
1 264 MET n 
1 265 CYS n 
1 266 ALA n 
1 267 SER n 
1 268 LEU n 
1 269 LYS n 
1 270 GLU n 
1 271 LEU n 
1 272 LEU n 
1 273 GLN n 
1 274 ASN n 
1 275 GLY n 
1 276 MET n 
1 277 ASN n 
1 278 GLY n 
1 279 ARG n 
1 280 THR n 
1 281 ILE n 
1 282 LEU n 
1 283 GLY n 
1 284 SER n 
1 285 ALA n 
1 286 LEU n 
1 287 LEU n 
1 288 GLU n 
1 289 ASP n 
1 290 GLU n 
1 291 PHE n 
1 292 THR n 
1 293 PRO n 
1 294 PHE n 
1 295 ASP n 
1 296 VAL n 
1 297 VAL n 
1 298 ARG n 
1 299 GLN n 
1 300 CYS n 
1 301 SER n 
1 302 GLY n 
1 303 VAL n 
1 304 THR n 
1 305 PHE n 
1 306 GLN 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                   306 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'rep, 1a-1b' 
_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      'Severe acute respiratory syndrome coronavirus 2' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     2697049 
_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 BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                           ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE                          ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE                        ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                   ? 'C4 H7 N O4'     133.103 
CL  non-polymer         . 'CHLORIDE ION'                    ? 'Cl -1'          35.453  
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 
NA  non-polymer         . 'SODIUM ION'                      ? 'Na 1'           22.990  
PHE 'L-peptide linking' y PHENYLALANINE                     ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE                           ? 'C5 H9 N O2'     115.130 
RD4 non-polymer         . 3-ethoxybenzene-1-carboximidamide ? 'C9 H12 N2 O'    164.204 
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   SER 1   1   1   SER SER A . n 
A 1 2   GLY 2   2   2   GLY GLY A . n 
A 1 3   PHE 3   3   3   PHE PHE A . n 
A 1 4   ARG 4   4   4   ARG ARG A . n 
A 1 5   LYS 5   5   5   LYS LYS A . n 
A 1 6   MET 6   6   6   MET MET A . n 
A 1 7   ALA 7   7   7   ALA ALA A . n 
A 1 8   PHE 8   8   8   PHE PHE A . n 
A 1 9   PRO 9   9   9   PRO PRO A . n 
A 1 10  SER 10  10  10  SER SER A . n 
A 1 11  GLY 11  11  11  GLY GLY A . n 
A 1 12  LYS 12  12  12  LYS LYS A . n 
A 1 13  VAL 13  13  13  VAL VAL A . n 
A 1 14  GLU 14  14  14  GLU GLU A . n 
A 1 15  GLY 15  15  15  GLY GLY A . n 
A 1 16  CYS 16  16  16  CYS CYS A . n 
A 1 17  MET 17  17  17  MET MET A . n 
A 1 18  VAL 18  18  18  VAL VAL A . n 
A 1 19  GLN 19  19  19  GLN GLN A . n 
A 1 20  VAL 20  20  20  VAL VAL A . n 
A 1 21  THR 21  21  21  THR THR A . n 
A 1 22  CYS 22  22  22  CYS CYS A . n 
A 1 23  GLY 23  23  23  GLY GLY A . n 
A 1 24  THR 24  24  24  THR THR A . n 
A 1 25  THR 25  25  25  THR THR A . n 
A 1 26  THR 26  26  26  THR THR A . n 
A 1 27  LEU 27  27  27  LEU LEU A . n 
A 1 28  ASN 28  28  28  ASN ASN A . n 
A 1 29  GLY 29  29  29  GLY GLY A . n 
A 1 30  LEU 30  30  30  LEU LEU A . n 
A 1 31  TRP 31  31  31  TRP TRP A . n 
A 1 32  LEU 32  32  32  LEU LEU A . n 
A 1 33  ASP 33  33  33  ASP ASP A . n 
A 1 34  ASP 34  34  34  ASP ASP A . n 
A 1 35  VAL 35  35  35  VAL VAL A . n 
A 1 36  VAL 36  36  36  VAL VAL A . n 
A 1 37  TYR 37  37  37  TYR TYR A . n 
A 1 38  CYS 38  38  38  CYS CYS A . n 
A 1 39  PRO 39  39  39  PRO PRO A . n 
A 1 40  ARG 40  40  40  ARG ARG A . n 
A 1 41  HIS 41  41  41  HIS HIS A . n 
A 1 42  VAL 42  42  42  VAL VAL A . n 
A 1 43  ILE 43  43  43  ILE ILE A . n 
A 1 44  CYS 44  44  44  CYS CYS A . n 
A 1 45  THR 45  45  45  THR THR A . n 
A 1 46  SER 46  46  46  SER SER A . n 
A 1 47  GLU 47  47  47  GLU GLU A . n 
A 1 48  ASP 48  48  48  ASP ASP A . n 
A 1 49  MET 49  49  49  MET MET A . n 
A 1 50  LEU 50  50  50  LEU LEU A . n 
A 1 51  ASN 51  51  51  ASN ASN A . n 
A 1 52  PRO 52  52  52  PRO PRO A . n 
A 1 53  ASN 53  53  53  ASN ASN A . n 
A 1 54  TYR 54  54  54  TYR TYR A . n 
A 1 55  GLU 55  55  55  GLU GLU A . n 
A 1 56  ASP 56  56  56  ASP ASP A . n 
A 1 57  LEU 57  57  57  LEU LEU A . n 
A 1 58  LEU 58  58  58  LEU LEU A . n 
A 1 59  ILE 59  59  59  ILE ILE A . n 
A 1 60  ARG 60  60  60  ARG ARG A . n 
A 1 61  LYS 61  61  61  LYS LYS A . n 
A 1 62  SER 62  62  62  SER SER A . n 
A 1 63  ASN 63  63  63  ASN ASN A . n 
A 1 64  HIS 64  64  64  HIS HIS A . n 
A 1 65  ASN 65  65  65  ASN ASN A . n 
A 1 66  PHE 66  66  66  PHE PHE A . n 
A 1 67  LEU 67  67  67  LEU LEU A . n 
A 1 68  VAL 68  68  68  VAL VAL A . n 
A 1 69  GLN 69  69  69  GLN GLN A . n 
A 1 70  ALA 70  70  70  ALA ALA A . n 
A 1 71  GLY 71  71  71  GLY GLY A . n 
A 1 72  ASN 72  72  72  ASN ASN A . n 
A 1 73  VAL 73  73  73  VAL VAL A . n 
A 1 74  GLN 74  74  74  GLN GLN A . n 
A 1 75  LEU 75  75  75  LEU LEU A . n 
A 1 76  ARG 76  76  76  ARG ARG A . n 
A 1 77  VAL 77  77  77  VAL VAL A . n 
A 1 78  ILE 78  78  78  ILE ILE A . n 
A 1 79  GLY 79  79  79  GLY GLY A . n 
A 1 80  HIS 80  80  80  HIS HIS A . n 
A 1 81  SER 81  81  81  SER SER A . n 
A 1 82  MET 82  82  82  MET MET A . n 
A 1 83  GLN 83  83  83  GLN GLN A . n 
A 1 84  ASN 84  84  84  ASN ASN A . n 
A 1 85  CYS 85  85  85  CYS CYS A . n 
A 1 86  VAL 86  86  86  VAL VAL A . n 
A 1 87  LEU 87  87  87  LEU LEU A . n 
A 1 88  LYS 88  88  88  LYS LYS A . n 
A 1 89  LEU 89  89  89  LEU LEU A . n 
A 1 90  LYS 90  90  90  LYS LYS A . n 
A 1 91  VAL 91  91  91  VAL VAL A . n 
A 1 92  ASP 92  92  92  ASP ASP A . n 
A 1 93  THR 93  93  93  THR THR A . n 
A 1 94  ALA 94  94  94  ALA ALA A . n 
A 1 95  ASN 95  95  95  ASN ASN A . n 
A 1 96  PRO 96  96  96  PRO PRO A . n 
A 1 97  LYS 97  97  97  LYS LYS A . n 
A 1 98  THR 98  98  98  THR THR A . n 
A 1 99  PRO 99  99  99  PRO PRO A . n 
A 1 100 LYS 100 100 100 LYS LYS A . n 
A 1 101 TYR 101 101 101 TYR TYR A . n 
A 1 102 LYS 102 102 102 LYS LYS A . n 
A 1 103 PHE 103 103 103 PHE PHE A . n 
A 1 104 VAL 104 104 104 VAL VAL A . n 
A 1 105 ARG 105 105 105 ARG ARG A . n 
A 1 106 ILE 106 106 106 ILE ILE A . n 
A 1 107 GLN 107 107 107 GLN GLN A . n 
A 1 108 PRO 108 108 108 PRO PRO A . n 
A 1 109 GLY 109 109 109 GLY GLY A . n 
A 1 110 GLN 110 110 110 GLN GLN A . n 
A 1 111 THR 111 111 111 THR THR A . n 
A 1 112 PHE 112 112 112 PHE PHE A . n 
A 1 113 SER 113 113 113 SER SER A . n 
A 1 114 VAL 114 114 114 VAL VAL A . n 
A 1 115 LEU 115 115 115 LEU LEU A . n 
A 1 116 ALA 116 116 116 ALA ALA A . n 
A 1 117 CYS 117 117 117 CYS CYS A . n 
A 1 118 TYR 118 118 118 TYR TYR A . n 
A 1 119 ASN 119 119 119 ASN ASN A . n 
A 1 120 GLY 120 120 120 GLY GLY A . n 
A 1 121 SER 121 121 121 SER SER A . n 
A 1 122 PRO 122 122 122 PRO PRO A . n 
A 1 123 SER 123 123 123 SER SER A . n 
A 1 124 GLY 124 124 124 GLY GLY A . n 
A 1 125 VAL 125 125 125 VAL VAL A . n 
A 1 126 TYR 126 126 126 TYR TYR A . n 
A 1 127 GLN 127 127 127 GLN GLN A . n 
A 1 128 CYS 128 128 128 CYS CYS A . n 
A 1 129 ALA 129 129 129 ALA ALA A . n 
A 1 130 MET 130 130 130 MET MET A . n 
A 1 131 ARG 131 131 131 ARG ARG A . n 
A 1 132 PRO 132 132 132 PRO PRO A . n 
A 1 133 ASN 133 133 133 ASN ASN A . n 
A 1 134 PHE 134 134 134 PHE PHE A . n 
A 1 135 THR 135 135 135 THR THR A . n 
A 1 136 ILE 136 136 136 ILE ILE A . n 
A 1 137 LYS 137 137 137 LYS LYS A . n 
A 1 138 GLY 138 138 138 GLY GLY A . n 
A 1 139 SER 139 139 139 SER SER A . n 
A 1 140 PHE 140 140 140 PHE PHE A . n 
A 1 141 LEU 141 141 141 LEU LEU A . n 
A 1 142 ASN 142 142 142 ASN ASN A . n 
A 1 143 GLY 143 143 143 GLY GLY A . n 
A 1 144 SER 144 144 144 SER SER A . n 
A 1 145 CYS 145 145 145 CYS CYS A . n 
A 1 146 GLY 146 146 146 GLY GLY A . n 
A 1 147 SER 147 147 147 SER SER A . n 
A 1 148 VAL 148 148 148 VAL VAL A . n 
A 1 149 GLY 149 149 149 GLY GLY A . n 
A 1 150 PHE 150 150 150 PHE PHE A . n 
A 1 151 ASN 151 151 151 ASN ASN A . n 
A 1 152 ILE 152 152 152 ILE ILE A . n 
A 1 153 ASP 153 153 153 ASP ASP A . n 
A 1 154 TYR 154 154 154 TYR TYR A . n 
A 1 155 ASP 155 155 155 ASP ASP A . n 
A 1 156 CYS 156 156 156 CYS CYS A . n 
A 1 157 VAL 157 157 157 VAL VAL A . n 
A 1 158 SER 158 158 158 SER SER A . n 
A 1 159 PHE 159 159 159 PHE PHE A . n 
A 1 160 CYS 160 160 160 CYS CYS A . n 
A 1 161 TYR 161 161 161 TYR TYR A . n 
A 1 162 MET 162 162 162 MET MET A . n 
A 1 163 HIS 163 163 163 HIS HIS A . n 
A 1 164 HIS 164 164 164 HIS HIS A . n 
A 1 165 MET 165 165 165 MET MET A . n 
A 1 166 GLU 166 166 166 GLU GLU A . n 
A 1 167 LEU 167 167 167 LEU LEU A . n 
A 1 168 PRO 168 168 168 PRO PRO A . n 
A 1 169 THR 169 169 169 THR THR A . n 
A 1 170 GLY 170 170 170 GLY GLY A . n 
A 1 171 VAL 171 171 171 VAL VAL A . n 
A 1 172 HIS 172 172 172 HIS HIS A . n 
A 1 173 ALA 173 173 173 ALA ALA A . n 
A 1 174 GLY 174 174 174 GLY GLY A . n 
A 1 175 THR 175 175 175 THR THR A . n 
A 1 176 ASP 176 176 176 ASP ASP A . n 
A 1 177 LEU 177 177 177 LEU LEU A . n 
A 1 178 GLU 178 178 178 GLU GLU A . n 
A 1 179 GLY 179 179 179 GLY GLY A . n 
A 1 180 ASN 180 180 180 ASN ASN A . n 
A 1 181 PHE 181 181 181 PHE PHE A . n 
A 1 182 TYR 182 182 182 TYR TYR A . n 
A 1 183 GLY 183 183 183 GLY GLY A . n 
A 1 184 PRO 184 184 184 PRO PRO A . n 
A 1 185 PHE 185 185 185 PHE PHE A . n 
A 1 186 VAL 186 186 186 VAL VAL A . n 
A 1 187 ASP 187 187 187 ASP ASP A . n 
A 1 188 ARG 188 188 188 ARG ARG A . n 
A 1 189 GLN 189 189 189 GLN GLN A . n 
A 1 190 THR 190 190 190 THR THR A . n 
A 1 191 ALA 191 191 191 ALA ALA A . n 
A 1 192 GLN 192 192 192 GLN GLN A . n 
A 1 193 ALA 193 193 193 ALA ALA A . n 
A 1 194 ALA 194 194 194 ALA ALA A . n 
A 1 195 GLY 195 195 195 GLY GLY A . n 
A 1 196 THR 196 196 196 THR THR A . n 
A 1 197 ASP 197 197 197 ASP ASP A . n 
A 1 198 THR 198 198 198 THR THR A . n 
A 1 199 THR 199 199 199 THR THR A . n 
A 1 200 ILE 200 200 200 ILE ILE A . n 
A 1 201 THR 201 201 201 THR THR A . n 
A 1 202 VAL 202 202 202 VAL VAL A . n 
A 1 203 ASN 203 203 203 ASN ASN A . n 
A 1 204 VAL 204 204 204 VAL VAL A . n 
A 1 205 LEU 205 205 205 LEU LEU A . n 
A 1 206 ALA 206 206 206 ALA ALA A . n 
A 1 207 TRP 207 207 207 TRP TRP A . n 
A 1 208 LEU 208 208 208 LEU LEU A . n 
A 1 209 TYR 209 209 209 TYR TYR A . n 
A 1 210 ALA 210 210 210 ALA ALA A . n 
A 1 211 ALA 211 211 211 ALA ALA A . n 
A 1 212 VAL 212 212 212 VAL VAL A . n 
A 1 213 ILE 213 213 213 ILE ILE A . n 
A 1 214 ASN 214 214 214 ASN ASN A . n 
A 1 215 GLY 215 215 215 GLY GLY A . n 
A 1 216 ASP 216 216 216 ASP ASP A . n 
A 1 217 ARG 217 217 217 ARG ARG A . n 
A 1 218 TRP 218 218 218 TRP TRP A . n 
A 1 219 PHE 219 219 219 PHE PHE A . n 
A 1 220 LEU 220 220 220 LEU LEU A . n 
A 1 221 ASN 221 221 221 ASN ASN A . n 
A 1 222 ARG 222 222 222 ARG ARG A . n 
A 1 223 PHE 223 223 223 PHE PHE A . n 
A 1 224 THR 224 224 224 THR THR A . n 
A 1 225 THR 225 225 225 THR THR A . n 
A 1 226 THR 226 226 226 THR THR A . n 
A 1 227 LEU 227 227 227 LEU LEU A . n 
A 1 228 ASN 228 228 228 ASN ASN A . n 
A 1 229 ASP 229 229 229 ASP ASP A . n 
A 1 230 PHE 230 230 230 PHE PHE A . n 
A 1 231 ASN 231 231 231 ASN ASN A . n 
A 1 232 LEU 232 232 232 LEU LEU A . n 
A 1 233 VAL 233 233 233 VAL VAL A . n 
A 1 234 ALA 234 234 234 ALA ALA A . n 
A 1 235 MET 235 235 235 MET MET A . n 
A 1 236 LYS 236 236 236 LYS LYS A . n 
A 1 237 TYR 237 237 237 TYR TYR A . n 
A 1 238 ASN 238 238 238 ASN ASN A . n 
A 1 239 TYR 239 239 239 TYR TYR A . n 
A 1 240 GLU 240 240 240 GLU GLU A . n 
A 1 241 PRO 241 241 241 PRO PRO A . n 
A 1 242 LEU 242 242 242 LEU LEU A . n 
A 1 243 THR 243 243 243 THR THR A . n 
A 1 244 GLN 244 244 244 GLN GLN A . n 
A 1 245 ASP 245 245 245 ASP ASP A . n 
A 1 246 HIS 246 246 246 HIS HIS A . n 
A 1 247 VAL 247 247 247 VAL VAL A . n 
A 1 248 ASP 248 248 248 ASP ASP A . n 
A 1 249 ILE 249 249 249 ILE ILE A . n 
A 1 250 LEU 250 250 250 LEU LEU A . n 
A 1 251 GLY 251 251 251 GLY GLY A . n 
A 1 252 PRO 252 252 252 PRO PRO A . n 
A 1 253 LEU 253 253 253 LEU LEU A . n 
A 1 254 SER 254 254 254 SER SER A . n 
A 1 255 ALA 255 255 255 ALA ALA A . n 
A 1 256 GLN 256 256 256 GLN GLN A . n 
A 1 257 THR 257 257 257 THR THR A . n 
A 1 258 GLY 258 258 258 GLY GLY A . n 
A 1 259 ILE 259 259 259 ILE ILE A . n 
A 1 260 ALA 260 260 260 ALA ALA A . n 
A 1 261 VAL 261 261 261 VAL VAL A . n 
A 1 262 LEU 262 262 262 LEU LEU A . n 
A 1 263 ASP 263 263 263 ASP ASP A . n 
A 1 264 MET 264 264 264 MET MET A . n 
A 1 265 CYS 265 265 265 CYS CYS A . n 
A 1 266 ALA 266 266 266 ALA ALA A . n 
A 1 267 SER 267 267 267 SER SER A . n 
A 1 268 LEU 268 268 268 LEU LEU A . n 
A 1 269 LYS 269 269 269 LYS LYS A . n 
A 1 270 GLU 270 270 270 GLU GLU A . n 
A 1 271 LEU 271 271 271 LEU LEU A . n 
A 1 272 LEU 272 272 272 LEU LEU A . n 
A 1 273 GLN 273 273 273 GLN GLN A . n 
A 1 274 ASN 274 274 274 ASN ASN A . n 
A 1 275 GLY 275 275 275 GLY GLY A . n 
A 1 276 MET 276 276 276 MET MET A . n 
A 1 277 ASN 277 277 277 ASN ASN A . n 
A 1 278 GLY 278 278 278 GLY GLY A . n 
A 1 279 ARG 279 279 279 ARG ARG A . n 
A 1 280 THR 280 280 280 THR THR A . n 
A 1 281 ILE 281 281 281 ILE ILE A . n 
A 1 282 LEU 282 282 282 LEU LEU A . n 
A 1 283 GLY 283 283 283 GLY GLY A . n 
A 1 284 SER 284 284 284 SER SER A . n 
A 1 285 ALA 285 285 285 ALA ALA A . n 
A 1 286 LEU 286 286 286 LEU LEU A . n 
A 1 287 LEU 287 287 287 LEU LEU A . n 
A 1 288 GLU 288 288 288 GLU GLU A . n 
A 1 289 ASP 289 289 289 ASP ASP A . n 
A 1 290 GLU 290 290 290 GLU GLU A . n 
A 1 291 PHE 291 291 291 PHE PHE A . n 
A 1 292 THR 292 292 292 THR THR A . n 
A 1 293 PRO 293 293 293 PRO PRO A . n 
A 1 294 PHE 294 294 294 PHE PHE A . n 
A 1 295 ASP 295 295 295 ASP ASP A . n 
A 1 296 VAL 296 296 296 VAL VAL A . n 
A 1 297 VAL 297 297 297 VAL VAL A . n 
A 1 298 ARG 298 298 298 ARG ARG A . n 
A 1 299 GLN 299 299 299 GLN GLN A . n 
A 1 300 CYS 300 300 300 CYS CYS A . n 
A 1 301 SER 301 301 ?   ?   ?   A . n 
A 1 302 GLY 302 302 ?   ?   ?   A . n 
A 1 303 VAL 303 303 ?   ?   ?   A . n 
A 1 304 THR 304 304 ?   ?   ?   A . n 
A 1 305 PHE 305 305 ?   ?   ?   A . n 
A 1 306 GLN 306 306 ?   ?   ?   A . n 
B 1 1   SER 1   1   1   SER SER B . n 
B 1 2   GLY 2   2   2   GLY GLY B . n 
B 1 3   PHE 3   3   3   PHE PHE B . n 
B 1 4   ARG 4   4   4   ARG ARG B . n 
B 1 5   LYS 5   5   5   LYS LYS B . n 
B 1 6   MET 6   6   6   MET MET B . n 
B 1 7   ALA 7   7   7   ALA ALA B . n 
B 1 8   PHE 8   8   8   PHE PHE B . n 
B 1 9   PRO 9   9   9   PRO PRO B . n 
B 1 10  SER 10  10  10  SER SER B . n 
B 1 11  GLY 11  11  11  GLY GLY B . n 
B 1 12  LYS 12  12  12  LYS LYS B . n 
B 1 13  VAL 13  13  13  VAL VAL B . n 
B 1 14  GLU 14  14  14  GLU GLU B . n 
B 1 15  GLY 15  15  15  GLY GLY B . n 
B 1 16  CYS 16  16  16  CYS CYS B . n 
B 1 17  MET 17  17  17  MET MET B . n 
B 1 18  VAL 18  18  18  VAL VAL B . n 
B 1 19  GLN 19  19  19  GLN GLN B . n 
B 1 20  VAL 20  20  20  VAL VAL B . n 
B 1 21  THR 21  21  21  THR THR B . n 
B 1 22  CYS 22  22  22  CYS CYS B . n 
B 1 23  GLY 23  23  23  GLY GLY B . n 
B 1 24  THR 24  24  24  THR THR B . n 
B 1 25  THR 25  25  25  THR THR B . n 
B 1 26  THR 26  26  26  THR THR B . n 
B 1 27  LEU 27  27  27  LEU LEU B . n 
B 1 28  ASN 28  28  28  ASN ASN B . n 
B 1 29  GLY 29  29  29  GLY GLY B . n 
B 1 30  LEU 30  30  30  LEU LEU B . n 
B 1 31  TRP 31  31  31  TRP TRP B . n 
B 1 32  LEU 32  32  32  LEU LEU B . n 
B 1 33  ASP 33  33  33  ASP ASP B . n 
B 1 34  ASP 34  34  34  ASP ASP B . n 
B 1 35  VAL 35  35  35  VAL VAL B . n 
B 1 36  VAL 36  36  36  VAL VAL B . n 
B 1 37  TYR 37  37  37  TYR TYR B . n 
B 1 38  CYS 38  38  38  CYS CYS B . n 
B 1 39  PRO 39  39  39  PRO PRO B . n 
B 1 40  ARG 40  40  40  ARG ARG B . n 
B 1 41  HIS 41  41  41  HIS HIS B . n 
B 1 42  VAL 42  42  42  VAL VAL B . n 
B 1 43  ILE 43  43  43  ILE ILE B . n 
B 1 44  CYS 44  44  44  CYS CYS B . n 
B 1 45  THR 45  45  45  THR THR B . n 
B 1 46  SER 46  46  46  SER SER B . n 
B 1 47  GLU 47  47  47  GLU GLU B . n 
B 1 48  ASP 48  48  48  ASP ASP B . n 
B 1 49  MET 49  49  49  MET MET B . n 
B 1 50  LEU 50  50  50  LEU LEU B . n 
B 1 51  ASN 51  51  51  ASN ASN B . n 
B 1 52  PRO 52  52  52  PRO PRO B . n 
B 1 53  ASN 53  53  53  ASN ASN B . n 
B 1 54  TYR 54  54  54  TYR TYR B . n 
B 1 55  GLU 55  55  55  GLU GLU B . n 
B 1 56  ASP 56  56  56  ASP ASP B . n 
B 1 57  LEU 57  57  57  LEU LEU B . n 
B 1 58  LEU 58  58  58  LEU LEU B . n 
B 1 59  ILE 59  59  59  ILE ILE B . n 
B 1 60  ARG 60  60  60  ARG ARG B . n 
B 1 61  LYS 61  61  61  LYS LYS B . n 
B 1 62  SER 62  62  62  SER SER B . n 
B 1 63  ASN 63  63  63  ASN ASN B . n 
B 1 64  HIS 64  64  64  HIS HIS B . n 
B 1 65  ASN 65  65  65  ASN ASN B . n 
B 1 66  PHE 66  66  66  PHE PHE B . n 
B 1 67  LEU 67  67  67  LEU LEU B . n 
B 1 68  VAL 68  68  68  VAL VAL B . n 
B 1 69  GLN 69  69  69  GLN GLN B . n 
B 1 70  ALA 70  70  70  ALA ALA B . n 
B 1 71  GLY 71  71  71  GLY GLY B . n 
B 1 72  ASN 72  72  72  ASN ASN B . n 
B 1 73  VAL 73  73  73  VAL VAL B . n 
B 1 74  GLN 74  74  74  GLN GLN B . n 
B 1 75  LEU 75  75  75  LEU LEU B . n 
B 1 76  ARG 76  76  76  ARG ARG B . n 
B 1 77  VAL 77  77  77  VAL VAL B . n 
B 1 78  ILE 78  78  78  ILE ILE B . n 
B 1 79  GLY 79  79  79  GLY GLY B . n 
B 1 80  HIS 80  80  80  HIS HIS B . n 
B 1 81  SER 81  81  81  SER SER B . n 
B 1 82  MET 82  82  82  MET MET B . n 
B 1 83  GLN 83  83  83  GLN GLN B . n 
B 1 84  ASN 84  84  84  ASN ASN B . n 
B 1 85  CYS 85  85  85  CYS CYS B . n 
B 1 86  VAL 86  86  86  VAL VAL B . n 
B 1 87  LEU 87  87  87  LEU LEU B . n 
B 1 88  LYS 88  88  88  LYS LYS B . n 
B 1 89  LEU 89  89  89  LEU LEU B . n 
B 1 90  LYS 90  90  90  LYS LYS B . n 
B 1 91  VAL 91  91  91  VAL VAL B . n 
B 1 92  ASP 92  92  92  ASP ASP B . n 
B 1 93  THR 93  93  93  THR THR B . n 
B 1 94  ALA 94  94  94  ALA ALA B . n 
B 1 95  ASN 95  95  95  ASN ASN B . n 
B 1 96  PRO 96  96  96  PRO PRO B . n 
B 1 97  LYS 97  97  97  LYS LYS B . n 
B 1 98  THR 98  98  98  THR THR B . n 
B 1 99  PRO 99  99  99  PRO PRO B . n 
B 1 100 LYS 100 100 100 LYS LYS B . n 
B 1 101 TYR 101 101 101 TYR TYR B . n 
B 1 102 LYS 102 102 102 LYS LYS B . n 
B 1 103 PHE 103 103 103 PHE PHE B . n 
B 1 104 VAL 104 104 104 VAL VAL B . n 
B 1 105 ARG 105 105 105 ARG ARG B . n 
B 1 106 ILE 106 106 106 ILE ILE B . n 
B 1 107 GLN 107 107 107 GLN GLN B . n 
B 1 108 PRO 108 108 108 PRO PRO B . n 
B 1 109 GLY 109 109 109 GLY GLY B . n 
B 1 110 GLN 110 110 110 GLN GLN B . n 
B 1 111 THR 111 111 111 THR THR B . n 
B 1 112 PHE 112 112 112 PHE PHE B . n 
B 1 113 SER 113 113 113 SER SER B . n 
B 1 114 VAL 114 114 114 VAL VAL B . n 
B 1 115 LEU 115 115 115 LEU LEU B . n 
B 1 116 ALA 116 116 116 ALA ALA B . n 
B 1 117 CYS 117 117 117 CYS CYS B . n 
B 1 118 TYR 118 118 118 TYR TYR B . n 
B 1 119 ASN 119 119 119 ASN ASN B . n 
B 1 120 GLY 120 120 120 GLY GLY B . n 
B 1 121 SER 121 121 121 SER SER B . n 
B 1 122 PRO 122 122 122 PRO PRO B . n 
B 1 123 SER 123 123 123 SER SER B . n 
B 1 124 GLY 124 124 124 GLY GLY B . n 
B 1 125 VAL 125 125 125 VAL VAL B . n 
B 1 126 TYR 126 126 126 TYR TYR B . n 
B 1 127 GLN 127 127 127 GLN GLN B . n 
B 1 128 CYS 128 128 128 CYS CYS B . n 
B 1 129 ALA 129 129 129 ALA ALA B . n 
B 1 130 MET 130 130 130 MET MET B . n 
B 1 131 ARG 131 131 131 ARG ARG B . n 
B 1 132 PRO 132 132 132 PRO PRO B . n 
B 1 133 ASN 133 133 133 ASN ASN B . n 
B 1 134 PHE 134 134 134 PHE PHE B . n 
B 1 135 THR 135 135 135 THR THR B . n 
B 1 136 ILE 136 136 136 ILE ILE B . n 
B 1 137 LYS 137 137 137 LYS LYS B . n 
B 1 138 GLY 138 138 138 GLY GLY B . n 
B 1 139 SER 139 139 139 SER SER B . n 
B 1 140 PHE 140 140 140 PHE PHE B . n 
B 1 141 LEU 141 141 141 LEU LEU B . n 
B 1 142 ASN 142 142 142 ASN ASN B . n 
B 1 143 GLY 143 143 143 GLY GLY B . n 
B 1 144 SER 144 144 144 SER SER B . n 
B 1 145 CYS 145 145 145 CYS CYS B . n 
B 1 146 GLY 146 146 146 GLY GLY B . n 
B 1 147 SER 147 147 147 SER SER B . n 
B 1 148 VAL 148 148 148 VAL VAL B . n 
B 1 149 GLY 149 149 149 GLY GLY B . n 
B 1 150 PHE 150 150 150 PHE PHE B . n 
B 1 151 ASN 151 151 151 ASN ASN B . n 
B 1 152 ILE 152 152 152 ILE ILE B . n 
B 1 153 ASP 153 153 153 ASP ASP B . n 
B 1 154 TYR 154 154 154 TYR TYR B . n 
B 1 155 ASP 155 155 155 ASP ASP B . n 
B 1 156 CYS 156 156 156 CYS CYS B . n 
B 1 157 VAL 157 157 157 VAL VAL B . n 
B 1 158 SER 158 158 158 SER SER B . n 
B 1 159 PHE 159 159 159 PHE PHE B . n 
B 1 160 CYS 160 160 160 CYS CYS B . n 
B 1 161 TYR 161 161 161 TYR TYR B . n 
B 1 162 MET 162 162 162 MET MET B . n 
B 1 163 HIS 163 163 163 HIS HIS B . n 
B 1 164 HIS 164 164 164 HIS HIS B . n 
B 1 165 MET 165 165 165 MET MET B . n 
B 1 166 GLU 166 166 166 GLU GLU B . n 
B 1 167 LEU 167 167 167 LEU LEU B . n 
B 1 168 PRO 168 168 168 PRO PRO B . n 
B 1 169 THR 169 169 169 THR THR B . n 
B 1 170 GLY 170 170 170 GLY GLY B . n 
B 1 171 VAL 171 171 171 VAL VAL B . n 
B 1 172 HIS 172 172 172 HIS HIS B . n 
B 1 173 ALA 173 173 173 ALA ALA B . n 
B 1 174 GLY 174 174 174 GLY GLY B . n 
B 1 175 THR 175 175 175 THR THR B . n 
B 1 176 ASP 176 176 176 ASP ASP B . n 
B 1 177 LEU 177 177 177 LEU LEU B . n 
B 1 178 GLU 178 178 178 GLU GLU B . n 
B 1 179 GLY 179 179 179 GLY GLY B . n 
B 1 180 ASN 180 180 180 ASN ASN B . n 
B 1 181 PHE 181 181 181 PHE PHE B . n 
B 1 182 TYR 182 182 182 TYR TYR B . n 
B 1 183 GLY 183 183 183 GLY GLY B . n 
B 1 184 PRO 184 184 184 PRO PRO B . n 
B 1 185 PHE 185 185 185 PHE PHE B . n 
B 1 186 VAL 186 186 186 VAL VAL B . n 
B 1 187 ASP 187 187 187 ASP ASP B . n 
B 1 188 ARG 188 188 188 ARG ARG B . n 
B 1 189 GLN 189 189 189 GLN GLN B . n 
B 1 190 THR 190 190 190 THR THR B . n 
B 1 191 ALA 191 191 191 ALA ALA B . n 
B 1 192 GLN 192 192 192 GLN GLN B . n 
B 1 193 ALA 193 193 193 ALA ALA B . n 
B 1 194 ALA 194 194 194 ALA ALA B . n 
B 1 195 GLY 195 195 195 GLY GLY B . n 
B 1 196 THR 196 196 196 THR THR B . n 
B 1 197 ASP 197 197 197 ASP ASP B . n 
B 1 198 THR 198 198 198 THR THR B . n 
B 1 199 THR 199 199 199 THR THR B . n 
B 1 200 ILE 200 200 200 ILE ILE B . n 
B 1 201 THR 201 201 201 THR THR B . n 
B 1 202 VAL 202 202 202 VAL VAL B . n 
B 1 203 ASN 203 203 203 ASN ASN B . n 
B 1 204 VAL 204 204 204 VAL VAL B . n 
B 1 205 LEU 205 205 205 LEU LEU B . n 
B 1 206 ALA 206 206 206 ALA ALA B . n 
B 1 207 TRP 207 207 207 TRP TRP B . n 
B 1 208 LEU 208 208 208 LEU LEU B . n 
B 1 209 TYR 209 209 209 TYR TYR B . n 
B 1 210 ALA 210 210 210 ALA ALA B . n 
B 1 211 ALA 211 211 211 ALA ALA B . n 
B 1 212 VAL 212 212 212 VAL VAL B . n 
B 1 213 ILE 213 213 213 ILE ILE B . n 
B 1 214 ASN 214 214 214 ASN ASN B . n 
B 1 215 GLY 215 215 215 GLY GLY B . n 
B 1 216 ASP 216 216 216 ASP ASP B . n 
B 1 217 ARG 217 217 217 ARG ARG B . n 
B 1 218 TRP 218 218 218 TRP TRP B . n 
B 1 219 PHE 219 219 219 PHE PHE B . n 
B 1 220 LEU 220 220 220 LEU LEU B . n 
B 1 221 ASN 221 221 221 ASN ASN B . n 
B 1 222 ARG 222 222 222 ARG ARG B . n 
B 1 223 PHE 223 223 223 PHE PHE B . n 
B 1 224 THR 224 224 224 THR THR B . n 
B 1 225 THR 225 225 225 THR THR B . n 
B 1 226 THR 226 226 226 THR THR B . n 
B 1 227 LEU 227 227 227 LEU LEU B . n 
B 1 228 ASN 228 228 228 ASN ASN B . n 
B 1 229 ASP 229 229 229 ASP ASP B . n 
B 1 230 PHE 230 230 230 PHE PHE B . n 
B 1 231 ASN 231 231 231 ASN ASN B . n 
B 1 232 LEU 232 232 232 LEU LEU B . n 
B 1 233 VAL 233 233 233 VAL VAL B . n 
B 1 234 ALA 234 234 234 ALA ALA B . n 
B 1 235 MET 235 235 235 MET MET B . n 
B 1 236 LYS 236 236 236 LYS LYS B . n 
B 1 237 TYR 237 237 237 TYR TYR B . n 
B 1 238 ASN 238 238 238 ASN ASN B . n 
B 1 239 TYR 239 239 239 TYR TYR B . n 
B 1 240 GLU 240 240 240 GLU GLU B . n 
B 1 241 PRO 241 241 241 PRO PRO B . n 
B 1 242 LEU 242 242 242 LEU LEU B . n 
B 1 243 THR 243 243 243 THR THR B . n 
B 1 244 GLN 244 244 244 GLN GLN B . n 
B 1 245 ASP 245 245 245 ASP ASP B . n 
B 1 246 HIS 246 246 246 HIS HIS B . n 
B 1 247 VAL 247 247 247 VAL VAL B . n 
B 1 248 ASP 248 248 248 ASP ASP B . n 
B 1 249 ILE 249 249 249 ILE ILE B . n 
B 1 250 LEU 250 250 250 LEU LEU B . n 
B 1 251 GLY 251 251 251 GLY GLY B . n 
B 1 252 PRO 252 252 252 PRO PRO B . n 
B 1 253 LEU 253 253 253 LEU LEU B . n 
B 1 254 SER 254 254 254 SER SER B . n 
B 1 255 ALA 255 255 255 ALA ALA B . n 
B 1 256 GLN 256 256 256 GLN GLN B . n 
B 1 257 THR 257 257 257 THR THR B . n 
B 1 258 GLY 258 258 258 GLY GLY B . n 
B 1 259 ILE 259 259 259 ILE ILE B . n 
B 1 260 ALA 260 260 260 ALA ALA B . n 
B 1 261 VAL 261 261 261 VAL VAL B . n 
B 1 262 LEU 262 262 262 LEU LEU B . n 
B 1 263 ASP 263 263 263 ASP ASP B . n 
B 1 264 MET 264 264 264 MET MET B . n 
B 1 265 CYS 265 265 265 CYS CYS B . n 
B 1 266 ALA 266 266 266 ALA ALA B . n 
B 1 267 SER 267 267 267 SER SER B . n 
B 1 268 LEU 268 268 268 LEU LEU B . n 
B 1 269 LYS 269 269 269 LYS LYS B . n 
B 1 270 GLU 270 270 270 GLU GLU B . n 
B 1 271 LEU 271 271 271 LEU LEU B . n 
B 1 272 LEU 272 272 272 LEU LEU B . n 
B 1 273 GLN 273 273 273 GLN GLN B . n 
B 1 274 ASN 274 274 274 ASN ASN B . n 
B 1 275 GLY 275 275 275 GLY GLY B . n 
B 1 276 MET 276 276 276 MET MET B . n 
B 1 277 ASN 277 277 277 ASN ASN B . n 
B 1 278 GLY 278 278 278 GLY GLY B . n 
B 1 279 ARG 279 279 279 ARG ARG B . n 
B 1 280 THR 280 280 280 THR THR B . n 
B 1 281 ILE 281 281 281 ILE ILE B . n 
B 1 282 LEU 282 282 282 LEU LEU B . n 
B 1 283 GLY 283 283 283 GLY GLY B . n 
B 1 284 SER 284 284 284 SER SER B . n 
B 1 285 ALA 285 285 285 ALA ALA B . n 
B 1 286 LEU 286 286 286 LEU LEU B . n 
B 1 287 LEU 287 287 287 LEU LEU B . n 
B 1 288 GLU 288 288 288 GLU GLU B . n 
B 1 289 ASP 289 289 289 ASP ASP B . n 
B 1 290 GLU 290 290 290 GLU GLU B . n 
B 1 291 PHE 291 291 291 PHE PHE B . n 
B 1 292 THR 292 292 292 THR THR B . n 
B 1 293 PRO 293 293 293 PRO PRO B . n 
B 1 294 PHE 294 294 294 PHE PHE B . n 
B 1 295 ASP 295 295 295 ASP ASP B . n 
B 1 296 VAL 296 296 296 VAL VAL B . n 
B 1 297 VAL 297 297 297 VAL VAL B . n 
B 1 298 ARG 298 298 298 ARG ARG B . n 
B 1 299 GLN 299 299 299 GLN GLN B . n 
B 1 300 CYS 300 300 300 CYS CYS B . n 
B 1 301 SER 301 301 301 SER SER B . n 
B 1 302 GLY 302 302 302 GLY GLY B . n 
B 1 303 VAL 303 303 303 VAL VAL B . n 
B 1 304 THR 304 304 304 THR THR B . n 
B 1 305 PHE 305 305 305 PHE PHE B . n 
B 1 306 GLN 306 306 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        RD4 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   RD4 
_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 
C 2 CL  1  401 410 CL  CL  A . 
D 3 RD4 1  402 501 RD4 LIG A . 
E 4 NA  1  401 406 NA  NA  B . 
F 2 CL  1  402 1   CL  CL  B . 
G 5 HOH 1  501 82  HOH HOH A . 
G 5 HOH 2  502 29  HOH HOH A . 
G 5 HOH 3  503 94  HOH HOH A . 
G 5 HOH 4  504 91  HOH HOH A . 
G 5 HOH 5  505 4   HOH HOH A . 
G 5 HOH 6  506 65  HOH HOH A . 
G 5 HOH 7  507 31  HOH HOH A . 
G 5 HOH 8  508 67  HOH HOH A . 
G 5 HOH 9  509 2   HOH HOH A . 
G 5 HOH 10 510 26  HOH HOH A . 
G 5 HOH 11 511 36  HOH HOH A . 
G 5 HOH 12 512 84  HOH HOH A . 
G 5 HOH 13 513 81  HOH HOH A . 
G 5 HOH 14 514 38  HOH HOH A . 
G 5 HOH 15 515 98  HOH HOH A . 
G 5 HOH 16 516 7   HOH HOH A . 
G 5 HOH 17 517 97  HOH HOH A . 
G 5 HOH 18 518 96  HOH HOH A . 
G 5 HOH 19 519 41  HOH HOH A . 
G 5 HOH 20 520 33  HOH HOH A . 
G 5 HOH 21 521 28  HOH HOH A . 
G 5 HOH 22 522 75  HOH HOH A . 
G 5 HOH 23 523 15  HOH HOH A . 
G 5 HOH 24 524 3   HOH HOH A . 
G 5 HOH 25 525 37  HOH HOH A . 
G 5 HOH 26 526 5   HOH HOH A . 
G 5 HOH 27 527 8   HOH HOH A . 
G 5 HOH 28 528 60  HOH HOH A . 
G 5 HOH 29 529 50  HOH HOH A . 
G 5 HOH 30 530 88  HOH HOH A . 
G 5 HOH 31 531 13  HOH HOH A . 
G 5 HOH 32 532 44  HOH HOH A . 
G 5 HOH 33 533 20  HOH HOH A . 
G 5 HOH 34 534 25  HOH HOH A . 
G 5 HOH 35 535 12  HOH HOH A . 
G 5 HOH 36 536 24  HOH HOH A . 
G 5 HOH 37 537 68  HOH HOH A . 
G 5 HOH 38 538 18  HOH HOH A . 
G 5 HOH 39 539 74  HOH HOH A . 
G 5 HOH 40 540 77  HOH HOH A . 
G 5 HOH 41 541 46  HOH HOH A . 
G 5 HOH 42 542 51  HOH HOH A . 
G 5 HOH 43 543 80  HOH HOH A . 
G 5 HOH 44 544 69  HOH HOH A . 
G 5 HOH 45 545 42  HOH HOH A . 
G 5 HOH 46 546 55  HOH HOH A . 
G 5 HOH 47 547 61  HOH HOH A . 
G 5 HOH 48 548 39  HOH HOH A . 
G 5 HOH 49 549 45  HOH HOH A . 
G 5 HOH 50 550 32  HOH HOH A . 
G 5 HOH 51 551 23  HOH HOH A . 
G 5 HOH 52 552 43  HOH HOH A . 
G 5 HOH 53 553 58  HOH HOH A . 
G 5 HOH 54 554 40  HOH HOH A . 
G 5 HOH 55 555 72  HOH HOH A . 
G 5 HOH 56 556 83  HOH HOH A . 
G 5 HOH 57 557 17  HOH HOH A . 
G 5 HOH 58 558 14  HOH HOH A . 
G 5 HOH 59 559 86  HOH HOH A . 
G 5 HOH 60 560 101 HOH HOH A . 
G 5 HOH 61 561 66  HOH HOH A . 
G 5 HOH 62 562 89  HOH HOH A . 
G 5 HOH 63 563 56  HOH HOH A . 
G 5 HOH 64 564 48  HOH HOH A . 
G 5 HOH 65 565 76  HOH HOH A . 
G 5 HOH 66 566 92  HOH HOH A . 
H 5 HOH 1  501 79  HOH HOH B . 
H 5 HOH 2  502 71  HOH HOH B . 
H 5 HOH 3  503 11  HOH HOH B . 
H 5 HOH 4  504 34  HOH HOH B . 
H 5 HOH 5  505 9   HOH HOH B . 
H 5 HOH 6  506 21  HOH HOH B . 
H 5 HOH 7  507 62  HOH HOH B . 
H 5 HOH 8  508 70  HOH HOH B . 
H 5 HOH 9  509 6   HOH HOH B . 
H 5 HOH 10 510 78  HOH HOH B . 
H 5 HOH 11 511 16  HOH HOH B . 
H 5 HOH 12 512 99  HOH HOH B . 
H 5 HOH 13 513 95  HOH HOH B . 
H 5 HOH 14 514 90  HOH HOH B . 
H 5 HOH 15 515 100 HOH HOH B . 
H 5 HOH 16 516 52  HOH HOH B . 
H 5 HOH 17 517 19  HOH HOH B . 
H 5 HOH 18 518 85  HOH HOH B . 
H 5 HOH 19 519 64  HOH HOH B . 
H 5 HOH 20 520 49  HOH HOH B . 
H 5 HOH 21 521 53  HOH HOH B . 
H 5 HOH 22 522 59  HOH HOH B . 
H 5 HOH 23 523 93  HOH HOH B . 
H 5 HOH 24 524 35  HOH HOH B . 
H 5 HOH 25 525 27  HOH HOH B . 
H 5 HOH 26 526 22  HOH HOH B . 
H 5 HOH 27 527 57  HOH HOH B . 
H 5 HOH 28 528 73  HOH HOH B . 
H 5 HOH 29 529 10  HOH HOH B . 
H 5 HOH 30 530 47  HOH HOH B . 
H 5 HOH 31 531 87  HOH HOH B . 
H 5 HOH 32 532 30  HOH HOH B . 
H 5 HOH 33 533 54  HOH HOH B . 
H 5 HOH 34 534 63  HOH HOH B . 
# 
loop_
_software.classification 
_software.name 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
refinement       REFMAC 5.8.0238 ? 1 
'data scaling'   XDS    .        ? 2 
'data reduction' XDS    .        ? 3 
phasing          PHASER .        ? 4 
# 
_cell.entry_id           7I1E 
_cell.length_a           67.920 
_cell.length_b           99.590 
_cell.length_c           103.670 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        90.00 
_cell.Z_PDB              8 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7I1E 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
# 
_exptl.entry_id          7I1E 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.59 
_exptl_crystal.density_percent_sol   52.61 
_exptl_crystal.density_meas          ? 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pdbx_details    
;0.2 M MIB (sodium malonate, imidazole, and boric acid in the molar ratios 2:3:3) pH 7.7, 23.5 % PEG 1500, 5 % DMSO, 1 mM DTT. Crystal seeds were used to ensure reproducible crystal growth.
;
_exptl_crystal_grow.temp            291 
_exptl_crystal_grow.pH              7.7 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.crystal_id             1 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.pdbx_collection_date   2022-12-06 
_diffrn_detector.type                   'DECTRIS PILATUS3 6M' 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_scattering_type             x-ray 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.monochromator                    ? 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9184 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.pdbx_wavelength_list        0.9184 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'BESSY BEAMLINE 14.1' 
_diffrn_source.pdbx_synchrotron_site       BESSY 
_diffrn_source.pdbx_synchrotron_beamline   14.1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7I1E 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             45.98 
_reflns.d_resolution_high            1.88 
_reflns.number_obs                   57498 
_reflns.percent_possible_obs         99.3 
_reflns.pdbx_Rmerge_I_obs            0.142 
_reflns.pdbx_netI_over_sigmaI        8.62 
_reflns.pdbx_Rrim_I_all              0.157 
_reflns.pdbx_CC_half                 0.997 
_reflns.pdbx_number_measured_all     333006 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.number_all                   ? 
_reflns.pdbx_Rsym_value              ? 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              ? 
# 
loop_
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_ordinal 
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.number_measured_obs 
_reflns_shell.number_unique_obs 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.percent_possible_obs 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_CC_half 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_redundancy 
1 1 1.88 1.99 51568 9151 1.33                 99.0 1.09  1.466                0.45299999999999996 ? ? ? ? 
1 2 1.99 2.13 53179 8654 0.841                99.7 1.89  0.919                0.701               ? ? ? ? 
1 3 2.13 2.3  48904 8061 0.529                99.4 3.02  0.579                0.846               ? ? ? ? 
1 4 2.30 2.52 42062 7424 0.34700000000000003  99.1 4.46  0.382                0.927               ? ? ? ? 
1 5 2.52 2.82 41478 6778 0.22899999999999998  99.7 7.30  0.251                0.97                ? ? ? ? 
1 6 2.82 3.25 35518 6008 0.134                99.6 12.34 0.14800000000000002  0.99                ? ? ? ? 
1 7 3.25 3.98 26557 5081 0.075                98.7 20.29 0.083                0.996               ? ? ? ? 
1 8 3.98 5.6  21711 4014 0.052000000000000005 99.6 28.76 0.057999999999999996 0.997               ? ? ? ? 
1 9 5.60 ?    12029 2327 0.040999999999999995 97.9 30.05 0.045                0.998               ? ? ? ? 
# 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.entry_id                                 7I1E 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     55398 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             45.98 
_refine.ls_d_res_high                            1.88 
_refine.ls_percent_reflns_obs                    99.28 
_refine.ls_R_factor_obs                          0.21747 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.21639 
_refine.ls_R_factor_R_free                       0.24618 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 3.7 
_refine.ls_number_reflns_R_free                  2100 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.953 
_refine.correlation_coeff_Fo_to_Fc_free          0.940 
_refine.B_iso_mean                               33.125 
_refine.aniso_B[1][1]                            -0.96 
_refine.aniso_B[2][2]                            1.15 
_refine.aniso_B[3][3]                            -0.18 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            -0.00 
_refine.aniso_B[2][3]                            -0.00 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       0.156 
_refine.pdbx_overall_ESU_R_Free                  0.142 
_refine.overall_SU_ML                            0.142 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             5.272 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        4681 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         15 
_refine_hist.number_atoms_solvent             100 
_refine_hist.number_atoms_total               4796 
_refine_hist.d_res_high                       1.88 
_refine_hist.d_res_low                        45.98 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
r_bond_refined_d             0.008  0.013  ? 5222  'X-RAY DIFFRACTION' ? 
r_bond_other_d               0.001  0.017  ? 4601  'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.517  1.642  ? 6925  'X-RAY DIFFRACTION' ? 
r_angle_other_deg            1.396  1.576  ? 10467 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       7.366  5.000  ? 663   'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       36.106 23.506 ? 251   'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       14.187 15.000 ? 795   'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       16.995 15.000 ? 22    'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.070  0.200  ? 653   'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.008  0.020  ? 5905  'X-RAY DIFFRACTION' ? 
r_gen_planes_other           0.002  0.020  ? 1077  'X-RAY DIFFRACTION' ? 
r_nbd_refined                ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_nbd_other                  ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_nbtor_refined              ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_nbtor_other                ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_refined        ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_other          ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_metal_ion_refined          ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_metal_ion_other            ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_refined       ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_other         ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_refined     ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_other       ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_refined ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_other   ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_mcbond_it                  2.863  3.410  ? 2665  'X-RAY DIFFRACTION' ? 
r_mcbond_other               2.863  3.409  ? 2664  'X-RAY DIFFRACTION' ? 
r_mcangle_it                 4.241  5.082  ? 3265  'X-RAY DIFFRACTION' ? 
r_mcangle_other              4.240  5.083  ? 3266  'X-RAY DIFFRACTION' ? 
r_scbond_it                  3.558  3.729  ? 2557  'X-RAY DIFFRACTION' ? 
r_scbond_other               3.557  3.729  ? 2558  'X-RAY DIFFRACTION' ? 
r_scangle_it                 ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_scangle_other              5.559  5.452  ? 3661  'X-RAY DIFFRACTION' ? 
r_long_range_B_refined       7.129  39.854 ? 5420  'X-RAY DIFFRACTION' ? 
r_long_range_B_other         7.130  39.840 ? 5408  'X-RAY DIFFRACTION' ? 
r_rigid_bond_restr           ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_sphericity_free            ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
r_sphericity_bonded          ?      ?      ? ?     'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.d_res_high                       1.880 
_refine_ls_shell.d_res_low                        1.929 
_refine_ls_shell.number_reflns_R_work             3991 
_refine_ls_shell.R_factor_R_work                  0.344 
_refine_ls_shell.percent_reflns_obs               98.60 
_refine_ls_shell.R_factor_R_free                  0.343 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             151 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
# 
_struct.entry_id                  7I1E 
_struct.title                     
;PanDDA analysis group deposition -- Main Protease (SARS-CoV-2) in complex with fragment G03 from the F2X-Entry Screen in orthorhombic space group
;
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7I1E 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
_struct_keywords.text            'SARS-CoV-2, fragment screen, main protease, VIRAL PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 2 ? 
G N N 5 ? 
H N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    R1AB_SARS2 
_struct_ref.pdbx_db_accession          P0DTD1 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SGFRKMAFPSGKVEGCMVQVTCGTTTLNGLWLDDVVYCPRHVICTSEDMLNPNYEDLLIRKSNHNFLVQAGNVQLRVIGH
SMQNCVLKLKVDTANPKTPKYKFVRIQPGQTFSVLACYNGSPSGVYQCAMRPNFTIKGSFLNGSCGSVGFNIDYDCVSFC
YMHHMELPTGVHAGTDLEGNFYGPFVDRQTAQAAGTDTTITVNVLAWLYAAVINGDRWFLNRFTTTLNDFNLVAMKYNYE
PLTQDHVDILGPLSAQTGIAVLDMCASLKELLQNGMNGRTILGSALLEDEFTPFDVVRQCSGVTFQ
;
_struct_ref.pdbx_align_begin           3264 
# 
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 7I1E A 1 ? 306 ? P0DTD1 3264 ? 3569 ? 1 306 
2 1 7I1E B 1 ? 306 ? P0DTD1 3264 ? 3569 ? 1 306 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
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)' 3240  ? 
1 MORE         -37   ? 
1 'SSA (A^2)'  25750 ? 
# 
_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 
# 
_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 SER A 10  ? GLY A 15  ? SER A 10  GLY A 15  1 ? 6  
HELX_P HELX_P2  AA2 HIS A 41  ? CYS A 44  ? HIS A 41  CYS A 44  5 ? 4  
HELX_P HELX_P3  AA3 SER A 46  ? LEU A 50  ? SER A 46  LEU A 50  5 ? 5  
HELX_P HELX_P4  AA4 ASN A 53  ? ARG A 60  ? ASN A 53  ARG A 60  1 ? 8  
HELX_P HELX_P5  AA5 SER A 62  ? HIS A 64  ? SER A 62  HIS A 64  5 ? 3  
HELX_P HELX_P6  AA6 ILE A 200 ? ASN A 214 ? ILE A 200 ASN A 214 1 ? 15 
HELX_P HELX_P7  AA7 THR A 226 ? LYS A 236 ? THR A 226 LYS A 236 1 ? 11 
HELX_P HELX_P8  AA8 THR A 243 ? LEU A 250 ? THR A 243 LEU A 250 1 ? 8  
HELX_P HELX_P9  AA9 LEU A 250 ? GLY A 258 ? LEU A 250 GLY A 258 1 ? 9  
HELX_P HELX_P10 AB1 ALA A 260 ? GLY A 275 ? ALA A 260 GLY A 275 1 ? 16 
HELX_P HELX_P11 AB2 THR A 292 ? CYS A 300 ? THR A 292 CYS A 300 1 ? 9  
HELX_P HELX_P12 AB3 SER B 10  ? GLY B 15  ? SER B 10  GLY B 15  1 ? 6  
HELX_P HELX_P13 AB4 HIS B 41  ? CYS B 44  ? HIS B 41  CYS B 44  5 ? 4  
HELX_P HELX_P14 AB5 GLU B 47  ? ASN B 51  ? GLU B 47  ASN B 51  5 ? 5  
HELX_P HELX_P15 AB6 ASN B 53  ? ARG B 60  ? ASN B 53  ARG B 60  1 ? 8  
HELX_P HELX_P16 AB7 SER B 62  ? HIS B 64  ? SER B 62  HIS B 64  5 ? 3  
HELX_P HELX_P17 AB8 ILE B 200 ? ASN B 214 ? ILE B 200 ASN B 214 1 ? 15 
HELX_P HELX_P18 AB9 THR B 226 ? TYR B 237 ? THR B 226 TYR B 237 1 ? 12 
HELX_P HELX_P19 AC1 THR B 243 ? LEU B 250 ? THR B 243 LEU B 250 1 ? 8  
HELX_P HELX_P20 AC2 LEU B 250 ? GLY B 258 ? LEU B 250 GLY B 258 1 ? 9  
HELX_P HELX_P21 AC3 ALA B 260 ? GLY B 275 ? ALA B 260 GLY B 275 1 ? 16 
HELX_P HELX_P22 AC4 THR B 292 ? CYS B 300 ? THR B 292 CYS B 300 1 ? 9  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? B ASN 221 O   ? ? ? 1_555 E NA . NA ? ? B ASN 221 B NA 401 1_555 ? ? ? ? ? ? ? 2.653 ? ? 
metalc2 metalc ? ? B ASN 221 OD1 ? ? ? 1_555 E NA . NA ? ? B ASN 221 B NA 401 1_555 ? ? ? ? ? ? ? 2.418 ? ? 
metalc3 metalc ? ? B PHE 223 O   ? ? ? 1_555 E NA . NA ? ? B PHE 223 B NA 401 1_555 ? ? ? ? ? ? ? 2.748 ? ? 
metalc4 metalc ? ? B ASP 263 O   ? ? ? 1_555 E NA . NA ? ? B ASP 263 B NA 401 1_555 ? ? ? ? ? ? ? 2.925 ? ? 
metalc5 metalc ? ? B ASP 263 OD1 ? ? ? 1_555 E NA . NA ? ? B ASP 263 B NA 401 1_555 ? ? ? ? ? ? ? 2.044 ? ? 
# 
_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  O   ? B ASN 221 ? B ASN 221 ? 1_555 NA ? E NA . ? B NA 401 ? 1_555 OD1 ? B ASN 221 ? B ASN 221 ? 1_555 72.5  ? 
2  O   ? B ASN 221 ? B ASN 221 ? 1_555 NA ? E NA . ? B NA 401 ? 1_555 O   ? B PHE 223 ? B PHE 223 ? 1_555 100.7 ? 
3  OD1 ? B ASN 221 ? B ASN 221 ? 1_555 NA ? E NA . ? B NA 401 ? 1_555 O   ? B PHE 223 ? B PHE 223 ? 1_555 92.1  ? 
4  O   ? B ASN 221 ? B ASN 221 ? 1_555 NA ? E NA . ? B NA 401 ? 1_555 O   ? B ASP 263 ? B ASP 263 ? 1_555 168.4 ? 
5  OD1 ? B ASN 221 ? B ASN 221 ? 1_555 NA ? E NA . ? B NA 401 ? 1_555 O   ? B ASP 263 ? B ASP 263 ? 1_555 110.0 ? 
6  O   ? B PHE 223 ? B PHE 223 ? 1_555 NA ? E NA . ? B NA 401 ? 1_555 O   ? B ASP 263 ? B ASP 263 ? 1_555 90.6  ? 
7  O   ? B ASN 221 ? B ASN 221 ? 1_555 NA ? E NA . ? B NA 401 ? 1_555 OD1 ? B ASP 263 ? B ASP 263 ? 1_555 98.1  ? 
8  OD1 ? B ASN 221 ? B ASN 221 ? 1_555 NA ? E NA . ? B NA 401 ? 1_555 OD1 ? B ASP 263 ? B ASP 263 ? 1_555 168.1 ? 
9  O   ? B PHE 223 ? B PHE 223 ? 1_555 NA ? E NA . ? B NA 401 ? 1_555 OD1 ? B ASP 263 ? B ASP 263 ? 1_555 82.3  ? 
10 O   ? B ASP 263 ? B ASP 263 ? 1_555 NA ? E NA . ? B NA 401 ? 1_555 OD1 ? B ASP 263 ? B ASP 263 ? 1_555 80.7  ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 7 ? 
AA2 ? 5 ? 
AA3 ? 3 ? 
AA4 ? 7 ? 
AA5 ? 5 ? 
AA6 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA3 1 2 ? parallel      
AA3 2 3 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA4 5 6 ? anti-parallel 
AA4 6 7 ? anti-parallel 
AA5 1 2 ? parallel      
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA5 4 5 ? anti-parallel 
AA6 1 2 ? parallel      
AA6 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 VAL A 73  ? LEU A 75  ? VAL A 73  LEU A 75  
AA1 2 PHE A 66  ? ALA A 70  ? PHE A 66  ALA A 70  
AA1 3 MET A 17  ? CYS A 22  ? MET A 17  CYS A 22  
AA1 4 THR A 25  ? LEU A 32  ? THR A 25  LEU A 32  
AA1 5 VAL A 35  ? PRO A 39  ? VAL A 35  PRO A 39  
AA1 6 VAL A 86  ? VAL A 91  ? VAL A 86  VAL A 91  
AA1 7 VAL A 77  ? GLN A 83  ? VAL A 77  GLN A 83  
AA2 1 TYR A 101 ? PHE A 103 ? TYR A 101 PHE A 103 
AA2 2 VAL A 157 ? GLU A 166 ? VAL A 157 GLU A 166 
AA2 3 VAL A 148 ? ASN A 151 ? VAL A 148 ASN A 151 
AA2 4 THR A 111 ? TYR A 118 ? THR A 111 TYR A 118 
AA2 5 SER A 121 ? ALA A 129 ? SER A 121 ALA A 129 
AA3 1 TYR A 101 ? PHE A 103 ? TYR A 101 PHE A 103 
AA3 2 VAL A 157 ? GLU A 166 ? VAL A 157 GLU A 166 
AA3 3 HIS A 172 ? THR A 175 ? HIS A 172 THR A 175 
AA4 1 VAL B 73  ? LEU B 75  ? VAL B 73  LEU B 75  
AA4 2 PHE B 66  ? ALA B 70  ? PHE B 66  ALA B 70  
AA4 3 MET B 17  ? CYS B 22  ? MET B 17  CYS B 22  
AA4 4 THR B 25  ? LEU B 32  ? THR B 25  LEU B 32  
AA4 5 VAL B 35  ? PRO B 39  ? VAL B 35  PRO B 39  
AA4 6 VAL B 86  ? VAL B 91  ? VAL B 86  VAL B 91  
AA4 7 VAL B 77  ? GLN B 83  ? VAL B 77  GLN B 83  
AA5 1 TYR B 101 ? PHE B 103 ? TYR B 101 PHE B 103 
AA5 2 CYS B 156 ? GLU B 166 ? CYS B 156 GLU B 166 
AA5 3 VAL B 148 ? ASP B 153 ? VAL B 148 ASP B 153 
AA5 4 THR B 111 ? TYR B 118 ? THR B 111 TYR B 118 
AA5 5 SER B 121 ? ALA B 129 ? SER B 121 ALA B 129 
AA6 1 TYR B 101 ? PHE B 103 ? TYR B 101 PHE B 103 
AA6 2 CYS B 156 ? GLU B 166 ? CYS B 156 GLU B 166 
AA6 3 HIS B 172 ? THR B 175 ? HIS B 172 THR B 175 
# 
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 LEU A 75  ? O LEU A 75  N VAL A 68  ? N VAL A 68  
AA1 2 3 O LEU A 67  ? O LEU A 67  N THR A 21  ? N THR A 21  
AA1 3 4 N VAL A 20  ? N VAL A 20  O LEU A 27  ? O LEU A 27  
AA1 4 5 N LEU A 30  ? N LEU A 30  O TYR A 37  ? O TYR A 37  
AA1 5 6 N CYS A 38  ? N CYS A 38  O LEU A 87  ? O LEU A 87  
AA1 6 7 O VAL A 86  ? O VAL A 86  N GLN A 83  ? N GLN A 83  
AA2 1 2 N LYS A 102 ? N LYS A 102 O PHE A 159 ? O PHE A 159 
AA2 2 3 O SER A 158 ? O SER A 158 N ASN A 151 ? N ASN A 151 
AA2 3 4 O PHE A 150 ? O PHE A 150 N SER A 113 ? N SER A 113 
AA2 4 5 N ALA A 116 ? N ALA A 116 O SER A 123 ? O SER A 123 
AA3 1 2 N LYS A 102 ? N LYS A 102 O PHE A 159 ? O PHE A 159 
AA3 2 3 N MET A 165 ? N MET A 165 O ALA A 173 ? O ALA A 173 
AA4 1 2 O LEU B 75  ? O LEU B 75  N VAL B 68  ? N VAL B 68  
AA4 2 3 O LEU B 67  ? O LEU B 67  N THR B 21  ? N THR B 21  
AA4 3 4 N VAL B 20  ? N VAL B 20  O LEU B 27  ? O LEU B 27  
AA4 4 5 N LEU B 30  ? N LEU B 30  O TYR B 37  ? O TYR B 37  
AA4 5 6 N VAL B 36  ? N VAL B 36  O LEU B 89  ? O LEU B 89  
AA4 6 7 O LYS B 88  ? O LYS B 88  N SER B 81  ? N SER B 81  
AA5 1 2 N LYS B 102 ? N LYS B 102 O PHE B 159 ? O PHE B 159 
AA5 2 3 O SER B 158 ? O SER B 158 N ASN B 151 ? N ASN B 151 
AA5 3 4 O PHE B 150 ? O PHE B 150 N SER B 113 ? N SER B 113 
AA5 4 5 N ALA B 116 ? N ALA B 116 O SER B 123 ? O SER B 123 
AA6 1 2 N LYS B 102 ? N LYS B 102 O PHE B 159 ? O PHE B 159 
AA6 2 3 N MET B 165 ? N MET B 165 O ALA B 173 ? O ALA B 173 
# 
_pdbx_entry_details.entry_id                   7I1E 
_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 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   OG 
_pdbx_validate_close_contact.auth_asym_id_1   B 
_pdbx_validate_close_contact.auth_comp_id_1   SER 
_pdbx_validate_close_contact.auth_seq_id_1    62 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   NE2 
_pdbx_validate_close_contact.auth_asym_id_2   B 
_pdbx_validate_close_contact.auth_comp_id_2   HIS 
_pdbx_validate_close_contact.auth_seq_id_2    64 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.11 
# 
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 LYS A 5   ? ? -55.89  97.84   
2  1 ASP A 33  ? ? 53.04   -121.41 
3  1 ASN A 51  ? ? -140.35 58.97   
4  1 ASN A 84  ? ? 58.65   -121.26 
5  1 ASP A 155 ? ? 69.67   -8.70   
6  1 ASP B 33  ? ? 50.28   -126.74 
7  1 ASN B 51  ? ? -163.14 70.76   
8  1 ASN B 84  ? ? 53.52   -125.25 
9  1 TYR B 154 ? ? 64.96   -105.68 
10 1 GLN B 189 ? ? -65.51  99.80   
11 1 ALA B 255 ? A -47.51  -72.26  
12 1 ALA B 255 ? B -47.51  -72.26  
# 
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 SER 301 ? A SER 301 
2 1 Y 1 A GLY 302 ? A GLY 302 
3 1 Y 1 A VAL 303 ? A VAL 303 
4 1 Y 1 A THR 304 ? A THR 304 
5 1 Y 1 A PHE 305 ? A PHE 305 
6 1 Y 1 A GLN 306 ? A GLN 306 
7 1 Y 1 B GLN 306 ? B GLN 306 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CL  CL   CL N N 74  
CYS N    N  N N 75  
CYS CA   C  N R 76  
CYS C    C  N N 77  
CYS O    O  N N 78  
CYS CB   C  N N 79  
CYS SG   S  N N 80  
CYS OXT  O  N N 81  
CYS H    H  N N 82  
CYS H2   H  N N 83  
CYS HA   H  N N 84  
CYS HB2  H  N N 85  
CYS HB3  H  N N 86  
CYS HG   H  N N 87  
CYS HXT  H  N N 88  
GLN N    N  N N 89  
GLN CA   C  N S 90  
GLN C    C  N N 91  
GLN O    O  N N 92  
GLN CB   C  N N 93  
GLN CG   C  N N 94  
GLN CD   C  N N 95  
GLN OE1  O  N N 96  
GLN NE2  N  N N 97  
GLN OXT  O  N N 98  
GLN H    H  N N 99  
GLN H2   H  N N 100 
GLN HA   H  N N 101 
GLN HB2  H  N N 102 
GLN HB3  H  N N 103 
GLN HG2  H  N N 104 
GLN HG3  H  N N 105 
GLN HE21 H  N N 106 
GLN HE22 H  N N 107 
GLN HXT  H  N N 108 
GLU N    N  N N 109 
GLU CA   C  N S 110 
GLU C    C  N N 111 
GLU O    O  N N 112 
GLU CB   C  N N 113 
GLU CG   C  N N 114 
GLU CD   C  N N 115 
GLU OE1  O  N N 116 
GLU OE2  O  N N 117 
GLU OXT  O  N N 118 
GLU H    H  N N 119 
GLU H2   H  N N 120 
GLU HA   H  N N 121 
GLU HB2  H  N N 122 
GLU HB3  H  N N 123 
GLU HG2  H  N N 124 
GLU HG3  H  N N 125 
GLU HE2  H  N N 126 
GLU HXT  H  N N 127 
GLY N    N  N N 128 
GLY CA   C  N N 129 
GLY C    C  N N 130 
GLY O    O  N N 131 
GLY OXT  O  N N 132 
GLY H    H  N N 133 
GLY H2   H  N N 134 
GLY HA2  H  N N 135 
GLY HA3  H  N N 136 
GLY HXT  H  N N 137 
HIS N    N  N N 138 
HIS CA   C  N S 139 
HIS C    C  N N 140 
HIS O    O  N N 141 
HIS CB   C  N N 142 
HIS CG   C  Y N 143 
HIS ND1  N  Y N 144 
HIS CD2  C  Y N 145 
HIS CE1  C  Y N 146 
HIS NE2  N  Y N 147 
HIS OXT  O  N N 148 
HIS H    H  N N 149 
HIS H2   H  N N 150 
HIS HA   H  N N 151 
HIS HB2  H  N N 152 
HIS HB3  H  N N 153 
HIS HD1  H  N N 154 
HIS HD2  H  N N 155 
HIS HE1  H  N N 156 
HIS HE2  H  N N 157 
HIS HXT  H  N N 158 
HOH O    O  N N 159 
HOH H1   H  N N 160 
HOH H2   H  N N 161 
ILE N    N  N N 162 
ILE CA   C  N S 163 
ILE C    C  N N 164 
ILE O    O  N N 165 
ILE CB   C  N S 166 
ILE CG1  C  N N 167 
ILE CG2  C  N N 168 
ILE CD1  C  N N 169 
ILE OXT  O  N N 170 
ILE H    H  N N 171 
ILE H2   H  N N 172 
ILE HA   H  N N 173 
ILE HB   H  N N 174 
ILE HG12 H  N N 175 
ILE HG13 H  N N 176 
ILE HG21 H  N N 177 
ILE HG22 H  N N 178 
ILE HG23 H  N N 179 
ILE HD11 H  N N 180 
ILE HD12 H  N N 181 
ILE HD13 H  N N 182 
ILE HXT  H  N N 183 
LEU N    N  N N 184 
LEU CA   C  N S 185 
LEU C    C  N N 186 
LEU O    O  N N 187 
LEU CB   C  N N 188 
LEU CG   C  N N 189 
LEU CD1  C  N N 190 
LEU CD2  C  N N 191 
LEU OXT  O  N N 192 
LEU H    H  N N 193 
LEU H2   H  N N 194 
LEU HA   H  N N 195 
LEU HB2  H  N N 196 
LEU HB3  H  N N 197 
LEU HG   H  N N 198 
LEU HD11 H  N N 199 
LEU HD12 H  N N 200 
LEU HD13 H  N N 201 
LEU HD21 H  N N 202 
LEU HD22 H  N N 203 
LEU HD23 H  N N 204 
LEU HXT  H  N N 205 
LYS N    N  N N 206 
LYS CA   C  N S 207 
LYS C    C  N N 208 
LYS O    O  N N 209 
LYS CB   C  N N 210 
LYS CG   C  N N 211 
LYS CD   C  N N 212 
LYS CE   C  N N 213 
LYS NZ   N  N N 214 
LYS OXT  O  N N 215 
LYS H    H  N N 216 
LYS H2   H  N N 217 
LYS HA   H  N N 218 
LYS HB2  H  N N 219 
LYS HB3  H  N N 220 
LYS HG2  H  N N 221 
LYS HG3  H  N N 222 
LYS HD2  H  N N 223 
LYS HD3  H  N N 224 
LYS HE2  H  N N 225 
LYS HE3  H  N N 226 
LYS HZ1  H  N N 227 
LYS HZ2  H  N N 228 
LYS HZ3  H  N N 229 
LYS HXT  H  N N 230 
MET N    N  N N 231 
MET CA   C  N S 232 
MET C    C  N N 233 
MET O    O  N N 234 
MET CB   C  N N 235 
MET CG   C  N N 236 
MET SD   S  N N 237 
MET CE   C  N N 238 
MET OXT  O  N N 239 
MET H    H  N N 240 
MET H2   H  N N 241 
MET HA   H  N N 242 
MET HB2  H  N N 243 
MET HB3  H  N N 244 
MET HG2  H  N N 245 
MET HG3  H  N N 246 
MET HE1  H  N N 247 
MET HE2  H  N N 248 
MET HE3  H  N N 249 
MET HXT  H  N N 250 
NA  NA   NA N N 251 
PHE N    N  N N 252 
PHE CA   C  N S 253 
PHE C    C  N N 254 
PHE O    O  N N 255 
PHE CB   C  N N 256 
PHE CG   C  Y N 257 
PHE CD1  C  Y N 258 
PHE CD2  C  Y N 259 
PHE CE1  C  Y N 260 
PHE CE2  C  Y N 261 
PHE CZ   C  Y N 262 
PHE OXT  O  N N 263 
PHE H    H  N N 264 
PHE H2   H  N N 265 
PHE HA   H  N N 266 
PHE HB2  H  N N 267 
PHE HB3  H  N N 268 
PHE HD1  H  N N 269 
PHE HD2  H  N N 270 
PHE HE1  H  N N 271 
PHE HE2  H  N N 272 
PHE HZ   H  N N 273 
PHE HXT  H  N N 274 
PRO N    N  N N 275 
PRO CA   C  N S 276 
PRO C    C  N N 277 
PRO O    O  N N 278 
PRO CB   C  N N 279 
PRO CG   C  N N 280 
PRO CD   C  N N 281 
PRO OXT  O  N N 282 
PRO H    H  N N 283 
PRO HA   H  N N 284 
PRO HB2  H  N N 285 
PRO HB3  H  N N 286 
PRO HG2  H  N N 287 
PRO HG3  H  N N 288 
PRO HD2  H  N N 289 
PRO HD3  H  N N 290 
PRO HXT  H  N N 291 
RD4 C4   C  Y N 292 
RD4 C5   C  Y N 293 
RD4 C6   C  Y N 294 
RD4 N1   N  N N 295 
RD4 C7   C  N N 296 
RD4 C8   C  N N 297 
RD4 C    C  N N 298 
RD4 N    N  N N 299 
RD4 C1   C  Y N 300 
RD4 O    O  N N 301 
RD4 C3   C  Y N 302 
RD4 C2   C  Y N 303 
RD4 H1   H  N N 304 
RD4 H2   H  N N 305 
RD4 H3   H  N N 306 
RD4 H4   H  N N 307 
RD4 H5   H  N N 308 
RD4 H6   H  N N 309 
RD4 H7   H  N N 310 
RD4 H8   H  N N 311 
RD4 H9   H  N N 312 
RD4 H10  H  N N 313 
RD4 H11  H  N N 314 
RD4 H12  H  N N 315 
SER N    N  N N 316 
SER CA   C  N S 317 
SER C    C  N N 318 
SER O    O  N N 319 
SER CB   C  N N 320 
SER OG   O  N N 321 
SER OXT  O  N N 322 
SER H    H  N N 323 
SER H2   H  N N 324 
SER HA   H  N N 325 
SER HB2  H  N N 326 
SER HB3  H  N N 327 
SER HG   H  N N 328 
SER HXT  H  N N 329 
THR N    N  N N 330 
THR CA   C  N S 331 
THR C    C  N N 332 
THR O    O  N N 333 
THR CB   C  N R 334 
THR OG1  O  N N 335 
THR CG2  C  N N 336 
THR OXT  O  N N 337 
THR H    H  N N 338 
THR H2   H  N N 339 
THR HA   H  N N 340 
THR HB   H  N N 341 
THR HG1  H  N N 342 
THR HG21 H  N N 343 
THR HG22 H  N N 344 
THR HG23 H  N N 345 
THR HXT  H  N N 346 
TRP N    N  N N 347 
TRP CA   C  N S 348 
TRP C    C  N N 349 
TRP O    O  N N 350 
TRP CB   C  N N 351 
TRP CG   C  Y N 352 
TRP CD1  C  Y N 353 
TRP CD2  C  Y N 354 
TRP NE1  N  Y N 355 
TRP CE2  C  Y N 356 
TRP CE3  C  Y N 357 
TRP CZ2  C  Y N 358 
TRP CZ3  C  Y N 359 
TRP CH2  C  Y N 360 
TRP OXT  O  N N 361 
TRP H    H  N N 362 
TRP H2   H  N N 363 
TRP HA   H  N N 364 
TRP HB2  H  N N 365 
TRP HB3  H  N N 366 
TRP HD1  H  N N 367 
TRP HE1  H  N N 368 
TRP HE3  H  N N 369 
TRP HZ2  H  N N 370 
TRP HZ3  H  N N 371 
TRP HH2  H  N N 372 
TRP HXT  H  N N 373 
TYR N    N  N N 374 
TYR CA   C  N S 375 
TYR C    C  N N 376 
TYR O    O  N N 377 
TYR CB   C  N N 378 
TYR CG   C  Y N 379 
TYR CD1  C  Y N 380 
TYR CD2  C  Y N 381 
TYR CE1  C  Y N 382 
TYR CE2  C  Y N 383 
TYR CZ   C  Y N 384 
TYR OH   O  N N 385 
TYR OXT  O  N N 386 
TYR H    H  N N 387 
TYR H2   H  N N 388 
TYR HA   H  N N 389 
TYR HB2  H  N N 390 
TYR HB3  H  N N 391 
TYR HD1  H  N N 392 
TYR HD2  H  N N 393 
TYR HE1  H  N N 394 
TYR HE2  H  N N 395 
TYR HH   H  N N 396 
TYR HXT  H  N N 397 
VAL N    N  N N 398 
VAL CA   C  N S 399 
VAL C    C  N N 400 
VAL O    O  N N 401 
VAL CB   C  N N 402 
VAL CG1  C  N N 403 
VAL CG2  C  N N 404 
VAL OXT  O  N N 405 
VAL H    H  N N 406 
VAL H2   H  N N 407 
VAL HA   H  N N 408 
VAL HB   H  N N 409 
VAL HG11 H  N N 410 
VAL HG12 H  N N 411 
VAL HG13 H  N N 412 
VAL HG21 H  N N 413 
VAL HG22 H  N N 414 
VAL HG23 H  N N 415 
VAL HXT  H  N N 416 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
PHE N   CA   sing N N 237 
PHE N   H    sing N N 238 
PHE N   H2   sing N N 239 
PHE CA  C    sing N N 240 
PHE CA  CB   sing N N 241 
PHE CA  HA   sing N N 242 
PHE C   O    doub N N 243 
PHE C   OXT  sing N N 244 
PHE CB  CG   sing N N 245 
PHE CB  HB2  sing N N 246 
PHE CB  HB3  sing N N 247 
PHE CG  CD1  doub Y N 248 
PHE CG  CD2  sing Y N 249 
PHE CD1 CE1  sing Y N 250 
PHE CD1 HD1  sing N N 251 
PHE CD2 CE2  doub Y N 252 
PHE CD2 HD2  sing N N 253 
PHE CE1 CZ   doub Y N 254 
PHE CE1 HE1  sing N N 255 
PHE CE2 CZ   sing Y N 256 
PHE CE2 HE2  sing N N 257 
PHE CZ  HZ   sing N N 258 
PHE OXT HXT  sing N N 259 
PRO N   CA   sing N N 260 
PRO N   CD   sing N N 261 
PRO N   H    sing N N 262 
PRO CA  C    sing N N 263 
PRO CA  CB   sing N N 264 
PRO CA  HA   sing N N 265 
PRO C   O    doub N N 266 
PRO C   OXT  sing N N 267 
PRO CB  CG   sing N N 268 
PRO CB  HB2  sing N N 269 
PRO CB  HB3  sing N N 270 
PRO CG  CD   sing N N 271 
PRO CG  HG2  sing N N 272 
PRO CG  HG3  sing N N 273 
PRO CD  HD2  sing N N 274 
PRO CD  HD3  sing N N 275 
PRO OXT HXT  sing N N 276 
RD4 N1  C    doub N N 277 
RD4 C3  C2   doub Y N 278 
RD4 C3  C4   sing Y N 279 
RD4 C2  C1   sing Y N 280 
RD4 C4  C5   doub Y N 281 
RD4 C1  C    sing N N 282 
RD4 C1  C6   doub Y N 283 
RD4 C   N    sing N N 284 
RD4 C5  C6   sing Y N 285 
RD4 C5  O    sing N N 286 
RD4 O   C7   sing N N 287 
RD4 C7  C8   sing N N 288 
RD4 C4  H1   sing N N 289 
RD4 C6  H2   sing N N 290 
RD4 N1  H3   sing N N 291 
RD4 C7  H4   sing N N 292 
RD4 C7  H5   sing N N 293 
RD4 C8  H6   sing N N 294 
RD4 C8  H7   sing N N 295 
RD4 C8  H8   sing N N 296 
RD4 N   H9   sing N N 297 
RD4 N   H10  sing N N 298 
RD4 C3  H11  sing N N 299 
RD4 C2  H12  sing N N 300 
SER N   CA   sing N N 301 
SER N   H    sing N N 302 
SER N   H2   sing N N 303 
SER CA  C    sing N N 304 
SER CA  CB   sing N N 305 
SER CA  HA   sing N N 306 
SER C   O    doub N N 307 
SER C   OXT  sing N N 308 
SER CB  OG   sing N N 309 
SER CB  HB2  sing N N 310 
SER CB  HB3  sing N N 311 
SER OG  HG   sing N N 312 
SER OXT HXT  sing N N 313 
THR N   CA   sing N N 314 
THR N   H    sing N N 315 
THR N   H2   sing N N 316 
THR CA  C    sing N N 317 
THR CA  CB   sing N N 318 
THR CA  HA   sing N N 319 
THR C   O    doub N N 320 
THR C   OXT  sing N N 321 
THR CB  OG1  sing N N 322 
THR CB  CG2  sing N N 323 
THR CB  HB   sing N N 324 
THR OG1 HG1  sing N N 325 
THR CG2 HG21 sing N N 326 
THR CG2 HG22 sing N N 327 
THR CG2 HG23 sing N N 328 
THR OXT HXT  sing N N 329 
TRP N   CA   sing N N 330 
TRP N   H    sing N N 331 
TRP N   H2   sing N N 332 
TRP CA  C    sing N N 333 
TRP CA  CB   sing N N 334 
TRP CA  HA   sing N N 335 
TRP C   O    doub N N 336 
TRP C   OXT  sing N N 337 
TRP CB  CG   sing N N 338 
TRP CB  HB2  sing N N 339 
TRP CB  HB3  sing N N 340 
TRP CG  CD1  doub Y N 341 
TRP CG  CD2  sing Y N 342 
TRP CD1 NE1  sing Y N 343 
TRP CD1 HD1  sing N N 344 
TRP CD2 CE2  doub Y N 345 
TRP CD2 CE3  sing Y N 346 
TRP NE1 CE2  sing Y N 347 
TRP NE1 HE1  sing N N 348 
TRP CE2 CZ2  sing Y N 349 
TRP CE3 CZ3  doub Y N 350 
TRP CE3 HE3  sing N N 351 
TRP CZ2 CH2  doub Y N 352 
TRP CZ2 HZ2  sing N N 353 
TRP CZ3 CH2  sing Y N 354 
TRP CZ3 HZ3  sing N N 355 
TRP CH2 HH2  sing N N 356 
TRP OXT HXT  sing N N 357 
TYR N   CA   sing N N 358 
TYR N   H    sing N N 359 
TYR N   H2   sing N N 360 
TYR CA  C    sing N N 361 
TYR CA  CB   sing N N 362 
TYR CA  HA   sing N N 363 
TYR C   O    doub N N 364 
TYR C   OXT  sing N N 365 
TYR CB  CG   sing N N 366 
TYR CB  HB2  sing N N 367 
TYR CB  HB3  sing N N 368 
TYR CG  CD1  doub Y N 369 
TYR CG  CD2  sing Y N 370 
TYR CD1 CE1  sing Y N 371 
TYR CD1 HD1  sing N N 372 
TYR CD2 CE2  doub Y N 373 
TYR CD2 HD2  sing N N 374 
TYR CE1 CZ   doub Y N 375 
TYR CE1 HE1  sing N N 376 
TYR CE2 CZ   sing Y N 377 
TYR CE2 HE2  sing N N 378 
TYR CZ  OH   sing N N 379 
TYR OH  HH   sing N N 380 
TYR OXT HXT  sing N N 381 
VAL N   CA   sing N N 382 
VAL N   H    sing N N 383 
VAL N   H2   sing N N 384 
VAL CA  C    sing N N 385 
VAL CA  CB   sing N N 386 
VAL CA  HA   sing N N 387 
VAL C   O    doub N N 388 
VAL C   OXT  sing N N 389 
VAL CB  CG1  sing N N 390 
VAL CB  CG2  sing N N 391 
VAL CB  HB   sing N N 392 
VAL CG1 HG11 sing N N 393 
VAL CG1 HG12 sing N N 394 
VAL CG1 HG13 sing N N 395 
VAL CG2 HG21 sing N N 396 
VAL CG2 HG22 sing N N 397 
VAL CG2 HG23 sing N N 398 
VAL OXT HXT  sing N N 399 
# 
_pdbx_audit_support.ordinal                1 
_pdbx_audit_support.funding_organization   'European Commission' 
_pdbx_audit_support.country                'European Union' 
_pdbx_audit_support.grant_number           871037 
# 
_pdbx_deposit_group.group_id            G_1002335 
_pdbx_deposit_group.group_description   
;Main Protease (SARS-CoV-2) complexed with fragments of the F2X-Entry Screen in the orthorhombic space group. PanDDA analysis of F2X-Entry Screen vs. the main protease of SARS-CoV-2, including auto-refined models with ligands placed according to PanDDA-map. The event maps are included in the mmcif and are the determining evidence for the ligands. 2Fo-Fc and Fo-Fc maps will be mostly not useful to consider here.
;
_pdbx_deposit_group.group_title         
;PanDDA analysis group deposition -- Main Protease (SARS-CoV-2) in complex with fragments from the F2X-Entry Screen in orthorhombic space group
;
_pdbx_deposit_group.group_type          'changed state' 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.accession_code   7BB2 
_pdbx_initial_refinement_model.source_name      PDB 
# 
_atom_sites.entry_id                    7I1E 
_atom_sites.fract_transf_matrix[1][1]   0.014723 
_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]   0.010041 
_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]   0.009646 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
CL 
N  
NA 
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . SER A 1 1   ? -13.690 -9.746  -12.515 1.00 42.36  ? 1   SER A N   1 
ATOM   2    C  CA  . SER A 1 1   ? -13.778 -9.022  -13.798 1.00 43.52  ? 1   SER A CA  1 
ATOM   3    C  C   . SER A 1 1   ? -12.759 -7.869  -13.803 1.00 44.21  ? 1   SER A C   1 
ATOM   4    O  O   . SER A 1 1   ? -11.871 -7.831  -12.907 1.00 42.00  ? 1   SER A O   1 
ATOM   5    C  CB  . SER A 1 1   ? -15.209 -8.557  -14.063 1.00 48.92  ? 1   SER A CB  1 
ATOM   6    O  OG  . SER A 1 1   ? -15.507 -7.350  -13.374 1.00 52.03  ? 1   SER A OG  1 
ATOM   7    N  N   . GLY A 1 2   ? -12.885 -6.953  -14.767 1.00 40.12  ? 2   GLY A N   1 
ATOM   8    C  CA  . GLY A 1 2   ? -11.916 -5.874  -15.009 1.00 39.21  ? 2   GLY A CA  1 
ATOM   9    C  C   . GLY A 1 2   ? -10.961 -6.328  -16.080 1.00 36.48  ? 2   GLY A C   1 
ATOM   10   O  O   . GLY A 1 2   ? -10.875 -7.532  -16.341 1.00 36.49  ? 2   GLY A O   1 
ATOM   11   N  N   . PHE A 1 3   ? -10.305 -5.388  -16.738 1.00 35.87  ? 3   PHE A N   1 
ATOM   12   C  CA  . PHE A 1 3   ? -9.366  -5.712  -17.828 1.00 34.68  ? 3   PHE A CA  1 
ATOM   13   C  C   . PHE A 1 3   ? -8.297  -4.627  -17.894 1.00 34.68  ? 3   PHE A C   1 
ATOM   14   O  O   . PHE A 1 3   ? -8.623  -3.470  -18.168 1.00 40.25  ? 3   PHE A O   1 
ATOM   15   C  CB  . PHE A 1 3   ? -10.118 -5.915  -19.147 1.00 39.46  ? 3   PHE A CB  1 
ATOM   16   C  CG  . PHE A 1 3   ? -9.372  -6.826  -20.081 1.00 36.64  ? 3   PHE A CG  1 
ATOM   17   C  CD1 . PHE A 1 3   ? -9.388  -8.196  -19.885 1.00 37.61  ? 3   PHE A CD1 1 
ATOM   18   C  CD2 . PHE A 1 3   ? -8.569  -6.305  -21.084 1.00 38.56  ? 3   PHE A CD2 1 
ATOM   19   C  CE1 . PHE A 1 3   ? -8.662  -9.035  -20.722 1.00 39.28  ? 3   PHE A CE1 1 
ATOM   20   C  CE2 . PHE A 1 3   ? -7.841  -7.138  -21.919 1.00 37.63  ? 3   PHE A CE2 1 
ATOM   21   C  CZ  . PHE A 1 3   ? -7.880  -8.502  -21.731 1.00 39.88  ? 3   PHE A CZ  1 
ATOM   22   N  N   . ARG A 1 4   ? -7.055  -5.036  -17.664 1.00 30.12  ? 4   ARG A N   1 
ATOM   23   C  CA  . ARG A 1 4   ? -5.874  -4.165  -17.484 1.00 30.64  ? 4   ARG A CA  1 
ATOM   24   C  C   . ARG A 1 4   ? -4.731  -4.694  -18.342 1.00 28.90  ? 4   ARG A C   1 
ATOM   25   O  O   . ARG A 1 4   ? -4.548  -5.944  -18.417 1.00 26.32  ? 4   ARG A O   1 
ATOM   26   C  CB  . ARG A 1 4   ? -5.424  -4.195  -16.018 1.00 33.05  ? 4   ARG A CB  1 
ATOM   27   C  CG  . ARG A 1 4   ? -6.263  -3.336  -15.075 1.00 36.20  ? 4   ARG A CG  1 
ATOM   28   C  CD  . ARG A 1 4   ? -5.755  -1.898  -15.109 1.00 39.53  ? 4   ARG A CD  1 
ATOM   29   N  NE  . ARG A 1 4   ? -6.340  -1.045  -14.084 1.00 46.37  ? 4   ARG A NE  1 
ATOM   30   C  CZ  . ARG A 1 4   ? -6.178  0.277   -14.046 1.00 52.60  ? 4   ARG A CZ  1 
ATOM   31   N  NH1 . ARG A 1 4   ? -5.395  0.854   -14.943 1.00 58.73  ? 4   ARG A NH1 1 
ATOM   32   N  NH2 . ARG A 1 4   ? -6.790  1.023   -13.132 1.00 44.82  ? 4   ARG A NH2 1 
ATOM   33   N  N   . LYS A 1 5   ? -3.942  -3.772  -18.883 1.00 31.14  ? 5   LYS A N   1 
ATOM   34   C  CA  . LYS A 1 5   ? -2.552  -4.023  -19.339 1.00 34.80  ? 5   LYS A CA  1 
ATOM   35   C  C   . LYS A 1 5   ? -1.727  -4.594  -18.188 1.00 32.14  ? 5   LYS A C   1 
ATOM   36   O  O   . LYS A 1 5   ? -1.230  -3.825  -17.367 1.00 34.84  ? 5   LYS A O   1 
ATOM   37   C  CB  . LYS A 1 5   ? -1.864  -2.730  -19.769 1.00 37.07  ? 5   LYS A CB  1 
ATOM   38   C  CG  . LYS A 1 5   ? -2.189  -2.309  -21.173 1.00 44.09  ? 5   LYS A CG  1 
ATOM   39   C  CD  . LYS A 1 5   ? -1.431  -3.063  -22.217 1.00 45.25  ? 5   LYS A CD  1 
ATOM   40   C  CE  . LYS A 1 5   ? -1.892  -2.669  -23.610 1.00 50.36  ? 5   LYS A CE  1 
ATOM   41   N  NZ  . LYS A 1 5   ? -1.930  -1.197  -23.811 1.00 52.77  ? 5   LYS A NZ  1 
ATOM   42   N  N   . MET A 1 6   ? -1.571  -5.899  -18.146 1.00 30.77  ? 6   MET A N   1 
ATOM   43   C  CA  . MET A 1 6   ? -0.954  -6.598  -16.995 1.00 29.71  ? 6   MET A CA  1 
ATOM   44   C  C   . MET A 1 6   ? 0.414   -7.116  -17.445 1.00 27.73  ? 6   MET A C   1 
ATOM   45   O  O   . MET A 1 6   ? 0.485   -7.816  -18.489 1.00 26.33  ? 6   MET A O   1 
ATOM   46   C  CB  . MET A 1 6   ? -1.877  -7.751  -16.616 1.00 31.12  ? 6   MET A CB  1 
ATOM   47   C  CG  . MET A 1 6   ? -1.573  -8.419  -15.311 1.00 37.16  ? 6   MET A CG  1 
ATOM   48   S  SD  . MET A 1 6   ? -2.838  -9.684  -14.992 1.00 42.53  ? 6   MET A SD  1 
ATOM   49   C  CE  . MET A 1 6   ? -4.266  -8.658  -14.661 1.00 39.70  ? 6   MET A CE  1 
ATOM   50   N  N   . ALA A 1 7   ? 1.456   -6.813  -16.684 1.00 25.25  ? 7   ALA A N   1 
ATOM   51   C  CA  . ALA A 1 7   ? 2.811   -7.352  -16.925 1.00 25.34  ? 7   ALA A CA  1 
ATOM   52   C  C   . ALA A 1 7   ? 2.996   -8.636  -16.112 1.00 25.83  ? 7   ALA A C   1 
ATOM   53   O  O   . ALA A 1 7   ? 2.263   -8.851  -15.130 1.00 21.66  ? 7   ALA A O   1 
ATOM   54   C  CB  . ALA A 1 7   ? 3.856   -6.338  -16.557 1.00 25.74  ? 7   ALA A CB  1 
ATOM   55   N  N   . PHE A 1 8   ? 4.000   -9.430  -16.460 1.00 23.00  ? 8   PHE A N   1 
ATOM   56   C  CA  . PHE A 1 8   ? 4.416   -10.584 -15.628 1.00 24.13  ? 8   PHE A CA  1 
ATOM   57   C  C   . PHE A 1 8   ? 5.092   -10.072 -14.368 1.00 22.25  ? 8   PHE A C   1 
ATOM   58   O  O   . PHE A 1 8   ? 5.743   -9.032  -14.389 1.00 22.39  ? 8   PHE A O   1 
ATOM   59   C  CB  . PHE A 1 8   ? 5.289   -11.553 -16.420 1.00 24.47  ? 8   PHE A CB  1 
ATOM   60   C  CG  . PHE A 1 8   ? 4.464   -12.393 -17.359 1.00 25.56  ? 8   PHE A CG  1 
ATOM   61   C  CD1 . PHE A 1 8   ? 3.725   -13.469 -16.885 1.00 27.62  ? 8   PHE A CD1 1 
ATOM   62   C  CD2 . PHE A 1 8   ? 4.394   -12.084 -18.704 1.00 25.71  ? 8   PHE A CD2 1 
ATOM   63   C  CE1 . PHE A 1 8   ? 2.951   -14.242 -17.749 1.00 31.33  ? 8   PHE A CE1 1 
ATOM   64   C  CE2 . PHE A 1 8   ? 3.628   -12.856 -19.568 1.00 26.61  ? 8   PHE A CE2 1 
ATOM   65   C  CZ  . PHE A 1 8   ? 2.908   -13.936 -19.091 1.00 28.78  ? 8   PHE A CZ  1 
ATOM   66   N  N   . PRO A 1 9   ? 4.959   -10.795 -13.228 1.00 21.32  ? 9   PRO A N   1 
ATOM   67   C  CA  . PRO A 1 9   ? 5.750   -10.480 -12.045 1.00 22.57  ? 9   PRO A CA  1 
ATOM   68   C  C   . PRO A 1 9   ? 7.242   -10.499 -12.447 1.00 24.25  ? 9   PRO A C   1 
ATOM   69   O  O   . PRO A 1 9   ? 7.678   -11.416 -13.121 1.00 23.66  ? 9   PRO A O   1 
ATOM   70   C  CB  . PRO A 1 9   ? 5.385   -11.573 -11.030 1.00 23.23  ? 9   PRO A CB  1 
ATOM   71   C  CG  . PRO A 1 9   ? 4.055   -12.139 -11.562 1.00 23.65  ? 9   PRO A CG  1 
ATOM   72   C  CD  . PRO A 1 9   ? 4.127   -11.997 -13.066 1.00 23.66  ? 9   PRO A CD  1 
ATOM   73   N  N   . SER A 1 10  ? 7.979   -9.471  -12.053 1.00 23.11  ? 10  SER A N   1 
ATOM   74   C  CA  . SER A 1 10  ? 9.302   -9.152  -12.624 1.00 22.27  ? 10  SER A CA  1 
ATOM   75   C  C   . SER A 1 10  ? 10.439  -9.753  -11.795 1.00 22.92  ? 10  SER A C   1 
ATOM   76   O  O   . SER A 1 10  ? 11.594  -9.647  -12.246 1.00 26.06  ? 10  SER A O   1 
ATOM   77   C  CB  . SER A 1 10  ? 9.440   -7.686  -12.770 1.00 23.23  ? 10  SER A CB  1 
ATOM   78   O  OG  . SER A 1 10  ? 9.431   -7.041  -11.511 1.00 23.51  ? 10  SER A OG  1 
ATOM   79   N  N   . GLY A 1 11  ? 10.154  -10.348 -10.638 1.00 23.01  ? 11  GLY A N   1 
ATOM   80   C  CA  . GLY A 1 11  ? 11.195  -10.779 -9.676  1.00 23.08  ? 11  GLY A CA  1 
ATOM   81   C  C   . GLY A 1 11  ? 12.225  -11.736 -10.281 1.00 21.24  ? 11  GLY A C   1 
ATOM   82   O  O   . GLY A 1 11  ? 13.419  -11.557 -10.010 1.00 20.63  ? 11  GLY A O   1 
ATOM   83   N  N   . LYS A 1 12  ? 11.801  -12.728 -11.070 1.00 21.20  ? 12  LYS A N   1 
ATOM   84   C  CA  . LYS A 1 12  ? 12.749  -13.694 -11.688 1.00 27.34  ? 12  LYS A CA  1 
ATOM   85   C  C   . LYS A 1 12  ? 13.729  -12.952 -12.603 1.00 26.79  ? 12  LYS A C   1 
ATOM   86   O  O   . LYS A 1 12  ? 14.855  -13.450 -12.781 1.00 32.29  ? 12  LYS A O   1 
ATOM   87   C  CB  . LYS A 1 12  ? 12.035  -14.767 -12.502 1.00 26.71  ? 12  LYS A CB  1 
ATOM   88   C  CG  . LYS A 1 12  ? 11.193  -15.718 -11.666 1.00 31.11  ? 12  LYS A CG  1 
ATOM   89   C  CD  . LYS A 1 12  ? 10.660  -16.870 -12.463 1.00 31.26  ? 12  LYS A CD  1 
ATOM   90   C  CE  . LYS A 1 12  ? 10.073  -17.941 -11.575 1.00 34.56  ? 12  LYS A CE  1 
ATOM   91   N  NZ  . LYS A 1 12  ? 9.168   -17.326 -10.586 1.00 35.44  ? 12  LYS A NZ  1 
ATOM   92   N  N   . VAL A 1 13  ? 13.325  -11.817 -13.168 1.00 22.97  ? 13  VAL A N   1 
ATOM   93   C  CA  . VAL A 1 13  ? 14.208  -11.034 -14.079 1.00 23.14  ? 13  VAL A CA  1 
ATOM   94   C  C   . VAL A 1 13  ? 15.051  -10.076 -13.249 1.00 19.98  ? 13  VAL A C   1 
ATOM   95   O  O   . VAL A 1 13  ? 16.190  -9.849  -13.600 1.00 20.10  ? 13  VAL A O   1 
ATOM   96   C  CB  . VAL A 1 13  ? 13.414  -10.309 -15.186 1.00 24.05  ? 13  VAL A CB  1 
ATOM   97   C  CG1 . VAL A 1 13  ? 14.323  -9.472  -16.094 1.00 23.94  ? 13  VAL A CG1 1 
ATOM   98   C  CG2 . VAL A 1 13  ? 12.594  -11.282 -16.009 1.00 24.78  ? 13  VAL A CG2 1 
ATOM   99   N  N   . GLU A 1 14  ? 14.464  -9.462  -12.230 1.00 21.58  ? 14  GLU A N   1 
ATOM   100  C  CA  . GLU A 1 14  ? 15.193  -8.566  -11.303 1.00 21.35  ? 14  GLU A CA  1 
ATOM   101  C  C   . GLU A 1 14  ? 16.508  -9.226  -10.835 1.00 23.83  ? 14  GLU A C   1 
ATOM   102  O  O   . GLU A 1 14  ? 17.507  -8.526  -10.766 1.00 24.66  ? 14  GLU A O   1 
ATOM   103  C  CB  . GLU A 1 14  ? 14.308  -8.230  -10.111 1.00 23.11  ? 14  GLU A CB  1 
ATOM   104  C  CG  . GLU A 1 14  ? 13.168  -7.276  -10.439 1.00 23.92  ? 14  GLU A CG  1 
ATOM   105  C  CD  . GLU A 1 14  ? 12.214  -7.105  -9.277  1.00 24.86  ? 14  GLU A CD  1 
ATOM   106  O  OE1 . GLU A 1 14  ? 12.701  -6.829  -8.217  1.00 29.06  ? 14  GLU A OE1 1 
ATOM   107  O  OE2 . GLU A 1 14  ? 10.977  -7.219  -9.470  1.00 26.34  ? 14  GLU A OE2 1 
ATOM   108  N  N   . GLY A 1 15  ? 16.503  -10.507 -10.481 1.00 25.47  ? 15  GLY A N   1 
ATOM   109  C  CA  . GLY A 1 15  ? 17.686  -11.165 -9.888  1.00 27.74  ? 15  GLY A CA  1 
ATOM   110  C  C   . GLY A 1 15  ? 18.761  -11.465 -10.930 1.00 28.60  ? 15  GLY A C   1 
ATOM   111  O  O   . GLY A 1 15  ? 19.759  -12.113 -10.564 1.00 28.16  ? 15  GLY A O   1 
ATOM   112  N  N   . CYS A 1 16  ? 18.570  -11.047 -12.189 1.00 28.37  ? 16  CYS A N   1 
ATOM   113  C  CA  . CYS A 1 16  ? 19.523  -11.294 -13.305 1.00 27.69  ? 16  CYS A CA  1 
ATOM   114  C  C   . CYS A 1 16  ? 20.144  -9.989  -13.817 1.00 29.08  ? 16  CYS A C   1 
ATOM   115  O  O   . CYS A 1 16  ? 21.047  -10.059 -14.708 1.00 23.73  ? 16  CYS A O   1 
ATOM   116  C  CB  . CYS A 1 16  ? 18.835  -11.965 -14.478 1.00 27.53  ? 16  CYS A CB  1 
ATOM   117  S  SG  . CYS A 1 16  ? 18.068  -13.550 -14.099 1.00 29.62  ? 16  CYS A SG  1 
ATOM   118  N  N   . MET A 1 17  ? 19.675  -8.837  -13.322 1.00 25.08  ? 17  MET A N   1 
ATOM   119  C  CA  . MET A 1 17  ? 20.052  -7.533  -13.904 1.00 25.24  ? 17  MET A CA  1 
ATOM   120  C  C   . MET A 1 17  ? 21.369  -7.070  -13.263 1.00 27.15  ? 17  MET A C   1 
ATOM   121  O  O   . MET A 1 17  ? 21.488  -7.085  -12.035 1.00 27.70  ? 17  MET A O   1 
ATOM   122  C  CB  . MET A 1 17  ? 18.959  -6.483  -13.701 1.00 25.50  ? 17  MET A CB  1 
ATOM   123  C  CG  . MET A 1 17  ? 17.673  -6.779  -14.464 1.00 24.90  ? 17  MET A CG  1 
ATOM   124  S  SD  . MET A 1 17  ? 17.849  -7.278  -16.202 1.00 25.88  ? 17  MET A SD  1 
ATOM   125  C  CE  . MET A 1 17  ? 18.756  -5.899  -16.894 1.00 23.86  ? 17  MET A CE  1 
ATOM   126  N  N   . VAL A 1 18  ? 22.348  -6.719  -14.079 1.00 26.19  ? 18  VAL A N   1 
ATOM   127  C  CA  . VAL A 1 18  ? 23.654  -6.194  -13.588 1.00 24.41  ? 18  VAL A CA  1 
ATOM   128  C  C   . VAL A 1 18  ? 23.996  -4.955  -14.391 1.00 26.32  ? 18  VAL A C   1 
ATOM   129  O  O   . VAL A 1 18  ? 23.274  -4.613  -15.360 1.00 25.20  ? 18  VAL A O   1 
ATOM   130  C  CB  . VAL A 1 18  ? 24.778  -7.240  -13.684 1.00 25.11  ? 18  VAL A CB  1 
ATOM   131  C  CG1 . VAL A 1 18  ? 24.477  -8.453  -12.843 1.00 25.39  ? 18  VAL A CG1 1 
ATOM   132  C  CG2 . VAL A 1 18  ? 25.077  -7.663  -15.120 1.00 27.09  ? 18  VAL A CG2 1 
ATOM   133  N  N   . GLN A 1 19  ? 25.051  -4.287  -13.961 1.00 26.46  ? 19  GLN A N   1 
ATOM   134  C  CA  . GLN A 1 19  ? 25.564  -3.070  -14.597 1.00 27.68  ? 19  GLN A CA  1 
ATOM   135  C  C   . GLN A 1 19  ? 26.847  -3.458  -15.335 1.00 29.56  ? 19  GLN A C   1 
ATOM   136  O  O   . GLN A 1 19  ? 27.660  -4.165  -14.759 1.00 26.80  ? 19  GLN A O   1 
ATOM   137  C  CB  . GLN A 1 19  ? 25.759  -2.035  -13.503 1.00 31.96  ? 19  GLN A CB  1 
ATOM   138  C  CG  . GLN A 1 19  ? 26.186  -0.688  -14.036 1.00 32.54  ? 19  GLN A CG  1 
ATOM   139  C  CD  . GLN A 1 19  ? 26.469  0.249   -12.894 1.00 37.78  ? 19  GLN A CD  1 
ATOM   140  O  OE1 . GLN A 1 19  ? 25.805  1.268   -12.746 1.00 39.38  ? 19  GLN A OE1 1 
ATOM   141  N  NE2 . GLN A 1 19  ? 27.467  -0.089  -12.089 1.00 38.37  ? 19  GLN A NE2 1 
ATOM   142  N  N   . VAL A 1 20  ? 26.950  -3.104  -16.610 1.00 30.05  ? 20  VAL A N   1 
ATOM   143  C  CA  . VAL A 1 20  ? 28.173  -3.301  -17.431 1.00 28.38  ? 20  VAL A CA  1 
ATOM   144  C  C   . VAL A 1 20  ? 28.759  -1.939  -17.784 1.00 29.59  ? 20  VAL A C   1 
ATOM   145  O  O   . VAL A 1 20  ? 28.029  -1.071  -18.294 1.00 27.77  ? 20  VAL A O   1 
ATOM   146  C  CB  . VAL A 1 20  ? 27.865  -4.121  -18.687 1.00 27.84  ? 20  VAL A CB  1 
ATOM   147  C  CG1 . VAL A 1 20  ? 29.136  -4.429  -19.464 1.00 26.67  ? 20  VAL A CG1 1 
ATOM   148  C  CG2 . VAL A 1 20  ? 27.120  -5.393  -18.310 1.00 29.09  ? 20  VAL A CG2 1 
ATOM   149  N  N   . THR A 1 21  ? 30.056  -1.774  -17.549 1.00 30.82  ? 21  THR A N   1 
ATOM   150  C  CA  . THR A 1 21  ? 30.796  -0.559  -17.944 1.00 31.81  ? 21  THR A CA  1 
ATOM   151  C  C   . THR A 1 21  ? 31.952  -0.965  -18.845 1.00 34.41  ? 21  THR A C   1 
ATOM   152  O  O   . THR A 1 21  ? 32.526  -2.055  -18.661 1.00 31.09  ? 21  THR A O   1 
ATOM   153  C  CB  . THR A 1 21  ? 31.287  0.244   -16.747 1.00 36.23  ? 21  THR A CB  1 
ATOM   154  O  OG1 . THR A 1 21  ? 30.141  0.469   -15.928 1.00 33.55  ? 21  THR A OG1 1 
ATOM   155  C  CG2 . THR A 1 21  ? 31.928  1.550   -17.160 1.00 38.22  ? 21  THR A CG2 1 
ATOM   156  N  N   . CYS A 1 22  ? 32.177  -0.150  -19.866 1.00 34.82  ? 22  CYS A N   1 
ATOM   157  C  CA  . CYS A 1 22  ? 33.307  -0.275  -20.801 1.00 36.97  ? 22  CYS A CA  1 
ATOM   158  C  C   . CYS A 1 22  ? 33.655  1.145   -21.211 1.00 38.56  ? 22  CYS A C   1 
ATOM   159  O  O   . CYS A 1 22  ? 32.751  1.852   -21.681 1.00 33.72  ? 22  CYS A O   1 
ATOM   160  C  CB  . CYS A 1 22  ? 32.920  -1.134  -21.993 1.00 39.43  ? 22  CYS A CB  1 
ATOM   161  S  SG  . CYS A 1 22  ? 34.318  -1.477  -23.069 1.00 44.33  ? 22  CYS A SG  1 
ATOM   162  N  N   . GLY A 1 23  ? 34.882  1.581   -20.940 1.00 37.61  ? 23  GLY A N   1 
ATOM   163  C  CA  . GLY A 1 23  ? 35.232  3.000   -21.100 1.00 32.36  ? 23  GLY A CA  1 
ATOM   164  C  C   . GLY A 1 23  ? 34.353  3.886   -20.231 1.00 32.70  ? 23  GLY A C   1 
ATOM   165  O  O   . GLY A 1 23  ? 34.213  3.605   -18.994 1.00 32.97  ? 23  GLY A O   1 
ATOM   166  N  N   . THR A 1 24  ? 33.737  4.907   -20.833 1.00 33.25  ? 24  THR A N   1 
ATOM   167  C  CA  . THR A 1 24  ? 32.841  5.864   -20.127 1.00 35.93  ? 24  THR A CA  1 
ATOM   168  C  C   . THR A 1 24  ? 31.359  5.454   -20.255 1.00 35.63  ? 24  THR A C   1 
ATOM   169  O  O   . THR A 1 24  ? 30.490  6.261   -19.826 1.00 33.27  ? 24  THR A O   1 
ATOM   170  C  CB  . THR A 1 24  ? 33.086  7.288   -20.637 1.00 37.34  ? 24  THR A CB  1 
ATOM   171  O  OG1 . THR A 1 24  ? 32.628  7.420   -21.973 1.00 38.84  ? 24  THR A OG1 1 
ATOM   172  C  CG2 . THR A 1 24  ? 34.550  7.664   -20.633 1.00 43.85  ? 24  THR A CG2 1 
ATOM   173  N  N   . THR A 1 25  ? 31.070  4.283   -20.840 1.00 33.83  ? 25  THR A N   1 
ATOM   174  C  CA  . THR A 1 25  ? 29.689  3.824   -21.172 1.00 34.21  ? 25  THR A CA  1 
ATOM   175  C  C   . THR A 1 25  ? 29.253  2.795   -20.135 1.00 31.55  ? 25  THR A C   1 
ATOM   176  O  O   . THR A 1 25  ? 29.913  1.755   -20.026 1.00 29.80  ? 25  THR A O   1 
ATOM   177  C  CB  . THR A 1 25  ? 29.565  3.235   -22.589 1.00 36.40  ? 25  THR A CB  1 
ATOM   178  O  OG1 . THR A 1 25  ? 30.066  4.167   -23.540 1.00 42.11  ? 25  THR A OG1 1 
ATOM   179  C  CG2 . THR A 1 25  ? 28.142  2.909   -22.982 1.00 37.08  ? 25  THR A CG2 1 
ATOM   180  N  N   . THR A 1 26  ? 28.148  3.085   -19.454 1.00 31.34  ? 26  THR A N   1 
ATOM   181  C  CA  . THR A 1 26  ? 27.460  2.167   -18.524 1.00 33.37  ? 26  THR A CA  1 
ATOM   182  C  C   . THR A 1 26  ? 26.063  1.835   -19.071 1.00 29.94  ? 26  THR A C   1 
ATOM   183  O  O   . THR A 1 26  ? 25.324  2.737   -19.413 1.00 28.92  ? 26  THR A O   1 
ATOM   184  C  CB  . THR A 1 26  ? 27.424  2.757   -17.106 1.00 33.78  ? 26  THR A CB  1 
ATOM   185  O  OG1 . THR A 1 26  ? 28.772  2.768   -16.635 1.00 38.54  ? 26  THR A OG1 1 
ATOM   186  C  CG2 . THR A 1 26  ? 26.587  1.939   -16.150 1.00 34.52  ? 26  THR A CG2 1 
ATOM   187  N  N   . LEU A 1 27  ? 25.721  0.553   -19.104 1.00 28.24  ? 27  LEU A N   1 
ATOM   188  C  CA  . LEU A 1 27  ? 24.340  0.100   -19.362 1.00 27.54  ? 27  LEU A CA  1 
ATOM   189  C  C   . LEU A 1 27  ? 24.078  -1.198  -18.598 1.00 27.14  ? 27  LEU A C   1 
ATOM   190  O  O   . LEU A 1 27  ? 24.924  -1.612  -17.730 1.00 27.20  ? 27  LEU A O   1 
ATOM   191  C  CB  . LEU A 1 27  ? 24.132  -0.033  -20.868 1.00 25.46  ? 27  LEU A CB  1 
ATOM   192  C  CG  . LEU A 1 27  ? 25.223  -0.719  -21.682 1.00 25.21  ? 27  LEU A CG  1 
ATOM   193  C  CD1 . LEU A 1 27  ? 25.317  -2.230  -21.387 1.00 24.31  ? 27  LEU A CD1 1 
ATOM   194  C  CD2 . LEU A 1 27  ? 24.934  -0.484  -23.170 1.00 26.52  ? 27  LEU A CD2 1 
ATOM   195  N  N   . ASN A 1 28  ? 22.940  -1.810  -18.893 1.00 22.26  ? 28  ASN A N   1 
ATOM   196  C  CA  . ASN A 1 28  ? 22.447  -3.013  -18.197 1.00 23.04  ? 28  ASN A CA  1 
ATOM   197  C  C   . ASN A 1 28  ? 22.939  -4.272  -18.894 1.00 22.65  ? 28  ASN A C   1 
ATOM   198  O  O   . ASN A 1 28  ? 22.992  -4.311  -20.130 1.00 23.97  ? 28  ASN A O   1 
ATOM   199  C  CB  . ASN A 1 28  ? 20.919  -2.966  -18.080 1.00 20.83  ? 28  ASN A CB  1 
ATOM   200  C  CG  . ASN A 1 28  ? 20.455  -1.654  -17.489 1.00 22.55  ? 28  ASN A CG  1 
ATOM   201  O  OD1 . ASN A 1 28  ? 20.598  -1.424  -16.282 1.00 24.14  ? 28  ASN A OD1 1 
ATOM   202  N  ND2 . ASN A 1 28  ? 19.897  -0.790  -18.330 1.00 21.32  ? 28  ASN A ND2 1 
ATOM   203  N  N   . GLY A 1 29  ? 23.175  -5.318  -18.112 1.00 22.69  ? 29  GLY A N   1 
ATOM   204  C  CA  . GLY A 1 29  ? 23.399  -6.669  -18.650 1.00 21.82  ? 29  GLY A CA  1 
ATOM   205  C  C   . GLY A 1 29  ? 22.491  -7.678  -17.991 1.00 21.20  ? 29  GLY A C   1 
ATOM   206  O  O   . GLY A 1 29  ? 21.907  -7.390  -16.903 1.00 23.25  ? 29  GLY A O   1 
ATOM   207  N  N   . LEU A 1 30  ? 22.321  -8.808  -18.658 1.00 23.37  ? 30  LEU A N   1 
ATOM   208  C  CA  . LEU A 1 30  ? 21.453  -9.898  -18.188 1.00 24.45  ? 30  LEU A CA  1 
ATOM   209  C  C   . LEU A 1 30  ? 22.333  -11.095 -17.822 1.00 25.94  ? 30  LEU A C   1 
ATOM   210  O  O   . LEU A 1 30  ? 23.008  -11.648 -18.710 1.00 24.32  ? 30  LEU A O   1 
ATOM   211  C  CB  . LEU A 1 30  ? 20.437  -10.233 -19.273 1.00 25.42  ? 30  LEU A CB  1 
ATOM   212  C  CG  . LEU A 1 30  ? 19.481  -11.338 -18.856 1.00 26.60  ? 30  LEU A CG  1 
ATOM   213  C  CD1 . LEU A 1 30  ? 18.423  -10.823 -17.877 1.00 27.57  ? 30  LEU A CD1 1 
ATOM   214  C  CD2 . LEU A 1 30  ? 18.839  -11.957 -20.063 1.00 26.30  ? 30  LEU A CD2 1 
ATOM   215  N  N   . TRP A 1 31  ? 22.349  -11.431 -16.543 1.00 28.36  ? 31  TRP A N   1 
ATOM   216  C  CA  . TRP A 1 31  ? 23.264  -12.424 -15.920 1.00 28.59  ? 31  TRP A CA  1 
ATOM   217  C  C   . TRP A 1 31  ? 22.498  -13.722 -15.744 1.00 28.86  ? 31  TRP A C   1 
ATOM   218  O  O   . TRP A 1 31  ? 21.590  -13.766 -14.857 1.00 28.12  ? 31  TRP A O   1 
ATOM   219  C  CB  . TRP A 1 31  ? 23.793  -11.896 -14.591 1.00 31.80  ? 31  TRP A CB  1 
ATOM   220  C  CG  . TRP A 1 31  ? 24.767  -12.772 -13.874 1.00 32.56  ? 31  TRP A CG  1 
ATOM   221  C  CD1 . TRP A 1 31  ? 25.550  -13.765 -14.386 1.00 37.31  ? 31  TRP A CD1 1 
ATOM   222  C  CD2 . TRP A 1 31  ? 25.103  -12.685 -12.481 1.00 34.98  ? 31  TRP A CD2 1 
ATOM   223  N  NE1 . TRP A 1 31  ? 26.326  -14.329 -13.399 1.00 38.12  ? 31  TRP A NE1 1 
ATOM   224  C  CE2 . TRP A 1 31  ? 26.091  -13.667 -12.226 1.00 37.13  ? 31  TRP A CE2 1 
ATOM   225  C  CE3 . TRP A 1 31  ? 24.676  -11.861 -11.435 1.00 35.91  ? 31  TRP A CE3 1 
ATOM   226  C  CZ2 . TRP A 1 31  ? 26.630  -13.860 -10.956 1.00 38.16  ? 31  TRP A CZ2 1 
ATOM   227  C  CZ3 . TRP A 1 31  ? 25.205  -12.050 -10.179 1.00 34.27  ? 31  TRP A CZ3 1 
ATOM   228  C  CH2 . TRP A 1 31  ? 26.169  -13.039 -9.947  1.00 36.25  ? 31  TRP A CH2 1 
ATOM   229  N  N   . LEU A 1 32  ? 22.801  -14.683 -16.619 1.00 26.53  ? 32  LEU A N   1 
ATOM   230  C  CA  . LEU A 1 32  ? 22.214  -16.033 -16.631 1.00 27.86  ? 32  LEU A CA  1 
ATOM   231  C  C   . LEU A 1 32  ? 23.362  -17.047 -16.562 1.00 31.93  ? 32  LEU A C   1 
ATOM   232  O  O   . LEU A 1 32  ? 24.298  -16.979 -17.402 1.00 30.13  ? 32  LEU A O   1 
ATOM   233  C  CB  . LEU A 1 32  ? 21.382  -16.200 -17.893 1.00 29.11  ? 32  LEU A CB  1 
ATOM   234  C  CG  . LEU A 1 32  ? 20.238  -15.205 -18.075 1.00 29.03  ? 32  LEU A CG  1 
ATOM   235  C  CD1 . LEU A 1 32  ? 19.671  -15.332 -19.487 1.00 29.32  ? 32  LEU A CD1 1 
ATOM   236  C  CD2 . LEU A 1 32  ? 19.144  -15.446 -17.032 1.00 27.54  ? 32  LEU A CD2 1 
ATOM   237  N  N   . ASP A 1 33  ? 23.299  -17.936 -15.565 1.00 35.49  ? 33  ASP A N   1 
ATOM   238  C  CA  . ASP A 1 33  ? 24.353  -18.943 -15.276 1.00 33.04  ? 33  ASP A CA  1 
ATOM   239  C  C   . ASP A 1 33  ? 25.657  -18.143 -15.162 1.00 31.87  ? 33  ASP A C   1 
ATOM   240  O  O   . ASP A 1 33  ? 25.690  -17.128 -14.391 1.00 31.08  ? 33  ASP A O   1 
ATOM   241  C  CB  . ASP A 1 33  ? 24.280  -20.052 -16.328 1.00 33.66  ? 33  ASP A CB  1 
ATOM   242  C  CG  . ASP A 1 33  ? 22.950  -20.793 -16.360 1.00 37.87  ? 33  ASP A CG  1 
ATOM   243  O  OD1 . ASP A 1 33  ? 22.457  -21.159 -15.280 1.00 48.26  ? 33  ASP A OD1 1 
ATOM   244  O  OD2 . ASP A 1 33  ? 22.406  -21.018 -17.472 1.00 42.62  ? 33  ASP A OD2 1 
ATOM   245  N  N   . ASP A 1 34  ? 26.659  -18.447 -15.986 1.00 33.31  ? 34  ASP A N   1 
ATOM   246  C  CA  . ASP A 1 34  ? 27.995  -17.809 -15.889 1.00 33.86  ? 34  ASP A CA  1 
ATOM   247  C  C   . ASP A 1 34  ? 28.215  -16.799 -17.035 1.00 37.56  ? 34  ASP A C   1 
ATOM   248  O  O   . ASP A 1 34  ? 29.398  -16.455 -17.318 1.00 33.19  ? 34  ASP A O   1 
ATOM   249  C  CB  . ASP A 1 34  ? 29.077  -18.890 -15.827 1.00 39.76  ? 34  ASP A CB  1 
ATOM   250  C  CG  . ASP A 1 34  ? 29.296  -19.695 -17.101 1.00 43.24  ? 34  ASP A CG  1 
ATOM   251  O  OD1 . ASP A 1 34  ? 28.301  -19.959 -17.831 1.00 44.22  ? 34  ASP A OD1 1 
ATOM   252  O  OD2 . ASP A 1 34  ? 30.479  -20.062 -17.358 1.00 54.99  ? 34  ASP A OD2 1 
ATOM   253  N  N   . VAL A 1 35  ? 27.137  -16.305 -17.657 1.00 34.70  ? 35  VAL A N   1 
ATOM   254  C  CA  . VAL A 1 35  ? 27.226  -15.351 -18.812 1.00 33.06  ? 35  VAL A CA  1 
ATOM   255  C  C   . VAL A 1 35  ? 26.425  -14.078 -18.529 1.00 32.75  ? 35  VAL A C   1 
ATOM   256  O  O   . VAL A 1 35  ? 25.276  -14.165 -18.020 1.00 28.32  ? 35  VAL A O   1 
ATOM   257  C  CB  . VAL A 1 35  ? 26.740  -15.989 -20.121 1.00 33.23  ? 35  VAL A CB  1 
ATOM   258  C  CG1 . VAL A 1 35  ? 26.892  -15.019 -21.286 1.00 33.93  ? 35  VAL A CG1 1 
ATOM   259  C  CG2 . VAL A 1 35  ? 27.447  -17.306 -20.417 1.00 35.46  ? 35  VAL A CG2 1 
ATOM   260  N  N   . VAL A 1 36  ? 27.019  -12.932 -18.848 1.00 30.11  ? 36  VAL A N   1 
ATOM   261  C  CA  . VAL A 1 36  ? 26.315  -11.622 -18.837 1.00 26.59  ? 36  VAL A CA  1 
ATOM   262  C  C   . VAL A 1 36  ? 26.119  -11.254 -20.304 1.00 27.27  ? 36  VAL A C   1 
ATOM   263  O  O   . VAL A 1 36  ? 27.127  -11.193 -21.038 1.00 28.41  ? 36  VAL A O   1 
ATOM   264  C  CB  . VAL A 1 36  ? 27.090  -10.533 -18.073 1.00 27.19  ? 36  VAL A CB  1 
ATOM   265  C  CG1 . VAL A 1 36  ? 26.539  -9.140  -18.324 1.00 27.45  ? 36  VAL A CG1 1 
ATOM   266  C  CG2 . VAL A 1 36  ? 27.116  -10.805 -16.576 1.00 30.80  ? 36  VAL A CG2 1 
ATOM   267  N  N   . TYR A 1 37  ? 24.867  -11.045 -20.715 1.00 26.50  ? 37  TYR A N   1 
ATOM   268  C  CA  . TYR A 1 37  ? 24.484  -10.593 -22.073 1.00 24.52  ? 37  TYR A CA  1 
ATOM   269  C  C   . TYR A 1 37  ? 24.235  -9.090  -22.046 1.00 25.42  ? 37  TYR A C   1 
ATOM   270  O  O   . TYR A 1 37  ? 23.502  -8.613  -21.147 1.00 25.78  ? 37  TYR A O   1 
ATOM   271  C  CB  . TYR A 1 37  ? 23.234  -11.314 -22.539 1.00 25.14  ? 37  TYR A CB  1 
ATOM   272  C  CG  . TYR A 1 37  ? 23.340  -12.811 -22.555 1.00 30.27  ? 37  TYR A CG  1 
ATOM   273  C  CD1 . TYR A 1 37  ? 23.201  -13.538 -21.382 1.00 30.59  ? 37  TYR A CD1 1 
ATOM   274  C  CD2 . TYR A 1 37  ? 23.549  -13.508 -23.736 1.00 28.70  ? 37  TYR A CD2 1 
ATOM   275  C  CE1 . TYR A 1 37  ? 23.295  -14.916 -21.374 1.00 29.67  ? 37  TYR A CE1 1 
ATOM   276  C  CE2 . TYR A 1 37  ? 23.618  -14.893 -23.745 1.00 32.06  ? 37  TYR A CE2 1 
ATOM   277  C  CZ  . TYR A 1 37  ? 23.511  -15.600 -22.555 1.00 32.52  ? 37  TYR A CZ  1 
ATOM   278  O  OH  . TYR A 1 37  ? 23.579  -16.968 -22.547 1.00 33.53  ? 37  TYR A OH  1 
ATOM   279  N  N   . CYS A 1 38  ? 24.821  -8.347  -22.986 1.00 25.19  ? 38  CYS A N   1 
ATOM   280  C  CA  . CYS A 1 38  ? 24.539  -6.895  -23.145 1.00 24.17  ? 38  CYS A CA  1 
ATOM   281  C  C   . CYS A 1 38  ? 24.689  -6.481  -24.609 1.00 23.61  ? 38  CYS A C   1 
ATOM   282  O  O   . CYS A 1 38  ? 25.206  -7.230  -25.427 1.00 25.80  ? 38  CYS A O   1 
ATOM   283  C  CB  . CYS A 1 38  ? 25.379  -6.043  -22.211 1.00 26.34  ? 38  CYS A CB  1 
ATOM   284  S  SG  . CYS A 1 38  ? 27.144  -5.943  -22.638 1.00 28.50  ? 38  CYS A SG  1 
ATOM   285  N  N   . PRO A 1 39  ? 24.187  -5.294  -24.999 1.00 25.26  ? 39  PRO A N   1 
ATOM   286  C  CA  . PRO A 1 39  ? 24.342  -4.825  -26.373 1.00 24.36  ? 39  PRO A CA  1 
ATOM   287  C  C   . PRO A 1 39  ? 25.843  -4.635  -26.634 1.00 23.84  ? 39  PRO A C   1 
ATOM   288  O  O   . PRO A 1 39  ? 26.553  -4.137  -25.809 1.00 22.46  ? 39  PRO A O   1 
ATOM   289  C  CB  . PRO A 1 39  ? 23.577  -3.495  -26.412 1.00 24.09  ? 39  PRO A CB  1 
ATOM   290  C  CG  . PRO A 1 39  ? 22.638  -3.573  -25.223 1.00 23.87  ? 39  PRO A CG  1 
ATOM   291  C  CD  . PRO A 1 39  ? 23.386  -4.366  -24.180 1.00 25.10  ? 39  PRO A CD  1 
ATOM   292  N  N   . ARG A 1 40  ? 26.288  -5.039  -27.804 1.00 24.72  ? 40  ARG A N   1 
ATOM   293  C  CA  . ARG A 1 40  ? 27.707  -4.918  -28.171 1.00 24.03  ? 40  ARG A CA  1 
ATOM   294  C  C   . ARG A 1 40  ? 28.101  -3.447  -28.331 1.00 25.23  ? 40  ARG A C   1 
ATOM   295  O  O   . ARG A 1 40  ? 29.311  -3.183  -28.195 1.00 27.39  ? 40  ARG A O   1 
ATOM   296  C  CB  . ARG A 1 40  ? 27.968  -5.760  -29.414 1.00 22.75  ? 40  ARG A CB  1 
ATOM   297  C  CG  . ARG A 1 40  ? 27.359  -5.213  -30.686 1.00 22.41  ? 40  ARG A CG  1 
ATOM   298  C  CD  . ARG A 1 40  ? 27.750  -6.096  -31.849 1.00 23.33  ? 40  ARG A CD  1 
ATOM   299  N  NE  . ARG A 1 40  ? 27.190  -5.564  -33.077 1.00 25.74  ? 40  ARG A NE  1 
ATOM   300  C  CZ  . ARG A 1 40  ? 27.512  -5.973  -34.306 1.00 27.71  ? 40  ARG A CZ  1 
ATOM   301  N  NH1 . ARG A 1 40  ? 28.415  -6.928  -34.489 1.00 28.35  ? 40  ARG A NH1 1 
ATOM   302  N  NH2 . ARG A 1 40  ? 26.952  -5.390  -35.340 1.00 25.56  ? 40  ARG A NH2 1 
ATOM   303  N  N   . HIS A 1 41  ? 27.172  -2.508  -28.537 1.00 23.00  ? 41  HIS A N   1 
ATOM   304  C  CA  . HIS A 1 41  ? 27.560  -1.082  -28.705 1.00 22.62  ? 41  HIS A CA  1 
ATOM   305  C  C   . HIS A 1 41  ? 28.160  -0.495  -27.412 1.00 23.10  ? 41  HIS A C   1 
ATOM   306  O  O   . HIS A 1 41  ? 28.625  0.651   -27.476 1.00 22.05  ? 41  HIS A O   1 
ATOM   307  C  CB  . HIS A 1 41  ? 26.433  -0.227  -29.294 1.00 23.08  ? 41  HIS A CB  1 
ATOM   308  C  CG  . HIS A 1 41  ? 25.236  0.014   -28.436 1.00 23.47  ? 41  HIS A CG  1 
ATOM   309  N  ND1 . HIS A 1 41  ? 25.269  0.772   -27.268 1.00 24.71  ? 41  HIS A ND1 1 
ATOM   310  C  CD2 . HIS A 1 41  ? 23.947  -0.347  -28.613 1.00 23.61  ? 41  HIS A CD2 1 
ATOM   311  C  CE1 . HIS A 1 41  ? 24.046  0.835   -26.757 1.00 24.85  ? 41  HIS A CE1 1 
ATOM   312  N  NE2 . HIS A 1 41  ? 23.218  0.136   -27.555 1.00 24.21  ? 41  HIS A NE2 1 
ATOM   313  N  N   . VAL A 1 42  ? 28.171  -1.222  -26.290 1.00 21.75  ? 42  VAL A N   1 
ATOM   314  C  CA  . VAL A 1 42  ? 28.813  -0.752  -25.021 1.00 24.31  ? 42  VAL A CA  1 
ATOM   315  C  C   . VAL A 1 42  ? 30.310  -0.501  -25.285 1.00 26.53  ? 42  VAL A C   1 
ATOM   316  O  O   . VAL A 1 42  ? 30.891  0.367   -24.599 1.00 28.29  ? 42  VAL A O   1 
ATOM   317  C  CB  . VAL A 1 42  ? 28.615  -1.752  -23.857 1.00 23.27  ? 42  VAL A CB  1 
ATOM   318  C  CG1 . VAL A 1 42  ? 29.340  -3.081  -24.046 1.00 22.10  ? 42  VAL A CG1 1 
ATOM   319  C  CG2 . VAL A 1 42  ? 29.002  -1.140  -22.518 1.00 25.10  ? 42  VAL A CG2 1 
ATOM   320  N  N   . ILE A 1 43  ? 30.903  -1.202  -26.263 1.00 30.90  ? 43  ILE A N   1 
ATOM   321  C  CA  . ILE A 1 43  ? 32.365  -1.082  -26.581 1.00 32.17  ? 43  ILE A CA  1 
ATOM   322  C  C   . ILE A 1 43  ? 32.641  0.075   -27.542 1.00 33.46  ? 43  ILE A C   1 
ATOM   323  O  O   . ILE A 1 43  ? 33.814  0.242   -27.848 1.00 35.18  ? 43  ILE A O   1 
ATOM   324  C  CB  . ILE A 1 43  ? 32.932  -2.382  -27.162 1.00 28.06  ? 43  ILE A CB  1 
ATOM   325  C  CG1 . ILE A 1 43  ? 32.512  -2.631  -28.619 1.00 27.58  ? 43  ILE A CG1 1 
ATOM   326  C  CG2 . ILE A 1 43  ? 32.592  -3.519  -26.249 1.00 27.81  ? 43  ILE A CG2 1 
ATOM   327  C  CD1 . ILE A 1 43  ? 33.131  -3.869  -29.230 1.00 27.77  ? 43  ILE A CD1 1 
ATOM   328  N  N   . CYS A 1 44  ? 31.620  0.800   -28.019 1.00 33.09  ? 44  CYS A N   1 
ATOM   329  C  CA  . CYS A 1 44  ? 31.790  1.958   -28.935 1.00 35.34  ? 44  CYS A CA  1 
ATOM   330  C  C   . CYS A 1 44  ? 32.152  3.214   -28.153 1.00 40.65  ? 44  CYS A C   1 
ATOM   331  O  O   . CYS A 1 44  ? 31.538  3.477   -27.109 1.00 39.67  ? 44  CYS A O   1 
ATOM   332  C  CB  . CYS A 1 44  ? 30.530  2.260   -29.725 1.00 35.79  ? 44  CYS A CB  1 
ATOM   333  S  SG  . CYS A 1 44  ? 30.151  0.934   -30.882 1.00 37.74  ? 44  CYS A SG  1 
ATOM   334  N  N   . THR A 1 45  ? 33.092  3.975   -28.703 1.00 43.86  ? 45  THR A N   1 
ATOM   335  C  CA  . THR A 1 45  ? 33.445  5.354   -28.283 1.00 45.77  ? 45  THR A CA  1 
ATOM   336  C  C   . THR A 1 45  ? 32.640  6.321   -29.158 1.00 50.14  ? 45  THR A C   1 
ATOM   337  O  O   . THR A 1 45  ? 31.760  5.851   -29.938 1.00 49.82  ? 45  THR A O   1 
ATOM   338  C  CB  . THR A 1 45  ? 34.960  5.575   -28.402 1.00 44.17  ? 45  THR A CB  1 
ATOM   339  O  OG1 . THR A 1 45  ? 35.265  5.478   -29.790 1.00 44.31  ? 45  THR A OG1 1 
ATOM   340  C  CG2 . THR A 1 45  ? 35.791  4.554   -27.661 1.00 45.36  ? 45  THR A CG2 1 
ATOM   341  N  N   . SER A 1 46  ? 32.960  7.611   -29.086 1.00 56.33  ? 46  SER A N   1 
ATOM   342  C  CA  . SER A 1 46  ? 32.215  8.693   -29.783 1.00 61.24  ? 46  SER A CA  1 
ATOM   343  C  C   . SER A 1 46  ? 32.390  8.631   -31.312 1.00 63.24  ? 46  SER A C   1 
ATOM   344  O  O   . SER A 1 46  ? 31.387  8.889   -32.002 1.00 60.08  ? 46  SER A O   1 
ATOM   345  C  CB  . SER A 1 46  ? 32.586  10.040  -29.231 1.00 62.61  ? 46  SER A CB  1 
ATOM   346  O  OG  . SER A 1 46  ? 32.016  10.199  -27.943 1.00 66.95  ? 46  SER A OG  1 
ATOM   347  N  N   . GLU A 1 47  ? 33.573  8.284   -31.843 1.00 70.61  ? 47  GLU A N   1 
ATOM   348  C  CA  . GLU A 1 47  ? 33.780  8.185   -33.324 1.00 72.63  ? 47  GLU A CA  1 
ATOM   349  C  C   . GLU A 1 47  ? 33.246  6.846   -33.857 1.00 66.85  ? 47  GLU A C   1 
ATOM   350  O  O   . GLU A 1 47  ? 32.916  6.781   -35.053 1.00 80.97  ? 47  GLU A O   1 
ATOM   351  C  CB  . GLU A 1 47  ? 35.244  8.320   -33.760 1.00 80.97  ? 47  GLU A CB  1 
ATOM   352  C  CG  . GLU A 1 47  ? 35.946  9.576   -33.281 1.00 84.35  ? 47  GLU A CG  1 
ATOM   353  C  CD  . GLU A 1 47  ? 36.655  9.414   -31.950 1.00 92.31  ? 47  GLU A CD  1 
ATOM   354  O  OE1 . GLU A 1 47  ? 37.086  8.287   -31.643 1.00 92.30  ? 47  GLU A OE1 1 
ATOM   355  O  OE2 . GLU A 1 47  ? 36.756  10.413  -31.220 1.00 105.19 ? 47  GLU A OE2 1 
ATOM   356  N  N   . ASP A 1 48  ? 33.135  5.824   -33.009 1.00 56.62  ? 48  ASP A N   1 
ATOM   357  C  CA  . ASP A 1 48  ? 32.702  4.460   -33.412 1.00 56.20  ? 48  ASP A CA  1 
ATOM   358  C  C   . ASP A 1 48  ? 31.191  4.429   -33.669 1.00 52.49  ? 48  ASP A C   1 
ATOM   359  O  O   . ASP A 1 48  ? 30.678  3.342   -33.927 1.00 59.79  ? 48  ASP A O   1 
ATOM   360  C  CB  . ASP A 1 48  ? 33.081  3.410   -32.358 1.00 50.59  ? 48  ASP A CB  1 
ATOM   361  C  CG  . ASP A 1 48  ? 34.558  3.453   -32.008 1.00 51.99  ? 48  ASP A CG  1 
ATOM   362  O  OD1 . ASP A 1 48  ? 35.372  3.526   -32.946 1.00 56.24  ? 48  ASP A OD1 1 
ATOM   363  O  OD2 . ASP A 1 48  ? 34.881  3.454   -30.804 1.00 47.64  ? 48  ASP A OD2 1 
ATOM   364  N  N   . MET A 1 49  ? 30.481  5.552   -33.598 1.00 47.11  ? 49  MET A N   1 
ATOM   365  C  CA  . MET A 1 49  ? 28.999  5.480   -33.534 1.00 49.28  ? 49  MET A CA  1 
ATOM   366  C  C   . MET A 1 49  ? 28.414  5.331   -34.956 1.00 43.52  ? 49  MET A C   1 
ATOM   367  O  O   . MET A 1 49  ? 27.390  4.640   -35.114 1.00 36.64  ? 49  MET A O   1 
ATOM   368  C  CB  . MET A 1 49  ? 28.431  6.696   -32.789 1.00 56.79  ? 49  MET A CB  1 
ATOM   369  C  CG  . MET A 1 49  ? 28.785  6.750   -31.281 1.00 65.07  ? 49  MET A CG  1 
ATOM   370  S  SD  . MET A 1 49  ? 28.629  5.177   -30.334 1.00 86.68  ? 49  MET A SD  1 
ATOM   371  C  CE  . MET A 1 49  ? 27.016  4.533   -30.794 1.00 81.44  ? 49  MET A CE  1 
ATOM   372  N  N   . LEU A 1 50  ? 29.072  5.879   -35.978 1.00 36.42  ? 50  LEU A N   1 
ATOM   373  C  CA  . LEU A 1 50  ? 28.545  5.875   -37.371 1.00 34.80  ? 50  LEU A CA  1 
ATOM   374  C  C   . LEU A 1 50  ? 28.807  4.523   -38.046 1.00 28.84  ? 50  LEU A C   1 
ATOM   375  O  O   . LEU A 1 50  ? 27.898  3.970   -38.663 1.00 28.62  ? 50  LEU A O   1 
ATOM   376  C  CB  . LEU A 1 50  ? 29.199  7.010   -38.169 1.00 42.48  ? 50  LEU A CB  1 
ATOM   377  C  CG  . LEU A 1 50  ? 28.454  8.347   -38.204 1.00 47.17  ? 50  LEU A CG  1 
ATOM   378  C  CD1 . LEU A 1 50  ? 26.974  8.134   -38.491 1.00 50.30  ? 50  LEU A CD1 1 
ATOM   379  C  CD2 . LEU A 1 50  ? 28.643  9.115   -36.910 1.00 49.13  ? 50  LEU A CD2 1 
ATOM   380  N  N   . ASN A 1 51  ? 30.032  4.024   -38.001 1.00 26.86  ? 51  ASN A N   1 
ATOM   381  C  CA  . ASN A 1 51  ? 30.421  2.810   -38.754 1.00 27.17  ? 51  ASN A CA  1 
ATOM   382  C  C   . ASN A 1 51  ? 31.340  1.970   -37.883 1.00 28.63  ? 51  ASN A C   1 
ATOM   383  O  O   . ASN A 1 51  ? 32.479  1.719   -38.240 1.00 29.51  ? 51  ASN A O   1 
ATOM   384  C  CB  . ASN A 1 51  ? 31.093  3.165   -40.078 1.00 26.65  ? 51  ASN A CB  1 
ATOM   385  C  CG  . ASN A 1 51  ? 30.101  3.794   -41.023 1.00 28.42  ? 51  ASN A CG  1 
ATOM   386  O  OD1 . ASN A 1 51  ? 29.355  3.082   -41.698 1.00 30.13  ? 51  ASN A OD1 1 
ATOM   387  N  ND2 . ASN A 1 51  ? 30.053  5.120   -41.016 1.00 25.81  ? 51  ASN A ND2 1 
ATOM   388  N  N   . PRO A 1 52  ? 30.877  1.542   -36.698 1.00 28.47  ? 52  PRO A N   1 
ATOM   389  C  CA  . PRO A 1 52  ? 31.688  0.689   -35.835 1.00 27.61  ? 52  PRO A CA  1 
ATOM   390  C  C   . PRO A 1 52  ? 32.077  -0.618  -36.529 1.00 26.03  ? 52  PRO A C   1 
ATOM   391  O  O   . PRO A 1 52  ? 31.248  -1.284  -37.153 1.00 24.41  ? 52  PRO A O   1 
ATOM   392  C  CB  . PRO A 1 52  ? 30.757  0.409   -34.644 1.00 28.61  ? 52  PRO A CB  1 
ATOM   393  C  CG  . PRO A 1 52  ? 29.388  0.559   -35.241 1.00 29.16  ? 52  PRO A CG  1 
ATOM   394  C  CD  . PRO A 1 52  ? 29.524  1.743   -36.174 1.00 28.92  ? 52  PRO A CD  1 
ATOM   395  N  N   . ASN A 1 53  ? 33.359  -0.942  -36.447 1.00 24.85  ? 53  ASN A N   1 
ATOM   396  C  CA  . ASN A 1 53  ? 33.881  -2.249  -36.876 1.00 27.49  ? 53  ASN A CA  1 
ATOM   397  C  C   . ASN A 1 53  ? 33.983  -3.081  -35.609 1.00 27.78  ? 53  ASN A C   1 
ATOM   398  O  O   . ASN A 1 53  ? 34.969  -2.978  -34.884 1.00 26.10  ? 53  ASN A O   1 
ATOM   399  C  CB  . ASN A 1 53  ? 35.216  -2.099  -37.596 1.00 29.35  ? 53  ASN A CB  1 
ATOM   400  C  CG  . ASN A 1 53  ? 35.620  -3.378  -38.284 1.00 34.57  ? 53  ASN A CG  1 
ATOM   401  O  OD1 . ASN A 1 53  ? 35.444  -4.466  -37.735 1.00 34.65  ? 53  ASN A OD1 1 
ATOM   402  N  ND2 . ASN A 1 53  ? 36.178  -3.249  -39.482 1.00 39.34  ? 53  ASN A ND2 1 
ATOM   403  N  N   . TYR A 1 54  ? 32.949  -3.829  -35.311 1.00 28.42  ? 54  TYR A N   1 
ATOM   404  C  CA  . TYR A 1 54  ? 32.811  -4.435  -33.980 1.00 28.22  ? 54  TYR A CA  1 
ATOM   405  C  C   . TYR A 1 54  ? 33.892  -5.502  -33.791 1.00 29.71  ? 54  TYR A C   1 
ATOM   406  O  O   . TYR A 1 54  ? 34.419  -5.564  -32.681 1.00 27.79  ? 54  TYR A O   1 
ATOM   407  C  CB  . TYR A 1 54  ? 31.390  -4.943  -33.787 1.00 26.69  ? 54  TYR A CB  1 
ATOM   408  C  CG  . TYR A 1 54  ? 30.399  -3.868  -33.455 1.00 25.92  ? 54  TYR A CG  1 
ATOM   409  C  CD1 . TYR A 1 54  ? 30.387  -3.271  -32.208 1.00 28.05  ? 54  TYR A CD1 1 
ATOM   410  C  CD2 . TYR A 1 54  ? 29.458  -3.459  -34.383 1.00 27.44  ? 54  TYR A CD2 1 
ATOM   411  C  CE1 . TYR A 1 54  ? 29.449  -2.313  -31.880 1.00 27.60  ? 54  TYR A CE1 1 
ATOM   412  C  CE2 . TYR A 1 54  ? 28.531  -2.484  -34.085 1.00 26.26  ? 54  TYR A CE2 1 
ATOM   413  C  CZ  . TYR A 1 54  ? 28.531  -1.900  -32.835 1.00 27.58  ? 54  TYR A CZ  1 
ATOM   414  O  OH  . TYR A 1 54  ? 27.606  -0.930  -32.570 1.00 24.23  ? 54  TYR A OH  1 
ATOM   415  N  N   . GLU A 1 55  ? 34.151  -6.339  -34.788 1.00 33.36  ? 55  GLU A N   1 
ATOM   416  C  CA  . GLU A 1 55  ? 35.216  -7.374  -34.725 1.00 38.55  ? 55  GLU A CA  1 
ATOM   417  C  C   . GLU A 1 55  ? 36.543  -6.672  -34.357 1.00 34.35  ? 55  GLU A C   1 
ATOM   418  O  O   . GLU A 1 55  ? 37.273  -7.138  -33.471 1.00 31.40  ? 55  GLU A O   1 
ATOM   419  C  CB  . GLU A 1 55  ? 35.204  -8.160  -36.041 1.00 44.90  ? 55  GLU A CB  1 
ATOM   420  C  CG  . GLU A 1 55  ? 36.374  -9.124  -36.221 1.00 60.77  ? 55  GLU A CG  1 
ATOM   421  C  CD  . GLU A 1 55  ? 36.681  -9.558  -37.657 1.00 66.08  ? 55  GLU A CD  1 
ATOM   422  O  OE1 . GLU A 1 55  ? 36.205  -8.895  -38.615 1.00 67.56  ? 55  GLU A OE1 1 
ATOM   423  O  OE2 . GLU A 1 55  ? 37.420  -10.556 -37.821 1.00 69.44  ? 55  GLU A OE2 1 
ATOM   424  N  N   . ASP A 1 56  ? 36.812  -5.511  -34.936 1.00 31.95  ? 56  ASP A N   1 
ATOM   425  C  CA  . ASP A 1 56  ? 38.076  -4.760  -34.705 1.00 30.60  ? 56  ASP A CA  1 
ATOM   426  C  C   . ASP A 1 56  ? 38.100  -4.202  -33.273 1.00 30.62  ? 56  ASP A C   1 
ATOM   427  O  O   . ASP A 1 56  ? 39.172  -4.257  -32.648 1.00 28.92  ? 56  ASP A O   1 
ATOM   428  C  CB  . ASP A 1 56  ? 38.243  -3.660  -35.762 1.00 29.41  ? 56  ASP A CB  1 
ATOM   429  C  CG  . ASP A 1 56  ? 39.518  -2.843  -35.582 1.00 32.79  ? 56  ASP A CG  1 
ATOM   430  O  OD1 . ASP A 1 56  ? 40.585  -3.401  -35.825 1.00 30.02  ? 56  ASP A OD1 1 
ATOM   431  O  OD2 . ASP A 1 56  ? 39.421  -1.668  -35.182 1.00 37.45  ? 56  ASP A OD2 1 
ATOM   432  N  N   . LEU A 1 57  ? 37.003  -3.607  -32.782 1.00 26.87  ? 57  LEU A N   1 
ATOM   433  C  CA  . LEU A 1 57  ? 36.991  -2.939  -31.455 1.00 29.54  ? 57  LEU A CA  1 
ATOM   434  C  C   . LEU A 1 57  ? 37.091  -4.004  -30.362 1.00 28.09  ? 57  LEU A C   1 
ATOM   435  O  O   . LEU A 1 57  ? 37.685  -3.703  -29.308 1.00 33.20  ? 57  LEU A O   1 
ATOM   436  C  CB  . LEU A 1 57  ? 35.705  -2.116  -31.295 1.00 29.77  ? 57  LEU A CB  1 
ATOM   437  C  CG  . LEU A 1 57  ? 35.579  -0.966  -32.286 1.00 32.03  ? 57  LEU A CG  1 
ATOM   438  C  CD1 . LEU A 1 57  ? 34.171  -0.382  -32.277 1.00 32.96  ? 57  LEU A CD1 1 
ATOM   439  C  CD2 . LEU A 1 57  ? 36.624  0.111   -32.016 1.00 30.56  ? 57  LEU A CD2 1 
ATOM   440  N  N   . LEU A 1 58  ? 36.483  -5.173  -30.573 1.00 27.85  ? 58  LEU A N   1 
ATOM   441  C  CA  . LEU A 1 58  ? 36.399  -6.225  -29.518 1.00 29.98  ? 58  LEU A CA  1 
ATOM   442  C  C   . LEU A 1 58  ? 37.752  -6.929  -29.343 1.00 29.28  ? 58  LEU A C   1 
ATOM   443  O  O   . LEU A 1 58  ? 38.126  -7.237  -28.186 1.00 30.65  ? 58  LEU A O   1 
ATOM   444  C  CB  . LEU A 1 58  ? 35.315  -7.257  -29.849 1.00 28.14  ? 58  LEU A CB  1 
ATOM   445  C  CG  . LEU A 1 58  ? 35.032  -8.269  -28.734 1.00 29.58  ? 58  LEU A CG  1 
ATOM   446  C  CD1 . LEU A 1 58  ? 34.509  -7.589  -27.469 1.00 30.43  ? 58  LEU A CD1 1 
ATOM   447  C  CD2 . LEU A 1 58  ? 34.044  -9.330  -29.196 1.00 30.34  ? 58  LEU A CD2 1 
ATOM   448  N  N   . ILE A 1 59  ? 38.455  -7.196  -30.438 1.00 31.29  ? 59  ILE A N   1 
ATOM   449  C  CA  . ILE A 1 59  ? 39.784  -7.874  -30.391 1.00 34.21  ? 59  ILE A CA  1 
ATOM   450  C  C   . ILE A 1 59  ? 40.774  -7.011  -29.586 1.00 30.68  ? 59  ILE A C   1 
ATOM   451  O  O   . ILE A 1 59  ? 41.743  -7.571  -29.047 1.00 35.07  ? 59  ILE A O   1 
ATOM   452  C  CB  . ILE A 1 59  ? 40.270  -8.209  -31.814 1.00 35.94  ? 59  ILE A CB  1 
ATOM   453  C  CG1 . ILE A 1 59  ? 41.286  -9.351  -31.792 1.00 39.51  ? 59  ILE A CG1 1 
ATOM   454  C  CG2 . ILE A 1 59  ? 40.823  -6.983  -32.499 1.00 36.01  ? 59  ILE A CG2 1 
ATOM   455  C  CD1 . ILE A 1 59  ? 41.550  -9.950  -33.154 1.00 41.50  ? 59  ILE A CD1 1 
ATOM   456  N  N   . ARG A 1 60  ? 40.521  -5.712  -29.457 1.00 29.76  ? 60  ARG A N   1 
ATOM   457  C  CA  . ARG A 1 60  ? 41.426  -4.759  -28.759 1.00 29.94  ? 60  ARG A CA  1 
ATOM   458  C  C   . ARG A 1 60  ? 41.125  -4.721  -27.258 1.00 31.96  ? 60  ARG A C   1 
ATOM   459  O  O   . ARG A 1 60  ? 41.900  -4.057  -26.529 1.00 35.07  ? 60  ARG A O   1 
ATOM   460  C  CB  . ARG A 1 60  ? 41.288  -3.374  -29.391 1.00 28.56  ? 60  ARG A CB  1 
ATOM   461  C  CG  . ARG A 1 60  ? 41.635  -3.360  -30.877 1.00 26.41  ? 60  ARG A CG  1 
ATOM   462  C  CD  . ARG A 1 60  ? 41.404  -1.994  -31.487 1.00 25.88  ? 60  ARG A CD  1 
ATOM   463  N  NE  . ARG A 1 60  ? 41.639  -2.030  -32.922 1.00 28.99  ? 60  ARG A NE  1 
ATOM   464  C  CZ  . ARG A 1 60  ? 42.753  -1.643  -33.546 1.00 29.49  ? 60  ARG A CZ  1 
ATOM   465  N  NH1 . ARG A 1 60  ? 43.786  -1.198  -32.862 1.00 27.82  ? 60  ARG A NH1 1 
ATOM   466  N  NH2 . ARG A 1 60  ? 42.832  -1.727  -34.855 1.00 26.87  ? 60  ARG A NH2 1 
ATOM   467  N  N   . LYS A 1 61  ? 40.076  -5.418  -26.818 1.00 30.80  ? 61  LYS A N   1 
ATOM   468  C  CA  . LYS A 1 61  ? 39.609  -5.413  -25.407 1.00 36.42  ? 61  LYS A CA  1 
ATOM   469  C  C   . LYS A 1 61  ? 40.184  -6.639  -24.692 1.00 37.54  ? 61  LYS A C   1 
ATOM   470  O  O   . LYS A 1 61  ? 40.323  -7.712  -25.321 1.00 35.80  ? 61  LYS A O   1 
ATOM   471  C  CB  . LYS A 1 61  ? 38.076  -5.381  -25.322 1.00 36.12  ? 61  LYS A CB  1 
ATOM   472  C  CG  . LYS A 1 61  ? 37.432  -4.183  -26.009 1.00 38.49  ? 61  LYS A CG  1 
ATOM   473  C  CD  . LYS A 1 61  ? 37.566  -2.877  -25.266 1.00 44.30  ? 61  LYS A CD  1 
ATOM   474  C  CE  . LYS A 1 61  ? 37.331  -1.670  -26.152 1.00 47.06  ? 61  LYS A CE  1 
ATOM   475  N  NZ  . LYS A 1 61  ? 37.088  -0.461  -25.339 1.00 54.10  ? 61  LYS A NZ  1 
ATOM   476  N  N   . SER A 1 62  ? 40.537  -6.458  -23.427 1.00 41.29  ? 62  SER A N   1 
ATOM   477  C  CA  . SER A 1 62  ? 40.816  -7.570  -22.484 1.00 47.33  ? 62  SER A CA  1 
ATOM   478  C  C   . SER A 1 62  ? 39.644  -7.688  -21.506 1.00 43.70  ? 62  SER A C   1 
ATOM   479  O  O   . SER A 1 62  ? 38.915  -6.687  -21.303 1.00 37.85  ? 62  SER A O   1 
ATOM   480  C  CB  . SER A 1 62  ? 42.134  -7.376  -21.773 1.00 51.32  ? 62  SER A CB  1 
ATOM   481  O  OG  . SER A 1 62  ? 42.464  -5.995  -21.676 1.00 60.00  ? 62  SER A OG  1 
ATOM   482  N  N   . ASN A 1 63  ? 39.480  -8.880  -20.936 1.00 43.18  ? 63  ASN A N   1 
ATOM   483  C  CA  . ASN A 1 63  ? 38.476  -9.198  -19.895 1.00 43.52  ? 63  ASN A CA  1 
ATOM   484  C  C   . ASN A 1 63  ? 38.401  -8.056  -18.858 1.00 44.91  ? 63  ASN A C   1 
ATOM   485  O  O   . ASN A 1 63  ? 37.283  -7.730  -18.409 1.00 40.79  ? 63  ASN A O   1 
ATOM   486  C  CB  . ASN A 1 63  ? 38.801  -10.559 -19.297 1.00 44.08  ? 63  ASN A CB  1 
ATOM   487  C  CG  . ASN A 1 63  ? 38.575  -11.706 -20.260 1.00 46.52  ? 63  ASN A CG  1 
ATOM   488  O  OD1 . ASN A 1 63  ? 37.709  -11.642 -21.134 1.00 46.11  ? 63  ASN A OD1 1 
ATOM   489  N  ND2 . ASN A 1 63  ? 39.322  -12.786 -20.076 1.00 40.11  ? 63  ASN A ND2 1 
ATOM   490  N  N   . HIS A 1 64  ? 39.519  -7.408  -18.522 1.00 45.90  ? 64  HIS A N   1 
ATOM   491  C  CA  . HIS A 1 64  ? 39.588  -6.392  -17.433 1.00 45.55  ? 64  HIS A CA  1 
ATOM   492  C  C   . HIS A 1 64  ? 39.154  -4.998  -17.889 1.00 44.28  ? 64  HIS A C   1 
ATOM   493  O  O   . HIS A 1 64  ? 39.048  -4.127  -17.002 1.00 44.49  ? 64  HIS A O   1 
ATOM   494  C  CB  . HIS A 1 64  ? 40.973  -6.356  -16.760 1.00 50.66  ? 64  HIS A CB  1 
ATOM   495  C  CG  . HIS A 1 64  ? 42.143  -6.108  -17.652 1.00 53.53  ? 64  HIS A CG  1 
ATOM   496  N  ND1 . HIS A 1 64  ? 42.868  -7.149  -18.218 1.00 59.42  ? 64  HIS A ND1 1 
ATOM   497  C  CD2 . HIS A 1 64  ? 42.771  -4.964  -18.014 1.00 58.34  ? 64  HIS A CD2 1 
ATOM   498  C  CE1 . HIS A 1 64  ? 43.878  -6.659  -18.905 1.00 58.15  ? 64  HIS A CE1 1 
ATOM   499  N  NE2 . HIS A 1 64  ? 43.843  -5.316  -18.796 1.00 56.16  ? 64  HIS A NE2 1 
ATOM   500  N  N   . ASN A 1 65  ? 38.905  -4.776  -19.182 1.00 39.61  ? 65  ASN A N   1 
ATOM   501  C  CA  . ASN A 1 65  ? 38.300  -3.507  -19.683 1.00 40.43  ? 65  ASN A CA  1 
ATOM   502  C  C   . ASN A 1 65  ? 36.783  -3.463  -19.367 1.00 37.32  ? 65  ASN A C   1 
ATOM   503  O  O   . ASN A 1 65  ? 36.194  -2.371  -19.460 1.00 37.36  ? 65  ASN A O   1 
ATOM   504  C  CB  . ASN A 1 65  ? 38.549  -3.309  -21.188 1.00 41.73  ? 65  ASN A CB  1 
ATOM   505  C  CG  . ASN A 1 65  ? 40.015  -3.176  -21.575 1.00 46.68  ? 65  ASN A CG  1 
ATOM   506  O  OD1 . ASN A 1 65  ? 40.486  -3.827  -22.506 1.00 48.58  ? 65  ASN A OD1 1 
ATOM   507  N  ND2 . ASN A 1 65  ? 40.760  -2.339  -20.878 1.00 49.95  ? 65  ASN A ND2 1 
ATOM   508  N  N   . PHE A 1 66  ? 36.157  -4.595  -19.040 1.00 36.70  ? 66  PHE A N   1 
ATOM   509  C  CA  . PHE A 1 66  ? 34.709  -4.722  -18.704 1.00 36.42  ? 66  PHE A CA  1 
ATOM   510  C  C   . PHE A 1 66  ? 34.519  -4.748  -17.182 1.00 37.56  ? 66  PHE A C   1 
ATOM   511  O  O   . PHE A 1 66  ? 34.922  -5.727  -16.574 1.00 38.81  ? 66  PHE A O   1 
ATOM   512  C  CB  . PHE A 1 66  ? 34.131  -6.021  -19.278 1.00 34.73  ? 66  PHE A CB  1 
ATOM   513  C  CG  . PHE A 1 66  ? 34.204  -6.107  -20.783 1.00 41.13  ? 66  PHE A CG  1 
ATOM   514  C  CD1 . PHE A 1 66  ? 33.443  -5.261  -21.582 1.00 41.90  ? 66  PHE A CD1 1 
ATOM   515  C  CD2 . PHE A 1 66  ? 35.050  -7.010  -21.407 1.00 43.60  ? 66  PHE A CD2 1 
ATOM   516  C  CE1 . PHE A 1 66  ? 33.527  -5.320  -22.966 1.00 44.46  ? 66  PHE A CE1 1 
ATOM   517  C  CE2 . PHE A 1 66  ? 35.146  -7.058  -22.792 1.00 44.20  ? 66  PHE A CE2 1 
ATOM   518  C  CZ  . PHE A 1 66  ? 34.383  -6.216  -23.570 1.00 44.68  ? 66  PHE A CZ  1 
ATOM   519  N  N   . LEU A 1 67  ? 33.899  -3.724  -16.607 1.00 39.43  ? 67  LEU A N   1 
ATOM   520  C  CA  . LEU A 1 67  ? 33.493  -3.670  -15.174 1.00 42.96  ? 67  LEU A CA  1 
ATOM   521  C  C   . LEU A 1 67  ? 32.017  -4.090  -15.052 1.00 40.37  ? 67  LEU A C   1 
ATOM   522  O  O   . LEU A 1 67  ? 31.117  -3.352  -15.513 1.00 39.00  ? 67  LEU A O   1 
ATOM   523  C  CB  . LEU A 1 67  ? 33.781  -2.266  -14.631 1.00 48.08  ? 67  LEU A CB  1 
ATOM   524  C  CG  . LEU A 1 67  ? 35.213  -1.789  -14.911 1.00 62.47  ? 67  LEU A CG  1 
ATOM   525  C  CD1 . LEU A 1 67  ? 35.342  -0.274  -14.845 1.00 65.43  ? 67  LEU A CD1 1 
ATOM   526  C  CD2 . LEU A 1 67  ? 36.221  -2.456  -13.973 1.00 67.78  ? 67  LEU A CD2 1 
ATOM   527  N  N   . VAL A 1 68  ? 31.798  -5.290  -14.523 1.00 37.92  ? 68  VAL A N   1 
ATOM   528  C  CA  . VAL A 1 68  ? 30.460  -5.882  -14.261 1.00 38.02  ? 68  VAL A CA  1 
ATOM   529  C  C   . VAL A 1 68  ? 30.231  -5.919  -12.750 1.00 42.82  ? 68  VAL A C   1 
ATOM   530  O  O   . VAL A 1 68  ? 31.071  -6.496  -12.021 1.00 38.09  ? 68  VAL A O   1 
ATOM   531  C  CB  . VAL A 1 68  ? 30.317  -7.286  -14.847 1.00 35.38  ? 68  VAL A CB  1 
ATOM   532  C  CG1 . VAL A 1 68  ? 28.954  -7.865  -14.503 1.00 38.33  ? 68  VAL A CG1 1 
ATOM   533  C  CG2 . VAL A 1 68  ? 30.554  -7.280  -16.350 1.00 41.04  ? 68  VAL A CG2 1 
ATOM   534  N  N   . GLN A 1 69  ? 29.085  -5.381  -12.337 1.00 38.96  ? 69  GLN A N   1 
ATOM   535  C  CA  . GLN A 1 69  ? 28.721  -5.129  -10.926 1.00 41.65  ? 69  GLN A CA  1 
ATOM   536  C  C   . GLN A 1 69  ? 27.292  -5.640  -10.686 1.00 39.70  ? 69  GLN A C   1 
ATOM   537  O  O   . GLN A 1 69  ? 26.368  -5.155  -11.366 1.00 32.57  ? 69  GLN A O   1 
ATOM   538  C  CB  . GLN A 1 69  ? 28.878  -3.636  -10.691 1.00 46.56  ? 69  GLN A CB  1 
ATOM   539  C  CG  . GLN A 1 69  ? 29.228  -3.275  -9.263  1.00 56.47  ? 69  GLN A CG  1 
ATOM   540  C  CD  . GLN A 1 69  ? 29.517  -1.798  -9.184  1.00 60.55  ? 69  GLN A CD  1 
ATOM   541  O  OE1 . GLN A 1 69  ? 30.426  -1.296  -9.847  1.00 57.85  ? 69  GLN A OE1 1 
ATOM   542  N  NE2 . GLN A 1 69  ? 28.716  -1.092  -8.398  1.00 63.50  ? 69  GLN A NE2 1 
ATOM   543  N  N   . ALA A 1 70  ? 27.141  -6.642  -9.817  1.00 40.12  ? 70  ALA A N   1 
ATOM   544  C  CA  . ALA A 1 70  ? 25.854  -7.224  -9.365  1.00 43.11  ? 70  ALA A CA  1 
ATOM   545  C  C   . ALA A 1 70  ? 25.560  -6.642  -7.982  1.00 47.60  ? 70  ALA A C   1 
ATOM   546  O  O   . ALA A 1 70  ? 26.189  -7.103  -7.004  1.00 45.63  ? 70  ALA A O   1 
ATOM   547  C  CB  . ALA A 1 70  ? 25.924  -8.735  -9.361  1.00 41.20  ? 70  ALA A CB  1 
ATOM   548  N  N   . GLY A 1 71  ? 24.710  -5.610  -7.939  1.00 44.94  ? 71  GLY A N   1 
ATOM   549  C  CA  . GLY A 1 71  ? 24.559  -4.694  -6.799  1.00 50.53  ? 71  GLY A CA  1 
ATOM   550  C  C   . GLY A 1 71  ? 25.896  -4.100  -6.394  1.00 54.91  ? 71  GLY A C   1 
ATOM   551  O  O   . GLY A 1 71  ? 26.398  -3.226  -7.115  1.00 60.47  ? 71  GLY A O   1 
ATOM   552  N  N   . ASN A 1 72  ? 26.461  -4.572  -5.282  1.00 58.41  ? 72  ASN A N   1 
ATOM   553  C  CA  . ASN A 1 72  ? 27.759  -4.102  -4.728  1.00 61.42  ? 72  ASN A CA  1 
ATOM   554  C  C   . ASN A 1 72  ? 28.904  -5.021  -5.161  1.00 58.71  ? 72  ASN A C   1 
ATOM   555  O  O   . ASN A 1 72  ? 30.049  -4.563  -5.188  1.00 65.02  ? 72  ASN A O   1 
ATOM   556  C  CB  . ASN A 1 72  ? 27.722  -4.032  -3.201  1.00 65.87  ? 72  ASN A CB  1 
ATOM   557  C  CG  . ASN A 1 72  ? 27.519  -2.625  -2.683  1.00 73.27  ? 72  ASN A CG  1 
ATOM   558  O  OD1 . ASN A 1 72  ? 27.223  -1.705  -3.447  1.00 75.45  ? 72  ASN A OD1 1 
ATOM   559  N  ND2 . ASN A 1 72  ? 27.672  -2.451  -1.381  1.00 76.70  ? 72  ASN A ND2 1 
ATOM   560  N  N   . VAL A 1 73  ? 28.614  -6.279  -5.463  1.00 58.26  ? 73  VAL A N   1 
ATOM   561  C  CA  . VAL A 1 73  ? 29.639  -7.280  -5.873  1.00 55.85  ? 73  VAL A CA  1 
ATOM   562  C  C   . VAL A 1 73  ? 30.171  -6.878  -7.258  1.00 59.45  ? 73  VAL A C   1 
ATOM   563  O  O   . VAL A 1 73  ? 29.346  -6.660  -8.168  1.00 50.51  ? 73  VAL A O   1 
ATOM   564  C  CB  . VAL A 1 73  ? 29.055  -8.710  -5.884  1.00 52.49  ? 73  VAL A CB  1 
ATOM   565  C  CG1 . VAL A 1 73  ? 30.077  -9.752  -6.341  1.00 53.36  ? 73  VAL A CG1 1 
ATOM   566  C  CG2 . VAL A 1 73  ? 28.467  -9.094  -4.532  1.00 51.28  ? 73  VAL A CG2 1 
ATOM   567  N  N   . GLN A 1 74  ? 31.495  -6.789  -7.409  1.00 52.27  ? 74  GLN A N   1 
ATOM   568  C  CA  . GLN A 1 74  ? 32.164  -6.806  -8.732  1.00 53.29  ? 74  GLN A CA  1 
ATOM   569  C  C   . GLN A 1 74  ? 32.243  -8.262  -9.180  1.00 45.10  ? 74  GLN A C   1 
ATOM   570  O  O   . GLN A 1 74  ? 32.707  -9.073  -8.412  1.00 49.00  ? 74  GLN A O   1 
ATOM   571  C  CB  . GLN A 1 74  ? 33.543  -6.149  -8.668  1.00 58.15  ? 74  GLN A CB  1 
ATOM   572  C  CG  . GLN A 1 74  ? 33.649  -4.867  -9.480  1.00 67.15  ? 74  GLN A CG  1 
ATOM   573  C  CD  . GLN A 1 74  ? 35.037  -4.263  -9.437  1.00 73.80  ? 74  GLN A CD  1 
ATOM   574  O  OE1 . GLN A 1 74  ? 35.992  -4.808  -9.994  1.00 70.65  ? 74  GLN A OE1 1 
ATOM   575  N  NE2 . GLN A 1 74  ? 35.161  -3.123  -8.770  1.00 78.21  ? 74  GLN A NE2 1 
ATOM   576  N  N   . LEU A 1 75  ? 31.756  -8.573  -10.374 1.00 44.64  ? 75  LEU A N   1 
ATOM   577  C  CA  . LEU A 1 75  ? 31.911  -9.895  -11.024 1.00 45.00  ? 75  LEU A CA  1 
ATOM   578  C  C   . LEU A 1 75  ? 33.159  -9.817  -11.904 1.00 49.33  ? 75  LEU A C   1 
ATOM   579  O  O   . LEU A 1 75  ? 33.366  -8.775  -12.559 1.00 57.08  ? 75  LEU A O   1 
ATOM   580  C  CB  . LEU A 1 75  ? 30.696  -10.233 -11.895 1.00 46.35  ? 75  LEU A CB  1 
ATOM   581  C  CG  . LEU A 1 75  ? 29.449  -10.779 -11.205 1.00 48.98  ? 75  LEU A CG  1 
ATOM   582  C  CD1 . LEU A 1 75  ? 28.327  -10.929 -12.223 1.00 45.49  ? 75  LEU A CD1 1 
ATOM   583  C  CD2 . LEU A 1 75  ? 29.729  -12.119 -10.527 1.00 50.11  ? 75  LEU A CD2 1 
ATOM   584  N  N   . ARG A 1 76  ? 33.940  -10.888 -11.941 1.00 46.63  ? 76  ARG A N   1 
ATOM   585  C  CA  . ARG A 1 76  ? 35.222  -10.928 -12.681 1.00 48.79  ? 76  ARG A CA  1 
ATOM   586  C  C   . ARG A 1 76  ? 34.923  -11.526 -14.062 1.00 40.37  ? 76  ARG A C   1 
ATOM   587  O  O   . ARG A 1 76  ? 34.342  -12.629 -14.122 1.00 34.24  ? 76  ARG A O   1 
ATOM   588  C  CB  . ARG A 1 76  ? 36.236  -11.705 -11.833 1.00 55.68  ? 76  ARG A CB  1 
ATOM   589  C  CG  . ARG A 1 76  ? 37.661  -11.703 -12.368 1.00 63.92  ? 76  ARG A CG  1 
ATOM   590  C  CD  . ARG A 1 76  ? 38.655  -12.397 -11.447 1.00 67.94  ? 76  ARG A CD  1 
ATOM   591  N  NE  . ARG A 1 76  ? 39.539  -13.270 -12.220 1.00 73.04  ? 76  ARG A NE  1 
ATOM   592  C  CZ  . ARG A 1 76  ? 39.465  -14.604 -12.284 1.00 77.97  ? 76  ARG A CZ  1 
ATOM   593  N  NH1 . ARG A 1 76  ? 38.554  -15.274 -11.587 1.00 78.83  ? 76  ARG A NH1 1 
ATOM   594  N  NH2 . ARG A 1 76  ? 40.322  -15.269 -13.046 1.00 73.03  ? 76  ARG A NH2 1 
ATOM   595  N  N   . VAL A 1 77  ? 35.234  -10.799 -15.134 1.00 37.67  ? 77  VAL A N   1 
ATOM   596  C  CA  . VAL A 1 77  ? 35.049  -11.316 -16.521 1.00 36.90  ? 77  VAL A CA  1 
ATOM   597  C  C   . VAL A 1 77  ? 36.254  -12.193 -16.853 1.00 37.93  ? 77  VAL A C   1 
ATOM   598  O  O   . VAL A 1 77  ? 37.366  -11.717 -16.642 1.00 38.30  ? 77  VAL A O   1 
ATOM   599  C  CB  . VAL A 1 77  ? 34.891  -10.166 -17.529 1.00 40.41  ? 77  VAL A CB  1 
ATOM   600  C  CG1 . VAL A 1 77  ? 34.915  -10.661 -18.970 1.00 39.47  ? 77  VAL A CG1 1 
ATOM   601  C  CG2 . VAL A 1 77  ? 33.634  -9.347  -17.251 1.00 41.99  ? 77  VAL A CG2 1 
ATOM   602  N  N   . ILE A 1 78  ? 36.024  -13.397 -17.380 1.00 39.96  ? 78  ILE A N   1 
ATOM   603  C  CA  . ILE A 1 78  ? 37.089  -14.391 -17.716 1.00 44.26  ? 78  ILE A CA  1 
ATOM   604  C  C   . ILE A 1 78  ? 37.015  -14.800 -19.199 1.00 45.38  ? 78  ILE A C   1 
ATOM   605  O  O   . ILE A 1 78  ? 37.835  -15.619 -19.633 1.00 35.43  ? 78  ILE A O   1 
ATOM   606  C  CB  . ILE A 1 78  ? 36.983  -15.611 -16.776 1.00 44.22  ? 78  ILE A CB  1 
ATOM   607  C  CG1 . ILE A 1 78  ? 35.750  -16.471 -17.056 1.00 43.96  ? 78  ILE A CG1 1 
ATOM   608  C  CG2 . ILE A 1 78  ? 37.020  -15.160 -15.324 1.00 47.40  ? 78  ILE A CG2 1 
ATOM   609  C  CD1 . ILE A 1 78  ? 35.618  -17.639 -16.120 1.00 42.28  ? 78  ILE A CD1 1 
ATOM   610  N  N   . GLY A 1 79  ? 36.067  -14.260 -19.963 1.00 42.06  ? 79  GLY A N   1 
ATOM   611  C  CA  . GLY A 1 79  ? 35.950  -14.530 -21.408 1.00 43.50  ? 79  GLY A CA  1 
ATOM   612  C  C   . GLY A 1 79  ? 34.992  -13.543 -22.046 1.00 42.15  ? 79  GLY A C   1 
ATOM   613  O  O   . GLY A 1 79  ? 34.176  -12.952 -21.323 1.00 39.17  ? 79  GLY A O   1 
ATOM   614  N  N   . HIS A 1 80  ? 35.101  -13.324 -23.348 1.00 42.74  ? 80  HIS A N   1 
ATOM   615  C  CA  . HIS A 1 80  ? 34.142  -12.460 -24.081 1.00 39.11  ? 80  HIS A CA  1 
ATOM   616  C  C   . HIS A 1 80  ? 34.091  -12.930 -25.523 1.00 42.53  ? 80  HIS A C   1 
ATOM   617  O  O   . HIS A 1 80  ? 35.136  -13.291 -26.058 1.00 37.10  ? 80  HIS A O   1 
ATOM   618  C  CB  . HIS A 1 80  ? 34.517  -10.988 -23.948 1.00 37.47  ? 80  HIS A CB  1 
ATOM   619  C  CG  . HIS A 1 80  ? 35.828  -10.629 -24.570 1.00 44.32  ? 80  HIS A CG  1 
ATOM   620  N  ND1 . HIS A 1 80  ? 36.945  -10.311 -23.817 1.00 49.41  ? 80  HIS A ND1 1 
ATOM   621  C  CD2 . HIS A 1 80  ? 36.204  -10.492 -25.861 1.00 45.47  ? 80  HIS A CD2 1 
ATOM   622  C  CE1 . HIS A 1 80  ? 37.949  -10.003 -24.621 1.00 49.99  ? 80  HIS A CE1 1 
ATOM   623  N  NE2 . HIS A 1 80  ? 37.514  -10.089 -25.878 1.00 45.41  ? 80  HIS A NE2 1 
ATOM   624  N  N   . SER A 1 81  ? 32.890  -12.970 -26.083 1.00 36.97  ? 81  SER A N   1 
ATOM   625  C  CA  . SER A 1 81  ? 32.642  -13.225 -27.510 1.00 35.77  ? 81  SER A CA  1 
ATOM   626  C  C   . SER A 1 81  ? 31.406  -12.437 -27.913 1.00 35.67  ? 81  SER A C   1 
ATOM   627  O  O   . SER A 1 81  ? 30.614  -12.046 -27.048 1.00 34.10  ? 81  SER A O   1 
ATOM   628  C  CB  . SER A 1 81  ? 32.420  -14.680 -27.773 1.00 36.91  ? 81  SER A CB  1 
ATOM   629  O  OG  . SER A 1 81  ? 31.159  -15.084 -27.263 1.00 35.53  ? 81  SER A OG  1 
ATOM   630  N  N   . MET A 1 82  ? 31.222  -12.334 -29.202 1.00 33.47  ? 82  MET A N   1 
ATOM   631  C  CA  . MET A 1 82  ? 30.111  -11.612 -29.824 1.00 34.34  ? 82  MET A CA  1 
ATOM   632  C  C   . MET A 1 82  ? 29.221  -12.651 -30.492 1.00 32.66  ? 82  MET A C   1 
ATOM   633  O  O   . MET A 1 82  ? 29.739  -13.563 -31.126 1.00 32.21  ? 82  MET A O   1 
ATOM   634  C  CB  . MET A 1 82  ? 30.724  -10.679 -30.859 1.00 36.03  ? 82  MET A CB  1 
ATOM   635  C  CG  . MET A 1 82  ? 29.767  -9.739  -31.494 1.00 38.80  ? 82  MET A CG  1 
ATOM   636  S  SD  . MET A 1 82  ? 30.704  -8.280  -31.955 1.00 36.14  ? 82  MET A SD  1 
ATOM   637  C  CE  . MET A 1 82  ? 31.758  -8.930  -33.255 1.00 37.03  ? 82  MET A CE  1 
ATOM   638  N  N   . GLN A 1 83  ? 27.914  -12.530 -30.346 1.00 30.64  ? 83  GLN A N   1 
ATOM   639  C  CA  . GLN A 1 83  ? 26.975  -13.287 -31.189 1.00 29.64  ? 83  GLN A CA  1 
ATOM   640  C  C   . GLN A 1 83  ? 26.030  -12.256 -31.797 1.00 29.24  ? 83  GLN A C   1 
ATOM   641  O  O   . GLN A 1 83  ? 25.189  -11.707 -31.048 1.00 25.03  ? 83  GLN A O   1 
ATOM   642  C  CB  . GLN A 1 83  ? 26.240  -14.358 -30.375 1.00 31.56  ? 83  GLN A CB  1 
ATOM   643  C  CG  . GLN A 1 83  ? 25.237  -15.163 -31.200 1.00 30.40  ? 83  GLN A CG  1 
ATOM   644  C  CD  . GLN A 1 83  ? 24.468  -16.102 -30.307 1.00 29.87  ? 83  GLN A CD  1 
ATOM   645  O  OE1 . GLN A 1 83  ? 24.659  -16.115 -29.092 1.00 32.73  ? 83  GLN A OE1 1 
ATOM   646  N  NE2 . GLN A 1 83  ? 23.611  -16.910 -30.901 1.00 32.66  ? 83  GLN A NE2 1 
ATOM   647  N  N   . ASN A 1 84  ? 26.208  -11.999 -33.090 1.00 25.62  ? 84  ASN A N   1 
ATOM   648  C  CA  . ASN A 1 84  ? 25.409  -11.003 -33.833 1.00 25.67  ? 84  ASN A CA  1 
ATOM   649  C  C   . ASN A 1 84  ? 25.633  -9.681  -33.110 1.00 23.71  ? 84  ASN A C   1 
ATOM   650  O  O   . ASN A 1 84  ? 26.794  -9.336  -32.978 1.00 22.25  ? 84  ASN A O   1 
ATOM   651  C  CB  . ASN A 1 84  ? 23.963  -11.490 -33.956 1.00 23.92  ? 84  ASN A CB  1 
ATOM   652  C  CG  . ASN A 1 84  ? 23.905  -12.816 -34.670 1.00 24.92  ? 84  ASN A CG  1 
ATOM   653  O  OD1 . ASN A 1 84  ? 24.375  -12.916 -35.791 1.00 29.27  ? 84  ASN A OD1 1 
ATOM   654  N  ND2 . ASN A 1 84  ? 23.302  -13.825 -34.072 1.00 24.56  ? 84  ASN A ND2 1 
ATOM   655  N  N   . CYS A 1 85  ? 24.580  -9.013  -32.600 1.00 23.84  ? 85  CYS A N   1 
ATOM   656  C  CA  . CYS A 1 85  ? 24.690  -7.658  -31.990 1.00 21.89  ? 85  CYS A CA  1 
ATOM   657  C  C   . CYS A 1 85  ? 24.731  -7.735  -30.457 1.00 21.50  ? 85  CYS A C   1 
ATOM   658  O  O   . CYS A 1 85  ? 24.617  -6.701  -29.796 1.00 20.07  ? 85  CYS A O   1 
ATOM   659  C  CB  . CYS A 1 85  ? 23.530  -6.784  -32.451 1.00 22.62  ? 85  CYS A CB  1 
ATOM   660  S  SG  . CYS A 1 85  ? 23.546  -6.527  -34.237 1.00 23.95  ? 85  CYS A SG  1 
ATOM   661  N  N   . VAL A 1 86  ? 24.852  -8.936  -29.903 1.00 23.33  ? 86  VAL A N   1 
ATOM   662  C  CA  . VAL A 1 86  ? 24.920  -9.116  -28.430 1.00 25.38  ? 86  VAL A CA  1 
ATOM   663  C  C   . VAL A 1 86  ? 26.333  -9.533  -28.027 1.00 26.29  ? 86  VAL A C   1 
ATOM   664  O  O   . VAL A 1 86  ? 26.972  -10.362 -28.726 1.00 21.98  ? 86  VAL A O   1 
ATOM   665  C  CB  . VAL A 1 86  ? 23.826  -10.092 -27.978 1.00 27.83  ? 86  VAL A CB  1 
ATOM   666  C  CG1 . VAL A 1 86  ? 24.178  -10.784 -26.695 1.00 30.47  ? 86  VAL A CG1 1 
ATOM   667  C  CG2 . VAL A 1 86  ? 22.486  -9.342  -27.878 1.00 29.55  ? 86  VAL A CG2 1 
ATOM   668  N  N   . LEU A 1 87  ? 26.807  -8.917  -26.956 1.00 25.38  ? 87  LEU A N   1 
ATOM   669  C  CA  . LEU A 1 87  ? 28.095  -9.263  -26.325 1.00 28.66  ? 87  LEU A CA  1 
ATOM   670  C  C   . LEU A 1 87  ? 27.817  -10.230 -25.169 1.00 29.36  ? 87  LEU A C   1 
ATOM   671  O  O   . LEU A 1 87  ? 26.838  -10.029 -24.426 1.00 26.18  ? 87  LEU A O   1 
ATOM   672  C  CB  . LEU A 1 87  ? 28.715  -7.956  -25.855 1.00 31.43  ? 87  LEU A CB  1 
ATOM   673  C  CG  . LEU A 1 87  ? 30.114  -8.077  -25.273 1.00 37.46  ? 87  LEU A CG  1 
ATOM   674  C  CD1 . LEU A 1 87  ? 31.121  -8.469  -26.344 1.00 41.32  ? 87  LEU A CD1 1 
ATOM   675  C  CD2 . LEU A 1 87  ? 30.493  -6.760  -24.620 1.00 40.34  ? 87  LEU A CD2 1 
ATOM   676  N  N   . LYS A 1 88  ? 28.610  -11.292 -25.072 1.00 30.68  ? 88  LYS A N   1 
ATOM   677  C  CA  . LYS A 1 88  ? 28.483  -12.341 -24.037 1.00 31.49  ? 88  LYS A CA  1 
ATOM   678  C  C   . LYS A 1 88  ? 29.766  -12.351 -23.231 1.00 33.11  ? 88  LYS A C   1 
ATOM   679  O  O   . LYS A 1 88  ? 30.774  -12.813 -23.784 1.00 34.82  ? 88  LYS A O   1 
ATOM   680  C  CB  . LYS A 1 88  ? 28.243  -13.707 -24.659 1.00 29.45  ? 88  LYS A CB  1 
ATOM   681  C  CG  . LYS A 1 88  ? 27.015  -13.744 -25.549 1.00 32.27  ? 88  LYS A CG  1 
ATOM   682  C  CD  . LYS A 1 88  ? 26.454  -15.131 -25.808 1.00 33.26  ? 88  LYS A CD  1 
ATOM   683  C  CE  . LYS A 1 88  ? 27.206  -15.830 -26.918 1.00 38.11  ? 88  LYS A CE  1 
ATOM   684  N  NZ  . LYS A 1 88  ? 26.410  -16.927 -27.508 1.00 42.83  ? 88  LYS A NZ  1 
ATOM   685  N  N   . LEU A 1 89  ? 29.714  -11.786 -22.028 1.00 31.71  ? 89  LEU A N   1 
ATOM   686  C  CA  . LEU A 1 89  ? 30.821  -11.769 -21.049 1.00 31.92  ? 89  LEU A CA  1 
ATOM   687  C  C   . LEU A 1 89  ? 30.720  -12.998 -20.164 1.00 37.25  ? 89  LEU A C   1 
ATOM   688  O  O   . LEU A 1 89  ? 29.726  -13.102 -19.396 1.00 35.48  ? 89  LEU A O   1 
ATOM   689  C  CB  . LEU A 1 89  ? 30.708  -10.507 -20.216 1.00 32.84  ? 89  LEU A CB  1 
ATOM   690  C  CG  . LEU A 1 89  ? 30.608  -9.253  -21.060 1.00 31.02  ? 89  LEU A CG  1 
ATOM   691  C  CD1 . LEU A 1 89  ? 30.616  -8.031  -20.186 1.00 31.45  ? 89  LEU A CD1 1 
ATOM   692  C  CD2 . LEU A 1 89  ? 31.753  -9.221  -22.049 1.00 32.10  ? 89  LEU A CD2 1 
ATOM   693  N  N   . LYS A 1 90  ? 31.722  -13.875 -20.245 1.00 37.67  ? 90  LYS A N   1 
ATOM   694  C  CA  . LYS A 1 90  ? 31.826  -15.011 -19.299 1.00 42.57  ? 90  LYS A CA  1 
ATOM   695  C  C   . LYS A 1 90  ? 32.346  -14.446 -17.979 1.00 39.71  ? 90  LYS A C   1 
ATOM   696  O  O   . LYS A 1 90  ? 33.258  -13.572 -18.007 1.00 36.82  ? 90  LYS A O   1 
ATOM   697  C  CB  . LYS A 1 90  ? 32.693  -16.132 -19.861 1.00 49.79  ? 90  LYS A CB  1 
ATOM   698  C  CG  . LYS A 1 90  ? 32.525  -17.456 -19.145 1.00 57.62  ? 90  LYS A CG  1 
ATOM   699  C  CD  . LYS A 1 90  ? 33.400  -18.515 -19.736 1.00 66.24  ? 90  LYS A CD  1 
ATOM   700  C  CE  . LYS A 1 90  ? 33.143  -19.881 -19.141 1.00 74.99  ? 90  LYS A CE  1 
ATOM   701  N  NZ  . LYS A 1 90  ? 34.032  -20.894 -19.755 1.00 78.71  ? 90  LYS A NZ  1 
ATOM   702  N  N   . VAL A 1 91  ? 31.713  -14.856 -16.877 1.00 38.73  ? 91  VAL A N   1 
ATOM   703  C  CA  . VAL A 1 91  ? 32.110  -14.442 -15.503 1.00 40.34  ? 91  VAL A CA  1 
ATOM   704  C  C   . VAL A 1 91  ? 32.476  -15.692 -14.695 1.00 40.18  ? 91  VAL A C   1 
ATOM   705  O  O   . VAL A 1 91  ? 32.117  -16.814 -15.126 1.00 40.90  ? 91  VAL A O   1 
ATOM   706  C  CB  . VAL A 1 91  ? 31.020  -13.591 -14.829 1.00 43.92  ? 91  VAL A CB  1 
ATOM   707  C  CG1 . VAL A 1 91  ? 30.904  -12.243 -15.523 1.00 50.33  ? 91  VAL A CG1 1 
ATOM   708  C  CG2 . VAL A 1 91  ? 29.669  -14.297 -14.785 1.00 46.04  ? 91  VAL A CG2 1 
ATOM   709  N  N   . ASP A 1 92  ? 33.203  -15.491 -13.592 1.00 45.42  ? 92  ASP A N   1 
ATOM   710  C  CA  . ASP A 1 92  ? 33.762  -16.583 -12.741 1.00 52.24  ? 92  ASP A CA  1 
ATOM   711  C  C   . ASP A 1 92  ? 32.702  -17.107 -11.758 1.00 54.00  ? 92  ASP A C   1 
ATOM   712  O  O   . ASP A 1 92  ? 32.988  -18.101 -11.097 1.00 50.54  ? 92  ASP A O   1 
ATOM   713  C  CB  . ASP A 1 92  ? 35.018  -16.127 -11.992 1.00 53.06  ? 92  ASP A CB  1 
ATOM   714  C  CG  . ASP A 1 92  ? 34.779  -15.016 -10.982 1.00 58.03  ? 92  ASP A CG  1 
ATOM   715  O  OD1 . ASP A 1 92  ? 33.657  -14.430 -10.966 1.00 58.87  ? 92  ASP A OD1 1 
ATOM   716  O  OD2 . ASP A 1 92  ? 35.717  -14.733 -10.221 1.00 59.13  ? 92  ASP A OD2 1 
ATOM   717  N  N   . THR A 1 93  ? 31.524  -16.473 -11.668 1.00 50.38  ? 93  THR A N   1 
ATOM   718  C  CA  . THR A 1 93  ? 30.403  -16.909 -10.794 1.00 42.85  ? 93  THR A CA  1 
ATOM   719  C  C   . THR A 1 93  ? 29.153  -17.134 -11.639 1.00 39.52  ? 93  THR A C   1 
ATOM   720  O  O   . THR A 1 93  ? 28.828  -16.261 -12.468 1.00 35.09  ? 93  THR A O   1 
ATOM   721  C  CB  . THR A 1 93  ? 30.067  -15.850 -9.742  1.00 46.70  ? 93  THR A CB  1 
ATOM   722  O  OG1 . THR A 1 93  ? 31.290  -15.370 -9.187  1.00 47.55  ? 93  THR A OG1 1 
ATOM   723  C  CG2 . THR A 1 93  ? 29.158  -16.382 -8.655  1.00 47.78  ? 93  THR A CG2 1 
ATOM   724  N  N   . ALA A 1 94  ? 28.484  -18.260 -11.437 1.00 34.95  ? 94  ALA A N   1 
ATOM   725  C  CA  . ALA A 1 94  ? 27.135  -18.518 -11.963 1.00 36.18  ? 94  ALA A CA  1 
ATOM   726  C  C   . ALA A 1 94  ? 26.156  -17.772 -11.062 1.00 35.48  ? 94  ALA A C   1 
ATOM   727  O  O   . ALA A 1 94  ? 26.390  -17.697 -9.839  1.00 37.56  ? 94  ALA A O   1 
ATOM   728  C  CB  . ALA A 1 94  ? 26.810  -19.984 -12.027 1.00 39.45  ? 94  ALA A CB  1 
ATOM   729  N  N   . ASN A 1 95  ? 25.145  -17.164 -11.665 1.00 35.41  ? 95  ASN A N   1 
ATOM   730  C  CA  . ASN A 1 95  ? 24.149  -16.354 -10.925 1.00 32.95  ? 95  ASN A CA  1 
ATOM   731  C  C   . ASN A 1 95  ? 23.301  -17.328 -10.117 1.00 29.46  ? 95  ASN A C   1 
ATOM   732  O  O   . ASN A 1 95  ? 22.580  -18.156 -10.680 1.00 27.58  ? 95  ASN A O   1 
ATOM   733  C  CB  . ASN A 1 95  ? 23.317  -15.518 -11.895 1.00 33.94  ? 95  ASN A CB  1 
ATOM   734  C  CG  . ASN A 1 95  ? 22.272  -14.684 -11.190 1.00 36.32  ? 95  ASN A CG  1 
ATOM   735  O  OD1 . ASN A 1 95  ? 22.278  -14.605 -9.960  1.00 29.96  ? 95  ASN A OD1 1 
ATOM   736  N  ND2 . ASN A 1 95  ? 21.387  -14.072 -11.974 1.00 36.13  ? 95  ASN A ND2 1 
ATOM   737  N  N   . PRO A 1 96  ? 23.344  -17.278 -8.773  1.00 32.14  ? 96  PRO A N   1 
ATOM   738  C  CA  . PRO A 1 96  ? 22.559  -18.225 -7.975  1.00 34.71  ? 96  PRO A CA  1 
ATOM   739  C  C   . PRO A 1 96  ? 21.045  -17.987 -8.118  1.00 35.85  ? 96  PRO A C   1 
ATOM   740  O  O   . PRO A 1 96  ? 20.278  -18.905 -7.870  1.00 35.91  ? 96  PRO A O   1 
ATOM   741  C  CB  . PRO A 1 96  ? 23.051  -17.984 -6.548  1.00 34.39  ? 96  PRO A CB  1 
ATOM   742  C  CG  . PRO A 1 96  ? 23.569  -16.565 -6.554  1.00 34.13  ? 96  PRO A CG  1 
ATOM   743  C  CD  . PRO A 1 96  ? 24.081  -16.303 -7.956  1.00 32.77  ? 96  PRO A CD  1 
ATOM   744  N  N   . LYS A 1 97  ? 20.641  -16.816 -8.624  1.00 36.40  ? 97  LYS A N   1 
ATOM   745  C  CA  . LYS A 1 97  ? 19.203  -16.468 -8.826  1.00 38.29  ? 97  LYS A CA  1 
ATOM   746  C  C   . LYS A 1 97  ? 18.742  -16.800 -10.252 1.00 39.30  ? 97  LYS A C   1 
ATOM   747  O  O   . LYS A 1 97  ? 17.588  -16.414 -10.610 1.00 31.74  ? 97  LYS A O   1 
ATOM   748  C  CB  . LYS A 1 97  ? 18.977  -14.976 -8.574  1.00 37.94  ? 97  LYS A CB  1 
ATOM   749  C  CG  . LYS A 1 97  ? 19.346  -14.487 -7.184  1.00 40.72  ? 97  LYS A CG  1 
ATOM   750  C  CD  . LYS A 1 97  ? 19.039  -13.018 -6.992  1.00 44.11  ? 97  LYS A CD  1 
ATOM   751  C  CE  . LYS A 1 97  ? 19.439  -12.483 -5.632  1.00 49.33  ? 97  LYS A CE  1 
ATOM   752  N  NZ  . LYS A 1 97  ? 18.534  -11.389 -5.206  1.00 55.20  ? 97  LYS A NZ  1 
ATOM   753  N  N   . THR A 1 98  ? 19.575  -17.460 -11.066 1.00 34.55  ? 98  THR A N   1 
ATOM   754  C  CA  . THR A 1 98  ? 19.183  -17.810 -12.455 1.00 32.45  ? 98  THR A CA  1 
ATOM   755  C  C   . THR A 1 98  ? 17.890  -18.605 -12.414 1.00 31.15  ? 98  THR A C   1 
ATOM   756  O  O   . THR A 1 98  ? 17.843  -19.626 -11.767 1.00 36.40  ? 98  THR A O   1 
ATOM   757  C  CB  . THR A 1 98  ? 20.269  -18.606 -13.189 1.00 31.58  ? 98  THR A CB  1 
ATOM   758  O  OG1 . THR A 1 98  ? 21.449  -17.818 -13.145 1.00 29.65  ? 98  THR A OG1 1 
ATOM   759  C  CG2 . THR A 1 98  ? 19.921  -18.898 -14.630 1.00 32.70  ? 98  THR A CG2 1 
ATOM   760  N  N   . PRO A 1 99  ? 16.798  -18.185 -13.086 1.00 30.54  ? 99  PRO A N   1 
ATOM   761  C  CA  . PRO A 1 99  ? 15.591  -19.002 -13.142 1.00 30.54  ? 99  PRO A CA  1 
ATOM   762  C  C   . PRO A 1 99  ? 15.609  -20.009 -14.300 1.00 33.19  ? 99  PRO A C   1 
ATOM   763  O  O   . PRO A 1 99  ? 16.500  -19.972 -15.114 1.00 33.72  ? 99  PRO A O   1 
ATOM   764  C  CB  . PRO A 1 99  ? 14.501  -17.949 -13.373 1.00 31.17  ? 99  PRO A CB  1 
ATOM   765  C  CG  . PRO A 1 99  ? 15.206  -16.928 -14.256 1.00 33.00  ? 99  PRO A CG  1 
ATOM   766  C  CD  . PRO A 1 99  ? 16.641  -16.894 -13.774 1.00 31.97  ? 99  PRO A CD  1 
ATOM   767  N  N   . LYS A 1 100 ? 14.611  -20.877 -14.360 1.00 32.48  ? 100 LYS A N   1 
ATOM   768  C  CA  . LYS A 1 100 ? 14.357  -21.627 -15.599 1.00 36.22  ? 100 LYS A CA  1 
ATOM   769  C  C   . LYS A 1 100 ? 14.098  -20.559 -16.659 1.00 33.74  ? 100 LYS A C   1 
ATOM   770  O  O   . LYS A 1 100 ? 13.269  -19.666 -16.433 1.00 29.66  ? 100 LYS A O   1 
ATOM   771  C  CB  . LYS A 1 100 ? 13.169  -22.574 -15.479 1.00 42.76  ? 100 LYS A CB  1 
ATOM   772  C  CG  . LYS A 1 100 ? 13.199  -23.517 -14.287 1.00 55.43  ? 100 LYS A CG  1 
ATOM   773  C  CD  . LYS A 1 100 ? 12.017  -24.462 -14.276 1.00 60.69  ? 100 LYS A CD  1 
ATOM   774  C  CE  . LYS A 1 100 ? 12.353  -25.839 -13.737 1.00 67.85  ? 100 LYS A CE  1 
ATOM   775  N  NZ  . LYS A 1 100 ? 11.309  -26.826 -14.107 1.00 70.33  ? 100 LYS A NZ  1 
ATOM   776  N  N   . TYR A 1 101 ? 14.835  -20.601 -17.751 1.00 31.34  ? 101 TYR A N   1 
ATOM   777  C  CA  . TYR A 1 101 ? 14.676  -19.608 -18.840 1.00 31.22  ? 101 TYR A CA  1 
ATOM   778  C  C   . TYR A 1 101 ? 14.905  -20.261 -20.183 1.00 33.10  ? 101 TYR A C   1 
ATOM   779  O  O   . TYR A 1 101 ? 15.493  -21.316 -20.238 1.00 31.81  ? 101 TYR A O   1 
ATOM   780  C  CB  . TYR A 1 101 ? 15.672  -18.470 -18.700 1.00 26.79  ? 101 TYR A CB  1 
ATOM   781  C  CG  . TYR A 1 101 ? 17.111  -18.812 -18.987 1.00 30.47  ? 101 TYR A CG  1 
ATOM   782  C  CD1 . TYR A 1 101 ? 17.656  -18.639 -20.254 1.00 31.22  ? 101 TYR A CD1 1 
ATOM   783  C  CD2 . TYR A 1 101 ? 17.942  -19.280 -17.988 1.00 29.87  ? 101 TYR A CD2 1 
ATOM   784  C  CE1 . TYR A 1 101 ? 18.980  -18.962 -20.521 1.00 29.75  ? 101 TYR A CE1 1 
ATOM   785  C  CE2 . TYR A 1 101 ? 19.273  -19.581 -18.232 1.00 33.92  ? 101 TYR A CE2 1 
ATOM   786  C  CZ  . TYR A 1 101 ? 19.800  -19.406 -19.500 1.00 32.34  ? 101 TYR A CZ  1 
ATOM   787  O  OH  . TYR A 1 101 ? 21.123  -19.690 -19.716 1.00 32.92  ? 101 TYR A OH  1 
ATOM   788  N  N   . LYS A 1 102 ? 14.458  -19.582 -21.223 1.00 32.30  ? 102 LYS A N   1 
ATOM   789  C  CA  . LYS A 1 102 ? 14.740  -19.921 -22.625 1.00 33.02  ? 102 LYS A CA  1 
ATOM   790  C  C   . LYS A 1 102 ? 14.825  -18.603 -23.390 1.00 30.94  ? 102 LYS A C   1 
ATOM   791  O  O   . LYS A 1 102 ? 14.344  -17.555 -22.853 1.00 27.60  ? 102 LYS A O   1 
ATOM   792  C  CB  . LYS A 1 102 ? 13.650  -20.817 -23.208 1.00 36.74  ? 102 LYS A CB  1 
ATOM   793  C  CG  . LYS A 1 102 ? 12.266  -20.185 -23.285 1.00 44.22  ? 102 LYS A CG  1 
ATOM   794  C  CD  . LYS A 1 102 ? 11.209  -21.132 -23.806 1.00 48.74  ? 102 LYS A CD  1 
ATOM   795  C  CE  . LYS A 1 102 ? 11.120  -22.387 -22.973 1.00 52.69  ? 102 LYS A CE  1 
ATOM   796  N  NZ  . LYS A 1 102 ? 9.991   -23.226 -23.422 1.00 63.13  ? 102 LYS A NZ  1 
ATOM   797  N  N   . PHE A 1 103 ? 15.376  -18.666 -24.597 1.00 27.28  ? 103 PHE A N   1 
ATOM   798  C  CA  . PHE A 1 103 ? 15.426  -17.531 -25.544 1.00 27.53  ? 103 PHE A CA  1 
ATOM   799  C  C   . PHE A 1 103 ? 14.484  -17.832 -26.675 1.00 29.62  ? 103 PHE A C   1 
ATOM   800  O  O   . PHE A 1 103 ? 14.597  -18.920 -27.251 1.00 30.46  ? 103 PHE A O   1 
ATOM   801  C  CB  . PHE A 1 103 ? 16.826  -17.304 -26.091 1.00 27.98  ? 103 PHE A CB  1 
ATOM   802  C  CG  . PHE A 1 103 ? 17.849  -16.906 -25.068 1.00 27.71  ? 103 PHE A CG  1 
ATOM   803  C  CD1 . PHE A 1 103 ? 17.471  -16.459 -23.805 1.00 28.61  ? 103 PHE A CD1 1 
ATOM   804  C  CD2 . PHE A 1 103 ? 19.191  -16.951 -25.376 1.00 27.61  ? 103 PHE A CD2 1 
ATOM   805  C  CE1 . PHE A 1 103 ? 18.413  -16.092 -22.869 1.00 25.89  ? 103 PHE A CE1 1 
ATOM   806  C  CE2 . PHE A 1 103 ? 20.134  -16.566 -24.436 1.00 27.45  ? 103 PHE A CE2 1 
ATOM   807  C  CZ  . PHE A 1 103 ? 19.742  -16.133 -23.191 1.00 28.29  ? 103 PHE A CZ  1 
ATOM   808  N  N   . VAL A 1 104 ? 13.573  -16.902 -26.955 1.00 28.98  ? 104 VAL A N   1 
ATOM   809  C  CA  . VAL A 1 104 ? 12.611  -17.075 -28.067 1.00 30.63  ? 104 VAL A CA  1 
ATOM   810  C  C   . VAL A 1 104 ? 12.583  -15.763 -28.848 1.00 25.71  ? 104 VAL A C   1 
ATOM   811  O  O   . VAL A 1 104 ? 12.531  -14.692 -28.232 1.00 28.09  ? 104 VAL A O   1 
ATOM   812  C  CB  . VAL A 1 104 ? 11.198  -17.483 -27.592 1.00 35.73  ? 104 VAL A CB  1 
ATOM   813  C  CG1 . VAL A 1 104 ? 11.188  -18.804 -26.831 1.00 41.31  ? 104 VAL A CG1 1 
ATOM   814  C  CG2 . VAL A 1 104 ? 10.573  -16.411 -26.732 1.00 38.15  ? 104 VAL A CG2 1 
ATOM   815  N  N   . ARG A 1 105 ? 12.568  -15.882 -30.159 1.00 23.46  ? 105 ARG A N   1 
ATOM   816  C  CA  . ARG A 1 105 ? 12.316  -14.762 -31.087 1.00 24.37  ? 105 ARG A CA  1 
ATOM   817  C  C   . ARG A 1 105 ? 10.826  -14.706 -31.358 1.00 26.29  ? 105 ARG A C   1 
ATOM   818  O  O   . ARG A 1 105 ? 10.298  -15.728 -31.795 1.00 32.17  ? 105 ARG A O   1 
ATOM   819  C  CB  . ARG A 1 105 ? 13.050  -14.963 -32.407 1.00 23.47  ? 105 ARG A CB  1 
ATOM   820  C  CG  . ARG A 1 105 ? 13.054  -13.712 -33.278 1.00 23.49  ? 105 ARG A CG  1 
ATOM   821  C  CD  . ARG A 1 105 ? 13.813  -13.974 -34.559 1.00 22.54  ? 105 ARG A CD  1 
ATOM   822  N  NE  . ARG A 1 105 ? 13.751  -12.809 -35.417 1.00 23.41  ? 105 ARG A NE  1 
ATOM   823  C  CZ  . ARG A 1 105 ? 14.470  -11.708 -35.232 1.00 23.93  ? 105 ARG A CZ  1 
ATOM   824  N  NH1 . ARG A 1 105 ? 15.312  -11.612 -34.214 1.00 26.41  ? 105 ARG A NH1 1 
ATOM   825  N  NH2 . ARG A 1 105 ? 14.313  -10.699 -36.053 1.00 23.66  ? 105 ARG A NH2 1 
ATOM   826  N  N   . ILE A 1 106 ? 10.199  -13.546 -31.168 1.00 26.40  ? 106 ILE A N   1 
ATOM   827  C  CA  . ILE A 1 106 ? 8.721   -13.410 -31.334 1.00 23.80  ? 106 ILE A CA  1 
ATOM   828  C  C   . ILE A 1 106 ? 8.392   -12.826 -32.710 1.00 24.66  ? 106 ILE A C   1 
ATOM   829  O  O   . ILE A 1 106 ? 9.294   -12.324 -33.403 1.00 25.95  ? 106 ILE A O   1 
ATOM   830  C  CB  . ILE A 1 106 ? 8.121   -12.577 -30.186 1.00 24.45  ? 106 ILE A CB  1 
ATOM   831  C  CG1 . ILE A 1 106 ? 8.795   -11.202 -30.065 1.00 26.54  ? 106 ILE A CG1 1 
ATOM   832  C  CG2 . ILE A 1 106 ? 8.207   -13.341 -28.876 1.00 26.80  ? 106 ILE A CG2 1 
ATOM   833  C  CD1 . ILE A 1 106 ? 8.103   -10.242 -29.108 1.00 26.35  ? 106 ILE A CD1 1 
ATOM   834  N  N   . GLN A 1 107 ? 7.117   -12.893 -33.089 1.00 23.74  ? 107 GLN A N   1 
ATOM   835  C  CA  . GLN A 1 107 ? 6.581   -12.281 -34.322 1.00 26.10  ? 107 GLN A CA  1 
ATOM   836  C  C   . GLN A 1 107 ? 5.831   -10.997 -33.983 1.00 22.78  ? 107 GLN A C   1 
ATOM   837  O  O   . GLN A 1 107 ? 5.369   -10.798 -32.862 1.00 19.98  ? 107 GLN A O   1 
ATOM   838  C  CB  . GLN A 1 107 ? 5.670   -13.285 -35.032 1.00 29.55  ? 107 GLN A CB  1 
ATOM   839  C  CG  . GLN A 1 107 ? 6.388   -14.587 -35.377 1.00 31.85  ? 107 GLN A CG  1 
ATOM   840  C  CD  . GLN A 1 107 ? 7.459   -14.358 -36.405 1.00 36.11  ? 107 GLN A CD  1 
ATOM   841  O  OE1 . GLN A 1 107 ? 7.212   -13.737 -37.430 1.00 36.72  ? 107 GLN A OE1 1 
ATOM   842  N  NE2 . GLN A 1 107 ? 8.657   -14.838 -36.127 1.00 36.16  ? 107 GLN A NE2 1 
ATOM   843  N  N   . PRO A 1 108 ? 5.695   -10.082 -34.959 1.00 25.29  ? 108 PRO A N   1 
ATOM   844  C  CA  . PRO A 1 108 ? 4.863   -8.908  -34.776 1.00 25.82  ? 108 PRO A CA  1 
ATOM   845  C  C   . PRO A 1 108 ? 3.482   -9.308  -34.249 1.00 27.46  ? 108 PRO A C   1 
ATOM   846  O  O   . PRO A 1 108 ? 2.933   -10.294 -34.695 1.00 25.25  ? 108 PRO A O   1 
ATOM   847  C  CB  . PRO A 1 108 ? 4.730   -8.307  -36.181 1.00 27.99  ? 108 PRO A CB  1 
ATOM   848  C  CG  . PRO A 1 108 ? 5.959   -8.809  -36.898 1.00 30.54  ? 108 PRO A CG  1 
ATOM   849  C  CD  . PRO A 1 108 ? 6.247   -10.180 -36.320 1.00 25.76  ? 108 PRO A CD  1 
ATOM   850  N  N   . GLY A 1 109 ? 2.961   -8.520  -33.317 1.00 25.88  ? 109 GLY A N   1 
ATOM   851  C  CA  . GLY A 1 109 ? 1.664   -8.770  -32.669 1.00 25.26  ? 109 GLY A CA  1 
ATOM   852  C  C   . GLY A 1 109 ? 1.850   -9.369  -31.296 1.00 24.93  ? 109 GLY A C   1 
ATOM   853  O  O   . GLY A 1 109 ? 0.982   -9.175  -30.443 1.00 25.44  ? 109 GLY A O   1 
ATOM   854  N  N   . GLN A 1 110 ? 2.962   -10.056 -31.079 1.00 23.71  ? 110 GLN A N   1 
ATOM   855  C  CA  . GLN A 1 110 ? 3.233   -10.705 -29.789 1.00 23.59  ? 110 GLN A CA  1 
ATOM   856  C  C   . GLN A 1 110 ? 3.467   -9.592  -28.761 1.00 23.31  ? 110 GLN A C   1 
ATOM   857  O  O   . GLN A 1 110 ? 4.089   -8.532  -29.084 1.00 22.07  ? 110 GLN A O   1 
ATOM   858  C  CB  . GLN A 1 110 ? 4.434   -11.653 -29.890 1.00 26.55  ? 110 GLN A CB  1 
ATOM   859  C  CG  . GLN A 1 110 ? 4.650   -12.514 -28.658 1.00 25.06  ? 110 GLN A CG  1 
ATOM   860  C  CD  . GLN A 1 110 ? 3.463   -13.360 -28.263 1.00 27.26  ? 110 GLN A CD  1 
ATOM   861  O  OE1 . GLN A 1 110 ? 2.642   -12.965 -27.414 1.00 23.92  ? 110 GLN A OE1 1 
ATOM   862  N  NE2 . GLN A 1 110 ? 3.414   -14.569 -28.814 1.00 22.36  ? 110 GLN A NE2 1 
ATOM   863  N  N   . THR A 1 111 ? 3.002   -9.848  -27.559 1.00 21.46  ? 111 THR A N   1 
ATOM   864  C  CA  . THR A 1 111 ? 3.223   -8.998  -26.379 1.00 21.54  ? 111 THR A CA  1 
ATOM   865  C  C   . THR A 1 111 ? 4.268   -9.615  -25.452 1.00 21.94  ? 111 THR A C   1 
ATOM   866  O  O   . THR A 1 111 ? 4.526   -10.847 -25.501 1.00 22.41  ? 111 THR A O   1 
ATOM   867  C  CB  . THR A 1 111 ? 1.897   -8.771  -25.645 1.00 20.76  ? 111 THR A CB  1 
ATOM   868  O  OG1 . THR A 1 111 ? 1.407   -10.048 -25.229 1.00 19.43  ? 111 THR A OG1 1 
ATOM   869  C  CG2 . THR A 1 111 ? 0.903   -8.044  -26.507 1.00 23.05  ? 111 THR A CG2 1 
ATOM   870  N  N   . PHE A 1 112 ? 4.852   -8.768  -24.608 1.00 21.46  ? 112 PHE A N   1 
ATOM   871  C  CA  . PHE A 1 112 ? 5.795   -9.168  -23.547 1.00 22.01  ? 112 PHE A CA  1 
ATOM   872  C  C   . PHE A 1 112 ? 5.886   -8.048  -22.516 1.00 22.85  ? 112 PHE A C   1 
ATOM   873  O  O   . PHE A 1 112 ? 5.488   -6.874  -22.775 1.00 19.91  ? 112 PHE A O   1 
ATOM   874  C  CB  . PHE A 1 112 ? 7.171   -9.502  -24.123 1.00 22.64  ? 112 PHE A CB  1 
ATOM   875  C  CG  . PHE A 1 112 ? 7.776   -8.422  -24.976 1.00 22.89  ? 112 PHE A CG  1 
ATOM   876  C  CD1 . PHE A 1 112 ? 7.446   -8.302  -26.322 1.00 26.41  ? 112 PHE A CD1 1 
ATOM   877  C  CD2 . PHE A 1 112 ? 8.612   -7.475  -24.419 1.00 24.56  ? 112 PHE A CD2 1 
ATOM   878  C  CE1 . PHE A 1 112 ? 8.005   -7.306  -27.109 1.00 26.18  ? 112 PHE A CE1 1 
ATOM   879  C  CE2 . PHE A 1 112 ? 9.157   -6.469  -25.200 1.00 22.66  ? 112 PHE A CE2 1 
ATOM   880  C  CZ  . PHE A 1 112 ? 8.852   -6.382  -26.540 1.00 25.68  ? 112 PHE A CZ  1 
ATOM   881  N  N   . SER A 1 113 ? 6.461   -8.399  -21.377 1.00 20.95  ? 113 SER A N   1 
ATOM   882  C  CA  . SER A 1 113 ? 6.767   -7.451  -20.286 1.00 20.49  ? 113 SER A CA  1 
ATOM   883  C  C   . SER A 1 113 ? 8.175   -6.886  -20.461 1.00 22.41  ? 113 SER A C   1 
ATOM   884  O  O   . SER A 1 113 ? 9.121   -7.665  -20.750 1.00 21.59  ? 113 SER A O   1 
ATOM   885  C  CB  . SER A 1 113 ? 6.594   -8.129  -18.952 1.00 22.35  ? 113 SER A CB  1 
ATOM   886  O  OG  . SER A 1 113 ? 5.260   -8.596  -18.815 1.00 20.62  ? 113 SER A OG  1 
ATOM   887  N  N   . VAL A 1 114 ? 8.344   -5.596  -20.211 1.00 18.84  ? 114 VAL A N   1 
ATOM   888  C  CA  . VAL A 1 114 ? 9.683   -4.953  -20.196 1.00 18.36  ? 114 VAL A CA  1 
ATOM   889  C  C   . VAL A 1 114 ? 10.027  -4.568  -18.753 1.00 18.97  ? 114 VAL A C   1 
ATOM   890  O  O   . VAL A 1 114 ? 9.191   -3.937  -18.081 1.00 18.38  ? 114 VAL A O   1 
ATOM   891  C  CB  . VAL A 1 114 ? 9.723   -3.738  -21.144 1.00 20.04  ? 114 VAL A CB  1 
ATOM   892  C  CG1 . VAL A 1 114 ? 10.970  -2.891  -20.949 1.00 19.74  ? 114 VAL A CG1 1 
ATOM   893  C  CG2 . VAL A 1 114 ? 9.593   -4.163  -22.599 1.00 21.22  ? 114 VAL A CG2 1 
ATOM   894  N  N   . LEU A 1 115 ? 11.226  -4.934  -18.297 1.00 17.57  ? 115 LEU A N   1 
ATOM   895  C  CA  . LEU A 1 115 ? 11.764  -4.474  -16.991 1.00 18.55  ? 115 LEU A CA  1 
ATOM   896  C  C   . LEU A 1 115 ? 12.750  -3.354  -17.285 1.00 19.82  ? 115 LEU A C   1 
ATOM   897  O  O   . LEU A 1 115 ? 13.899  -3.633  -17.682 1.00 18.25  ? 115 LEU A O   1 
ATOM   898  C  CB  . LEU A 1 115 ? 12.423  -5.609  -16.204 1.00 19.04  ? 115 LEU A CB  1 
ATOM   899  C  CG  . LEU A 1 115 ? 12.857  -5.220  -14.789 1.00 19.88  ? 115 LEU A CG  1 
ATOM   900  C  CD1 . LEU A 1 115 ? 11.672  -4.925  -13.883 1.00 20.59  ? 115 LEU A CD1 1 
ATOM   901  C  CD2 . LEU A 1 115 ? 13.695  -6.301  -14.174 1.00 20.62  ? 115 LEU A CD2 1 
ATOM   902  N  N   . ALA A 1 116 ? 12.264  -2.119  -17.228 1.00 18.75  ? 116 ALA A N   1 
ATOM   903  C  CA  . ALA A 1 116 ? 13.124  -0.949  -17.466 1.00 20.99  ? 116 ALA A CA  1 
ATOM   904  C  C   . ALA A 1 116 ? 14.136  -0.836  -16.307 1.00 20.92  ? 116 ALA A C   1 
ATOM   905  O  O   . ALA A 1 116 ? 13.708  -0.784  -15.143 1.00 19.02  ? 116 ALA A O   1 
ATOM   906  C  CB  . ALA A 1 116 ? 12.287  0.292   -17.617 1.00 20.57  ? 116 ALA A CB  1 
ATOM   907  N  N   . CYS A 1 117 ? 15.425  -0.791  -16.651 1.00 22.10  ? 117 CYS A N   1 
ATOM   908  C  CA  . CYS A 1 117 ? 16.568  -0.734  -15.715 1.00 24.18  ? 117 CYS A CA  1 
ATOM   909  C  C   . CYS A 1 117 ? 17.536  0.401   -16.036 1.00 24.51  ? 117 CYS A C   1 
ATOM   910  O  O   . CYS A 1 117 ? 17.716  0.765   -17.233 1.00 23.77  ? 117 CYS A O   1 
ATOM   911  C  CB  . CYS A 1 117 ? 17.351  -2.023  -15.752 1.00 25.24  ? 117 CYS A CB  1 
ATOM   912  S  SG  . CYS A 1 117 ? 16.333  -3.393  -15.174 1.00 30.93  ? 117 CYS A SG  1 
ATOM   913  N  N   . TYR A 1 118 ? 18.118  0.953   -14.980 1.00 23.77  ? 118 TYR A N   1 
ATOM   914  C  CA  . TYR A 1 118 ? 19.138  2.031   -15.040 1.00 27.27  ? 118 TYR A CA  1 
ATOM   915  C  C   . TYR A 1 118 ? 20.241  1.624   -14.074 1.00 30.18  ? 118 TYR A C   1 
ATOM   916  O  O   . TYR A 1 118 ? 19.903  1.283   -12.917 1.00 28.71  ? 118 TYR A O   1 
ATOM   917  C  CB  . TYR A 1 118 ? 18.494  3.385   -14.741 1.00 28.52  ? 118 TYR A CB  1 
ATOM   918  C  CG  . TYR A 1 118 ? 17.447  3.753   -15.769 1.00 28.21  ? 118 TYR A CG  1 
ATOM   919  C  CD1 . TYR A 1 118 ? 17.783  4.363   -16.969 1.00 26.18  ? 118 TYR A CD1 1 
ATOM   920  C  CD2 . TYR A 1 118 ? 16.124  3.404   -15.578 1.00 28.21  ? 118 TYR A CD2 1 
ATOM   921  C  CE1 . TYR A 1 118 ? 16.832  4.639   -17.936 1.00 26.27  ? 118 TYR A CE1 1 
ATOM   922  C  CE2 . TYR A 1 118 ? 15.158  3.663   -16.542 1.00 27.82  ? 118 TYR A CE2 1 
ATOM   923  C  CZ  . TYR A 1 118 ? 15.506  4.280   -17.727 1.00 26.43  ? 118 TYR A CZ  1 
ATOM   924  O  OH  . TYR A 1 118 ? 14.522  4.565   -18.629 1.00 22.88  ? 118 TYR A OH  1 
ATOM   925  N  N   . ASN A 1 119 ? 21.481  1.534   -14.564 1.00 32.59  ? 119 ASN A N   1 
ATOM   926  C  CA  . ASN A 1 119 ? 22.666  1.166   -13.738 1.00 32.24  ? 119 ASN A CA  1 
ATOM   927  C  C   . ASN A 1 119 ? 22.482  -0.207  -13.105 1.00 30.31  ? 119 ASN A C   1 
ATOM   928  O  O   . ASN A 1 119 ? 22.967  -0.392  -11.986 1.00 32.57  ? 119 ASN A O   1 
ATOM   929  C  CB  . ASN A 1 119 ? 22.892  2.182   -12.631 1.00 34.76  ? 119 ASN A CB  1 
ATOM   930  C  CG  . ASN A 1 119 ? 23.321  3.492   -13.235 1.00 38.43  ? 119 ASN A CG  1 
ATOM   931  O  OD1 . ASN A 1 119 ? 22.659  4.499   -13.048 1.00 47.09  ? 119 ASN A OD1 1 
ATOM   932  N  ND2 . ASN A 1 119 ? 24.403  3.468   -13.992 1.00 38.75  ? 119 ASN A ND2 1 
ATOM   933  N  N   . GLY A 1 120 ? 21.848  -1.140  -13.818 1.00 25.78  ? 120 GLY A N   1 
ATOM   934  C  CA  . GLY A 1 120 ? 21.589  -2.511  -13.336 1.00 26.39  ? 120 GLY A CA  1 
ATOM   935  C  C   . GLY A 1 120 ? 20.504  -2.579  -12.263 1.00 28.01  ? 120 GLY A C   1 
ATOM   936  O  O   . GLY A 1 120 ? 20.282  -3.681  -11.752 1.00 28.11  ? 120 GLY A O   1 
ATOM   937  N  N   . SER A 1 121 ? 19.815  -1.477  -11.965 1.00 26.06  ? 121 SER A N   1 
ATOM   938  C  CA  . SER A 1 121 ? 18.721  -1.432  -10.956 1.00 32.48  ? 121 SER A CA  1 
ATOM   939  C  C   . SER A 1 121 ? 17.380  -1.302  -11.667 1.00 29.33  ? 121 SER A C   1 
ATOM   940  O  O   . SER A 1 121 ? 17.180  -0.378  -12.449 1.00 26.22  ? 121 SER A O   1 
ATOM   941  C  CB  . SER A 1 121 ? 18.910  -0.297  -9.992  1.00 32.76  ? 121 SER A CB  1 
ATOM   942  O  OG  . SER A 1 121 ? 20.148  -0.447  -9.321  1.00 43.45  ? 121 SER A OG  1 
ATOM   943  N  N   . PRO A 1 122 ? 16.417  -2.198  -11.387 1.00 31.06  ? 122 PRO A N   1 
ATOM   944  C  CA  . PRO A 1 122 ? 15.125  -2.153  -12.071 1.00 32.02  ? 122 PRO A CA  1 
ATOM   945  C  C   . PRO A 1 122 ? 14.367  -0.889  -11.656 1.00 28.68  ? 122 PRO A C   1 
ATOM   946  O  O   . PRO A 1 122 ? 14.387  -0.554  -10.500 1.00 30.41  ? 122 PRO A O   1 
ATOM   947  C  CB  . PRO A 1 122 ? 14.407  -3.435  -11.628 1.00 33.33  ? 122 PRO A CB  1 
ATOM   948  C  CG  . PRO A 1 122 ? 15.478  -4.265  -10.950 1.00 37.65  ? 122 PRO A CG  1 
ATOM   949  C  CD  . PRO A 1 122 ? 16.485  -3.275  -10.390 1.00 33.90  ? 122 PRO A CD  1 
ATOM   950  N  N   . SER A 1 123 ? 13.766  -0.206  -12.625 1.00 28.20  ? 123 SER A N   1 
ATOM   951  C  CA  . SER A 1 123 ? 12.969  1.031   -12.423 1.00 31.13  ? 123 SER A CA  1 
ATOM   952  C  C   . SER A 1 123 ? 11.461  0.716   -12.462 1.00 28.82  ? 123 SER A C   1 
ATOM   953  O  O   . SER A 1 123 ? 10.706  1.306   -11.690 1.00 25.90  ? 123 SER A O   1 
ATOM   954  C  CB  . SER A 1 123 ? 13.349  2.057   -13.448 1.00 32.80  ? 123 SER A CB  1 
ATOM   955  O  OG  . SER A 1 123 ? 12.596  3.241   -13.283 1.00 43.49  ? 123 SER A OG  1 
ATOM   956  N  N   . GLY A 1 124 ? 11.014  -0.146  -13.365 1.00 25.50  ? 124 GLY A N   1 
ATOM   957  C  CA  . GLY A 1 124 ? 9.568   -0.376  -13.551 1.00 25.71  ? 124 GLY A CA  1 
ATOM   958  C  C   . GLY A 1 124 ? 9.281   -1.489  -14.523 1.00 22.15  ? 124 GLY A C   1 
ATOM   959  O  O   . GLY A 1 124 ? 10.180  -1.886  -15.321 1.00 20.18  ? 124 GLY A O   1 
ATOM   960  N  N   . VAL A 1 125 ? 8.040   -1.957  -14.509 1.00 21.19  ? 125 VAL A N   1 
ATOM   961  C  CA  . VAL A 1 125 ? 7.636   -3.016  -15.446 1.00 21.72  ? 125 VAL A CA  1 
ATOM   962  C  C   . VAL A 1 125 ? 6.397   -2.568  -16.202 1.00 22.68  ? 125 VAL A C   1 
ATOM   963  O  O   . VAL A 1 125 ? 5.476   -1.980  -15.597 1.00 20.78  ? 125 VAL A O   1 
ATOM   964  C  CB  . VAL A 1 125 ? 7.475   -4.352  -14.695 1.00 24.70  ? 125 VAL A CB  1 
ATOM   965  C  CG1 . VAL A 1 125 ? 6.496   -4.255  -13.564 1.00 27.06  ? 125 VAL A CG1 1 
ATOM   966  C  CG2 . VAL A 1 125 ? 7.130   -5.506  -15.619 1.00 25.47  ? 125 VAL A CG2 1 
ATOM   967  N  N   . TYR A 1 126 ? 6.364   -2.855  -17.494 1.00 20.37  ? 126 TYR A N   1 
ATOM   968  C  CA  . TYR A 1 126 ? 5.167   -2.553  -18.319 1.00 22.10  ? 126 TYR A CA  1 
ATOM   969  C  C   . TYR A 1 126 ? 5.063   -3.552  -19.462 1.00 21.64  ? 126 TYR A C   1 
ATOM   970  O  O   . TYR A 1 126 ? 6.043   -4.278  -19.762 1.00 21.95  ? 126 TYR A O   1 
ATOM   971  C  CB  . TYR A 1 126 ? 5.201   -1.093  -18.788 1.00 22.07  ? 126 TYR A CB  1 
ATOM   972  C  CG  . TYR A 1 126 ? 6.450   -0.700  -19.540 1.00 21.91  ? 126 TYR A CG  1 
ATOM   973  C  CD1 . TYR A 1 126 ? 6.572   -0.895  -20.902 1.00 21.57  ? 126 TYR A CD1 1 
ATOM   974  C  CD2 . TYR A 1 126 ? 7.510   -0.121  -18.882 1.00 22.99  ? 126 TYR A CD2 1 
ATOM   975  C  CE1 . TYR A 1 126 ? 7.732   -0.552  -21.580 1.00 24.69  ? 126 TYR A CE1 1 
ATOM   976  C  CE2 . TYR A 1 126 ? 8.656   0.258   -19.549 1.00 24.44  ? 126 TYR A CE2 1 
ATOM   977  C  CZ  . TYR A 1 126 ? 8.776   0.041   -20.902 1.00 23.58  ? 126 TYR A CZ  1 
ATOM   978  O  OH  . TYR A 1 126 ? 9.937   0.420   -21.509 1.00 28.26  ? 126 TYR A OH  1 
ATOM   979  N  N   . GLN A 1 127 ? 3.872   -3.577  -20.058 1.00 22.62  ? 127 GLN A N   1 
ATOM   980  C  CA  . GLN A 1 127 ? 3.532   -4.402  -21.231 1.00 25.56  ? 127 GLN A CA  1 
ATOM   981  C  C   . GLN A 1 127 ? 3.764   -3.622  -22.522 1.00 25.83  ? 127 GLN A C   1 
ATOM   982  O  O   . GLN A 1 127 ? 3.517   -2.420  -22.584 1.00 26.27  ? 127 GLN A O   1 
ATOM   983  C  CB  . GLN A 1 127 ? 2.063   -4.824  -21.241 1.00 28.56  ? 127 GLN A CB  1 
ATOM   984  C  CG  . GLN A 1 127 ? 1.796   -6.029  -20.395 1.00 28.86  ? 127 GLN A CG  1 
ATOM   985  C  CD  . GLN A 1 127 ? 2.577   -7.234  -20.864 1.00 28.74  ? 127 GLN A CD  1 
ATOM   986  O  OE1 . GLN A 1 127 ? 3.588   -7.591  -20.276 1.00 32.25  ? 127 GLN A OE1 1 
ATOM   987  N  NE2 . GLN A 1 127 ? 2.068   -7.899  -21.882 1.00 24.70  ? 127 GLN A NE2 1 
ATOM   988  N  N   A CYS A 1 128 ? 4.298   -4.329  -23.524 0.34 24.53  ? 128 CYS A N   1 
ATOM   989  N  N   B CYS A 1 128 ? 4.192   -4.319  -23.564 0.15 24.97  ? 128 CYS A N   1 
ATOM   990  N  N   C CYS A 1 128 ? 4.298   -4.329  -23.524 0.34 24.53  ? 128 CYS A N   1 
ATOM   991  N  N   D CYS A 1 128 ? 4.192   -4.319  -23.564 0.15 24.97  ? 128 CYS A N   1 
ATOM   992  C  CA  A CYS A 1 128 ? 4.580   -3.864  -24.905 0.34 23.66  ? 128 CYS A CA  1 
ATOM   993  C  CA  B CYS A 1 128 ? 4.249   -3.749  -24.925 0.15 24.39  ? 128 CYS A CA  1 
ATOM   994  C  CA  C CYS A 1 128 ? 4.580   -3.864  -24.905 0.34 23.66  ? 128 CYS A CA  1 
ATOM   995  C  CA  D CYS A 1 128 ? 4.249   -3.749  -24.925 0.15 24.39  ? 128 CYS A CA  1 
ATOM   996  C  C   A CYS A 1 128 ? 4.076   -4.906  -25.903 0.34 23.91  ? 128 CYS A C   1 
ATOM   997  C  C   B CYS A 1 128 ? 4.300   -4.882  -25.946 0.15 24.31  ? 128 CYS A C   1 
ATOM   998  C  C   C CYS A 1 128 ? 4.076   -4.906  -25.903 0.34 23.91  ? 128 CYS A C   1 
ATOM   999  C  C   D CYS A 1 128 ? 4.300   -4.882  -25.946 0.15 24.31  ? 128 CYS A C   1 
ATOM   1000 O  O   A CYS A 1 128 ? 3.790   -6.034  -25.454 0.34 22.87  ? 128 CYS A O   1 
ATOM   1001 O  O   B CYS A 1 128 ? 4.652   -6.025  -25.583 0.15 23.61  ? 128 CYS A O   1 
ATOM   1002 O  O   C CYS A 1 128 ? 3.790   -6.034  -25.454 0.34 22.87  ? 128 CYS A O   1 
ATOM   1003 O  O   D CYS A 1 128 ? 4.652   -6.025  -25.583 0.15 23.61  ? 128 CYS A O   1 
ATOM   1004 C  CB  A CYS A 1 128 ? 6.073   -3.729  -25.154 0.34 24.14  ? 128 CYS A CB  1 
ATOM   1005 C  CB  B CYS A 1 128 ? 5.448   -2.831  -25.090 0.15 24.63  ? 128 CYS A CB  1 
ATOM   1006 C  CB  C CYS A 1 128 ? 6.073   -3.729  -25.154 0.34 24.14  ? 128 CYS A CB  1 
ATOM   1007 C  CB  D CYS A 1 128 ? 5.448   -2.831  -25.090 0.15 24.63  ? 128 CYS A CB  1 
ATOM   1008 S  SG  A CYS A 1 128 ? 6.745   -2.162  -24.564 0.34 26.71  ? 128 CYS A SG  1 
ATOM   1009 S  SG  B CYS A 1 128 ? 6.984   -3.768  -25.251 0.15 25.68  ? 128 CYS A SG  1 
ATOM   1010 S  SG  C CYS A 1 128 ? 6.745   -2.162  -24.564 0.34 26.71  ? 128 CYS A SG  1 
ATOM   1011 S  SG  D CYS A 1 128 ? 6.984   -3.768  -25.251 0.15 25.68  ? 128 CYS A SG  1 
ATOM   1012 N  N   . ALA A 1 129 ? 3.982   -4.527  -27.183 1.00 24.55  ? 129 ALA A N   1 
ATOM   1013 C  CA  . ALA A 1 129 ? 3.831   -5.442  -28.323 1.00 23.86  ? 129 ALA A CA  1 
ATOM   1014 C  C   . ALA A 1 129 ? 4.964   -5.160  -29.289 1.00 22.03  ? 129 ALA A C   1 
ATOM   1015 O  O   . ALA A 1 129 ? 5.399   -4.010  -29.393 1.00 25.33  ? 129 ALA A O   1 
ATOM   1016 C  CB  . ALA A 1 129 ? 2.523   -5.193  -29.014 1.00 24.93  ? 129 ALA A CB  1 
ATOM   1017 N  N   . MET A 1 130 ? 5.384   -6.181  -30.001 1.00 22.32  ? 130 MET A N   1 
ATOM   1018 C  CA  . MET A 1 130 ? 6.203   -6.019  -31.221 1.00 22.82  ? 130 MET A CA  1 
ATOM   1019 C  C   . MET A 1 130 ? 5.263   -5.482  -32.306 1.00 23.76  ? 130 MET A C   1 
ATOM   1020 O  O   . MET A 1 130 ? 4.300   -6.216  -32.723 1.00 23.54  ? 130 MET A O   1 
ATOM   1021 C  CB  . MET A 1 130 ? 6.812   -7.358  -31.617 1.00 23.02  ? 130 MET A CB  1 
ATOM   1022 C  CG  . MET A 1 130 ? 7.729   -7.317  -32.815 1.00 25.03  ? 130 MET A CG  1 
ATOM   1023 S  SD  . MET A 1 130 ? 9.033   -6.100  -32.611 1.00 24.72  ? 130 MET A SD  1 
ATOM   1024 C  CE  . MET A 1 130 ? 9.920   -6.809  -31.220 1.00 22.15  ? 130 MET A CE  1 
ATOM   1025 N  N   . ARG A 1 131 ? 5.439   -4.212  -32.664 1.00 20.85  ? 131 ARG A N   1 
ATOM   1026 C  CA  . ARG A 1 131 ? 4.633   -3.568  -33.727 1.00 22.35  ? 131 ARG A CA  1 
ATOM   1027 C  C   . ARG A 1 131 ? 4.897   -4.284  -35.053 1.00 22.56  ? 131 ARG A C   1 
ATOM   1028 O  O   . ARG A 1 131 ? 5.962   -4.874  -35.252 1.00 23.35  ? 131 ARG A O   1 
ATOM   1029 C  CB  . ARG A 1 131 ? 4.977   -2.086  -33.852 1.00 21.74  ? 131 ARG A CB  1 
ATOM   1030 C  CG  . ARG A 1 131 ? 4.809   -1.259  -32.584 1.00 23.94  ? 131 ARG A CG  1 
ATOM   1031 C  CD  . ARG A 1 131 ? 3.475   -1.401  -31.909 1.00 23.42  ? 131 ARG A CD  1 
ATOM   1032 N  NE  . ARG A 1 131 ? 2.404   -1.135  -32.858 1.00 25.24  ? 131 ARG A NE  1 
ATOM   1033 C  CZ  . ARG A 1 131 ? 1.107   -1.300  -32.583 1.00 25.10  ? 131 ARG A CZ  1 
ATOM   1034 N  NH1 . ARG A 1 131 ? 0.715   -1.649  -31.369 1.00 20.50  ? 131 ARG A NH1 1 
ATOM   1035 N  NH2 . ARG A 1 131 ? 0.223   -1.123  -33.551 1.00 25.44  ? 131 ARG A NH2 1 
ATOM   1036 N  N   . PRO A 1 132 ? 3.932   -4.249  -35.999 1.00 23.35  ? 132 PRO A N   1 
ATOM   1037 C  CA  . PRO A 1 132 ? 4.141   -4.789  -37.348 1.00 22.44  ? 132 PRO A CA  1 
ATOM   1038 C  C   . PRO A 1 132 ? 5.397   -4.228  -38.020 1.00 20.84  ? 132 PRO A C   1 
ATOM   1039 O  O   . PRO A 1 132 ? 5.931   -4.872  -38.856 1.00 22.91  ? 132 PRO A O   1 
ATOM   1040 C  CB  . PRO A 1 132 ? 2.875   -4.347  -38.104 1.00 23.52  ? 132 PRO A CB  1 
ATOM   1041 C  CG  . PRO A 1 132 ? 1.833   -4.332  -37.005 1.00 22.98  ? 132 PRO A CG  1 
ATOM   1042 C  CD  . PRO A 1 132 ? 2.572   -3.706  -35.829 1.00 22.20  ? 132 PRO A CD  1 
ATOM   1043 N  N   . ASN A 1 133 ? 5.833   -3.033  -37.643 1.00 22.05  ? 133 ASN A N   1 
ATOM   1044 C  CA  . ASN A 1 133 ? 7.040   -2.407  -38.237 1.00 21.35  ? 133 ASN A CA  1 
ATOM   1045 C  C   . ASN A 1 133 ? 8.294   -2.760  -37.428 1.00 22.58  ? 133 ASN A C   1 
ATOM   1046 O  O   . ASN A 1 133 ? 9.301   -2.110  -37.665 1.00 22.30  ? 133 ASN A O   1 
ATOM   1047 C  CB  . ASN A 1 133 ? 6.912   -0.896  -38.395 1.00 22.38  ? 133 ASN A CB  1 
ATOM   1048 C  CG  . ASN A 1 133 ? 6.871   -0.116  -37.095 1.00 22.89  ? 133 ASN A CG  1 
ATOM   1049 O  OD1 . ASN A 1 133 ? 6.982   -0.677  -36.000 1.00 22.60  ? 133 ASN A OD1 1 
ATOM   1050 N  ND2 . ASN A 1 133 ? 6.703   1.195   -37.228 1.00 23.27  ? 133 ASN A ND2 1 
ATOM   1051 N  N   . PHE A 1 134 ? 8.221   -3.740  -36.524 1.00 22.17  ? 134 PHE A N   1 
ATOM   1052 C  CA  . PHE A 1 134 ? 9.371   -4.325  -35.794 1.00 24.36  ? 134 PHE A CA  1 
ATOM   1053 C  C   . PHE A 1 134 ? 9.961   -3.326  -34.795 1.00 25.03  ? 134 PHE A C   1 
ATOM   1054 O  O   . PHE A 1 134 ? 11.137  -3.533  -34.413 1.00 26.64  ? 134 PHE A O   1 
ATOM   1055 C  CB  . PHE A 1 134 ? 10.466  -4.800  -36.752 1.00 23.36  ? 134 PHE A CB  1 
ATOM   1056 C  CG  . PHE A 1 134 ? 9.968   -5.923  -37.609 1.00 26.98  ? 134 PHE A CG  1 
ATOM   1057 C  CD1 . PHE A 1 134 ? 9.797   -7.186  -37.066 1.00 29.26  ? 134 PHE A CD1 1 
ATOM   1058 C  CD2 . PHE A 1 134 ? 9.611   -5.693  -38.927 1.00 28.24  ? 134 PHE A CD2 1 
ATOM   1059 C  CE1 . PHE A 1 134 ? 9.308   -8.223  -37.847 1.00 32.31  ? 134 PHE A CE1 1 
ATOM   1060 C  CE2 . PHE A 1 134 ? 9.120   -6.731  -39.704 1.00 32.86  ? 134 PHE A CE2 1 
ATOM   1061 C  CZ  . PHE A 1 134 ? 8.975   -7.992  -39.163 1.00 29.43  ? 134 PHE A CZ  1 
ATOM   1062 N  N   . THR A 1 135 ? 9.193   -2.306  -34.391 1.00 22.94  ? 135 THR A N   1 
ATOM   1063 C  CA  . THR A 1 135 ? 9.547   -1.440  -33.253 1.00 21.26  ? 135 THR A CA  1 
ATOM   1064 C  C   . THR A 1 135 ? 8.665   -1.777  -32.059 1.00 21.53  ? 135 THR A C   1 
ATOM   1065 O  O   . THR A 1 135 ? 7.645   -2.474  -32.220 1.00 22.37  ? 135 THR A O   1 
ATOM   1066 C  CB  . THR A 1 135 ? 9.447   0.029   -33.654 1.00 23.74  ? 135 THR A CB  1 
ATOM   1067 O  OG1 . THR A 1 135 ? 8.077   0.389   -33.895 1.00 25.75  ? 135 THR A OG1 1 
ATOM   1068 C  CG2 . THR A 1 135 ? 10.308  0.343   -34.859 1.00 23.77  ? 135 THR A CG2 1 
ATOM   1069 N  N   . ILE A 1 136 ? 9.010   -1.234  -30.893 1.00 21.54  ? 136 ILE A N   1 
ATOM   1070 C  CA  . ILE A 1 136 ? 8.123   -1.262  -29.700 1.00 21.67  ? 136 ILE A CA  1 
ATOM   1071 C  C   . ILE A 1 136 ? 7.969   0.164   -29.199 1.00 21.81  ? 136 ILE A C   1 
ATOM   1072 O  O   . ILE A 1 136 ? 8.907   0.932   -29.356 1.00 22.90  ? 136 ILE A O   1 
ATOM   1073 C  CB  . ILE A 1 136 ? 8.636   -2.217  -28.613 1.00 25.56  ? 136 ILE A CB  1 
ATOM   1074 C  CG1 . ILE A 1 136 ? 9.865   -1.663  -27.888 1.00 25.36  ? 136 ILE A CG1 1 
ATOM   1075 C  CG2 . ILE A 1 136 ? 8.918   -3.585  -29.230 1.00 25.29  ? 136 ILE A CG2 1 
ATOM   1076 C  CD1 . ILE A 1 136 ? 10.272  -2.463  -26.691 1.00 26.89  ? 136 ILE A CD1 1 
ATOM   1077 N  N   . LYS A 1 137 ? 6.791   0.479   -28.674 1.00 23.53  ? 137 LYS A N   1 
ATOM   1078 C  CA  . LYS A 1 137 ? 6.466   1.801   -28.080 1.00 25.73  ? 137 LYS A CA  1 
ATOM   1079 C  C   . LYS A 1 137 ? 6.783   1.686   -26.599 1.00 25.23  ? 137 LYS A C   1 
ATOM   1080 O  O   . LYS A 1 137 ? 5.946   1.255   -25.823 1.00 23.95  ? 137 LYS A O   1 
ATOM   1081 C  CB  . LYS A 1 137 ? 5.010   2.182   -28.359 1.00 31.79  ? 137 LYS A CB  1 
ATOM   1082 C  CG  . LYS A 1 137 ? 4.641   2.041   -29.825 1.00 38.64  ? 137 LYS A CG  1 
ATOM   1083 C  CD  . LYS A 1 137 ? 3.377   2.754   -30.219 1.00 44.82  ? 137 LYS A CD  1 
ATOM   1084 C  CE  . LYS A 1 137 ? 3.268   2.845   -31.725 1.00 54.93  ? 137 LYS A CE  1 
ATOM   1085 N  NZ  . LYS A 1 137 ? 2.354   3.939   -32.128 1.00 64.05  ? 137 LYS A NZ  1 
ATOM   1086 N  N   . GLY A 1 138 ? 8.035   1.944   -26.258 1.00 23.16  ? 138 GLY A N   1 
ATOM   1087 C  CA  . GLY A 1 138 ? 8.506   1.741   -24.892 1.00 22.83  ? 138 GLY A CA  1 
ATOM   1088 C  C   . GLY A 1 138 ? 8.516   3.028   -24.116 1.00 21.89  ? 138 GLY A C   1 
ATOM   1089 O  O   . GLY A 1 138 ? 8.081   4.084   -24.614 1.00 22.14  ? 138 GLY A O   1 
ATOM   1090 N  N   . SER A 1 139 ? 9.062   2.932   -22.917 1.00 22.49  ? 139 SER A N   1 
ATOM   1091 C  CA  . SER A 1 139 ? 9.405   4.091   -22.078 1.00 22.52  ? 139 SER A CA  1 
ATOM   1092 C  C   . SER A 1 139 ? 10.838  3.861   -21.609 1.00 22.47  ? 139 SER A C   1 
ATOM   1093 O  O   . SER A 1 139 ? 11.061  3.021   -20.740 1.00 20.27  ? 139 SER A O   1 
ATOM   1094 C  CB  . SER A 1 139 ? 8.430   4.245   -20.942 1.00 22.73  ? 139 SER A CB  1 
ATOM   1095 O  OG  . SER A 1 139 ? 8.840   5.343   -20.158 1.00 24.92  ? 139 SER A OG  1 
ATOM   1096 N  N   . PHE A 1 140 ? 11.762  4.541   -22.262 1.00 21.52  ? 140 PHE A N   1 
ATOM   1097 C  CA  . PHE A 1 140 ? 13.204  4.255   -22.168 1.00 23.62  ? 140 PHE A CA  1 
ATOM   1098 C  C   . PHE A 1 140 ? 13.955  5.589   -22.170 1.00 26.53  ? 140 PHE A C   1 
ATOM   1099 O  O   . PHE A 1 140 ? 13.817  6.360   -23.132 1.00 27.36  ? 140 PHE A O   1 
ATOM   1100 C  CB  . PHE A 1 140 ? 13.655  3.397   -23.351 1.00 23.06  ? 140 PHE A CB  1 
ATOM   1101 C  CG  . PHE A 1 140 ? 13.284  1.940   -23.280 1.00 23.32  ? 140 PHE A CG  1 
ATOM   1102 C  CD1 . PHE A 1 140 ? 13.671  1.182   -22.181 1.00 25.44  ? 140 PHE A CD1 1 
ATOM   1103 C  CD2 . PHE A 1 140 ? 12.561  1.315   -24.291 1.00 23.24  ? 140 PHE A CD2 1 
ATOM   1104 C  CE1 . PHE A 1 140 ? 13.378  -0.166  -22.101 1.00 23.96  ? 140 PHE A CE1 1 
ATOM   1105 C  CE2 . PHE A 1 140 ? 12.317  -0.053  -24.230 1.00 23.49  ? 140 PHE A CE2 1 
ATOM   1106 C  CZ  . PHE A 1 140 ? 12.724  -0.788  -23.140 1.00 23.31  ? 140 PHE A CZ  1 
ATOM   1107 N  N   . LEU A 1 141 ? 14.753  5.821   -21.132 1.00 27.28  ? 141 LEU A N   1 
ATOM   1108 C  CA  . LEU A 1 141 ? 15.632  7.003   -21.072 1.00 30.53  ? 141 LEU A CA  1 
ATOM   1109 C  C   . LEU A 1 141 ? 17.064  6.528   -21.304 1.00 32.01  ? 141 LEU A C   1 
ATOM   1110 O  O   . LEU A 1 141 ? 17.310  5.309   -21.448 1.00 31.43  ? 141 LEU A O   1 
ATOM   1111 C  CB  . LEU A 1 141 ? 15.462  7.702   -19.722 1.00 34.49  ? 141 LEU A CB  1 
ATOM   1112 C  CG  . LEU A 1 141 ? 14.030  8.084   -19.342 1.00 40.02  ? 141 LEU A CG  1 
ATOM   1113 C  CD1 . LEU A 1 141 ? 14.001  8.704   -17.950 1.00 43.65  ? 141 LEU A CD1 1 
ATOM   1114 C  CD2 . LEU A 1 141 ? 13.403  9.029   -20.360 1.00 42.23  ? 141 LEU A CD2 1 
ATOM   1115 N  N   . ASN A 1 142 ? 17.985  7.478   -21.343 1.00 32.23  ? 142 ASN A N   1 
ATOM   1116 C  CA  . ASN A 1 142 ? 19.436  7.195   -21.435 1.00 32.25  ? 142 ASN A CA  1 
ATOM   1117 C  C   . ASN A 1 142 ? 19.795  6.269   -20.275 1.00 30.55  ? 142 ASN A C   1 
ATOM   1118 O  O   . ASN A 1 142 ? 19.243  6.440   -19.158 1.00 26.88  ? 142 ASN A O   1 
ATOM   1119 C  CB  . ASN A 1 142 ? 20.248  8.488   -21.494 1.00 38.83  ? 142 ASN A CB  1 
ATOM   1120 C  CG  . ASN A 1 142 ? 19.873  9.308   -22.718 1.00 47.74  ? 142 ASN A CG  1 
ATOM   1121 O  OD1 . ASN A 1 142 ? 19.110  10.264  -22.616 1.00 58.60  ? 142 ASN A OD1 1 
ATOM   1122 N  ND2 . ASN A 1 142 ? 20.335  8.907   -23.891 1.00 52.80  ? 142 ASN A ND2 1 
ATOM   1123 N  N   . GLY A 1 143 ? 20.577  5.241   -20.583 1.00 26.85  ? 143 GLY A N   1 
ATOM   1124 C  CA  . GLY A 1 143 ? 21.018  4.248   -19.594 1.00 27.96  ? 143 GLY A CA  1 
ATOM   1125 C  C   . GLY A 1 143 ? 20.182  2.985   -19.631 1.00 26.48  ? 143 GLY A C   1 
ATOM   1126 O  O   . GLY A 1 143 ? 20.539  2.044   -18.916 1.00 25.23  ? 143 GLY A O   1 
ATOM   1127 N  N   . SER A 1 144 ? 19.096  2.948   -20.413 1.00 24.23  ? 144 SER A N   1 
ATOM   1128 C  CA  . SER A 1 144 ? 18.133  1.817   -20.376 1.00 22.99  ? 144 SER A CA  1 
ATOM   1129 C  C   . SER A 1 144 ? 18.583  0.704   -21.314 1.00 22.19  ? 144 SER A C   1 
ATOM   1130 O  O   . SER A 1 144 ? 17.982  -0.381  -21.248 1.00 19.61  ? 144 SER A O   1 
ATOM   1131 C  CB  . SER A 1 144 ? 16.711  2.269   -20.689 1.00 21.08  ? 144 SER A CB  1 
ATOM   1132 O  OG  . SER A 1 144 ? 16.688  2.972   -21.908 1.00 22.28  ? 144 SER A OG  1 
ATOM   1133 N  N   . CYS A 1 145 ? 19.595  0.927   -22.158 1.00 22.14  ? 145 CYS A N   1 
ATOM   1134 C  CA  . CYS A 1 145 ? 20.091  -0.158  -23.048 1.00 22.35  ? 145 CYS A CA  1 
ATOM   1135 C  C   . CYS A 1 145 ? 20.476  -1.391  -22.229 1.00 22.13  ? 145 CYS A C   1 
ATOM   1136 O  O   . CYS A 1 145 ? 21.017  -1.243  -21.134 1.00 20.53  ? 145 CYS A O   1 
ATOM   1137 C  CB  . CYS A 1 145 ? 21.279  0.292   -23.872 1.00 25.30  ? 145 CYS A CB  1 
ATOM   1138 S  SG  . CYS A 1 145 ? 20.791  1.632   -24.986 1.00 27.66  ? 145 CYS A SG  1 
ATOM   1139 N  N   . GLY A 1 146 ? 20.106  -2.562  -22.727 1.00 21.21  ? 146 GLY A N   1 
ATOM   1140 C  CA  . GLY A 1 146 ? 20.332  -3.840  -22.043 1.00 24.97  ? 146 GLY A CA  1 
ATOM   1141 C  C   . GLY A 1 146 ? 19.138  -4.250  -21.194 1.00 22.77  ? 146 GLY A C   1 
ATOM   1142 O  O   . GLY A 1 146 ? 19.134  -5.408  -20.759 1.00 21.81  ? 146 GLY A O   1 
ATOM   1143 N  N   . SER A 1 147 ? 18.160  -3.365  -20.974 1.00 21.66  ? 147 SER A N   1 
ATOM   1144 C  CA  . SER A 1 147 ? 16.825  -3.743  -20.424 1.00 19.84  ? 147 SER A CA  1 
ATOM   1145 C  C   . SER A 1 147 ? 16.222  -4.847  -21.301 1.00 18.73  ? 147 SER A C   1 
ATOM   1146 O  O   . SER A 1 147 ? 16.424  -4.824  -22.497 1.00 17.46  ? 147 SER A O   1 
ATOM   1147 C  CB  . SER A 1 147 ? 15.894  -2.560  -20.337 1.00 19.48  ? 147 SER A CB  1 
ATOM   1148 O  OG  . SER A 1 147 ? 16.285  -1.624  -19.330 1.00 19.05  ? 147 SER A OG  1 
ATOM   1149 N  N   . VAL A 1 148 ? 15.482  -5.795  -20.732 1.00 18.79  ? 148 VAL A N   1 
ATOM   1150 C  CA  . VAL A 1 148 ? 14.958  -6.919  -21.532 1.00 17.01  ? 148 VAL A CA  1 
ATOM   1151 C  C   . VAL A 1 148 ? 13.440  -6.987  -21.463 1.00 18.02  ? 148 VAL A C   1 
ATOM   1152 O  O   . VAL A 1 148 ? 12.821  -6.418  -20.525 1.00 17.82  ? 148 VAL A O   1 
ATOM   1153 C  CB  . VAL A 1 148 ? 15.590  -8.254  -21.122 1.00 20.33  ? 148 VAL A CB  1 
ATOM   1154 C  CG1 . VAL A 1 148 ? 17.085  -8.243  -21.373 1.00 19.39  ? 148 VAL A CG1 1 
ATOM   1155 C  CG2 . VAL A 1 148 ? 15.272  -8.640  -19.687 1.00 21.30  ? 148 VAL A CG2 1 
ATOM   1156 N  N   . GLY A 1 149 ? 12.893  -7.679  -22.459 1.00 17.80  ? 149 GLY A N   1 
ATOM   1157 C  CA  . GLY A 1 149 ? 11.486  -8.055  -22.600 1.00 17.21  ? 149 GLY A CA  1 
ATOM   1158 C  C   . GLY A 1 149 ? 11.351  -9.547  -22.409 1.00 19.34  ? 149 GLY A C   1 
ATOM   1159 O  O   . GLY A 1 149 ? 12.278  -10.307 -22.836 1.00 20.93  ? 149 GLY A O   1 
ATOM   1160 N  N   . PHE A 1 150 ? 10.277  -9.982  -21.753 1.00 20.67  ? 150 PHE A N   1 
ATOM   1161 C  CA  . PHE A 1 150 ? 10.120  -11.394 -21.343 1.00 21.59  ? 150 PHE A CA  1 
ATOM   1162 C  C   . PHE A 1 150 ? 8.644   -11.739 -21.224 1.00 23.11  ? 150 PHE A C   1 
ATOM   1163 O  O   . PHE A 1 150 ? 7.806   -10.852 -20.999 1.00 19.19  ? 150 PHE A O   1 
ATOM   1164 C  CB  . PHE A 1 150 ? 10.867  -11.690 -20.039 1.00 20.51  ? 150 PHE A CB  1 
ATOM   1165 C  CG  . PHE A 1 150 ? 10.431  -10.825 -18.893 1.00 19.72  ? 150 PHE A CG  1 
ATOM   1166 C  CD1 . PHE A 1 150 ? 10.907  -9.531  -18.789 1.00 21.80  ? 150 PHE A CD1 1 
ATOM   1167 C  CD2 . PHE A 1 150 ? 9.536   -11.290 -17.947 1.00 20.89  ? 150 PHE A CD2 1 
ATOM   1168 C  CE1 . PHE A 1 150 ? 10.491  -8.695  -17.762 1.00 23.74  ? 150 PHE A CE1 1 
ATOM   1169 C  CE2 . PHE A 1 150 ? 9.108   -10.453 -16.920 1.00 22.46  ? 150 PHE A CE2 1 
ATOM   1170 C  CZ  . PHE A 1 150 ? 9.590   -9.163  -16.824 1.00 23.84  ? 150 PHE A CZ  1 
ATOM   1171 N  N   . ASN A 1 151 ? 8.352   -13.035 -21.356 1.00 25.58  ? 151 ASN A N   1 
ATOM   1172 C  CA  . ASN A 1 151 ? 7.089   -13.635 -20.875 1.00 25.43  ? 151 ASN A CA  1 
ATOM   1173 C  C   . ASN A 1 151 ? 7.469   -14.669 -19.813 1.00 30.16  ? 151 ASN A C   1 
ATOM   1174 O  O   . ASN A 1 151 ? 8.647   -15.153 -19.781 1.00 32.47  ? 151 ASN A O   1 
ATOM   1175 C  CB  . ASN A 1 151 ? 6.243   -14.261 -21.980 1.00 25.48  ? 151 ASN A CB  1 
ATOM   1176 C  CG  . ASN A 1 151 ? 5.620   -13.228 -22.888 1.00 26.79  ? 151 ASN A CG  1 
ATOM   1177 O  OD1 . ASN A 1 151 ? 4.645   -12.580 -22.517 1.00 30.02  ? 151 ASN A OD1 1 
ATOM   1178 N  ND2 . ASN A 1 151 ? 6.158   -13.089 -24.090 1.00 25.23  ? 151 ASN A ND2 1 
ATOM   1179 N  N   . ILE A 1 152 ? 6.516   -14.957 -18.938 1.00 29.80  ? 152 ILE A N   1 
ATOM   1180 C  CA  . ILE A 1 152 ? 6.653   -16.051 -17.956 1.00 31.89  ? 152 ILE A CA  1 
ATOM   1181 C  C   . ILE A 1 152 ? 5.360   -16.862 -17.990 1.00 39.55  ? 152 ILE A C   1 
ATOM   1182 O  O   . ILE A 1 152 ? 4.555   -16.720 -17.075 1.00 42.92  ? 152 ILE A O   1 
ATOM   1183 C  CB  . ILE A 1 152 ? 6.944   -15.526 -16.550 1.00 30.63  ? 152 ILE A CB  1 
ATOM   1184 C  CG1 . ILE A 1 152 ? 8.012   -14.431 -16.523 1.00 27.70  ? 152 ILE A CG1 1 
ATOM   1185 C  CG2 . ILE A 1 152 ? 7.318   -16.716 -15.680 1.00 32.70  ? 152 ILE A CG2 1 
ATOM   1186 C  CD1 . ILE A 1 152 ? 8.409   -14.001 -15.125 1.00 28.19  ? 152 ILE A CD1 1 
ATOM   1187 N  N   . ASP A 1 153 ? 5.189   -17.689 -19.009 1.00 46.64  ? 153 ASP A N   1 
ATOM   1188 C  CA  . ASP A 1 153 ? 4.168   -18.760 -18.989 1.00 58.47  ? 153 ASP A CA  1 
ATOM   1189 C  C   . ASP A 1 153 ? 4.847   -19.942 -18.262 1.00 61.39  ? 153 ASP A C   1 
ATOM   1190 O  O   . ASP A 1 153 ? 5.963   -20.338 -18.681 1.00 56.56  ? 153 ASP A O   1 
ATOM   1191 C  CB  . ASP A 1 153 ? 3.591   -18.955 -20.405 1.00 58.16  ? 153 ASP A CB  1 
ATOM   1192 C  CG  . ASP A 1 153 ? 3.145   -17.675 -21.136 1.00 56.35  ? 153 ASP A CG  1 
ATOM   1193 O  OD1 . ASP A 1 153 ? 2.384   -16.886 -20.562 1.00 53.98  ? 153 ASP A OD1 1 
ATOM   1194 O  OD2 . ASP A 1 153 ? 3.561   -17.459 -22.295 1.00 49.10  ? 153 ASP A OD2 1 
ATOM   1195 N  N   . TYR A 1 154 ? 4.267   -20.371 -17.127 1.00 69.74  ? 154 TYR A N   1 
ATOM   1196 C  CA  . TYR A 1 154 ? 4.494   -21.665 -16.414 1.00 73.60  ? 154 TYR A CA  1 
ATOM   1197 C  C   . TYR A 1 154 ? 5.911   -21.766 -15.814 1.00 67.20  ? 154 TYR A C   1 
ATOM   1198 O  O   . TYR A 1 154 ? 6.629   -22.732 -16.116 1.00 71.23  ? 154 TYR A O   1 
ATOM   1199 C  CB  . TYR A 1 154 ? 4.198   -22.857 -17.340 1.00 84.91  ? 154 TYR A CB  1 
ATOM   1200 C  CG  . TYR A 1 154 ? 3.026   -22.693 -18.284 1.00 98.33  ? 154 TYR A CG  1 
ATOM   1201 C  CD1 . TYR A 1 154 ? 1.720   -22.959 -17.890 1.00 102.24 ? 154 TYR A CD1 1 
ATOM   1202 C  CD2 . TYR A 1 154 ? 3.227   -22.282 -19.595 1.00 106.37 ? 154 TYR A CD2 1 
ATOM   1203 C  CE1 . TYR A 1 154 ? 0.653   -22.802 -18.768 1.00 104.30 ? 154 TYR A CE1 1 
ATOM   1204 C  CE2 . TYR A 1 154 ? 2.174   -22.121 -20.483 1.00 105.06 ? 154 TYR A CE2 1 
ATOM   1205 C  CZ  . TYR A 1 154 ? 0.879   -22.380 -20.070 1.00 103.80 ? 154 TYR A CZ  1 
ATOM   1206 O  OH  . TYR A 1 154 ? -0.141  -22.209 -20.964 1.00 90.65  ? 154 TYR A OH  1 
ATOM   1207 N  N   . ASP A 1 155 ? 6.299   -20.829 -14.943 1.00 62.56  ? 155 ASP A N   1 
ATOM   1208 C  CA  . ASP A 1 155 ? 7.555   -20.876 -14.130 1.00 59.36  ? 155 ASP A CA  1 
ATOM   1209 C  C   . ASP A 1 155 ? 8.822   -20.696 -14.976 1.00 51.85  ? 155 ASP A C   1 
ATOM   1210 O  O   . ASP A 1 155 ? 9.910   -20.581 -14.374 1.00 52.16  ? 155 ASP A O   1 
ATOM   1211 C  CB  . ASP A 1 155 ? 7.712   -22.195 -13.366 1.00 67.78  ? 155 ASP A CB  1 
ATOM   1212 C  CG  . ASP A 1 155 ? 7.591   -22.050 -11.853 1.00 76.09  ? 155 ASP A CG  1 
ATOM   1213 O  OD1 . ASP A 1 155 ? 7.960   -20.969 -11.316 1.00 77.97  ? 155 ASP A OD1 1 
ATOM   1214 O  OD2 . ASP A 1 155 ? 7.130   -23.024 -11.220 1.00 85.39  ? 155 ASP A OD2 1 
ATOM   1215 N  N   . CYS A 1 156 ? 8.718   -20.698 -16.306 1.00 42.82  ? 156 CYS A N   1 
ATOM   1216 C  CA  . CYS A 1 156 ? 9.890   -20.559 -17.212 1.00 37.74  ? 156 CYS A CA  1 
ATOM   1217 C  C   . CYS A 1 156 ? 9.895   -19.166 -17.855 1.00 31.32  ? 156 CYS A C   1 
ATOM   1218 O  O   . CYS A 1 156 ? 8.886   -18.778 -18.464 1.00 28.85  ? 156 CYS A O   1 
ATOM   1219 C  CB  . CYS A 1 156 ? 9.882   -21.647 -18.272 1.00 38.03  ? 156 CYS A CB  1 
ATOM   1220 S  SG  . CYS A 1 156 ? 11.241  -21.478 -19.453 1.00 38.50  ? 156 CYS A SG  1 
ATOM   1221 N  N   . VAL A 1 157 ? 10.995  -18.448 -17.706 1.00 28.56  ? 157 VAL A N   1 
ATOM   1222 C  CA  . VAL A 1 157 ? 11.136  -17.059 -18.214 1.00 29.93  ? 157 VAL A CA  1 
ATOM   1223 C  C   . VAL A 1 157 ? 11.595  -17.121 -19.665 1.00 26.46  ? 157 VAL A C   1 
ATOM   1224 O  O   . VAL A 1 157 ? 12.727  -17.545 -19.906 1.00 28.98  ? 157 VAL A O   1 
ATOM   1225 C  CB  . VAL A 1 157 ? 12.126  -16.258 -17.364 1.00 28.24  ? 157 VAL A CB  1 
ATOM   1226 C  CG1 . VAL A 1 157 ? 12.325  -14.866 -17.940 1.00 31.54  ? 157 VAL A CG1 1 
ATOM   1227 C  CG2 . VAL A 1 157 ? 11.695  -16.198 -15.920 1.00 28.39  ? 157 VAL A CG2 1 
ATOM   1228 N  N   . SER A 1 158 ? 10.761  -16.690 -20.600 1.00 24.85  ? 158 SER A N   1 
ATOM   1229 C  CA  . SER A 1 158 ? 11.134  -16.663 -22.031 1.00 26.95  ? 158 SER A CA  1 
ATOM   1230 C  C   . SER A 1 158 ? 11.616  -15.248 -22.396 1.00 27.80  ? 158 SER A C   1 
ATOM   1231 O  O   . SER A 1 158 ? 10.770  -14.308 -22.486 1.00 25.15  ? 158 SER A O   1 
ATOM   1232 C  CB  . SER A 1 158 ? 10.027  -17.157 -22.893 1.00 28.59  ? 158 SER A CB  1 
ATOM   1233 O  OG  . SER A 1 158 ? 8.850   -16.374 -22.713 1.00 36.08  ? 158 SER A OG  1 
ATOM   1234 N  N   . PHE A 1 159 ? 12.934  -15.078 -22.547 1.00 24.30  ? 159 PHE A N   1 
ATOM   1235 C  CA  . PHE A 1 159 ? 13.529  -13.793 -22.971 1.00 23.17  ? 159 PHE A CA  1 
ATOM   1236 C  C   . PHE A 1 159 ? 13.334  -13.620 -24.483 1.00 22.58  ? 159 PHE A C   1 
ATOM   1237 O  O   . PHE A 1 159 ? 13.781  -14.487 -25.262 1.00 23.92  ? 159 PHE A O   1 
ATOM   1238 C  CB  . PHE A 1 159 ? 14.994  -13.728 -22.540 1.00 23.53  ? 159 PHE A CB  1 
ATOM   1239 C  CG  . PHE A 1 159 ? 15.194  -13.686 -21.048 1.00 24.05  ? 159 PHE A CG  1 
ATOM   1240 C  CD1 . PHE A 1 159 ? 14.889  -12.541 -20.324 1.00 23.27  ? 159 PHE A CD1 1 
ATOM   1241 C  CD2 . PHE A 1 159 ? 15.690  -14.786 -20.368 1.00 22.83  ? 159 PHE A CD2 1 
ATOM   1242 C  CE1 . PHE A 1 159 ? 15.089  -12.503 -18.951 1.00 24.56  ? 159 PHE A CE1 1 
ATOM   1243 C  CE2 . PHE A 1 159 ? 15.885  -14.747 -18.997 1.00 22.79  ? 159 PHE A CE2 1 
ATOM   1244 C  CZ  . PHE A 1 159 ? 15.578  -13.609 -18.290 1.00 25.06  ? 159 PHE A CZ  1 
ATOM   1245 N  N   . CYS A 1 160 ? 12.738  -12.499 -24.907 1.00 22.96  ? 160 CYS A N   1 
ATOM   1246 C  CA  . CYS A 1 160 ? 12.443  -12.227 -26.337 1.00 20.80  ? 160 CYS A CA  1 
ATOM   1247 C  C   . CYS A 1 160 ? 12.975  -10.887 -26.827 1.00 19.52  ? 160 CYS A C   1 
ATOM   1248 O  O   . CYS A 1 160 ? 12.966  -10.712 -28.053 1.00 22.35  ? 160 CYS A O   1 
ATOM   1249 C  CB  . CYS A 1 160 ? 10.953  -12.295 -26.643 1.00 21.25  ? 160 CYS A CB  1 
ATOM   1250 S  SG  . CYS A 1 160 ? 9.977   -11.211 -25.591 1.00 23.76  ? 160 CYS A SG  1 
ATOM   1251 N  N   . TYR A 1 161 ? 13.417  -9.983  -25.956 1.00 19.22  ? 161 TYR A N   1 
ATOM   1252 C  CA  . TYR A 1 161 ? 13.859  -8.644  -26.398 1.00 19.04  ? 161 TYR A CA  1 
ATOM   1253 C  C   . TYR A 1 161 ? 14.976  -8.131  -25.493 1.00 19.24  ? 161 TYR A C   1 
ATOM   1254 O  O   . TYR A 1 161 ? 14.929  -8.310  -24.255 1.00 17.49  ? 161 TYR A O   1 
ATOM   1255 C  CB  . TYR A 1 161 ? 12.647  -7.697  -26.458 1.00 19.70  ? 161 TYR A CB  1 
ATOM   1256 C  CG  . TYR A 1 161 ? 12.947  -6.263  -26.841 1.00 18.12  ? 161 TYR A CG  1 
ATOM   1257 C  CD1 . TYR A 1 161 ? 13.287  -5.313  -25.898 1.00 19.69  ? 161 TYR A CD1 1 
ATOM   1258 C  CD2 . TYR A 1 161 ? 12.915  -5.855  -28.162 1.00 20.06  ? 161 TYR A CD2 1 
ATOM   1259 C  CE1 . TYR A 1 161 ? 13.530  -3.987  -26.246 1.00 19.56  ? 161 TYR A CE1 1 
ATOM   1260 C  CE2 . TYR A 1 161 ? 13.215  -4.552  -28.535 1.00 20.00  ? 161 TYR A CE2 1 
ATOM   1261 C  CZ  . TYR A 1 161 ? 13.513  -3.609  -27.580 1.00 19.58  ? 161 TYR A CZ  1 
ATOM   1262 O  OH  . TYR A 1 161 ? 13.770  -2.329  -27.999 1.00 21.33  ? 161 TYR A OH  1 
ATOM   1263 N  N   . MET A 1 162 ? 15.981  -7.510  -26.106 1.00 19.75  ? 162 MET A N   1 
ATOM   1264 C  CA  . MET A 1 162 ? 16.976  -6.671  -25.397 1.00 19.19  ? 162 MET A CA  1 
ATOM   1265 C  C   . MET A 1 162 ? 17.027  -5.307  -26.077 1.00 18.13  ? 162 MET A C   1 
ATOM   1266 O  O   . MET A 1 162 ? 17.160  -5.253  -27.313 1.00 17.34  ? 162 MET A O   1 
ATOM   1267 C  CB  . MET A 1 162 ? 18.377  -7.277  -25.434 1.00 20.18  ? 162 MET A CB  1 
ATOM   1268 C  CG  . MET A 1 162 ? 19.404  -6.409  -24.705 1.00 23.04  ? 162 MET A CG  1 
ATOM   1269 S  SD  . MET A 1 162 ? 21.029  -7.233  -24.521 1.00 27.71  ? 162 MET A SD  1 
ATOM   1270 C  CE  . MET A 1 162 ? 20.796  -7.991  -22.917 1.00 24.09  ? 162 MET A CE  1 
ATOM   1271 N  N   . HIS A 1 163 ? 16.993  -4.255  -25.281 1.00 19.06  ? 163 HIS A N   1 
ATOM   1272 C  CA  . HIS A 1 163 ? 16.824  -2.873  -25.786 1.00 19.91  ? 163 HIS A CA  1 
ATOM   1273 C  C   . HIS A 1 163 ? 18.174  -2.320  -26.272 1.00 20.59  ? 163 HIS A C   1 
ATOM   1274 O  O   . HIS A 1 163 ? 19.164  -2.321  -25.484 1.00 18.96  ? 163 HIS A O   1 
ATOM   1275 C  CB  . HIS A 1 163 ? 16.175  -1.985  -24.735 1.00 21.02  ? 163 HIS A CB  1 
ATOM   1276 C  CG  . HIS A 1 163 ? 15.976  -0.599  -25.235 1.00 20.31  ? 163 HIS A CG  1 
ATOM   1277 N  ND1 . HIS A 1 163 ? 15.305  -0.348  -26.397 1.00 20.62  ? 163 HIS A ND1 1 
ATOM   1278 C  CD2 . HIS A 1 163 ? 16.408  0.591   -24.769 1.00 20.79  ? 163 HIS A CD2 1 
ATOM   1279 C  CE1 . HIS A 1 163 ? 15.284  0.957   -26.606 1.00 21.88  ? 163 HIS A CE1 1 
ATOM   1280 N  NE2 . HIS A 1 163 ? 15.975  1.550   -25.639 1.00 21.54  ? 163 HIS A NE2 1 
ATOM   1281 N  N   . HIS A 1 164 ? 18.219  -1.846  -27.521 1.00 19.20  ? 164 HIS A N   1 
ATOM   1282 C  CA  . HIS A 1 164 ? 19.458  -1.282  -28.119 1.00 22.28  ? 164 HIS A CA  1 
ATOM   1283 C  C   . HIS A 1 164 ? 19.348  0.223   -28.365 1.00 22.17  ? 164 HIS A C   1 
ATOM   1284 O  O   . HIS A 1 164 ? 20.369  0.926   -28.152 1.00 23.29  ? 164 HIS A O   1 
ATOM   1285 C  CB  . HIS A 1 164 ? 19.847  -2.029  -29.398 1.00 20.94  ? 164 HIS A CB  1 
ATOM   1286 C  CG  . HIS A 1 164 ? 20.420  -3.378  -29.166 1.00 21.54  ? 164 HIS A CG  1 
ATOM   1287 N  ND1 . HIS A 1 164 ? 21.705  -3.697  -29.558 1.00 21.87  ? 164 HIS A ND1 1 
ATOM   1288 C  CD2 . HIS A 1 164 ? 19.906  -4.487  -28.601 1.00 20.58  ? 164 HIS A CD2 1 
ATOM   1289 C  CE1 . HIS A 1 164 ? 21.944  -4.952  -29.250 1.00 21.52  ? 164 HIS A CE1 1 
ATOM   1290 N  NE2 . HIS A 1 164 ? 20.867  -5.459  -28.662 1.00 21.02  ? 164 HIS A NE2 1 
ATOM   1291 N  N   . MET A 1 165 ? 18.225  0.746   -28.850 1.00 24.17  ? 165 MET A N   1 
ATOM   1292 C  CA  . MET A 1 165 ? 18.250  2.165   -29.306 1.00 25.51  ? 165 MET A CA  1 
ATOM   1293 C  C   . MET A 1 165 ? 16.858  2.784   -29.473 1.00 24.25  ? 165 MET A C   1 
ATOM   1294 O  O   . MET A 1 165 ? 15.854  2.062   -29.629 1.00 21.28  ? 165 MET A O   1 
ATOM   1295 C  CB  . MET A 1 165 ? 18.993  2.291   -30.635 1.00 27.20  ? 165 MET A CB  1 
ATOM   1296 C  CG  . MET A 1 165 ? 18.382  1.460   -31.714 1.00 32.10  ? 165 MET A CG  1 
ATOM   1297 S  SD  . MET A 1 165 ? 19.387  1.450   -33.202 1.00 44.83  ? 165 MET A SD  1 
ATOM   1298 C  CE  . MET A 1 165 ? 18.346  0.524   -34.325 1.00 59.62  ? 165 MET A CE  1 
ATOM   1299 N  N   . GLU A 1 166 ? 16.832  4.117   -29.486 1.00 23.58  ? 166 GLU A N   1 
ATOM   1300 C  CA  . GLU A 1 166 ? 15.604  4.915   -29.732 1.00 24.39  ? 166 GLU A CA  1 
ATOM   1301 C  C   . GLU A 1 166 ? 15.704  5.530   -31.124 1.00 25.08  ? 166 GLU A C   1 
ATOM   1302 O  O   . GLU A 1 166 ? 16.752  6.100   -31.441 1.00 24.75  ? 166 GLU A O   1 
ATOM   1303 C  CB  . GLU A 1 166 ? 15.395  6.017   -28.692 1.00 25.52  ? 166 GLU A CB  1 
ATOM   1304 C  CG  . GLU A 1 166 ? 14.021  6.673   -28.828 1.00 26.69  ? 166 GLU A CG  1 
ATOM   1305 C  CD  . GLU A 1 166 ? 13.610  7.595   -27.700 1.00 27.54  ? 166 GLU A CD  1 
ATOM   1306 O  OE1 . GLU A 1 166 ? 13.450  7.141   -26.552 1.00 26.31  ? 166 GLU A OE1 1 
ATOM   1307 O  OE2 . GLU A 1 166 ? 13.480  8.776   -27.963 1.00 27.61  ? 166 GLU A OE2 1 
ATOM   1308 N  N   . LEU A 1 167 ? 14.669  5.353   -31.937 1.00 25.17  ? 167 LEU A N   1 
ATOM   1309 C  CA  . LEU A 1 167 ? 14.653  5.873   -33.327 1.00 26.78  ? 167 LEU A CA  1 
ATOM   1310 C  C   . LEU A 1 167 ? 14.081  7.280   -33.284 1.00 29.55  ? 167 LEU A C   1 
ATOM   1311 O  O   . LEU A 1 167 ? 13.538  7.684   -32.269 1.00 28.60  ? 167 LEU A O   1 
ATOM   1312 C  CB  . LEU A 1 167 ? 13.855  4.940   -34.250 1.00 27.55  ? 167 LEU A CB  1 
ATOM   1313 C  CG  . LEU A 1 167 ? 14.453  3.543   -34.472 1.00 28.41  ? 167 LEU A CG  1 
ATOM   1314 C  CD1 . LEU A 1 167 ? 13.346  2.550   -34.790 1.00 29.79  ? 167 LEU A CD1 1 
ATOM   1315 C  CD2 . LEU A 1 167 ? 15.503  3.541   -35.569 1.00 29.71  ? 167 LEU A CD2 1 
ATOM   1316 N  N   . PRO A 1 168 ? 14.230  8.085   -34.361 1.00 35.29  ? 168 PRO A N   1 
ATOM   1317 C  CA  . PRO A 1 168 ? 13.851  9.497   -34.319 1.00 37.12  ? 168 PRO A CA  1 
ATOM   1318 C  C   . PRO A 1 168 ? 12.377  9.771   -34.021 1.00 33.79  ? 168 PRO A C   1 
ATOM   1319 O  O   . PRO A 1 168 ? 12.125  10.788  -33.462 1.00 40.19  ? 168 PRO A O   1 
ATOM   1320 C  CB  . PRO A 1 168 ? 14.229  10.008  -35.721 1.00 38.08  ? 168 PRO A CB  1 
ATOM   1321 C  CG  . PRO A 1 168 ? 15.370  9.088   -36.120 1.00 40.83  ? 168 PRO A CG  1 
ATOM   1322 C  CD  . PRO A 1 168 ? 14.909  7.732   -35.622 1.00 39.40  ? 168 PRO A CD  1 
ATOM   1323 N  N   . THR A 1 169 ? 11.449  8.883   -34.376 1.00 31.33  ? 169 THR A N   1 
ATOM   1324 C  CA  . THR A 1 169 ? 10.013  9.055   -34.026 1.00 31.24  ? 169 THR A CA  1 
ATOM   1325 C  C   . THR A 1 169 ? 9.738   8.721   -32.558 1.00 30.08  ? 169 THR A C   1 
ATOM   1326 O  O   . THR A 1 169 ? 8.570   8.748   -32.181 1.00 33.05  ? 169 THR A O   1 
ATOM   1327 C  CB  . THR A 1 169 ? 9.107   8.264   -34.972 1.00 34.57  ? 169 THR A CB  1 
ATOM   1328 O  OG1 . THR A 1 169 ? 9.450   6.882   -34.900 1.00 38.77  ? 169 THR A OG1 1 
ATOM   1329 C  CG2 . THR A 1 169 ? 9.246   8.731   -36.406 1.00 35.33  ? 169 THR A CG2 1 
ATOM   1330 N  N   . GLY A 1 170 ? 10.740  8.453   -31.727 1.00 29.51  ? 170 GLY A N   1 
ATOM   1331 C  CA  . GLY A 1 170 ? 10.512  8.161   -30.295 1.00 30.00  ? 170 GLY A CA  1 
ATOM   1332 C  C   . GLY A 1 170 ? 10.112  6.713   -30.012 1.00 29.06  ? 170 GLY A C   1 
ATOM   1333 O  O   . GLY A 1 170 ? 9.777   6.424   -28.865 1.00 31.79  ? 170 GLY A O   1 
ATOM   1334 N  N   . VAL A 1 171 ? 10.233  5.807   -30.984 1.00 27.35  ? 171 VAL A N   1 
ATOM   1335 C  CA  . VAL A 1 171 ? 9.963   4.356   -30.788 1.00 26.06  ? 171 VAL A CA  1 
ATOM   1336 C  C   . VAL A 1 171 ? 11.302  3.619   -30.651 1.00 24.52  ? 171 VAL A C   1 
ATOM   1337 O  O   . VAL A 1 171 ? 12.370  4.222   -30.844 1.00 23.98  ? 171 VAL A O   1 
ATOM   1338 C  CB  . VAL A 1 171 ? 9.083   3.794   -31.921 1.00 25.15  ? 171 VAL A CB  1 
ATOM   1339 C  CG1 . VAL A 1 171 ? 7.738   4.528   -31.943 1.00 27.08  ? 171 VAL A CG1 1 
ATOM   1340 C  CG2 . VAL A 1 171 ? 9.765   3.838   -33.277 1.00 24.53  ? 171 VAL A CG2 1 
ATOM   1341 N  N   . HIS A 1 172 ? 11.244  2.344   -30.302 1.00 22.42  ? 172 HIS A N   1 
ATOM   1342 C  CA  . HIS A 1 172 ? 12.429  1.614   -29.790 1.00 22.58  ? 172 HIS A CA  1 
ATOM   1343 C  C   . HIS A 1 172 ? 12.693  0.381   -30.641 1.00 23.29  ? 172 HIS A C   1 
ATOM   1344 O  O   . HIS A 1 172 ? 11.727  -0.192  -31.219 1.00 20.89  ? 172 HIS A O   1 
ATOM   1345 C  CB  . HIS A 1 172 ? 12.213  1.322   -28.308 1.00 21.96  ? 172 HIS A CB  1 
ATOM   1346 C  CG  . HIS A 1 172 ? 12.003  2.585   -27.536 1.00 21.45  ? 172 HIS A CG  1 
ATOM   1347 N  ND1 . HIS A 1 172 ? 10.776  2.914   -26.996 1.00 18.90  ? 172 HIS A ND1 1 
ATOM   1348 C  CD2 . HIS A 1 172 ? 12.837  3.615   -27.252 1.00 21.92  ? 172 HIS A CD2 1 
ATOM   1349 C  CE1 . HIS A 1 172 ? 10.865  4.094   -26.396 1.00 20.71  ? 172 HIS A CE1 1 
ATOM   1350 N  NE2 . HIS A 1 172 ? 12.124  4.544   -26.534 1.00 22.92  ? 172 HIS A NE2 1 
ATOM   1351 N  N   . ALA A 1 173 ? 13.979  0.047   -30.753 1.00 20.61  ? 173 ALA A N   1 
ATOM   1352 C  CA  . ALA A 1 173 ? 14.484  -1.068  -31.564 1.00 19.22  ? 173 ALA A CA  1 
ATOM   1353 C  C   . ALA A 1 173 ? 15.506  -1.860  -30.761 1.00 20.14  ? 173 ALA A C   1 
ATOM   1354 O  O   . ALA A 1 173 ? 16.239  -1.298  -29.914 1.00 18.27  ? 173 ALA A O   1 
ATOM   1355 C  CB  . ALA A 1 173 ? 15.052  -0.558  -32.860 1.00 20.62  ? 173 ALA A CB  1 
ATOM   1356 N  N   . GLY A 1 174 ? 15.513  -3.162  -30.996 1.00 22.03  ? 174 GLY A N   1 
ATOM   1357 C  CA  . GLY A 1 174 ? 16.350  -4.070  -30.210 1.00 20.39  ? 174 GLY A CA  1 
ATOM   1358 C  C   . GLY A 1 174 ? 16.458  -5.415  -30.878 1.00 21.26  ? 174 GLY A C   1 
ATOM   1359 O  O   . GLY A 1 174 ? 16.004  -5.596  -32.055 1.00 21.32  ? 174 GLY A O   1 
ATOM   1360 N  N   . THR A 1 175 ? 16.985  -6.362  -30.122 1.00 21.46  ? 175 THR A N   1 
ATOM   1361 C  CA  . THR A 1 175 ? 17.353  -7.688  -30.644 1.00 19.81  ? 175 THR A CA  1 
ATOM   1362 C  C   . THR A 1 175 ? 16.638  -8.741  -29.846 1.00 20.32  ? 175 THR A C   1 
ATOM   1363 O  O   . THR A 1 175 ? 16.183  -8.454  -28.746 1.00 19.52  ? 175 THR A O   1 
ATOM   1364 C  CB  . THR A 1 175 ? 18.862  -7.946  -30.565 1.00 19.22  ? 175 THR A CB  1 
ATOM   1365 O  OG1 . THR A 1 175 ? 19.270  -7.986  -29.203 1.00 18.91  ? 175 THR A OG1 1 
ATOM   1366 C  CG2 . THR A 1 175 ? 19.623  -6.866  -31.284 1.00 19.92  ? 175 THR A CG2 1 
ATOM   1367 N  N   . ASP A 1 176 ? 16.617  -9.942  -30.402 1.00 19.10  ? 176 ASP A N   1 
ATOM   1368 C  CA  . ASP A 1 176 ? 16.359  -11.146 -29.591 1.00 20.81  ? 176 ASP A CA  1 
ATOM   1369 C  C   . ASP A 1 176 ? 17.619  -11.386 -28.759 1.00 22.34  ? 176 ASP A C   1 
ATOM   1370 O  O   . ASP A 1 176 ? 18.618  -10.597 -28.902 1.00 21.54  ? 176 ASP A O   1 
ATOM   1371 C  CB  . ASP A 1 176 ? 15.907  -12.309 -30.476 1.00 22.70  ? 176 ASP A CB  1 
ATOM   1372 C  CG  . ASP A 1 176 ? 16.975  -12.827 -31.423 1.00 22.60  ? 176 ASP A CG  1 
ATOM   1373 O  OD1 . ASP A 1 176 ? 18.191  -12.683 -31.117 1.00 24.01  ? 176 ASP A OD1 1 
ATOM   1374 O  OD2 . ASP A 1 176 ? 16.589  -13.268 -32.485 1.00 22.13  ? 176 ASP A OD2 1 
ATOM   1375 N  N   . LEU A 1 177 ? 17.598  -12.397 -27.885 1.00 22.70  ? 177 LEU A N   1 
ATOM   1376 C  CA  . LEU A 1 177 ? 18.753  -12.684 -26.993 1.00 23.71  ? 177 LEU A CA  1 
ATOM   1377 C  C   . LEU A 1 177 ? 19.814  -13.493 -27.742 1.00 24.27  ? 177 LEU A C   1 
ATOM   1378 O  O   . LEU A 1 177 ? 20.848  -13.766 -27.113 1.00 28.38  ? 177 LEU A O   1 
ATOM   1379 C  CB  . LEU A 1 177 ? 18.304  -13.399 -25.718 1.00 23.72  ? 177 LEU A CB  1 
ATOM   1380 C  CG  . LEU A 1 177 ? 17.904  -12.462 -24.582 1.00 22.78  ? 177 LEU A CG  1 
ATOM   1381 C  CD1 . LEU A 1 177 ? 19.108  -11.707 -24.034 1.00 23.51  ? 177 LEU A CD1 1 
ATOM   1382 C  CD2 . LEU A 1 177 ? 16.841  -11.484 -25.063 1.00 26.06  ? 177 LEU A CD2 1 
ATOM   1383 N  N   . GLU A 1 178 ? 19.618  -13.799 -29.028 1.00 25.49  ? 178 GLU A N   1 
ATOM   1384 C  CA  . GLU A 1 178 ? 20.726  -14.290 -29.904 1.00 27.76  ? 178 GLU A CA  1 
ATOM   1385 C  C   . GLU A 1 178 ? 21.377  -13.119 -30.639 1.00 26.49  ? 178 GLU A C   1 
ATOM   1386 O  O   . GLU A 1 178 ? 22.258  -13.395 -31.484 1.00 25.96  ? 178 GLU A O   1 
ATOM   1387 C  CB  . GLU A 1 178 ? 20.240  -15.344 -30.894 1.00 31.09  ? 178 GLU A CB  1 
ATOM   1388 C  CG  . GLU A 1 178 ? 19.687  -16.564 -30.194 1.00 38.31  ? 178 GLU A CG  1 
ATOM   1389 C  CD  . GLU A 1 178 ? 19.307  -17.686 -31.138 1.00 41.87  ? 178 GLU A CD  1 
ATOM   1390 O  OE1 . GLU A 1 178 ? 18.772  -17.397 -32.223 1.00 47.63  ? 178 GLU A OE1 1 
ATOM   1391 O  OE2 . GLU A 1 178 ? 19.595  -18.833 -30.794 1.00 48.37  ? 178 GLU A OE2 1 
ATOM   1392 N  N   . GLY A 1 179 ? 20.948  -11.876 -30.364 1.00 23.71  ? 179 GLY A N   1 
ATOM   1393 C  CA  . GLY A 1 179 ? 21.573  -10.657 -30.919 1.00 22.00  ? 179 GLY A CA  1 
ATOM   1394 C  C   . GLY A 1 179 ? 21.077  -10.272 -32.306 1.00 21.39  ? 179 GLY A C   1 
ATOM   1395 O  O   . GLY A 1 179 ? 21.675  -9.366  -32.912 1.00 25.06  ? 179 GLY A O   1 
ATOM   1396 N  N   . ASN A 1 180 ? 20.060  -10.927 -32.858 1.00 24.59  ? 180 ASN A N   1 
ATOM   1397 C  CA  . ASN A 1 180 ? 19.493  -10.535 -34.187 1.00 23.54  ? 180 ASN A CA  1 
ATOM   1398 C  C   . ASN A 1 180 ? 18.426  -9.470  -33.983 1.00 25.07  ? 180 ASN A C   1 
ATOM   1399 O  O   . ASN A 1 180 ? 17.477  -9.707  -33.163 1.00 24.04  ? 180 ASN A O   1 
ATOM   1400 C  CB  . ASN A 1 180 ? 18.914  -11.708 -34.953 1.00 25.04  ? 180 ASN A CB  1 
ATOM   1401 C  CG  . ASN A 1 180 ? 19.983  -12.749 -35.230 1.00 26.97  ? 180 ASN A CG  1 
ATOM   1402 O  OD1 . ASN A 1 180 ? 19.906  -13.872 -34.742 1.00 31.39  ? 180 ASN A OD1 1 
ATOM   1403 N  ND2 . ASN A 1 180 ? 21.032  -12.344 -35.906 1.00 27.79  ? 180 ASN A ND2 1 
ATOM   1404 N  N   . PHE A 1 181 ? 18.601  -8.334  -34.657 1.00 23.35  ? 181 PHE A N   1 
ATOM   1405 C  CA  . PHE A 1 181 ? 17.653  -7.202  -34.586 1.00 23.34  ? 181 PHE A CA  1 
ATOM   1406 C  C   . PHE A 1 181 ? 16.291  -7.700  -35.060 1.00 22.11  ? 181 PHE A C   1 
ATOM   1407 O  O   . PHE A 1 181 ? 16.224  -8.571  -35.972 1.00 21.68  ? 181 PHE A O   1 
ATOM   1408 C  CB  . PHE A 1 181 ? 18.121  -5.994  -35.399 1.00 22.32  ? 181 PHE A CB  1 
ATOM   1409 C  CG  . PHE A 1 181 ? 18.822  -4.944  -34.584 1.00 20.85  ? 181 PHE A CG  1 
ATOM   1410 C  CD1 . PHE A 1 181 ? 20.204  -4.971  -34.427 1.00 24.06  ? 181 PHE A CD1 1 
ATOM   1411 C  CD2 . PHE A 1 181 ? 18.109  -3.938  -33.957 1.00 22.39  ? 181 PHE A CD2 1 
ATOM   1412 C  CE1 . PHE A 1 181 ? 20.849  -4.015  -33.643 1.00 23.18  ? 181 PHE A CE1 1 
ATOM   1413 C  CE2 . PHE A 1 181 ? 18.751  -2.982  -33.181 1.00 22.13  ? 181 PHE A CE2 1 
ATOM   1414 C  CZ  . PHE A 1 181 ? 20.121  -3.024  -33.024 1.00 22.00  ? 181 PHE A CZ  1 
ATOM   1415 N  N   . TYR A 1 182 ? 15.246  -7.150  -34.441 1.00 20.48  ? 182 TYR A N   1 
ATOM   1416 C  CA  . TYR A 1 182 ? 13.881  -7.105  -35.005 1.00 20.38  ? 182 TYR A CA  1 
ATOM   1417 C  C   . TYR A 1 182 ? 13.855  -6.008  -36.074 1.00 20.84  ? 182 TYR A C   1 
ATOM   1418 O  O   . TYR A 1 182 ? 14.313  -4.894  -35.839 1.00 23.42  ? 182 TYR A O   1 
ATOM   1419 C  CB  . TYR A 1 182 ? 12.847  -6.945  -33.892 1.00 20.78  ? 182 TYR A CB  1 
ATOM   1420 C  CG  . TYR A 1 182 ? 12.728  -8.121  -32.948 1.00 22.49  ? 182 TYR A CG  1 
ATOM   1421 C  CD1 . TYR A 1 182 ? 12.025  -9.263  -33.320 1.00 23.30  ? 182 TYR A CD1 1 
ATOM   1422 C  CD2 . TYR A 1 182 ? 13.294  -8.103  -31.678 1.00 22.47  ? 182 TYR A CD2 1 
ATOM   1423 C  CE1 . TYR A 1 182 ? 11.885  -10.345 -32.468 1.00 20.56  ? 182 TYR A CE1 1 
ATOM   1424 C  CE2 . TYR A 1 182 ? 13.131  -9.172  -30.798 1.00 21.08  ? 182 TYR A CE2 1 
ATOM   1425 C  CZ  . TYR A 1 182 ? 12.434  -10.306 -31.197 1.00 20.66  ? 182 TYR A CZ  1 
ATOM   1426 O  OH  . TYR A 1 182 ? 12.289  -11.386 -30.343 1.00 19.04  ? 182 TYR A OH  1 
ATOM   1427 N  N   . GLY A 1 183 ? 13.354  -6.353  -37.251 1.00 22.11  ? 183 GLY A N   1 
ATOM   1428 C  CA  . GLY A 1 183 ? 13.222  -5.436  -38.387 1.00 22.75  ? 183 GLY A CA  1 
ATOM   1429 C  C   . GLY A 1 183 ? 14.566  -5.163  -39.045 1.00 27.31  ? 183 GLY A C   1 
ATOM   1430 O  O   . GLY A 1 183 ? 15.570  -5.838  -38.803 1.00 30.19  ? 183 GLY A O   1 
ATOM   1431 N  N   . PRO A 1 184 ? 14.615  -4.146  -39.915 1.00 28.23  ? 184 PRO A N   1 
ATOM   1432 C  CA  . PRO A 1 184 ? 15.808  -3.893  -40.726 1.00 30.42  ? 184 PRO A CA  1 
ATOM   1433 C  C   . PRO A 1 184 ? 16.862  -3.019  -40.028 1.00 28.18  ? 184 PRO A C   1 
ATOM   1434 O  O   . PRO A 1 184 ? 17.686  -2.523  -40.676 1.00 31.02  ? 184 PRO A O   1 
ATOM   1435 C  CB  . PRO A 1 184 ? 15.167  -3.191  -41.941 1.00 29.43  ? 184 PRO A CB  1 
ATOM   1436 C  CG  . PRO A 1 184 ? 14.027  -2.390  -41.342 1.00 29.76  ? 184 PRO A CG  1 
ATOM   1437 C  CD  . PRO A 1 184 ? 13.504  -3.226  -40.198 1.00 30.33  ? 184 PRO A CD  1 
ATOM   1438 N  N   . PHE A 1 185 ? 16.808  -2.878  -38.708 1.00 28.24  ? 185 PHE A N   1 
ATOM   1439 C  CA  . PHE A 1 185 ? 17.641  -1.909  -37.968 1.00 25.86  ? 185 PHE A CA  1 
ATOM   1440 C  C   . PHE A 1 185 ? 19.035  -2.501  -37.746 1.00 23.02  ? 185 PHE A C   1 
ATOM   1441 O  O   . PHE A 1 185 ? 19.235  -3.743  -37.779 1.00 22.42  ? 185 PHE A O   1 
ATOM   1442 C  CB  . PHE A 1 185 ? 16.926  -1.496  -36.682 1.00 26.99  ? 185 PHE A CB  1 
ATOM   1443 C  CG  . PHE A 1 185 ? 15.552  -0.977  -36.981 1.00 24.71  ? 185 PHE A CG  1 
ATOM   1444 C  CD1 . PHE A 1 185 ? 15.415  0.143   -37.779 1.00 24.23  ? 185 PHE A CD1 1 
ATOM   1445 C  CD2 . PHE A 1 185 ? 14.419  -1.658  -36.578 1.00 26.42  ? 185 PHE A CD2 1 
ATOM   1446 C  CE1 . PHE A 1 185 ? 14.164  0.598   -38.148 1.00 22.42  ? 185 PHE A CE1 1 
ATOM   1447 C  CE2 . PHE A 1 185 ? 13.167  -1.194  -36.942 1.00 25.49  ? 185 PHE A CE2 1 
ATOM   1448 C  CZ  . PHE A 1 185 ? 13.047  -0.067  -37.718 1.00 23.90  ? 185 PHE A CZ  1 
ATOM   1449 N  N   . VAL A 1 186 ? 19.976  -1.589  -37.568 1.00 24.17  ? 186 VAL A N   1 
ATOM   1450 C  CA  . VAL A 1 186 ? 21.408  -1.886  -37.277 1.00 27.36  ? 186 VAL A CA  1 
ATOM   1451 C  C   . VAL A 1 186 ? 21.872  -1.040  -36.085 1.00 27.87  ? 186 VAL A C   1 
ATOM   1452 O  O   . VAL A 1 186 ? 21.313  0.068   -35.859 1.00 27.21  ? 186 VAL A O   1 
ATOM   1453 C  CB  . VAL A 1 186 ? 22.283  -1.608  -38.510 1.00 26.40  ? 186 VAL A CB  1 
ATOM   1454 C  CG1 . VAL A 1 186 ? 21.990  -2.573  -39.631 1.00 25.07  ? 186 VAL A CG1 1 
ATOM   1455 C  CG2 . VAL A 1 186 ? 22.123  -0.176  -38.986 1.00 27.15  ? 186 VAL A CG2 1 
ATOM   1456 N  N   . ASP A 1 187 ? 22.893  -1.532  -35.379 1.00 24.93  ? 187 ASP A N   1 
ATOM   1457 C  CA  . ASP A 1 187 ? 23.476  -0.836  -34.212 1.00 23.86  ? 187 ASP A CA  1 
ATOM   1458 C  C   . ASP A 1 187 ? 24.557  0.110   -34.729 1.00 25.76  ? 187 ASP A C   1 
ATOM   1459 O  O   . ASP A 1 187 ? 25.729  -0.039  -34.346 1.00 22.55  ? 187 ASP A O   1 
ATOM   1460 C  CB  . ASP A 1 187 ? 23.918  -1.831  -33.143 1.00 22.88  ? 187 ASP A CB  1 
ATOM   1461 C  CG  . ASP A 1 187 ? 24.847  -2.956  -33.567 1.00 22.66  ? 187 ASP A CG  1 
ATOM   1462 O  OD1 . ASP A 1 187 ? 25.122  -3.114  -34.779 1.00 22.13  ? 187 ASP A OD1 1 
ATOM   1463 O  OD2 . ASP A 1 187 ? 25.276  -3.710  -32.659 1.00 23.31  ? 187 ASP A OD2 1 
ATOM   1464 N  N   . ARG A 1 188 ? 24.121  1.096   -35.509 1.00 26.38  ? 188 ARG A N   1 
ATOM   1465 C  CA  . ARG A 1 188 ? 24.912  2.248   -36.018 1.00 27.80  ? 188 ARG A CA  1 
ATOM   1466 C  C   . ARG A 1 188 ? 24.030  3.489   -35.901 1.00 26.00  ? 188 ARG A C   1 
ATOM   1467 O  O   . ARG A 1 188 ? 22.812  3.376   -36.116 1.00 22.55  ? 188 ARG A O   1 
ATOM   1468 C  CB  . ARG A 1 188 ? 25.254  2.101   -37.516 1.00 28.77  ? 188 ARG A CB  1 
ATOM   1469 C  CG  . ARG A 1 188 ? 26.210  0.974   -37.871 1.00 28.97  ? 188 ARG A CG  1 
ATOM   1470 C  CD  . ARG A 1 188 ? 26.131  0.627   -39.353 1.00 29.06  ? 188 ARG A CD  1 
ATOM   1471 N  NE  . ARG A 1 188 ? 26.455  1.775   -40.170 1.00 28.57  ? 188 ARG A NE  1 
ATOM   1472 C  CZ  . ARG A 1 188 ? 26.160  1.899   -41.468 1.00 30.73  ? 188 ARG A CZ  1 
ATOM   1473 N  NH1 . ARG A 1 188 ? 25.474  0.950   -42.076 1.00 31.26  ? 188 ARG A NH1 1 
ATOM   1474 N  NH2 . ARG A 1 188 ? 26.527  2.986   -42.149 1.00 27.82  ? 188 ARG A NH2 1 
ATOM   1475 N  N   . GLN A 1 189 ? 24.631  4.650   -35.709 1.00 30.11  ? 189 GLN A N   1 
ATOM   1476 C  CA  . GLN A 1 189 ? 23.872  5.924   -35.627 1.00 33.59  ? 189 GLN A CA  1 
ATOM   1477 C  C   . GLN A 1 189 ? 23.740  6.576   -36.999 1.00 35.96  ? 189 GLN A C   1 
ATOM   1478 O  O   . GLN A 1 189 ? 23.537  7.791   -37.026 1.00 42.53  ? 189 GLN A O   1 
ATOM   1479 C  CB  . GLN A 1 189 ? 24.522  6.818   -34.579 1.00 39.65  ? 189 GLN A CB  1 
ATOM   1480 C  CG  . GLN A 1 189 ? 24.224  6.277   -33.185 1.00 48.65  ? 189 GLN A CG  1 
ATOM   1481 C  CD  . GLN A 1 189 ? 24.286  7.332   -32.105 1.00 60.26  ? 189 GLN A CD  1 
ATOM   1482 O  OE1 . GLN A 1 189 ? 25.065  8.286   -32.178 1.00 63.96  ? 189 GLN A OE1 1 
ATOM   1483 N  NE2 . GLN A 1 189 ? 23.460  7.158   -31.082 1.00 60.27  ? 189 GLN A NE2 1 
ATOM   1484 N  N   . THR A 1 190 ? 23.815  5.793   -38.081 1.00 33.80  ? 190 THR A N   1 
ATOM   1485 C  CA  . THR A 1 190 ? 23.413  6.207   -39.447 1.00 35.28  ? 190 THR A CA  1 
ATOM   1486 C  C   . THR A 1 190 ? 21.904  6.482   -39.403 1.00 33.80  ? 190 THR A C   1 
ATOM   1487 O  O   . THR A 1 190 ? 21.221  5.861   -38.573 1.00 33.81  ? 190 THR A O   1 
ATOM   1488 C  CB  . THR A 1 190 ? 23.836  5.141   -40.474 1.00 34.20  ? 190 THR A CB  1 
ATOM   1489 O  OG1 . THR A 1 190 ? 23.842  5.745   -41.768 1.00 39.13  ? 190 THR A OG1 1 
ATOM   1490 C  CG2 . THR A 1 190 ? 22.932  3.925   -40.462 1.00 32.15  ? 190 THR A CG2 1 
ATOM   1491 N  N   . ALA A 1 191 ? 21.411  7.400   -40.232 1.00 35.59  ? 191 ALA A N   1 
ATOM   1492 C  CA  . ALA A 1 191 ? 19.965  7.704   -40.380 1.00 39.45  ? 191 ALA A CA  1 
ATOM   1493 C  C   . ALA A 1 191 ? 19.191  6.401   -40.603 1.00 35.62  ? 191 ALA A C   1 
ATOM   1494 O  O   . ALA A 1 191 ? 19.536  5.641   -41.521 1.00 32.36  ? 191 ALA A O   1 
ATOM   1495 C  CB  . ALA A 1 191 ? 19.718  8.669   -41.518 1.00 43.69  ? 191 ALA A CB  1 
ATOM   1496 N  N   . GLN A 1 192 ? 18.237  6.116   -39.723 1.00 34.99  ? 192 GLN A N   1 
ATOM   1497 C  CA  . GLN A 1 192 ? 17.289  4.975   -39.848 1.00 34.14  ? 192 GLN A CA  1 
ATOM   1498 C  C   . GLN A 1 192 ? 15.917  5.469   -39.393 1.00 33.96  ? 192 GLN A C   1 
ATOM   1499 O  O   . GLN A 1 192 ? 15.849  6.299   -38.456 1.00 33.37  ? 192 GLN A O   1 
ATOM   1500 C  CB  . GLN A 1 192 ? 17.679  3.798   -38.950 1.00 32.37  ? 192 GLN A CB  1 
ATOM   1501 C  CG  . GLN A 1 192 ? 19.129  3.383   -39.050 1.00 32.11  ? 192 GLN A CG  1 
ATOM   1502 C  CD  . GLN A 1 192 ? 19.416  2.236   -38.118 1.00 31.77  ? 192 GLN A CD  1 
ATOM   1503 O  OE1 . GLN A 1 192 ? 18.834  1.165   -38.230 1.00 29.75  ? 192 GLN A OE1 1 
ATOM   1504 N  NE2 . GLN A 1 192 ? 20.332  2.458   -37.193 1.00 34.12  ? 192 GLN A NE2 1 
ATOM   1505 N  N   . ALA A 1 193 ? 14.856  4.961   -39.998 1.00 35.70  ? 193 ALA A N   1 
ATOM   1506 C  CA  . ALA A 1 193 ? 13.481  5.332   -39.590 1.00 37.98  ? 193 ALA A CA  1 
ATOM   1507 C  C   . ALA A 1 193 ? 12.594  4.107   -39.757 1.00 35.84  ? 193 ALA A C   1 
ATOM   1508 O  O   . ALA A 1 193 ? 12.875  3.278   -40.628 1.00 32.67  ? 193 ALA A O   1 
ATOM   1509 C  CB  . ALA A 1 193 ? 12.985  6.541   -40.357 1.00 35.48  ? 193 ALA A CB  1 
ATOM   1510 N  N   . ALA A 1 194 ? 11.626  3.965   -38.858 1.00 39.61  ? 194 ALA A N   1 
ATOM   1511 C  CA  . ALA A 1 194 ? 10.687  2.828   -38.849 1.00 38.71  ? 194 ALA A CA  1 
ATOM   1512 C  C   . ALA A 1 194 ? 9.761   2.981   -40.050 1.00 38.11  ? 194 ALA A C   1 
ATOM   1513 O  O   . ALA A 1 194 ? 9.475   4.132   -40.409 1.00 34.93  ? 194 ALA A O   1 
ATOM   1514 C  CB  . ALA A 1 194 ? 9.921   2.826   -37.559 1.00 43.75  ? 194 ALA A CB  1 
ATOM   1515 N  N   . GLY A 1 195 ? 9.377   1.866   -40.667 1.00 40.70  ? 195 GLY A N   1 
ATOM   1516 C  CA  . GLY A 1 195 ? 8.259   1.807   -41.619 1.00 40.48  ? 195 GLY A CA  1 
ATOM   1517 C  C   . GLY A 1 195 ? 6.994   2.389   -41.002 1.00 38.76  ? 195 GLY A C   1 
ATOM   1518 O  O   . GLY A 1 195 ? 6.885   2.445   -39.749 1.00 32.34  ? 195 GLY A O   1 
ATOM   1519 N  N   . THR A 1 196 ? 6.083   2.872   -41.849 1.00 39.07  ? 196 THR A N   1 
ATOM   1520 C  CA  . THR A 1 196 ? 4.700   3.253   -41.462 1.00 37.68  ? 196 THR A CA  1 
ATOM   1521 C  C   . THR A 1 196 ? 4.135   2.083   -40.657 1.00 33.06  ? 196 THR A C   1 
ATOM   1522 O  O   . THR A 1 196 ? 4.162   0.962   -41.160 1.00 41.03  ? 196 THR A O   1 
ATOM   1523 C  CB  . THR A 1 196 ? 3.833   3.557   -42.693 1.00 41.19  ? 196 THR A CB  1 
ATOM   1524 O  OG1 . THR A 1 196 ? 4.021   2.482   -43.620 1.00 48.45  ? 196 THR A OG1 1 
ATOM   1525 C  CG2 . THR A 1 196 ? 4.187   4.880   -43.340 1.00 40.98  ? 196 THR A CG2 1 
ATOM   1526 N  N   . ASP A 1 197 ? 3.686   2.345   -39.443 1.00 29.87  ? 197 ASP A N   1 
ATOM   1527 C  CA  . ASP A 1 197 ? 3.137   1.312   -38.542 1.00 32.20  ? 197 ASP A CA  1 
ATOM   1528 C  C   . ASP A 1 197 ? 1.678   1.025   -38.915 1.00 38.10  ? 197 ASP A C   1 
ATOM   1529 O  O   . ASP A 1 197 ? 1.033   1.886   -39.565 1.00 43.41  ? 197 ASP A O   1 
ATOM   1530 C  CB  . ASP A 1 197 ? 3.198   1.723   -37.072 1.00 30.39  ? 197 ASP A CB  1 
ATOM   1531 C  CG  . ASP A 1 197 ? 3.145   0.478   -36.193 1.00 31.77  ? 197 ASP A CG  1 
ATOM   1532 O  OD1 . ASP A 1 197 ? 3.467   -0.621  -36.746 1.00 30.40  ? 197 ASP A OD1 1 
ATOM   1533 O  OD2 . ASP A 1 197 ? 2.779   0.601   -35.012 1.00 28.94  ? 197 ASP A OD2 1 
ATOM   1534 N  N   . THR A 1 198 ? 1.178   -0.141  -38.516 1.00 33.23  ? 198 THR A N   1 
ATOM   1535 C  CA  . THR A 1 198 ? -0.224  -0.538  -38.762 1.00 30.55  ? 198 THR A CA  1 
ATOM   1536 C  C   . THR A 1 198 ? -0.813  -1.067  -37.458 1.00 24.47  ? 198 THR A C   1 
ATOM   1537 O  O   . THR A 1 198 ? -0.065  -1.257  -36.479 1.00 22.98  ? 198 THR A O   1 
ATOM   1538 C  CB  . THR A 1 198 ? -0.281  -1.524  -39.925 1.00 32.25  ? 198 THR A CB  1 
ATOM   1539 O  OG1 . THR A 1 198 ? 0.503   -2.632  -39.505 1.00 35.10  ? 198 THR A OG1 1 
ATOM   1540 C  CG2 . THR A 1 198 ? 0.257   -0.955  -41.219 1.00 31.62  ? 198 THR A CG2 1 
ATOM   1541 N  N   . THR A 1 199 ? -2.126  -1.217  -37.421 1.00 21.57  ? 199 THR A N   1 
ATOM   1542 C  CA  . THR A 1 199 ? -2.837  -1.745  -36.244 1.00 20.27  ? 199 THR A CA  1 
ATOM   1543 C  C   . THR A 1 199 ? -2.857  -3.259  -36.327 1.00 19.63  ? 199 THR A C   1 
ATOM   1544 O  O   . THR A 1 199 ? -3.013  -3.809  -37.425 1.00 22.32  ? 199 THR A O   1 
ATOM   1545 C  CB  . THR A 1 199 ? -4.238  -1.143  -36.137 1.00 23.21  ? 199 THR A CB  1 
ATOM   1546 O  OG1 . THR A 1 199 ? -4.057  0.265   -36.085 1.00 23.04  ? 199 THR A OG1 1 
ATOM   1547 C  CG2 . THR A 1 199 ? -4.982  -1.614  -34.909 1.00 23.12  ? 199 THR A CG2 1 
ATOM   1548 N  N   . ILE A 1 200 ? -2.705  -3.911  -35.175 1.00 20.16  ? 200 ILE A N   1 
ATOM   1549 C  CA  . ILE A 1 200 ? -2.621  -5.388  -35.126 1.00 20.17  ? 200 ILE A CA  1 
ATOM   1550 C  C   . ILE A 1 200 ? -4.055  -5.903  -35.030 1.00 22.25  ? 200 ILE A C   1 
ATOM   1551 O  O   . ILE A 1 200 ? -4.592  -6.028  -33.898 1.00 21.84  ? 200 ILE A O   1 
ATOM   1552 C  CB  . ILE A 1 200 ? -1.736  -5.888  -33.981 1.00 19.24  ? 200 ILE A CB  1 
ATOM   1553 C  CG1 . ILE A 1 200 ? -0.328  -5.291  -34.033 1.00 22.06  ? 200 ILE A CG1 1 
ATOM   1554 C  CG2 . ILE A 1 200 ? -1.684  -7.398  -33.991 1.00 18.42  ? 200 ILE A CG2 1 
ATOM   1555 C  CD1 . ILE A 1 200 ? 0.278   -5.112  -32.672 1.00 24.18  ? 200 ILE A CD1 1 
ATOM   1556 N  N   . THR A 1 201 ? -4.641  -6.168  -36.191 1.00 23.77  ? 201 THR A N   1 
ATOM   1557 C  CA  . THR A 1 201 ? -6.082  -6.473  -36.352 1.00 23.38  ? 201 THR A CA  1 
ATOM   1558 C  C   . THR A 1 201 ? -6.490  -7.626  -35.423 1.00 22.47  ? 201 THR A C   1 
ATOM   1559 O  O   . THR A 1 201 ? -7.479  -7.469  -34.657 1.00 25.70  ? 201 THR A O   1 
ATOM   1560 C  CB  . THR A 1 201 ? -6.366  -6.736  -37.834 1.00 22.25  ? 201 THR A CB  1 
ATOM   1561 O  OG1 . THR A 1 201 ? -5.858  -5.601  -38.533 1.00 19.79  ? 201 THR A OG1 1 
ATOM   1562 C  CG2 . THR A 1 201 ? -7.843  -6.960  -38.101 1.00 23.94  ? 201 THR A CG2 1 
ATOM   1563 N  N   . VAL A 1 202 ? -5.815  -8.763  -35.501 1.00 22.01  ? 202 VAL A N   1 
ATOM   1564 C  CA  . VAL A 1 202 ? -6.145  -9.946  -34.659 1.00 20.65  ? 202 VAL A CA  1 
ATOM   1565 C  C   . VAL A 1 202 ? -6.217  -9.552  -33.179 1.00 22.81  ? 202 VAL A C   1 
ATOM   1566 O  O   . VAL A 1 202 ? -7.081  -10.094 -32.474 1.00 20.71  ? 202 VAL A O   1 
ATOM   1567 C  CB  . VAL A 1 202 ? -5.168  -11.104 -34.893 1.00 20.87  ? 202 VAL A CB  1 
ATOM   1568 C  CG1 . VAL A 1 202 ? -3.729  -10.777 -34.499 1.00 21.12  ? 202 VAL A CG1 1 
ATOM   1569 C  CG2 . VAL A 1 202 ? -5.650  -12.344 -34.173 1.00 22.01  ? 202 VAL A CG2 1 
ATOM   1570 N  N   . ASN A 1 203 ? -5.335  -8.670  -32.703 1.00 22.64  ? 203 ASN A N   1 
ATOM   1571 C  CA  . ASN A 1 203 ? -5.329  -8.265  -31.270 1.00 23.38  ? 203 ASN A CA  1 
ATOM   1572 C  C   . ASN A 1 203 ? -6.560  -7.377  -30.997 1.00 23.33  ? 203 ASN A C   1 
ATOM   1573 O  O   . ASN A 1 203 ? -7.132  -7.487  -29.894 1.00 22.37  ? 203 ASN A O   1 
ATOM   1574 C  CB  . ASN A 1 203 ? -4.027  -7.566  -30.874 1.00 22.95  ? 203 ASN A CB  1 
ATOM   1575 C  CG  . ASN A 1 203 ? -2.824  -8.480  -30.799 1.00 23.71  ? 203 ASN A CG  1 
ATOM   1576 O  OD1 . ASN A 1 203 ? -2.945  -9.697  -30.971 1.00 21.48  ? 203 ASN A OD1 1 
ATOM   1577 N  ND2 . ASN A 1 203 ? -1.660  -7.897  -30.488 1.00 22.43  ? 203 ASN A ND2 1 
ATOM   1578 N  N   . VAL A 1 204 ? -6.943  -6.505  -31.923 1.00 21.88  ? 204 VAL A N   1 
ATOM   1579 C  CA  . VAL A 1 204 ? -8.147  -5.643  -31.743 1.00 23.02  ? 204 VAL A CA  1 
ATOM   1580 C  C   . VAL A 1 204 ? -9.364  -6.563  -31.570 1.00 23.20  ? 204 VAL A C   1 
ATOM   1581 O  O   . VAL A 1 204 ? -10.124 -6.366  -30.607 1.00 24.35  ? 204 VAL A O   1 
ATOM   1582 C  CB  . VAL A 1 204 ? -8.328  -4.637  -32.890 1.00 24.62  ? 204 VAL A CB  1 
ATOM   1583 C  CG1 . VAL A 1 204 ? -9.675  -3.925  -32.802 1.00 26.74  ? 204 VAL A CG1 1 
ATOM   1584 C  CG2 . VAL A 1 204 ? -7.198  -3.613  -32.926 1.00 21.74  ? 204 VAL A CG2 1 
ATOM   1585 N  N   . LEU A 1 205 ? -9.496  -7.576  -32.417 1.00 22.23  ? 205 LEU A N   1 
ATOM   1586 C  CA  . LEU A 1 205 ? -10.638 -8.522  -32.342 1.00 23.70  ? 205 LEU A CA  1 
ATOM   1587 C  C   . LEU A 1 205 ? -10.622 -9.241  -30.995 1.00 24.65  ? 205 LEU A C   1 
ATOM   1588 O  O   . LEU A 1 205 ? -11.710 -9.446  -30.399 1.00 22.74  ? 205 LEU A O   1 
ATOM   1589 C  CB  . LEU A 1 205 ? -10.555 -9.511  -33.502 1.00 21.54  ? 205 LEU A CB  1 
ATOM   1590 C  CG  . LEU A 1 205 ? -10.771 -8.895  -34.873 1.00 22.11  ? 205 LEU A CG  1 
ATOM   1591 C  CD1 . LEU A 1 205 ? -10.409 -9.893  -35.953 1.00 22.71  ? 205 LEU A CD1 1 
ATOM   1592 C  CD2 . LEU A 1 205 ? -12.207 -8.411  -35.022 1.00 22.93  ? 205 LEU A CD2 1 
ATOM   1593 N  N   . ALA A 1 206 ? -9.446  -9.657  -30.522 1.00 26.88  ? 206 ALA A N   1 
ATOM   1594 C  CA  . ALA A 1 206 ? -9.334  -10.411 -29.251 1.00 24.99  ? 206 ALA A CA  1 
ATOM   1595 C  C   . ALA A 1 206 ? -9.842  -9.521  -28.107 1.00 22.93  ? 206 ALA A C   1 
ATOM   1596 O  O   . ALA A 1 206 ? -10.541 -10.007 -27.211 1.00 24.16  ? 206 ALA A O   1 
ATOM   1597 C  CB  . ALA A 1 206 ? -7.908  -10.881 -29.032 1.00 25.84  ? 206 ALA A CB  1 
ATOM   1598 N  N   . TRP A 1 207 ? -9.509  -8.252  -28.153 1.00 21.36  ? 207 TRP A N   1 
ATOM   1599 C  CA  . TRP A 1 207 ? -9.888  -7.273  -27.116 1.00 23.50  ? 207 TRP A CA  1 
ATOM   1600 C  C   . TRP A 1 207 ? -11.391 -7.011  -27.174 1.00 25.16  ? 207 TRP A C   1 
ATOM   1601 O  O   . TRP A 1 207 ? -11.987 -6.819  -26.098 1.00 25.60  ? 207 TRP A O   1 
ATOM   1602 C  CB  . TRP A 1 207 ? -9.045  -6.022  -27.337 1.00 24.00  ? 207 TRP A CB  1 
ATOM   1603 C  CG  . TRP A 1 207 ? -9.370  -4.824  -26.518 1.00 23.63  ? 207 TRP A CG  1 
ATOM   1604 C  CD1 . TRP A 1 207 ? -8.983  -4.536  -25.240 1.00 26.49  ? 207 TRP A CD1 1 
ATOM   1605 C  CD2 . TRP A 1 207 ? -10.059 -3.669  -27.010 1.00 24.76  ? 207 TRP A CD2 1 
ATOM   1606 N  NE1 . TRP A 1 207 ? -9.424  -3.285  -24.891 1.00 25.19  ? 207 TRP A NE1 1 
ATOM   1607 C  CE2 . TRP A 1 207 ? -10.060 -2.724  -25.970 1.00 28.06  ? 207 TRP A CE2 1 
ATOM   1608 C  CE3 . TRP A 1 207 ? -10.680 -3.359  -28.223 1.00 26.55  ? 207 TRP A CE3 1 
ATOM   1609 C  CZ2 . TRP A 1 207 ? -10.681 -1.489  -26.111 1.00 27.89  ? 207 TRP A CZ2 1 
ATOM   1610 C  CZ3 . TRP A 1 207 ? -11.252 -2.121  -28.375 1.00 28.42  ? 207 TRP A CZ3 1 
ATOM   1611 C  CH2 . TRP A 1 207 ? -11.266 -1.213  -27.320 1.00 28.26  ? 207 TRP A CH2 1 
ATOM   1612 N  N   . LEU A 1 208 ? -12.000 -7.051  -28.367 1.00 25.97  ? 208 LEU A N   1 
ATOM   1613 C  CA  . LEU A 1 208 ? -13.483 -6.892  -28.481 1.00 25.73  ? 208 LEU A CA  1 
ATOM   1614 C  C   . LEU A 1 208 ? -14.146 -8.123  -27.855 1.00 25.38  ? 208 LEU A C   1 
ATOM   1615 O  O   . LEU A 1 208 ? -15.160 -7.946  -27.152 1.00 26.37  ? 208 LEU A O   1 
ATOM   1616 C  CB  . LEU A 1 208 ? -13.918 -6.743  -29.935 1.00 22.83  ? 208 LEU A CB  1 
ATOM   1617 C  CG  . LEU A 1 208 ? -13.578 -5.424  -30.605 1.00 25.08  ? 208 LEU A CG  1 
ATOM   1618 C  CD1 . LEU A 1 208 ? -13.950 -5.498  -32.065 1.00 24.39  ? 208 LEU A CD1 1 
ATOM   1619 C  CD2 . LEU A 1 208 ? -14.252 -4.242  -29.934 1.00 26.88  ? 208 LEU A CD2 1 
ATOM   1620 N  N   . TYR A 1 209 ? -13.570 -9.308  -28.058 1.00 24.72  ? 209 TYR A N   1 
ATOM   1621 C  CA  . TYR A 1 209 ? -13.992 -10.564 -27.380 1.00 25.33  ? 209 TYR A CA  1 
ATOM   1622 C  C   . TYR A 1 209 ? -13.867 -10.410 -25.859 1.00 27.34  ? 209 TYR A C   1 
ATOM   1623 O  O   . TYR A 1 209 ? -14.833 -10.750 -25.158 1.00 28.74  ? 209 TYR A O   1 
ATOM   1624 C  CB  . TYR A 1 209 ? -13.214 -11.781 -27.896 1.00 24.00  ? 209 TYR A CB  1 
ATOM   1625 C  CG  . TYR A 1 209 ? -13.769 -12.398 -29.160 1.00 23.70  ? 209 TYR A CG  1 
ATOM   1626 C  CD1 . TYR A 1 209 ? -15.056 -12.918 -29.217 1.00 24.17  ? 209 TYR A CD1 1 
ATOM   1627 C  CD2 . TYR A 1 209 ? -13.045 -12.389 -30.339 1.00 26.55  ? 209 TYR A CD2 1 
ATOM   1628 C  CE1 . TYR A 1 209 ? -15.580 -13.447 -30.386 1.00 25.77  ? 209 TYR A CE1 1 
ATOM   1629 C  CE2 . TYR A 1 209 ? -13.550 -12.923 -31.516 1.00 25.58  ? 209 TYR A CE2 1 
ATOM   1630 C  CZ  . TYR A 1 209 ? -14.830 -13.453 -31.554 1.00 26.81  ? 209 TYR A CZ  1 
ATOM   1631 O  OH  . TYR A 1 209 ? -15.336 -14.000 -32.719 1.00 23.01  ? 209 TYR A OH  1 
ATOM   1632 N  N   . ALA A 1 210 ? -12.750 -9.870  -25.367 1.00 26.95  ? 210 ALA A N   1 
ATOM   1633 C  CA  . ALA A 1 210 ? -12.563 -9.539  -23.932 1.00 28.70  ? 210 ALA A CA  1 
ATOM   1634 C  C   . ALA A 1 210 ? -13.750 -8.695  -23.452 1.00 29.65  ? 210 ALA A C   1 
ATOM   1635 O  O   . ALA A 1 210 ? -14.286 -8.987  -22.360 1.00 29.26  ? 210 ALA A O   1 
ATOM   1636 C  CB  . ALA A 1 210 ? -11.271 -8.800  -23.681 1.00 27.63  ? 210 ALA A CB  1 
ATOM   1637 N  N   . ALA A 1 211 ? -14.098 -7.652  -24.204 1.00 27.92  ? 211 ALA A N   1 
ATOM   1638 C  CA  . ALA A 1 211 ? -15.115 -6.663  -23.807 1.00 29.12  ? 211 ALA A CA  1 
ATOM   1639 C  C   . ALA A 1 211 ? -16.439 -7.395  -23.627 1.00 29.48  ? 211 ALA A C   1 
ATOM   1640 O  O   . ALA A 1 211 ? -17.099 -7.142  -22.608 1.00 30.57  ? 211 ALA A O   1 
ATOM   1641 C  CB  . ALA A 1 211 ? -15.228 -5.551  -24.826 1.00 30.50  ? 211 ALA A CB  1 
ATOM   1642 N  N   . VAL A 1 212 ? -16.758 -8.312  -24.548 1.00 27.07  ? 212 VAL A N   1 
ATOM   1643 C  CA  . VAL A 1 212 ? -18.013 -9.110  -24.509 1.00 29.52  ? 212 VAL A CA  1 
ATOM   1644 C  C   . VAL A 1 212 ? -18.001 -10.056 -23.305 1.00 31.79  ? 212 VAL A C   1 
ATOM   1645 O  O   . VAL A 1 212 ? -18.982 -10.109 -22.542 1.00 33.58  ? 212 VAL A O   1 
ATOM   1646 C  CB  . VAL A 1 212 ? -18.227 -9.849  -25.837 1.00 28.37  ? 212 VAL A CB  1 
ATOM   1647 C  CG1 . VAL A 1 212 ? -19.299 -10.922 -25.717 1.00 27.38  ? 212 VAL A CG1 1 
ATOM   1648 C  CG2 . VAL A 1 212 ? -18.574 -8.854  -26.940 1.00 26.75  ? 212 VAL A CG2 1 
ATOM   1649 N  N   . ILE A 1 213 ? -16.929 -10.796 -23.122 1.00 32.19  ? 213 ILE A N   1 
ATOM   1650 C  CA  . ILE A 1 213 ? -16.746 -11.635 -21.905 1.00 30.09  ? 213 ILE A CA  1 
ATOM   1651 C  C   . ILE A 1 213 ? -17.031 -10.798 -20.651 1.00 31.79  ? 213 ILE A C   1 
ATOM   1652 O  O   . ILE A 1 213 ? -17.670 -11.324 -19.726 1.00 32.71  ? 213 ILE A O   1 
ATOM   1653 C  CB  . ILE A 1 213 ? -15.326 -12.206 -21.906 1.00 29.08  ? 213 ILE A CB  1 
ATOM   1654 C  CG1 . ILE A 1 213 ? -15.237 -13.351 -22.921 1.00 30.76  ? 213 ILE A CG1 1 
ATOM   1655 C  CG2 . ILE A 1 213 ? -14.915 -12.588 -20.484 1.00 29.83  ? 213 ILE A CG2 1 
ATOM   1656 C  CD1 . ILE A 1 213 ? -13.836 -13.753 -23.312 1.00 29.71  ? 213 ILE A CD1 1 
ATOM   1657 N  N   . ASN A 1 214 ? -16.587 -9.542  -20.620 1.00 31.42  ? 214 ASN A N   1 
ATOM   1658 C  CA  . ASN A 1 214 ? -16.715 -8.647  -19.443 1.00 35.66  ? 214 ASN A CA  1 
ATOM   1659 C  C   . ASN A 1 214 ? -18.063 -7.902  -19.452 1.00 35.45  ? 214 ASN A C   1 
ATOM   1660 O  O   . ASN A 1 214 ? -18.270 -7.044  -18.572 1.00 36.08  ? 214 ASN A O   1 
ATOM   1661 C  CB  . ASN A 1 214 ? -15.507 -7.713  -19.351 1.00 40.74  ? 214 ASN A CB  1 
ATOM   1662 C  CG  . ASN A 1 214 ? -14.304 -8.393  -18.719 1.00 48.39  ? 214 ASN A CG  1 
ATOM   1663 O  OD1 . ASN A 1 214 ? -13.579 -9.144  -19.378 1.00 52.37  ? 214 ASN A OD1 1 
ATOM   1664 N  ND2 . ASN A 1 214 ? -14.106 -8.160  -17.428 1.00 45.40  ? 214 ASN A ND2 1 
ATOM   1665 N  N   . GLY A 1 215 ? -18.953 -8.214  -20.389 1.00 32.38  ? 215 GLY A N   1 
ATOM   1666 C  CA  . GLY A 1 215 ? -20.375 -7.829  -20.310 1.00 36.37  ? 215 GLY A CA  1 
ATOM   1667 C  C   . GLY A 1 215 ? -20.801 -6.673  -21.206 1.00 38.64  ? 215 GLY A C   1 
ATOM   1668 O  O   . GLY A 1 215 ? -21.951 -6.231  -21.080 1.00 40.66  ? 215 GLY A O   1 
ATOM   1669 N  N   A ASP A 1 216 ? -19.888 -6.172  -22.050 0.24 37.22  ? 216 ASP A N   1 
ATOM   1670 N  N   B ASP A 1 216 ? -19.938 -6.217  -22.119 0.26 37.23  ? 216 ASP A N   1 
ATOM   1671 N  N   C ASP A 1 216 ? -19.888 -6.172  -22.050 0.24 37.22  ? 216 ASP A N   1 
ATOM   1672 N  N   D ASP A 1 216 ? -19.938 -6.217  -22.119 0.26 37.23  ? 216 ASP A N   1 
ATOM   1673 C  CA  A ASP A 1 216 ? -20.149 -5.101  -23.050 0.24 36.73  ? 216 ASP A CA  1 
ATOM   1674 C  CA  B ASP A 1 216 ? -20.238 -5.053  -22.995 0.26 37.14  ? 216 ASP A CA  1 
ATOM   1675 C  CA  C ASP A 1 216 ? -20.149 -5.101  -23.050 0.24 36.73  ? 216 ASP A CA  1 
ATOM   1676 C  CA  D ASP A 1 216 ? -20.238 -5.053  -22.995 0.26 37.14  ? 216 ASP A CA  1 
ATOM   1677 C  C   A ASP A 1 216 ? -20.672 -5.754  -24.334 0.24 36.94  ? 216 ASP A C   1 
ATOM   1678 C  C   B ASP A 1 216 ? -20.588 -5.560  -24.400 0.26 37.05  ? 216 ASP A C   1 
ATOM   1679 C  C   C ASP A 1 216 ? -20.672 -5.754  -24.334 0.24 36.94  ? 216 ASP A C   1 
ATOM   1680 C  C   D ASP A 1 216 ? -20.588 -5.560  -24.400 0.26 37.05  ? 216 ASP A C   1 
ATOM   1681 O  O   A ASP A 1 216 ? -19.985 -6.661  -24.844 0.24 35.72  ? 216 ASP A O   1 
ATOM   1682 O  O   B ASP A 1 216 ? -19.692 -6.130  -25.061 0.26 34.11  ? 216 ASP A O   1 
ATOM   1683 O  O   C ASP A 1 216 ? -19.985 -6.661  -24.844 0.24 35.72  ? 216 ASP A O   1 
ATOM   1684 O  O   D ASP A 1 216 ? -19.692 -6.130  -25.061 0.26 34.11  ? 216 ASP A O   1 
ATOM   1685 C  CB  A ASP A 1 216 ? -18.886 -4.293  -23.374 0.24 37.28  ? 216 ASP A CB  1 
ATOM   1686 C  CB  B ASP A 1 216 ? -19.089 -4.041  -22.992 0.26 38.20  ? 216 ASP A CB  1 
ATOM   1687 C  CB  C ASP A 1 216 ? -18.886 -4.293  -23.374 0.24 37.28  ? 216 ASP A CB  1 
ATOM   1688 C  CB  D ASP A 1 216 ? -19.089 -4.041  -22.992 0.26 38.20  ? 216 ASP A CB  1 
ATOM   1689 C  CG  A ASP A 1 216 ? -18.292 -3.521  -22.206 0.24 36.56  ? 216 ASP A CG  1 
ATOM   1690 C  CG  B ASP A 1 216 ? -19.581 -2.605  -22.963 0.26 38.74  ? 216 ASP A CG  1 
ATOM   1691 C  CG  C ASP A 1 216 ? -18.292 -3.521  -22.206 0.24 36.56  ? 216 ASP A CG  1 
ATOM   1692 C  CG  D ASP A 1 216 ? -19.581 -2.605  -22.963 0.26 38.74  ? 216 ASP A CG  1 
ATOM   1693 O  OD1 A ASP A 1 216 ? -19.022 -3.305  -21.215 0.24 36.62  ? 216 ASP A OD1 1 
ATOM   1694 O  OD1 B ASP A 1 216 ? -20.817 -2.417  -22.990 0.26 41.15  ? 216 ASP A OD1 1 
ATOM   1695 O  OD1 C ASP A 1 216 ? -19.022 -3.305  -21.215 0.24 36.62  ? 216 ASP A OD1 1 
ATOM   1696 O  OD1 D ASP A 1 216 ? -20.817 -2.417  -22.990 0.26 41.15  ? 216 ASP A OD1 1 
ATOM   1697 O  OD2 A ASP A 1 216 ? -17.095 -3.143  -22.295 0.24 34.93  ? 216 ASP A OD2 1 
ATOM   1698 O  OD2 B ASP A 1 216 ? -18.733 -1.687  -22.908 0.26 37.08  ? 216 ASP A OD2 1 
ATOM   1699 O  OD2 C ASP A 1 216 ? -17.095 -3.143  -22.295 0.24 34.93  ? 216 ASP A OD2 1 
ATOM   1700 O  OD2 D ASP A 1 216 ? -18.733 -1.687  -22.908 0.26 37.08  ? 216 ASP A OD2 1 
ATOM   1701 N  N   . ARG A 1 217 ? -21.833 -5.323  -24.840 1.00 35.11  ? 217 ARG A N   1 
ATOM   1702 C  CA  . ARG A 1 217 ? -22.362 -5.830  -26.141 1.00 35.28  ? 217 ARG A CA  1 
ATOM   1703 C  C   . ARG A 1 217 ? -22.754 -4.700  -27.093 1.00 33.48  ? 217 ARG A C   1 
ATOM   1704 O  O   . ARG A 1 217 ? -23.218 -5.032  -28.219 1.00 28.18  ? 217 ARG A O   1 
ATOM   1705 C  CB  . ARG A 1 217 ? -23.561 -6.753  -25.926 1.00 38.14  ? 217 ARG A CB  1 
ATOM   1706 C  CG  . ARG A 1 217 ? -23.180 -8.105  -25.342 1.00 40.49  ? 217 ARG A CG  1 
ATOM   1707 C  CD  . ARG A 1 217 ? -24.362 -9.032  -25.293 1.00 43.76  ? 217 ARG A CD  1 
ATOM   1708 N  NE  . ARG A 1 217 ? -24.864 -9.366  -26.630 1.00 46.45  ? 217 ARG A NE  1 
ATOM   1709 C  CZ  . ARG A 1 217 ? -24.610 -10.498 -27.293 1.00 47.60  ? 217 ARG A CZ  1 
ATOM   1710 N  NH1 . ARG A 1 217 ? -23.831 -11.426 -26.756 1.00 44.81  ? 217 ARG A NH1 1 
ATOM   1711 N  NH2 . ARG A 1 217 ? -25.137 -10.689 -28.496 1.00 47.25  ? 217 ARG A NH2 1 
ATOM   1712 N  N   . TRP A 1 218 ? -22.551 -3.437  -26.719 1.00 30.34  ? 218 TRP A N   1 
ATOM   1713 C  CA  . TRP A 1 218 ? -23.173 -2.315  -27.463 1.00 28.56  ? 218 TRP A CA  1 
ATOM   1714 C  C   . TRP A 1 218 ? -22.694 -2.238  -28.926 1.00 28.06  ? 218 TRP A C   1 
ATOM   1715 O  O   . TRP A 1 218 ? -23.466 -1.702  -29.760 1.00 25.24  ? 218 TRP A O   1 
ATOM   1716 C  CB  . TRP A 1 218 ? -22.967 -0.986  -26.757 1.00 29.32  ? 218 TRP A CB  1 
ATOM   1717 C  CG  . TRP A 1 218 ? -21.547 -0.532  -26.641 1.00 32.51  ? 218 TRP A CG  1 
ATOM   1718 C  CD1 . TRP A 1 218 ? -20.748 -0.629  -25.538 1.00 33.07  ? 218 TRP A CD1 1 
ATOM   1719 C  CD2 . TRP A 1 218 ? -20.795 0.187   -27.627 1.00 31.70  ? 218 TRP A CD2 1 
ATOM   1720 N  NE1 . TRP A 1 218 ? -19.550 -0.018  -25.774 1.00 34.48  ? 218 TRP A NE1 1 
ATOM   1721 C  CE2 . TRP A 1 218 ? -19.536 0.466   -27.053 1.00 32.23  ? 218 TRP A CE2 1 
ATOM   1722 C  CE3 . TRP A 1 218 ? -21.054 0.618   -28.938 1.00 32.66  ? 218 TRP A CE3 1 
ATOM   1723 C  CZ2 . TRP A 1 218 ? -18.549 1.163   -27.748 1.00 32.74  ? 218 TRP A CZ2 1 
ATOM   1724 C  CZ3 . TRP A 1 218 ? -20.077 1.313   -29.621 1.00 30.99  ? 218 TRP A CZ3 1 
ATOM   1725 C  CH2 . TRP A 1 218 ? -18.835 1.559   -29.036 1.00 30.03  ? 218 TRP A CH2 1 
ATOM   1726 N  N   . PHE A 1 219 ? -21.481 -2.694  -29.237 1.00 24.52  ? 219 PHE A N   1 
ATOM   1727 C  CA  . PHE A 1 219 ? -20.822 -2.461  -30.545 1.00 24.97  ? 219 PHE A CA  1 
ATOM   1728 C  C   . PHE A 1 219 ? -21.092 -3.626  -31.484 1.00 26.11  ? 219 PHE A C   1 
ATOM   1729 O  O   . PHE A 1 219 ? -20.627 -3.584  -32.642 1.00 30.26  ? 219 PHE A O   1 
ATOM   1730 C  CB  . PHE A 1 219 ? -19.302 -2.307  -30.374 1.00 27.13  ? 219 PHE A CB  1 
ATOM   1731 C  CG  . PHE A 1 219 ? -18.692 -3.331  -29.453 1.00 24.86  ? 219 PHE A CG  1 
ATOM   1732 C  CD1 . PHE A 1 219 ? -18.354 -4.589  -29.907 1.00 23.72  ? 219 PHE A CD1 1 
ATOM   1733 C  CD2 . PHE A 1 219 ? -18.530 -3.049  -28.104 1.00 25.93  ? 219 PHE A CD2 1 
ATOM   1734 C  CE1 . PHE A 1 219 ? -17.845 -5.540  -29.034 1.00 25.40  ? 219 PHE A CE1 1 
ATOM   1735 C  CE2 . PHE A 1 219 ? -18.008 -3.997  -27.238 1.00 25.36  ? 219 PHE A CE2 1 
ATOM   1736 C  CZ  . PHE A 1 219 ? -17.679 -5.244  -27.697 1.00 24.11  ? 219 PHE A CZ  1 
ATOM   1737 N  N   . LEU A 1 220 ? -21.782 -4.667  -31.040 1.00 26.78  ? 220 LEU A N   1 
ATOM   1738 C  CA  . LEU A 1 220 ? -22.102 -5.795  -31.952 1.00 27.74  ? 220 LEU A CA  1 
ATOM   1739 C  C   . LEU A 1 220 ? -23.157 -5.337  -32.965 1.00 30.88  ? 220 LEU A C   1 
ATOM   1740 O  O   . LEU A 1 220 ? -23.825 -4.316  -32.725 1.00 28.44  ? 220 LEU A O   1 
ATOM   1741 C  CB  . LEU A 1 220 ? -22.606 -6.988  -31.146 1.00 30.33  ? 220 LEU A CB  1 
ATOM   1742 C  CG  . LEU A 1 220 ? -21.649 -7.520  -30.085 1.00 31.66  ? 220 LEU A CG  1 
ATOM   1743 C  CD1 . LEU A 1 220 ? -22.301 -8.667  -29.338 1.00 32.34  ? 220 LEU A CD1 1 
ATOM   1744 C  CD2 . LEU A 1 220 ? -20.338 -7.979  -30.732 1.00 33.14  ? 220 LEU A CD2 1 
ATOM   1745 N  N   . ASN A 1 221 ? -23.289 -6.051  -34.077 1.00 30.28  ? 221 ASN A N   1 
ATOM   1746 C  CA  . ASN A 1 221 ? -24.314 -5.718  -35.094 1.00 28.16  ? 221 ASN A CA  1 
ATOM   1747 C  C   . ASN A 1 221 ? -24.852 -7.016  -35.667 1.00 32.02  ? 221 ASN A C   1 
ATOM   1748 O  O   . ASN A 1 221 ? -24.297 -8.086  -35.369 1.00 31.95  ? 221 ASN A O   1 
ATOM   1749 C  CB  . ASN A 1 221 ? -23.779 -4.779  -36.168 1.00 26.97  ? 221 ASN A CB  1 
ATOM   1750 C  CG  . ASN A 1 221 ? -22.729 -5.399  -37.074 1.00 29.77  ? 221 ASN A CG  1 
ATOM   1751 O  OD1 . ASN A 1 221 ? -22.642 -6.622  -37.213 1.00 29.53  ? 221 ASN A OD1 1 
ATOM   1752 N  ND2 . ASN A 1 221 ? -21.943 -4.552  -37.728 1.00 31.74  ? 221 ASN A ND2 1 
ATOM   1753 N  N   . ARG A 1 222 ? -25.900 -6.912  -36.473 1.00 36.77  ? 222 ARG A N   1 
ATOM   1754 C  CA  . ARG A 1 222 ? -26.569 -8.103  -37.043 1.00 38.70  ? 222 ARG A CA  1 
ATOM   1755 C  C   . ARG A 1 222 ? -25.866 -8.506  -38.331 1.00 36.17  ? 222 ARG A C   1 
ATOM   1756 O  O   . ARG A 1 222 ? -26.333 -9.430  -38.975 1.00 37.62  ? 222 ARG A O   1 
ATOM   1757 C  CB  . ARG A 1 222 ? -28.047 -7.801  -37.272 1.00 47.25  ? 222 ARG A CB  1 
ATOM   1758 C  CG  . ARG A 1 222 ? -28.301 -6.621  -38.201 1.00 57.55  ? 222 ARG A CG  1 
ATOM   1759 C  CD  . ARG A 1 222 ? -29.774 -6.548  -38.572 1.00 65.89  ? 222 ARG A CD  1 
ATOM   1760 N  NE  . ARG A 1 222 ? -30.020 -5.722  -39.738 1.00 69.19  ? 222 ARG A NE  1 
ATOM   1761 C  CZ  . ARG A 1 222 ? -29.844 -6.110  -40.998 1.00 78.66  ? 222 ARG A CZ  1 
ATOM   1762 N  NH1 . ARG A 1 222 ? -29.412 -7.333  -41.277 1.00 82.52  ? 222 ARG A NH1 1 
ATOM   1763 N  NH2 . ARG A 1 222 ? -30.106 -5.268  -41.985 1.00 79.92  ? 222 ARG A NH2 1 
ATOM   1764 N  N   . PHE A 1 223 ? -24.751 -7.879  -38.683 1.00 36.91  ? 223 PHE A N   1 
ATOM   1765 C  CA  . PHE A 1 223 ? -24.052 -8.176  -39.951 1.00 36.32  ? 223 PHE A CA  1 
ATOM   1766 C  C   . PHE A 1 223 ? -22.936 -9.206  -39.774 1.00 33.88  ? 223 PHE A C   1 
ATOM   1767 O  O   . PHE A 1 223 ? -22.425 -9.456  -38.658 1.00 31.09  ? 223 PHE A O   1 
ATOM   1768 C  CB  . PHE A 1 223 ? -23.488 -6.906  -40.580 1.00 40.28  ? 223 PHE A CB  1 
ATOM   1769 C  CG  . PHE A 1 223 ? -24.577 -5.970  -41.009 1.00 41.03  ? 223 PHE A CG  1 
ATOM   1770 C  CD1 . PHE A 1 223 ? -25.416 -6.314  -42.050 1.00 46.33  ? 223 PHE A CD1 1 
ATOM   1771 C  CD2 . PHE A 1 223 ? -24.803 -4.785  -40.326 1.00 48.50  ? 223 PHE A CD2 1 
ATOM   1772 C  CE1 . PHE A 1 223 ? -26.447 -5.469  -42.431 1.00 54.44  ? 223 PHE A CE1 1 
ATOM   1773 C  CE2 . PHE A 1 223 ? -25.842 -3.947  -40.698 1.00 51.15  ? 223 PHE A CE2 1 
ATOM   1774 C  CZ  . PHE A 1 223 ? -26.662 -4.288  -41.753 1.00 52.71  ? 223 PHE A CZ  1 
ATOM   1775 N  N   . THR A 1 224 ? -22.551 -9.752  -40.921 1.00 31.20  ? 224 THR A N   1 
ATOM   1776 C  CA  . THR A 1 224 ? -21.329 -10.562 -41.106 1.00 33.99  ? 224 THR A CA  1 
ATOM   1777 C  C   . THR A 1 224 ? -20.541 -9.989  -42.289 1.00 30.16  ? 224 THR A C   1 
ATOM   1778 O  O   . THR A 1 224 ? -20.957 -8.963  -42.870 1.00 27.99  ? 224 THR A O   1 
ATOM   1779 C  CB  . THR A 1 224 ? -21.657 -12.052 -41.271 1.00 38.72  ? 224 THR A CB  1 
ATOM   1780 O  OG1 . THR A 1 224 ? -20.428 -12.729 -41.002 1.00 38.56  ? 224 THR A OG1 1 
ATOM   1781 C  CG2 . THR A 1 224 ? -22.184 -12.422 -42.647 1.00 40.55  ? 224 THR A CG2 1 
ATOM   1782 N  N   . THR A 1 225 ? -19.404 -10.605 -42.598 1.00 29.68  ? 225 THR A N   1 
ATOM   1783 C  CA  . THR A 1 225 ? -18.520 -10.162 -43.701 1.00 27.05  ? 225 THR A CA  1 
ATOM   1784 C  C   . THR A 1 225 ? -17.769 -11.385 -44.170 1.00 23.84  ? 225 THR A C   1 
ATOM   1785 O  O   . THR A 1 225 ? -17.654 -12.305 -43.386 1.00 25.71  ? 225 THR A O   1 
ATOM   1786 C  CB  . THR A 1 225 ? -17.568 -9.037  -43.262 1.00 28.29  ? 225 THR A CB  1 
ATOM   1787 O  OG1 . THR A 1 225 ? -16.780 -8.654  -44.400 1.00 26.80  ? 225 THR A OG1 1 
ATOM   1788 C  CG2 . THR A 1 225 ? -16.672 -9.464  -42.117 1.00 27.96  ? 225 THR A CG2 1 
ATOM   1789 N  N   . THR A 1 226 ? -17.357 -11.404 -45.426 1.00 23.56  ? 226 THR A N   1 
ATOM   1790 C  CA  . THR A 1 226 ? -16.322 -12.330 -45.931 1.00 23.68  ? 226 THR A CA  1 
ATOM   1791 C  C   . THR A 1 226 ? -14.967 -11.849 -45.407 1.00 24.42  ? 226 THR A C   1 
ATOM   1792 O  O   . THR A 1 226 ? -14.813 -10.639 -45.104 1.00 22.24  ? 226 THR A O   1 
ATOM   1793 C  CB  . THR A 1 226 ? -16.286 -12.422 -47.464 1.00 23.27  ? 226 THR A CB  1 
ATOM   1794 O  OG1 . THR A 1 226 ? -15.820 -11.183 -47.996 1.00 22.06  ? 226 THR A OG1 1 
ATOM   1795 C  CG2 . THR A 1 226 ? -17.633 -12.799 -48.061 1.00 22.59  ? 226 THR A CG2 1 
ATOM   1796 N  N   . LEU A 1 227 ? -14.022 -12.766 -45.293 1.00 27.45  ? 227 LEU A N   1 
ATOM   1797 C  CA  . LEU A 1 227 ? -12.658 -12.412 -44.851 1.00 28.50  ? 227 LEU A CA  1 
ATOM   1798 C  C   . LEU A 1 227 ? -12.072 -11.419 -45.845 1.00 27.15  ? 227 LEU A C   1 
ATOM   1799 O  O   . LEU A 1 227 ? -11.433 -10.451 -45.409 1.00 27.54  ? 227 LEU A O   1 
ATOM   1800 C  CB  . LEU A 1 227 ? -11.807 -13.672 -44.789 1.00 30.10  ? 227 LEU A CB  1 
ATOM   1801 C  CG  . LEU A 1 227 ? -10.392 -13.464 -44.263 1.00 29.25  ? 227 LEU A CG  1 
ATOM   1802 C  CD1 . LEU A 1 227 ? -10.372 -12.670 -42.952 1.00 27.90  ? 227 LEU A CD1 1 
ATOM   1803 C  CD2 . LEU A 1 227 ? -9.734  -14.814 -44.096 1.00 28.96  ? 227 LEU A CD2 1 
ATOM   1804 N  N   . ASN A 1 228 ? -12.248 -11.670 -47.146 1.00 24.90  ? 228 ASN A N   1 
ATOM   1805 C  CA  . ASN A 1 228 ? -11.670 -10.779 -48.184 1.00 25.81  ? 228 ASN A CA  1 
ATOM   1806 C  C   . ASN A 1 228 ? -12.255 -9.362  -48.084 1.00 23.64  ? 228 ASN A C   1 
ATOM   1807 O  O   . ASN A 1 228 ? -11.475 -8.388  -48.184 1.00 23.79  ? 228 ASN A O   1 
ATOM   1808 C  CB  . ASN A 1 228 ? -11.908 -11.292 -49.604 1.00 30.11  ? 228 ASN A CB  1 
ATOM   1809 C  CG  . ASN A 1 228 ? -10.993 -10.586 -50.578 1.00 35.62  ? 228 ASN A CG  1 
ATOM   1810 O  OD1 . ASN A 1 228 ? -9.767  -10.702 -50.465 1.00 48.00  ? 228 ASN A OD1 1 
ATOM   1811 N  ND2 . ASN A 1 228 ? -11.562 -9.823  -51.496 1.00 40.36  ? 228 ASN A ND2 1 
ATOM   1812 N  N   . ASP A 1 229 ? -13.590 -9.218  -47.993 1.00 23.27  ? 229 ASP A N   1 
ATOM   1813 C  CA  . ASP A 1 229 ? -14.222 -7.869  -47.891 1.00 23.60  ? 229 ASP A CA  1 
ATOM   1814 C  C   . ASP A 1 229 ? -13.743 -7.166  -46.603 1.00 23.06  ? 229 ASP A C   1 
ATOM   1815 O  O   . ASP A 1 229 ? -13.528 -5.945  -46.609 1.00 21.81  ? 229 ASP A O   1 
ATOM   1816 C  CB  . ASP A 1 229 ? -15.751 -7.963  -47.932 1.00 24.58  ? 229 ASP A CB  1 
ATOM   1817 C  CG  . ASP A 1 229 ? -16.302 -8.175  -49.332 1.00 26.91  ? 229 ASP A CG  1 
ATOM   1818 O  OD1 . ASP A 1 229 ? -15.520 -7.978  -50.284 1.00 25.17  ? 229 ASP A OD1 1 
ATOM   1819 O  OD2 . ASP A 1 229 ? -17.522 -8.506  -49.445 1.00 26.11  ? 229 ASP A OD2 1 
ATOM   1820 N  N   . PHE A 1 230 ? -13.609 -7.905  -45.512 1.00 24.05  ? 230 PHE A N   1 
ATOM   1821 C  CA  . PHE A 1 230 ? -13.070 -7.335  -44.256 1.00 23.83  ? 230 PHE A CA  1 
ATOM   1822 C  C   . PHE A 1 230 ? -11.681 -6.733  -44.521 1.00 24.16  ? 230 PHE A C   1 
ATOM   1823 O  O   . PHE A 1 230 ? -11.453 -5.555  -44.164 1.00 23.26  ? 230 PHE A O   1 
ATOM   1824 C  CB  . PHE A 1 230 ? -13.023 -8.373  -43.141 1.00 25.73  ? 230 PHE A CB  1 
ATOM   1825 C  CG  . PHE A 1 230 ? -12.331 -7.790  -41.943 1.00 26.59  ? 230 PHE A CG  1 
ATOM   1826 C  CD1 . PHE A 1 230 ? -12.963 -6.825  -41.176 1.00 26.59  ? 230 PHE A CD1 1 
ATOM   1827 C  CD2 . PHE A 1 230 ? -11.000 -8.092  -41.692 1.00 27.46  ? 230 PHE A CD2 1 
ATOM   1828 C  CE1 . PHE A 1 230 ? -12.304 -6.249  -40.106 1.00 27.84  ? 230 PHE A CE1 1 
ATOM   1829 C  CE2 . PHE A 1 230 ? -10.333 -7.494  -40.639 1.00 24.88  ? 230 PHE A CE2 1 
ATOM   1830 C  CZ  . PHE A 1 230 ? -10.981 -6.560  -39.868 1.00 28.42  ? 230 PHE A CZ  1 
ATOM   1831 N  N   . ASN A 1 231 ? -10.793 -7.480  -45.175 1.00 24.06  ? 231 ASN A N   1 
ATOM   1832 C  CA  . ASN A 1 231 ? -9.390  -7.013  -45.363 1.00 26.04  ? 231 ASN A CA  1 
ATOM   1833 C  C   . ASN A 1 231 ? -9.382  -5.793  -46.282 1.00 26.67  ? 231 ASN A C   1 
ATOM   1834 O  O   . ASN A 1 231 ? -8.599  -4.871  -46.030 1.00 24.10  ? 231 ASN A O   1 
ATOM   1835 C  CB  . ASN A 1 231 ? -8.463  -8.132  -45.826 1.00 26.19  ? 231 ASN A CB  1 
ATOM   1836 C  CG  . ASN A 1 231 ? -8.132  -9.061  -44.684 1.00 28.18  ? 231 ASN A CG  1 
ATOM   1837 O  OD1 . ASN A 1 231 ? -7.956  -8.615  -43.553 1.00 31.82  ? 231 ASN A OD1 1 
ATOM   1838 N  ND2 . ASN A 1 231 ? -8.111  -10.352 -44.946 1.00 27.79  ? 231 ASN A ND2 1 
ATOM   1839 N  N   . LEU A 1 232 ? -10.231 -5.778  -47.306 1.00 26.57  ? 232 LEU A N   1 
ATOM   1840 C  CA  . LEU A 1 232 ? -10.320 -4.624  -48.230 1.00 25.83  ? 232 LEU A CA  1 
ATOM   1841 C  C   . LEU A 1 232 ? -10.746 -3.368  -47.469 1.00 25.34  ? 232 LEU A C   1 
ATOM   1842 O  O   . LEU A 1 232 ? -10.211 -2.297  -47.753 1.00 27.90  ? 232 LEU A O   1 
ATOM   1843 C  CB  . LEU A 1 232 ? -11.293 -4.951  -49.360 1.00 26.53  ? 232 LEU A CB  1 
ATOM   1844 C  CG  . LEU A 1 232 ? -10.778 -5.973  -50.370 1.00 25.71  ? 232 LEU A CG  1 
ATOM   1845 C  CD1 . LEU A 1 232 ? -11.917 -6.367  -51.304 1.00 27.83  ? 232 LEU A CD1 1 
ATOM   1846 C  CD2 . LEU A 1 232 ? -9.559  -5.436  -51.141 1.00 24.61  ? 232 LEU A CD2 1 
ATOM   1847 N  N   . VAL A 1 233 ? -11.639 -3.483  -46.492 1.00 24.40  ? 233 VAL A N   1 
ATOM   1848 C  CA  . VAL A 1 233 ? -12.042 -2.310  -45.667 1.00 25.52  ? 233 VAL A CA  1 
ATOM   1849 C  C   . VAL A 1 233 ? -10.922 -1.960  -44.670 1.00 24.26  ? 233 VAL A C   1 
ATOM   1850 O  O   . VAL A 1 233 ? -10.537 -0.765  -44.614 1.00 25.45  ? 233 VAL A O   1 
ATOM   1851 C  CB  . VAL A 1 233 ? -13.357 -2.580  -44.928 1.00 25.70  ? 233 VAL A CB  1 
ATOM   1852 C  CG1 . VAL A 1 233 ? -13.678 -1.459  -43.945 1.00 25.98  ? 233 VAL A CG1 1 
ATOM   1853 C  CG2 . VAL A 1 233 ? -14.485 -2.784  -45.923 1.00 23.37  ? 233 VAL A CG2 1 
ATOM   1854 N  N   . ALA A 1 234 ? -10.458 -2.942  -43.899 1.00 25.13  ? 234 ALA A N   1 
ATOM   1855 C  CA  . ALA A 1 234 ? -9.542  -2.725  -42.746 1.00 26.53  ? 234 ALA A CA  1 
ATOM   1856 C  C   . ALA A 1 234 ? -8.245  -2.079  -43.245 1.00 26.21  ? 234 ALA A C   1 
ATOM   1857 O  O   . ALA A 1 234 ? -7.689  -1.205  -42.563 1.00 29.01  ? 234 ALA A O   1 
ATOM   1858 C  CB  . ALA A 1 234 ? -9.263  -4.012  -42.026 1.00 26.25  ? 234 ALA A CB  1 
ATOM   1859 N  N   . MET A 1 235 ? -7.787  -2.454  -44.428 1.00 28.96  ? 235 MET A N   1 
ATOM   1860 C  CA  . MET A 1 235 ? -6.490  -1.938  -44.912 1.00 31.32  ? 235 MET A CA  1 
ATOM   1861 C  C   . MET A 1 235 ? -6.624  -0.452  -45.242 1.00 27.92  ? 235 MET A C   1 
ATOM   1862 O  O   . MET A 1 235 ? -5.623  0.270   -45.137 1.00 25.12  ? 235 MET A O   1 
ATOM   1863 C  CB  . MET A 1 235 ? -5.982  -2.794  -46.068 1.00 39.03  ? 235 MET A CB  1 
ATOM   1864 C  CG  . MET A 1 235 ? -5.635  -4.182  -45.511 1.00 50.02  ? 235 MET A CG  1 
ATOM   1865 S  SD  . MET A 1 235 ? -5.095  -5.410  -46.703 1.00 63.84  ? 235 MET A SD  1 
ATOM   1866 C  CE  . MET A 1 235 ? -3.615  -4.593  -47.305 1.00 53.67  ? 235 MET A CE  1 
ATOM   1867 N  N   . LYS A 1 236 ? -7.834  0.034   -45.505 1.00 27.52  ? 236 LYS A N   1 
ATOM   1868 C  CA  . LYS A 1 236 ? -8.028  1.481   -45.771 1.00 26.87  ? 236 LYS A CA  1 
ATOM   1869 C  C   . LYS A 1 236 ? -7.891  2.269   -44.469 1.00 24.98  ? 236 LYS A C   1 
ATOM   1870 O  O   . LYS A 1 236 ? -7.805  3.518   -44.553 1.00 24.56  ? 236 LYS A O   1 
ATOM   1871 C  CB  . LYS A 1 236 ? -9.381  1.743   -46.431 1.00 28.79  ? 236 LYS A CB  1 
ATOM   1872 C  CG  . LYS A 1 236 ? -9.549  1.026   -47.758 1.00 30.30  ? 236 LYS A CG  1 
ATOM   1873 C  CD  . LYS A 1 236 ? -10.971 1.081   -48.307 1.00 30.78  ? 236 LYS A CD  1 
ATOM   1874 C  CE  . LYS A 1 236 ? -11.057 0.334   -49.621 1.00 30.70  ? 236 LYS A CE  1 
ATOM   1875 N  NZ  . LYS A 1 236 ? -12.385 0.508   -50.254 1.00 35.38  ? 236 LYS A NZ  1 
ATOM   1876 N  N   . TYR A 1 237 ? -7.898  1.599   -43.317 1.00 24.57  ? 237 TYR A N   1 
ATOM   1877 C  CA  . TYR A 1 237 ? -7.593  2.246   -42.011 1.00 25.98  ? 237 TYR A CA  1 
ATOM   1878 C  C   . TYR A 1 237 ? -6.193  1.880   -41.506 1.00 25.85  ? 237 TYR A C   1 
ATOM   1879 O  O   . TYR A 1 237 ? -5.934  2.095   -40.319 1.00 25.87  ? 237 TYR A O   1 
ATOM   1880 C  CB  . TYR A 1 237 ? -8.641  1.866   -40.971 1.00 25.41  ? 237 TYR A CB  1 
ATOM   1881 C  CG  . TYR A 1 237 ? -10.053 2.259   -41.342 1.00 26.77  ? 237 TYR A CG  1 
ATOM   1882 C  CD1 . TYR A 1 237 ? -10.871 1.397   -42.048 1.00 28.55  ? 237 TYR A CD1 1 
ATOM   1883 C  CD2 . TYR A 1 237 ? -10.585 3.485   -40.965 1.00 26.66  ? 237 TYR A CD2 1 
ATOM   1884 C  CE1 . TYR A 1 237 ? -12.186 1.729   -42.352 1.00 28.84  ? 237 TYR A CE1 1 
ATOM   1885 C  CE2 . TYR A 1 237 ? -11.900 3.829   -41.254 1.00 26.69  ? 237 TYR A CE2 1 
ATOM   1886 C  CZ  . TYR A 1 237 ? -12.700 2.958   -41.970 1.00 28.99  ? 237 TYR A CZ  1 
ATOM   1887 O  OH  . TYR A 1 237 ? -13.987 3.292   -42.272 1.00 32.38  ? 237 TYR A OH  1 
ATOM   1888 N  N   . ASN A 1 238 ? -5.333  1.310   -42.340 1.00 26.47  ? 238 ASN A N   1 
ATOM   1889 C  CA  . ASN A 1 238 ? -3.944  0.947   -41.951 1.00 26.97  ? 238 ASN A CA  1 
ATOM   1890 C  C   . ASN A 1 238 ? -3.964  -0.159  -40.903 1.00 26.57  ? 238 ASN A C   1 
ATOM   1891 O  O   . ASN A 1 238 ? -3.069  -0.176  -40.025 1.00 24.54  ? 238 ASN A O   1 
ATOM   1892 C  CB  . ASN A 1 238 ? -3.175  2.166   -41.431 1.00 32.04  ? 238 ASN A CB  1 
ATOM   1893 C  CG  . ASN A 1 238 ? -2.291  2.765   -42.497 1.00 37.02  ? 238 ASN A CG  1 
ATOM   1894 O  OD1 . ASN A 1 238 ? -2.099  2.169   -43.555 1.00 42.66  ? 238 ASN A OD1 1 
ATOM   1895 N  ND2 . ASN A 1 238 ? -1.765  3.944   -42.235 1.00 44.20  ? 238 ASN A ND2 1 
ATOM   1896 N  N   . TYR A 1 239 ? -4.947  -1.046  -40.996 1.00 21.28  ? 239 TYR A N   1 
ATOM   1897 C  CA  . TYR A 1 239 ? -5.020  -2.292  -40.212 1.00 22.45  ? 239 TYR A CA  1 
ATOM   1898 C  C   . TYR A 1 239 ? -4.235  -3.367  -40.950 1.00 22.12  ? 239 TYR A C   1 
ATOM   1899 O  O   . TYR A 1 239 ? -4.290  -3.407  -42.197 1.00 24.10  ? 239 TYR A O   1 
ATOM   1900 C  CB  . TYR A 1 239 ? -6.487  -2.683  -40.000 1.00 22.07  ? 239 TYR A CB  1 
ATOM   1901 C  CG  . TYR A 1 239 ? -7.077  -2.096  -38.754 1.00 21.79  ? 239 TYR A CG  1 
ATOM   1902 C  CD1 . TYR A 1 239 ? -7.138  -0.719  -38.558 1.00 23.59  ? 239 TYR A CD1 1 
ATOM   1903 C  CD2 . TYR A 1 239 ? -7.477  -2.920  -37.725 1.00 21.00  ? 239 TYR A CD2 1 
ATOM   1904 C  CE1 . TYR A 1 239 ? -7.637  -0.180  -37.383 1.00 22.31  ? 239 TYR A CE1 1 
ATOM   1905 C  CE2 . TYR A 1 239 ? -7.974  -2.399  -36.551 1.00 23.12  ? 239 TYR A CE2 1 
ATOM   1906 C  CZ  . TYR A 1 239 ? -8.071  -1.032  -36.385 1.00 22.69  ? 239 TYR A CZ  1 
ATOM   1907 O  OH  . TYR A 1 239 ? -8.561  -0.572  -35.209 1.00 25.02  ? 239 TYR A OH  1 
ATOM   1908 N  N   . GLU A 1 240 ? -3.563  -4.229  -40.206 1.00 23.45  ? 240 GLU A N   1 
ATOM   1909 C  CA  . GLU A 1 240 ? -2.880  -5.407  -40.768 1.00 26.60  ? 240 GLU A CA  1 
ATOM   1910 C  C   . GLU A 1 240 ? -3.918  -6.313  -41.411 1.00 28.68  ? 240 GLU A C   1 
ATOM   1911 O  O   . GLU A 1 240 ? -5.054  -6.373  -40.940 1.00 27.16  ? 240 GLU A O   1 
ATOM   1912 C  CB  . GLU A 1 240 ? -2.173  -6.210  -39.680 1.00 29.08  ? 240 GLU A CB  1 
ATOM   1913 C  CG  . GLU A 1 240 ? -0.888  -5.585  -39.245 1.00 31.09  ? 240 GLU A CG  1 
ATOM   1914 C  CD  . GLU A 1 240 ? 0.165   -5.759  -40.310 1.00 32.88  ? 240 GLU A CD  1 
ATOM   1915 O  OE1 . GLU A 1 240 ? 0.546   -6.911  -40.564 1.00 36.36  ? 240 GLU A OE1 1 
ATOM   1916 O  OE2 . GLU A 1 240 ? 0.530   -4.745  -40.914 1.00 35.69  ? 240 GLU A OE2 1 
ATOM   1917 N  N   . PRO A 1 241 ? -3.546  -7.059  -42.477 1.00 28.16  ? 241 PRO A N   1 
ATOM   1918 C  CA  . PRO A 1 241 ? -4.414  -8.107  -42.995 1.00 28.98  ? 241 PRO A CA  1 
ATOM   1919 C  C   . PRO A 1 241 ? -4.638  -9.187  -41.925 1.00 27.28  ? 241 PRO A C   1 
ATOM   1920 O  O   . PRO A 1 241 ? -3.718  -9.547  -41.179 1.00 25.54  ? 241 PRO A O   1 
ATOM   1921 C  CB  . PRO A 1 241 ? -3.671  -8.658  -44.230 1.00 29.10  ? 241 PRO A CB  1 
ATOM   1922 C  CG  . PRO A 1 241 ? -2.702  -7.550  -44.611 1.00 29.74  ? 241 PRO A CG  1 
ATOM   1923 C  CD  . PRO A 1 241 ? -2.327  -6.891  -43.296 1.00 30.90  ? 241 PRO A CD  1 
ATOM   1924 N  N   . LEU A 1 242 ? -5.880  -9.644  -41.848 1.00 24.56  ? 242 LEU A N   1 
ATOM   1925 C  CA  . LEU A 1 242 ? -6.297  -10.805 -41.037 1.00 24.26  ? 242 LEU A CA  1 
ATOM   1926 C  C   . LEU A 1 242 ? -6.207  -12.039 -41.929 1.00 26.61  ? 242 LEU A C   1 
ATOM   1927 O  O   . LEU A 1 242 ? -6.859  -12.066 -42.969 1.00 28.20  ? 242 LEU A O   1 
ATOM   1928 C  CB  . LEU A 1 242 ? -7.734  -10.582 -40.557 1.00 25.18  ? 242 LEU A CB  1 
ATOM   1929 C  CG  . LEU A 1 242 ? -8.172  -11.514 -39.426 1.00 26.35  ? 242 LEU A CG  1 
ATOM   1930 C  CD1 . LEU A 1 242 ? -7.553  -11.052 -38.101 1.00 24.75  ? 242 LEU A CD1 1 
ATOM   1931 C  CD2 . LEU A 1 242 ? -9.706  -11.605 -39.334 1.00 26.71  ? 242 LEU A CD2 1 
ATOM   1932 N  N   . THR A 1 243 ? -5.399  -13.002 -41.530 1.00 27.41  ? 243 THR A N   1 
ATOM   1933 C  CA  . THR A 1 243 ? -5.173  -14.272 -42.246 1.00 27.37  ? 243 THR A CA  1 
ATOM   1934 C  C   . THR A 1 243 ? -6.072  -15.347 -41.653 1.00 26.88  ? 243 THR A C   1 
ATOM   1935 O  O   . THR A 1 243 ? -6.633  -15.153 -40.551 1.00 24.62  ? 243 THR A O   1 
ATOM   1936 C  CB  . THR A 1 243 ? -3.714  -14.707 -42.095 1.00 27.03  ? 243 THR A CB  1 
ATOM   1937 O  OG1 . THR A 1 243 ? -3.534  -15.121 -40.733 1.00 24.28  ? 243 THR A OG1 1 
ATOM   1938 C  CG2 . THR A 1 243 ? -2.723  -13.632 -42.497 1.00 26.75  ? 243 THR A CG2 1 
ATOM   1939 N  N   A GLN A 1 244 ? -6.189  -16.477 -42.350 0.24 26.75  ? 244 GLN A N   1 
ATOM   1940 N  N   B GLN A 1 244 ? -6.189  -16.477 -42.350 0.24 26.75  ? 244 GLN A N   1 
ATOM   1941 N  N   C GLN A 1 244 ? -6.198  -16.482 -42.345 0.26 26.96  ? 244 GLN A N   1 
ATOM   1942 N  N   D GLN A 1 244 ? -6.198  -16.482 -42.345 0.26 26.96  ? 244 GLN A N   1 
ATOM   1943 C  CA  A GLN A 1 244 ? -6.949  -17.646 -41.843 0.24 27.58  ? 244 GLN A CA  1 
ATOM   1944 C  CA  B GLN A 1 244 ? -6.949  -17.646 -41.843 0.24 27.58  ? 244 GLN A CA  1 
ATOM   1945 C  CA  C GLN A 1 244 ? -6.971  -17.640 -41.824 0.26 28.01  ? 244 GLN A CA  1 
ATOM   1946 C  CA  D GLN A 1 244 ? -6.971  -17.640 -41.824 0.26 28.01  ? 244 GLN A CA  1 
ATOM   1947 C  C   A GLN A 1 244 ? -6.324  -18.126 -40.527 0.24 26.98  ? 244 GLN A C   1 
ATOM   1948 C  C   B GLN A 1 244 ? -6.324  -18.126 -40.527 0.24 26.98  ? 244 GLN A C   1 
ATOM   1949 C  C   C GLN A 1 244 ? -6.324  -18.138 -40.524 0.26 27.14  ? 244 GLN A C   1 
ATOM   1950 C  C   D GLN A 1 244 ? -6.324  -18.138 -40.524 0.26 27.14  ? 244 GLN A C   1 
ATOM   1951 O  O   A GLN A 1 244 ? -7.075  -18.618 -39.667 0.24 28.02  ? 244 GLN A O   1 
ATOM   1952 O  O   B GLN A 1 244 ? -7.075  -18.618 -39.667 0.24 28.02  ? 244 GLN A O   1 
ATOM   1953 O  O   C GLN A 1 244 ? -7.060  -18.656 -39.669 0.26 28.25  ? 244 GLN A O   1 
ATOM   1954 O  O   D GLN A 1 244 ? -7.060  -18.656 -39.669 0.26 28.25  ? 244 GLN A O   1 
ATOM   1955 C  CB  A GLN A 1 244 ? -6.994  -18.767 -42.881 0.24 28.10  ? 244 GLN A CB  1 
ATOM   1956 C  CB  B GLN A 1 244 ? -6.994  -18.767 -42.881 0.24 28.10  ? 244 GLN A CB  1 
ATOM   1957 C  CB  C GLN A 1 244 ? -7.086  -18.763 -42.856 0.26 28.93  ? 244 GLN A CB  1 
ATOM   1958 C  CB  D GLN A 1 244 ? -7.086  -18.763 -42.856 0.26 28.93  ? 244 GLN A CB  1 
ATOM   1959 C  CG  A GLN A 1 244 ? -7.880  -19.931 -42.454 0.24 28.53  ? 244 GLN A CG  1 
ATOM   1960 C  CG  B GLN A 1 244 ? -7.880  -19.931 -42.454 0.24 28.53  ? 244 GLN A CG  1 
ATOM   1961 C  CG  C GLN A 1 244 ? -7.977  -19.914 -42.394 0.26 29.64  ? 244 GLN A CG  1 
ATOM   1962 C  CG  D GLN A 1 244 ? -7.977  -19.914 -42.394 0.26 29.64  ? 244 GLN A CG  1 
ATOM   1963 C  CD  A GLN A 1 244 ? -9.303  -19.483 -42.225 0.24 28.99  ? 244 GLN A CD  1 
ATOM   1964 C  CD  B GLN A 1 244 ? -9.303  -19.483 -42.225 0.24 28.99  ? 244 GLN A CD  1 
ATOM   1965 C  CD  C GLN A 1 244 ? -9.374  -19.459 -42.043 0.26 30.54  ? 244 GLN A CD  1 
ATOM   1966 C  CD  D GLN A 1 244 ? -9.374  -19.459 -42.043 0.26 30.54  ? 244 GLN A CD  1 
ATOM   1967 O  OE1 A GLN A 1 244 ? -9.895  -18.808 -43.066 0.24 29.50  ? 244 GLN A OE1 1 
ATOM   1968 O  OE1 B GLN A 1 244 ? -9.895  -18.808 -43.066 0.24 29.50  ? 244 GLN A OE1 1 
ATOM   1969 O  OE1 C GLN A 1 244 ? -9.958  -18.610 -42.715 0.26 32.25  ? 244 GLN A OE1 1 
ATOM   1970 O  OE1 D GLN A 1 244 ? -9.958  -18.610 -42.715 0.26 32.25  ? 244 GLN A OE1 1 
ATOM   1971 N  NE2 A GLN A 1 244 ? -9.857  -19.846 -41.078 0.24 28.57  ? 244 GLN A NE2 1 
ATOM   1972 N  NE2 B GLN A 1 244 ? -9.857  -19.846 -41.078 0.24 28.57  ? 244 GLN A NE2 1 
ATOM   1973 N  NE2 C GLN A 1 244 ? -9.922  -20.022 -40.978 0.26 29.91  ? 244 GLN A NE2 1 
ATOM   1974 N  NE2 D GLN A 1 244 ? -9.922  -20.022 -40.978 0.26 29.91  ? 244 GLN A NE2 1 
ATOM   1975 N  N   . ASP A 1 245 ? -5.006  -17.984 -40.369 1.00 26.84  ? 245 ASP A N   1 
ATOM   1976 C  CA  . ASP A 1 245 ? -4.313  -18.341 -39.098 1.00 29.16  ? 245 ASP A CA  1 
ATOM   1977 C  C   . ASP A 1 245 ? -4.915  -17.556 -37.935 1.00 28.51  ? 245 ASP A C   1 
ATOM   1978 O  O   . ASP A 1 245 ? -5.286  -18.164 -36.911 1.00 26.61  ? 245 ASP A O   1 
ATOM   1979 C  CB  . ASP A 1 245 ? -2.815  -18.068 -39.152 1.00 34.08  ? 245 ASP A CB  1 
ATOM   1980 C  CG  . ASP A 1 245 ? -2.087  -19.286 -39.659 1.00 37.29  ? 245 ASP A CG  1 
ATOM   1981 O  OD1 . ASP A 1 245 ? -2.712  -20.064 -40.374 1.00 40.62  ? 245 ASP A OD1 1 
ATOM   1982 O  OD2 . ASP A 1 245 ? -0.929  -19.451 -39.290 1.00 47.03  ? 245 ASP A OD2 1 
ATOM   1983 N  N   . HIS A 1 246 ? -5.042  -16.253 -38.127 1.00 26.27  ? 246 HIS A N   1 
ATOM   1984 C  CA  . HIS A 1 246 ? -5.683  -15.337 -37.158 1.00 26.70  ? 246 HIS A CA  1 
ATOM   1985 C  C   . HIS A 1 246 ? -7.112  -15.802 -36.839 1.00 26.70  ? 246 HIS A C   1 
ATOM   1986 O  O   . HIS A 1 246 ? -7.510  -15.813 -35.635 1.00 28.51  ? 246 HIS A O   1 
ATOM   1987 C  CB  . HIS A 1 246 ? -5.657  -13.928 -37.727 1.00 23.33  ? 246 HIS A CB  1 
ATOM   1988 C  CG  . HIS A 1 246 ? -4.271  -13.396 -37.868 1.00 22.66  ? 246 HIS A CG  1 
ATOM   1989 N  ND1 . HIS A 1 246 ? -3.955  -12.379 -38.736 1.00 21.50  ? 246 HIS A ND1 1 
ATOM   1990 C  CD2 . HIS A 1 246 ? -3.132  -13.695 -37.205 1.00 22.62  ? 246 HIS A CD2 1 
ATOM   1991 C  CE1 . HIS A 1 246 ? -2.670  -12.111 -38.639 1.00 22.14  ? 246 HIS A CE1 1 
ATOM   1992 N  NE2 . HIS A 1 246 ? -2.165  -12.867 -37.669 1.00 22.60  ? 246 HIS A NE2 1 
ATOM   1993 N  N   . VAL A 1 247 ? -7.880  -16.123 -37.874 1.00 27.08  ? 247 VAL A N   1 
ATOM   1994 C  CA  . VAL A 1 247 ? -9.284  -16.591 -37.693 1.00 28.18  ? 247 VAL A CA  1 
ATOM   1995 C  C   . VAL A 1 247 ? -9.299  -17.866 -36.834 1.00 28.43  ? 247 VAL A C   1 
ATOM   1996 O  O   . VAL A 1 247 ? -10.131 -17.972 -35.938 1.00 27.39  ? 247 VAL A O   1 
ATOM   1997 C  CB  . VAL A 1 247 ? -10.008 -16.771 -39.044 1.00 27.74  ? 247 VAL A CB  1 
ATOM   1998 C  CG1 . VAL A 1 247 ? -11.420 -17.332 -38.864 1.00 29.09  ? 247 VAL A CG1 1 
ATOM   1999 C  CG2 . VAL A 1 247 ? -10.081 -15.462 -39.798 1.00 26.96  ? 247 VAL A CG2 1 
ATOM   2000 N  N   A ASP A 1 248 ? -8.391  -18.807 -37.118 0.24 28.97  ? 248 ASP A N   1 
ATOM   2001 N  N   B ASP A 1 248 ? -8.391  -18.807 -37.118 0.24 28.97  ? 248 ASP A N   1 
ATOM   2002 N  N   C ASP A 1 248 ? -8.382  -18.800 -37.117 0.26 29.23  ? 248 ASP A N   1 
ATOM   2003 N  N   D ASP A 1 248 ? -8.382  -18.800 -37.117 0.26 29.23  ? 248 ASP A N   1 
ATOM   2004 C  CA  A ASP A 1 248 ? -8.230  -20.067 -36.344 0.24 28.72  ? 248 ASP A CA  1 
ATOM   2005 C  CA  B ASP A 1 248 ? -8.230  -20.067 -36.344 0.24 28.72  ? 248 ASP A CA  1 
ATOM   2006 C  CA  C ASP A 1 248 ? -8.210  -20.071 -36.361 0.26 29.05  ? 248 ASP A CA  1 
ATOM   2007 C  CA  D ASP A 1 248 ? -8.210  -20.071 -36.361 0.26 29.05  ? 248 ASP A CA  1 
ATOM   2008 C  C   A ASP A 1 248 ? -7.902  -19.717 -34.888 0.24 29.31  ? 248 ASP A C   1 
ATOM   2009 C  C   B ASP A 1 248 ? -7.902  -19.717 -34.888 0.24 29.31  ? 248 ASP A C   1 
ATOM   2010 C  C   C ASP A 1 248 ? -7.874  -19.746 -34.899 0.26 29.55  ? 248 ASP A C   1 
ATOM   2011 C  C   D ASP A 1 248 ? -7.874  -19.746 -34.899 0.26 29.55  ? 248 ASP A C   1 
ATOM   2012 O  O   A ASP A 1 248 ? -8.597  -20.235 -33.990 0.24 28.84  ? 248 ASP A O   1 
ATOM   2013 O  O   B ASP A 1 248 ? -8.597  -20.235 -33.990 0.24 28.84  ? 248 ASP A O   1 
ATOM   2014 O  O   C ASP A 1 248 ? -8.531  -20.319 -34.006 0.26 29.21  ? 248 ASP A O   1 
ATOM   2015 O  O   D ASP A 1 248 ? -8.531  -20.319 -34.006 0.26 29.21  ? 248 ASP A O   1 
ATOM   2016 C  CB  A ASP A 1 248 ? -7.151  -20.973 -36.948 0.24 29.19  ? 248 ASP A CB  1 
ATOM   2017 C  CB  B ASP A 1 248 ? -7.151  -20.973 -36.948 0.24 29.19  ? 248 ASP A CB  1 
ATOM   2018 C  CB  C ASP A 1 248 ? -7.141  -20.965 -37.002 0.26 29.74  ? 248 ASP A CB  1 
ATOM   2019 C  CB  D ASP A 1 248 ? -7.141  -20.965 -37.002 0.26 29.74  ? 248 ASP A CB  1 
ATOM   2020 C  CG  A ASP A 1 248 ? -7.506  -21.557 -38.308 0.24 29.23  ? 248 ASP A CG  1 
ATOM   2021 C  CG  B ASP A 1 248 ? -7.506  -21.557 -38.308 0.24 29.23  ? 248 ASP A CG  1 
ATOM   2022 C  CG  C ASP A 1 248 ? -7.540  -21.537 -38.355 0.26 29.92  ? 248 ASP A CG  1 
ATOM   2023 C  CG  D ASP A 1 248 ? -7.540  -21.537 -38.355 0.26 29.92  ? 248 ASP A CG  1 
ATOM   2024 O  OD1 A ASP A 1 248 ? -8.645  -21.339 -38.774 0.24 29.41  ? 248 ASP A OD1 1 
ATOM   2025 O  OD1 B ASP A 1 248 ? -8.645  -21.339 -38.774 0.24 29.41  ? 248 ASP A OD1 1 
ATOM   2026 O  OD1 C ASP A 1 248 ? -8.752  -21.578 -38.649 0.26 30.10  ? 248 ASP A OD1 1 
ATOM   2027 O  OD1 D ASP A 1 248 ? -8.752  -21.578 -38.649 0.26 30.10  ? 248 ASP A OD1 1 
ATOM   2028 O  OD2 A ASP A 1 248 ? -6.637  -22.224 -38.892 0.24 29.58  ? 248 ASP A OD2 1 
ATOM   2029 O  OD2 B ASP A 1 248 ? -6.637  -22.224 -38.892 0.24 29.58  ? 248 ASP A OD2 1 
ATOM   2030 O  OD2 C ASP A 1 248 ? -6.635  -21.931 -39.108 0.26 30.75  ? 248 ASP A OD2 1 
ATOM   2031 O  OD2 D ASP A 1 248 ? -6.635  -21.931 -39.108 0.26 30.75  ? 248 ASP A OD2 1 
ATOM   2032 N  N   . ILE A 1 249 ? -6.907  -18.848 -34.666 1.00 29.00  ? 249 ILE A N   1 
ATOM   2033 C  CA  . ILE A 1 249 ? -6.440  -18.488 -33.288 1.00 29.68  ? 249 ILE A CA  1 
ATOM   2034 C  C   . ILE A 1 249 ? -7.592  -17.929 -32.434 1.00 29.80  ? 249 ILE A C   1 
ATOM   2035 O  O   . ILE A 1 249 ? -7.594  -18.183 -31.221 1.00 30.41  ? 249 ILE A O   1 
ATOM   2036 C  CB  . ILE A 1 249 ? -5.232  -17.529 -33.362 1.00 33.83  ? 249 ILE A CB  1 
ATOM   2037 C  CG1 . ILE A 1 249 ? -3.982  -18.266 -33.876 1.00 36.45  ? 249 ILE A CG1 1 
ATOM   2038 C  CG2 . ILE A 1 249 ? -4.962  -16.877 -32.015 1.00 31.85  ? 249 ILE A CG2 1 
ATOM   2039 C  CD1 . ILE A 1 249 ? -2.821  -17.359 -34.281 1.00 38.62  ? 249 ILE A CD1 1 
ATOM   2040 N  N   . LEU A 1 250 ? -8.559  -17.221 -33.027 1.00 30.67  ? 250 LEU A N   1 
ATOM   2041 C  CA  . LEU A 1 250 ? -9.717  -16.616 -32.296 1.00 27.24  ? 250 LEU A CA  1 
ATOM   2042 C  C   . LEU A 1 250 ? -10.831 -17.651 -32.047 1.00 25.75  ? 250 LEU A C   1 
ATOM   2043 O  O   . LEU A 1 250 ? -11.748 -17.329 -31.269 1.00 28.53  ? 250 LEU A O   1 
ATOM   2044 C  CB  . LEU A 1 250 ? -10.232 -15.403 -33.083 1.00 25.18  ? 250 LEU A CB  1 
ATOM   2045 C  CG  . LEU A 1 250 ? -9.303  -14.190 -33.115 1.00 28.50  ? 250 LEU A CG  1 
ATOM   2046 C  CD1 . LEU A 1 250 ? -9.629  -13.303 -34.313 1.00 29.51  ? 250 LEU A CD1 1 
ATOM   2047 C  CD2 . LEU A 1 250 ? -9.376  -13.363 -31.829 1.00 27.93  ? 250 LEU A CD2 1 
ATOM   2048 N  N   . GLY A 1 251 ? -10.757 -18.857 -32.631 1.00 27.14  ? 251 GLY A N   1 
ATOM   2049 C  CA  . GLY A 1 251 ? -11.827 -19.872 -32.558 1.00 27.86  ? 251 GLY A CA  1 
ATOM   2050 C  C   . GLY A 1 251 ? -12.317 -20.066 -31.121 1.00 32.94  ? 251 GLY A C   1 
ATOM   2051 O  O   . GLY A 1 251 ? -13.506 -20.000 -30.833 1.00 40.09  ? 251 GLY A O   1 
ATOM   2052 N  N   . PRO A 1 252 ? -11.419 -20.335 -30.158 1.00 33.68  ? 252 PRO A N   1 
ATOM   2053 C  CA  . PRO A 1 252 ? -11.810 -20.474 -28.745 1.00 34.10  ? 252 PRO A CA  1 
ATOM   2054 C  C   . PRO A 1 252 ? -12.609 -19.302 -28.148 1.00 31.42  ? 252 PRO A C   1 
ATOM   2055 O  O   . PRO A 1 252 ? -13.595 -19.549 -27.466 1.00 33.17  ? 252 PRO A O   1 
ATOM   2056 C  CB  . PRO A 1 252 ? -10.457 -20.624 -28.021 1.00 30.50  ? 252 PRO A CB  1 
ATOM   2057 C  CG  . PRO A 1 252 ? -9.537  -21.209 -29.046 1.00 29.58  ? 252 PRO A CG  1 
ATOM   2058 C  CD  . PRO A 1 252 ? -10.015 -20.707 -30.396 1.00 31.32  ? 252 PRO A CD  1 
ATOM   2059 N  N   . LEU A 1 253 ? -12.203 -18.064 -28.418 1.00 29.89  ? 253 LEU A N   1 
ATOM   2060 C  CA  . LEU A 1 253 ? -12.943 -16.869 -27.934 1.00 27.68  ? 253 LEU A CA  1 
ATOM   2061 C  C   . LEU A 1 253 ? -14.326 -16.805 -28.621 1.00 29.20  ? 253 LEU A C   1 
ATOM   2062 O  O   . LEU A 1 253 ? -15.317 -16.458 -27.946 1.00 28.43  ? 253 LEU A O   1 
ATOM   2063 C  CB  . LEU A 1 253 ? -12.106 -15.613 -28.200 1.00 26.67  ? 253 LEU A CB  1 
ATOM   2064 C  CG  . LEU A 1 253 ? -10.927 -15.392 -27.248 1.00 27.41  ? 253 LEU A CG  1 
ATOM   2065 C  CD1 . LEU A 1 253 ? -9.914  -14.443 -27.852 1.00 25.17  ? 253 LEU A CD1 1 
ATOM   2066 C  CD2 . LEU A 1 253 ? -11.386 -14.833 -25.905 1.00 27.98  ? 253 LEU A CD2 1 
ATOM   2067 N  N   . SER A 1 254 ? -14.386 -17.076 -29.926 1.00 28.77  ? 254 SER A N   1 
ATOM   2068 C  CA  . SER A 1 254 ? -15.637 -17.295 -30.696 1.00 31.61  ? 254 SER A CA  1 
ATOM   2069 C  C   . SER A 1 254 ? -16.570 -18.249 -29.925 1.00 32.23  ? 254 SER A C   1 
ATOM   2070 O  O   . SER A 1 254 ? -17.763 -17.932 -29.715 1.00 28.20  ? 254 SER A O   1 
ATOM   2071 C  CB  . SER A 1 254 ? -15.322 -17.858 -32.059 1.00 31.20  ? 254 SER A CB  1 
ATOM   2072 O  OG  . SER A 1 254 ? -16.462 -17.802 -32.891 1.00 34.86  ? 254 SER A OG  1 
ATOM   2073 N  N   . ALA A 1 255 ? -16.041 -19.406 -29.545 1.00 31.83  ? 255 ALA A N   1 
ATOM   2074 C  CA  . ALA A 1 255 ? -16.781 -20.515 -28.903 1.00 33.31  ? 255 ALA A CA  1 
ATOM   2075 C  C   . ALA A 1 255 ? -17.260 -20.066 -27.531 1.00 31.03  ? 255 ALA A C   1 
ATOM   2076 O  O   . ALA A 1 255 ? -18.431 -20.214 -27.245 1.00 34.73  ? 255 ALA A O   1 
ATOM   2077 C  CB  . ALA A 1 255 ? -15.908 -21.746 -28.808 1.00 34.92  ? 255 ALA A CB  1 
ATOM   2078 N  N   . GLN A 1 256 ? -16.400 -19.459 -26.735 1.00 33.53  ? 256 GLN A N   1 
ATOM   2079 C  CA  . GLN A 1 256 ? -16.786 -18.990 -25.388 1.00 37.18  ? 256 GLN A CA  1 
ATOM   2080 C  C   . GLN A 1 256 ? -17.903 -17.931 -25.469 1.00 37.32  ? 256 GLN A C   1 
ATOM   2081 O  O   . GLN A 1 256 ? -18.722 -17.864 -24.545 1.00 35.33  ? 256 GLN A O   1 
ATOM   2082 C  CB  . GLN A 1 256 ? -15.553 -18.467 -24.656 1.00 45.03  ? 256 GLN A CB  1 
ATOM   2083 C  CG  . GLN A 1 256 ? -15.801 -18.229 -23.180 1.00 48.93  ? 256 GLN A CG  1 
ATOM   2084 C  CD  . GLN A 1 256 ? -14.574 -17.614 -22.575 1.00 55.00  ? 256 GLN A CD  1 
ATOM   2085 O  OE1 . GLN A 1 256 ? -13.450 -17.975 -22.921 1.00 57.29  ? 256 GLN A OE1 1 
ATOM   2086 N  NE2 . GLN A 1 256 ? -14.793 -16.659 -21.687 1.00 62.64  ? 256 GLN A NE2 1 
ATOM   2087 N  N   . THR A 1 257 ? -17.913 -17.060 -26.470 1.00 34.08  ? 257 THR A N   1 
ATOM   2088 C  CA  . THR A 1 257 ? -18.841 -15.901 -26.502 1.00 33.15  ? 257 THR A CA  1 
ATOM   2089 C  C   . THR A 1 257 ? -20.030 -16.206 -27.426 1.00 37.21  ? 257 THR A C   1 
ATOM   2090 O  O   . THR A 1 257 ? -21.010 -15.453 -27.359 1.00 36.45  ? 257 THR A O   1 
ATOM   2091 C  CB  . THR A 1 257 ? -18.129 -14.621 -26.954 1.00 34.80  ? 257 THR A CB  1 
ATOM   2092 O  OG1 . THR A 1 257 ? -17.704 -14.838 -28.304 1.00 30.39  ? 257 THR A OG1 1 
ATOM   2093 C  CG2 . THR A 1 257 ? -16.961 -14.246 -26.067 1.00 35.95  ? 257 THR A CG2 1 
ATOM   2094 N  N   . GLY A 1 258 ? -19.925 -17.227 -28.288 1.00 34.66  ? 258 GLY A N   1 
ATOM   2095 C  CA  . GLY A 1 258 ? -20.947 -17.534 -29.303 1.00 36.97  ? 258 GLY A CA  1 
ATOM   2096 C  C   . GLY A 1 258 ? -21.010 -16.504 -30.430 1.00 39.45  ? 258 GLY A C   1 
ATOM   2097 O  O   . GLY A 1 258 ? -22.019 -16.516 -31.153 1.00 36.61  ? 258 GLY A O   1 
ATOM   2098 N  N   . ILE A 1 259 ? -19.988 -15.654 -30.614 1.00 33.25  ? 259 ILE A N   1 
ATOM   2099 C  CA  . ILE A 1 259 ? -19.933 -14.682 -31.749 1.00 30.55  ? 259 ILE A CA  1 
ATOM   2100 C  C   . ILE A 1 259 ? -18.887 -15.174 -32.749 1.00 29.66  ? 259 ILE A C   1 
ATOM   2101 O  O   . ILE A 1 259 ? -17.701 -15.238 -32.375 1.00 30.73  ? 259 ILE A O   1 
ATOM   2102 C  CB  . ILE A 1 259 ? -19.648 -13.257 -31.244 1.00 31.53  ? 259 ILE A CB  1 
ATOM   2103 C  CG1 . ILE A 1 259 ? -20.643 -12.853 -30.148 1.00 32.05  ? 259 ILE A CG1 1 
ATOM   2104 C  CG2 . ILE A 1 259 ? -19.636 -12.276 -32.401 1.00 29.64  ? 259 ILE A CG2 1 
ATOM   2105 C  CD1 . ILE A 1 259 ? -20.314 -11.570 -29.430 1.00 34.02  ? 259 ILE A CD1 1 
ATOM   2106 N  N   . ALA A 1 260 ? -19.310 -15.558 -33.956 1.00 27.95  ? 260 ALA A N   1 
ATOM   2107 C  CA  . ALA A 1 260 ? -18.421 -16.059 -35.031 1.00 29.02  ? 260 ALA A CA  1 
ATOM   2108 C  C   . ALA A 1 260 ? -17.346 -15.007 -35.309 1.00 26.70  ? 260 ALA A C   1 
ATOM   2109 O  O   . ALA A 1 260 ? -17.636 -13.782 -35.241 1.00 24.66  ? 260 ALA A O   1 
ATOM   2110 C  CB  . ALA A 1 260 ? -19.200 -16.362 -36.299 1.00 29.82  ? 260 ALA A CB  1 
ATOM   2111 N  N   . VAL A 1 261 ? -16.153 -15.461 -35.678 1.00 26.63  ? 261 VAL A N   1 
ATOM   2112 C  CA  . VAL A 1 261 ? -15.015 -14.538 -35.923 1.00 26.03  ? 261 VAL A CA  1 
ATOM   2113 C  C   . VAL A 1 261 ? -15.424 -13.486 -36.961 1.00 25.40  ? 261 VAL A C   1 
ATOM   2114 O  O   . VAL A 1 261 ? -15.268 -12.289 -36.704 1.00 25.29  ? 261 VAL A O   1 
ATOM   2115 C  CB  . VAL A 1 261 ? -13.756 -15.309 -36.340 1.00 27.11  ? 261 VAL A CB  1 
ATOM   2116 C  CG1 . VAL A 1 261 ? -12.681 -14.349 -36.806 1.00 25.52  ? 261 VAL A CG1 1 
ATOM   2117 C  CG2 . VAL A 1 261 ? -13.257 -16.224 -35.221 1.00 28.37  ? 261 VAL A CG2 1 
ATOM   2118 N  N   . LEU A 1 262 ? -15.999 -13.878 -38.093 1.00 26.13  ? 262 LEU A N   1 
ATOM   2119 C  CA  . LEU A 1 262 ? -16.363 -12.861 -39.112 1.00 24.91  ? 262 LEU A CA  1 
ATOM   2120 C  C   . LEU A 1 262 ? -17.561 -11.997 -38.703 1.00 26.20  ? 262 LEU A C   1 
ATOM   2121 O  O   . LEU A 1 262 ? -17.686 -10.917 -39.282 1.00 26.12  ? 262 LEU A O   1 
ATOM   2122 C  CB  . LEU A 1 262 ? -16.637 -13.565 -40.431 1.00 26.90  ? 262 LEU A CB  1 
ATOM   2123 C  CG  . LEU A 1 262 ? -15.420 -14.227 -41.062 1.00 28.90  ? 262 LEU A CG  1 
ATOM   2124 C  CD1 . LEU A 1 262 ? -15.883 -15.089 -42.229 1.00 32.40  ? 262 LEU A CD1 1 
ATOM   2125 C  CD2 . LEU A 1 262 ? -14.400 -13.205 -41.522 1.00 28.22  ? 262 LEU A CD2 1 
ATOM   2126 N  N   . ASP A 1 263 ? -18.403 -12.403 -37.746 1.00 26.49  ? 263 ASP A N   1 
ATOM   2127 C  CA  . ASP A 1 263 ? -19.410 -11.473 -37.167 1.00 28.47  ? 263 ASP A CA  1 
ATOM   2128 C  C   . ASP A 1 263 ? -18.650 -10.406 -36.367 1.00 24.96  ? 263 ASP A C   1 
ATOM   2129 O  O   . ASP A 1 263 ? -19.007 -9.220  -36.432 1.00 23.45  ? 263 ASP A O   1 
ATOM   2130 C  CB  . ASP A 1 263 ? -20.464 -12.172 -36.295 1.00 33.42  ? 263 ASP A CB  1 
ATOM   2131 C  CG  . ASP A 1 263 ? -21.446 -13.039 -37.068 1.00 40.47  ? 263 ASP A CG  1 
ATOM   2132 O  OD1 . ASP A 1 263 ? -21.365 -13.072 -38.325 1.00 48.86  ? 263 ASP A OD1 1 
ATOM   2133 O  OD2 . ASP A 1 263 ? -22.303 -13.656 -36.419 1.00 42.23  ? 263 ASP A OD2 1 
ATOM   2134 N  N   . MET A 1 264 ? -17.647 -10.803 -35.591 1.00 25.17  ? 264 MET A N   1 
ATOM   2135 C  CA  . MET A 1 264 ? -16.852 -9.800  -34.834 1.00 24.12  ? 264 MET A CA  1 
ATOM   2136 C  C   . MET A 1 264 ? -16.148 -8.895  -35.852 1.00 24.62  ? 264 MET A C   1 
ATOM   2137 O  O   . MET A 1 264 ? -16.117 -7.688  -35.610 1.00 25.11  ? 264 MET A O   1 
ATOM   2138 C  CB  . MET A 1 264 ? -15.868 -10.435 -33.851 1.00 24.73  ? 264 MET A CB  1 
ATOM   2139 C  CG  . MET A 1 264 ? -15.301 -9.450  -32.847 1.00 25.53  ? 264 MET A CG  1 
ATOM   2140 S  SD  . MET A 1 264 ? -16.551 -8.677  -31.732 1.00 25.55  ? 264 MET A SD  1 
ATOM   2141 C  CE  . MET A 1 264 ? -16.634 -9.938  -30.473 1.00 24.12  ? 264 MET A CE  1 
ATOM   2142 N  N   . CYS A 1 265 ? -15.702 -9.415  -37.001 1.00 24.66  ? 265 CYS A N   1 
ATOM   2143 C  CA  . CYS A 1 265 ? -15.056 -8.560  -38.033 1.00 25.13  ? 265 CYS A CA  1 
ATOM   2144 C  C   . CYS A 1 265 ? -16.034 -7.481  -38.499 1.00 25.15  ? 265 CYS A C   1 
ATOM   2145 O  O   . CYS A 1 265 ? -15.619 -6.305  -38.638 1.00 23.77  ? 265 CYS A O   1 
ATOM   2146 C  CB  . CYS A 1 265 ? -14.497 -9.390  -39.174 1.00 26.35  ? 265 CYS A CB  1 
ATOM   2147 S  SG  . CYS A 1 265 ? -13.092 -10.410 -38.647 1.00 26.29  ? 265 CYS A SG  1 
ATOM   2148 N  N   . ALA A 1 266 ? -17.317 -7.839  -38.678 1.00 25.18  ? 266 ALA A N   1 
ATOM   2149 C  CA  . ALA A 1 266 ? -18.355 -6.872  -39.111 1.00 25.03  ? 266 ALA A CA  1 
ATOM   2150 C  C   . ALA A 1 266 ? -18.472 -5.759  -38.056 1.00 23.99  ? 266 ALA A C   1 
ATOM   2151 O  O   . ALA A 1 266 ? -18.564 -4.570  -38.408 1.00 25.54  ? 266 ALA A O   1 
ATOM   2152 C  CB  . ALA A 1 266 ? -19.678 -7.577  -39.350 1.00 26.46  ? 266 ALA A CB  1 
ATOM   2153 N  N   . SER A 1 267 ? -18.437 -6.119  -36.780 1.00 27.90  ? 267 SER A N   1 
ATOM   2154 C  CA  . SER A 1 267 ? -18.499 -5.164  -35.651 1.00 26.51  ? 267 SER A CA  1 
ATOM   2155 C  C   . SER A 1 267 ? -17.307 -4.213  -35.756 1.00 25.97  ? 267 SER A C   1 
ATOM   2156 O  O   . SER A 1 267 ? -17.503 -2.993  -35.765 1.00 24.17  ? 267 SER A O   1 
ATOM   2157 C  CB  . SER A 1 267 ? -18.559 -5.912  -34.341 1.00 30.97  ? 267 SER A CB  1 
ATOM   2158 O  OG  . SER A 1 267 ? -18.520 -5.004  -33.252 1.00 38.71  ? 267 SER A OG  1 
ATOM   2159 N  N   . LEU A 1 268 ? -16.100 -4.755  -35.924 1.00 27.96  ? 268 LEU A N   1 
ATOM   2160 C  CA  . LEU A 1 268 ? -14.883 -3.922  -36.115 1.00 24.51  ? 268 LEU A CA  1 
ATOM   2161 C  C   . LEU A 1 268 ? -15.055 -2.990  -37.332 1.00 24.49  ? 268 LEU A C   1 
ATOM   2162 O  O   . LEU A 1 268 ? -14.746 -1.791  -37.189 1.00 26.84  ? 268 LEU A O   1 
ATOM   2163 C  CB  . LEU A 1 268 ? -13.653 -4.830  -36.222 1.00 24.27  ? 268 LEU A CB  1 
ATOM   2164 C  CG  . LEU A 1 268 ? -12.322 -4.117  -36.447 1.00 23.40  ? 268 LEU A CG  1 
ATOM   2165 C  CD1 . LEU A 1 268 ? -12.163 -2.944  -35.495 1.00 22.90  ? 268 LEU A CD1 1 
ATOM   2166 C  CD2 . LEU A 1 268 ? -11.159 -5.083  -36.285 1.00 24.29  ? 268 LEU A CD2 1 
ATOM   2167 N  N   . LYS A 1 269 ? -15.534 -3.465  -38.489 1.00 26.42  ? 269 LYS A N   1 
ATOM   2168 C  CA  . LYS A 1 269 ? -15.694 -2.587  -39.685 1.00 25.55  ? 269 LYS A CA  1 
ATOM   2169 C  C   . LYS A 1 269 ? -16.563 -1.380  -39.352 1.00 23.19  ? 269 LYS A C   1 
ATOM   2170 O  O   . LYS A 1 269 ? -16.232 -0.253  -39.778 1.00 23.57  ? 269 LYS A O   1 
ATOM   2171 C  CB  . LYS A 1 269 ? -16.349 -3.317  -40.855 1.00 31.37  ? 269 LYS A CB  1 
ATOM   2172 C  CG  . LYS A 1 269 ? -15.385 -4.091  -41.726 1.00 38.20  ? 269 LYS A CG  1 
ATOM   2173 C  CD  . LYS A 1 269 ? -16.028 -5.240  -42.483 1.00 39.83  ? 269 LYS A CD  1 
ATOM   2174 C  CE  . LYS A 1 269 ? -16.921 -4.762  -43.599 1.00 39.70  ? 269 LYS A CE  1 
ATOM   2175 N  NZ  . LYS A 1 269 ? -17.362 -5.930  -44.397 1.00 40.23  ? 269 LYS A NZ  1 
ATOM   2176 N  N   . GLU A 1 270 ? -17.659 -1.616  -38.628 1.00 24.26  ? 270 GLU A N   1 
ATOM   2177 C  CA  . GLU A 1 270 ? -18.621 -0.558  -38.221 1.00 26.34  ? 270 GLU A CA  1 
ATOM   2178 C  C   . GLU A 1 270 ? -17.961 0.418   -37.243 1.00 24.35  ? 270 GLU A C   1 
ATOM   2179 O  O   . GLU A 1 270 ? -18.144 1.612   -37.399 1.00 24.29  ? 270 GLU A O   1 
ATOM   2180 C  CB  . GLU A 1 270 ? -19.856 -1.198  -37.586 1.00 25.65  ? 270 GLU A CB  1 
ATOM   2181 C  CG  . GLU A 1 270 ? -20.845 -0.173  -37.118 1.00 29.43  ? 270 GLU A CG  1 
ATOM   2182 C  CD  . GLU A 1 270 ? -22.220 -0.779  -36.918 1.00 31.33  ? 270 GLU A CD  1 
ATOM   2183 O  OE1 . GLU A 1 270 ? -22.871 -1.103  -37.916 1.00 29.68  ? 270 GLU A OE1 1 
ATOM   2184 O  OE2 . GLU A 1 270 ? -22.580 -1.001  -35.779 1.00 34.30  ? 270 GLU A OE2 1 
ATOM   2185 N  N   . LEU A 1 271 ? -17.192 -0.091  -36.277 1.00 25.86  ? 271 LEU A N   1 
ATOM   2186 C  CA  . LEU A 1 271 ? -16.505 0.749   -35.258 1.00 25.70  ? 271 LEU A CA  1 
ATOM   2187 C  C   . LEU A 1 271 ? -15.496 1.648   -35.962 1.00 23.73  ? 271 LEU A C   1 
ATOM   2188 O  O   . LEU A 1 271 ? -15.346 2.779   -35.535 1.00 24.30  ? 271 LEU A O   1 
ATOM   2189 C  CB  . LEU A 1 271 ? -15.802 -0.161  -34.246 1.00 27.18  ? 271 LEU A CB  1 
ATOM   2190 C  CG  . LEU A 1 271 ? -16.651 -0.688  -33.098 1.00 24.99  ? 271 LEU A CG  1 
ATOM   2191 C  CD1 . LEU A 1 271 ? -15.923 -1.792  -32.342 1.00 26.87  ? 271 LEU A CD1 1 
ATOM   2192 C  CD2 . LEU A 1 271 ? -17.010 0.454   -32.159 1.00 25.60  ? 271 LEU A CD2 1 
ATOM   2193 N  N   . LEU A 1 272 ? -14.847 1.157   -37.023 1.00 23.57  ? 272 LEU A N   1 
ATOM   2194 C  CA  . LEU A 1 272 ? -13.853 1.955   -37.787 1.00 23.46  ? 272 LEU A CA  1 
ATOM   2195 C  C   . LEU A 1 272 ? -14.602 3.050   -38.533 1.00 24.12  ? 272 LEU A C   1 
ATOM   2196 O  O   . LEU A 1 272 ? -14.050 4.142   -38.667 1.00 26.19  ? 272 LEU A O   1 
ATOM   2197 C  CB  . LEU A 1 272 ? -13.050 1.062   -38.742 1.00 22.27  ? 272 LEU A CB  1 
ATOM   2198 C  CG  . LEU A 1 272 ? -12.048 0.145   -38.059 1.00 25.25  ? 272 LEU A CG  1 
ATOM   2199 C  CD1 . LEU A 1 272 ? -11.477 -0.911  -38.999 1.00 25.33  ? 272 LEU A CD1 1 
ATOM   2200 C  CD2 . LEU A 1 272 ? -10.919 0.980   -37.471 1.00 27.55  ? 272 LEU A CD2 1 
ATOM   2201 N  N   . GLN A 1 273 ? -15.801 2.741   -39.023 1.00 24.05  ? 273 GLN A N   1 
ATOM   2202 C  CA  . GLN A 1 273 ? -16.663 3.682   -39.778 1.00 25.14  ? 273 GLN A CA  1 
ATOM   2203 C  C   . GLN A 1 273 ? -17.277 4.728   -38.829 1.00 25.69  ? 273 GLN A C   1 
ATOM   2204 O  O   . GLN A 1 273 ? -17.386 5.889   -39.226 1.00 24.96  ? 273 GLN A O   1 
ATOM   2205 C  CB  . GLN A 1 273 ? -17.724 2.861   -40.507 1.00 25.77  ? 273 GLN A CB  1 
ATOM   2206 C  CG  . GLN A 1 273 ? -18.943 3.638   -40.968 1.00 27.74  ? 273 GLN A CG  1 
ATOM   2207 C  CD  . GLN A 1 273 ? -20.034 2.659   -41.352 1.00 29.64  ? 273 GLN A CD  1 
ATOM   2208 O  OE1 . GLN A 1 273 ? -21.026 2.456   -40.657 1.00 29.80  ? 273 GLN A OE1 1 
ATOM   2209 N  NE2 . GLN A 1 273 ? -19.816 1.996   -42.464 1.00 24.15  ? 273 GLN A NE2 1 
ATOM   2210 N  N   . ASN A 1 274 ? -17.721 4.334   -37.634 1.00 26.61  ? 274 ASN A N   1 
ATOM   2211 C  CA  . ASN A 1 274 ? -18.553 5.211   -36.774 1.00 27.06  ? 274 ASN A CA  1 
ATOM   2212 C  C   . ASN A 1 274 ? -17.703 5.884   -35.687 1.00 30.94  ? 274 ASN A C   1 
ATOM   2213 O  O   . ASN A 1 274 ? -18.093 6.972   -35.254 1.00 29.28  ? 274 ASN A O   1 
ATOM   2214 C  CB  . ASN A 1 274 ? -19.733 4.445   -36.149 1.00 26.36  ? 274 ASN A CB  1 
ATOM   2215 C  CG  . ASN A 1 274 ? -20.710 3.913   -37.184 1.00 26.16  ? 274 ASN A CG  1 
ATOM   2216 O  OD1 . ASN A 1 274 ? -20.643 4.315   -38.352 1.00 23.70  ? 274 ASN A OD1 1 
ATOM   2217 N  ND2 . ASN A 1 274 ? -21.564 2.979   -36.779 1.00 23.91  ? 274 ASN A ND2 1 
ATOM   2218 N  N   . GLY A 1 275 ? -16.609 5.264   -35.246 1.00 32.88  ? 275 GLY A N   1 
ATOM   2219 C  CA  . GLY A 1 275 ? -15.982 5.616   -33.954 1.00 35.17  ? 275 GLY A CA  1 
ATOM   2220 C  C   . GLY A 1 275 ? -16.869 5.160   -32.804 1.00 35.05  ? 275 GLY A C   1 
ATOM   2221 O  O   . GLY A 1 275 ? -17.675 4.234   -32.999 1.00 35.53  ? 275 GLY A O   1 
ATOM   2222 N  N   . MET A 1 276 ? -16.737 5.756   -31.627 1.00 33.18  ? 276 MET A N   1 
ATOM   2223 C  CA  . MET A 1 276 ? -17.360 5.192   -30.403 1.00 37.92  ? 276 MET A CA  1 
ATOM   2224 C  C   . MET A 1 276 ? -18.571 6.017   -29.958 1.00 37.08  ? 276 MET A C   1 
ATOM   2225 O  O   . MET A 1 276 ? -19.311 5.526   -29.057 1.00 36.01  ? 276 MET A O   1 
ATOM   2226 C  CB  . MET A 1 276 ? -16.315 5.115   -29.285 1.00 39.03  ? 276 MET A CB  1 
ATOM   2227 C  CG  . MET A 1 276 ? -15.198 4.155   -29.659 1.00 41.66  ? 276 MET A CG  1 
ATOM   2228 S  SD  . MET A 1 276 ? -14.554 3.298   -28.250 1.00 53.09  ? 276 MET A SD  1 
ATOM   2229 C  CE  . MET A 1 276 ? -13.333 2.284   -29.077 1.00 53.26  ? 276 MET A CE  1 
ATOM   2230 N  N   . ASN A 1 277 ? -18.759 7.212   -30.516 1.00 38.57  ? 277 ASN A N   1 
ATOM   2231 C  CA  . ASN A 1 277 ? -19.947 8.047   -30.202 1.00 42.90  ? 277 ASN A CA  1 
ATOM   2232 C  C   . ASN A 1 277 ? -19.963 8.270   -28.677 1.00 41.80  ? 277 ASN A C   1 
ATOM   2233 O  O   . ASN A 1 277 ? -21.017 8.047   -28.048 1.00 39.37  ? 277 ASN A O   1 
ATOM   2234 C  CB  . ASN A 1 277 ? -21.205 7.351   -30.733 1.00 49.53  ? 277 ASN A CB  1 
ATOM   2235 C  CG  . ASN A 1 277 ? -22.451 8.213   -30.736 1.00 61.34  ? 277 ASN A CG  1 
ATOM   2236 O  OD1 . ASN A 1 277 ? -23.541 7.729   -31.041 1.00 74.97  ? 277 ASN A OD1 1 
ATOM   2237 N  ND2 . ASN A 1 277 ? -22.311 9.485   -30.397 1.00 65.54  ? 277 ASN A ND2 1 
ATOM   2238 N  N   . GLY A 1 278 ? -18.819 8.653   -28.101 1.00 38.22  ? 278 GLY A N   1 
ATOM   2239 C  CA  . GLY A 1 278 ? -18.696 9.055   -26.688 1.00 36.52  ? 278 GLY A CA  1 
ATOM   2240 C  C   . GLY A 1 278 ? -18.587 7.847   -25.770 1.00 39.24  ? 278 GLY A C   1 
ATOM   2241 O  O   . GLY A 1 278 ? -18.362 8.022   -24.577 1.00 41.28  ? 278 GLY A O   1 
ATOM   2242 N  N   . ARG A 1 279 ? -18.749 6.632   -26.278 1.00 38.18  ? 279 ARG A N   1 
ATOM   2243 C  CA  . ARG A 1 279 ? -18.683 5.437   -25.407 1.00 39.25  ? 279 ARG A CA  1 
ATOM   2244 C  C   . ARG A 1 279 ? -17.211 5.048   -25.263 1.00 36.36  ? 279 ARG A C   1 
ATOM   2245 O  O   . ARG A 1 279 ? -16.350 5.710   -25.859 1.00 36.93  ? 279 ARG A O   1 
ATOM   2246 C  CB  . ARG A 1 279 ? -19.548 4.298   -25.946 1.00 43.14  ? 279 ARG A CB  1 
ATOM   2247 C  CG  . ARG A 1 279 ? -21.037 4.532   -25.739 1.00 49.15  ? 279 ARG A CG  1 
ATOM   2248 C  CD  . ARG A 1 279 ? -21.876 3.598   -26.573 1.00 54.09  ? 279 ARG A CD  1 
ATOM   2249 N  NE  . ARG A 1 279 ? -22.231 4.243   -27.823 1.00 63.27  ? 279 ARG A NE  1 
ATOM   2250 C  CZ  . ARG A 1 279 ? -23.122 3.777   -28.690 1.00 70.63  ? 279 ARG A CZ  1 
ATOM   2251 N  NH1 . ARG A 1 279 ? -23.742 2.630   -28.459 1.00 73.44  ? 279 ARG A NH1 1 
ATOM   2252 N  NH2 . ARG A 1 279 ? -23.397 4.466   -29.785 1.00 72.34  ? 279 ARG A NH2 1 
ATOM   2253 N  N   . THR A 1 280 ? -16.954 4.071   -24.408 1.00 35.82  ? 280 THR A N   1 
ATOM   2254 C  CA  . THR A 1 280 ? -15.615 3.489   -24.166 1.00 37.62  ? 280 THR A CA  1 
ATOM   2255 C  C   . THR A 1 280 ? -15.802 1.986   -24.184 1.00 35.50  ? 280 THR A C   1 
ATOM   2256 O  O   . THR A 1 280 ? -16.957 1.531   -24.030 1.00 39.25  ? 280 THR A O   1 
ATOM   2257 C  CB  . THR A 1 280 ? -14.975 3.973   -22.856 1.00 36.76  ? 280 THR A CB  1 
ATOM   2258 O  OG1 . THR A 1 280 ? -15.786 3.507   -21.784 1.00 38.28  ? 280 THR A OG1 1 
ATOM   2259 C  CG2 . THR A 1 280 ? -14.850 5.474   -22.750 1.00 35.86  ? 280 THR A CG2 1 
ATOM   2260 N  N   . ILE A 1 281 ? -14.726 1.271   -24.482 1.00 36.21  ? 281 ILE A N   1 
ATOM   2261 C  CA  . ILE A 1 281 ? -14.669 -0.210  -24.360 1.00 33.94  ? 281 ILE A CA  1 
ATOM   2262 C  C   . ILE A 1 281 ? -13.502 -0.521  -23.433 1.00 31.28  ? 281 ILE A C   1 
ATOM   2263 O  O   . ILE A 1 281 ? -12.398 -0.030  -23.706 1.00 29.20  ? 281 ILE A O   1 
ATOM   2264 C  CB  . ILE A 1 281 ? -14.542 -0.894  -25.735 1.00 34.23  ? 281 ILE A CB  1 
ATOM   2265 C  CG1 . ILE A 1 281 ? -15.695 -0.505  -26.656 1.00 32.18  ? 281 ILE A CG1 1 
ATOM   2266 C  CG2 . ILE A 1 281 ? -14.449 -2.400  -25.573 1.00 37.07  ? 281 ILE A CG2 1 
ATOM   2267 C  CD1 . ILE A 1 281 ? -15.506 -0.968  -28.077 1.00 33.95  ? 281 ILE A CD1 1 
ATOM   2268 N  N   . LEU A 1 282 ? -13.791 -1.226  -22.342 1.00 32.86  ? 282 LEU A N   1 
ATOM   2269 C  CA  . LEU A 1 282 ? -12.812 -1.651  -21.321 1.00 33.06  ? 282 LEU A CA  1 
ATOM   2270 C  C   . LEU A 1 282 ? -11.958 -0.451  -20.918 1.00 33.52  ? 282 LEU A C   1 
ATOM   2271 O  O   . LEU A 1 282 ? -10.755 -0.600  -20.842 1.00 36.08  ? 282 LEU A O   1 
ATOM   2272 C  CB  . LEU A 1 282 ? -11.980 -2.786  -21.921 1.00 30.87  ? 282 LEU A CB  1 
ATOM   2273 C  CG  . LEU A 1 282 ? -12.788 -4.043  -22.227 1.00 31.02  ? 282 LEU A CG  1 
ATOM   2274 C  CD1 . LEU A 1 282 ? -11.966 -5.070  -22.976 1.00 32.58  ? 282 LEU A CD1 1 
ATOM   2275 C  CD2 . LEU A 1 282 ? -13.327 -4.654  -20.944 1.00 31.76  ? 282 LEU A CD2 1 
ATOM   2276 N  N   . GLY A 1 283 ? -12.571 0.711   -20.725 1.00 35.21  ? 283 GLY A N   1 
ATOM   2277 C  CA  . GLY A 1 283 ? -11.866 1.920   -20.263 1.00 35.47  ? 283 GLY A CA  1 
ATOM   2278 C  C   . GLY A 1 283 ? -11.160 2.654   -21.386 1.00 36.80  ? 283 GLY A C   1 
ATOM   2279 O  O   . GLY A 1 283 ? -10.524 3.668   -21.116 1.00 37.47  ? 283 GLY A O   1 
ATOM   2280 N  N   . SER A 1 284 ? -11.247 2.197   -22.630 1.00 36.90  ? 284 SER A N   1 
ATOM   2281 C  CA  . SER A 1 284 ? -10.521 2.871   -23.732 1.00 33.55  ? 284 SER A CA  1 
ATOM   2282 C  C   . SER A 1 284 ? -11.515 3.569   -24.662 1.00 30.92  ? 284 SER A C   1 
ATOM   2283 O  O   . SER A 1 284 ? -12.593 3.016   -24.905 1.00 33.21  ? 284 SER A O   1 
ATOM   2284 C  CB  . SER A 1 284 ? -9.638  1.925   -24.483 1.00 33.66  ? 284 SER A CB  1 
ATOM   2285 O  OG  . SER A 1 284 ? -8.901  2.667   -25.452 1.00 36.96  ? 284 SER A OG  1 
ATOM   2286 N  N   . ALA A 1 285 ? -11.143 4.736   -25.173 1.00 31.90  ? 285 ALA A N   1 
ATOM   2287 C  CA  . ALA A 1 285 ? -11.888 5.443   -26.239 1.00 31.96  ? 285 ALA A CA  1 
ATOM   2288 C  C   . ALA A 1 285 ? -11.220 5.214   -27.600 1.00 32.47  ? 285 ALA A C   1 
ATOM   2289 O  O   . ALA A 1 285 ? -11.702 5.809   -28.569 1.00 31.56  ? 285 ALA A O   1 
ATOM   2290 C  CB  . ALA A 1 285 ? -11.979 6.907   -25.909 1.00 33.76  ? 285 ALA A CB  1 
ATOM   2291 N  N   . LEU A 1 286 ? -10.144 4.412   -27.666 1.00 32.32  ? 286 LEU A N   1 
ATOM   2292 C  CA  . LEU A 1 286 ? -9.530  3.940   -28.940 1.00 31.43  ? 286 LEU A CA  1 
ATOM   2293 C  C   . LEU A 1 286 ? -9.632  2.412   -29.020 1.00 28.30  ? 286 LEU A C   1 
ATOM   2294 O  O   . LEU A 1 286 ? -9.760  1.744   -27.977 1.00 26.34  ? 286 LEU A O   1 
ATOM   2295 C  CB  . LEU A 1 286 ? -8.059  4.355   -29.004 1.00 37.94  ? 286 LEU A CB  1 
ATOM   2296 C  CG  . LEU A 1 286 ? -7.763  5.847   -29.139 1.00 42.56  ? 286 LEU A CG  1 
ATOM   2297 C  CD1 . LEU A 1 286 ? -6.272  6.058   -29.303 1.00 40.17  ? 286 LEU A CD1 1 
ATOM   2298 C  CD2 . LEU A 1 286 ? -8.532  6.499   -30.297 1.00 46.72  ? 286 LEU A CD2 1 
ATOM   2299 N  N   . LEU A 1 287 ? -9.460  1.854   -30.214 1.00 24.57  ? 287 LEU A N   1 
ATOM   2300 C  CA  . LEU A 1 287 ? -9.389  0.373   -30.394 1.00 26.36  ? 287 LEU A CA  1 
ATOM   2301 C  C   . LEU A 1 287 ? -7.986  -0.123  -30.001 1.00 26.08  ? 287 LEU A C   1 
ATOM   2302 O  O   . LEU A 1 287 ? -7.000  0.322   -30.588 1.00 27.73  ? 287 LEU A O   1 
ATOM   2303 C  CB  . LEU A 1 287 ? -9.765  0.033   -31.844 1.00 27.57  ? 287 LEU A CB  1 
ATOM   2304 C  CG  . LEU A 1 287 ? -11.150 0.566   -32.242 1.00 27.16  ? 287 LEU A CG  1 
ATOM   2305 C  CD1 . LEU A 1 287 ? -11.440 0.406   -33.719 1.00 26.76  ? 287 LEU A CD1 1 
ATOM   2306 C  CD2 . LEU A 1 287 ? -12.209 -0.105  -31.411 1.00 27.86  ? 287 LEU A CD2 1 
ATOM   2307 N  N   . GLU A 1 288 ? -7.916  -0.957  -28.976 1.00 26.82  ? 288 GLU A N   1 
ATOM   2308 C  CA  . GLU A 1 288 ? -6.652  -1.399  -28.337 1.00 28.90  ? 288 GLU A CA  1 
ATOM   2309 C  C   . GLU A 1 288 ? -6.109  -2.582  -29.124 1.00 26.16  ? 288 GLU A C   1 
ATOM   2310 O  O   . GLU A 1 288 ? -6.885  -3.556  -29.349 1.00 27.18  ? 288 GLU A O   1 
ATOM   2311 C  CB  . GLU A 1 288 ? -6.892  -1.810  -26.882 1.00 32.24  ? 288 GLU A CB  1 
ATOM   2312 C  CG  . GLU A 1 288 ? -6.627  -0.701  -25.888 1.00 42.99  ? 288 GLU A CG  1 
ATOM   2313 C  CD  . GLU A 1 288 ? -5.170  -0.261  -25.916 1.00 43.35  ? 288 GLU A CD  1 
ATOM   2314 O  OE1 . GLU A 1 288 ? -4.273  -1.153  -25.966 1.00 48.69  ? 288 GLU A OE1 1 
ATOM   2315 O  OE2 . GLU A 1 288 ? -4.945  0.964   -25.985 1.00 52.21  ? 288 GLU A OE2 1 
ATOM   2316 N  N   . ASP A 1 289 ? -4.813  -2.559  -29.442 1.00 25.61  ? 289 ASP A N   1 
ATOM   2317 C  CA  . ASP A 1 289 ? -4.194  -3.640  -30.262 1.00 23.64  ? 289 ASP A CA  1 
ATOM   2318 C  C   . ASP A 1 289 ? -3.000  -4.263  -29.550 1.00 22.60  ? 289 ASP A C   1 
ATOM   2319 O  O   . ASP A 1 289 ? -2.288  -5.023  -30.245 1.00 23.01  ? 289 ASP A O   1 
ATOM   2320 C  CB  . ASP A 1 289 ? -3.866  -3.161  -31.686 1.00 22.48  ? 289 ASP A CB  1 
ATOM   2321 C  CG  . ASP A 1 289 ? -2.623  -2.291  -31.821 1.00 23.08  ? 289 ASP A CG  1 
ATOM   2322 O  OD1 . ASP A 1 289 ? -2.136  -1.747  -30.791 1.00 21.15  ? 289 ASP A OD1 1 
ATOM   2323 O  OD2 . ASP A 1 289 ? -2.164  -2.146  -32.962 1.00 19.08  ? 289 ASP A OD2 1 
ATOM   2324 N  N   . GLU A 1 290 ? -2.811  -4.056  -28.231 1.00 21.30  ? 290 GLU A N   1 
ATOM   2325 C  CA  . GLU A 1 290 ? -1.621  -4.645  -27.549 1.00 22.17  ? 290 GLU A CA  1 
ATOM   2326 C  C   . GLU A 1 290 ? -2.031  -5.728  -26.545 1.00 21.61  ? 290 GLU A C   1 
ATOM   2327 O  O   . GLU A 1 290 ? -1.222  -6.039  -25.642 1.00 22.49  ? 290 GLU A O   1 
ATOM   2328 C  CB  . GLU A 1 290 ? -0.711  -3.546  -27.001 1.00 23.52  ? 290 GLU A CB  1 
ATOM   2329 C  CG  . GLU A 1 290 ? -0.053  -2.766  -28.126 1.00 26.01  ? 290 GLU A CG  1 
ATOM   2330 C  CD  . GLU A 1 290 ? 1.266   -2.049  -27.829 1.00 27.03  ? 290 GLU A CD  1 
ATOM   2331 O  OE1 . GLU A 1 290 ? 1.647   -1.961  -26.637 1.00 22.53  ? 290 GLU A OE1 1 
ATOM   2332 O  OE2 . GLU A 1 290 ? 1.879   -1.525  -28.805 1.00 26.72  ? 290 GLU A OE2 1 
ATOM   2333 N  N   . PHE A 1 291 ? -3.160  -6.400  -26.784 1.00 21.62  ? 291 PHE A N   1 
ATOM   2334 C  CA  . PHE A 1 291 ? -3.571  -7.660  -26.104 1.00 24.25  ? 291 PHE A CA  1 
ATOM   2335 C  C   . PHE A 1 291 ? -3.738  -8.759  -27.154 1.00 25.95  ? 291 PHE A C   1 
ATOM   2336 O  O   . PHE A 1 291 ? -4.555  -8.554  -28.053 1.00 26.16  ? 291 PHE A O   1 
ATOM   2337 C  CB  . PHE A 1 291 ? -4.921  -7.517  -25.396 1.00 25.99  ? 291 PHE A CB  1 
ATOM   2338 C  CG  . PHE A 1 291 ? -4.950  -6.533  -24.264 1.00 28.47  ? 291 PHE A CG  1 
ATOM   2339 C  CD1 . PHE A 1 291 ? -4.534  -6.910  -22.995 1.00 27.45  ? 291 PHE A CD1 1 
ATOM   2340 C  CD2 . PHE A 1 291 ? -5.385  -5.232  -24.472 1.00 31.30  ? 291 PHE A CD2 1 
ATOM   2341 C  CE1 . PHE A 1 291 ? -4.582  -6.002  -21.947 1.00 33.08  ? 291 PHE A CE1 1 
ATOM   2342 C  CE2 . PHE A 1 291 ? -5.413  -4.321  -23.427 1.00 32.54  ? 291 PHE A CE2 1 
ATOM   2343 C  CZ  . PHE A 1 291 ? -5.009  -4.706  -22.166 1.00 35.52  ? 291 PHE A CZ  1 
ATOM   2344 N  N   . THR A 1 292 ? -3.054  -9.889  -26.991 1.00 24.93  ? 292 THR A N   1 
ATOM   2345 C  CA  . THR A 1 292 ? -3.165  -11.066 -27.889 1.00 24.09  ? 292 THR A CA  1 
ATOM   2346 C  C   . THR A 1 292 ? -4.356  -11.921 -27.482 1.00 23.82  ? 292 THR A C   1 
ATOM   2347 O  O   . THR A 1 292 ? -4.869  -11.843 -26.364 1.00 22.47  ? 292 THR A O   1 
ATOM   2348 C  CB  . THR A 1 292 ? -1.898  -11.917 -27.865 1.00 22.63  ? 292 THR A CB  1 
ATOM   2349 O  OG1 . THR A 1 292 ? -1.769  -12.480 -26.571 1.00 23.61  ? 292 THR A OG1 1 
ATOM   2350 C  CG2 . THR A 1 292 ? -0.664  -11.103 -28.190 1.00 25.92  ? 292 THR A CG2 1 
ATOM   2351 N  N   . PRO A 1 293 ? -4.844  -12.777 -28.394 1.00 24.52  ? 293 PRO A N   1 
ATOM   2352 C  CA  . PRO A 1 293 ? -5.832  -13.793 -28.020 1.00 24.86  ? 293 PRO A CA  1 
ATOM   2353 C  C   . PRO A 1 293 ? -5.421  -14.572 -26.764 1.00 25.86  ? 293 PRO A C   1 
ATOM   2354 O  O   . PRO A 1 293 ? -6.247  -14.810 -25.912 1.00 22.38  ? 293 PRO A O   1 
ATOM   2355 C  CB  . PRO A 1 293 ? -5.864  -14.669 -29.264 1.00 24.71  ? 293 PRO A CB  1 
ATOM   2356 C  CG  . PRO A 1 293 ? -5.638  -13.673 -30.393 1.00 25.76  ? 293 PRO A CG  1 
ATOM   2357 C  CD  . PRO A 1 293 ? -4.598  -12.719 -29.845 1.00 27.08  ? 293 PRO A CD  1 
ATOM   2358 N  N   . PHE A 1 294 ? -4.132  -14.903 -26.640 1.00 26.23  ? 294 PHE A N   1 
ATOM   2359 C  CA  . PHE A 1 294 ? -3.625  -15.696 -25.495 1.00 26.30  ? 294 PHE A CA  1 
ATOM   2360 C  C   . PHE A 1 294 ? -3.708  -14.837 -24.225 1.00 25.67  ? 294 PHE A C   1 
ATOM   2361 O  O   . PHE A 1 294 ? -4.159  -15.342 -23.204 1.00 28.12  ? 294 PHE A O   1 
ATOM   2362 C  CB  . PHE A 1 294 ? -2.233  -16.229 -25.823 1.00 31.04  ? 294 PHE A CB  1 
ATOM   2363 C  CG  . PHE A 1 294 ? -1.637  -17.146 -24.776 1.00 39.00  ? 294 PHE A CG  1 
ATOM   2364 C  CD1 . PHE A 1 294 ? -1.116  -16.646 -23.584 1.00 42.68  ? 294 PHE A CD1 1 
ATOM   2365 C  CD2 . PHE A 1 294 ? -1.541  -18.512 -25.008 1.00 41.93  ? 294 PHE A CD2 1 
ATOM   2366 C  CE1 . PHE A 1 294 ? -0.552  -17.491 -22.636 1.00 43.29  ? 294 PHE A CE1 1 
ATOM   2367 C  CE2 . PHE A 1 294 ? -0.972  -19.355 -24.060 1.00 44.96  ? 294 PHE A CE2 1 
ATOM   2368 C  CZ  . PHE A 1 294 ? -0.477  -18.845 -22.880 1.00 43.58  ? 294 PHE A CZ  1 
ATOM   2369 N  N   . ASP A 1 295 ? -3.316  -13.563 -24.288 1.00 25.05  ? 295 ASP A N   1 
ATOM   2370 C  CA  . ASP A 1 295 ? -3.408  -12.628 -23.136 1.00 23.60  ? 295 ASP A CA  1 
ATOM   2371 C  C   . ASP A 1 295 ? -4.870  -12.511 -22.683 1.00 28.77  ? 295 ASP A C   1 
ATOM   2372 O  O   . ASP A 1 295 ? -5.098  -12.434 -21.459 1.00 26.48  ? 295 ASP A O   1 
ATOM   2373 C  CB  . ASP A 1 295 ? -2.941  -11.231 -23.500 1.00 24.52  ? 295 ASP A CB  1 
ATOM   2374 C  CG  . ASP A 1 295 ? -1.481  -11.139 -23.894 1.00 23.47  ? 295 ASP A CG  1 
ATOM   2375 O  OD1 . ASP A 1 295 ? -0.721  -12.054 -23.559 1.00 25.04  ? 295 ASP A OD1 1 
ATOM   2376 O  OD2 . ASP A 1 295 ? -1.150  -10.139 -24.561 1.00 23.64  ? 295 ASP A OD2 1 
ATOM   2377 N  N   . VAL A 1 296 ? -5.810  -12.462 -23.632 1.00 25.12  ? 296 VAL A N   1 
ATOM   2378 C  CA  . VAL A 1 296 ? -7.254  -12.280 -23.311 1.00 27.01  ? 296 VAL A CA  1 
ATOM   2379 C  C   . VAL A 1 296 ? -7.698  -13.499 -22.522 1.00 29.66  ? 296 VAL A C   1 
ATOM   2380 O  O   . VAL A 1 296 ? -8.304  -13.312 -21.438 1.00 30.71  ? 296 VAL A O   1 
ATOM   2381 C  CB  . VAL A 1 296 ? -8.135  -12.014 -24.545 1.00 26.75  ? 296 VAL A CB  1 
ATOM   2382 C  CG1 . VAL A 1 296 ? -9.616  -12.244 -24.273 1.00 27.43  ? 296 VAL A CG1 1 
ATOM   2383 C  CG2 . VAL A 1 296 ? -7.943  -10.596 -25.029 1.00 26.61  ? 296 VAL A CG2 1 
ATOM   2384 N  N   . VAL A 1 297 ? -7.326  -14.699 -22.968 1.00 33.09  ? 297 VAL A N   1 
ATOM   2385 C  CA  . VAL A 1 297 ? -7.727  -15.943 -22.252 1.00 34.16  ? 297 VAL A CA  1 
ATOM   2386 C  C   . VAL A 1 297 ? -7.051  -16.031 -20.877 1.00 35.01  ? 297 VAL A C   1 
ATOM   2387 O  O   . VAL A 1 297 ? -7.741  -16.417 -19.918 1.00 36.76  ? 297 VAL A O   1 
ATOM   2388 C  CB  . VAL A 1 297 ? -7.469  -17.184 -23.112 1.00 35.35  ? 297 VAL A CB  1 
ATOM   2389 C  CG1 . VAL A 1 297 ? -7.453  -18.450 -22.273 1.00 36.47  ? 297 VAL A CG1 1 
ATOM   2390 C  CG2 . VAL A 1 297 ? -8.502  -17.265 -24.216 1.00 33.11  ? 297 VAL A CG2 1 
ATOM   2391 N  N   . ARG A 1 298 ? -5.764  -15.690 -20.770 1.00 37.58  ? 298 ARG A N   1 
ATOM   2392 C  CA  . ARG A 1 298 ? -5.004  -15.703 -19.487 1.00 36.28  ? 298 ARG A CA  1 
ATOM   2393 C  C   . ARG A 1 298 ? -5.714  -14.786 -18.478 1.00 36.78  ? 298 ARG A C   1 
ATOM   2394 O  O   . ARG A 1 298 ? -5.849  -15.184 -17.325 1.00 35.78  ? 298 ARG A O   1 
ATOM   2395 C  CB  . ARG A 1 298 ? -3.533  -15.317 -19.712 1.00 38.48  ? 298 ARG A CB  1 
ATOM   2396 C  CG  . ARG A 1 298 ? -2.806  -14.647 -18.541 1.00 43.32  ? 298 ARG A CG  1 
ATOM   2397 C  CD  . ARG A 1 298 ? -1.727  -13.636 -18.987 1.00 49.05  ? 298 ARG A CD  1 
ATOM   2398 N  NE  . ARG A 1 298 ? -0.943  -13.027 -17.900 1.00 45.07  ? 298 ARG A NE  1 
ATOM   2399 C  CZ  . ARG A 1 298 ? -0.210  -11.913 -17.984 1.00 39.11  ? 298 ARG A CZ  1 
ATOM   2400 N  NH1 . ARG A 1 298 ? -0.074  -11.263 -19.124 1.00 38.66  ? 298 ARG A NH1 1 
ATOM   2401 N  NH2 . ARG A 1 298 ? 0.437   -11.484 -16.912 1.00 42.93  ? 298 ARG A NH2 1 
ATOM   2402 N  N   . GLN A 1 299 ? -6.126  -13.585 -18.883 1.00 33.34  ? 299 GLN A N   1 
ATOM   2403 C  CA  . GLN A 1 299 ? -6.662  -12.563 -17.948 1.00 37.55  ? 299 GLN A CA  1 
ATOM   2404 C  C   . GLN A 1 299 ? -8.154  -12.801 -17.663 1.00 41.06  ? 299 GLN A C   1 
ATOM   2405 O  O   . GLN A 1 299 ? -8.579  -12.370 -16.578 1.00 45.51  ? 299 GLN A O   1 
ATOM   2406 C  CB  . GLN A 1 299 ? -6.401  -11.142 -18.467 1.00 35.70  ? 299 GLN A CB  1 
ATOM   2407 C  CG  . GLN A 1 299 ? -6.942  -10.062 -17.534 1.00 36.53  ? 299 GLN A CG  1 
ATOM   2408 C  CD  . GLN A 1 299 ? -6.341  -8.683  -17.685 1.00 34.17  ? 299 GLN A CD  1 
ATOM   2409 O  OE1 . GLN A 1 299 ? -6.745  -7.740  -17.016 1.00 33.26  ? 299 GLN A OE1 1 
ATOM   2410 N  NE2 . GLN A 1 299 ? -5.394  -8.528  -18.590 1.00 35.71  ? 299 GLN A NE2 1 
ATOM   2411 N  N   . CYS A 1 300 ? -8.910  -13.472 -18.549 1.00 44.59  ? 300 CYS A N   1 
ATOM   2412 C  CA  . CYS A 1 300 ? -10.400 -13.627 -18.462 1.00 45.62  ? 300 CYS A CA  1 
ATOM   2413 C  C   . CYS A 1 300 ? -10.820 -14.986 -17.871 1.00 93.81  ? 300 CYS A C   1 
ATOM   2414 O  O   . CYS A 1 300 ? -10.086 -15.947 -17.635 1.00 92.20  ? 300 CYS A O   1 
ATOM   2415 C  CB  . CYS A 1 300 ? -11.059 -13.425 -19.826 1.00 45.84  ? 300 CYS A CB  1 
ATOM   2416 S  SG  . CYS A 1 300 ? -11.064 -11.691 -20.373 1.00 44.96  ? 300 CYS A SG  1 
ATOM   2417 N  N   . SER B 1 1   ? 12.730  8.463   -24.292 1.00 31.22  ? 1   SER B N   1 
ATOM   2418 C  CA  . SER B 1 1   ? 11.346  8.956   -24.207 1.00 29.41  ? 1   SER B CA  1 
ATOM   2419 C  C   . SER B 1 1   ? 10.333  7.806   -24.305 1.00 27.00  ? 1   SER B C   1 
ATOM   2420 O  O   . SER B 1 1   ? 10.709  6.627   -24.269 1.00 26.41  ? 1   SER B O   1 
ATOM   2421 C  CB  . SER B 1 1   ? 11.087  10.014  -25.258 1.00 31.87  ? 1   SER B CB  1 
ATOM   2422 O  OG  . SER B 1 1   ? 11.314  9.505   -26.551 1.00 31.21  ? 1   SER B OG  1 
ATOM   2423 N  N   . GLY B 1 2   ? 9.066   8.194   -24.364 1.00 25.72  ? 2   GLY B N   1 
ATOM   2424 C  CA  . GLY B 1 2   ? 7.896   7.315   -24.340 1.00 28.53  ? 2   GLY B CA  1 
ATOM   2425 C  C   . GLY B 1 2   ? 7.248   7.452   -22.982 1.00 28.84  ? 2   GLY B C   1 
ATOM   2426 O  O   . GLY B 1 2   ? 7.888   7.977   -22.068 1.00 28.64  ? 2   GLY B O   1 
ATOM   2427 N  N   . PHE B 1 3   ? 6.038   6.959   -22.840 1.00 28.55  ? 3   PHE B N   1 
ATOM   2428 C  CA  . PHE B 1 3   ? 5.289   7.088   -21.580 1.00 30.21  ? 3   PHE B CA  1 
ATOM   2429 C  C   . PHE B 1 3   ? 4.315   5.936   -21.482 1.00 27.24  ? 3   PHE B C   1 
ATOM   2430 O  O   . PHE B 1 3   ? 3.515   5.737   -22.398 1.00 32.08  ? 3   PHE B O   1 
ATOM   2431 C  CB  . PHE B 1 3   ? 4.549   8.423   -21.482 1.00 29.62  ? 3   PHE B CB  1 
ATOM   2432 C  CG  . PHE B 1 3   ? 4.229   8.755   -20.048 1.00 29.73  ? 3   PHE B CG  1 
ATOM   2433 C  CD1 . PHE B 1 3   ? 5.252   9.065   -19.175 1.00 28.63  ? 3   PHE B CD1 1 
ATOM   2434 C  CD2 . PHE B 1 3   ? 2.938   8.648   -19.557 1.00 29.62  ? 3   PHE B CD2 1 
ATOM   2435 C  CE1 . PHE B 1 3   ? 4.981   9.350   -17.844 1.00 34.24  ? 3   PHE B CE1 1 
ATOM   2436 C  CE2 . PHE B 1 3   ? 2.664   8.928   -18.228 1.00 30.81  ? 3   PHE B CE2 1 
ATOM   2437 C  CZ  . PHE B 1 3   ? 3.689   9.278   -17.372 1.00 32.13  ? 3   PHE B CZ  1 
ATOM   2438 N  N   . ARG B 1 4   ? 4.442   5.174   -20.405 1.00 26.96  ? 4   ARG B N   1 
ATOM   2439 C  CA  . ARG B 1 4   ? 3.692   3.915   -20.223 1.00 25.62  ? 4   ARG B CA  1 
ATOM   2440 C  C   . ARG B 1 4   ? 3.211   3.872   -18.775 1.00 26.34  ? 4   ARG B C   1 
ATOM   2441 O  O   . ARG B 1 4   ? 3.888   4.429   -17.886 1.00 25.45  ? 4   ARG B O   1 
ATOM   2442 C  CB  . ARG B 1 4   ? 4.600   2.724   -20.553 1.00 27.07  ? 4   ARG B CB  1 
ATOM   2443 C  CG  . ARG B 1 4   ? 4.656   2.395   -22.030 1.00 33.01  ? 4   ARG B CG  1 
ATOM   2444 C  CD  . ARG B 1 4   ? 3.676   1.276   -22.379 1.00 34.24  ? 4   ARG B CD  1 
ATOM   2445 N  NE  . ARG B 1 4   ? 3.850   0.960   -23.785 1.00 37.35  ? 4   ARG B NE  1 
ATOM   2446 C  CZ  . ARG B 1 4   ? 2.982   0.295   -24.529 1.00 37.96  ? 4   ARG B CZ  1 
ATOM   2447 N  NH1 . ARG B 1 4   ? 1.871   -0.180  -23.987 1.00 41.31  ? 4   ARG B NH1 1 
ATOM   2448 N  NH2 . ARG B 1 4   ? 3.242   0.100   -25.809 1.00 30.05  ? 4   ARG B NH2 1 
ATOM   2449 N  N   . LYS B 1 5   ? 2.074   3.232   -18.574 1.00 24.78  ? 5   LYS B N   1 
ATOM   2450 C  CA  . LYS B 1 5   ? 1.594   2.848   -17.238 1.00 26.70  ? 5   LYS B CA  1 
ATOM   2451 C  C   . LYS B 1 5   ? 2.534   1.765   -16.707 1.00 26.73  ? 5   LYS B C   1 
ATOM   2452 O  O   . LYS B 1 5   ? 2.597   0.660   -17.255 1.00 22.92  ? 5   LYS B O   1 
ATOM   2453 C  CB  . LYS B 1 5   ? 0.146   2.387   -17.312 1.00 30.15  ? 5   LYS B CB  1 
ATOM   2454 C  CG  . LYS B 1 5   ? -0.533  2.333   -15.962 1.00 34.77  ? 5   LYS B CG  1 
ATOM   2455 C  CD  . LYS B 1 5   ? -2.009  2.454   -16.109 1.00 39.72  ? 5   LYS B CD  1 
ATOM   2456 C  CE  . LYS B 1 5   ? -2.438  3.895   -16.300 1.00 46.37  ? 5   LYS B CE  1 
ATOM   2457 N  NZ  . LYS B 1 5   ? -3.814  3.974   -16.839 1.00 54.54  ? 5   LYS B NZ  1 
ATOM   2458 N  N   . MET B 1 6   ? 3.288   2.116   -15.688 1.00 26.03  ? 6   MET B N   1 
ATOM   2459 C  CA  . MET B 1 6   ? 4.444   1.304   -15.272 1.00 26.20  ? 6   MET B CA  1 
ATOM   2460 C  C   . MET B 1 6   ? 4.223   0.933   -13.815 1.00 22.05  ? 6   MET B C   1 
ATOM   2461 O  O   . MET B 1 6   ? 4.006   1.831   -13.028 1.00 18.98  ? 6   MET B O   1 
ATOM   2462 C  CB  . MET B 1 6   ? 5.683   2.173   -15.477 1.00 28.95  ? 6   MET B CB  1 
ATOM   2463 C  CG  . MET B 1 6   ? 6.976   1.573   -15.065 1.00 33.61  ? 6   MET B CG  1 
ATOM   2464 S  SD  . MET B 1 6   ? 8.277   2.789   -15.439 1.00 36.27  ? 6   MET B SD  1 
ATOM   2465 C  CE  . MET B 1 6   ? 8.330   2.741   -17.226 1.00 34.28  ? 6   MET B CE  1 
ATOM   2466 N  N   . ALA B 1 7   ? 4.293   -0.353  -13.481 1.00 21.34  ? 7   ALA B N   1 
ATOM   2467 C  CA  . ALA B 1 7   ? 4.224   -0.841  -12.091 1.00 19.83  ? 7   ALA B CA  1 
ATOM   2468 C  C   . ALA B 1 7   ? 5.615   -0.753  -11.479 1.00 21.79  ? 7   ALA B C   1 
ATOM   2469 O  O   . ALA B 1 7   ? 6.587   -0.720  -12.242 1.00 20.67  ? 7   ALA B O   1 
ATOM   2470 C  CB  . ALA B 1 7   ? 3.699   -2.258  -12.080 1.00 21.38  ? 7   ALA B CB  1 
ATOM   2471 N  N   . PHE B 1 8   ? 5.716   -0.797  -10.159 1.00 20.37  ? 8   PHE B N   1 
ATOM   2472 C  CA  . PHE B 1 8   ? 7.011   -1.074  -9.489  1.00 21.95  ? 8   PHE B CA  1 
ATOM   2473 C  C   . PHE B 1 8   ? 7.420   -2.509  -9.762  1.00 20.85  ? 8   PHE B C   1 
ATOM   2474 O  O   . PHE B 1 8   ? 6.585   -3.375  -9.961  1.00 20.21  ? 8   PHE B O   1 
ATOM   2475 C  CB  . PHE B 1 8   ? 6.919   -0.850  -7.987  1.00 23.06  ? 8   PHE B CB  1 
ATOM   2476 C  CG  . PHE B 1 8   ? 6.881   0.602   -7.641  1.00 22.82  ? 8   PHE B CG  1 
ATOM   2477 C  CD1 . PHE B 1 8   ? 8.049   1.323   -7.626  1.00 26.16  ? 8   PHE B CD1 1 
ATOM   2478 C  CD2 . PHE B 1 8   ? 5.690   1.261   -7.379  1.00 25.98  ? 8   PHE B CD2 1 
ATOM   2479 C  CE1 . PHE B 1 8   ? 8.047   2.674   -7.317  1.00 27.54  ? 8   PHE B CE1 1 
ATOM   2480 C  CE2 . PHE B 1 8   ? 5.689   2.616   -7.070  1.00 26.19  ? 8   PHE B CE2 1 
ATOM   2481 C  CZ  . PHE B 1 8   ? 6.871   3.325   -7.057  1.00 28.08  ? 8   PHE B CZ  1 
ATOM   2482 N  N   . PRO B 1 9   ? 8.730   -2.801  -9.763  1.00 22.95  ? 9   PRO B N   1 
ATOM   2483 C  CA  . PRO B 1 9   ? 9.197   -4.174  -9.910  1.00 21.80  ? 9   PRO B CA  1 
ATOM   2484 C  C   . PRO B 1 9   ? 8.693   -4.940  -8.678  1.00 21.73  ? 9   PRO B C   1 
ATOM   2485 O  O   . PRO B 1 9   ? 8.790   -4.419  -7.601  1.00 23.82  ? 9   PRO B O   1 
ATOM   2486 C  CB  . PRO B 1 9   ? 10.723  -4.054  -9.910  1.00 23.93  ? 9   PRO B CB  1 
ATOM   2487 C  CG  . PRO B 1 9   ? 10.999  -2.572  -10.161 1.00 24.03  ? 9   PRO B CG  1 
ATOM   2488 C  CD  . PRO B 1 9   ? 9.824   -1.845  -9.554  1.00 23.13  ? 9   PRO B CD  1 
ATOM   2489 N  N   . SER B 1 10  ? 8.143   -6.126  -8.874  1.00 21.70  ? 10  SER B N   1 
ATOM   2490 C  CA  . SER B 1 10  ? 7.293   -6.804  -7.858  1.00 21.82  ? 10  SER B CA  1 
ATOM   2491 C  C   . SER B 1 10  ? 8.076   -7.849  -7.052  1.00 21.90  ? 10  SER B C   1 
ATOM   2492 O  O   . SER B 1 10  ? 7.481   -8.465  -6.141  1.00 22.32  ? 10  SER B O   1 
ATOM   2493 C  CB  . SER B 1 10  ? 6.081   -7.400  -8.513  1.00 21.00  ? 10  SER B CB  1 
ATOM   2494 O  OG  . SER B 1 10  ? 6.444   -8.227  -9.601  1.00 19.58  ? 10  SER B OG  1 
ATOM   2495 N  N   . GLY B 1 11  ? 9.360   -8.051  -7.350  1.00 22.13  ? 11  GLY B N   1 
ATOM   2496 C  CA  . GLY B 1 11  ? 10.143  -9.152  -6.775  1.00 22.94  ? 11  GLY B CA  1 
ATOM   2497 C  C   . GLY B 1 11  ? 10.087  -9.144  -5.245  1.00 23.44  ? 11  GLY B C   1 
ATOM   2498 O  O   . GLY B 1 11  ? 9.948   -10.193 -4.659  1.00 24.21  ? 11  GLY B O   1 
ATOM   2499 N  N   . LYS B 1 12  ? 10.241  -7.996  -4.606  1.00 23.45  ? 12  LYS B N   1 
ATOM   2500 C  CA  . LYS B 1 12  ? 10.271  -7.927  -3.124  1.00 26.37  ? 12  LYS B CA  1 
ATOM   2501 C  C   . LYS B 1 12  ? 8.945   -8.426  -2.545  1.00 25.24  ? 12  LYS B C   1 
ATOM   2502 O  O   . LYS B 1 12  ? 8.929   -8.919  -1.445  1.00 25.18  ? 12  LYS B O   1 
ATOM   2503 C  CB  . LYS B 1 12  ? 10.539  -6.498  -2.683  1.00 29.01  ? 12  LYS B CB  1 
ATOM   2504 C  CG  . LYS B 1 12  ? 11.981  -6.044  -2.841  1.00 31.53  ? 12  LYS B CG  1 
ATOM   2505 C  CD  . LYS B 1 12  ? 12.143  -4.594  -2.419  1.00 34.87  ? 12  LYS B CD  1 
ATOM   2506 C  CE  . LYS B 1 12  ? 13.579  -4.189  -2.170  1.00 38.23  ? 12  LYS B CE  1 
ATOM   2507 N  NZ  . LYS B 1 12  ? 14.420  -4.523  -3.335  1.00 43.20  ? 12  LYS B NZ  1 
ATOM   2508 N  N   . VAL B 1 13  ? 7.861   -8.331  -3.293  1.00 25.55  ? 13  VAL B N   1 
ATOM   2509 C  CA  . VAL B 1 13  ? 6.516   -8.733  -2.814  1.00 24.38  ? 13  VAL B CA  1 
ATOM   2510 C  C   . VAL B 1 13  ? 6.228   -10.182 -3.198  1.00 25.17  ? 13  VAL B C   1 
ATOM   2511 O  O   . VAL B 1 13  ? 5.601   -10.885 -2.368  1.00 24.32  ? 13  VAL B O   1 
ATOM   2512 C  CB  . VAL B 1 13  ? 5.464   -7.770  -3.365  1.00 22.52  ? 13  VAL B CB  1 
ATOM   2513 C  CG1 . VAL B 1 13  ? 4.083   -8.159  -2.886  1.00 24.66  ? 13  VAL B CG1 1 
ATOM   2514 C  CG2 . VAL B 1 13  ? 5.825   -6.356  -2.980  1.00 22.15  ? 13  VAL B CG2 1 
ATOM   2515 N  N   . GLU B 1 14  ? 6.650   -10.627 -4.388  1.00 22.30  ? 14  GLU B N   1 
ATOM   2516 C  CA  . GLU B 1 14  ? 6.515   -12.047 -4.810  1.00 25.17  ? 14  GLU B CA  1 
ATOM   2517 C  C   . GLU B 1 14  ? 7.006   -12.967 -3.679  1.00 25.44  ? 14  GLU B C   1 
ATOM   2518 O  O   . GLU B 1 14  ? 6.308   -13.954 -3.399  1.00 26.92  ? 14  GLU B O   1 
ATOM   2519 C  CB  . GLU B 1 14  ? 7.295   -12.319 -6.101  1.00 22.41  ? 14  GLU B CB  1 
ATOM   2520 C  CG  . GLU B 1 14  ? 6.692   -11.590 -7.275  1.00 24.31  ? 14  GLU B CG  1 
ATOM   2521 C  CD  . GLU B 1 14  ? 7.580   -11.577 -8.500  1.00 26.21  ? 14  GLU B CD  1 
ATOM   2522 O  OE1 . GLU B 1 14  ? 7.956   -12.659 -8.898  1.00 24.74  ? 14  GLU B OE1 1 
ATOM   2523 O  OE2 . GLU B 1 14  ? 7.853   -10.479 -9.062  1.00 27.24  ? 14  GLU B OE2 1 
ATOM   2524 N  N   . GLY B 1 15  ? 8.142   -12.630 -3.066  1.00 27.35  ? 15  GLY B N   1 
ATOM   2525 C  CA  . GLY B 1 15  ? 8.785   -13.390 -1.972  1.00 28.64  ? 15  GLY B CA  1 
ATOM   2526 C  C   . GLY B 1 15  ? 7.933   -13.447 -0.707  1.00 29.43  ? 15  GLY B C   1 
ATOM   2527 O  O   . GLY B 1 15  ? 8.329   -14.168 0.230   1.00 25.91  ? 15  GLY B O   1 
ATOM   2528 N  N   . CYS B 1 16  ? 6.809   -12.721 -0.653  1.00 26.22  ? 16  CYS B N   1 
ATOM   2529 C  CA  . CYS B 1 16  ? 5.968   -12.621 0.572   1.00 25.61  ? 16  CYS B CA  1 
ATOM   2530 C  C   . CYS B 1 16  ? 4.628   -13.325 0.391   1.00 22.92  ? 16  CYS B C   1 
ATOM   2531 O  O   . CYS B 1 16  ? 3.902   -13.493 1.398   1.00 24.56  ? 16  CYS B O   1 
ATOM   2532 C  CB  . CYS B 1 16  ? 5.760   -11.166 0.951   1.00 25.19  ? 16  CYS B CB  1 
ATOM   2533 S  SG  . CYS B 1 16  ? 7.295   -10.325 1.385   1.00 27.58  ? 16  CYS B SG  1 
ATOM   2534 N  N   . MET B 1 17  ? 4.276   -13.751 -0.822  1.00 25.28  ? 17  MET B N   1 
ATOM   2535 C  CA  . MET B 1 17  ? 2.917   -14.262 -1.084  1.00 23.87  ? 17  MET B CA  1 
ATOM   2536 C  C   . MET B 1 17  ? 2.850   -15.747 -0.696  1.00 28.43  ? 17  MET B C   1 
ATOM   2537 O  O   . MET B 1 17  ? 3.768   -16.498 -1.028  1.00 26.76  ? 17  MET B O   1 
ATOM   2538 C  CB  . MET B 1 17  ? 2.513   -14.106 -2.550  1.00 25.37  ? 17  MET B CB  1 
ATOM   2539 C  CG  . MET B 1 17  ? 2.498   -12.660 -3.028  1.00 25.78  ? 17  MET B CG  1 
ATOM   2540 S  SD  . MET B 1 17  ? 1.676   -11.545 -1.899  1.00 23.88  ? 17  MET B SD  1 
ATOM   2541 C  CE  . MET B 1 17  ? 0.044   -12.269 -1.777  1.00 23.96  ? 17  MET B CE  1 
ATOM   2542 N  N   . VAL B 1 18  ? 1.766   -16.138 -0.031  1.00 26.26  ? 18  VAL B N   1 
ATOM   2543 C  CA  . VAL B 1 18  ? 1.509   -17.543 0.379   1.00 27.19  ? 18  VAL B CA  1 
ATOM   2544 C  C   . VAL B 1 18  ? 0.048   -17.863 0.104   1.00 25.19  ? 18  VAL B C   1 
ATOM   2545 O  O   . VAL B 1 18  ? -0.754  -16.947 -0.126  1.00 29.45  ? 18  VAL B O   1 
ATOM   2546 C  CB  . VAL B 1 18  ? 1.868   -17.781 1.861   1.00 23.94  ? 18  VAL B CB  1 
ATOM   2547 C  CG1 . VAL B 1 18  ? 3.310   -17.449 2.164   1.00 23.92  ? 18  VAL B CG1 1 
ATOM   2548 C  CG2 . VAL B 1 18  ? 0.949   -17.037 2.808   1.00 25.85  ? 18  VAL B CG2 1 
ATOM   2549 N  N   . GLN B 1 19  ? -0.293  -19.130 0.237   1.00 29.61  ? 19  GLN B N   1 
ATOM   2550 C  CA  . GLN B 1 19  ? -1.666  -19.652 0.105   1.00 31.11  ? 19  GLN B CA  1 
ATOM   2551 C  C   . GLN B 1 19  ? -2.233  -19.862 1.495   1.00 30.82  ? 19  GLN B C   1 
ATOM   2552 O  O   . GLN B 1 19  ? -1.519  -20.425 2.343   1.00 35.89  ? 19  GLN B O   1 
ATOM   2553 C  CB  . GLN B 1 19  ? -1.640  -20.972 -0.661  1.00 36.26  ? 19  GLN B CB  1 
ATOM   2554 C  CG  . GLN B 1 19  ? -3.030  -21.434 -1.025  1.00 39.91  ? 19  GLN B CG  1 
ATOM   2555 C  CD  . GLN B 1 19  ? -3.015  -22.753 -1.744  1.00 45.30  ? 19  GLN B CD  1 
ATOM   2556 O  OE1 . GLN B 1 19  ? -3.718  -22.929 -2.737  1.00 47.71  ? 19  GLN B OE1 1 
ATOM   2557 N  NE2 . GLN B 1 19  ? -2.219  -23.681 -1.231  1.00 43.60  ? 19  GLN B NE2 1 
ATOM   2558 N  N   . VAL B 1 20  ? -3.455  -19.400 1.728   1.00 31.88  ? 20  VAL B N   1 
ATOM   2559 C  CA  . VAL B 1 20  ? -4.164  -19.579 3.027   1.00 34.04  ? 20  VAL B CA  1 
ATOM   2560 C  C   . VAL B 1 20  ? -5.477  -20.293 2.720   1.00 35.87  ? 20  VAL B C   1 
ATOM   2561 O  O   . VAL B 1 20  ? -6.213  -19.832 1.827   1.00 34.01  ? 20  VAL B O   1 
ATOM   2562 C  CB  . VAL B 1 20  ? -4.385  -18.235 3.753   1.00 33.12  ? 20  VAL B CB  1 
ATOM   2563 C  CG1 . VAL B 1 20  ? -5.102  -18.431 5.076   1.00 34.84  ? 20  VAL B CG1 1 
ATOM   2564 C  CG2 . VAL B 1 20  ? -3.065  -17.496 3.981   1.00 32.93  ? 20  VAL B CG2 1 
ATOM   2565 N  N   . THR B 1 21  ? -5.716  -21.422 3.386   1.00 40.90  ? 21  THR B N   1 
ATOM   2566 C  CA  . THR B 1 21  ? -6.963  -22.211 3.260   1.00 39.24  ? 21  THR B CA  1 
ATOM   2567 C  C   . THR B 1 21  ? -7.586  -22.373 4.647   1.00 41.32  ? 21  THR B C   1 
ATOM   2568 O  O   . THR B 1 21  ? -6.860  -22.756 5.587   1.00 42.49  ? 21  THR B O   1 
ATOM   2569 C  CB  . THR B 1 21  ? -6.731  -23.585 2.622   1.00 38.04  ? 21  THR B CB  1 
ATOM   2570 O  OG1 . THR B 1 21  ? -6.012  -23.458 1.397   1.00 33.91  ? 21  THR B OG1 1 
ATOM   2571 C  CG2 . THR B 1 21  ? -8.042  -24.294 2.365   1.00 40.35  ? 21  THR B CG2 1 
ATOM   2572 N  N   . CYS B 1 22  ? -8.875  -22.070 4.747   1.00 41.92  ? 22  CYS B N   1 
ATOM   2573 C  CA  . CYS B 1 22  ? -9.731  -22.298 5.938   1.00 45.26  ? 22  CYS B CA  1 
ATOM   2574 C  C   . CYS B 1 22  ? -10.987 -23.022 5.450   1.00 45.07  ? 22  CYS B C   1 
ATOM   2575 O  O   . CYS B 1 22  ? -11.818 -22.373 4.795   1.00 47.31  ? 22  CYS B O   1 
ATOM   2576 C  CB  . CYS B 1 22  ? -10.062 -20.982 6.635   1.00 44.32  ? 22  CYS B CB  1 
ATOM   2577 S  SG  . CYS B 1 22  ? -10.793 -21.179 8.277   1.00 44.52  ? 22  CYS B SG  1 
ATOM   2578 N  N   . GLY B 1 23  ? -11.056 -24.338 5.680   1.00 47.02  ? 23  GLY B N   1 
ATOM   2579 C  CA  . GLY B 1 23  ? -12.141 -25.216 5.193   1.00 44.14  ? 23  GLY B CA  1 
ATOM   2580 C  C   . GLY B 1 23  ? -12.151 -25.279 3.679   1.00 38.28  ? 23  GLY B C   1 
ATOM   2581 O  O   . GLY B 1 23  ? -11.160 -25.719 3.106   1.00 40.31  ? 23  GLY B O   1 
ATOM   2582 N  N   . THR B 1 24  ? -13.197 -24.777 3.040   1.00 40.99  ? 24  THR B N   1 
ATOM   2583 C  CA  . THR B 1 24  ? -13.337 -24.831 1.560   1.00 48.13  ? 24  THR B CA  1 
ATOM   2584 C  C   . THR B 1 24  ? -12.688 -23.608 0.886   1.00 44.89  ? 24  THR B C   1 
ATOM   2585 O  O   . THR B 1 24  ? -12.454 -23.705 -0.328  1.00 42.78  ? 24  THR B O   1 
ATOM   2586 C  CB  . THR B 1 24  ? -14.802 -24.994 1.110   1.00 50.57  ? 24  THR B CB  1 
ATOM   2587 O  OG1 . THR B 1 24  ? -15.658 -24.031 1.722   1.00 50.27  ? 24  THR B OG1 1 
ATOM   2588 C  CG2 . THR B 1 24  ? -15.343 -26.376 1.402   1.00 54.32  ? 24  THR B CG2 1 
ATOM   2589 N  N   . THR B 1 25  ? -12.417 -22.514 1.609   1.00 49.85  ? 25  THR B N   1 
ATOM   2590 C  CA  . THR B 1 25  ? -11.918 -21.235 1.017   1.00 45.12  ? 25  THR B CA  1 
ATOM   2591 C  C   . THR B 1 25  ? -10.391 -21.249 0.947   1.00 42.76  ? 25  THR B C   1 
ATOM   2592 O  O   . THR B 1 25  ? -9.728  -21.309 2.002   1.00 41.98  ? 25  THR B O   1 
ATOM   2593 C  CB  . THR B 1 25  ? -12.386 -19.996 1.791   1.00 49.31  ? 25  THR B CB  1 
ATOM   2594 O  OG1 . THR B 1 25  ? -13.790 -20.119 1.984   1.00 47.46  ? 25  THR B OG1 1 
ATOM   2595 C  CG2 . THR B 1 25  ? -12.115 -18.691 1.070   1.00 49.20  ? 25  THR B CG2 1 
ATOM   2596 N  N   . THR B 1 26  ? -9.849  -21.178 -0.266  1.00 42.18  ? 26  THR B N   1 
ATOM   2597 C  CA  . THR B 1 26  ? -8.428  -20.844 -0.490  1.00 41.84  ? 26  THR B CA  1 
ATOM   2598 C  C   . THR B 1 26  ? -8.344  -19.404 -1.009  1.00 38.90  ? 26  THR B C   1 
ATOM   2599 O  O   . THR B 1 26  ? -9.181  -19.023 -1.822  1.00 35.60  ? 26  THR B O   1 
ATOM   2600 C  CB  . THR B 1 26  ? -7.776  -21.894 -1.387  1.00 40.78  ? 26  THR B CB  1 
ATOM   2601 O  OG1 . THR B 1 26  ? -7.862  -23.101 -0.638  1.00 47.35  ? 26  THR B OG1 1 
ATOM   2602 C  CG2 . THR B 1 26  ? -6.324  -21.608 -1.694  1.00 44.18  ? 26  THR B CG2 1 
ATOM   2603 N  N   . LEU B 1 27  ? -7.356  -18.640 -0.534  1.00 35.71  ? 27  LEU B N   1 
ATOM   2604 C  CA  . LEU B 1 27  ? -7.019  -17.310 -1.097  1.00 31.43  ? 27  LEU B CA  1 
ATOM   2605 C  C   . LEU B 1 27  ? -5.576  -16.982 -0.707  1.00 30.00  ? 27  LEU B C   1 
ATOM   2606 O  O   . LEU B 1 27  ? -4.843  -17.902 -0.257  1.00 29.26  ? 27  LEU B O   1 
ATOM   2607 C  CB  . LEU B 1 27  ? -8.037  -16.283 -0.589  1.00 30.29  ? 27  LEU B CB  1 
ATOM   2608 C  CG  . LEU B 1 27  ? -8.353  -16.339 0.909   1.00 28.42  ? 27  LEU B CG  1 
ATOM   2609 C  CD1 . LEU B 1 27  ? -7.195  -15.879 1.780   1.00 27.28  ? 27  LEU B CD1 1 
ATOM   2610 C  CD2 . LEU B 1 27  ? -9.579  -15.517 1.200   1.00 29.63  ? 27  LEU B CD2 1 
ATOM   2611 N  N   . ASN B 1 28  ? -5.175  -15.725 -0.837  1.00 27.81  ? 28  ASN B N   1 
ATOM   2612 C  CA  . ASN B 1 28  ? -3.745  -15.331 -0.721  1.00 26.26  ? 28  ASN B CA  1 
ATOM   2613 C  C   . ASN B 1 28  ? -3.488  -14.686 0.630   1.00 24.88  ? 28  ASN B C   1 
ATOM   2614 O  O   . ASN B 1 28  ? -4.368  -14.007 1.163   1.00 28.65  ? 28  ASN B O   1 
ATOM   2615 C  CB  . ASN B 1 28  ? -3.313  -14.407 -1.863  1.00 26.07  ? 28  ASN B CB  1 
ATOM   2616 C  CG  . ASN B 1 28  ? -3.628  -14.995 -3.222  1.00 24.64  ? 28  ASN B CG  1 
ATOM   2617 O  OD1 . ASN B 1 28  ? -2.857  -15.787 -3.726  1.00 22.95  ? 28  ASN B OD1 1 
ATOM   2618 N  ND2 . ASN B 1 28  ? -4.737  -14.599 -3.830  1.00 24.88  ? 28  ASN B ND2 1 
ATOM   2619 N  N   . GLY B 1 29  ? -2.280  -14.890 1.134   1.00 25.74  ? 29  GLY B N   1 
ATOM   2620 C  CA  . GLY B 1 29  ? -1.787  -14.261 2.358   1.00 25.40  ? 29  GLY B CA  1 
ATOM   2621 C  C   . GLY B 1 29  ? -0.493  -13.528 2.077   1.00 25.09  ? 29  GLY B C   1 
ATOM   2622 O  O   . GLY B 1 29  ? 0.238   -13.885 1.120   1.00 24.70  ? 29  GLY B O   1 
ATOM   2623 N  N   . LEU B 1 30  ? -0.202  -12.552 2.911   1.00 22.15  ? 30  LEU B N   1 
ATOM   2624 C  CA  . LEU B 1 30  ? 1.067   -11.814 2.876   1.00 23.08  ? 30  LEU B CA  1 
ATOM   2625 C  C   . LEU B 1 30  ? 1.900   -12.232 4.099   1.00 26.16  ? 30  LEU B C   1 
ATOM   2626 O  O   . LEU B 1 30  ? 1.475   -11.970 5.241   1.00 26.46  ? 30  LEU B O   1 
ATOM   2627 C  CB  . LEU B 1 30  ? 0.734   -10.317 2.870   1.00 21.93  ? 30  LEU B CB  1 
ATOM   2628 C  CG  . LEU B 1 30  ? 1.942   -9.393  2.716   1.00 20.92  ? 30  LEU B CG  1 
ATOM   2629 C  CD1 . LEU B 1 30  ? 2.562   -9.514  1.333   1.00 21.06  ? 30  LEU B CD1 1 
ATOM   2630 C  CD2 . LEU B 1 30  ? 1.572   -7.946  3.004   1.00 19.98  ? 30  LEU B CD2 1 
ATOM   2631 N  N   . TRP B 1 31  ? 3.061   -12.847 3.862   1.00 27.29  ? 31  TRP B N   1 
ATOM   2632 C  CA  . TRP B 1 31  ? 3.962   -13.395 4.906   1.00 27.08  ? 31  TRP B CA  1 
ATOM   2633 C  C   . TRP B 1 31  ? 5.102   -12.411 5.162   1.00 26.05  ? 31  TRP B C   1 
ATOM   2634 O  O   . TRP B 1 31  ? 6.015   -12.354 4.328   1.00 24.36  ? 31  TRP B O   1 
ATOM   2635 C  CB  . TRP B 1 31  ? 4.489   -14.768 4.473   1.00 29.15  ? 31  TRP B CB  1 
ATOM   2636 C  CG  . TRP B 1 31  ? 5.358   -15.446 5.491   1.00 30.56  ? 31  TRP B CG  1 
ATOM   2637 C  CD1 . TRP B 1 31  ? 5.403   -15.217 6.837   1.00 31.55  ? 31  TRP B CD1 1 
ATOM   2638 C  CD2 . TRP B 1 31  ? 6.273   -16.521 5.240   1.00 33.16  ? 31  TRP B CD2 1 
ATOM   2639 N  NE1 . TRP B 1 31  ? 6.308   -16.049 7.441   1.00 33.78  ? 31  TRP B NE1 1 
ATOM   2640 C  CE2 . TRP B 1 31  ? 6.845   -16.872 6.484   1.00 37.11  ? 31  TRP B CE2 1 
ATOM   2641 C  CE3 . TRP B 1 31  ? 6.658   -17.212 4.086   1.00 32.58  ? 31  TRP B CE3 1 
ATOM   2642 C  CZ2 . TRP B 1 31  ? 7.793   -17.885 6.598   1.00 36.03  ? 31  TRP B CZ2 1 
ATOM   2643 C  CZ3 . TRP B 1 31  ? 7.587   -18.220 4.204   1.00 35.63  ? 31  TRP B CZ3 1 
ATOM   2644 C  CH2 . TRP B 1 31  ? 8.146   -18.544 5.445   1.00 34.80  ? 31  TRP B CH2 1 
ATOM   2645 N  N   . LEU B 1 32  ? 5.050   -11.698 6.282   1.00 24.48  ? 32  LEU B N   1 
ATOM   2646 C  CA  . LEU B 1 32  ? 6.075   -10.715 6.719   1.00 27.51  ? 32  LEU B CA  1 
ATOM   2647 C  C   . LEU B 1 32  ? 6.538   -11.055 8.142   1.00 26.52  ? 32  LEU B C   1 
ATOM   2648 O  O   . LEU B 1 32  ? 5.693   -11.176 9.039   1.00 28.24  ? 32  LEU B O   1 
ATOM   2649 C  CB  . LEU B 1 32  ? 5.476   -9.310  6.681   1.00 29.70  ? 32  LEU B CB  1 
ATOM   2650 C  CG  . LEU B 1 32  ? 5.035   -8.817  5.304   1.00 31.38  ? 32  LEU B CG  1 
ATOM   2651 C  CD1 . LEU B 1 32  ? 4.300   -7.491  5.433   1.00 30.39  ? 32  LEU B CD1 1 
ATOM   2652 C  CD2 . LEU B 1 32  ? 6.224   -8.693  4.373   1.00 31.27  ? 32  LEU B CD2 1 
ATOM   2653 N  N   . ASP B 1 33  ? 7.844   -11.113 8.358   1.00 29.65  ? 33  ASP B N   1 
ATOM   2654 C  CA  . ASP B 1 33  ? 8.400   -11.567 9.658   1.00 28.70  ? 33  ASP B CA  1 
ATOM   2655 C  C   . ASP B 1 33  ? 7.691   -12.893 9.962   1.00 28.90  ? 33  ASP B C   1 
ATOM   2656 O  O   . ASP B 1 33  ? 7.653   -13.759 9.052   1.00 28.13  ? 33  ASP B O   1 
ATOM   2657 C  CB  . ASP B 1 33  ? 8.265   -10.452 10.699  1.00 30.66  ? 33  ASP B CB  1 
ATOM   2658 C  CG  . ASP B 1 33  ? 8.870   -9.119  10.268  1.00 32.48  ? 33  ASP B CG  1 
ATOM   2659 O  OD1 . ASP B 1 33  ? 10.101  -9.060  10.101  1.00 37.29  ? 33  ASP B OD1 1 
ATOM   2660 O  OD2 . ASP B 1 33  ? 8.096   -8.130  10.112  1.00 33.30  ? 33  ASP B OD2 1 
ATOM   2661 N  N   . ASP B 1 34  ? 7.073   -13.055 11.134  1.00 28.23  ? 34  ASP B N   1 
ATOM   2662 C  CA  . ASP B 1 34  ? 6.447   -14.354 11.502  1.00 30.26  ? 34  ASP B CA  1 
ATOM   2663 C  C   . ASP B 1 34  ? 4.918   -14.236 11.510  1.00 29.83  ? 34  ASP B C   1 
ATOM   2664 O  O   . ASP B 1 34  ? 4.281   -15.024 12.225  1.00 33.85  ? 34  ASP B O   1 
ATOM   2665 C  CB  . ASP B 1 34  ? 7.027   -14.879 12.822  1.00 32.66  ? 34  ASP B CB  1 
ATOM   2666 C  CG  . ASP B 1 34  ? 6.756   -13.996 14.029  1.00 34.15  ? 34  ASP B CG  1 
ATOM   2667 O  OD1 . ASP B 1 34  ? 6.427   -12.807 13.837  1.00 32.75  ? 34  ASP B OD1 1 
ATOM   2668 O  OD2 . ASP B 1 34  ? 6.858   -14.509 15.149  1.00 38.33  ? 34  ASP B OD2 1 
ATOM   2669 N  N   . VAL B 1 35  ? 4.332   -13.362 10.690  1.00 26.79  ? 35  VAL B N   1 
ATOM   2670 C  CA  . VAL B 1 35  ? 2.843   -13.273 10.580  1.00 25.85  ? 35  VAL B CA  1 
ATOM   2671 C  C   . VAL B 1 35  ? 2.407   -13.407 9.121   1.00 27.35  ? 35  VAL B C   1 
ATOM   2672 O  O   . VAL B 1 35  ? 3.113   -12.891 8.231   1.00 27.13  ? 35  VAL B O   1 
ATOM   2673 C  CB  . VAL B 1 35  ? 2.326   -11.958 11.172  1.00 26.24  ? 35  VAL B CB  1 
ATOM   2674 C  CG1 . VAL B 1 35  ? 0.825   -11.867 11.062  1.00 25.27  ? 35  VAL B CG1 1 
ATOM   2675 C  CG2 . VAL B 1 35  ? 2.779   -11.763 12.610  1.00 28.33  ? 35  VAL B CG2 1 
ATOM   2676 N  N   . VAL B 1 36  ? 1.255   -14.050 8.911   1.00 28.87  ? 36  VAL B N   1 
ATOM   2677 C  CA  . VAL B 1 36  ? 0.554   -14.098 7.599   1.00 29.96  ? 36  VAL B CA  1 
ATOM   2678 C  C   . VAL B 1 36  ? -0.711  -13.258 7.725   1.00 29.38  ? 36  VAL B C   1 
ATOM   2679 O  O   . VAL B 1 36  ? -1.502  -13.531 8.646   1.00 30.31  ? 36  VAL B O   1 
ATOM   2680 C  CB  . VAL B 1 36  ? 0.260   -15.534 7.142   1.00 29.93  ? 36  VAL B CB  1 
ATOM   2681 C  CG1 . VAL B 1 36  ? -0.523  -15.545 5.845   1.00 30.22  ? 36  VAL B CG1 1 
ATOM   2682 C  CG2 . VAL B 1 36  ? 1.554   -16.323 7.002   1.00 28.78  ? 36  VAL B CG2 1 
ATOM   2683 N  N   . TYR B 1 37  ? -0.851  -12.254 6.853   1.00 27.55  ? 37  TYR B N   1 
ATOM   2684 C  CA  . TYR B 1 37  ? -2.018  -11.346 6.775   1.00 24.44  ? 37  TYR B CA  1 
ATOM   2685 C  C   . TYR B 1 37  ? -2.920  -11.788 5.635   1.00 24.36  ? 37  TYR B C   1 
ATOM   2686 O  O   . TYR B 1 37  ? -2.411  -11.996 4.514   1.00 25.42  ? 37  TYR B O   1 
ATOM   2687 C  CB  . TYR B 1 37  ? -1.565  -9.902  6.553   1.00 23.38  ? 37  TYR B CB  1 
ATOM   2688 C  CG  . TYR B 1 37  ? -0.606  -9.410  7.600   1.00 22.76  ? 37  TYR B CG  1 
ATOM   2689 C  CD1 . TYR B 1 37  ? 0.744   -9.709  7.531   1.00 24.92  ? 37  TYR B CD1 1 
ATOM   2690 C  CD2 . TYR B 1 37  ? -1.047  -8.676  8.689   1.00 23.90  ? 37  TYR B CD2 1 
ATOM   2691 C  CE1 . TYR B 1 37  ? 1.630   -9.284  8.513   1.00 26.75  ? 37  TYR B CE1 1 
ATOM   2692 C  CE2 . TYR B 1 37  ? -0.178  -8.215  9.669   1.00 23.07  ? 37  TYR B CE2 1 
ATOM   2693 C  CZ  . TYR B 1 37  ? 1.168   -8.527  9.585   1.00 26.28  ? 37  TYR B CZ  1 
ATOM   2694 O  OH  . TYR B 1 37  ? 2.027   -8.110  10.558  1.00 27.65  ? 37  TYR B OH  1 
ATOM   2695 N  N   . CYS B 1 38  ? -4.222  -11.885 5.890   1.00 21.79  ? 38  CYS B N   1 
ATOM   2696 C  CA  . CYS B 1 38  ? -5.216  -12.211 4.853   1.00 23.31  ? 38  CYS B CA  1 
ATOM   2697 C  C   . CYS B 1 38  ? -6.555  -11.624 5.263   1.00 24.30  ? 38  CYS B C   1 
ATOM   2698 O  O   . CYS B 1 38  ? -6.736  -11.165 6.386   1.00 23.75  ? 38  CYS B O   1 
ATOM   2699 C  CB  . CYS B 1 38  ? -5.315  -13.714 4.609   1.00 27.67  ? 38  CYS B CB  1 
ATOM   2700 S  SG  . CYS B 1 38  ? -6.110  -14.648 5.952   1.00 28.15  ? 38  CYS B SG  1 
ATOM   2701 N  N   . PRO B 1 39  ? -7.531  -11.581 4.342   1.00 25.00  ? 39  PRO B N   1 
ATOM   2702 C  CA  . PRO B 1 39  ? -8.854  -11.079 4.682   1.00 25.24  ? 39  PRO B CA  1 
ATOM   2703 C  C   . PRO B 1 39  ? -9.530  -12.000 5.712   1.00 27.20  ? 39  PRO B C   1 
ATOM   2704 O  O   . PRO B 1 39  ? -9.419  -13.206 5.588   1.00 27.11  ? 39  PRO B O   1 
ATOM   2705 C  CB  . PRO B 1 39  ? -9.568  -11.111 3.327   1.00 24.00  ? 39  PRO B CB  1 
ATOM   2706 C  CG  . PRO B 1 39  ? -8.450  -11.050 2.330   1.00 24.22  ? 39  PRO B CG  1 
ATOM   2707 C  CD  . PRO B 1 39  ? -7.418  -11.964 2.926   1.00 24.21  ? 39  PRO B CD  1 
ATOM   2708 N  N   . ARG B 1 40  ? -10.201 -11.420 6.703   1.00 27.39  ? 40  ARG B N   1 
ATOM   2709 C  CA  . ARG B 1 40  ? -10.824 -12.211 7.794   1.00 27.60  ? 40  ARG B CA  1 
ATOM   2710 C  C   . ARG B 1 40  ? -11.951 -13.048 7.201   1.00 29.04  ? 40  ARG B C   1 
ATOM   2711 O  O   . ARG B 1 40  ? -12.302 -14.072 7.810   1.00 33.38  ? 40  ARG B O   1 
ATOM   2712 C  CB  . ARG B 1 40  ? -11.348 -11.321 8.921   1.00 29.71  ? 40  ARG B CB  1 
ATOM   2713 C  CG  . ARG B 1 40  ? -12.462 -10.365 8.518   1.00 29.05  ? 40  ARG B CG  1 
ATOM   2714 C  CD  . ARG B 1 40  ? -12.947 -9.649  9.749   1.00 26.90  ? 40  ARG B CD  1 
ATOM   2715 N  NE  . ARG B 1 40  ? -13.998 -8.726  9.410   1.00 26.38  ? 40  ARG B NE  1 
ATOM   2716 C  CZ  . ARG B 1 40  ? -14.719 -8.028  10.275  1.00 26.86  ? 40  ARG B CZ  1 
ATOM   2717 N  NH1 . ARG B 1 40  ? -14.470 -8.090  11.573  1.00 27.82  ? 40  ARG B NH1 1 
ATOM   2718 N  NH2 . ARG B 1 40  ? -15.667 -7.225  9.825   1.00 27.33  ? 40  ARG B NH2 1 
ATOM   2719 N  N   . HIS B 1 41  ? -12.484 -12.672 6.042   1.00 28.26  ? 41  HIS B N   1 
ATOM   2720 C  CA  . HIS B 1 41  ? -13.636 -13.406 5.461   1.00 31.46  ? 41  HIS B CA  1 
ATOM   2721 C  C   . HIS B 1 41  ? -13.240 -14.801 4.967   1.00 28.93  ? 41  HIS B C   1 
ATOM   2722 O  O   . HIS B 1 41  ? -14.162 -15.556 4.646   1.00 31.73  ? 41  HIS B O   1 
ATOM   2723 C  CB  . HIS B 1 41  ? -14.383 -12.581 4.422   1.00 30.61  ? 41  HIS B CB  1 
ATOM   2724 C  CG  . HIS B 1 41  ? -13.712 -12.420 3.101   1.00 32.01  ? 41  HIS B CG  1 
ATOM   2725 N  ND1 . HIS B 1 41  ? -13.355 -13.488 2.301   1.00 35.46  ? 41  HIS B ND1 1 
ATOM   2726 C  CD2 . HIS B 1 41  ? -13.419 -11.305 2.395   1.00 34.26  ? 41  HIS B CD2 1 
ATOM   2727 C  CE1 . HIS B 1 41  ? -12.842 -13.038 1.168   1.00 34.84  ? 41  HIS B CE1 1 
ATOM   2728 N  NE2 . HIS B 1 41  ? -12.879 -11.700 1.196   1.00 34.43  ? 41  HIS B NE2 1 
ATOM   2729 N  N   . VAL B 1 42  ? -11.963 -15.166 4.991   1.00 30.97  ? 42  VAL B N   1 
ATOM   2730 C  CA  . VAL B 1 42  ? -11.492 -16.548 4.680   1.00 31.20  ? 42  VAL B CA  1 
ATOM   2731 C  C   . VAL B 1 42  ? -12.192 -17.547 5.617   1.00 37.66  ? 42  VAL B C   1 
ATOM   2732 O  O   . VAL B 1 42  ? -12.383 -18.712 5.174   1.00 41.22  ? 42  VAL B O   1 
ATOM   2733 C  CB  . VAL B 1 42  ? -9.966  -16.661 4.812   1.00 31.71  ? 42  VAL B CB  1 
ATOM   2734 C  CG1 . VAL B 1 42  ? -9.490  -16.608 6.257   1.00 27.04  ? 42  VAL B CG1 1 
ATOM   2735 C  CG2 . VAL B 1 42  ? -9.434  -17.914 4.120   1.00 34.84  ? 42  VAL B CG2 1 
ATOM   2736 N  N   . ILE B 1 43  ? -12.559 -17.121 6.838   1.00 35.10  ? 43  ILE B N   1 
ATOM   2737 C  CA  . ILE B 1 43  ? -13.149 -18.017 7.884   1.00 39.28  ? 43  ILE B CA  1 
ATOM   2738 C  C   . ILE B 1 43  ? -14.631 -18.260 7.600   1.00 40.30  ? 43  ILE B C   1 
ATOM   2739 O  O   . ILE B 1 43  ? -15.203 -19.072 8.308   1.00 50.07  ? 43  ILE B O   1 
ATOM   2740 C  CB  . ILE B 1 43  ? -12.979 -17.484 9.322   1.00 35.05  ? 43  ILE B CB  1 
ATOM   2741 C  CG1 . ILE B 1 43  ? -13.912 -16.306 9.605   1.00 34.27  ? 43  ILE B CG1 1 
ATOM   2742 C  CG2 . ILE B 1 43  ? -11.522 -17.195 9.622   1.00 35.72  ? 43  ILE B CG2 1 
ATOM   2743 C  CD1 . ILE B 1 43  ? -13.720 -15.684 10.953  1.00 34.67  ? 43  ILE B CD1 1 
ATOM   2744 N  N   . CYS B 1 44  ? -15.232 -17.577 6.631   1.00 42.56  ? 44  CYS B N   1 
ATOM   2745 C  CA  . CYS B 1 44  ? -16.700 -17.583 6.417   1.00 41.40  ? 44  CYS B CA  1 
ATOM   2746 C  C   . CYS B 1 44  ? -17.101 -18.630 5.382   1.00 47.08  ? 44  CYS B C   1 
ATOM   2747 O  O   . CYS B 1 44  ? -16.450 -18.703 4.352   1.00 46.04  ? 44  CYS B O   1 
ATOM   2748 C  CB  . CYS B 1 44  ? -17.183 -16.220 5.958   1.00 39.17  ? 44  CYS B CB  1 
ATOM   2749 S  SG  . CYS B 1 44  ? -17.060 -15.009 7.294   1.00 44.57  ? 44  CYS B SG  1 
ATOM   2750 N  N   . THR B 1 45  ? -18.150 -19.406 5.677   1.00 56.17  ? 45  THR B N   1 
ATOM   2751 C  CA  . THR B 1 45  ? -18.877 -20.224 4.672   1.00 61.13  ? 45  THR B CA  1 
ATOM   2752 C  C   . THR B 1 45  ? -19.733 -19.246 3.867   1.00 65.76  ? 45  THR B C   1 
ATOM   2753 O  O   . THR B 1 45  ? -19.769 -18.055 4.258   1.00 63.55  ? 45  THR B O   1 
ATOM   2754 C  CB  . THR B 1 45  ? -19.714 -21.341 5.316   1.00 56.83  ? 45  THR B CB  1 
ATOM   2755 O  OG1 . THR B 1 45  ? -20.837 -20.740 5.961   1.00 55.02  ? 45  THR B OG1 1 
ATOM   2756 C  CG2 . THR B 1 45  ? -18.934 -22.160 6.321   1.00 55.18  ? 45  THR B CG2 1 
ATOM   2757 N  N   . SER B 1 46  ? -20.375 -19.724 2.797   1.00 74.18  ? 46  SER B N   1 
ATOM   2758 C  CA  . SER B 1 46  ? -21.330 -18.944 1.966   1.00 78.13  ? 46  SER B CA  1 
ATOM   2759 C  C   . SER B 1 46  ? -22.474 -18.449 2.852   1.00 76.24  ? 46  SER B C   1 
ATOM   2760 O  O   . SER B 1 46  ? -22.827 -17.252 2.757   1.00 80.60  ? 46  SER B O   1 
ATOM   2761 C  CB  . SER B 1 46  ? -21.848 -19.760 0.819   1.00 80.94  ? 46  SER B CB  1 
ATOM   2762 O  OG  . SER B 1 46  ? -20.777 -20.192 0.003   1.00 89.78  ? 46  SER B OG  1 
ATOM   2763 N  N   . GLU B 1 47  ? -23.007 -19.344 3.686   1.00 72.19  ? 47  GLU B N   1 
ATOM   2764 C  CA  . GLU B 1 47  ? -24.089 -19.047 4.660   1.00 71.99  ? 47  GLU B CA  1 
ATOM   2765 C  C   . GLU B 1 47  ? -23.647 -17.899 5.581   1.00 65.18  ? 47  GLU B C   1 
ATOM   2766 O  O   . GLU B 1 47  ? -24.397 -16.904 5.721   1.00 56.23  ? 47  GLU B O   1 
ATOM   2767 C  CB  . GLU B 1 47  ? -24.420 -20.307 5.460   1.00 78.75  ? 47  GLU B CB  1 
ATOM   2768 C  CG  . GLU B 1 47  ? -25.127 -21.377 4.649   1.00 87.86  ? 47  GLU B CG  1 
ATOM   2769 C  CD  . GLU B 1 47  ? -25.755 -22.448 5.517   1.00 94.77  ? 47  GLU B CD  1 
ATOM   2770 O  OE1 . GLU B 1 47  ? -25.075 -22.894 6.467   1.00 98.38  ? 47  GLU B OE1 1 
ATOM   2771 O  OE2 . GLU B 1 47  ? -26.925 -22.811 5.263   1.00 101.31 ? 47  GLU B OE2 1 
ATOM   2772 N  N   . ASP B 1 48  ? -22.464 -18.037 6.183   1.00 58.71  ? 48  ASP B N   1 
ATOM   2773 C  CA  . ASP B 1 48  ? -21.885 -17.038 7.120   1.00 58.23  ? 48  ASP B CA  1 
ATOM   2774 C  C   . ASP B 1 48  ? -21.841 -15.660 6.447   1.00 53.90  ? 48  ASP B C   1 
ATOM   2775 O  O   . ASP B 1 48  ? -22.193 -14.675 7.104   1.00 48.72  ? 48  ASP B O   1 
ATOM   2776 C  CB  . ASP B 1 48  ? -20.478 -17.439 7.569   1.00 58.14  ? 48  ASP B CB  1 
ATOM   2777 C  CG  . ASP B 1 48  ? -20.435 -18.668 8.466   1.00 59.86  ? 48  ASP B CG  1 
ATOM   2778 O  OD1 . ASP B 1 48  ? -21.340 -18.803 9.317   1.00 57.29  ? 48  ASP B OD1 1 
ATOM   2779 O  OD2 . ASP B 1 48  ? -19.500 -19.485 8.298   1.00 56.20  ? 48  ASP B OD2 1 
ATOM   2780 N  N   . MET B 1 49  ? -21.447 -15.601 5.170   1.00 55.87  ? 49  MET B N   1 
ATOM   2781 C  CA  . MET B 1 49  ? -21.120 -14.327 4.470   1.00 50.21  ? 49  MET B CA  1 
ATOM   2782 C  C   . MET B 1 49  ? -22.352 -13.419 4.394   1.00 50.06  ? 49  MET B C   1 
ATOM   2783 O  O   . MET B 1 49  ? -22.164 -12.217 4.128   1.00 40.43  ? 49  MET B O   1 
ATOM   2784 C  CB  . MET B 1 49  ? -20.577 -14.561 3.056   1.00 51.42  ? 49  MET B CB  1 
ATOM   2785 C  CG  . MET B 1 49  ? -19.069 -14.808 3.007   1.00 52.22  ? 49  MET B CG  1 
ATOM   2786 S  SD  . MET B 1 49  ? -18.100 -13.466 3.763   1.00 50.88  ? 49  MET B SD  1 
ATOM   2787 C  CE  . MET B 1 49  ? -17.856 -12.394 2.345   1.00 60.43  ? 49  MET B CE  1 
ATOM   2788 N  N   . LEU B 1 50  ? -23.569 -13.934 4.599   1.00 47.40  ? 50  LEU B N   1 
ATOM   2789 C  CA  . LEU B 1 50  ? -24.770 -13.070 4.472   1.00 47.62  ? 50  LEU B CA  1 
ATOM   2790 C  C   . LEU B 1 50  ? -24.832 -12.097 5.655   1.00 43.71  ? 50  LEU B C   1 
ATOM   2791 O  O   . LEU B 1 50  ? -25.313 -10.959 5.475   1.00 43.82  ? 50  LEU B O   1 
ATOM   2792 C  CB  . LEU B 1 50  ? -26.031 -13.934 4.376   1.00 53.51  ? 50  LEU B CB  1 
ATOM   2793 C  CG  . LEU B 1 50  ? -26.365 -14.442 2.976   1.00 59.92  ? 50  LEU B CG  1 
ATOM   2794 C  CD1 . LEU B 1 50  ? -25.304 -15.416 2.483   1.00 60.21  ? 50  LEU B CD1 1 
ATOM   2795 C  CD2 . LEU B 1 50  ? -27.748 -15.093 2.961   1.00 64.05  ? 50  LEU B CD2 1 
ATOM   2796 N  N   . ASN B 1 51  ? -24.378 -12.518 6.827   1.00 45.68  ? 51  ASN B N   1 
ATOM   2797 C  CA  . ASN B 1 51  ? -24.514 -11.726 8.075   1.00 45.71  ? 51  ASN B CA  1 
ATOM   2798 C  C   . ASN B 1 51  ? -23.539 -12.299 9.090   1.00 42.17  ? 51  ASN B C   1 
ATOM   2799 O  O   . ASN B 1 51  ? -23.922 -12.967 10.037  1.00 39.36  ? 51  ASN B O   1 
ATOM   2800 C  CB  . ASN B 1 51  ? -25.963 -11.742 8.568   1.00 51.63  ? 51  ASN B CB  1 
ATOM   2801 C  CG  . ASN B 1 51  ? -26.285 -10.609 9.519   1.00 53.90  ? 51  ASN B CG  1 
ATOM   2802 O  OD1 . ASN B 1 51  ? -26.992 -10.809 10.501  1.00 58.04  ? 51  ASN B OD1 1 
ATOM   2803 N  ND2 . ASN B 1 51  ? -25.786 -9.417  9.232   1.00 54.03  ? 51  ASN B ND2 1 
ATOM   2804 N  N   . PRO B 1 52  ? -22.223 -12.101 8.895   1.00 42.13  ? 52  PRO B N   1 
ATOM   2805 C  CA  . PRO B 1 52  ? -21.228 -12.797 9.711   1.00 37.60  ? 52  PRO B CA  1 
ATOM   2806 C  C   . PRO B 1 52  ? -21.011 -12.143 11.083  1.00 35.53  ? 52  PRO B C   1 
ATOM   2807 O  O   . PRO B 1 52  ? -21.063 -10.918 11.215  1.00 33.32  ? 52  PRO B O   1 
ATOM   2808 C  CB  . PRO B 1 52  ? -19.984 -12.728 8.821   1.00 41.64  ? 52  PRO B CB  1 
ATOM   2809 C  CG  . PRO B 1 52  ? -20.138 -11.404 8.085   1.00 42.86  ? 52  PRO B CG  1 
ATOM   2810 C  CD  . PRO B 1 52  ? -21.628 -11.248 7.856   1.00 42.29  ? 52  PRO B CD  1 
ATOM   2811 N  N   . ASN B 1 53  ? -20.793 -12.971 12.100  1.00 35.51  ? 53  ASN B N   1 
ATOM   2812 C  CA  . ASN B 1 53  ? -20.349 -12.503 13.435  1.00 39.30  ? 53  ASN B CA  1 
ATOM   2813 C  C   . ASN B 1 53  ? -18.912 -12.995 13.578  1.00 42.23  ? 53  ASN B C   1 
ATOM   2814 O  O   . ASN B 1 53  ? -18.709 -14.202 13.912  1.00 38.73  ? 53  ASN B O   1 
ATOM   2815 C  CB  . ASN B 1 53  ? -21.283 -12.954 14.568  1.00 43.66  ? 53  ASN B CB  1 
ATOM   2816 C  CG  . ASN B 1 53  ? -20.883 -12.385 15.918  1.00 46.98  ? 53  ASN B CG  1 
ATOM   2817 O  OD1 . ASN B 1 53  ? -19.816 -11.768 16.075  1.00 43.40  ? 53  ASN B OD1 1 
ATOM   2818 N  ND2 . ASN B 1 53  ? -21.732 -12.596 16.911  1.00 47.80  ? 53  ASN B ND2 1 
ATOM   2819 N  N   . TYR B 1 54  ? -17.949 -12.140 13.216  1.00 40.91  ? 54  TYR B N   1 
ATOM   2820 C  CA  . TYR B 1 54  ? -16.538 -12.572 13.035  1.00 41.57  ? 54  TYR B CA  1 
ATOM   2821 C  C   . TYR B 1 54  ? -15.948 -12.873 14.414  1.00 41.30  ? 54  TYR B C   1 
ATOM   2822 O  O   . TYR B 1 54  ? -15.197 -13.862 14.502  1.00 43.39  ? 54  TYR B O   1 
ATOM   2823 C  CB  . TYR B 1 54  ? -15.709 -11.542 12.263  1.00 38.65  ? 54  TYR B CB  1 
ATOM   2824 C  CG  . TYR B 1 54  ? -15.977 -11.457 10.777  1.00 32.20  ? 54  TYR B CG  1 
ATOM   2825 C  CD1 . TYR B 1 54  ? -15.381 -12.332 9.889   1.00 31.97  ? 54  TYR B CD1 1 
ATOM   2826 C  CD2 . TYR B 1 54  ? -16.821 -10.490 10.255  1.00 30.71  ? 54  TYR B CD2 1 
ATOM   2827 C  CE1 . TYR B 1 54  ? -15.626 -12.264 8.526   1.00 29.99  ? 54  TYR B CE1 1 
ATOM   2828 C  CE2 . TYR B 1 54  ? -17.064 -10.395 8.896   1.00 29.41  ? 54  TYR B CE2 1 
ATOM   2829 C  CZ  . TYR B 1 54  ? -16.465 -11.287 8.022   1.00 30.44  ? 54  TYR B CZ  1 
ATOM   2830 O  OH  . TYR B 1 54  ? -16.668 -11.176 6.667   1.00 29.19  ? 54  TYR B OH  1 
ATOM   2831 N  N   . GLU B 1 55  ? -16.312 -12.060 15.419  1.00 48.94  ? 55  GLU B N   1 
ATOM   2832 C  CA  . GLU B 1 55  ? -16.034 -12.296 16.866  1.00 52.49  ? 55  GLU B CA  1 
ATOM   2833 C  C   . GLU B 1 55  ? -16.240 -13.781 17.141  1.00 52.68  ? 55  GLU B C   1 
ATOM   2834 O  O   . GLU B 1 55  ? -15.237 -14.468 17.472  1.00 48.08  ? 55  GLU B O   1 
ATOM   2835 C  CB  . GLU B 1 55  ? -16.984 -11.522 17.793  1.00 57.56  ? 55  GLU B CB  1 
ATOM   2836 C  CG  . GLU B 1 55  ? -16.942 -10.010 17.634  1.00 61.23  ? 55  GLU B CG  1 
ATOM   2837 C  CD  . GLU B 1 55  ? -17.326 -9.250  18.889  1.00 59.92  ? 55  GLU B CD  1 
ATOM   2838 O  OE1 . GLU B 1 55  ? -18.529 -9.267  19.245  1.00 60.33  ? 55  GLU B OE1 1 
ATOM   2839 O  OE2 . GLU B 1 55  ? -16.415 -8.674  19.525  1.00 53.45  ? 55  GLU B OE2 1 
ATOM   2840 N  N   . ASP B 1 56  ? -17.485 -14.228 16.899  1.00 50.14  ? 56  ASP B N   1 
ATOM   2841 C  CA  . ASP B 1 56  ? -18.020 -15.569 17.232  1.00 48.72  ? 56  ASP B CA  1 
ATOM   2842 C  C   . ASP B 1 56  ? -17.400 -16.611 16.304  1.00 47.47  ? 56  ASP B C   1 
ATOM   2843 O  O   . ASP B 1 56  ? -16.921 -17.634 16.816  1.00 50.62  ? 56  ASP B O   1 
ATOM   2844 C  CB  . ASP B 1 56  ? -19.549 -15.612 17.155  1.00 49.46  ? 56  ASP B CB  1 
ATOM   2845 C  CG  . ASP B 1 56  ? -20.109 -16.844 17.847  1.00 50.53  ? 56  ASP B CG  1 
ATOM   2846 O  OD1 . ASP B 1 56  ? -19.766 -17.042 19.028  1.00 53.46  ? 56  ASP B OD1 1 
ATOM   2847 O  OD2 . ASP B 1 56  ? -20.822 -17.625 17.194  1.00 46.34  ? 56  ASP B OD2 1 
ATOM   2848 N  N   . LEU B 1 57  ? -17.415 -16.390 14.989  1.00 47.49  ? 57  LEU B N   1 
ATOM   2849 C  CA  . LEU B 1 57  ? -16.880 -17.388 14.025  1.00 49.10  ? 57  LEU B CA  1 
ATOM   2850 C  C   . LEU B 1 57  ? -15.402 -17.651 14.329  1.00 52.91  ? 57  LEU B C   1 
ATOM   2851 O  O   . LEU B 1 57  ? -14.931 -18.779 14.056  1.00 49.57  ? 57  LEU B O   1 
ATOM   2852 C  CB  . LEU B 1 57  ? -17.061 -16.894 12.584  1.00 55.05  ? 57  LEU B CB  1 
ATOM   2853 C  CG  . LEU B 1 57  ? -18.509 -16.780 12.107  1.00 56.10  ? 57  LEU B CG  1 
ATOM   2854 C  CD1 . LEU B 1 57  ? -18.606 -16.002 10.806  1.00 54.82  ? 57  LEU B CD1 1 
ATOM   2855 C  CD2 . LEU B 1 57  ? -19.132 -18.162 11.961  1.00 57.53  ? 57  LEU B CD2 1 
ATOM   2856 N  N   . LEU B 1 58  ? -14.687 -16.646 14.839  1.00 54.24  ? 58  LEU B N   1 
ATOM   2857 C  CA  . LEU B 1 58  ? -13.213 -16.719 15.001  1.00 59.17  ? 58  LEU B CA  1 
ATOM   2858 C  C   . LEU B 1 58  ? -12.851 -17.515 16.265  1.00 65.15  ? 58  LEU B C   1 
ATOM   2859 O  O   . LEU B 1 58  ? -11.969 -18.402 16.180  1.00 58.13  ? 58  LEU B O   1 
ATOM   2860 C  CB  . LEU B 1 58  ? -12.638 -15.302 15.060  1.00 55.61  ? 58  LEU B CB  1 
ATOM   2861 C  CG  . LEU B 1 58  ? -11.129 -15.240 15.277  1.00 55.13  ? 58  LEU B CG  1 
ATOM   2862 C  CD1 . LEU B 1 58  ? -10.387 -15.863 14.105  1.00 51.90  ? 58  LEU B CD1 1 
ATOM   2863 C  CD2 . LEU B 1 58  ? -10.677 -13.806 15.522  1.00 57.72  ? 58  LEU B CD2 1 
ATOM   2864 N  N   . ILE B 1 59  ? -13.470 -17.196 17.407  1.00 75.13  ? 59  ILE B N   1 
ATOM   2865 C  CA  . ILE B 1 59  ? -13.185 -17.899 18.697  1.00 79.16  ? 59  ILE B CA  1 
ATOM   2866 C  C   . ILE B 1 59  ? -13.413 -19.399 18.469  1.00 75.37  ? 59  ILE B C   1 
ATOM   2867 O  O   . ILE B 1 59  ? -12.608 -20.192 18.967  1.00 77.24  ? 59  ILE B O   1 
ATOM   2868 C  CB  . ILE B 1 59  ? -14.006 -17.350 19.890  1.00 76.35  ? 59  ILE B CB  1 
ATOM   2869 C  CG1 . ILE B 1 59  ? -15.515 -17.477 19.671  1.00 80.05  ? 59  ILE B CG1 1 
ATOM   2870 C  CG2 . ILE B 1 59  ? -13.611 -15.917 20.217  1.00 72.21  ? 59  ILE B CG2 1 
ATOM   2871 C  CD1 . ILE B 1 59  ? -16.233 -18.197 20.784  1.00 81.74  ? 59  ILE B CD1 1 
ATOM   2872 N  N   . ARG B 1 60  ? -14.423 -19.758 17.673  1.00 77.02  ? 60  ARG B N   1 
ATOM   2873 C  CA  . ARG B 1 60  ? -14.763 -21.165 17.335  1.00 81.77  ? 60  ARG B CA  1 
ATOM   2874 C  C   . ARG B 1 60  ? -13.609 -21.856 16.607  1.00 76.16  ? 60  ARG B C   1 
ATOM   2875 O  O   . ARG B 1 60  ? -13.533 -23.082 16.700  1.00 77.60  ? 60  ARG B O   1 
ATOM   2876 C  CB  . ARG B 1 60  ? -15.982 -21.234 16.416  1.00 92.40  ? 60  ARG B CB  1 
ATOM   2877 C  CG  . ARG B 1 60  ? -17.297 -20.841 17.071  1.00 98.69  ? 60  ARG B CG  1 
ATOM   2878 C  CD  . ARG B 1 60  ? -18.384 -20.926 16.024  1.00 106.85 ? 60  ARG B CD  1 
ATOM   2879 N  NE  . ARG B 1 60  ? -19.716 -20.727 16.563  1.00 117.20 ? 60  ARG B NE  1 
ATOM   2880 C  CZ  . ARG B 1 60  ? -20.815 -20.649 15.819  1.00 124.78 ? 60  ARG B CZ  1 
ATOM   2881 N  NH1 . ARG B 1 60  ? -20.731 -20.748 14.499  1.00 121.66 ? 60  ARG B NH1 1 
ATOM   2882 N  NH2 . ARG B 1 60  ? -21.992 -20.468 16.398  1.00 123.82 ? 60  ARG B NH2 1 
ATOM   2883 N  N   . LYS B 1 61  ? -12.795 -21.112 15.853  1.00 79.41  ? 61  LYS B N   1 
ATOM   2884 C  CA  . LYS B 1 61  ? -11.669 -21.680 15.061  1.00 76.88  ? 61  LYS B CA  1 
ATOM   2885 C  C   . LYS B 1 61  ? -10.452 -21.878 15.965  1.00 69.39  ? 61  LYS B C   1 
ATOM   2886 O  O   . LYS B 1 61  ? -10.420 -21.308 17.077  1.00 71.93  ? 61  LYS B O   1 
ATOM   2887 C  CB  . LYS B 1 61  ? -11.267 -20.767 13.897  1.00 77.35  ? 61  LYS B CB  1 
ATOM   2888 C  CG  . LYS B 1 61  ? -12.373 -20.444 12.906  1.00 71.49  ? 61  LYS B CG  1 
ATOM   2889 C  CD  . LYS B 1 61  ? -12.493 -21.438 11.788  1.00 69.89  ? 61  LYS B CD  1 
ATOM   2890 C  CE  . LYS B 1 61  ? -13.830 -21.324 11.088  1.00 72.07  ? 61  LYS B CE  1 
ATOM   2891 N  NZ  . LYS B 1 61  ? -14.087 -22.490 10.212  1.00 73.03  ? 61  LYS B NZ  1 
ATOM   2892 N  N   . SER B 1 62  ? -9.476  -22.631 15.466  1.00 64.04  ? 62  SER B N   1 
ATOM   2893 C  CA  . SER B 1 62  ? -8.156  -22.832 16.109  1.00 69.16  ? 62  SER B CA  1 
ATOM   2894 C  C   . SER B 1 62  ? -7.066  -22.964 15.046  1.00 60.00  ? 62  SER B C   1 
ATOM   2895 O  O   . SER B 1 62  ? -7.370  -23.309 13.897  1.00 59.43  ? 62  SER B O   1 
ATOM   2896 C  CB  . SER B 1 62  ? -8.181  -24.024 17.005  1.00 77.04  ? 62  SER B CB  1 
ATOM   2897 O  OG  . SER B 1 62  ? -8.695  -25.135 16.297  1.00 91.15  ? 62  SER B OG  1 
ATOM   2898 N  N   . ASN B 1 63  ? -5.827  -22.726 15.459  1.00 58.13  ? 63  ASN B N   1 
ATOM   2899 C  CA  . ASN B 1 63  ? -4.632  -22.637 14.584  1.00 58.93  ? 63  ASN B CA  1 
ATOM   2900 C  C   . ASN B 1 63  ? -4.667  -23.704 13.487  1.00 65.04  ? 63  ASN B C   1 
ATOM   2901 O  O   . ASN B 1 63  ? -4.450  -23.347 12.311  1.00 67.56  ? 63  ASN B O   1 
ATOM   2902 C  CB  . ASN B 1 63  ? -3.363  -22.746 15.419  1.00 51.03  ? 63  ASN B CB  1 
ATOM   2903 C  CG  . ASN B 1 63  ? -3.237  -21.585 16.374  1.00 52.33  ? 63  ASN B CG  1 
ATOM   2904 O  OD1 . ASN B 1 63  ? -3.945  -20.588 16.235  1.00 48.98  ? 63  ASN B OD1 1 
ATOM   2905 N  ND2 . ASN B 1 63  ? -2.339  -21.700 17.337  1.00 54.01  ? 63  ASN B ND2 1 
ATOM   2906 N  N   . HIS B 1 64  ? -4.919  -24.957 13.875  1.00 71.19  ? 64  HIS B N   1 
ATOM   2907 C  CA  . HIS B 1 64  ? -4.968  -26.160 13.000  1.00 70.43  ? 64  HIS B CA  1 
ATOM   2908 C  C   . HIS B 1 64  ? -6.054  -26.014 11.912  1.00 65.69  ? 64  HIS B C   1 
ATOM   2909 O  O   . HIS B 1 64  ? -5.945  -26.715 10.897  1.00 65.61  ? 64  HIS B O   1 
ATOM   2910 C  CB  . HIS B 1 64  ? -5.128  -27.415 13.877  1.00 82.53  ? 64  HIS B CB  1 
ATOM   2911 C  CG  . HIS B 1 64  ? -6.109  -27.269 15.001  1.00 91.40  ? 64  HIS B CG  1 
ATOM   2912 N  ND1 . HIS B 1 64  ? -5.707  -27.119 16.323  1.00 90.43  ? 64  HIS B ND1 1 
ATOM   2913 C  CD2 . HIS B 1 64  ? -7.463  -27.236 15.014  1.00 92.58  ? 64  HIS B CD2 1 
ATOM   2914 C  CE1 . HIS B 1 64  ? -6.771  -27.005 17.095  1.00 88.44  ? 64  HIS B CE1 1 
ATOM   2915 N  NE2 . HIS B 1 64  ? -7.858  -27.077 16.318  1.00 90.53  ? 64  HIS B NE2 1 
ATOM   2916 N  N   . ASN B 1 65  ? -7.041  -25.121 12.077  1.00 57.54  ? 65  ASN B N   1 
ATOM   2917 C  CA  . ASN B 1 65  ? -8.085  -24.846 11.047  1.00 59.20  ? 65  ASN B CA  1 
ATOM   2918 C  C   . ASN B 1 65  ? -7.530  -24.039 9.865   1.00 55.93  ? 65  ASN B C   1 
ATOM   2919 O  O   . ASN B 1 65  ? -8.247  -23.935 8.866   1.00 59.25  ? 65  ASN B O   1 
ATOM   2920 C  CB  . ASN B 1 65  ? -9.265  -24.046 11.598  1.00 61.41  ? 65  ASN B CB  1 
ATOM   2921 C  CG  . ASN B 1 65  ? -10.018 -24.791 12.675  1.00 65.13  ? 65  ASN B CG  1 
ATOM   2922 O  OD1 . ASN B 1 65  ? -10.117 -24.331 13.817  1.00 67.54  ? 65  ASN B OD1 1 
ATOM   2923 N  ND2 . ASN B 1 65  ? -10.538 -25.948 12.309  1.00 65.61  ? 65  ASN B ND2 1 
ATOM   2924 N  N   . PHE B 1 66  ? -6.341  -23.447 9.981   1.00 48.97  ? 66  PHE B N   1 
ATOM   2925 C  CA  . PHE B 1 66  ? -5.733  -22.603 8.922   1.00 48.20  ? 66  PHE B CA  1 
ATOM   2926 C  C   . PHE B 1 66  ? -4.521  -23.336 8.337   1.00 42.36  ? 66  PHE B C   1 
ATOM   2927 O  O   . PHE B 1 66  ? -3.570  -23.596 9.082   1.00 42.47  ? 66  PHE B O   1 
ATOM   2928 C  CB  . PHE B 1 66  ? -5.347  -21.225 9.477   1.00 46.62  ? 66  PHE B CB  1 
ATOM   2929 C  CG  . PHE B 1 66  ? -6.464  -20.435 10.113  1.00 42.21  ? 66  PHE B CG  1 
ATOM   2930 C  CD1 . PHE B 1 66  ? -7.345  -19.696 9.345   1.00 41.25  ? 66  PHE B CD1 1 
ATOM   2931 C  CD2 . PHE B 1 66  ? -6.622  -20.416 11.490  1.00 42.77  ? 66  PHE B CD2 1 
ATOM   2932 C  CE1 . PHE B 1 66  ? -8.369  -18.973 9.937   1.00 40.69  ? 66  PHE B CE1 1 
ATOM   2933 C  CE2 . PHE B 1 66  ? -7.635  -19.681 12.084  1.00 40.26  ? 66  PHE B CE2 1 
ATOM   2934 C  CZ  . PHE B 1 66  ? -8.506  -18.958 11.305  1.00 41.79  ? 66  PHE B CZ  1 
ATOM   2935 N  N   . LEU B 1 67  ? -4.569  -23.655 7.041   1.00 40.41  ? 67  LEU B N   1 
ATOM   2936 C  CA  . LEU B 1 67  ? -3.447  -24.242 6.267   1.00 43.11  ? 67  LEU B CA  1 
ATOM   2937 C  C   . LEU B 1 67  ? -2.742  -23.144 5.460   1.00 45.98  ? 67  LEU B C   1 
ATOM   2938 O  O   . LEU B 1 67  ? -3.372  -22.537 4.553   1.00 41.04  ? 67  LEU B O   1 
ATOM   2939 C  CB  . LEU B 1 67  ? -3.991  -25.319 5.328   1.00 46.61  ? 67  LEU B CB  1 
ATOM   2940 C  CG  . LEU B 1 67  ? -4.724  -26.448 6.039   1.00 54.23  ? 67  LEU B CG  1 
ATOM   2941 C  CD1 . LEU B 1 67  ? -6.074  -26.743 5.390   1.00 51.46  ? 67  LEU B CD1 1 
ATOM   2942 C  CD2 . LEU B 1 67  ? -3.830  -27.681 6.093   1.00 57.30  ? 67  LEU B CD2 1 
ATOM   2943 N  N   . VAL B 1 68  ? -1.467  -22.939 5.762   1.00 40.37  ? 68  VAL B N   1 
ATOM   2944 C  CA  . VAL B 1 68  ? -0.614  -21.899 5.139   1.00 40.35  ? 68  VAL B CA  1 
ATOM   2945 C  C   . VAL B 1 68  ? 0.503   -22.610 4.384   1.00 39.06  ? 68  VAL B C   1 
ATOM   2946 O  O   . VAL B 1 68  ? 1.271   -23.338 5.013   1.00 39.83  ? 68  VAL B O   1 
ATOM   2947 C  CB  . VAL B 1 68  ? -0.061  -20.912 6.180   1.00 40.60  ? 68  VAL B CB  1 
ATOM   2948 C  CG1 . VAL B 1 68  ? 0.724   -19.785 5.517   1.00 44.60  ? 68  VAL B CG1 1 
ATOM   2949 C  CG2 . VAL B 1 68  ? -1.155  -20.355 7.070   1.00 42.01  ? 68  VAL B CG2 1 
ATOM   2950 N  N   . GLN B 1 69  ? 0.574   -22.375 3.076   1.00 39.50  ? 69  GLN B N   1 
ATOM   2951 C  CA  . GLN B 1 69  ? 1.558   -23.009 2.169   1.00 41.40  ? 69  GLN B CA  1 
ATOM   2952 C  C   . GLN B 1 69  ? 2.407   -21.898 1.529   1.00 37.16  ? 69  GLN B C   1 
ATOM   2953 O  O   . GLN B 1 69  ? 1.849   -21.039 0.863   1.00 31.25  ? 69  GLN B O   1 
ATOM   2954 C  CB  . GLN B 1 69  ? 0.799   -23.895 1.182   1.00 45.06  ? 69  GLN B CB  1 
ATOM   2955 C  CG  . GLN B 1 69  ? 1.333   -25.325 1.115   1.00 55.90  ? 69  GLN B CG  1 
ATOM   2956 C  CD  . GLN B 1 69  ? 0.459   -26.272 0.315   1.00 60.57  ? 69  GLN B CD  1 
ATOM   2957 O  OE1 . GLN B 1 69  ? -0.772  -26.236 0.373   1.00 61.72  ? 69  GLN B OE1 1 
ATOM   2958 N  NE2 . GLN B 1 69  ? 1.099   -27.134 -0.460  1.00 67.10  ? 69  GLN B NE2 1 
ATOM   2959 N  N   . ALA B 1 70  ? 3.710   -21.889 1.797   1.00 36.47  ? 70  ALA B N   1 
ATOM   2960 C  CA  . ALA B 1 70  ? 4.712   -21.044 1.123   1.00 40.39  ? 70  ALA B CA  1 
ATOM   2961 C  C   . ALA B 1 70  ? 5.352   -21.889 0.018   1.00 48.35  ? 70  ALA B C   1 
ATOM   2962 O  O   . ALA B 1 70  ? 6.348   -22.602 0.299   1.00 49.61  ? 70  ALA B O   1 
ATOM   2963 C  CB  . ALA B 1 70  ? 5.719   -20.531 2.127   1.00 39.75  ? 70  ALA B CB  1 
ATOM   2964 N  N   . GLY B 1 71  ? 4.762   -21.848 -1.182  1.00 59.48  ? 71  GLY B N   1 
ATOM   2965 C  CA  . GLY B 1 71  ? 5.026   -22.794 -2.286  1.00 58.39  ? 71  GLY B CA  1 
ATOM   2966 C  C   . GLY B 1 71  ? 4.626   -24.208 -1.895  1.00 61.04  ? 71  GLY B C   1 
ATOM   2967 O  O   . GLY B 1 71  ? 3.442   -24.417 -1.564  1.00 61.17  ? 71  GLY B O   1 
ATOM   2968 N  N   . ASN B 1 72  ? 5.594   -25.132 -1.870  1.00 69.80  ? 72  ASN B N   1 
ATOM   2969 C  CA  . ASN B 1 72  ? 5.409   -26.576 -1.538  1.00 76.08  ? 72  ASN B CA  1 
ATOM   2970 C  C   . ASN B 1 72  ? 5.901   -26.849 -0.103  1.00 72.02  ? 72  ASN B C   1 
ATOM   2971 O  O   . ASN B 1 72  ? 6.287   -27.990 0.184   1.00 78.63  ? 72  ASN B O   1 
ATOM   2972 C  CB  . ASN B 1 72  ? 6.138   -27.459 -2.563  1.00 87.10  ? 72  ASN B CB  1 
ATOM   2973 C  CG  . ASN B 1 72  ? 5.267   -28.526 -3.207  1.00 94.62  ? 72  ASN B CG  1 
ATOM   2974 O  OD1 . ASN B 1 72  ? 4.158   -28.248 -3.662  1.00 95.33  ? 72  ASN B OD1 1 
ATOM   2975 N  ND2 . ASN B 1 72  ? 5.772   -29.748 -3.292  1.00 98.85  ? 72  ASN B ND2 1 
ATOM   2976 N  N   . VAL B 1 73  ? 5.895   -25.832 0.762   1.00 68.77  ? 73  VAL B N   1 
ATOM   2977 C  CA  . VAL B 1 73  ? 6.271   -25.913 2.204   1.00 64.51  ? 73  VAL B CA  1 
ATOM   2978 C  C   . VAL B 1 73  ? 5.033   -25.554 3.024   1.00 63.55  ? 73  VAL B C   1 
ATOM   2979 O  O   . VAL B 1 73  ? 4.423   -24.512 2.732   1.00 63.47  ? 73  VAL B O   1 
ATOM   2980 C  CB  . VAL B 1 73  ? 7.424   -24.950 2.549   1.00 61.27  ? 73  VAL B CB  1 
ATOM   2981 C  CG1 . VAL B 1 73  ? 7.737   -24.951 4.037   1.00 57.13  ? 73  VAL B CG1 1 
ATOM   2982 C  CG2 . VAL B 1 73  ? 8.666   -25.236 1.726   1.00 59.67  ? 73  VAL B CG2 1 
ATOM   2983 N  N   . GLN B 1 74  ? 4.698   -26.367 4.022   1.00 62.22  ? 74  GLN B N   1 
ATOM   2984 C  CA  . GLN B 1 74  ? 3.652   -26.046 5.023   1.00 61.11  ? 74  GLN B CA  1 
ATOM   2985 C  C   . GLN B 1 74  ? 4.302   -25.146 6.068   1.00 62.47  ? 74  GLN B C   1 
ATOM   2986 O  O   . GLN B 1 74  ? 5.451   -25.431 6.468   1.00 62.25  ? 74  GLN B O   1 
ATOM   2987 C  CB  . GLN B 1 74  ? 3.081   -27.304 5.674   1.00 69.58  ? 74  GLN B CB  1 
ATOM   2988 C  CG  . GLN B 1 74  ? 2.299   -28.185 4.712   1.00 78.49  ? 74  GLN B CG  1 
ATOM   2989 C  CD  . GLN B 1 74  ? 0.995   -27.562 4.277   1.00 88.74  ? 74  GLN B CD  1 
ATOM   2990 O  OE1 . GLN B 1 74  ? 0.591   -27.687 3.124   1.00 98.37  ? 74  GLN B OE1 1 
ATOM   2991 N  NE2 . GLN B 1 74  ? 0.321   -26.891 5.201   1.00 93.59  ? 74  GLN B NE2 1 
ATOM   2992 N  N   . LEU B 1 75  ? 3.620   -24.062 6.423   1.00 57.91  ? 75  LEU B N   1 
ATOM   2993 C  CA  . LEU B 1 75  ? 3.947   -23.227 7.599   1.00 54.55  ? 75  LEU B CA  1 
ATOM   2994 C  C   . LEU B 1 75  ? 3.079   -23.718 8.760   1.00 56.01  ? 75  LEU B C   1 
ATOM   2995 O  O   . LEU B 1 75  ? 1.916   -24.069 8.506   1.00 53.90  ? 75  LEU B O   1 
ATOM   2996 C  CB  . LEU B 1 75  ? 3.666   -21.755 7.276   1.00 55.93  ? 75  LEU B CB  1 
ATOM   2997 C  CG  . LEU B 1 75  ? 4.585   -21.105 6.245   1.00 53.35  ? 75  LEU B CG  1 
ATOM   2998 C  CD1 . LEU B 1 75  ? 4.304   -19.616 6.138   1.00 52.02  ? 75  LEU B CD1 1 
ATOM   2999 C  CD2 . LEU B 1 75  ? 6.046   -21.325 6.597   1.00 53.88  ? 75  LEU B CD2 1 
ATOM   3000 N  N   . ARG B 1 76  ? 3.647   -23.763 9.966   1.00 54.68  ? 76  ARG B N   1 
ATOM   3001 C  CA  . ARG B 1 76  ? 2.919   -24.059 11.223  1.00 54.78  ? 76  ARG B CA  1 
ATOM   3002 C  C   . ARG B 1 76  ? 2.346   -22.743 11.758  1.00 47.44  ? 76  ARG B C   1 
ATOM   3003 O  O   . ARG B 1 76  ? 3.149   -21.830 12.104  1.00 40.27  ? 76  ARG B O   1 
ATOM   3004 C  CB  . ARG B 1 76  ? 3.852   -24.725 12.243  1.00 63.29  ? 76  ARG B CB  1 
ATOM   3005 C  CG  . ARG B 1 76  ? 3.135   -25.308 13.457  1.00 72.41  ? 76  ARG B CG  1 
ATOM   3006 C  CD  . ARG B 1 76  ? 4.057   -26.114 14.358  1.00 81.77  ? 76  ARG B CD  1 
ATOM   3007 N  NE  . ARG B 1 76  ? 4.589   -27.287 13.664  1.00 87.69  ? 76  ARG B NE  1 
ATOM   3008 C  CZ  . ARG B 1 76  ? 4.071   -28.521 13.696  1.00 91.77  ? 76  ARG B CZ  1 
ATOM   3009 N  NH1 . ARG B 1 76  ? 2.988   -28.793 14.407  1.00 92.78  ? 76  ARG B NH1 1 
ATOM   3010 N  NH2 . ARG B 1 76  ? 4.651   -29.493 13.011  1.00 88.03  ? 76  ARG B NH2 1 
ATOM   3011 N  N   . VAL B 1 77  ? 1.019   -22.649 11.803  1.00 42.97  ? 77  VAL B N   1 
ATOM   3012 C  CA  . VAL B 1 77  ? 0.279   -21.541 12.470  1.00 44.01  ? 77  VAL B CA  1 
ATOM   3013 C  C   . VAL B 1 77  ? 0.228   -21.863 13.962  1.00 44.64  ? 77  VAL B C   1 
ATOM   3014 O  O   . VAL B 1 77  ? -0.305  -22.935 14.301  1.00 47.05  ? 77  VAL B O   1 
ATOM   3015 C  CB  . VAL B 1 77  ? -1.141  -21.368 11.903  1.00 42.96  ? 77  VAL B CB  1 
ATOM   3016 C  CG1 . VAL B 1 77  ? -1.892  -20.249 12.593  1.00 43.58  ? 77  VAL B CG1 1 
ATOM   3017 C  CG2 . VAL B 1 77  ? -1.135  -21.162 10.398  1.00 46.86  ? 77  VAL B CG2 1 
ATOM   3018 N  N   . ILE B 1 78  ? 0.752   -20.962 14.795  1.00 38.78  ? 78  ILE B N   1 
ATOM   3019 C  CA  . ILE B 1 78  ? 0.861   -21.116 16.275  1.00 38.33  ? 78  ILE B CA  1 
ATOM   3020 C  C   . ILE B 1 78  ? 0.068   -20.015 16.981  1.00 39.14  ? 78  ILE B C   1 
ATOM   3021 O  O   . ILE B 1 78  ? 0.135   -19.940 18.221  1.00 42.61  ? 78  ILE B O   1 
ATOM   3022 C  CB  . ILE B 1 78  ? 2.341   -21.086 16.707  1.00 39.16  ? 78  ILE B CB  1 
ATOM   3023 C  CG1 . ILE B 1 78  ? 2.984   -19.724 16.445  1.00 38.94  ? 78  ILE B CG1 1 
ATOM   3024 C  CG2 . ILE B 1 78  ? 3.131   -22.198 16.038  1.00 40.28  ? 78  ILE B CG2 1 
ATOM   3025 C  CD1 . ILE B 1 78  ? 4.369   -19.579 17.063  1.00 39.53  ? 78  ILE B CD1 1 
ATOM   3026 N  N   . GLY B 1 79  ? -0.648  -19.174 16.239  1.00 38.52  ? 79  GLY B N   1 
ATOM   3027 C  CA  . GLY B 1 79  ? -1.494  -18.114 16.817  1.00 38.81  ? 79  GLY B CA  1 
ATOM   3028 C  C   . GLY B 1 79  ? -2.385  -17.507 15.751  1.00 41.29  ? 79  GLY B C   1 
ATOM   3029 O  O   . GLY B 1 79  ? -2.011  -17.583 14.550  1.00 37.04  ? 79  GLY B O   1 
ATOM   3030 N  N   . HIS B 1 80  ? -3.532  -16.958 16.155  1.00 38.40  ? 80  HIS B N   1 
ATOM   3031 C  CA  . HIS B 1 80  ? -4.489  -16.295 15.238  1.00 41.00  ? 80  HIS B CA  1 
ATOM   3032 C  C   . HIS B 1 80  ? -5.186  -15.171 15.986  1.00 40.63  ? 80  HIS B C   1 
ATOM   3033 O  O   . HIS B 1 80  ? -5.702  -15.407 17.087  1.00 39.09  ? 80  HIS B O   1 
ATOM   3034 C  CB  . HIS B 1 80  ? -5.461  -17.287 14.605  1.00 44.65  ? 80  HIS B CB  1 
ATOM   3035 C  CG  . HIS B 1 80  ? -6.416  -17.890 15.572  1.00 50.77  ? 80  HIS B CG  1 
ATOM   3036 N  ND1 . HIS B 1 80  ? -6.064  -18.934 16.409  1.00 52.02  ? 80  HIS B ND1 1 
ATOM   3037 C  CD2 . HIS B 1 80  ? -7.704  -17.597 15.847  1.00 56.81  ? 80  HIS B CD2 1 
ATOM   3038 C  CE1 . HIS B 1 80  ? -7.103  -19.259 17.159  1.00 55.31  ? 80  HIS B CE1 1 
ATOM   3039 N  NE2 . HIS B 1 80  ? -8.121  -18.449 16.839  1.00 57.88  ? 80  HIS B NE2 1 
ATOM   3040 N  N   . SER B 1 81  ? -5.153  -13.978 15.414  1.00 34.62  ? 81  SER B N   1 
ATOM   3041 C  CA  . SER B 1 81  ? -5.893  -12.802 15.910  1.00 31.71  ? 81  SER B CA  1 
ATOM   3042 C  C   . SER B 1 81  ? -6.484  -12.084 14.709  1.00 36.58  ? 81  SER B C   1 
ATOM   3043 O  O   . SER B 1 81  ? -6.056  -12.363 13.564  1.00 34.63  ? 81  SER B O   1 
ATOM   3044 C  CB  . SER B 1 81  ? -5.005  -11.869 16.670  1.00 34.27  ? 81  SER B CB  1 
ATOM   3045 O  OG  . SER B 1 81  ? -3.839  -11.596 15.921  1.00 36.33  ? 81  SER B OG  1 
ATOM   3046 N  N   . MET B 1 82  ? -7.387  -11.149 14.990  1.00 37.35  ? 82  MET B N   1 
ATOM   3047 C  CA  . MET B 1 82  ? -8.054  -10.315 13.976  1.00 37.86  ? 82  MET B CA  1 
ATOM   3048 C  C   . MET B 1 82  ? -7.792  -8.842  14.306  1.00 35.09  ? 82  MET B C   1 
ATOM   3049 O  O   . MET B 1 82  ? -7.854  -8.439  15.466  1.00 33.97  ? 82  MET B O   1 
ATOM   3050 C  CB  . MET B 1 82  ? -9.537  -10.683 13.967  1.00 40.03  ? 82  MET B CB  1 
ATOM   3051 C  CG  . MET B 1 82  ? -10.480 -9.664  13.383  1.00 43.98  ? 82  MET B CG  1 
ATOM   3052 S  SD  . MET B 1 82  ? -12.196 -10.303 13.441  1.00 49.62  ? 82  MET B SD  1 
ATOM   3053 C  CE  . MET B 1 82  ? -11.938 -11.878 12.616  1.00 44.56  ? 82  MET B CE  1 
ATOM   3054 N  N   . GLN B 1 83  ? -7.457  -8.064  13.290  1.00 32.48  ? 83  GLN B N   1 
ATOM   3055 C  CA  . GLN B 1 83  ? -7.337  -6.597  13.417  1.00 31.19  ? 83  GLN B CA  1 
ATOM   3056 C  C   . GLN B 1 83  ? -8.241  -5.974  12.358  1.00 28.61  ? 83  GLN B C   1 
ATOM   3057 O  O   . GLN B 1 83  ? -7.948  -6.105  11.129  1.00 23.65  ? 83  GLN B O   1 
ATOM   3058 C  CB  . GLN B 1 83  ? -5.893  -6.142  13.272  1.00 32.55  ? 83  GLN B CB  1 
ATOM   3059 C  CG  . GLN B 1 83  ? -5.823  -4.629  13.248  1.00 31.85  ? 83  GLN B CG  1 
ATOM   3060 C  CD  . GLN B 1 83  ? -4.424  -4.090  13.160  1.00 37.33  ? 83  GLN B CD  1 
ATOM   3061 O  OE1 . GLN B 1 83  ? -3.465  -4.797  12.846  1.00 38.53  ? 83  GLN B OE1 1 
ATOM   3062 N  NE2 . GLN B 1 83  ? -4.312  -2.809  13.459  1.00 37.91  ? 83  GLN B NE2 1 
ATOM   3063 N  N   . ASN B 1 84  ? -9.350  -5.392  12.808  1.00 28.99  ? 84  ASN B N   1 
ATOM   3064 C  CA  . ASN B 1 84  ? -10.381 -4.861  11.883  1.00 26.40  ? 84  ASN B CA  1 
ATOM   3065 C  C   . ASN B 1 84  ? -10.752 -6.011  10.932  1.00 25.23  ? 84  ASN B C   1 
ATOM   3066 O  O   . ASN B 1 84  ? -11.011 -7.121  11.438  1.00 22.70  ? 84  ASN B O   1 
ATOM   3067 C  CB  . ASN B 1 84  ? -9.841  -3.584  11.242  1.00 26.81  ? 84  ASN B CB  1 
ATOM   3068 C  CG  . ASN B 1 84  ? -9.485  -2.526  12.273  1.00 29.26  ? 84  ASN B CG  1 
ATOM   3069 O  OD1 . ASN B 1 84  ? -10.304 -2.171  13.121  1.00 27.76  ? 84  ASN B OD1 1 
ATOM   3070 N  ND2 . ASN B 1 84  ? -8.266  -2.012  12.218  1.00 27.63  ? 84  ASN B ND2 1 
ATOM   3071 N  N   . CYS B 1 85  ? -10.665 -5.818  9.613   1.00 24.41  ? 85  CYS B N   1 
ATOM   3072 C  CA  . CYS B 1 85  ? -11.123 -6.824  8.626   1.00 25.22  ? 85  CYS B CA  1 
ATOM   3073 C  C   . CYS B 1 85  ? -9.972  -7.712  8.156   1.00 24.75  ? 85  CYS B C   1 
ATOM   3074 O  O   . CYS B 1 85  ? -10.154 -8.457  7.177   1.00 25.62  ? 85  CYS B O   1 
ATOM   3075 C  CB  . CYS B 1 85  ? -11.799 -6.175  7.432   1.00 23.88  ? 85  CYS B CB  1 
ATOM   3076 S  SG  . CYS B 1 85  ? -13.227 -5.161  7.889   1.00 26.42  ? 85  CYS B SG  1 
ATOM   3077 N  N   . VAL B 1 86  ? -8.848  -7.690  8.846   1.00 24.00  ? 86  VAL B N   1 
ATOM   3078 C  CA  . VAL B 1 86  ? -7.664  -8.496  8.482   1.00 26.08  ? 86  VAL B CA  1 
ATOM   3079 C  C   . VAL B 1 86  ? -7.423  -9.547  9.570   1.00 26.89  ? 86  VAL B C   1 
ATOM   3080 O  O   . VAL B 1 86  ? -7.400  -9.194  10.765  1.00 27.48  ? 86  VAL B O   1 
ATOM   3081 C  CB  . VAL B 1 86  ? -6.476  -7.550  8.234   1.00 26.86  ? 86  VAL B CB  1 
ATOM   3082 C  CG1 . VAL B 1 86  ? -5.149  -8.113  8.659   1.00 31.78  ? 86  VAL B CG1 1 
ATOM   3083 C  CG2 . VAL B 1 86  ? -6.436  -7.152  6.773   1.00 26.99  ? 86  VAL B CG2 1 
ATOM   3084 N  N   . LEU B 1 87  ? -7.216  -10.785 9.145   1.00 23.80  ? 87  LEU B N   1 
ATOM   3085 C  CA  . LEU B 1 87  ? -6.761  -11.917 9.988   1.00 26.54  ? 87  LEU B CA  1 
ATOM   3086 C  C   . LEU B 1 87  ? -5.218  -11.950 10.030  1.00 25.80  ? 87  LEU B C   1 
ATOM   3087 O  O   . LEU B 1 87  ? -4.591  -11.849 8.973   1.00 27.26  ? 87  LEU B O   1 
ATOM   3088 C  CB  . LEU B 1 87  ? -7.382  -13.193 9.404   1.00 26.84  ? 87  LEU B CB  1 
ATOM   3089 C  CG  . LEU B 1 87  ? -7.165  -14.488 10.181  1.00 31.08  ? 87  LEU B CG  1 
ATOM   3090 C  CD1 . LEU B 1 87  ? -7.852  -14.454 11.545  1.00 34.15  ? 87  LEU B CD1 1 
ATOM   3091 C  CD2 . LEU B 1 87  ? -7.679  -15.666 9.372   1.00 33.28  ? 87  LEU B CD2 1 
ATOM   3092 N  N   . LYS B 1 88  ? -4.638  -12.019 11.228  1.00 27.00  ? 88  LYS B N   1 
ATOM   3093 C  CA  . LYS B 1 88  ? -3.187  -12.196 11.477  1.00 29.76  ? 88  LYS B CA  1 
ATOM   3094 C  C   . LYS B 1 88  ? -2.938  -13.633 11.962  1.00 31.62  ? 88  LYS B C   1 
ATOM   3095 O  O   . LYS B 1 88  ? -3.478  -14.027 13.032  1.00 31.28  ? 88  LYS B O   1 
ATOM   3096 C  CB  . LYS B 1 88  ? -2.692  -11.150 12.469  1.00 31.92  ? 88  LYS B CB  1 
ATOM   3097 C  CG  . LYS B 1 88  ? -3.010  -9.716  12.060  1.00 34.38  ? 88  LYS B CG  1 
ATOM   3098 C  CD  . LYS B 1 88  ? -2.211  -8.692  12.799  1.00 37.72  ? 88  LYS B CD  1 
ATOM   3099 C  CE  . LYS B 1 88  ? -2.670  -8.470  14.215  1.00 45.12  ? 88  LYS B CE  1 
ATOM   3100 N  NZ  . LYS B 1 88  ? -1.911  -7.355  14.841  1.00 47.72  ? 88  LYS B NZ  1 
ATOM   3101 N  N   . LEU B 1 89  ? -2.247  -14.432 11.158  1.00 27.37  ? 89  LEU B N   1 
ATOM   3102 C  CA  . LEU B 1 89  ? -1.905  -15.828 11.516  1.00 29.30  ? 89  LEU B CA  1 
ATOM   3103 C  C   . LEU B 1 89  ? -0.438  -15.856 11.903  1.00 30.31  ? 89  LEU B C   1 
ATOM   3104 O  O   . LEU B 1 89  ? 0.419   -15.696 11.012  1.00 30.72  ? 89  LEU B O   1 
ATOM   3105 C  CB  . LEU B 1 89  ? -2.205  -16.761 10.347  1.00 32.21  ? 89  LEU B CB  1 
ATOM   3106 C  CG  . LEU B 1 89  ? -3.669  -16.796 9.922   1.00 33.57  ? 89  LEU B CG  1 
ATOM   3107 C  CD1 . LEU B 1 89  ? -3.886  -17.756 8.763   1.00 35.75  ? 89  LEU B CD1 1 
ATOM   3108 C  CD2 . LEU B 1 89  ? -4.549  -17.173 11.091  1.00 35.64  ? 89  LEU B CD2 1 
ATOM   3109 N  N   . LYS B 1 90  ? -0.164  -15.953 13.202  1.00 31.30  ? 90  LYS B N   1 
ATOM   3110 C  CA  . LYS B 1 90  ? 1.221   -16.111 13.701  1.00 35.47  ? 90  LYS B CA  1 
ATOM   3111 C  C   . LYS B 1 90  ? 1.693   -17.492 13.267  1.00 33.88  ? 90  LYS B C   1 
ATOM   3112 O  O   . LYS B 1 90  ? 0.904   -18.442 13.409  1.00 34.31  ? 90  LYS B O   1 
ATOM   3113 C  CB  . LYS B 1 90  ? 1.359   -15.952 15.217  1.00 40.95  ? 90  LYS B CB  1 
ATOM   3114 C  CG  . LYS B 1 90  ? 2.792   -15.614 15.618  1.00 48.01  ? 90  LYS B CG  1 
ATOM   3115 C  CD  . LYS B 1 90  ? 3.053   -15.511 17.101  1.00 55.03  ? 90  LYS B CD  1 
ATOM   3116 C  CE  . LYS B 1 90  ? 4.504   -15.172 17.394  1.00 61.82  ? 90  LYS B CE  1 
ATOM   3117 N  NZ  . LYS B 1 90  ? 4.784   -15.129 18.849  1.00 67.08  ? 90  LYS B NZ  1 
ATOM   3118 N  N   . VAL B 1 91  ? 2.918   -17.552 12.732  1.00 34.96  ? 91  VAL B N   1 
ATOM   3119 C  CA  . VAL B 1 91  ? 3.555   -18.789 12.199  1.00 34.02  ? 91  VAL B CA  1 
ATOM   3120 C  C   . VAL B 1 91  ? 4.876   -19.010 12.931  1.00 37.47  ? 91  VAL B C   1 
ATOM   3121 O  O   . VAL B 1 91  ? 5.408   -18.030 13.524  1.00 35.64  ? 91  VAL B O   1 
ATOM   3122 C  CB  . VAL B 1 91  ? 3.732   -18.720 10.668  1.00 37.30  ? 91  VAL B CB  1 
ATOM   3123 C  CG1 . VAL B 1 91  ? 2.385   -18.760 9.977   1.00 36.08  ? 91  VAL B CG1 1 
ATOM   3124 C  CG2 . VAL B 1 91  ? 4.544   -17.519 10.204  1.00 38.96  ? 91  VAL B CG2 1 
ATOM   3125 N  N   . ASP B 1 92  ? 5.394   -20.243 12.896  1.00 39.53  ? 92  ASP B N   1 
ATOM   3126 C  CA  . ASP B 1 92  ? 6.577   -20.625 13.714  1.00 42.35  ? 92  ASP B CA  1 
ATOM   3127 C  C   . ASP B 1 92  ? 7.860   -20.088 13.066  1.00 45.36  ? 92  ASP B C   1 
ATOM   3128 O  O   . ASP B 1 92  ? 8.896   -20.140 13.720  1.00 45.87  ? 92  ASP B O   1 
ATOM   3129 C  CB  . ASP B 1 92  ? 6.648   -22.137 13.933  1.00 45.75  ? 92  ASP B CB  1 
ATOM   3130 C  CG  . ASP B 1 92  ? 6.807   -22.965 12.666  1.00 50.94  ? 92  ASP B CG  1 
ATOM   3131 O  OD1 . ASP B 1 92  ? 6.701   -22.398 11.548  1.00 55.84  ? 92  ASP B OD1 1 
ATOM   3132 O  OD2 . ASP B 1 92  ? 7.023   -24.178 12.804  1.00 55.25  ? 92  ASP B OD2 1 
ATOM   3133 N  N   . THR B 1 93  ? 7.797   -19.590 11.825  1.00 43.93  ? 93  THR B N   1 
ATOM   3134 C  CA  . THR B 1 93  ? 8.988   -19.258 11.014  1.00 38.07  ? 93  THR B CA  1 
ATOM   3135 C  C   . THR B 1 93  ? 8.861   -17.851 10.431  1.00 39.63  ? 93  THR B C   1 
ATOM   3136 O  O   . THR B 1 93  ? 7.823   -17.526 9.837   1.00 36.59  ? 93  THR B O   1 
ATOM   3137 C  CB  . THR B 1 93  ? 9.186   -20.291 9.909   1.00 40.53  ? 93  THR B CB  1 
ATOM   3138 O  OG1 . THR B 1 93  ? 9.083   -21.526 10.608  1.00 44.58  ? 93  THR B OG1 1 
ATOM   3139 C  CG2 . THR B 1 93  ? 10.516  -20.158 9.197   1.00 41.57  ? 93  THR B CG2 1 
ATOM   3140 N  N   . ALA B 1 94  ? 9.900   -17.046 10.631  1.00 36.00  ? 94  ALA B N   1 
ATOM   3141 C  CA  . ALA B 1 94  ? 10.057  -15.729 9.998   1.00 37.07  ? 94  ALA B CA  1 
ATOM   3142 C  C   . ALA B 1 94  ? 10.334  -15.939 8.510   1.00 40.30  ? 94  ALA B C   1 
ATOM   3143 O  O   . ALA B 1 94  ? 11.136  -16.841 8.158   1.00 38.08  ? 94  ALA B O   1 
ATOM   3144 C  CB  . ALA B 1 94  ? 11.167  -14.966 10.669  1.00 36.92  ? 94  ALA B CB  1 
ATOM   3145 N  N   . ASN B 1 95  ? 9.677   -15.148 7.663   1.00 39.54  ? 95  ASN B N   1 
ATOM   3146 C  CA  . ASN B 1 95  ? 9.938   -15.150 6.204   1.00 35.59  ? 95  ASN B CA  1 
ATOM   3147 C  C   . ASN B 1 95  ? 11.379  -14.691 6.009   1.00 34.44  ? 95  ASN B C   1 
ATOM   3148 O  O   . ASN B 1 95  ? 11.677  -13.523 6.255   1.00 34.16  ? 95  ASN B O   1 
ATOM   3149 C  CB  . ASN B 1 95  ? 8.931   -14.270 5.449   1.00 35.39  ? 95  ASN B CB  1 
ATOM   3150 C  CG  . ASN B 1 95  ? 9.113   -14.359 3.950   1.00 32.72  ? 95  ASN B CG  1 
ATOM   3151 O  OD1 . ASN B 1 95  ? 10.057  -14.991 3.504   1.00 25.25  ? 95  ASN B OD1 1 
ATOM   3152 N  ND2 . ASN B 1 95  ? 8.226   -13.727 3.187   1.00 30.13  ? 95  ASN B ND2 1 
ATOM   3153 N  N   . PRO B 1 96  ? 12.312  -15.558 5.531   1.00 31.11  ? 96  PRO B N   1 
ATOM   3154 C  CA  . PRO B 1 96  ? 13.690  -15.122 5.330   1.00 33.03  ? 96  PRO B CA  1 
ATOM   3155 C  C   . PRO B 1 96  ? 13.777  -14.100 4.185   1.00 34.34  ? 96  PRO B C   1 
ATOM   3156 O  O   . PRO B 1 96  ? 14.798  -13.471 4.041   1.00 36.25  ? 96  PRO B O   1 
ATOM   3157 C  CB  . PRO B 1 96  ? 14.439  -16.415 4.966   1.00 33.67  ? 96  PRO B CB  1 
ATOM   3158 C  CG  . PRO B 1 96  ? 13.376  -17.332 4.391   1.00 33.48  ? 96  PRO B CG  1 
ATOM   3159 C  CD  . PRO B 1 96  ? 12.076  -16.934 5.061   1.00 32.25  ? 96  PRO B CD  1 
ATOM   3160 N  N   . LYS B 1 97  ? 12.716  -13.965 3.387   1.00 32.54  ? 97  LYS B N   1 
ATOM   3161 C  CA  . LYS B 1 97  ? 12.644  -13.001 2.254   1.00 33.71  ? 97  LYS B CA  1 
ATOM   3162 C  C   . LYS B 1 97  ? 11.866  -11.742 2.650   1.00 35.76  ? 97  LYS B C   1 
ATOM   3163 O  O   . LYS B 1 97  ? 11.524  -10.954 1.750   1.00 35.58  ? 97  LYS B O   1 
ATOM   3164 C  CB  . LYS B 1 97  ? 11.994  -13.679 1.047   1.00 38.06  ? 97  LYS B CB  1 
ATOM   3165 C  CG  . LYS B 1 97  ? 12.769  -14.873 0.511   1.00 42.81  ? 97  LYS B CG  1 
ATOM   3166 C  CD  . LYS B 1 97  ? 12.025  -15.622 -0.547  1.00 47.00  ? 97  LYS B CD  1 
ATOM   3167 C  CE  . LYS B 1 97  ? 12.865  -16.713 -1.178  1.00 53.33  ? 97  LYS B CE  1 
ATOM   3168 N  NZ  . LYS B 1 97  ? 12.011  -17.560 -2.036  1.00 60.10  ? 97  LYS B NZ  1 
ATOM   3169 N  N   . THR B 1 98  ? 11.613  -11.512 3.937   1.00 31.04  ? 98  THR B N   1 
ATOM   3170 C  CA  . THR B 1 98  ? 10.946  -10.265 4.385   1.00 32.19  ? 98  THR B CA  1 
ATOM   3171 C  C   . THR B 1 98  ? 11.783  -9.073  3.943   1.00 30.04  ? 98  THR B C   1 
ATOM   3172 O  O   . THR B 1 98  ? 12.922  -8.918  4.387   1.00 31.43  ? 98  THR B O   1 
ATOM   3173 C  CB  . THR B 1 98  ? 10.773  -10.180 5.906   1.00 30.68  ? 98  THR B CB  1 
ATOM   3174 O  OG1 . THR B 1 98  ? 10.045  -11.335 6.292   1.00 29.34  ? 98  THR B OG1 1 
ATOM   3175 C  CG2 . THR B 1 98  ? 10.055  -8.923  6.352   1.00 30.42  ? 98  THR B CG2 1 
ATOM   3176 N  N   . PRO B 1 99  ? 11.231  -8.170  3.103   1.00 26.64  ? 99  PRO B N   1 
ATOM   3177 C  CA  . PRO B 1 99  ? 11.933  -6.934  2.752   1.00 25.80  ? 99  PRO B CA  1 
ATOM   3178 C  C   . PRO B 1 99  ? 11.800  -5.868  3.838   1.00 26.79  ? 99  PRO B C   1 
ATOM   3179 O  O   . PRO B 1 99  ? 10.999  -6.040  4.717   1.00 29.83  ? 99  PRO B O   1 
ATOM   3180 C  CB  . PRO B 1 99  ? 11.172  -6.477  1.509   1.00 27.15  ? 99  PRO B CB  1 
ATOM   3181 C  CG  . PRO B 1 99  ? 9.737   -6.937  1.774   1.00 26.63  ? 99  PRO B CG  1 
ATOM   3182 C  CD  . PRO B 1 99  ? 9.885   -8.266  2.499   1.00 26.19  ? 99  PRO B CD  1 
ATOM   3183 N  N   . LYS B 1 100 ? 12.557  -4.781  3.735   1.00 27.69  ? 100 LYS B N   1 
ATOM   3184 C  CA  . LYS B 1 100 ? 12.302  -3.559  4.527   1.00 31.01  ? 100 LYS B CA  1 
ATOM   3185 C  C   . LYS B 1 100 ? 10.895  -3.085  4.140   1.00 29.27  ? 100 LYS B C   1 
ATOM   3186 O  O   . LYS B 1 100 ? 10.642  -2.937  2.919   1.00 27.22  ? 100 LYS B O   1 
ATOM   3187 C  CB  . LYS B 1 100 ? 13.378  -2.509  4.249   1.00 36.19  ? 100 LYS B CB  1 
ATOM   3188 C  CG  . LYS B 1 100 ? 13.307  -1.282  5.140   1.00 46.80  ? 100 LYS B CG  1 
ATOM   3189 C  CD  . LYS B 1 100 ? 14.254  -0.168  4.727   1.00 55.08  ? 100 LYS B CD  1 
ATOM   3190 C  CE  . LYS B 1 100 ? 14.221  1.024   5.662   1.00 60.73  ? 100 LYS B CE  1 
ATOM   3191 N  NZ  . LYS B 1 100 ? 15.074  0.803   6.854   1.00 67.71  ? 100 LYS B NZ  1 
ATOM   3192 N  N   . TYR B 1 101 ? 9.988   -2.898  5.098   1.00 23.96  ? 101 TYR B N   1 
ATOM   3193 C  CA  . TYR B 1 101 ? 8.571   -2.585  4.754   1.00 25.74  ? 101 TYR B CA  1 
ATOM   3194 C  C   . TYR B 1 101 ? 7.910   -1.727  5.835   1.00 27.19  ? 101 TYR B C   1 
ATOM   3195 O  O   . TYR B 1 101 ? 8.348   -1.701  7.019   1.00 23.92  ? 101 TYR B O   1 
ATOM   3196 C  CB  . TYR B 1 101 ? 7.754   -3.860  4.482   1.00 25.68  ? 101 TYR B CB  1 
ATOM   3197 C  CG  . TYR B 1 101 ? 7.311   -4.592  5.723   1.00 25.47  ? 101 TYR B CG  1 
ATOM   3198 C  CD1 . TYR B 1 101 ? 6.141   -4.240  6.375   1.00 24.45  ? 101 TYR B CD1 1 
ATOM   3199 C  CD2 . TYR B 1 101 ? 8.095   -5.593  6.284   1.00 25.47  ? 101 TYR B CD2 1 
ATOM   3200 C  CE1 . TYR B 1 101 ? 5.767   -4.855  7.557   1.00 25.16  ? 101 TYR B CE1 1 
ATOM   3201 C  CE2 . TYR B 1 101 ? 7.716   -6.243  7.450   1.00 27.09  ? 101 TYR B CE2 1 
ATOM   3202 C  CZ  . TYR B 1 101 ? 6.535   -5.872  8.084   1.00 26.63  ? 101 TYR B CZ  1 
ATOM   3203 O  OH  . TYR B 1 101 ? 6.136   -6.462  9.244   1.00 26.75  ? 101 TYR B OH  1 
ATOM   3204 N  N   . LYS B 1 102 ? 6.902   -0.975  5.404   1.00 26.76  ? 102 LYS B N   1 
ATOM   3205 C  CA  . LYS B 1 102 ? 5.941   -0.285  6.291   1.00 30.55  ? 102 LYS B CA  1 
ATOM   3206 C  C   . LYS B 1 102 ? 4.528   -0.637  5.817   1.00 27.36  ? 102 LYS B C   1 
ATOM   3207 O  O   . LYS B 1 102 ? 4.326   -0.891  4.617   1.00 27.03  ? 102 LYS B O   1 
ATOM   3208 C  CB  . LYS B 1 102 ? 6.010   1.244   6.192   1.00 35.80  ? 102 LYS B CB  1 
ATOM   3209 C  CG  . LYS B 1 102 ? 7.385   1.878   6.122   1.00 46.47  ? 102 LYS B CG  1 
ATOM   3210 C  CD  . LYS B 1 102 ? 7.309   3.380   5.922   1.00 47.51  ? 102 LYS B CD  1 
ATOM   3211 C  CE  . LYS B 1 102 ? 8.649   4.049   6.142   1.00 58.07  ? 102 LYS B CE  1 
ATOM   3212 N  NZ  . LYS B 1 102 ? 8.560   5.519   5.978   1.00 65.33  ? 102 LYS B NZ  1 
ATOM   3213 N  N   . PHE B 1 103 ? 3.558   -0.526  6.707   1.00 25.31  ? 103 PHE B N   1 
ATOM   3214 C  CA  . PHE B 1 103 ? 2.124   -0.437  6.343   1.00 23.63  ? 103 PHE B CA  1 
ATOM   3215 C  C   . PHE B 1 103 ? 1.747   1.033   6.243   1.00 24.47  ? 103 PHE B C   1 
ATOM   3216 O  O   . PHE B 1 103 ? 2.013   1.775   7.191   1.00 26.06  ? 103 PHE B O   1 
ATOM   3217 C  CB  . PHE B 1 103 ? 1.273   -1.134  7.398   1.00 25.70  ? 103 PHE B CB  1 
ATOM   3218 C  CG  . PHE B 1 103 ? 1.416   -2.629  7.421   1.00 25.43  ? 103 PHE B CG  1 
ATOM   3219 C  CD1 . PHE B 1 103 ? 2.013   -3.309  6.370   1.00 24.91  ? 103 PHE B CD1 1 
ATOM   3220 C  CD2 . PHE B 1 103 ? 0.904   -3.356  8.478   1.00 26.61  ? 103 PHE B CD2 1 
ATOM   3221 C  CE1 . PHE B 1 103 ? 2.128   -4.692  6.403   1.00 27.93  ? 103 PHE B CE1 1 
ATOM   3222 C  CE2 . PHE B 1 103 ? 1.000   -4.742  8.489   1.00 26.16  ? 103 PHE B CE2 1 
ATOM   3223 C  CZ  . PHE B 1 103 ? 1.604   -5.406  7.461   1.00 26.09  ? 103 PHE B CZ  1 
ATOM   3224 N  N   . VAL B 1 104 ? 1.187   1.445   5.113   1.00 21.95  ? 104 VAL B N   1 
ATOM   3225 C  CA  . VAL B 1 104 ? 0.803   2.858   4.846   1.00 24.97  ? 104 VAL B CA  1 
ATOM   3226 C  C   . VAL B 1 104 ? -0.640  2.883   4.363   1.00 26.10  ? 104 VAL B C   1 
ATOM   3227 O  O   . VAL B 1 104 ? -1.072  1.934   3.664   1.00 28.36  ? 104 VAL B O   1 
ATOM   3228 C  CB  . VAL B 1 104 ? 1.776   3.476   3.829   1.00 31.54  ? 104 VAL B CB  1 
ATOM   3229 C  CG1 . VAL B 1 104 ? 1.410   4.908   3.478   1.00 38.21  ? 104 VAL B CG1 1 
ATOM   3230 C  CG2 . VAL B 1 104 ? 3.203   3.407   4.385   1.00 29.08  ? 104 VAL B CG2 1 
ATOM   3231 N  N   . ARG B 1 105 ? -1.387  3.912   4.753   1.00 23.68  ? 105 ARG B N   1 
ATOM   3232 C  CA  . ARG B 1 105 ? -2.751  4.135   4.221   1.00 24.35  ? 105 ARG B CA  1 
ATOM   3233 C  C   . ARG B 1 105 ? -2.670  5.257   3.196   1.00 25.30  ? 105 ARG B C   1 
ATOM   3234 O  O   . ARG B 1 105 ? -2.135  6.320   3.552   1.00 28.69  ? 105 ARG B O   1 
ATOM   3235 C  CB  . ARG B 1 105 ? -3.742  4.490   5.329   1.00 27.43  ? 105 ARG B CB  1 
ATOM   3236 C  CG  . ARG B 1 105 ? -5.138  4.731   4.781   1.00 26.71  ? 105 ARG B CG  1 
ATOM   3237 C  CD  . ARG B 1 105 ? -6.209  4.674   5.827   1.00 25.53  ? 105 ARG B CD  1 
ATOM   3238 N  NE  . ARG B 1 105 ? -7.525  4.828   5.243   1.00 25.13  ? 105 ARG B NE  1 
ATOM   3239 C  CZ  . ARG B 1 105 ? -8.386  3.838   4.975   1.00 25.32  ? 105 ARG B CZ  1 
ATOM   3240 N  NH1 . ARG B 1 105 ? -8.070  2.573   5.197   1.00 23.13  ? 105 ARG B NH1 1 
ATOM   3241 N  NH2 . ARG B 1 105 ? -9.577  4.126   4.475   1.00 25.26  ? 105 ARG B NH2 1 
ATOM   3242 N  N   . ILE B 1 106 ? -3.117  5.027   1.964   1.00 23.38  ? 106 ILE B N   1 
ATOM   3243 C  CA  . ILE B 1 106 ? -2.979  6.046   0.886   1.00 25.05  ? 106 ILE B CA  1 
ATOM   3244 C  C   . ILE B 1 106 ? -4.229  6.923   0.800   1.00 25.82  ? 106 ILE B C   1 
ATOM   3245 O  O   . ILE B 1 106 ? -5.285  6.548   1.317   1.00 26.08  ? 106 ILE B O   1 
ATOM   3246 C  CB  . ILE B 1 106 ? -2.649  5.409   -0.479  1.00 27.56  ? 106 ILE B CB  1 
ATOM   3247 C  CG1 . ILE B 1 106 ? -3.676  4.343   -0.880  1.00 27.41  ? 106 ILE B CG1 1 
ATOM   3248 C  CG2 . ILE B 1 106 ? -1.218  4.899   -0.471  1.00 29.16  ? 106 ILE B CG2 1 
ATOM   3249 C  CD1 . ILE B 1 106 ? -3.569  3.884   -2.307  1.00 30.86  ? 106 ILE B CD1 1 
ATOM   3250 N  N   . GLN B 1 107 ? -4.081  8.059   0.127   1.00 27.10  ? 107 GLN B N   1 
ATOM   3251 C  CA  . GLN B 1 107 ? -5.164  9.047   -0.122  1.00 29.94  ? 107 GLN B CA  1 
ATOM   3252 C  C   . GLN B 1 107 ? -5.773  8.757   -1.485  1.00 28.25  ? 107 GLN B C   1 
ATOM   3253 O  O   . GLN B 1 107 ? -5.076  8.265   -2.372  1.00 24.60  ? 107 GLN B O   1 
ATOM   3254 C  CB  . GLN B 1 107 ? -4.576  10.465  -0.126  1.00 32.09  ? 107 GLN B CB  1 
ATOM   3255 C  CG  . GLN B 1 107 ? -4.215  10.966  1.269   1.00 43.65  ? 107 GLN B CG  1 
ATOM   3256 C  CD  . GLN B 1 107 ? -5.447  10.942  2.136   1.00 47.93  ? 107 GLN B CD  1 
ATOM   3257 O  OE1 . GLN B 1 107 ? -6.440  11.608  1.848   1.00 58.20  ? 107 GLN B OE1 1 
ATOM   3258 N  NE2 . GLN B 1 107 ? -5.410  10.123  3.174   1.00 60.37  ? 107 GLN B NE2 1 
ATOM   3259 N  N   . PRO B 1 108 ? -7.072  9.059   -1.688  1.00 31.25  ? 108 PRO B N   1 
ATOM   3260 C  CA  . PRO B 1 108 ? -7.665  9.047   -3.022  1.00 32.11  ? 108 PRO B CA  1 
ATOM   3261 C  C   . PRO B 1 108 ? -6.824  9.882   -3.988  1.00 28.62  ? 108 PRO B C   1 
ATOM   3262 O  O   . PRO B 1 108 ? -6.368  10.931  -3.602  1.00 26.82  ? 108 PRO B O   1 
ATOM   3263 C  CB  . PRO B 1 108 ? -9.036  9.716   -2.832  1.00 34.47  ? 108 PRO B CB  1 
ATOM   3264 C  CG  . PRO B 1 108 ? -9.367  9.429   -1.397  1.00 35.94  ? 108 PRO B CG  1 
ATOM   3265 C  CD  . PRO B 1 108 ? -8.039  9.475   -0.662  1.00 33.77  ? 108 PRO B CD  1 
ATOM   3266 N  N   . GLY B 1 109 ? -6.650  9.391   -5.216  1.00 28.79  ? 109 GLY B N   1 
ATOM   3267 C  CA  . GLY B 1 109 ? -5.819  10.038  -6.245  1.00 26.85  ? 109 GLY B CA  1 
ATOM   3268 C  C   . GLY B 1 109 ? -4.410  9.493   -6.250  1.00 27.84  ? 109 GLY B C   1 
ATOM   3269 O  O   . GLY B 1 109 ? -3.673  9.794   -7.214  1.00 27.72  ? 109 GLY B O   1 
ATOM   3270 N  N   . GLN B 1 110 ? -3.999  8.774   -5.204  1.00 25.59  ? 110 GLN B N   1 
ATOM   3271 C  CA  . GLN B 1 110 ? -2.618  8.226   -5.133  1.00 26.35  ? 110 GLN B CA  1 
ATOM   3272 C  C   . GLN B 1 110 ? -2.613  6.903   -5.886  1.00 23.71  ? 110 GLN B C   1 
ATOM   3273 O  O   . GLN B 1 110 ? -3.686  6.251   -5.990  1.00 22.34  ? 110 GLN B O   1 
ATOM   3274 C  CB  . GLN B 1 110 ? -2.098  8.077   -3.706  1.00 32.46  ? 110 GLN B CB  1 
ATOM   3275 C  CG  . GLN B 1 110 ? -2.042  9.400   -2.955  1.00 41.05  ? 110 GLN B CG  1 
ATOM   3276 C  CD  . GLN B 1 110 ? -1.174  9.342   -1.714  1.00 55.95  ? 110 GLN B CD  1 
ATOM   3277 O  OE1 . GLN B 1 110 ? -1.526  8.765   -0.674  1.00 60.01  ? 110 GLN B OE1 1 
ATOM   3278 N  NE2 . GLN B 1 110 ? -0.009  9.969   -1.804  1.00 68.37  ? 110 GLN B NE2 1 
ATOM   3279 N  N   . THR B 1 111 ? -1.480  6.558   -6.480  1.00 21.85  ? 111 THR B N   1 
ATOM   3280 C  CA  . THR B 1 111 ? -1.364  5.328   -7.309  1.00 22.39  ? 111 THR B CA  1 
ATOM   3281 C  C   . THR B 1 111 ? -0.573  4.266   -6.547  1.00 21.04  ? 111 THR B C   1 
ATOM   3282 O  O   . THR B 1 111 ? 0.094   4.569   -5.569  1.00 23.61  ? 111 THR B O   1 
ATOM   3283 C  CB  . THR B 1 111 ? -0.750  5.628   -8.674  1.00 22.12  ? 111 THR B CB  1 
ATOM   3284 O  OG1 . THR B 1 111 ? 0.514   6.232   -8.432  1.00 22.34  ? 111 THR B OG1 1 
ATOM   3285 C  CG2 . THR B 1 111 ? -1.645  6.533   -9.482  1.00 23.26  ? 111 THR B CG2 1 
ATOM   3286 N  N   . PHE B 1 112 ? -0.663  3.031   -7.005  1.00 22.32  ? 112 PHE B N   1 
ATOM   3287 C  CA  . PHE B 1 112 ? 0.116   1.916   -6.448  1.00 21.90  ? 112 PHE B CA  1 
ATOM   3288 C  C   . PHE B 1 112 ? 0.060   0.757   -7.425  1.00 19.76  ? 112 PHE B C   1 
ATOM   3289 O  O   . PHE B 1 112 ? -0.780  0.714   -8.323  1.00 18.55  ? 112 PHE B O   1 
ATOM   3290 C  CB  . PHE B 1 112 ? -0.388  1.522   -5.059  1.00 21.75  ? 112 PHE B CB  1 
ATOM   3291 C  CG  . PHE B 1 112 ? -1.839  1.108   -5.021  1.00 22.32  ? 112 PHE B CG  1 
ATOM   3292 C  CD1 . PHE B 1 112 ? -2.836  2.050   -4.897  1.00 22.01  ? 112 PHE B CD1 1 
ATOM   3293 C  CD2 . PHE B 1 112 ? -2.198  -0.227  -5.074  1.00 21.07  ? 112 PHE B CD2 1 
ATOM   3294 C  CE1 . PHE B 1 112 ? -4.166  1.675   -4.808  1.00 24.03  ? 112 PHE B CE1 1 
ATOM   3295 C  CE2 . PHE B 1 112 ? -3.522  -0.605  -4.954  1.00 23.47  ? 112 PHE B CE2 1 
ATOM   3296 C  CZ  . PHE B 1 112 ? -4.508  0.348   -4.844  1.00 23.23  ? 112 PHE B CZ  1 
ATOM   3297 N  N   . SER B 1 113 ? 0.985   -0.160  -7.216  1.00 19.34  ? 113 SER B N   1 
ATOM   3298 C  CA  . SER B 1 113 ? 1.109   -1.400  -8.005  1.00 18.96  ? 113 SER B CA  1 
ATOM   3299 C  C   . SER B 1 113 ? 0.346   -2.494  -7.275  1.00 21.00  ? 113 SER B C   1 
ATOM   3300 O  O   . SER B 1 113 ? 0.508   -2.593  -6.051  1.00 19.76  ? 113 SER B O   1 
ATOM   3301 C  CB  . SER B 1 113 ? 2.556   -1.774  -8.143  1.00 21.90  ? 113 SER B CB  1 
ATOM   3302 O  OG  . SER B 1 113 ? 3.294   -0.722  -8.744  1.00 22.64  ? 113 SER B OG  1 
ATOM   3303 N  N   . VAL B 1 114 ? -0.381  -3.308  -8.027  1.00 22.63  ? 114 VAL B N   1 
ATOM   3304 C  CA  . VAL B 1 114 ? -1.112  -4.499  -7.543  1.00 22.44  ? 114 VAL B CA  1 
ATOM   3305 C  C   . VAL B 1 114 ? -0.395  -5.728  -8.086  1.00 22.99  ? 114 VAL B C   1 
ATOM   3306 O  O   . VAL B 1 114 ? -0.179  -5.830  -9.313  1.00 22.10  ? 114 VAL B O   1 
ATOM   3307 C  CB  . VAL B 1 114 ? -2.572  -4.468  -8.009  1.00 24.43  ? 114 VAL B CB  1 
ATOM   3308 C  CG1 . VAL B 1 114 ? -3.287  -5.764  -7.670  1.00 24.35  ? 114 VAL B CG1 1 
ATOM   3309 C  CG2 . VAL B 1 114 ? -3.301  -3.276  -7.407  1.00 26.54  ? 114 VAL B CG2 1 
ATOM   3310 N  N   . LEU B 1 115 ? -0.029  -6.630  -7.195  1.00 22.87  ? 115 LEU B N   1 
ATOM   3311 C  CA  . LEU B 1 115 ? 0.458   -7.959  -7.621  1.00 20.96  ? 115 LEU B CA  1 
ATOM   3312 C  C   . LEU B 1 115 ? -0.703  -8.933  -7.491  1.00 20.93  ? 115 LEU B C   1 
ATOM   3313 O  O   . LEU B 1 115 ? -0.986  -9.420  -6.360  1.00 19.47  ? 115 LEU B O   1 
ATOM   3314 C  CB  . LEU B 1 115 ? 1.673   -8.359  -6.794  1.00 20.39  ? 115 LEU B CB  1 
ATOM   3315 C  CG  . LEU B 1 115 ? 2.279   -9.698  -7.193  1.00 20.19  ? 115 LEU B CG  1 
ATOM   3316 C  CD1 . LEU B 1 115 ? 2.902   -9.617  -8.571  1.00 18.80  ? 115 LEU B CD1 1 
ATOM   3317 C  CD2 . LEU B 1 115 ? 3.293   -10.113 -6.156  1.00 21.25  ? 115 LEU B CD2 1 
ATOM   3318 N  N   . ALA B 1 116 ? -1.374  -9.186  -8.607  1.00 20.51  ? 116 ALA B N   1 
ATOM   3319 C  CA  . ALA B 1 116 ? -2.506  -10.135 -8.671  1.00 21.67  ? 116 ALA B CA  1 
ATOM   3320 C  C   . ALA B 1 116 ? -1.964  -11.558 -8.486  1.00 22.96  ? 116 ALA B C   1 
ATOM   3321 O  O   . ALA B 1 116 ? -0.953  -11.889 -9.129  1.00 27.29  ? 116 ALA B O   1 
ATOM   3322 C  CB  . ALA B 1 116 ? -3.243  -9.965  -9.968  1.00 20.49  ? 116 ALA B CB  1 
ATOM   3323 N  N   . CYS B 1 117 ? -2.564  -12.326 -7.573  1.00 24.30  ? 117 CYS B N   1 
ATOM   3324 C  CA  . CYS B 1 117 ? -2.114  -13.677 -7.143  1.00 26.07  ? 117 CYS B CA  1 
ATOM   3325 C  C   . CYS B 1 117 ? -3.303  -14.638 -7.071  1.00 27.23  ? 117 CYS B C   1 
ATOM   3326 O  O   . CYS B 1 117 ? -4.417  -14.192 -6.805  1.00 27.75  ? 117 CYS B O   1 
ATOM   3327 C  CB  . CYS B 1 117 ? -1.504  -13.668 -5.753  1.00 25.90  ? 117 CYS B CB  1 
ATOM   3328 S  SG  . CYS B 1 117 ? 0.003   -12.689 -5.577  1.00 31.35  ? 117 CYS B SG  1 
ATOM   3329 N  N   . TYR B 1 118 ? -3.044  -15.925 -7.295  1.00 30.41  ? 118 TYR B N   1 
ATOM   3330 C  CA  . TYR B 1 118 ? -4.020  -17.046 -7.252  1.00 30.62  ? 118 TYR B CA  1 
ATOM   3331 C  C   . TYR B 1 118 ? -3.300  -18.218 -6.580  1.00 31.97  ? 118 TYR B C   1 
ATOM   3332 O  O   . TYR B 1 118 ? -2.121  -18.475 -6.941  1.00 30.38  ? 118 TYR B O   1 
ATOM   3333 C  CB  . TYR B 1 118 ? -4.535  -17.359 -8.661  1.00 30.21  ? 118 TYR B CB  1 
ATOM   3334 C  CG  . TYR B 1 118 ? -5.274  -16.195 -9.255  1.00 32.90  ? 118 TYR B CG  1 
ATOM   3335 C  CD1 . TYR B 1 118 ? -4.606  -15.237 -10.008 1.00 35.95  ? 118 TYR B CD1 1 
ATOM   3336 C  CD2 . TYR B 1 118 ? -6.620  -15.985 -8.984  1.00 33.95  ? 118 TYR B CD2 1 
ATOM   3337 C  CE1 . TYR B 1 118 ? -5.260  -14.126 -10.523 1.00 31.49  ? 118 TYR B CE1 1 
ATOM   3338 C  CE2 . TYR B 1 118 ? -7.283  -14.867 -9.469  1.00 34.00  ? 118 TYR B CE2 1 
ATOM   3339 C  CZ  . TYR B 1 118 ? -6.592  -13.931 -10.228 1.00 32.11  ? 118 TYR B CZ  1 
ATOM   3340 O  OH  . TYR B 1 118 ? -7.216  -12.834 -10.731 1.00 32.47  ? 118 TYR B OH  1 
ATOM   3341 N  N   . ASN B 1 119 ? -3.913  -18.794 -5.541  1.00 35.75  ? 119 ASN B N   1 
ATOM   3342 C  CA  . ASN B 1 119 ? -3.369  -19.963 -4.796  1.00 36.61  ? 119 ASN B CA  1 
ATOM   3343 C  C   . ASN B 1 119 ? -1.982  -19.610 -4.259  1.00 35.74  ? 119 ASN B C   1 
ATOM   3344 O  O   . ASN B 1 119 ? -1.107  -20.471 -4.274  1.00 35.76  ? 119 ASN B O   1 
ATOM   3345 C  CB  . ASN B 1 119 ? -3.279  -21.217 -5.678  1.00 40.77  ? 119 ASN B CB  1 
ATOM   3346 C  CG  . ASN B 1 119 ? -4.622  -21.592 -6.268  1.00 44.01  ? 119 ASN B CG  1 
ATOM   3347 O  OD1 . ASN B 1 119 ? -4.774  -21.685 -7.487  1.00 54.75  ? 119 ASN B OD1 1 
ATOM   3348 N  ND2 . ASN B 1 119 ? -5.620  -21.734 -5.414  1.00 47.33  ? 119 ASN B ND2 1 
ATOM   3349 N  N   . GLY B 1 120 ? -1.772  -18.359 -3.848  1.00 32.97  ? 120 GLY B N   1 
ATOM   3350 C  CA  . GLY B 1 120 ? -0.485  -17.912 -3.301  1.00 29.52  ? 120 GLY B CA  1 
ATOM   3351 C  C   . GLY B 1 120 ? 0.552   -17.696 -4.383  1.00 29.47  ? 120 GLY B C   1 
ATOM   3352 O  O   . GLY B 1 120 ? 1.657   -17.324 -4.036  1.00 30.62  ? 120 GLY B O   1 
ATOM   3353 N  N   . SER B 1 121 ? 0.202   -17.834 -5.656  1.00 30.71  ? 121 SER B N   1 
ATOM   3354 C  CA  . SER B 1 121 ? 1.167   -17.710 -6.777  1.00 34.00  ? 121 SER B CA  1 
ATOM   3355 C  C   . SER B 1 121 ? 1.030   -16.377 -7.530  1.00 28.51  ? 121 SER B C   1 
ATOM   3356 O  O   . SER B 1 121 ? -0.003  -16.105 -8.141  1.00 27.46  ? 121 SER B O   1 
ATOM   3357 C  CB  . SER B 1 121 ? 1.022   -18.877 -7.701  1.00 34.64  ? 121 SER B CB  1 
ATOM   3358 O  OG  . SER B 1 121 ? 2.188   -18.979 -8.488  1.00 42.39  ? 121 SER B OG  1 
ATOM   3359 N  N   . PRO B 1 122 ? 2.066   -15.509 -7.548  1.00 29.25  ? 122 PRO B N   1 
ATOM   3360 C  CA  . PRO B 1 122 ? 1.980   -14.250 -8.296  1.00 27.74  ? 122 PRO B CA  1 
ATOM   3361 C  C   . PRO B 1 122 ? 1.658   -14.489 -9.779  1.00 28.91  ? 122 PRO B C   1 
ATOM   3362 O  O   . PRO B 1 122 ? 2.286   -15.304 -10.427 1.00 28.81  ? 122 PRO B O   1 
ATOM   3363 C  CB  . PRO B 1 122 ? 3.364   -13.636 -8.108  1.00 27.92  ? 122 PRO B CB  1 
ATOM   3364 C  CG  . PRO B 1 122 ? 3.805   -14.193 -6.784  1.00 30.77  ? 122 PRO B CG  1 
ATOM   3365 C  CD  . PRO B 1 122 ? 3.338   -15.632 -6.811  1.00 27.95  ? 122 PRO B CD  1 
ATOM   3366 N  N   . SER B 1 123 ? 0.695   -13.755 -10.301 1.00 27.59  ? 123 SER B N   1 
ATOM   3367 C  CA  . SER B 1 123 ? 0.151   -13.975 -11.663 1.00 30.96  ? 123 SER B CA  1 
ATOM   3368 C  C   . SER B 1 123 ? 0.409   -12.771 -12.585 1.00 26.58  ? 123 SER B C   1 
ATOM   3369 O  O   . SER B 1 123 ? 0.604   -12.974 -13.777 1.00 27.34  ? 123 SER B O   1 
ATOM   3370 C  CB  . SER B 1 123 ? -1.305  -14.316 -11.535 1.00 34.71  ? 123 SER B CB  1 
ATOM   3371 O  OG  . SER B 1 123 ? -2.012  -13.990 -12.705 1.00 43.91  ? 123 SER B OG  1 
ATOM   3372 N  N   . GLY B 1 124 ? 0.370   -11.549 -12.066 1.00 24.70  ? 124 GLY B N   1 
ATOM   3373 C  CA  . GLY B 1 124 ? 0.468   -10.343 -12.895 1.00 21.58  ? 124 GLY B CA  1 
ATOM   3374 C  C   . GLY B 1 124 ? 0.617   -9.131  -12.022 1.00 20.16  ? 124 GLY B C   1 
ATOM   3375 O  O   . GLY B 1 124 ? 0.237   -9.176  -10.844 1.00 21.82  ? 124 GLY B O   1 
ATOM   3376 N  N   A VAL B 1 125 ? 1.212   -8.076  -12.577 0.13 20.67  ? 125 VAL B N   1 
ATOM   3377 N  N   B VAL B 1 125 ? 1.190   -8.061  -12.571 0.37 20.10  ? 125 VAL B N   1 
ATOM   3378 N  N   C VAL B 1 125 ? 1.212   -8.076  -12.577 0.13 20.67  ? 125 VAL B N   1 
ATOM   3379 N  N   D VAL B 1 125 ? 1.190   -8.061  -12.571 0.37 20.10  ? 125 VAL B N   1 
ATOM   3380 C  CA  A VAL B 1 125 ? 1.371   -6.757  -11.905 0.13 20.85  ? 125 VAL B CA  1 
ATOM   3381 C  CA  B VAL B 1 125 ? 1.358   -6.767  -11.856 0.37 20.42  ? 125 VAL B CA  1 
ATOM   3382 C  CA  C VAL B 1 125 ? 1.371   -6.757  -11.905 0.13 20.85  ? 125 VAL B CA  1 
ATOM   3383 C  CA  D VAL B 1 125 ? 1.358   -6.767  -11.856 0.37 20.42  ? 125 VAL B CA  1 
ATOM   3384 C  C   A VAL B 1 125 ? 0.738   -5.695  -12.803 0.13 21.10  ? 125 VAL B C   1 
ATOM   3385 C  C   B VAL B 1 125 ? 0.858   -5.637  -12.760 0.37 20.83  ? 125 VAL B C   1 
ATOM   3386 C  C   C VAL B 1 125 ? 0.738   -5.695  -12.803 0.13 21.10  ? 125 VAL B C   1 
ATOM   3387 C  C   D VAL B 1 125 ? 0.858   -5.637  -12.760 0.37 20.83  ? 125 VAL B C   1 
ATOM   3388 O  O   A VAL B 1 125 ? 0.835   -5.821  -14.036 0.13 20.46  ? 125 VAL B O   1 
ATOM   3389 O  O   B VAL B 1 125 ? 1.184   -5.641  -13.948 0.37 19.27  ? 125 VAL B O   1 
ATOM   3390 O  O   C VAL B 1 125 ? 0.835   -5.821  -14.036 0.13 20.46  ? 125 VAL B O   1 
ATOM   3391 O  O   D VAL B 1 125 ? 1.184   -5.641  -13.948 0.37 19.27  ? 125 VAL B O   1 
ATOM   3392 C  CB  A VAL B 1 125 ? 2.846   -6.436  -11.605 0.13 21.15  ? 125 VAL B CB  1 
ATOM   3393 C  CB  B VAL B 1 125 ? 2.810   -6.553  -11.388 0.37 21.23  ? 125 VAL B CB  1 
ATOM   3394 C  CB  C VAL B 1 125 ? 2.846   -6.436  -11.605 0.13 21.15  ? 125 VAL B CB  1 
ATOM   3395 C  CB  D VAL B 1 125 ? 2.810   -6.553  -11.388 0.37 21.23  ? 125 VAL B CB  1 
ATOM   3396 C  CG1 A VAL B 1 125 ? 2.984   -5.591  -10.348 0.13 21.12  ? 125 VAL B CG1 1 
ATOM   3397 C  CG1 B VAL B 1 125 ? 3.809   -6.535  -12.540 0.37 21.26  ? 125 VAL B CG1 1 
ATOM   3398 C  CG1 C VAL B 1 125 ? 2.984   -5.591  -10.348 0.13 21.12  ? 125 VAL B CG1 1 
ATOM   3399 C  CG1 D VAL B 1 125 ? 3.809   -6.535  -12.540 0.37 21.26  ? 125 VAL B CG1 1 
ATOM   3400 C  CG2 A VAL B 1 125 ? 3.685   -7.699  -11.497 0.13 21.21  ? 125 VAL B CG2 1 
ATOM   3401 C  CG2 B VAL B 1 125 ? 2.927   -5.298  -10.541 0.37 21.41  ? 125 VAL B CG2 1 
ATOM   3402 C  CG2 C VAL B 1 125 ? 3.685   -7.699  -11.497 0.13 21.21  ? 125 VAL B CG2 1 
ATOM   3403 C  CG2 D VAL B 1 125 ? 2.927   -5.298  -10.541 0.37 21.41  ? 125 VAL B CG2 1 
ATOM   3404 N  N   . TYR B 1 126 ? 0.075   -4.713  -12.196 1.00 21.72  ? 126 TYR B N   1 
ATOM   3405 C  CA  . TYR B 1 126 ? -0.442  -3.539  -12.928 1.00 21.65  ? 126 TYR B CA  1 
ATOM   3406 C  C   . TYR B 1 126 ? -0.558  -2.378  -11.948 1.00 21.66  ? 126 TYR B C   1 
ATOM   3407 O  O   . TYR B 1 126 ? -0.629  -2.580  -10.712 1.00 19.75  ? 126 TYR B O   1 
ATOM   3408 C  CB  . TYR B 1 126 ? -1.776  -3.854  -13.592 1.00 22.69  ? 126 TYR B CB  1 
ATOM   3409 C  CG  . TYR B 1 126 ? -2.826  -4.447  -12.690 1.00 25.10  ? 126 TYR B CG  1 
ATOM   3410 C  CD1 . TYR B 1 126 ? -3.679  -3.640  -11.942 1.00 25.29  ? 126 TYR B CD1 1 
ATOM   3411 C  CD2 . TYR B 1 126 ? -2.986  -5.816  -12.599 1.00 26.08  ? 126 TYR B CD2 1 
ATOM   3412 C  CE1 . TYR B 1 126 ? -4.638  -4.186  -11.104 1.00 27.08  ? 126 TYR B CE1 1 
ATOM   3413 C  CE2 . TYR B 1 126 ? -3.949  -6.374  -11.766 1.00 28.68  ? 126 TYR B CE2 1 
ATOM   3414 C  CZ  . TYR B 1 126 ? -4.778  -5.563  -11.020 1.00 26.90  ? 126 TYR B CZ  1 
ATOM   3415 O  OH  . TYR B 1 126 ? -5.756  -6.130  -10.252 1.00 38.91  ? 126 TYR B OH  1 
ATOM   3416 N  N   . GLN B 1 127 ? -0.592  -1.184  -12.527 1.00 19.86  ? 127 GLN B N   1 
ATOM   3417 C  CA  . GLN B 1 127 ? -0.703  0.094   -11.801 1.00 22.74  ? 127 GLN B CA  1 
ATOM   3418 C  C   . GLN B 1 127 ? -2.206  0.420   -11.695 1.00 25.08  ? 127 GLN B C   1 
ATOM   3419 O  O   . GLN B 1 127 ? -2.972  0.180   -12.653 1.00 25.52  ? 127 GLN B O   1 
ATOM   3420 C  CB  . GLN B 1 127 ? 0.149   1.087   -12.595 1.00 22.81  ? 127 GLN B CB  1 
ATOM   3421 C  CG  . GLN B 1 127 ? 0.620   2.316   -11.866 1.00 23.80  ? 127 GLN B CG  1 
ATOM   3422 C  CD  . GLN B 1 127 ? 1.529   2.084   -10.695 1.00 22.52  ? 127 GLN B CD  1 
ATOM   3423 O  OE1 . GLN B 1 127 ? 1.928   0.951   -10.333 1.00 24.31  ? 127 GLN B OE1 1 
ATOM   3424 N  NE2 . GLN B 1 127 ? 1.830   3.189   -10.049 1.00 24.99  ? 127 GLN B NE2 1 
ATOM   3425 N  N   A CYS B 1 128 ? -2.622  0.885   -10.506 0.30 24.98  ? 128 CYS B N   1 
ATOM   3426 N  N   B CYS B 1 128 ? -2.630  0.990   -10.574 0.20 25.79  ? 128 CYS B N   1 
ATOM   3427 N  N   C CYS B 1 128 ? -2.622  0.885   -10.506 0.30 24.98  ? 128 CYS B N   1 
ATOM   3428 N  N   D CYS B 1 128 ? -2.630  0.990   -10.574 0.20 25.79  ? 128 CYS B N   1 
ATOM   3429 C  CA  A CYS B 1 128 ? -3.990  1.376   -10.170 0.30 25.83  ? 128 CYS B CA  1 
ATOM   3430 C  CA  B CYS B 1 128 ? -4.007  1.517   -10.443 0.20 26.75  ? 128 CYS B CA  1 
ATOM   3431 C  CA  C CYS B 1 128 ? -3.990  1.376   -10.170 0.30 25.83  ? 128 CYS B CA  1 
ATOM   3432 C  CA  D CYS B 1 128 ? -4.007  1.517   -10.443 0.20 26.75  ? 128 CYS B CA  1 
ATOM   3433 C  C   A CYS B 1 128 ? -3.906  2.758   -9.509  0.30 25.15  ? 128 CYS B C   1 
ATOM   3434 C  C   B CYS B 1 128 ? -4.049  2.617   -9.385  0.20 26.42  ? 128 CYS B C   1 
ATOM   3435 C  C   C CYS B 1 128 ? -3.906  2.758   -9.509  0.30 25.15  ? 128 CYS B C   1 
ATOM   3436 C  C   D CYS B 1 128 ? -4.049  2.617   -9.385  0.20 26.42  ? 128 CYS B C   1 
ATOM   3437 O  O   A CYS B 1 128 ? -2.836  3.087   -8.974  0.30 24.47  ? 128 CYS B O   1 
ATOM   3438 O  O   B CYS B 1 128 ? -3.225  2.600   -8.450  0.20 27.32  ? 128 CYS B O   1 
ATOM   3439 O  O   C CYS B 1 128 ? -2.836  3.087   -8.974  0.30 24.47  ? 128 CYS B O   1 
ATOM   3440 O  O   D CYS B 1 128 ? -3.225  2.600   -8.450  0.20 27.32  ? 128 CYS B O   1 
ATOM   3441 C  CB  A CYS B 1 128 ? -4.705  0.451   -9.189  0.30 26.00  ? 128 CYS B CB  1 
ATOM   3442 C  CB  B CYS B 1 128 ? -4.987  0.401   -10.116 0.20 27.74  ? 128 CYS B CB  1 
ATOM   3443 C  CB  C CYS B 1 128 ? -4.705  0.451   -9.189  0.30 26.00  ? 128 CYS B CB  1 
ATOM   3444 C  CB  D CYS B 1 128 ? -4.987  0.401   -10.116 0.20 27.74  ? 128 CYS B CB  1 
ATOM   3445 S  SG  A CYS B 1 128 ? -5.452  -1.011  -9.959  0.30 29.35  ? 128 CYS B SG  1 
ATOM   3446 S  SG  B CYS B 1 128 ? -4.609  -0.407  -8.544  0.20 28.92  ? 128 CYS B SG  1 
ATOM   3447 S  SG  C CYS B 1 128 ? -5.452  -1.011  -9.959  0.30 29.35  ? 128 CYS B SG  1 
ATOM   3448 S  SG  D CYS B 1 128 ? -4.609  -0.407  -8.544  0.20 28.92  ? 128 CYS B SG  1 
ATOM   3449 N  N   . ALA B 1 129 ? -4.993  3.535   -9.559  1.00 26.13  ? 129 ALA B N   1 
ATOM   3450 C  CA  . ALA B 1 129 ? -5.220  4.665   -8.654  1.00 25.76  ? 129 ALA B CA  1 
ATOM   3451 C  C   . ALA B 1 129 ? -6.379  4.276   -7.731  1.00 23.61  ? 129 ALA B C   1 
ATOM   3452 O  O   . ALA B 1 129 ? -7.290  3.548   -8.141  1.00 24.05  ? 129 ALA B O   1 
ATOM   3453 C  CB  . ALA B 1 129 ? -5.503  5.926   -9.431  1.00 28.22  ? 129 ALA B CB  1 
ATOM   3454 N  N   . MET B 1 130 ? -6.275  4.728   -6.496  1.00 23.63  ? 130 MET B N   1 
ATOM   3455 C  CA  . MET B 1 130 ? -7.389  4.806   -5.532  1.00 24.10  ? 130 MET B CA  1 
ATOM   3456 C  C   . MET B 1 130 ? -8.321  5.913   -6.035  1.00 23.46  ? 130 MET B C   1 
ATOM   3457 O  O   . MET B 1 130 ? -7.892  7.076   -6.090  1.00 24.32  ? 130 MET B O   1 
ATOM   3458 C  CB  . MET B 1 130 ? -6.812  5.146   -4.163  1.00 23.71  ? 130 MET B CB  1 
ATOM   3459 C  CG  . MET B 1 130 ? -7.805  5.227   -3.019  1.00 26.52  ? 130 MET B CG  1 
ATOM   3460 S  SD  . MET B 1 130 ? -8.807  3.748   -2.803  1.00 30.94  ? 130 MET B SD  1 
ATOM   3461 C  CE  . MET B 1 130 ? -7.593  2.524   -2.329  1.00 29.87  ? 130 MET B CE  1 
ATOM   3462 N  N   . ARG B 1 131 ? -9.497  5.531   -6.509  1.00 23.59  ? 131 ARG B N   1 
ATOM   3463 C  CA  . ARG B 1 131 ? -10.467 6.469   -7.111  1.00 22.94  ? 131 ARG B CA  1 
ATOM   3464 C  C   . ARG B 1 131 ? -10.947 7.380   -5.982  1.00 26.33  ? 131 ARG B C   1 
ATOM   3465 O  O   . ARG B 1 131 ? -10.843 7.021   -4.798  1.00 22.33  ? 131 ARG B O   1 
ATOM   3466 C  CB  . ARG B 1 131 ? -11.651 5.736   -7.735  1.00 23.49  ? 131 ARG B CB  1 
ATOM   3467 C  CG  . ARG B 1 131 ? -11.309 4.776   -8.865  1.00 27.59  ? 131 ARG B CG  1 
ATOM   3468 C  CD  . ARG B 1 131 ? -10.592 5.399   -10.032 1.00 27.57  ? 131 ARG B CD  1 
ATOM   3469 N  NE  . ARG B 1 131 ? -11.100 6.695   -10.442 1.00 25.85  ? 131 ARG B NE  1 
ATOM   3470 C  CZ  . ARG B 1 131 ? -10.457 7.513   -11.268 1.00 26.74  ? 131 ARG B CZ  1 
ATOM   3471 N  NH1 . ARG B 1 131 ? -9.273  7.167   -11.758 1.00 25.58  ? 131 ARG B NH1 1 
ATOM   3472 N  NH2 . ARG B 1 131 ? -10.980 8.690   -11.569 1.00 24.55  ? 131 ARG B NH2 1 
ATOM   3473 N  N   . PRO B 1 132 ? -11.424 8.601   -6.314  1.00 26.24  ? 132 PRO B N   1 
ATOM   3474 C  CA  . PRO B 1 132 ? -12.085 9.452   -5.330  1.00 26.21  ? 132 PRO B CA  1 
ATOM   3475 C  C   . PRO B 1 132 ? -13.217 8.726   -4.597  1.00 24.43  ? 132 PRO B C   1 
ATOM   3476 O  O   . PRO B 1 132 ? -13.414 9.053   -3.464  1.00 23.76  ? 132 PRO B O   1 
ATOM   3477 C  CB  . PRO B 1 132 ? -12.599 10.628  -6.178  1.00 27.22  ? 132 PRO B CB  1 
ATOM   3478 C  CG  . PRO B 1 132 ? -11.570 10.730  -7.290  1.00 25.65  ? 132 PRO B CG  1 
ATOM   3479 C  CD  . PRO B 1 132 ? -11.205 9.290   -7.601  1.00 24.95  ? 132 PRO B CD  1 
ATOM   3480 N  N   . ASN B 1 133 ? -13.888 7.754   -5.223  1.00 22.94  ? 133 ASN B N   1 
ATOM   3481 C  CA  . ASN B 1 133 ? -15.024 7.018   -4.584  1.00 23.89  ? 133 ASN B CA  1 
ATOM   3482 C  C   . ASN B 1 133 ? -14.505 5.803   -3.796  1.00 26.89  ? 133 ASN B C   1 
ATOM   3483 O  O   . ASN B 1 133 ? -15.332 4.961   -3.361  1.00 25.90  ? 133 ASN B O   1 
ATOM   3484 C  CB  . ASN B 1 133 ? -16.092 6.601   -5.599  1.00 22.62  ? 133 ASN B CB  1 
ATOM   3485 C  CG  . ASN B 1 133 ? -15.677 5.468   -6.518  1.00 25.32  ? 133 ASN B CG  1 
ATOM   3486 O  OD1 . ASN B 1 133 ? -14.518 5.025   -6.488  1.00 22.36  ? 133 ASN B OD1 1 
ATOM   3487 N  ND2 . ASN B 1 133 ? -16.604 5.027   -7.378  1.00 22.20  ? 133 ASN B ND2 1 
ATOM   3488 N  N   . PHE B 1 134 ? -13.183 5.665   -3.683  1.00 24.78  ? 134 PHE B N   1 
ATOM   3489 C  CA  . PHE B 1 134 ? -12.463 4.696   -2.816  1.00 23.44  ? 134 PHE B CA  1 
ATOM   3490 C  C   . PHE B 1 134 ? -12.544 3.289   -3.390  1.00 24.14  ? 134 PHE B C   1 
ATOM   3491 O  O   . PHE B 1 134 ? -12.242 2.323   -2.651  1.00 29.01  ? 134 PHE B O   1 
ATOM   3492 C  CB  . PHE B 1 134 ? -12.968 4.707   -1.370  1.00 25.03  ? 134 PHE B CB  1 
ATOM   3493 C  CG  . PHE B 1 134 ? -12.543 5.898   -0.556  1.00 24.48  ? 134 PHE B CG  1 
ATOM   3494 C  CD1 . PHE B 1 134 ? -11.225 6.056   -0.161  1.00 25.44  ? 134 PHE B CD1 1 
ATOM   3495 C  CD2 . PHE B 1 134 ? -13.461 6.897   -0.249  1.00 27.93  ? 134 PHE B CD2 1 
ATOM   3496 C  CE1 . PHE B 1 134 ? -10.846 7.162   0.590   1.00 28.36  ? 134 PHE B CE1 1 
ATOM   3497 C  CE2 . PHE B 1 134 ? -13.083 8.015   0.480   1.00 27.80  ? 134 PHE B CE2 1 
ATOM   3498 C  CZ  . PHE B 1 134 ? -11.774 8.147   0.891   1.00 29.15  ? 134 PHE B CZ  1 
ATOM   3499 N  N   . THR B 1 135 ? -12.831 3.164   -4.681  1.00 22.96  ? 135 THR B N   1 
ATOM   3500 C  CA  . THR B 1 135 ? -12.698 1.879   -5.404  1.00 22.80  ? 135 THR B CA  1 
ATOM   3501 C  C   . THR B 1 135 ? -11.393 1.924   -6.190  1.00 23.97  ? 135 THR B C   1 
ATOM   3502 O  O   . THR B 1 135 ? -10.798 3.019   -6.292  1.00 25.37  ? 135 THR B O   1 
ATOM   3503 C  CB  . THR B 1 135 ? -13.909 1.624   -6.303  1.00 24.34  ? 135 THR B CB  1 
ATOM   3504 O  OG1 . THR B 1 135 ? -13.939 2.588   -7.357  1.00 23.79  ? 135 THR B OG1 1 
ATOM   3505 C  CG2 . THR B 1 135 ? -15.204 1.680   -5.531  1.00 26.27  ? 135 THR B CG2 1 
ATOM   3506 N  N   . ILE B 1 136 ? -10.941 0.774   -6.657  1.00 23.46  ? 136 ILE B N   1 
ATOM   3507 C  CA  . ILE B 1 136 ? -9.895  0.688   -7.706  1.00 24.65  ? 136 ILE B CA  1 
ATOM   3508 C  C   . ILE B 1 136 ? -10.507 -0.068  -8.890  1.00 26.30  ? 136 ILE B C   1 
ATOM   3509 O  O   . ILE B 1 136 ? -11.403 -0.935  -8.678  1.00 25.97  ? 136 ILE B O   1 
ATOM   3510 C  CB  . ILE B 1 136 ? -8.578  0.060   -7.189  1.00 28.12  ? 136 ILE B CB  1 
ATOM   3511 C  CG1 . ILE B 1 136 ? -8.656  -1.455  -7.018  1.00 28.63  ? 136 ILE B CG1 1 
ATOM   3512 C  CG2 . ILE B 1 136 ? -8.096  0.736   -5.907  1.00 27.75  ? 136 ILE B CG2 1 
ATOM   3513 C  CD1 . ILE B 1 136 ? -7.339  -2.087  -6.607  1.00 29.75  ? 136 ILE B CD1 1 
ATOM   3514 N  N   . LYS B 1 137 ? -10.085 0.285   -10.099 1.00 26.39  ? 137 LYS B N   1 
ATOM   3515 C  CA  . LYS B 1 137 ? -10.488 -0.422  -11.333 1.00 29.29  ? 137 LYS B CA  1 
ATOM   3516 C  C   . LYS B 1 137 ? -9.408  -1.454  -11.603 1.00 29.32  ? 137 LYS B C   1 
ATOM   3517 O  O   . LYS B 1 137 ? -8.431  -1.139  -12.299 1.00 27.78  ? 137 LYS B O   1 
ATOM   3518 C  CB  . LYS B 1 137 ? -10.685 0.582   -12.464 1.00 34.74  ? 137 LYS B CB  1 
ATOM   3519 C  CG  . LYS B 1 137 ? -11.735 1.625   -12.143 1.00 39.43  ? 137 LYS B CG  1 
ATOM   3520 C  CD  . LYS B 1 137 ? -12.070 2.547   -13.271 1.00 45.55  ? 137 LYS B CD  1 
ATOM   3521 C  CE  . LYS B 1 137 ? -13.122 3.551   -12.859 1.00 54.23  ? 137 LYS B CE  1 
ATOM   3522 N  NZ  . LYS B 1 137 ? -13.498 4.431   -13.987 1.00 62.63  ? 137 LYS B NZ  1 
ATOM   3523 N  N   . GLY B 1 138 ? -9.558  -2.622  -10.983 1.00 28.65  ? 138 GLY B N   1 
ATOM   3524 C  CA  . GLY B 1 138 ? -8.537  -3.676  -11.010 1.00 30.65  ? 138 GLY B CA  1 
ATOM   3525 C  C   . GLY B 1 138 ? -8.897  -4.711  -12.038 1.00 28.78  ? 138 GLY B C   1 
ATOM   3526 O  O   . GLY B 1 138 ? -9.869  -4.504  -12.791 1.00 30.94  ? 138 GLY B O   1 
ATOM   3527 N  N   . SER B 1 139 ? -8.142  -5.798  -12.051 1.00 27.50  ? 139 SER B N   1 
ATOM   3528 C  CA  . SER B 1 139 ? -8.444  -6.988  -12.867 1.00 26.62  ? 139 SER B CA  1 
ATOM   3529 C  C   . SER B 1 139 ? -8.243  -8.172  -11.945 1.00 29.33  ? 139 SER B C   1 
ATOM   3530 O  O   . SER B 1 139 ? -7.089  -8.443  -11.556 1.00 25.96  ? 139 SER B O   1 
ATOM   3531 C  CB  . SER B 1 139 ? -7.613  -7.070  -14.092 1.00 28.93  ? 139 SER B CB  1 
ATOM   3532 O  OG  . SER B 1 139 ? -7.782  -8.337  -14.704 1.00 32.50  ? 139 SER B OG  1 
ATOM   3533 N  N   . PHE B 1 140 ? -9.353  -8.741  -11.487 1.00 28.21  ? 140 PHE B N   1 
ATOM   3534 C  CA  . PHE B 1 140 ? -9.333  -9.736  -10.390 1.00 31.73  ? 140 PHE B CA  1 
ATOM   3535 C  C   . PHE B 1 140 ? -10.345 -10.829 -10.713 1.00 37.50  ? 140 PHE B C   1 
ATOM   3536 O  O   . PHE B 1 140 ? -11.471 -10.474 -11.159 1.00 35.91  ? 140 PHE B O   1 
ATOM   3537 C  CB  . PHE B 1 140 ? -9.681  -9.074  -9.058  1.00 31.42  ? 140 PHE B CB  1 
ATOM   3538 C  CG  . PHE B 1 140 ? -8.628  -8.153  -8.488  1.00 30.77  ? 140 PHE B CG  1 
ATOM   3539 C  CD1 . PHE B 1 140 ? -7.373  -8.631  -8.111  1.00 30.83  ? 140 PHE B CD1 1 
ATOM   3540 C  CD2 . PHE B 1 140 ? -8.916  -6.815  -8.278  1.00 32.58  ? 140 PHE B CD2 1 
ATOM   3541 C  CE1 . PHE B 1 140 ? -6.427  -7.788  -7.550  1.00 27.85  ? 140 PHE B CE1 1 
ATOM   3542 C  CE2 . PHE B 1 140 ? -7.974  -5.969  -7.710  1.00 32.68  ? 140 PHE B CE2 1 
ATOM   3543 C  CZ  . PHE B 1 140 ? -6.743  -6.460  -7.327  1.00 31.85  ? 140 PHE B CZ  1 
ATOM   3544 N  N   . LEU B 1 141 ? -9.946  -12.092 -10.531 1.00 36.13  ? 141 LEU B N   1 
ATOM   3545 C  CA  . LEU B 1 141 ? -10.873 -13.245 -10.660 1.00 41.50  ? 141 LEU B CA  1 
ATOM   3546 C  C   . LEU B 1 141 ? -11.002 -13.945 -9.307  1.00 43.34  ? 141 LEU B C   1 
ATOM   3547 O  O   . LEU B 1 141 ? -10.272 -13.589 -8.379  1.00 40.82  ? 141 LEU B O   1 
ATOM   3548 C  CB  . LEU B 1 141 ? -10.369 -14.196 -11.751 1.00 39.22  ? 141 LEU B CB  1 
ATOM   3549 C  CG  . LEU B 1 141 ? -10.214 -13.559 -13.138 1.00 42.36  ? 141 LEU B CG  1 
ATOM   3550 C  CD1 . LEU B 1 141 ? -9.725  -14.595 -14.139 1.00 45.41  ? 141 LEU B CD1 1 
ATOM   3551 C  CD2 . LEU B 1 141 ? -11.508 -12.909 -13.621 1.00 38.62  ? 141 LEU B CD2 1 
ATOM   3552 N  N   . ASN B 1 142 ? -11.916 -14.910 -9.228  1.00 47.23  ? 142 ASN B N   1 
ATOM   3553 C  CA  . ASN B 1 142 ? -12.077 -15.818 -8.061  1.00 48.10  ? 142 ASN B CA  1 
ATOM   3554 C  C   . ASN B 1 142 ? -10.700 -16.318 -7.610  1.00 41.51  ? 142 ASN B C   1 
ATOM   3555 O  O   . ASN B 1 142 ? -9.962  -16.870 -8.460  1.00 36.23  ? 142 ASN B O   1 
ATOM   3556 C  CB  . ASN B 1 142 ? -13.006 -16.990 -8.392  1.00 55.21  ? 142 ASN B CB  1 
ATOM   3557 C  CG  . ASN B 1 142 ? -14.395 -16.530 -8.783  1.00 63.36  ? 142 ASN B CG  1 
ATOM   3558 O  OD1 . ASN B 1 142 ? -14.683 -15.330 -8.794  1.00 67.48  ? 142 ASN B OD1 1 
ATOM   3559 N  ND2 . ASN B 1 142 ? -15.260 -17.477 -9.111  1.00 64.39  ? 142 ASN B ND2 1 
ATOM   3560 N  N   . GLY B 1 143 ? -10.379 -16.138 -6.323  1.00 38.01  ? 143 GLY B N   1 
ATOM   3561 C  CA  . GLY B 1 143 ? -9.108  -16.583 -5.711  1.00 36.49  ? 143 GLY B CA  1 
ATOM   3562 C  C   . GLY B 1 143 ? -8.063  -15.468 -5.633  1.00 33.61  ? 143 GLY B C   1 
ATOM   3563 O  O   . GLY B 1 143 ? -6.973  -15.736 -5.117  1.00 29.59  ? 143 GLY B O   1 
ATOM   3564 N  N   . SER B 1 144 ? -8.362  -14.263 -6.133  1.00 30.67  ? 144 SER B N   1 
ATOM   3565 C  CA  . SER B 1 144 ? -7.439  -13.088 -6.070  1.00 31.38  ? 144 SER B CA  1 
ATOM   3566 C  C   . SER B 1 144 ? -7.478  -12.417 -4.687  1.00 28.54  ? 144 SER B C   1 
ATOM   3567 O  O   . SER B 1 144 ? -6.602  -11.579 -4.412  1.00 25.94  ? 144 SER B O   1 
ATOM   3568 C  CB  . SER B 1 144 ? -7.732  -12.073 -7.157  1.00 28.24  ? 144 SER B CB  1 
ATOM   3569 O  OG  . SER B 1 144 ? -9.052  -11.579 -7.037  1.00 28.30  ? 144 SER B OG  1 
ATOM   3570 N  N   . CYS B 1 145 ? -8.469  -12.721 -3.843  1.00 26.69  ? 145 CYS B N   1 
ATOM   3571 C  CA  . CYS B 1 145 ? -8.574  -12.075 -2.506  1.00 24.62  ? 145 CYS B CA  1 
ATOM   3572 C  C   . CYS B 1 145 ? -7.266  -12.274 -1.755  1.00 23.76  ? 145 CYS B C   1 
ATOM   3573 O  O   . CYS B 1 145 ? -6.676  -13.384 -1.828  1.00 25.16  ? 145 CYS B O   1 
ATOM   3574 C  CB  . CYS B 1 145 ? -9.747  -12.609 -1.700  1.00 27.01  ? 145 CYS B CB  1 
ATOM   3575 S  SG  . CYS B 1 145 ? -11.343 -12.159 -2.403  1.00 30.57  ? 145 CYS B SG  1 
ATOM   3576 N  N   . GLY B 1 146 ? -6.814  -11.217 -1.076  1.00 23.85  ? 146 GLY B N   1 
ATOM   3577 C  CA  . GLY B 1 146 ? -5.526  -11.197 -0.364  1.00 22.21  ? 146 GLY B CA  1 
ATOM   3578 C  C   . GLY B 1 146 ? -4.365  -10.742 -1.226  1.00 22.97  ? 146 GLY B C   1 
ATOM   3579 O  O   . GLY B 1 146 ? -3.252  -10.609 -0.667  1.00 21.84  ? 146 GLY B O   1 
ATOM   3580 N  N   . SER B 1 147 ? -4.539  -10.623 -2.549  1.00 23.26  ? 147 SER B N   1 
ATOM   3581 C  CA  . SER B 1 147 ? -3.569  -9.897  -3.416  1.00 22.55  ? 147 SER B CA  1 
ATOM   3582 C  C   . SER B 1 147 ? -3.302  -8.533  -2.767  1.00 22.31  ? 147 SER B C   1 
ATOM   3583 O  O   . SER B 1 147 ? -4.268  -7.928  -2.227  1.00 21.75  ? 147 SER B O   1 
ATOM   3584 C  CB  . SER B 1 147 ? -4.092  -9.735  -4.809  1.00 20.27  ? 147 SER B CB  1 
ATOM   3585 O  OG  . SER B 1 147 ? -4.191  -10.975 -5.483  1.00 22.81  ? 147 SER B OG  1 
ATOM   3586 N  N   . VAL B 1 148 ? -2.084  -8.001  -2.858  1.00 25.70  ? 148 VAL B N   1 
ATOM   3587 C  CA  . VAL B 1 148 ? -1.768  -6.682  -2.223  1.00 25.09  ? 148 VAL B CA  1 
ATOM   3588 C  C   . VAL B 1 148 ? -1.334  -5.613  -3.227  1.00 23.52  ? 148 VAL B C   1 
ATOM   3589 O  O   . VAL B 1 148 ? -0.925  -5.927  -4.349  1.00 22.19  ? 148 VAL B O   1 
ATOM   3590 C  CB  . VAL B 1 148 ? -0.732  -6.854  -1.114  1.00 27.77  ? 148 VAL B CB  1 
ATOM   3591 C  CG1 . VAL B 1 148 ? -1.317  -7.708  -0.003  1.00 27.36  ? 148 VAL B CG1 1 
ATOM   3592 C  CG2 . VAL B 1 148 ? 0.574   -7.439  -1.625  1.00 26.72  ? 148 VAL B CG2 1 
ATOM   3593 N  N   . GLY B 1 149 ? -1.446  -4.369  -2.779  1.00 23.90  ? 149 GLY B N   1 
ATOM   3594 C  CA  . GLY B 1 149 ? -1.031  -3.153  -3.486  1.00 21.67  ? 149 GLY B CA  1 
ATOM   3595 C  C   . GLY B 1 149 ? 0.079   -2.511  -2.689  1.00 22.76  ? 149 GLY B C   1 
ATOM   3596 O  O   . GLY B 1 149 ? 0.045   -2.586  -1.427  1.00 21.61  ? 149 GLY B O   1 
ATOM   3597 N  N   . PHE B 1 150 ? 1.057   -1.938  -3.370  1.00 22.01  ? 150 PHE B N   1 
ATOM   3598 C  CA  . PHE B 1 150 ? 2.288   -1.441  -2.716  1.00 21.53  ? 150 PHE B CA  1 
ATOM   3599 C  C   . PHE B 1 150 ? 2.928   -0.339  -3.556  1.00 22.57  ? 150 PHE B C   1 
ATOM   3600 O  O   . PHE B 1 150 ? 2.645   -0.205  -4.753  1.00 20.14  ? 150 PHE B O   1 
ATOM   3601 C  CB  . PHE B 1 150 ? 3.294   -2.575  -2.534  1.00 21.77  ? 150 PHE B CB  1 
ATOM   3602 C  CG  . PHE B 1 150 ? 3.784   -3.184  -3.822  1.00 21.57  ? 150 PHE B CG  1 
ATOM   3603 C  CD1 . PHE B 1 150 ? 3.012   -4.094  -4.507  1.00 25.18  ? 150 PHE B CD1 1 
ATOM   3604 C  CD2 . PHE B 1 150 ? 5.035   -2.885  -4.329  1.00 23.53  ? 150 PHE B CD2 1 
ATOM   3605 C  CE1 . PHE B 1 150 ? 3.441   -4.637  -5.705  1.00 25.89  ? 150 PHE B CE1 1 
ATOM   3606 C  CE2 . PHE B 1 150 ? 5.465   -3.441  -5.526  1.00 21.73  ? 150 PHE B CE2 1 
ATOM   3607 C  CZ  . PHE B 1 150 ? 4.676   -4.324  -6.204  1.00 22.23  ? 150 PHE B CZ  1 
ATOM   3608 N  N   . ASN B 1 151 ? 3.791   0.423   -2.895  1.00 22.07  ? 151 ASN B N   1 
ATOM   3609 C  CA  . ASN B 1 151 ? 4.747   1.352   -3.536  1.00 24.62  ? 151 ASN B CA  1 
ATOM   3610 C  C   . ASN B 1 151 ? 6.124   0.969   -3.008  1.00 24.42  ? 151 ASN B C   1 
ATOM   3611 O  O   . ASN B 1 151 ? 6.195   0.361   -1.938  1.00 23.97  ? 151 ASN B O   1 
ATOM   3612 C  CB  . ASN B 1 151 ? 4.416   2.819   -3.234  1.00 26.18  ? 151 ASN B CB  1 
ATOM   3613 C  CG  . ASN B 1 151 ? 3.147   3.264   -3.928  1.00 29.64  ? 151 ASN B CG  1 
ATOM   3614 O  OD1 . ASN B 1 151 ? 3.172   3.536   -5.116  1.00 30.17  ? 151 ASN B OD1 1 
ATOM   3615 N  ND2 . ASN B 1 151 ? 2.033   3.305   -3.215  1.00 25.27  ? 151 ASN B ND2 1 
ATOM   3616 N  N   . ILE B 1 152 ? 7.162   1.338   -3.734  1.00 26.43  ? 152 ILE B N   1 
ATOM   3617 C  CA  . ILE B 1 152 ? 8.566   1.188   -3.282  1.00 30.39  ? 152 ILE B CA  1 
ATOM   3618 C  C   . ILE B 1 152 ? 9.182   2.586   -3.237  1.00 37.99  ? 152 ILE B C   1 
ATOM   3619 O  O   . ILE B 1 152 ? 9.015   3.351   -4.215  1.00 34.12  ? 152 ILE B O   1 
ATOM   3620 C  CB  . ILE B 1 152 ? 9.320   0.225   -4.199  1.00 31.32  ? 152 ILE B CB  1 
ATOM   3621 C  CG1 . ILE B 1 152 ? 8.587   -1.110  -4.331  1.00 30.71  ? 152 ILE B CG1 1 
ATOM   3622 C  CG2 . ILE B 1 152 ? 10.751  0.056   -3.708  1.00 32.25  ? 152 ILE B CG2 1 
ATOM   3623 C  CD1 . ILE B 1 152 ? 9.360   -2.181  -5.082  1.00 35.33  ? 152 ILE B CD1 1 
ATOM   3624 N  N   . ASP B 1 153 ? 9.816   2.916   -2.113  1.00 45.58  ? 153 ASP B N   1 
ATOM   3625 C  CA  . ASP B 1 153 ? 10.643  4.140   -1.925  1.00 51.30  ? 153 ASP B CA  1 
ATOM   3626 C  C   . ASP B 1 153 ? 12.042  3.680   -1.525  1.00 56.36  ? 153 ASP B C   1 
ATOM   3627 O  O   . ASP B 1 153 ? 12.178  3.238   -0.373  1.00 58.92  ? 153 ASP B O   1 
ATOM   3628 C  CB  . ASP B 1 153 ? 9.986   5.045   -0.887  1.00 54.35  ? 153 ASP B CB  1 
ATOM   3629 C  CG  . ASP B 1 153 ? 8.578   5.447   -1.303  1.00 60.91  ? 153 ASP B CG  1 
ATOM   3630 O  OD1 . ASP B 1 153 ? 8.469   6.223   -2.266  1.00 70.71  ? 153 ASP B OD1 1 
ATOM   3631 O  OD2 . ASP B 1 153 ? 7.595   4.951   -0.696  1.00 58.88  ? 153 ASP B OD2 1 
ATOM   3632 N  N   . TYR B 1 154 ? 12.996  3.714   -2.467  1.00 62.89  ? 154 TYR B N   1 
ATOM   3633 C  CA  . TYR B 1 154 ? 14.376  3.162   -2.347  1.00 68.18  ? 154 TYR B CA  1 
ATOM   3634 C  C   . TYR B 1 154 ? 14.317  1.638   -2.202  1.00 69.40  ? 154 TYR B C   1 
ATOM   3635 O  O   . TYR B 1 154 ? 14.058  0.947   -3.212  1.00 70.45  ? 154 TYR B O   1 
ATOM   3636 C  CB  . TYR B 1 154 ? 15.129  3.842   -1.200  1.00 74.33  ? 154 TYR B CB  1 
ATOM   3637 C  CG  . TYR B 1 154 ? 15.099  5.338   -1.327  1.00 82.96  ? 154 TYR B CG  1 
ATOM   3638 C  CD1 . TYR B 1 154 ? 15.945  5.990   -2.212  1.00 83.77  ? 154 TYR B CD1 1 
ATOM   3639 C  CD2 . TYR B 1 154 ? 14.158  6.087   -0.636  1.00 84.02  ? 154 TYR B CD2 1 
ATOM   3640 C  CE1 . TYR B 1 154 ? 15.886  7.364   -2.373  1.00 87.40  ? 154 TYR B CE1 1 
ATOM   3641 C  CE2 . TYR B 1 154 ? 14.087  7.461   -0.784  1.00 85.73  ? 154 TYR B CE2 1 
ATOM   3642 C  CZ  . TYR B 1 154 ? 14.958  8.099   -1.652  1.00 89.40  ? 154 TYR B CZ  1 
ATOM   3643 O  OH  . TYR B 1 154 ? 14.900  9.452   -1.799  1.00 92.14  ? 154 TYR B OH  1 
ATOM   3644 N  N   . ASP B 1 155 ? 14.560  1.136   -0.989  1.00 63.97  ? 155 ASP B N   1 
ATOM   3645 C  CA  . ASP B 1 155 ? 14.596  -0.314  -0.666  1.00 63.49  ? 155 ASP B CA  1 
ATOM   3646 C  C   . ASP B 1 155 ? 13.332  -0.698  0.126   1.00 54.44  ? 155 ASP B C   1 
ATOM   3647 O  O   . ASP B 1 155 ? 13.100  -1.921  0.302   1.00 52.62  ? 155 ASP B O   1 
ATOM   3648 C  CB  . ASP B 1 155 ? 15.872  -0.645  0.114   1.00 67.47  ? 155 ASP B CB  1 
ATOM   3649 C  CG  . ASP B 1 155 ? 16.036  0.210   1.366   1.00 74.02  ? 155 ASP B CG  1 
ATOM   3650 O  OD1 . ASP B 1 155 ? 15.612  1.405   1.342   1.00 71.69  ? 155 ASP B OD1 1 
ATOM   3651 O  OD2 . ASP B 1 155 ? 16.565  -0.324  2.362   1.00 75.21  ? 155 ASP B OD2 1 
ATOM   3652 N  N   . CYS B 1 156 ? 12.532  0.288   0.560   1.00 42.08  ? 156 CYS B N   1 
ATOM   3653 C  CA  . CYS B 1 156 ? 11.407  0.084   1.515   1.00 37.62  ? 156 CYS B CA  1 
ATOM   3654 C  C   . CYS B 1 156 ? 10.091  -0.100  0.745   1.00 31.81  ? 156 CYS B C   1 
ATOM   3655 O  O   . CYS B 1 156 ? 9.707   0.790   -0.013  1.00 27.23  ? 156 CYS B O   1 
ATOM   3656 C  CB  . CYS B 1 156 ? 11.298  1.217   2.529   1.00 36.24  ? 156 CYS B CB  1 
ATOM   3657 S  SG  . CYS B 1 156 ? 9.871   1.041   3.640   1.00 36.91  ? 156 CYS B SG  1 
ATOM   3658 N  N   . VAL B 1 157 ? 9.459   -1.259  0.909   1.00 26.61  ? 157 VAL B N   1 
ATOM   3659 C  CA  . VAL B 1 157 ? 8.118   -1.539  0.342   1.00 27.24  ? 157 VAL B CA  1 
ATOM   3660 C  C   . VAL B 1 157 ? 7.046   -0.998  1.300   1.00 25.60  ? 157 VAL B C   1 
ATOM   3661 O  O   . VAL B 1 157 ? 6.968   -1.453  2.444   1.00 27.50  ? 157 VAL B O   1 
ATOM   3662 C  CB  . VAL B 1 157 ? 7.934   -3.031  0.061   1.00 25.41  ? 157 VAL B CB  1 
ATOM   3663 C  CG1 . VAL B 1 157 ? 6.526   -3.280  -0.461  1.00 26.61  ? 157 VAL B CG1 1 
ATOM   3664 C  CG2 . VAL B 1 157 ? 8.973   -3.528  -0.915  1.00 25.95  ? 157 VAL B CG2 1 
ATOM   3665 N  N   . SER B 1 158 ? 6.228   -0.071  0.835   1.00 21.94  ? 158 SER B N   1 
ATOM   3666 C  CA  . SER B 1 158 ? 5.073   0.462   1.597   1.00 23.04  ? 158 SER B CA  1 
ATOM   3667 C  C   . SER B 1 158 ? 3.814   -0.270  1.123   1.00 20.89  ? 158 SER B C   1 
ATOM   3668 O  O   . SER B 1 158 ? 3.381   0.008   0.013   1.00 20.08  ? 158 SER B O   1 
ATOM   3669 C  CB  . SER B 1 158 ? 4.957   1.961   1.423   1.00 22.08  ? 158 SER B CB  1 
ATOM   3670 O  OG  . SER B 1 158 ? 6.069   2.583   2.039   1.00 25.61  ? 158 SER B OG  1 
ATOM   3671 N  N   . PHE B 1 159 ? 3.283   -1.206  1.908   1.00 20.43  ? 159 PHE B N   1 
ATOM   3672 C  CA  . PHE B 1 159 ? 2.029   -1.936  1.589   1.00 20.64  ? 159 PHE B CA  1 
ATOM   3673 C  C   . PHE B 1 159 ? 0.815   -1.080  1.966   1.00 21.38  ? 159 PHE B C   1 
ATOM   3674 O  O   . PHE B 1 159 ? 0.741   -0.599  3.124   1.00 22.07  ? 159 PHE B O   1 
ATOM   3675 C  CB  . PHE B 1 159 ? 1.947   -3.263  2.323   1.00 20.20  ? 159 PHE B CB  1 
ATOM   3676 C  CG  . PHE B 1 159 ? 3.033   -4.250  1.973   1.00 21.30  ? 159 PHE B CG  1 
ATOM   3677 C  CD1 . PHE B 1 159 ? 2.931   -5.026  0.832   1.00 22.28  ? 159 PHE B CD1 1 
ATOM   3678 C  CD2 . PHE B 1 159 ? 4.086   -4.490  2.851   1.00 22.38  ? 159 PHE B CD2 1 
ATOM   3679 C  CE1 . PHE B 1 159 ? 3.885   -5.989  0.535   1.00 22.87  ? 159 PHE B CE1 1 
ATOM   3680 C  CE2 . PHE B 1 159 ? 5.042   -5.451  2.556   1.00 23.21  ? 159 PHE B CE2 1 
ATOM   3681 C  CZ  . PHE B 1 159 ? 4.960   -6.174  1.384   1.00 22.53  ? 159 PHE B CZ  1 
ATOM   3682 N  N   . CYS B 1 160 ? -0.099  -0.885  1.013   1.00 21.11  ? 160 CYS B N   1 
ATOM   3683 C  CA  . CYS B 1 160 ? -1.214  0.092   1.142   1.00 21.31  ? 160 CYS B CA  1 
ATOM   3684 C  C   . CYS B 1 160 ? -2.576  -0.559  0.878   1.00 20.51  ? 160 CYS B C   1 
ATOM   3685 O  O   . CYS B 1 160 ? -3.584  0.076   1.185   1.00 21.34  ? 160 CYS B O   1 
ATOM   3686 C  CB  . CYS B 1 160 ? -0.979  1.296   0.236   1.00 19.44  ? 160 CYS B CB  1 
ATOM   3687 S  SG  . CYS B 1 160 ? -0.899  0.919   -1.538  1.00 23.18  ? 160 CYS B SG  1 
ATOM   3688 N  N   . TYR B 1 161 ? -2.629  -1.767  0.310   1.00 19.32  ? 161 TYR B N   1 
ATOM   3689 C  CA  . TYR B 1 161 ? -3.911  -2.315  -0.164  1.00 19.93  ? 161 TYR B CA  1 
ATOM   3690 C  C   . TYR B 1 161 ? -3.912  -3.825  -0.000  1.00 19.62  ? 161 TYR B C   1 
ATOM   3691 O  O   . TYR B 1 161 ? -2.906  -4.445  -0.333  1.00 21.30  ? 161 TYR B O   1 
ATOM   3692 C  CB  . TYR B 1 161 ? -4.195  -1.940  -1.622  1.00 20.87  ? 161 TYR B CB  1 
ATOM   3693 C  CG  . TYR B 1 161 ? -5.522  -2.442  -2.151  1.00 20.56  ? 161 TYR B CG  1 
ATOM   3694 C  CD1 . TYR B 1 161 ? -6.699  -1.755  -1.911  1.00 22.19  ? 161 TYR B CD1 1 
ATOM   3695 C  CD2 . TYR B 1 161 ? -5.601  -3.605  -2.908  1.00 20.09  ? 161 TYR B CD2 1 
ATOM   3696 C  CE1 . TYR B 1 161 ? -7.911  -2.220  -2.395  1.00 22.29  ? 161 TYR B CE1 1 
ATOM   3697 C  CE2 . TYR B 1 161 ? -6.795  -4.071  -3.416  1.00 20.34  ? 161 TYR B CE2 1 
ATOM   3698 C  CZ  . TYR B 1 161 ? -7.961  -3.391  -3.134  1.00 20.75  ? 161 TYR B CZ  1 
ATOM   3699 O  OH  . TYR B 1 161 ? -9.158  -3.855  -3.610  1.00 21.00  ? 161 TYR B OH  1 
ATOM   3700 N  N   . MET B 1 162 ? -5.053  -4.360  0.425   1.00 20.15  ? 162 MET B N   1 
ATOM   3701 C  CA  . MET B 1 162 ? -5.330  -5.810  0.390   1.00 21.17  ? 162 MET B CA  1 
ATOM   3702 C  C   . MET B 1 162 ? -6.708  -6.017  -0.236  1.00 21.78  ? 162 MET B C   1 
ATOM   3703 O  O   . MET B 1 162 ? -7.662  -5.312  0.135   1.00 20.50  ? 162 MET B O   1 
ATOM   3704 C  CB  . MET B 1 162 ? -5.276  -6.451  1.772   1.00 23.54  ? 162 MET B CB  1 
ATOM   3705 C  CG  . MET B 1 162 ? -5.527  -7.926  1.672   1.00 27.57  ? 162 MET B CG  1 
ATOM   3706 S  SD  . MET B 1 162 ? -5.231  -8.835  3.192   1.00 31.92  ? 162 MET B SD  1 
ATOM   3707 C  CE  . MET B 1 162 ? -3.596  -9.490  2.869   1.00 32.66  ? 162 MET B CE  1 
ATOM   3708 N  N   . HIS B 1 163 ? -6.771  -6.873  -1.258  1.00 21.74  ? 163 HIS B N   1 
ATOM   3709 C  CA  . HIS B 1 163 ? -8.013  -7.064  -2.046  1.00 21.59  ? 163 HIS B CA  1 
ATOM   3710 C  C   . HIS B 1 163 ? -9.011  -7.940  -1.263  1.00 23.57  ? 163 HIS B C   1 
ATOM   3711 O  O   . HIS B 1 163 ? -8.639  -9.082  -0.831  1.00 23.22  ? 163 HIS B O   1 
ATOM   3712 C  CB  . HIS B 1 163 ? -7.704  -7.633  -3.443  1.00 20.46  ? 163 HIS B CB  1 
ATOM   3713 C  CG  . HIS B 1 163 ? -8.937  -7.783  -4.262  1.00 21.05  ? 163 HIS B CG  1 
ATOM   3714 N  ND1 . HIS B 1 163 ? -9.815  -6.740  -4.487  1.00 22.91  ? 163 HIS B ND1 1 
ATOM   3715 C  CD2 . HIS B 1 163 ? -9.486  -8.859  -4.859  1.00 23.67  ? 163 HIS B CD2 1 
ATOM   3716 C  CE1 . HIS B 1 163 ? -10.845 -7.181  -5.188  1.00 22.64  ? 163 HIS B CE1 1 
ATOM   3717 N  NE2 . HIS B 1 163 ? -10.644 -8.458  -5.459  1.00 21.86  ? 163 HIS B NE2 1 
ATOM   3718 N  N   . HIS B 1 164 ? -10.260 -7.488  -1.173  1.00 23.54  ? 164 HIS B N   1 
ATOM   3719 C  CA  . HIS B 1 164 ? -11.343 -8.193  -0.446  1.00 25.40  ? 164 HIS B CA  1 
ATOM   3720 C  C   . HIS B 1 164 ? -12.532 -8.551  -1.351  1.00 27.05  ? 164 HIS B C   1 
ATOM   3721 O  O   . HIS B 1 164 ? -13.064 -9.637  -1.150  1.00 28.84  ? 164 HIS B O   1 
ATOM   3722 C  CB  . HIS B 1 164 ? -11.825 -7.345  0.730   1.00 25.53  ? 164 HIS B CB  1 
ATOM   3723 C  CG  . HIS B 1 164 ? -10.906 -7.324  1.907   1.00 23.94  ? 164 HIS B CG  1 
ATOM   3724 N  ND1 . HIS B 1 164 ? -11.254 -7.886  3.128   1.00 25.40  ? 164 HIS B ND1 1 
ATOM   3725 C  CD2 . HIS B 1 164 ? -9.665  -6.820  2.060   1.00 23.42  ? 164 HIS B CD2 1 
ATOM   3726 C  CE1 . HIS B 1 164 ? -10.281 -7.673  3.996   1.00 24.90  ? 164 HIS B CE1 1 
ATOM   3727 N  NE2 . HIS B 1 164 ? -9.282  -7.023  3.363   1.00 23.75  ? 164 HIS B NE2 1 
ATOM   3728 N  N   . MET B 1 165 ? -12.963 -7.700  -2.294  1.00 26.25  ? 165 MET B N   1 
ATOM   3729 C  CA  . MET B 1 165 ? -14.227 -8.002  -3.009  1.00 29.81  ? 165 MET B CA  1 
ATOM   3730 C  C   . MET B 1 165 ? -14.359 -7.223  -4.317  1.00 31.68  ? 165 MET B C   1 
ATOM   3731 O  O   . MET B 1 165 ? -13.703 -6.156  -4.507  1.00 26.54  ? 165 MET B O   1 
ATOM   3732 C  CB  . MET B 1 165 ? -15.428 -7.674  -2.106  1.00 30.37  ? 165 MET B CB  1 
ATOM   3733 C  CG  . MET B 1 165 ? -15.598 -6.185  -1.831  1.00 35.67  ? 165 MET B CG  1 
ATOM   3734 S  SD  . MET B 1 165 ? -16.712 -5.742  -0.446  1.00 41.42  ? 165 MET B SD  1 
ATOM   3735 C  CE  . MET B 1 165 ? -16.155 -6.964  0.732   1.00 45.85  ? 165 MET B CE  1 
ATOM   3736 N  N   . GLU B 1 166 ? -15.256 -7.713  -5.168  1.00 30.94  ? 166 GLU B N   1 
ATOM   3737 C  CA  . GLU B 1 166 ? -15.675 -7.014  -6.399  1.00 33.00  ? 166 GLU B CA  1 
ATOM   3738 C  C   . GLU B 1 166 ? -17.082 -6.464  -6.173  1.00 34.24  ? 166 GLU B C   1 
ATOM   3739 O  O   . GLU B 1 166 ? -17.948 -7.216  -5.681  1.00 34.11  ? 166 GLU B O   1 
ATOM   3740 C  CB  . GLU B 1 166 ? -15.608 -7.959  -7.601  1.00 33.25  ? 166 GLU B CB  1 
ATOM   3741 C  CG  . GLU B 1 166 ? -15.894 -7.253  -8.918  1.00 32.91  ? 166 GLU B CG  1 
ATOM   3742 C  CD  . GLU B 1 166 ? -15.712 -8.143  -10.129 1.00 32.68  ? 166 GLU B CD  1 
ATOM   3743 O  OE1 . GLU B 1 166 ? -14.562 -8.446  -10.477 1.00 34.09  ? 166 GLU B OE1 1 
ATOM   3744 O  OE2 . GLU B 1 166 ? -16.728 -8.550  -10.708 1.00 38.13  ? 166 GLU B OE2 1 
ATOM   3745 N  N   . LEU B 1 167 ? -17.300 -5.212  -6.536  1.00 32.00  ? 167 LEU B N   1 
ATOM   3746 C  CA  . LEU B 1 167 ? -18.630 -4.566  -6.487  1.00 31.04  ? 167 LEU B CA  1 
ATOM   3747 C  C   . LEU B 1 167 ? -19.405 -4.878  -7.767  1.00 36.56  ? 167 LEU B C   1 
ATOM   3748 O  O   . LEU B 1 167 ? -18.852 -5.281  -8.800  1.00 34.14  ? 167 LEU B O   1 
ATOM   3749 C  CB  . LEU B 1 167 ? -18.451 -3.056  -6.292  1.00 29.68  ? 167 LEU B CB  1 
ATOM   3750 C  CG  . LEU B 1 167 ? -17.861 -2.651  -4.943  1.00 28.75  ? 167 LEU B CG  1 
ATOM   3751 C  CD1 . LEU B 1 167 ? -17.557 -1.169  -4.900  1.00 28.97  ? 167 LEU B CD1 1 
ATOM   3752 C  CD2 . LEU B 1 167 ? -18.786 -3.046  -3.807  1.00 31.33  ? 167 LEU B CD2 1 
ATOM   3753 N  N   . PRO B 1 168 ? -20.744 -4.717  -7.714  1.00 37.70  ? 168 PRO B N   1 
ATOM   3754 C  CA  . PRO B 1 168 ? -21.621 -5.053  -8.835  1.00 38.43  ? 168 PRO B CA  1 
ATOM   3755 C  C   . PRO B 1 168 ? -21.222 -4.472  -10.196 1.00 39.57  ? 168 PRO B C   1 
ATOM   3756 O  O   . PRO B 1 168 ? -21.509 -5.109  -11.167 1.00 41.52  ? 168 PRO B O   1 
ATOM   3757 C  CB  . PRO B 1 168 ? -22.953 -4.429  -8.390  1.00 38.91  ? 168 PRO B CB  1 
ATOM   3758 C  CG  . PRO B 1 168 ? -22.917 -4.638  -6.905  1.00 42.67  ? 168 PRO B CG  1 
ATOM   3759 C  CD  . PRO B 1 168 ? -21.496 -4.261  -6.534  1.00 40.53  ? 168 PRO B CD  1 
ATOM   3760 N  N   . THR B 1 169 ? -20.592 -3.297  -10.218 1.00 40.21  ? 169 THR B N   1 
ATOM   3761 C  CA  . THR B 1 169 ? -20.193 -2.592  -11.462 1.00 39.18  ? 169 THR B CA  1 
ATOM   3762 C  C   . THR B 1 169 ? -18.855 -3.100  -12.029 1.00 38.53  ? 169 THR B C   1 
ATOM   3763 O  O   . THR B 1 169 ? -18.457 -2.552  -13.062 1.00 38.08  ? 169 THR B O   1 
ATOM   3764 C  CB  . THR B 1 169 ? -20.127 -1.086  -11.203 1.00 39.16  ? 169 THR B CB  1 
ATOM   3765 O  OG1 . THR B 1 169 ? -19.316 -0.907  -10.043 1.00 39.80  ? 169 THR B OG1 1 
ATOM   3766 C  CG2 . THR B 1 169 ? -21.500 -0.491  -10.988 1.00 40.50  ? 169 THR B CG2 1 
ATOM   3767 N  N   . GLY B 1 170 ? -18.172 -4.076  -11.415 1.00 37.27  ? 170 GLY B N   1 
ATOM   3768 C  CA  . GLY B 1 170 ? -16.874 -4.589  -11.918 1.00 34.68  ? 170 GLY B CA  1 
ATOM   3769 C  C   . GLY B 1 170 ? -15.654 -3.921  -11.286 1.00 35.18  ? 170 GLY B C   1 
ATOM   3770 O  O   . GLY B 1 170 ? -14.528 -4.328  -11.609 1.00 39.74  ? 170 GLY B O   1 
ATOM   3771 N  N   . VAL B 1 171 ? -15.844 -2.957  -10.384 1.00 29.85  ? 171 VAL B N   1 
ATOM   3772 C  CA  . VAL B 1 171 ? -14.738 -2.282  -9.653  1.00 27.79  ? 171 VAL B CA  1 
ATOM   3773 C  C   . VAL B 1 171 ? -14.513 -3.007  -8.320  1.00 27.37  ? 171 VAL B C   1 
ATOM   3774 O  O   . VAL B 1 171 ? -15.318 -3.922  -7.978  1.00 26.57  ? 171 VAL B O   1 
ATOM   3775 C  CB  . VAL B 1 171 ? -14.998 -0.765  -9.490  1.00 30.56  ? 171 VAL B CB  1 
ATOM   3776 C  CG1 . VAL B 1 171 ? -15.124 -0.093  -10.864 1.00 30.70  ? 171 VAL B CG1 1 
ATOM   3777 C  CG2 . VAL B 1 171 ? -16.211 -0.460  -8.606  1.00 29.91  ? 171 VAL B CG2 1 
ATOM   3778 N  N   . HIS B 1 172 ? -13.397 -2.692  -7.653  1.00 26.04  ? 172 HIS B N   1 
ATOM   3779 C  CA  . HIS B 1 172 ? -12.814 -3.537  -6.569  1.00 26.04  ? 172 HIS B CA  1 
ATOM   3780 C  C   . HIS B 1 172 ? -12.673 -2.738  -5.277  1.00 22.66  ? 172 HIS B C   1 
ATOM   3781 O  O   . HIS B 1 172 ? -12.452 -1.512  -5.326  1.00 25.09  ? 172 HIS B O   1 
ATOM   3782 C  CB  . HIS B 1 172 ? -11.512 -4.179  -7.062  1.00 25.85  ? 172 HIS B CB  1 
ATOM   3783 C  CG  . HIS B 1 172 ? -11.751 -5.016  -8.277  1.00 30.04  ? 172 HIS B CG  1 
ATOM   3784 N  ND1 . HIS B 1 172 ? -11.362 -4.622  -9.539  1.00 27.95  ? 172 HIS B ND1 1 
ATOM   3785 C  CD2 . HIS B 1 172 ? -12.412 -6.186  -8.436  1.00 30.46  ? 172 HIS B CD2 1 
ATOM   3786 C  CE1 . HIS B 1 172 ? -11.744 -5.522  -10.416 1.00 29.32  ? 172 HIS B CE1 1 
ATOM   3787 N  NE2 . HIS B 1 172 ? -12.388 -6.492  -9.765  1.00 30.22  ? 172 HIS B NE2 1 
ATOM   3788 N  N   . ALA B 1 173 ? -12.830 -3.410  -4.147  1.00 21.43  ? 173 ALA B N   1 
ATOM   3789 C  CA  . ALA B 1 173 ? -12.773 -2.788  -2.815  1.00 21.28  ? 173 ALA B CA  1 
ATOM   3790 C  C   . ALA B 1 173 ? -11.903 -3.638  -1.903  1.00 21.80  ? 173 ALA B C   1 
ATOM   3791 O  O   . ALA B 1 173 ? -11.959 -4.887  -2.016  1.00 24.18  ? 173 ALA B O   1 
ATOM   3792 C  CB  . ALA B 1 173 ? -14.160 -2.653  -2.251  1.00 21.72  ? 173 ALA B CB  1 
ATOM   3793 N  N   . GLY B 1 174 ? -11.155 -2.974  -1.027  1.00 21.76  ? 174 GLY B N   1 
ATOM   3794 C  CA  . GLY B 1 174 ? -10.258 -3.638  -0.073  1.00 20.99  ? 174 GLY B CA  1 
ATOM   3795 C  C   . GLY B 1 174 ? -9.881  -2.723  1.080   1.00 20.98  ? 174 GLY B C   1 
ATOM   3796 O  O   . GLY B 1 174 ? -10.497 -1.648  1.255   1.00 18.93  ? 174 GLY B O   1 
ATOM   3797 N  N   . THR B 1 175 ? -8.869  -3.152  1.821   1.00 21.17  ? 175 THR B N   1 
ATOM   3798 C  CA  . THR B 1 175 ? -8.465  -2.560  3.108   1.00 21.10  ? 175 THR B CA  1 
ATOM   3799 C  C   . THR B 1 175 ? -7.020  -2.133  3.003   1.00 20.39  ? 175 THR B C   1 
ATOM   3800 O  O   . THR B 1 175 ? -6.328  -2.586  2.082   1.00 22.05  ? 175 THR B O   1 
ATOM   3801 C  CB  . THR B 1 175 ? -8.635  -3.558  4.252   1.00 20.87  ? 175 THR B CB  1 
ATOM   3802 O  OG1 . THR B 1 175 ? -7.760  -4.671  4.044   1.00 20.01  ? 175 THR B OG1 1 
ATOM   3803 C  CG2 . THR B 1 175 ? -10.073 -4.013  4.366   1.00 22.22  ? 175 THR B CG2 1 
ATOM   3804 N  N   . ASP B 1 176 ? -6.597  -1.309  3.942   1.00 20.62  ? 176 ASP B N   1 
ATOM   3805 C  CA  . ASP B 1 176 ? -5.158  -1.140  4.173   1.00 21.06  ? 176 ASP B CA  1 
ATOM   3806 C  C   . ASP B 1 176 ? -4.712  -2.412  4.889   1.00 21.35  ? 176 ASP B C   1 
ATOM   3807 O  O   . ASP B 1 176 ? -5.562  -3.333  5.104   1.00 18.47  ? 176 ASP B O   1 
ATOM   3808 C  CB  . ASP B 1 176 ? -4.890  0.155   4.909   1.00 22.14  ? 176 ASP B CB  1 
ATOM   3809 C  CG  . ASP B 1 176 ? -5.527  0.201   6.276   1.00 23.16  ? 176 ASP B CG  1 
ATOM   3810 O  OD1 . ASP B 1 176 ? -5.802  -0.878  6.854   1.00 24.24  ? 176 ASP B OD1 1 
ATOM   3811 O  OD2 . ASP B 1 176 ? -5.767  1.293   6.713   1.00 20.51  ? 176 ASP B OD2 1 
ATOM   3812 N  N   . LEU B 1 177 ? -3.441  -2.486  5.274   1.00 20.74  ? 177 LEU B N   1 
ATOM   3813 C  CA  . LEU B 1 177 ? -2.914  -3.744  5.847   1.00 20.18  ? 177 LEU B CA  1 
ATOM   3814 C  C   . LEU B 1 177 ? -3.246  -3.815  7.330   1.00 22.63  ? 177 LEU B C   1 
ATOM   3815 O  O   . LEU B 1 177 ? -2.878  -4.816  7.954   1.00 25.73  ? 177 LEU B O   1 
ATOM   3816 C  CB  . LEU B 1 177 ? -1.411  -3.848  5.577   1.00 21.65  ? 177 LEU B CB  1 
ATOM   3817 C  CG  . LEU B 1 177 ? -1.080  -4.717  4.372   1.00 23.28  ? 177 LEU B CG  1 
ATOM   3818 C  CD1 . LEU B 1 177 ? -1.451  -6.169  4.624   1.00 25.36  ? 177 LEU B CD1 1 
ATOM   3819 C  CD2 . LEU B 1 177 ? -1.769  -4.213  3.117   1.00 23.01  ? 177 LEU B CD2 1 
ATOM   3820 N  N   . GLU B 1 178 ? -3.910  -2.802  7.877   1.00 23.47  ? 178 GLU B N   1 
ATOM   3821 C  CA  . GLU B 1 178 ? -4.402  -2.823  9.272   1.00 24.31  ? 178 GLU B CA  1 
ATOM   3822 C  C   . GLU B 1 178 ? -5.895  -3.171  9.250   1.00 24.40  ? 178 GLU B C   1 
ATOM   3823 O  O   . GLU B 1 178 ? -6.523  -3.107  10.317  1.00 26.17  ? 178 GLU B O   1 
ATOM   3824 C  CB  . GLU B 1 178 ? -4.107  -1.491  9.963   1.00 27.64  ? 178 GLU B CB  1 
ATOM   3825 C  CG  . GLU B 1 178 ? -2.618  -1.190  10.093  1.00 31.28  ? 178 GLU B CG  1 
ATOM   3826 C  CD  . GLU B 1 178 ? -2.341  0.053   10.923  1.00 38.61  ? 178 GLU B CD  1 
ATOM   3827 O  OE1 . GLU B 1 178 ? -3.109  1.002   10.828  1.00 42.77  ? 178 GLU B OE1 1 
ATOM   3828 O  OE2 . GLU B 1 178 ? -1.379  0.048   11.689  1.00 58.12  ? 178 GLU B OE2 1 
ATOM   3829 N  N   . GLY B 1 179 ? -6.447  -3.492  8.074   1.00 22.87  ? 179 GLY B N   1 
ATOM   3830 C  CA  . GLY B 1 179 ? -7.820  -4.021  7.926   1.00 22.95  ? 179 GLY B CA  1 
ATOM   3831 C  C   . GLY B 1 179 ? -8.909  -2.964  7.867   1.00 22.32  ? 179 GLY B C   1 
ATOM   3832 O  O   . GLY B 1 179 ? -10.085 -3.347  7.978   1.00 26.15  ? 179 GLY B O   1 
ATOM   3833 N  N   . ASN B 1 180 ? -8.566  -1.685  7.739   1.00 22.78  ? 180 ASN B N   1 
ATOM   3834 C  CA  . ASN B 1 180 ? -9.563  -0.607  7.559   1.00 22.44  ? 180 ASN B CA  1 
ATOM   3835 C  C   . ASN B 1 180 ? -9.926  -0.511  6.083   1.00 23.08  ? 180 ASN B C   1 
ATOM   3836 O  O   . ASN B 1 180 ? -9.004  -0.310  5.239   1.00 21.09  ? 180 ASN B O   1 
ATOM   3837 C  CB  . ASN B 1 180 ? -9.030  0.747   8.003   1.00 25.84  ? 180 ASN B CB  1 
ATOM   3838 C  CG  . ASN B 1 180 ? -8.455  0.740   9.397   1.00 31.45  ? 180 ASN B CG  1 
ATOM   3839 O  OD1 . ASN B 1 180 ? -9.165  0.437   10.354  1.00 28.20  ? 180 ASN B OD1 1 
ATOM   3840 N  ND2 . ASN B 1 180 ? -7.182  1.122   9.508   1.00 32.09  ? 180 ASN B ND2 1 
ATOM   3841 N  N   . PHE B 1 181 ? -11.209 -0.617  5.767   1.00 23.22  ? 181 PHE B N   1 
ATOM   3842 C  CA  . PHE B 1 181 ? -11.694 -0.454  4.374   1.00 23.55  ? 181 PHE B CA  1 
ATOM   3843 C  C   . PHE B 1 181 ? -11.305 0.931   3.846   1.00 23.96  ? 181 PHE B C   1 
ATOM   3844 O  O   . PHE B 1 181 ? -11.305 1.935   4.605   1.00 22.44  ? 181 PHE B O   1 
ATOM   3845 C  CB  . PHE B 1 181 ? -13.203 -0.669  4.247   1.00 23.14  ? 181 PHE B CB  1 
ATOM   3846 C  CG  . PHE B 1 181 ? -13.513 -2.045  3.727   1.00 23.23  ? 181 PHE B CG  1 
ATOM   3847 C  CD1 . PHE B 1 181 ? -13.448 -2.318  2.373   1.00 24.16  ? 181 PHE B CD1 1 
ATOM   3848 C  CD2 . PHE B 1 181 ? -13.717 -3.082  4.608   1.00 23.20  ? 181 PHE B CD2 1 
ATOM   3849 C  CE1 . PHE B 1 181 ? -13.650 -3.609  1.916   1.00 26.30  ? 181 PHE B CE1 1 
ATOM   3850 C  CE2 . PHE B 1 181 ? -13.921 -4.368  4.149   1.00 24.21  ? 181 PHE B CE2 1 
ATOM   3851 C  CZ  . PHE B 1 181 ? -13.888 -4.625  2.803   1.00 25.68  ? 181 PHE B CZ  1 
ATOM   3852 N  N   . TYR B 1 182 ? -10.945 0.977   2.561   1.00 22.95  ? 182 TYR B N   1 
ATOM   3853 C  CA  . TYR B 1 182 ? -11.033 2.195   1.726   1.00 21.53  ? 182 TYR B CA  1 
ATOM   3854 C  C   . TYR B 1 182 ? -12.491 2.293   1.268   1.00 21.29  ? 182 TYR B C   1 
ATOM   3855 O  O   . TYR B 1 182 ? -12.938 1.379   0.588   1.00 24.26  ? 182 TYR B O   1 
ATOM   3856 C  CB  . TYR B 1 182 ? -10.098 2.114   0.527   1.00 21.86  ? 182 TYR B CB  1 
ATOM   3857 C  CG  . TYR B 1 182 ? -8.642  2.184   0.900   1.00 22.47  ? 182 TYR B CG  1 
ATOM   3858 C  CD1 . TYR B 1 182 ? -8.047  3.394   1.227   1.00 23.44  ? 182 TYR B CD1 1 
ATOM   3859 C  CD2 . TYR B 1 182 ? -7.867  1.036   0.968   1.00 20.40  ? 182 TYR B CD2 1 
ATOM   3860 C  CE1 . TYR B 1 182 ? -6.703  3.460   1.567   1.00 23.65  ? 182 TYR B CE1 1 
ATOM   3861 C  CE2 . TYR B 1 182 ? -6.534  1.088   1.333   1.00 18.88  ? 182 TYR B CE2 1 
ATOM   3862 C  CZ  . TYR B 1 182 ? -5.943  2.298   1.627   1.00 21.26  ? 182 TYR B CZ  1 
ATOM   3863 O  OH  . TYR B 1 182 ? -4.600  2.331   1.950   1.00 19.51  ? 182 TYR B OH  1 
ATOM   3864 N  N   . GLY B 1 183 ? -13.203 3.333   1.695   1.00 20.32  ? 183 GLY B N   1 
ATOM   3865 C  CA  . GLY B 1 183 ? -14.573 3.631   1.230   1.00 22.09  ? 183 GLY B CA  1 
ATOM   3866 C  C   . GLY B 1 183 ? -15.623 3.037   2.161   1.00 22.14  ? 183 GLY B C   1 
ATOM   3867 O  O   . GLY B 1 183 ? -15.295 2.317   3.116   1.00 23.83  ? 183 GLY B O   1 
ATOM   3868 N  N   . PRO B 1 184 ? -16.914 3.297   1.868   1.00 23.70  ? 184 PRO B N   1 
ATOM   3869 C  CA  . PRO B 1 184 ? -18.013 2.931   2.766   1.00 25.43  ? 184 PRO B CA  1 
ATOM   3870 C  C   . PRO B 1 184 ? -18.529 1.491   2.604   1.00 29.63  ? 184 PRO B C   1 
ATOM   3871 O  O   . PRO B 1 184 ? -19.749 1.292   2.428   1.00 27.47  ? 184 PRO B O   1 
ATOM   3872 C  CB  . PRO B 1 184 ? -19.092 3.975   2.416   1.00 25.39  ? 184 PRO B CB  1 
ATOM   3873 C  CG  . PRO B 1 184 ? -18.843 4.336   0.960   1.00 25.53  ? 184 PRO B CG  1 
ATOM   3874 C  CD  . PRO B 1 184 ? -17.348 4.162   0.757   1.00 25.77  ? 184 PRO B CD  1 
ATOM   3875 N  N   . PHE B 1 185 ? -17.616 0.516   2.703   1.00 25.18  ? 185 PHE B N   1 
ATOM   3876 C  CA  . PHE B 1 185 ? -17.876 -0.905  2.351   1.00 24.56  ? 185 PHE B CA  1 
ATOM   3877 C  C   . PHE B 1 185 ? -17.702 -1.772  3.590   1.00 25.32  ? 185 PHE B C   1 
ATOM   3878 O  O   . PHE B 1 185 ? -16.988 -1.407  4.516   1.00 23.75  ? 185 PHE B O   1 
ATOM   3879 C  CB  . PHE B 1 185 ? -17.017 -1.362  1.160   1.00 26.13  ? 185 PHE B CB  1 
ATOM   3880 C  CG  . PHE B 1 185 ? -17.100 -0.404  -0.006  1.00 25.48  ? 185 PHE B CG  1 
ATOM   3881 C  CD1 . PHE B 1 185 ? -18.297 -0.214  -0.688  1.00 24.78  ? 185 PHE B CD1 1 
ATOM   3882 C  CD2 . PHE B 1 185 ? -16.010 0.368   -0.361  1.00 25.10  ? 185 PHE B CD2 1 
ATOM   3883 C  CE1 . PHE B 1 185 ? -18.397 0.727   -1.701  1.00 26.29  ? 185 PHE B CE1 1 
ATOM   3884 C  CE2 . PHE B 1 185 ? -16.099 1.277   -1.403  1.00 25.61  ? 185 PHE B CE2 1 
ATOM   3885 C  CZ  . PHE B 1 185 ? -17.297 1.474   -2.058  1.00 26.45  ? 185 PHE B CZ  1 
ATOM   3886 N  N   . VAL B 1 186 ? -18.348 -2.926  3.571   1.00 25.29  ? 186 VAL B N   1 
ATOM   3887 C  CA  . VAL B 1 186 ? -18.244 -3.935  4.651   1.00 26.81  ? 186 VAL B CA  1 
ATOM   3888 C  C   . VAL B 1 186 ? -17.977 -5.279  3.986   1.00 27.88  ? 186 VAL B C   1 
ATOM   3889 O  O   . VAL B 1 186 ? -18.435 -5.473  2.820   1.00 28.44  ? 186 VAL B O   1 
ATOM   3890 C  CB  . VAL B 1 186 ? -19.535 -3.972  5.476   1.00 30.25  ? 186 VAL B CB  1 
ATOM   3891 C  CG1 . VAL B 1 186 ? -19.820 -2.634  6.125   1.00 32.13  ? 186 VAL B CG1 1 
ATOM   3892 C  CG2 . VAL B 1 186 ? -20.700 -4.430  4.609   1.00 29.23  ? 186 VAL B CG2 1 
ATOM   3893 N  N   . ASP B 1 187 ? -17.272 -6.155  4.693   1.00 27.33  ? 187 ASP B N   1 
ATOM   3894 C  CA  . ASP B 1 187 ? -16.964 -7.542  4.251   1.00 29.85  ? 187 ASP B CA  1 
ATOM   3895 C  C   . ASP B 1 187 ? -18.134 -8.475  4.619   1.00 31.50  ? 187 ASP B C   1 
ATOM   3896 O  O   . ASP B 1 187 ? -17.957 -9.402  5.428   1.00 35.02  ? 187 ASP B O   1 
ATOM   3897 C  CB  . ASP B 1 187 ? -15.621 -7.996  4.810   1.00 27.44  ? 187 ASP B CB  1 
ATOM   3898 C  CG  . ASP B 1 187 ? -15.475 -7.883  6.315   1.00 26.79  ? 187 ASP B CG  1 
ATOM   3899 O  OD1 . ASP B 1 187 ? -16.377 -7.354  6.968   1.00 29.62  ? 187 ASP B OD1 1 
ATOM   3900 O  OD2 . ASP B 1 187 ? -14.456 -8.320  6.811   1.00 25.39  ? 187 ASP B OD2 1 
ATOM   3901 N  N   . ARG B 1 188 ? -19.283 -8.263  4.003   1.00 36.97  ? 188 ARG B N   1 
ATOM   3902 C  CA  . ARG B 1 188 ? -20.394 -9.248  3.995   1.00 44.40  ? 188 ARG B CA  1 
ATOM   3903 C  C   . ARG B 1 188 ? -21.058 -9.233  2.619   1.00 44.23  ? 188 ARG B C   1 
ATOM   3904 O  O   . ARG B 1 188 ? -21.081 -8.158  1.961   1.00 36.43  ? 188 ARG B O   1 
ATOM   3905 C  CB  . ARG B 1 188 ? -21.407 -8.959  5.110   1.00 51.25  ? 188 ARG B CB  1 
ATOM   3906 C  CG  . ARG B 1 188 ? -22.538 -8.012  4.733   1.00 58.70  ? 188 ARG B CG  1 
ATOM   3907 C  CD  . ARG B 1 188 ? -23.321 -7.565  5.956   1.00 64.11  ? 188 ARG B CD  1 
ATOM   3908 N  NE  . ARG B 1 188 ? -22.351 -7.104  6.940   1.00 74.22  ? 188 ARG B NE  1 
ATOM   3909 C  CZ  . ARG B 1 188 ? -22.454 -7.240  8.255   1.00 79.44  ? 188 ARG B CZ  1 
ATOM   3910 N  NH1 . ARG B 1 188 ? -23.511 -7.827  8.794   1.00 89.63  ? 188 ARG B NH1 1 
ATOM   3911 N  NH2 . ARG B 1 188 ? -21.475 -6.803  9.027   1.00 76.55  ? 188 ARG B NH2 1 
ATOM   3912 N  N   . GLN B 1 189 ? -21.583 -10.387 2.206   1.00 49.99  ? 189 GLN B N   1 
ATOM   3913 C  CA  . GLN B 1 189 ? -22.468 -10.487 1.024   1.00 55.37  ? 189 GLN B CA  1 
ATOM   3914 C  C   . GLN B 1 189 ? -23.744 -9.712  1.364   1.00 56.68  ? 189 GLN B C   1 
ATOM   3915 O  O   . GLN B 1 189 ? -24.565 -10.227 2.136   1.00 55.95  ? 189 GLN B O   1 
ATOM   3916 C  CB  . GLN B 1 189 ? -22.742 -11.943 0.647   1.00 60.80  ? 189 GLN B CB  1 
ATOM   3917 C  CG  . GLN B 1 189 ? -23.714 -12.085 -0.513  1.00 67.02  ? 189 GLN B CG  1 
ATOM   3918 C  CD  . GLN B 1 189 ? -23.369 -11.167 -1.663  1.00 74.93  ? 189 GLN B CD  1 
ATOM   3919 O  OE1 . GLN B 1 189 ? -23.952 -10.094 -1.828  1.00 81.47  ? 189 GLN B OE1 1 
ATOM   3920 N  NE2 . GLN B 1 189 ? -22.389 -11.574 -2.452  1.00 74.54  ? 189 GLN B NE2 1 
ATOM   3921 N  N   . THR B 1 190 ? -23.835 -8.476  0.871   1.00 53.12  ? 190 THR B N   1 
ATOM   3922 C  CA  . THR B 1 190 ? -25.007 -7.578  0.996   1.00 51.77  ? 190 THR B CA  1 
ATOM   3923 C  C   . THR B 1 190 ? -24.993 -6.657  -0.222  1.00 52.65  ? 190 THR B C   1 
ATOM   3924 O  O   . THR B 1 190 ? -24.148 -6.869  -1.111  1.00 58.72  ? 190 THR B O   1 
ATOM   3925 C  CB  . THR B 1 190 ? -25.035 -6.831  2.338   1.00 53.60  ? 190 THR B CB  1 
ATOM   3926 O  OG1 . THR B 1 190 ? -26.366 -6.371  2.552   1.00 49.57  ? 190 THR B OG1 1 
ATOM   3927 C  CG2 . THR B 1 190 ? -24.119 -5.627  2.418   1.00 54.18  ? 190 THR B CG2 1 
ATOM   3928 N  N   . ALA B 1 191 ? -25.917 -5.697  -0.250  1.00 53.80  ? 191 ALA B N   1 
ATOM   3929 C  CA  . ALA B 1 191 ? -26.127 -4.734  -1.354  1.00 48.46  ? 191 ALA B CA  1 
ATOM   3930 C  C   . ALA B 1 191 ? -25.195 -3.546  -1.132  1.00 40.67  ? 191 ALA B C   1 
ATOM   3931 O  O   . ALA B 1 191 ? -25.389 -2.828  -0.115  1.00 41.41  ? 191 ALA B O   1 
ATOM   3932 C  CB  . ALA B 1 191 ? -27.579 -4.311  -1.374  1.00 46.03  ? 191 ALA B CB  1 
ATOM   3933 N  N   . GLN B 1 192 ? -24.181 -3.390  -1.986  1.00 37.35  ? 192 GLN B N   1 
ATOM   3934 C  CA  . GLN B 1 192 ? -23.199 -2.274  -1.901  1.00 34.16  ? 192 GLN B CA  1 
ATOM   3935 C  C   . GLN B 1 192 ? -22.879 -1.805  -3.312  1.00 36.49  ? 192 GLN B C   1 
ATOM   3936 O  O   . GLN B 1 192 ? -22.770 -2.661  -4.215  1.00 42.30  ? 192 GLN B O   1 
ATOM   3937 C  CB  . GLN B 1 192 ? -21.905 -2.685  -1.195  1.00 32.71  ? 192 GLN B CB  1 
ATOM   3938 C  CG  . GLN B 1 192 ? -22.084 -3.711  -0.088  1.00 29.91  ? 192 GLN B CG  1 
ATOM   3939 C  CD  . GLN B 1 192 ? -20.833 -3.872  0.740   1.00 30.39  ? 192 GLN B CD  1 
ATOM   3940 O  OE1 . GLN B 1 192 ? -20.263 -2.895  1.211   1.00 30.07  ? 192 GLN B OE1 1 
ATOM   3941 N  NE2 . GLN B 1 192 ? -20.406 -5.110  0.935   1.00 29.44  ? 192 GLN B NE2 1 
ATOM   3942 N  N   . ALA B 1 193 ? -22.762 -0.495  -3.488  1.00 37.39  ? 193 ALA B N   1 
ATOM   3943 C  CA  . ALA B 1 193 ? -22.456 0.145   -4.784  1.00 38.85  ? 193 ALA B CA  1 
ATOM   3944 C  C   . ALA B 1 193 ? -21.367 1.201   -4.575  1.00 40.00  ? 193 ALA B C   1 
ATOM   3945 O  O   . ALA B 1 193 ? -21.357 1.880   -3.550  1.00 36.37  ? 193 ALA B O   1 
ATOM   3946 C  CB  . ALA B 1 193 ? -23.696 0.766   -5.377  1.00 37.30  ? 193 ALA B CB  1 
ATOM   3947 N  N   . ALA B 1 194 ? -20.502 1.346   -5.564  1.00 44.83  ? 194 ALA B N   1 
ATOM   3948 C  CA  . ALA B 1 194 ? -19.565 2.476   -5.660  1.00 48.53  ? 194 ALA B CA  1 
ATOM   3949 C  C   . ALA B 1 194 ? -20.377 3.768   -5.830  1.00 49.49  ? 194 ALA B C   1 
ATOM   3950 O  O   . ALA B 1 194 ? -21.294 3.790   -6.683  1.00 46.64  ? 194 ALA B O   1 
ATOM   3951 C  CB  . ALA B 1 194 ? -18.632 2.227   -6.820  1.00 51.62  ? 194 ALA B CB  1 
ATOM   3952 N  N   . GLY B 1 195 ? -20.078 4.784   -5.016  1.00 46.02  ? 195 GLY B N   1 
ATOM   3953 C  CA  . GLY B 1 195 ? -20.526 6.174   -5.215  1.00 42.08  ? 195 GLY B CA  1 
ATOM   3954 C  C   . GLY B 1 195 ? -20.183 6.662   -6.610  1.00 42.47  ? 195 GLY B C   1 
ATOM   3955 O  O   . GLY B 1 195 ? -19.355 6.028   -7.301  1.00 37.08  ? 195 GLY B O   1 
ATOM   3956 N  N   . THR B 1 196 ? -20.813 7.741   -7.062  1.00 41.19  ? 196 THR B N   1 
ATOM   3957 C  CA  . THR B 1 196 ? -20.467 8.350   -8.367  1.00 40.63  ? 196 THR B CA  1 
ATOM   3958 C  C   . THR B 1 196 ? -19.002 8.796   -8.238  1.00 38.26  ? 196 THR B C   1 
ATOM   3959 O  O   . THR B 1 196 ? -18.619 9.372   -7.208  1.00 39.42  ? 196 THR B O   1 
ATOM   3960 C  CB  . THR B 1 196 ? -21.509 9.397   -8.795  1.00 45.12  ? 196 THR B CB  1 
ATOM   3961 O  OG1 . THR B 1 196 ? -21.551 10.471  -7.860  1.00 51.62  ? 196 THR B OG1 1 
ATOM   3962 C  CG2 . THR B 1 196 ? -22.907 8.826   -8.901  1.00 43.53  ? 196 THR B CG2 1 
ATOM   3963 N  N   . ASP B 1 197 ? -18.187 8.438   -9.214  1.00 37.60  ? 197 ASP B N   1 
ATOM   3964 C  CA  . ASP B 1 197 ? -16.740 8.742   -9.218  1.00 35.09  ? 197 ASP B CA  1 
ATOM   3965 C  C   . ASP B 1 197 ? -16.521 10.139  -9.787  1.00 34.58  ? 197 ASP B C   1 
ATOM   3966 O  O   . ASP B 1 197 ? -17.414 10.684  -10.443 1.00 36.19  ? 197 ASP B O   1 
ATOM   3967 C  CB  . ASP B 1 197 ? -15.979 7.705   -10.033 1.00 33.14  ? 197 ASP B CB  1 
ATOM   3968 C  CG  . ASP B 1 197 ? -14.555 7.468   -9.540  1.00 33.17  ? 197 ASP B CG  1 
ATOM   3969 O  OD1 . ASP B 1 197 ? -14.137 8.082   -8.492  1.00 29.93  ? 197 ASP B OD1 1 
ATOM   3970 O  OD2 . ASP B 1 197 ? -13.896 6.650   -10.178 1.00 33.24  ? 197 ASP B OD2 1 
ATOM   3971 N  N   . THR B 1 198 ? -15.346 10.690  -9.538  1.00 35.26  ? 198 THR B N   1 
ATOM   3972 C  CA  . THR B 1 198 ? -14.916 11.978  -10.121 1.00 37.68  ? 198 THR B CA  1 
ATOM   3973 C  C   . THR B 1 198 ? -13.561 11.755  -10.777 1.00 34.10  ? 198 THR B C   1 
ATOM   3974 O  O   . THR B 1 198 ? -12.893 10.741  -10.462 1.00 31.76  ? 198 THR B O   1 
ATOM   3975 C  CB  . THR B 1 198 ? -14.875 13.085  -9.064  1.00 39.92  ? 198 THR B CB  1 
ATOM   3976 O  OG1 . THR B 1 198 ? -14.341 12.508  -7.874  1.00 40.20  ? 198 THR B OG1 1 
ATOM   3977 C  CG2 . THR B 1 198 ? -16.234 13.691  -8.788  1.00 43.79  ? 198 THR B CG2 1 
ATOM   3978 N  N   . THR B 1 199 ? -13.161 12.706  -11.604 1.00 32.23  ? 199 THR B N   1 
ATOM   3979 C  CA  . THR B 1 199 ? -11.846 12.689  -12.283 1.00 28.84  ? 199 THR B CA  1 
ATOM   3980 C  C   . THR B 1 199 ? -10.798 13.347  -11.387 1.00 26.78  ? 199 THR B C   1 
ATOM   3981 O  O   . THR B 1 199 ? -11.061 14.441  -10.786 1.00 27.79  ? 199 THR B O   1 
ATOM   3982 C  CB  . THR B 1 199 ? -11.938 13.299  -13.685 1.00 27.30  ? 199 THR B CB  1 
ATOM   3983 O  OG1 . THR B 1 199 ? -12.868 12.501  -14.408 1.00 30.08  ? 199 THR B OG1 1 
ATOM   3984 C  CG2 . THR B 1 199 ? -10.617 13.250  -14.413 1.00 30.34  ? 199 THR B CG2 1 
ATOM   3985 N  N   . ILE B 1 200 ? -9.613  12.750  -11.348 1.00 23.66  ? 200 ILE B N   1 
ATOM   3986 C  CA  . ILE B 1 200 ? -8.515  13.256  -10.490 1.00 24.77  ? 200 ILE B CA  1 
ATOM   3987 C  C   . ILE B 1 200 ? -7.786  14.359  -11.259 1.00 28.45  ? 200 ILE B C   1 
ATOM   3988 O  O   . ILE B 1 200 ? -6.876  14.066  -12.040 1.00 25.54  ? 200 ILE B O   1 
ATOM   3989 C  CB  . ILE B 1 200 ? -7.578  12.129  -10.027 1.00 24.20  ? 200 ILE B CB  1 
ATOM   3990 C  CG1 . ILE B 1 200 ? -8.343  10.913  -9.496  1.00 23.07  ? 200 ILE B CG1 1 
ATOM   3991 C  CG2 . ILE B 1 200 ? -6.574  12.660  -9.013  1.00 22.64  ? 200 ILE B CG2 1 
ATOM   3992 C  CD1 . ILE B 1 200 ? -7.570  9.621   -9.604  1.00 24.30  ? 200 ILE B CD1 1 
ATOM   3993 N  N   . THR B 1 201 ? -8.109  15.617  -10.952 1.00 30.71  ? 201 THR B N   1 
ATOM   3994 C  CA  . THR B 1 201 ? -7.669  16.797  -11.729 1.00 28.07  ? 201 THR B CA  1 
ATOM   3995 C  C   . THR B 1 201 ? -6.144  16.901  -11.756 1.00 27.72  ? 201 THR B C   1 
ATOM   3996 O  O   . THR B 1 201 ? -5.550  17.108  -12.854 1.00 26.68  ? 201 THR B O   1 
ATOM   3997 C  CB  . THR B 1 201 ? -8.325  18.064  -11.169 1.00 28.78  ? 201 THR B CB  1 
ATOM   3998 O  OG1 . THR B 1 201 ? -9.716  17.782  -11.048 1.00 26.97  ? 201 THR B OG1 1 
ATOM   3999 C  CG2 . THR B 1 201 ? -8.108  19.254  -12.073 1.00 31.74  ? 201 THR B CG2 1 
ATOM   4000 N  N   . VAL B 1 202 ? -5.509  16.816  -10.597 1.00 26.33  ? 202 VAL B N   1 
ATOM   4001 C  CA  . VAL B 1 202 ? -4.045  17.055  -10.506 1.00 26.12  ? 202 VAL B CA  1 
ATOM   4002 C  C   . VAL B 1 202 ? -3.278  15.995  -11.315 1.00 25.95  ? 202 VAL B C   1 
ATOM   4003 O  O   . VAL B 1 202 ? -2.171  16.311  -11.816 1.00 25.82  ? 202 VAL B O   1 
ATOM   4004 C  CB  . VAL B 1 202 ? -3.579  17.120  -9.048  1.00 26.66  ? 202 VAL B CB  1 
ATOM   4005 C  CG1 . VAL B 1 202 ? -3.858  15.819  -8.300  1.00 28.70  ? 202 VAL B CG1 1 
ATOM   4006 C  CG2 . VAL B 1 202 ? -2.112  17.499  -8.976  1.00 28.05  ? 202 VAL B CG2 1 
ATOM   4007 N  N   . ASN B 1 203 ? -3.827  14.783  -11.412 1.00 24.02  ? 203 ASN B N   1 
ATOM   4008 C  CA  . ASN B 1 203 ? -3.220  13.665  -12.177 1.00 24.16  ? 203 ASN B CA  1 
ATOM   4009 C  C   . ASN B 1 203 ? -3.396  13.918  -13.684 1.00 22.47  ? 203 ASN B C   1 
ATOM   4010 O  O   . ASN B 1 203 ? -2.478  13.646  -14.425 1.00 20.33  ? 203 ASN B O   1 
ATOM   4011 C  CB  . ASN B 1 203 ? -3.835  12.326  -11.766 1.00 23.03  ? 203 ASN B CB  1 
ATOM   4012 C  CG  . ASN B 1 203 ? -3.402  11.829  -10.403 1.00 23.29  ? 203 ASN B CG  1 
ATOM   4013 O  OD1 . ASN B 1 203 ? -2.705  12.525  -9.659  1.00 24.03  ? 203 ASN B OD1 1 
ATOM   4014 N  ND2 . ASN B 1 203 ? -3.839  10.620  -10.061 1.00 21.11  ? 203 ASN B ND2 1 
ATOM   4015 N  N   . VAL B 1 204 ? -4.553  14.396  -14.124 1.00 24.52  ? 204 VAL B N   1 
ATOM   4016 C  CA  . VAL B 1 204 ? -4.747  14.757  -15.557 1.00 26.22  ? 204 VAL B CA  1 
ATOM   4017 C  C   . VAL B 1 204 ? -3.704  15.809  -15.939 1.00 26.84  ? 204 VAL B C   1 
ATOM   4018 O  O   . VAL B 1 204 ? -3.032  15.661  -16.981 1.00 26.15  ? 204 VAL B O   1 
ATOM   4019 C  CB  . VAL B 1 204 ? -6.160  15.270  -15.877 1.00 26.61  ? 204 VAL B CB  1 
ATOM   4020 C  CG1 . VAL B 1 204 ? -6.237  15.684  -17.353 1.00 27.08  ? 204 VAL B CG1 1 
ATOM   4021 C  CG2 . VAL B 1 204 ? -7.238  14.251  -15.575 1.00 25.03  ? 204 VAL B CG2 1 
ATOM   4022 N  N   . LEU B 1 205 ? -3.582  16.860  -15.140 1.00 28.96  ? 205 LEU B N   1 
ATOM   4023 C  CA  . LEU B 1 205 ? -2.588  17.928  -15.402 1.00 29.81  ? 205 LEU B CA  1 
ATOM   4024 C  C   . LEU B 1 205 ? -1.186  17.311  -15.433 1.00 29.25  ? 205 LEU B C   1 
ATOM   4025 O  O   . LEU B 1 205 ? -0.407  17.704  -16.297 1.00 29.61  ? 205 LEU B O   1 
ATOM   4026 C  CB  . LEU B 1 205 ? -2.723  19.028  -14.341 1.00 31.53  ? 205 LEU B CB  1 
ATOM   4027 C  CG  . LEU B 1 205 ? -4.017  19.839  -14.446 1.00 35.07  ? 205 LEU B CG  1 
ATOM   4028 C  CD1 . LEU B 1 205 ? -4.336  20.582  -13.148 1.00 36.65  ? 205 LEU B CD1 1 
ATOM   4029 C  CD2 . LEU B 1 205 ? -3.930  20.809  -15.612 1.00 33.97  ? 205 LEU B CD2 1 
ATOM   4030 N  N   . ALA B 1 206 ? -0.871  16.374  -14.538 1.00 27.30  ? 206 ALA B N   1 
ATOM   4031 C  CA  . ALA B 1 206 ? 0.452   15.715  -14.508 1.00 28.28  ? 206 ALA B CA  1 
ATOM   4032 C  C   . ALA B 1 206 ? 0.690   15.030  -15.859 1.00 30.01  ? 206 ALA B C   1 
ATOM   4033 O  O   . ALA B 1 206 ? 1.817   15.089  -16.395 1.00 28.82  ? 206 ALA B O   1 
ATOM   4034 C  CB  . ALA B 1 206 ? 0.540   14.712  -13.386 1.00 28.36  ? 206 ALA B CB  1 
ATOM   4035 N  N   . TRP B 1 207 ? -0.348  14.394  -16.376 1.00 26.31  ? 207 TRP B N   1 
ATOM   4036 C  CA  . TRP B 1 207 ? -0.270  13.588  -17.618 1.00 28.32  ? 207 TRP B CA  1 
ATOM   4037 C  C   . TRP B 1 207 ? -0.092  14.543  -18.796 1.00 29.77  ? 207 TRP B C   1 
ATOM   4038 O  O   . TRP B 1 207 ? 0.742   14.246  -19.666 1.00 29.21  ? 207 TRP B O   1 
ATOM   4039 C  CB  . TRP B 1 207 ? -1.514  12.713  -17.732 1.00 26.30  ? 207 TRP B CB  1 
ATOM   4040 C  CG  . TRP B 1 207 ? -1.760  12.016  -19.031 1.00 25.52  ? 207 TRP B CG  1 
ATOM   4041 C  CD1 . TRP B 1 207 ? -1.212  10.846  -19.472 1.00 26.48  ? 207 TRP B CD1 1 
ATOM   4042 C  CD2 . TRP B 1 207 ? -2.800  12.336  -19.962 1.00 26.06  ? 207 TRP B CD2 1 
ATOM   4043 N  NE1 . TRP B 1 207 ? -1.758  10.489  -20.679 1.00 24.01  ? 207 TRP B NE1 1 
ATOM   4044 C  CE2 . TRP B 1 207 ? -2.743  11.373  -20.994 1.00 24.32  ? 207 TRP B CE2 1 
ATOM   4045 C  CE3 . TRP B 1 207 ? -3.702  13.398  -20.065 1.00 25.33  ? 207 TRP B CE3 1 
ATOM   4046 C  CZ2 . TRP B 1 207 ? -3.563  11.429  -22.114 1.00 28.03  ? 207 TRP B CZ2 1 
ATOM   4047 C  CZ3 . TRP B 1 207 ? -4.531  13.442  -21.160 1.00 30.52  ? 207 TRP B CZ3 1 
ATOM   4048 C  CH2 . TRP B 1 207 ? -4.470  12.463  -22.163 1.00 27.67  ? 207 TRP B CH2 1 
ATOM   4049 N  N   . LEU B 1 208 ? -0.801  15.669  -18.794 1.00 29.51  ? 208 LEU B N   1 
ATOM   4050 C  CA  . LEU B 1 208 ? -0.602  16.720  -19.832 1.00 30.29  ? 208 LEU B CA  1 
ATOM   4051 C  C   . LEU B 1 208 ? 0.868   17.186  -19.804 1.00 30.31  ? 208 LEU B C   1 
ATOM   4052 O  O   . LEU B 1 208 ? 1.472   17.344  -20.880 1.00 29.78  ? 208 LEU B O   1 
ATOM   4053 C  CB  . LEU B 1 208 ? -1.591  17.871  -19.621 1.00 29.15  ? 208 LEU B CB  1 
ATOM   4054 C  CG  . LEU B 1 208 ? -3.056  17.563  -19.907 1.00 29.46  ? 208 LEU B CG  1 
ATOM   4055 C  CD1 . LEU B 1 208 ? -3.917  18.811  -19.710 1.00 33.13  ? 208 LEU B CD1 1 
ATOM   4056 C  CD2 . LEU B 1 208 ? -3.257  17.049  -21.317 1.00 31.11  ? 208 LEU B CD2 1 
ATOM   4057 N  N   . TYR B 1 209 ? 1.488   17.322  -18.637 1.00 31.64  ? 209 TYR B N   1 
ATOM   4058 C  CA  . TYR B 1 209 ? 2.934   17.639  -18.557 1.00 33.77  ? 209 TYR B CA  1 
ATOM   4059 C  C   . TYR B 1 209 ? 3.782   16.524  -19.206 1.00 38.08  ? 209 TYR B C   1 
ATOM   4060 O  O   . TYR B 1 209 ? 4.676   16.864  -20.001 1.00 37.73  ? 209 TYR B O   1 
ATOM   4061 C  CB  . TYR B 1 209 ? 3.380   17.914  -17.126 1.00 36.99  ? 209 TYR B CB  1 
ATOM   4062 C  CG  . TYR B 1 209 ? 3.049   19.311  -16.661 1.00 43.41  ? 209 TYR B CG  1 
ATOM   4063 C  CD1 . TYR B 1 209 ? 3.616   20.437  -17.257 1.00 45.18  ? 209 TYR B CD1 1 
ATOM   4064 C  CD2 . TYR B 1 209 ? 2.142   19.505  -15.633 1.00 42.73  ? 209 TYR B CD2 1 
ATOM   4065 C  CE1 . TYR B 1 209 ? 3.273   21.717  -16.839 1.00 46.18  ? 209 TYR B CE1 1 
ATOM   4066 C  CE2 . TYR B 1 209 ? 1.794   20.772  -15.202 1.00 45.22  ? 209 TYR B CE2 1 
ATOM   4067 C  CZ  . TYR B 1 209 ? 2.360   21.887  -15.804 1.00 51.73  ? 209 TYR B CZ  1 
ATOM   4068 O  OH  . TYR B 1 209 ? 1.982   23.122  -15.346 1.00 45.46  ? 209 TYR B OH  1 
ATOM   4069 N  N   . ALA B 1 210 ? 3.544   15.249  -18.875 1.00 32.94  ? 210 ALA B N   1 
ATOM   4070 C  CA  . ALA B 1 210 ? 4.155   14.083  -19.557 1.00 31.19  ? 210 ALA B CA  1 
ATOM   4071 C  C   . ALA B 1 210 ? 3.969   14.197  -21.072 1.00 32.31  ? 210 ALA B C   1 
ATOM   4072 O  O   . ALA B 1 210 ? 4.899   13.848  -21.808 1.00 30.45  ? 210 ALA B O   1 
ATOM   4073 C  CB  . ALA B 1 210 ? 3.562   12.784  -19.069 1.00 29.20  ? 210 ALA B CB  1 
ATOM   4074 N  N   . ALA B 1 211 ? 2.807   14.627  -21.540 1.00 30.89  ? 211 ALA B N   1 
ATOM   4075 C  CA  . ALA B 1 211 ? 2.566   14.689  -22.991 1.00 34.55  ? 211 ALA B CA  1 
ATOM   4076 C  C   . ALA B 1 211 ? 3.522   15.731  -23.596 1.00 37.48  ? 211 ALA B C   1 
ATOM   4077 O  O   . ALA B 1 211 ? 4.183   15.424  -24.595 1.00 36.16  ? 211 ALA B O   1 
ATOM   4078 C  CB  . ALA B 1 211 ? 1.135   14.971  -23.283 1.00 30.87  ? 211 ALA B CB  1 
ATOM   4079 N  N   . VAL B 1 212 ? 3.626   16.898  -22.970 1.00 34.73  ? 212 VAL B N   1 
ATOM   4080 C  CA  . VAL B 1 212 ? 4.474   18.017  -23.456 1.00 36.02  ? 212 VAL B CA  1 
ATOM   4081 C  C   . VAL B 1 212 ? 5.920   17.536  -23.480 1.00 34.54  ? 212 VAL B C   1 
ATOM   4082 O  O   . VAL B 1 212 ? 6.551   17.678  -24.515 1.00 40.28  ? 212 VAL B O   1 
ATOM   4083 C  CB  . VAL B 1 212 ? 4.310   19.291  -22.604 1.00 35.55  ? 212 VAL B CB  1 
ATOM   4084 C  CG1 . VAL B 1 212 ? 5.361   20.328  -22.979 1.00 36.67  ? 212 VAL B CG1 1 
ATOM   4085 C  CG2 . VAL B 1 212 ? 2.910   19.863  -22.742 1.00 32.96  ? 212 VAL B CG2 1 
ATOM   4086 N  N   . ILE B 1 213 ? 6.398   16.971  -22.381 1.00 32.98  ? 213 ILE B N   1 
ATOM   4087 C  CA  . ILE B 1 213 ? 7.772   16.416  -22.243 1.00 37.49  ? 213 ILE B CA  1 
ATOM   4088 C  C   . ILE B 1 213 ? 8.052   15.443  -23.397 1.00 39.51  ? 213 ILE B C   1 
ATOM   4089 O  O   . ILE B 1 213 ? 9.190   15.402  -23.852 1.00 36.98  ? 213 ILE B O   1 
ATOM   4090 C  CB  . ILE B 1 213 ? 7.923   15.740  -20.871 1.00 43.02  ? 213 ILE B CB  1 
ATOM   4091 C  CG1 . ILE B 1 213 ? 7.952   16.782  -19.747 1.00 42.96  ? 213 ILE B CG1 1 
ATOM   4092 C  CG2 . ILE B 1 213 ? 9.128   14.804  -20.839 1.00 42.57  ? 213 ILE B CG2 1 
ATOM   4093 C  CD1 . ILE B 1 213 ? 7.979   16.186  -18.361 1.00 41.54  ? 213 ILE B CD1 1 
ATOM   4094 N  N   . ASN B 1 214 ? 7.049   14.697  -23.853 1.00 37.12  ? 214 ASN B N   1 
ATOM   4095 C  CA  . ASN B 1 214 ? 7.184   13.762  -25.001 1.00 36.78  ? 214 ASN B CA  1 
ATOM   4096 C  C   . ASN B 1 214 ? 6.928   14.452  -26.350 1.00 36.47  ? 214 ASN B C   1 
ATOM   4097 O  O   . ASN B 1 214 ? 6.919   13.740  -27.355 1.00 40.84  ? 214 ASN B O   1 
ATOM   4098 C  CB  . ASN B 1 214 ? 6.256   12.558  -24.820 1.00 34.02  ? 214 ASN B CB  1 
ATOM   4099 C  CG  . ASN B 1 214 ? 6.860   11.576  -23.842 1.00 34.19  ? 214 ASN B CG  1 
ATOM   4100 O  OD1 . ASN B 1 214 ? 7.647   10.720  -24.232 1.00 36.27  ? 214 ASN B OD1 1 
ATOM   4101 N  ND2 . ASN B 1 214 ? 6.611   11.782  -22.560 1.00 35.43  ? 214 ASN B ND2 1 
ATOM   4102 N  N   . GLY B 1 215 ? 6.685   15.760  -26.396 1.00 39.06  ? 215 GLY B N   1 
ATOM   4103 C  CA  . GLY B 1 215 ? 6.495   16.511  -27.658 1.00 38.48  ? 215 GLY B CA  1 
ATOM   4104 C  C   . GLY B 1 215 ? 5.074   16.471  -28.189 1.00 38.12  ? 215 GLY B C   1 
ATOM   4105 O  O   . GLY B 1 215 ? 4.879   16.839  -29.341 1.00 34.30  ? 215 GLY B O   1 
ATOM   4106 N  N   . ASP B 1 216 ? 4.101   16.017  -27.400 1.00 41.45  ? 216 ASP B N   1 
ATOM   4107 C  CA  . ASP B 1 216 ? 2.662   16.248  -27.687 1.00 44.30  ? 216 ASP B CA  1 
ATOM   4108 C  C   . ASP B 1 216 ? 2.326   17.621  -27.098 1.00 45.96  ? 216 ASP B C   1 
ATOM   4109 O  O   . ASP B 1 216 ? 2.377   17.750  -25.861 1.00 52.45  ? 216 ASP B O   1 
ATOM   4110 C  CB  . ASP B 1 216 ? 1.783   15.143  -27.097 1.00 48.46  ? 216 ASP B CB  1 
ATOM   4111 C  CG  . ASP B 1 216 ? 1.067   14.298  -28.127 1.00 46.17  ? 216 ASP B CG  1 
ATOM   4112 O  OD1 . ASP B 1 216 ? 0.945   14.771  -29.265 1.00 51.08  ? 216 ASP B OD1 1 
ATOM   4113 O  OD2 . ASP B 1 216 ? 0.599   13.196  -27.760 1.00 42.37  ? 216 ASP B OD2 1 
ATOM   4114 N  N   . ARG B 1 217 ? 2.063   18.611  -27.944 1.00 44.52  ? 217 ARG B N   1 
ATOM   4115 C  CA  . ARG B 1 217 ? 2.006   20.037  -27.535 1.00 48.32  ? 217 ARG B CA  1 
ATOM   4116 C  C   . ARG B 1 217 ? 0.796   20.746  -28.132 1.00 42.06  ? 217 ARG B C   1 
ATOM   4117 O  O   . ARG B 1 217 ? 0.627   21.928  -27.812 1.00 43.70  ? 217 ARG B O   1 
ATOM   4118 C  CB  . ARG B 1 217 ? 3.275   20.760  -27.998 1.00 52.95  ? 217 ARG B CB  1 
ATOM   4119 C  CG  . ARG B 1 217 ? 4.533   20.331  -27.258 1.00 56.74  ? 217 ARG B CG  1 
ATOM   4120 C  CD  . ARG B 1 217 ? 5.729   21.130  -27.749 1.00 60.73  ? 217 ARG B CD  1 
ATOM   4121 N  NE  . ARG B 1 217 ? 5.665   22.548  -27.395 1.00 63.31  ? 217 ARG B NE  1 
ATOM   4122 C  CZ  . ARG B 1 217 ? 6.266   23.116  -26.345 1.00 61.40  ? 217 ARG B CZ  1 
ATOM   4123 N  NH1 . ARG B 1 217 ? 7.003   22.405  -25.504 1.00 60.50  ? 217 ARG B NH1 1 
ATOM   4124 N  NH2 . ARG B 1 217 ? 6.125   24.413  -26.137 1.00 66.56  ? 217 ARG B NH2 1 
ATOM   4125 N  N   . TRP B 1 218 ? -0.018  20.076  -28.942 1.00 39.34  ? 218 TRP B N   1 
ATOM   4126 C  CA  . TRP B 1 218 ? -1.076  20.762  -29.723 1.00 41.19  ? 218 TRP B CA  1 
ATOM   4127 C  C   . TRP B 1 218 ? -2.063  21.493  -28.803 1.00 43.60  ? 218 TRP B C   1 
ATOM   4128 O  O   . TRP B 1 218 ? -2.562  22.549  -29.213 1.00 43.89  ? 218 TRP B O   1 
ATOM   4129 C  CB  . TRP B 1 218 ? -1.787  19.793  -30.666 1.00 39.01  ? 218 TRP B CB  1 
ATOM   4130 C  CG  . TRP B 1 218 ? -2.524  18.674  -30.006 1.00 45.44  ? 218 TRP B CG  1 
ATOM   4131 C  CD1 . TRP B 1 218 ? -2.125  17.368  -29.952 1.00 47.20  ? 218 TRP B CD1 1 
ATOM   4132 C  CD2 . TRP B 1 218 ? -3.815  18.733  -29.366 1.00 51.24  ? 218 TRP B CD2 1 
ATOM   4133 N  NE1 . TRP B 1 218 ? -3.066  16.608  -29.311 1.00 51.38  ? 218 TRP B NE1 1 
ATOM   4134 C  CE2 . TRP B 1 218 ? -4.108  17.417  -28.935 1.00 50.72  ? 218 TRP B CE2 1 
ATOM   4135 C  CE3 . TRP B 1 218 ? -4.738  19.758  -29.099 1.00 52.04  ? 218 TRP B CE3 1 
ATOM   4136 C  CZ2 . TRP B 1 218 ? -5.283  17.105  -28.257 1.00 54.04  ? 218 TRP B CZ2 1 
ATOM   4137 C  CZ3 . TRP B 1 218 ? -5.899  19.447  -28.423 1.00 50.73  ? 218 TRP B CZ3 1 
ATOM   4138 C  CH2 . TRP B 1 218 ? -6.168  18.136  -28.014 1.00 53.75  ? 218 TRP B CH2 1 
ATOM   4139 N  N   . PHE B 1 219 ? -2.373  20.922  -27.635 1.00 44.64  ? 219 PHE B N   1 
ATOM   4140 C  CA  . PHE B 1 219 ? -3.453  21.370  -26.713 1.00 41.06  ? 219 PHE B CA  1 
ATOM   4141 C  C   . PHE B 1 219 ? -3.003  22.621  -25.968 1.00 39.86  ? 219 PHE B C   1 
ATOM   4142 O  O   . PHE B 1 219 ? -3.831  23.163  -25.244 1.00 49.52  ? 219 PHE B O   1 
ATOM   4143 C  CB  . PHE B 1 219 ? -3.805  20.274  -25.692 1.00 41.44  ? 219 PHE B CB  1 
ATOM   4144 C  CG  . PHE B 1 219 ? -2.608  19.657  -25.006 1.00 40.90  ? 219 PHE B CG  1 
ATOM   4145 C  CD1 . PHE B 1 219 ? -1.953  20.317  -23.978 1.00 38.16  ? 219 PHE B CD1 1 
ATOM   4146 C  CD2 . PHE B 1 219 ? -2.120  18.414  -25.407 1.00 41.81  ? 219 PHE B CD2 1 
ATOM   4147 C  CE1 . PHE B 1 219 ? -0.847  19.750  -23.363 1.00 40.65  ? 219 PHE B CE1 1 
ATOM   4148 C  CE2 . PHE B 1 219 ? -1.004  17.858  -24.807 1.00 35.01  ? 219 PHE B CE2 1 
ATOM   4149 C  CZ  . PHE B 1 219 ? -0.374  18.526  -23.781 1.00 41.91  ? 219 PHE B CZ  1 
ATOM   4150 N  N   . LEU B 1 220 ? -1.720  22.978  -26.008 1.00 36.22  ? 220 LEU B N   1 
ATOM   4151 C  CA  . LEU B 1 220 ? -1.258  24.234  -25.378 1.00 44.95  ? 220 LEU B CA  1 
ATOM   4152 C  C   . LEU B 1 220 ? -1.964  25.412  -26.054 1.00 47.80  ? 220 LEU B C   1 
ATOM   4153 O  O   . LEU B 1 220 ? -2.528  25.243  -27.160 1.00 46.64  ? 220 LEU B O   1 
ATOM   4154 C  CB  . LEU B 1 220 ? 0.262   24.350  -25.474 1.00 47.00  ? 220 LEU B CB  1 
ATOM   4155 C  CG  . LEU B 1 220 ? 1.015   23.218  -24.777 1.00 50.78  ? 220 LEU B CG  1 
ATOM   4156 C  CD1 . LEU B 1 220 ? 2.515   23.331  -24.998 1.00 47.02  ? 220 LEU B CD1 1 
ATOM   4157 C  CD2 . LEU B 1 220 ? 0.688   23.180  -23.287 1.00 53.96  ? 220 LEU B CD2 1 
ATOM   4158 N  N   . ASN B 1 221 ? -2.013  26.542  -25.352 1.00 52.16  ? 221 ASN B N   1 
ATOM   4159 C  CA  . ASN B 1 221 ? -2.670  27.786  -25.834 1.00 41.92  ? 221 ASN B CA  1 
ATOM   4160 C  C   . ASN B 1 221 ? -2.042  28.962  -25.103 1.00 41.34  ? 221 ASN B C   1 
ATOM   4161 O  O   . ASN B 1 221 ? -1.264  28.737  -24.144 1.00 41.55  ? 221 ASN B O   1 
ATOM   4162 C  CB  . ASN B 1 221 ? -4.190  27.745  -25.693 1.00 40.99  ? 221 ASN B CB  1 
ATOM   4163 C  CG  . ASN B 1 221 ? -4.706  27.614  -24.270 1.00 39.57  ? 221 ASN B CG  1 
ATOM   4164 O  OD1 . ASN B 1 221 ? -4.040  27.971  -23.291 1.00 35.99  ? 221 ASN B OD1 1 
ATOM   4165 N  ND2 . ASN B 1 221 ? -5.918  27.116  -24.158 1.00 32.16  ? 221 ASN B ND2 1 
ATOM   4166 N  N   . ARG B 1 222 ? -2.364  30.172  -25.557 1.00 36.23  ? 222 ARG B N   1 
ATOM   4167 C  CA  . ARG B 1 222 ? -1.795  31.437  -25.030 1.00 33.39  ? 222 ARG B CA  1 
ATOM   4168 C  C   . ARG B 1 222 ? -2.417  31.791  -23.684 1.00 29.00  ? 222 ARG B C   1 
ATOM   4169 O  O   . ARG B 1 222 ? -1.876  32.678  -23.067 1.00 31.97  ? 222 ARG B O   1 
ATOM   4170 C  CB  . ARG B 1 222 ? -2.017  32.604  -26.006 1.00 35.26  ? 222 ARG B CB  1 
ATOM   4171 C  CG  . ARG B 1 222 ? -3.473  32.986  -26.271 1.00 37.23  ? 222 ARG B CG  1 
ATOM   4172 C  CD  . ARG B 1 222 ? -3.642  34.376  -26.900 1.00 39.74  ? 222 ARG B CD  1 
ATOM   4173 N  NE  . ARG B 1 222 ? -2.791  34.516  -28.076 1.00 41.62  ? 222 ARG B NE  1 
ATOM   4174 C  CZ  . ARG B 1 222 ? -1.888  35.465  -28.281 1.00 37.97  ? 222 ARG B CZ  1 
ATOM   4175 N  NH1 . ARG B 1 222 ? -1.707  36.443  -27.408 1.00 41.95  ? 222 ARG B NH1 1 
ATOM   4176 N  NH2 . ARG B 1 222 ? -1.178  35.441  -29.392 1.00 38.90  ? 222 ARG B NH2 1 
ATOM   4177 N  N   . PHE B 1 223 ? -3.513  31.166  -23.269 1.00 31.52  ? 223 PHE B N   1 
ATOM   4178 C  CA  . PHE B 1 223 ? -4.345  31.680  -22.149 1.00 33.43  ? 223 PHE B CA  1 
ATOM   4179 C  C   . PHE B 1 223 ? -3.799  31.225  -20.789 1.00 40.86  ? 223 PHE B C   1 
ATOM   4180 O  O   . PHE B 1 223 ? -2.882  30.360  -20.674 1.00 35.62  ? 223 PHE B O   1 
ATOM   4181 C  CB  . PHE B 1 223 ? -5.806  31.289  -22.361 1.00 32.08  ? 223 PHE B CB  1 
ATOM   4182 C  CG  . PHE B 1 223 ? -6.357  31.765  -23.676 1.00 31.51  ? 223 PHE B CG  1 
ATOM   4183 C  CD1 . PHE B 1 223 ? -6.539  33.123  -23.931 1.00 35.02  ? 223 PHE B CD1 1 
ATOM   4184 C  CD2 . PHE B 1 223 ? -6.599  30.861  -24.700 1.00 34.92  ? 223 PHE B CD2 1 
ATOM   4185 C  CE1 . PHE B 1 223 ? -7.001  33.557  -25.171 1.00 35.33  ? 223 PHE B CE1 1 
ATOM   4186 C  CE2 . PHE B 1 223 ? -7.061  31.290  -25.933 1.00 32.34  ? 223 PHE B CE2 1 
ATOM   4187 C  CZ  . PHE B 1 223 ? -7.247  32.639  -26.171 1.00 36.68  ? 223 PHE B CZ  1 
ATOM   4188 N  N   . THR B 1 224 ? -4.326  31.854  -19.741 1.00 43.94  ? 224 THR B N   1 
ATOM   4189 C  CA  . THR B 1 224 ? -4.134  31.399  -18.350 1.00 41.93  ? 224 THR B CA  1 
ATOM   4190 C  C   . THR B 1 224 ? -5.461  31.512  -17.599 1.00 42.36  ? 224 THR B C   1 
ATOM   4191 O  O   . THR B 1 224 ? -6.519  31.747  -18.241 1.00 41.70  ? 224 THR B O   1 
ATOM   4192 C  CB  . THR B 1 224 ? -2.967  32.134  -17.703 1.00 47.91  ? 224 THR B CB  1 
ATOM   4193 O  OG1 . THR B 1 224 ? -2.834  31.423  -16.474 1.00 52.64  ? 224 THR B OG1 1 
ATOM   4194 C  CG2 . THR B 1 224 ? -3.218  33.616  -17.509 1.00 48.89  ? 224 THR B CG2 1 
ATOM   4195 N  N   . THR B 1 225 ? -5.450  31.248  -16.298 1.00 42.44  ? 225 THR B N   1 
ATOM   4196 C  CA  . THR B 1 225 ? -6.715  31.226  -15.523 1.00 46.26  ? 225 THR B CA  1 
ATOM   4197 C  C   . THR B 1 225 ? -6.424  31.354  -14.031 1.00 45.76  ? 225 THR B C   1 
ATOM   4198 O  O   . THR B 1 225 ? -5.275  31.644  -13.657 1.00 47.17  ? 225 THR B O   1 
ATOM   4199 C  CB  . THR B 1 225 ? -7.546  29.972  -15.832 1.00 49.50  ? 225 THR B CB  1 
ATOM   4200 O  OG1 . THR B 1 225 ? -8.845  30.130  -15.255 1.00 53.55  ? 225 THR B OG1 1 
ATOM   4201 C  CG2 . THR B 1 225 ? -6.893  28.709  -15.313 1.00 53.08  ? 225 THR B CG2 1 
ATOM   4202 N  N   . THR B 1 226 ? -7.456  31.151  -13.215 1.00 52.85  ? 226 THR B N   1 
ATOM   4203 C  CA  . THR B 1 226 ? -7.341  31.102  -11.735 1.00 52.51  ? 226 THR B CA  1 
ATOM   4204 C  C   . THR B 1 226 ? -8.071  29.875  -11.191 1.00 43.16  ? 226 THR B C   1 
ATOM   4205 O  O   . THR B 1 226 ? -9.034  29.375  -11.855 1.00 41.12  ? 226 THR B O   1 
ATOM   4206 C  CB  . THR B 1 226 ? -7.877  32.386  -11.098 1.00 48.07  ? 226 THR B CB  1 
ATOM   4207 O  OG1 . THR B 1 226 ? -9.236  32.519  -11.529 1.00 44.67  ? 226 THR B OG1 1 
ATOM   4208 C  CG2 . THR B 1 226 ? -7.009  33.571  -11.478 1.00 51.59  ? 226 THR B CG2 1 
ATOM   4209 N  N   . LEU B 1 227 ? -7.627  29.449  -10.008 1.00 49.81  ? 227 LEU B N   1 
ATOM   4210 C  CA  . LEU B 1 227 ? -8.253  28.355  -9.227  1.00 51.34  ? 227 LEU B CA  1 
ATOM   4211 C  C   . LEU B 1 227 ? -9.779  28.495  -9.313  1.00 50.64  ? 227 LEU B C   1 
ATOM   4212 O  O   . LEU B 1 227 ? -10.422 27.576  -9.874  1.00 49.54  ? 227 LEU B O   1 
ATOM   4213 C  CB  . LEU B 1 227 ? -7.735  28.405  -7.784  1.00 55.18  ? 227 LEU B CB  1 
ATOM   4214 C  CG  . LEU B 1 227 ? -6.754  27.310  -7.333  1.00 61.17  ? 227 LEU B CG  1 
ATOM   4215 C  CD1 . LEU B 1 227 ? -6.677  26.146  -8.320  1.00 63.89  ? 227 LEU B CD1 1 
ATOM   4216 C  CD2 . LEU B 1 227 ? -5.360  27.866  -7.055  1.00 57.51  ? 227 LEU B CD2 1 
ATOM   4217 N  N   . ASN B 1 228 ? -10.346 29.622  -8.863  1.00 54.46  ? 228 ASN B N   1 
ATOM   4218 C  CA  . ASN B 1 228 ? -11.821 29.778  -8.724  1.00 53.48  ? 228 ASN B CA  1 
ATOM   4219 C  C   . ASN B 1 228 ? -12.503 29.553  -10.070 1.00 50.76  ? 228 ASN B C   1 
ATOM   4220 O  O   . ASN B 1 228 ? -13.478 28.782  -10.133 1.00 54.42  ? 228 ASN B O   1 
ATOM   4221 C  CB  . ASN B 1 228 ? -12.220 31.148  -8.182  1.00 60.72  ? 228 ASN B CB  1 
ATOM   4222 C  CG  . ASN B 1 228 ? -11.862 31.309  -6.724  1.00 60.98  ? 228 ASN B CG  1 
ATOM   4223 O  OD1 . ASN B 1 228 ? -10.750 30.971  -6.315  1.00 60.50  ? 228 ASN B OD1 1 
ATOM   4224 N  ND2 . ASN B 1 228 ? -12.801 31.821  -5.945  1.00 62.61  ? 228 ASN B ND2 1 
ATOM   4225 N  N   . ASP B 1 229 ? -12.014 30.223  -11.108 1.00 54.75  ? 229 ASP B N   1 
ATOM   4226 C  CA  . ASP B 1 229 ? -12.581 30.118  -12.472 1.00 52.54  ? 229 ASP B CA  1 
ATOM   4227 C  C   . ASP B 1 229 ? -12.458 28.657  -12.916 1.00 44.98  ? 229 ASP B C   1 
ATOM   4228 O  O   . ASP B 1 229 ? -13.482 28.054  -13.333 1.00 40.97  ? 229 ASP B O   1 
ATOM   4229 C  CB  . ASP B 1 229 ? -11.879 31.108  -13.405 1.00 58.97  ? 229 ASP B CB  1 
ATOM   4230 C  CG  . ASP B 1 229 ? -12.286 32.552  -13.156 1.00 64.83  ? 229 ASP B CG  1 
ATOM   4231 O  OD1 . ASP B 1 229 ? -13.416 32.920  -13.570 1.00 58.45  ? 229 ASP B OD1 1 
ATOM   4232 O  OD2 . ASP B 1 229 ? -11.492 33.282  -12.515 1.00 62.60  ? 229 ASP B OD2 1 
ATOM   4233 N  N   . PHE B 1 230 ? -11.247 28.104  -12.824 1.00 46.47  ? 230 PHE B N   1 
ATOM   4234 C  CA  . PHE B 1 230 ? -10.991 26.710  -13.278 1.00 48.32  ? 230 PHE B CA  1 
ATOM   4235 C  C   . PHE B 1 230 ? -11.875 25.758  -12.462 1.00 48.25  ? 230 PHE B C   1 
ATOM   4236 O  O   . PHE B 1 230 ? -12.636 24.941  -13.050 1.00 49.51  ? 230 PHE B O   1 
ATOM   4237 C  CB  . PHE B 1 230 ? -9.511  26.337  -13.200 1.00 52.40  ? 230 PHE B CB  1 
ATOM   4238 C  CG  . PHE B 1 230 ? -9.308  24.911  -13.640 1.00 57.41  ? 230 PHE B CG  1 
ATOM   4239 C  CD1 . PHE B 1 230 ? -9.549  24.546  -14.957 1.00 57.13  ? 230 PHE B CD1 1 
ATOM   4240 C  CD2 . PHE B 1 230 ? -9.013  23.920  -12.719 1.00 53.59  ? 230 PHE B CD2 1 
ATOM   4241 C  CE1 . PHE B 1 230 ? -9.431  23.226  -15.352 1.00 56.25  ? 230 PHE B CE1 1 
ATOM   4242 C  CE2 . PHE B 1 230 ? -8.903  22.600  -13.118 1.00 52.83  ? 230 PHE B CE2 1 
ATOM   4243 C  CZ  . PHE B 1 230 ? -9.102  22.260  -14.432 1.00 54.80  ? 230 PHE B CZ  1 
ATOM   4244 N  N   . ASN B 1 231 ? -11.874 25.935  -11.135 1.00 49.74  ? 231 ASN B N   1 
ATOM   4245 C  CA  . ASN B 1 231 ? -12.605 25.032  -10.205 1.00 48.07  ? 231 ASN B CA  1 
ATOM   4246 C  C   . ASN B 1 231 ? -14.089 25.022  -10.543 1.00 50.18  ? 231 ASN B C   1 
ATOM   4247 O  O   . ASN B 1 231 ? -14.700 23.944  -10.447 1.00 57.14  ? 231 ASN B O   1 
ATOM   4248 C  CB  . ASN B 1 231 ? -12.298 25.339  -8.738  1.00 44.97  ? 231 ASN B CB  1 
ATOM   4249 C  CG  . ASN B 1 231 ? -11.081 24.565  -8.296  1.00 40.43  ? 231 ASN B CG  1 
ATOM   4250 O  OD1 . ASN B 1 231 ? -10.953 23.409  -8.676  1.00 48.02  ? 231 ASN B OD1 1 
ATOM   4251 N  ND2 . ASN B 1 231 ? -10.149 25.188  -7.600  1.00 38.18  ? 231 ASN B ND2 1 
ATOM   4252 N  N   . LEU B 1 232 ? -14.647 26.146  -10.980 1.00 56.90  ? 232 LEU B N   1 
ATOM   4253 C  CA  . LEU B 1 232 ? -16.093 26.207  -11.311 1.00 61.16  ? 232 LEU B CA  1 
ATOM   4254 C  C   . LEU B 1 232 ? -16.379 25.387  -12.568 1.00 57.98  ? 232 LEU B C   1 
ATOM   4255 O  O   . LEU B 1 232 ? -17.481 24.842  -12.672 1.00 59.58  ? 232 LEU B O   1 
ATOM   4256 C  CB  . LEU B 1 232 ? -16.518 27.669  -11.447 1.00 70.17  ? 232 LEU B CB  1 
ATOM   4257 C  CG  . LEU B 1 232 ? -16.747 28.356  -10.100 1.00 77.60  ? 232 LEU B CG  1 
ATOM   4258 C  CD1 . LEU B 1 232 ? -16.529 29.860  -10.196 1.00 76.95  ? 232 LEU B CD1 1 
ATOM   4259 C  CD2 . LEU B 1 232 ? -18.134 28.023  -9.550  1.00 76.37  ? 232 LEU B CD2 1 
ATOM   4260 N  N   . VAL B 1 233 ? -15.407 25.257  -13.466 1.00 68.00  ? 233 VAL B N   1 
ATOM   4261 C  CA  . VAL B 1 233 ? -15.558 24.391  -14.671 1.00 72.81  ? 233 VAL B CA  1 
ATOM   4262 C  C   . VAL B 1 233 ? -15.339 22.937  -14.245 1.00 66.80  ? 233 VAL B C   1 
ATOM   4263 O  O   . VAL B 1 233 ? -16.125 22.081  -14.680 1.00 67.80  ? 233 VAL B O   1 
ATOM   4264 C  CB  . VAL B 1 233 ? -14.611 24.817  -15.808 1.00 78.69  ? 233 VAL B CB  1 
ATOM   4265 C  CG1 . VAL B 1 233 ? -14.903 24.046  -17.085 1.00 80.08  ? 233 VAL B CG1 1 
ATOM   4266 C  CG2 . VAL B 1 233 ? -14.693 26.314  -16.061 1.00 78.41  ? 233 VAL B CG2 1 
ATOM   4267 N  N   . ALA B 1 234 ? -14.328 22.680  -13.410 1.00 67.22  ? 234 ALA B N   1 
ATOM   4268 C  CA  . ALA B 1 234 ? -14.022 21.331  -12.878 1.00 68.40  ? 234 ALA B CA  1 
ATOM   4269 C  C   . ALA B 1 234 ? -15.301 20.726  -12.291 1.00 65.48  ? 234 ALA B C   1 
ATOM   4270 O  O   . ALA B 1 234 ? -15.736 19.679  -12.804 1.00 65.53  ? 234 ALA B O   1 
ATOM   4271 C  CB  . ALA B 1 234 ? -12.912 21.386  -11.858 1.00 80.71  ? 234 ALA B CB  1 
ATOM   4272 N  N   . MET B 1 235 ? -15.904 21.390  -11.296 1.00 68.19  ? 235 MET B N   1 
ATOM   4273 C  CA  . MET B 1 235 ? -17.124 20.896  -10.605 1.00 64.27  ? 235 MET B CA  1 
ATOM   4274 C  C   . MET B 1 235 ? -18.186 20.529  -11.641 1.00 59.93  ? 235 MET B C   1 
ATOM   4275 O  O   . MET B 1 235 ? -18.841 19.492  -11.457 1.00 55.72  ? 235 MET B O   1 
ATOM   4276 C  CB  . MET B 1 235 ? -17.730 21.925  -9.654  1.00 72.08  ? 235 MET B CB  1 
ATOM   4277 C  CG  . MET B 1 235 ? -19.006 21.404  -9.009  1.00 83.00  ? 235 MET B CG  1 
ATOM   4278 S  SD  . MET B 1 235 ? -19.887 22.622  -8.015  1.00 99.62  ? 235 MET B SD  1 
ATOM   4279 C  CE  . MET B 1 235 ? -18.764 22.804  -6.634  1.00 86.93  ? 235 MET B CE  1 
ATOM   4280 N  N   . LYS B 1 236 ? -18.346 21.340  -12.691 1.00 59.93  ? 236 LYS B N   1 
ATOM   4281 C  CA  . LYS B 1 236 ? -19.356 21.081  -13.751 1.00 62.31  ? 236 LYS B CA  1 
ATOM   4282 C  C   . LYS B 1 236 ? -19.041 19.773  -14.484 1.00 54.96  ? 236 LYS B C   1 
ATOM   4283 O  O   . LYS B 1 236 ? -20.002 19.086  -14.869 1.00 51.57  ? 236 LYS B O   1 
ATOM   4284 C  CB  . LYS B 1 236 ? -19.430 22.233  -14.757 1.00 72.52  ? 236 LYS B CB  1 
ATOM   4285 C  CG  . LYS B 1 236 ? -20.618 22.163  -15.716 1.00 82.60  ? 236 LYS B CG  1 
ATOM   4286 C  CD  . LYS B 1 236 ? -20.643 23.269  -16.763 1.00 90.02  ? 236 LYS B CD  1 
ATOM   4287 C  CE  . LYS B 1 236 ? -20.491 24.667  -16.192 1.00 91.28  ? 236 LYS B CE  1 
ATOM   4288 N  NZ  . LYS B 1 236 ? -21.491 24.953  -15.135 1.00 97.49  ? 236 LYS B NZ  1 
ATOM   4289 N  N   . TYR B 1 237 ? -17.756 19.444  -14.686 1.00 53.47  ? 237 TYR B N   1 
ATOM   4290 C  CA  . TYR B 1 237 ? -17.337 18.242  -15.459 1.00 52.71  ? 237 TYR B CA  1 
ATOM   4291 C  C   . TYR B 1 237 ? -17.004 17.081  -14.520 1.00 48.12  ? 237 TYR B C   1 
ATOM   4292 O  O   . TYR B 1 237 ? -16.427 16.095  -15.002 1.00 36.50  ? 237 TYR B O   1 
ATOM   4293 C  CB  . TYR B 1 237 ? -16.200 18.595  -16.418 1.00 53.45  ? 237 TYR B CB  1 
ATOM   4294 C  CG  . TYR B 1 237 ? -16.678 19.405  -17.596 1.00 55.36  ? 237 TYR B CG  1 
ATOM   4295 C  CD1 . TYR B 1 237 ? -16.733 20.790  -17.528 1.00 57.06  ? 237 TYR B CD1 1 
ATOM   4296 C  CD2 . TYR B 1 237 ? -17.142 18.784  -18.748 1.00 54.69  ? 237 TYR B CD2 1 
ATOM   4297 C  CE1 . TYR B 1 237 ? -17.206 21.542  -18.590 1.00 54.92  ? 237 TYR B CE1 1 
ATOM   4298 C  CE2 . TYR B 1 237 ? -17.610 19.519  -19.823 1.00 51.75  ? 237 TYR B CE2 1 
ATOM   4299 C  CZ  . TYR B 1 237 ? -17.642 20.900  -19.736 1.00 56.80  ? 237 TYR B CZ  1 
ATOM   4300 O  OH  . TYR B 1 237 ? -18.102 21.645  -20.779 1.00 65.16  ? 237 TYR B OH  1 
ATOM   4301 N  N   . ASN B 1 238 ? -17.426 17.157  -13.252 1.00 47.52  ? 238 ASN B N   1 
ATOM   4302 C  CA  . ASN B 1 238 ? -17.233 16.063  -12.263 1.00 42.97  ? 238 ASN B CA  1 
ATOM   4303 C  C   . ASN B 1 238 ? -15.733 15.835  -12.050 1.00 38.80  ? 238 ASN B C   1 
ATOM   4304 O  O   . ASN B 1 238 ? -15.314 14.687  -11.900 1.00 39.87  ? 238 ASN B O   1 
ATOM   4305 C  CB  . ASN B 1 238 ? -17.954 14.791  -12.708 1.00 47.80  ? 238 ASN B CB  1 
ATOM   4306 C  CG  . ASN B 1 238 ? -19.297 14.660  -12.041 1.00 58.19  ? 238 ASN B CG  1 
ATOM   4307 O  OD1 . ASN B 1 238 ? -19.531 15.281  -11.011 1.00 60.78  ? 238 ASN B OD1 1 
ATOM   4308 N  ND2 . ASN B 1 238 ? -20.183 13.869  -12.623 1.00 62.54  ? 238 ASN B ND2 1 
ATOM   4309 N  N   . TYR B 1 239 ? -14.965 16.917  -12.028 1.00 36.77  ? 239 TYR B N   1 
ATOM   4310 C  CA  . TYR B 1 239 ? -13.519 16.938  -11.741 1.00 37.59  ? 239 TYR B CA  1 
ATOM   4311 C  C   . TYR B 1 239 ? -13.341 17.331  -10.279 1.00 38.28  ? 239 TYR B C   1 
ATOM   4312 O  O   . TYR B 1 239 ? -14.050 18.207  -9.806  1.00 39.19  ? 239 TYR B O   1 
ATOM   4313 C  CB  . TYR B 1 239 ? -12.795 17.892  -12.692 1.00 35.75  ? 239 TYR B CB  1 
ATOM   4314 C  CG  . TYR B 1 239 ? -12.275 17.226  -13.944 1.00 33.19  ? 239 TYR B CG  1 
ATOM   4315 C  CD1 . TYR B 1 239 ? -13.121 16.495  -14.760 1.00 30.80  ? 239 TYR B CD1 1 
ATOM   4316 C  CD2 . TYR B 1 239 ? -10.933 17.312  -14.296 1.00 31.05  ? 239 TYR B CD2 1 
ATOM   4317 C  CE1 . TYR B 1 239 ? -12.651 15.867  -15.903 1.00 31.22  ? 239 TYR B CE1 1 
ATOM   4318 C  CE2 . TYR B 1 239 ? -10.446 16.690  -15.433 1.00 29.37  ? 239 TYR B CE2 1 
ATOM   4319 C  CZ  . TYR B 1 239 ? -11.311 15.981  -16.241 1.00 31.09  ? 239 TYR B CZ  1 
ATOM   4320 O  OH  . TYR B 1 239 ? -10.829 15.370  -17.355 1.00 32.15  ? 239 TYR B OH  1 
ATOM   4321 N  N   . GLU B 1 240 ? -12.399 16.692  -9.597  1.00 39.04  ? 240 GLU B N   1 
ATOM   4322 C  CA  . GLU B 1 240 ? -12.002 17.075  -8.225  1.00 38.46  ? 240 GLU B CA  1 
ATOM   4323 C  C   . GLU B 1 240 ? -11.607 18.545  -8.241  1.00 40.69  ? 240 GLU B C   1 
ATOM   4324 O  O   . GLU B 1 240 ? -10.989 19.020  -9.193  1.00 37.03  ? 240 GLU B O   1 
ATOM   4325 C  CB  . GLU B 1 240 ? -10.864 16.192  -7.697  1.00 36.59  ? 240 GLU B CB  1 
ATOM   4326 C  CG  . GLU B 1 240 ? -11.321 14.787  -7.370  1.00 43.13  ? 240 GLU B CG  1 
ATOM   4327 C  CD  . GLU B 1 240 ? -12.318 14.707  -6.228  1.00 42.20  ? 240 GLU B CD  1 
ATOM   4328 O  OE1 . GLU B 1 240 ? -11.908 14.964  -5.107  1.00 45.31  ? 240 GLU B OE1 1 
ATOM   4329 O  OE2 . GLU B 1 240 ? -13.487 14.386  -6.472  1.00 42.07  ? 240 GLU B OE2 1 
ATOM   4330 N  N   . PRO B 1 241 ? -11.951 19.303  -7.174  1.00 40.25  ? 241 PRO B N   1 
ATOM   4331 C  CA  . PRO B 1 241 ? -11.366 20.617  -6.955  1.00 41.29  ? 241 PRO B CA  1 
ATOM   4332 C  C   . PRO B 1 241 ? -9.835  20.541  -6.954  1.00 41.27  ? 241 PRO B C   1 
ATOM   4333 O  O   . PRO B 1 241 ? -9.260  19.618  -6.410  1.00 42.69  ? 241 PRO B O   1 
ATOM   4334 C  CB  . PRO B 1 241 ? -11.950 21.055  -5.602  1.00 43.01  ? 241 PRO B CB  1 
ATOM   4335 C  CG  . PRO B 1 241 ? -13.288 20.331  -5.554  1.00 45.63  ? 241 PRO B CG  1 
ATOM   4336 C  CD  . PRO B 1 241 ? -12.983 18.982  -6.175  1.00 45.30  ? 241 PRO B CD  1 
ATOM   4337 N  N   . LEU B 1 242 ? -9.214  21.497  -7.639  1.00 39.23  ? 242 LEU B N   1 
ATOM   4338 C  CA  . LEU B 1 242 ? -7.753  21.686  -7.643  1.00 36.67  ? 242 LEU B CA  1 
ATOM   4339 C  C   . LEU B 1 242 ? -7.400  22.703  -6.568  1.00 38.18  ? 242 LEU B C   1 
ATOM   4340 O  O   . LEU B 1 242 ? -7.976  23.802  -6.570  1.00 40.52  ? 242 LEU B O   1 
ATOM   4341 C  CB  . LEU B 1 242 ? -7.317  22.198  -9.011  1.00 39.44  ? 242 LEU B CB  1 
ATOM   4342 C  CG  . LEU B 1 242 ? -5.804  22.222  -9.222  1.00 41.50  ? 242 LEU B CG  1 
ATOM   4343 C  CD1 . LEU B 1 242 ? -5.257  20.818  -9.532  1.00 39.06  ? 242 LEU B CD1 1 
ATOM   4344 C  CD2 . LEU B 1 242 ? -5.459  23.193  -10.338 1.00 42.31  ? 242 LEU B CD2 1 
ATOM   4345 N  N   . THR B 1 243 ? -6.445  22.352  -5.727  1.00 39.74  ? 243 THR B N   1 
ATOM   4346 C  CA  . THR B 1 243 ? -6.052  23.140  -4.542  1.00 43.00  ? 243 THR B CA  1 
ATOM   4347 C  C   . THR B 1 243 ? -4.699  23.749  -4.805  1.00 40.42  ? 243 THR B C   1 
ATOM   4348 O  O   . THR B 1 243 ? -4.061  23.356  -5.795  1.00 38.44  ? 243 THR B O   1 
ATOM   4349 C  CB  . THR B 1 243 ? -6.006  22.279  -3.275  1.00 39.35  ? 243 THR B CB  1 
ATOM   4350 O  OG1 . THR B 1 243 ? -4.886  21.400  -3.339  1.00 41.28  ? 243 THR B OG1 1 
ATOM   4351 C  CG2 . THR B 1 243 ? -7.268  21.474  -3.094  1.00 40.58  ? 243 THR B CG2 1 
ATOM   4352 N  N   . GLN B 1 244 ? -4.298  24.652  -3.916  1.00 43.76  ? 244 GLN B N   1 
ATOM   4353 C  CA  . GLN B 1 244 ? -2.965  25.287  -3.936  1.00 44.87  ? 244 GLN B CA  1 
ATOM   4354 C  C   . GLN B 1 244 ? -1.895  24.212  -3.719  1.00 50.11  ? 244 GLN B C   1 
ATOM   4355 O  O   . GLN B 1 244 ? -0.787  24.358  -4.282  1.00 55.08  ? 244 GLN B O   1 
ATOM   4356 C  CB  . GLN B 1 244 ? -2.838  26.373  -2.869  1.00 43.80  ? 244 GLN B CB  1 
ATOM   4357 C  CG  . GLN B 1 244 ? -1.444  26.981  -2.845  1.00 43.46  ? 244 GLN B CG  1 
ATOM   4358 C  CD  . GLN B 1 244 ? -1.068  27.496  -4.214  1.00 44.93  ? 244 GLN B CD  1 
ATOM   4359 O  OE1 . GLN B 1 244 ? -1.907  28.049  -4.930  1.00 43.02  ? 244 GLN B OE1 1 
ATOM   4360 N  NE2 . GLN B 1 244 ? 0.180   27.278  -4.603  1.00 48.58  ? 244 GLN B NE2 1 
ATOM   4361 N  N   . ASP B 1 245 ? -2.202  23.177  -2.933  1.00 46.73  ? 245 ASP B N   1 
ATOM   4362 C  CA  . ASP B 1 245 ? -1.244  22.074  -2.646  1.00 47.51  ? 245 ASP B CA  1 
ATOM   4363 C  C   . ASP B 1 245 ? -0.929  21.348  -3.980  1.00 41.94  ? 245 ASP B C   1 
ATOM   4364 O  O   . ASP B 1 245 ? 0.247   21.071  -4.270  1.00 38.73  ? 245 ASP B O   1 
ATOM   4365 C  CB  . ASP B 1 245 ? -1.807  21.198  -1.519  1.00 51.37  ? 245 ASP B CB  1 
ATOM   4366 C  CG  . ASP B 1 245 ? -1.054  19.895  -1.301  1.00 64.34  ? 245 ASP B CG  1 
ATOM   4367 O  OD1 . ASP B 1 245 ? 0.182   19.957  -1.060  1.00 65.45  ? 245 ASP B OD1 1 
ATOM   4368 O  OD2 . ASP B 1 245 ? -1.705  18.815  -1.402  1.00 73.27  ? 245 ASP B OD2 1 
ATOM   4369 N  N   . HIS B 1 246 ? -1.938  21.099  -4.802  1.00 39.33  ? 246 HIS B N   1 
ATOM   4370 C  CA  . HIS B 1 246 ? -1.797  20.446  -6.131  1.00 39.40  ? 246 HIS B CA  1 
ATOM   4371 C  C   . HIS B 1 246 ? -0.888  21.292  -7.030  1.00 40.56  ? 246 HIS B C   1 
ATOM   4372 O  O   . HIS B 1 246 ? 0.002   20.737  -7.718  1.00 33.41  ? 246 HIS B O   1 
ATOM   4373 C  CB  . HIS B 1 246 ? -3.179  20.250  -6.766  1.00 35.41  ? 246 HIS B CB  1 
ATOM   4374 C  CG  . HIS B 1 246 ? -4.069  19.283  -6.056  1.00 35.00  ? 246 HIS B CG  1 
ATOM   4375 N  ND1 . HIS B 1 246 ? -5.460  19.336  -6.179  1.00 35.76  ? 246 HIS B ND1 1 
ATOM   4376 C  CD2 . HIS B 1 246 ? -3.798  18.230  -5.257  1.00 32.48  ? 246 HIS B CD2 1 
ATOM   4377 C  CE1 . HIS B 1 246 ? -5.996  18.358  -5.477  1.00 35.42  ? 246 HIS B CE1 1 
ATOM   4378 N  NE2 . HIS B 1 246 ? -5.006  17.660  -4.916  1.00 33.77  ? 246 HIS B NE2 1 
ATOM   4379 N  N   . VAL B 1 247 ? -1.119  22.604  -7.044  1.00 43.40  ? 247 VAL B N   1 
ATOM   4380 C  CA  . VAL B 1 247 ? -0.339  23.539  -7.898  1.00 44.54  ? 247 VAL B CA  1 
ATOM   4381 C  C   . VAL B 1 247 ? 1.129   23.461  -7.496  1.00 44.82  ? 247 VAL B C   1 
ATOM   4382 O  O   . VAL B 1 247 ? 1.982   23.410  -8.371  1.00 49.22  ? 247 VAL B O   1 
ATOM   4383 C  CB  . VAL B 1 247 ? -0.888  24.978  -7.856  1.00 44.69  ? 247 VAL B CB  1 
ATOM   4384 C  CG1 . VAL B 1 247 ? 0.029   25.950  -8.589  1.00 44.49  ? 247 VAL B CG1 1 
ATOM   4385 C  CG2 . VAL B 1 247 ? -2.304  25.036  -8.423  1.00 43.27  ? 247 VAL B CG2 1 
ATOM   4386 N  N   A ASP B 1 248 ? 1.412   23.429  -6.194  0.25 46.59  ? 248 ASP B N   1 
ATOM   4387 N  N   B ASP B 1 248 ? 1.412   23.429  -6.194  0.25 46.59  ? 248 ASP B N   1 
ATOM   4388 N  N   C ASP B 1 248 ? 1.383   23.485  -6.182  0.25 47.53  ? 248 ASP B N   1 
ATOM   4389 N  N   D ASP B 1 248 ? 1.383   23.485  -6.182  0.25 47.53  ? 248 ASP B N   1 
ATOM   4390 C  CA  A ASP B 1 248 ? 2.798   23.383  -5.655  0.25 45.89  ? 248 ASP B CA  1 
ATOM   4391 C  CA  B ASP B 1 248 ? 2.798   23.383  -5.655  0.25 45.89  ? 248 ASP B CA  1 
ATOM   4392 C  CA  C ASP B 1 248 ? 2.721   23.336  -5.543  0.25 47.55  ? 248 ASP B CA  1 
ATOM   4393 C  CA  D ASP B 1 248 ? 2.721   23.336  -5.543  0.25 47.55  ? 248 ASP B CA  1 
ATOM   4394 C  C   A ASP B 1 248 ? 3.447   22.035  -6.011  0.25 46.21  ? 248 ASP B C   1 
ATOM   4395 C  C   B ASP B 1 248 ? 3.447   22.035  -6.011  0.25 46.21  ? 248 ASP B C   1 
ATOM   4396 C  C   C ASP B 1 248 ? 3.404   22.059  -6.048  0.25 47.24  ? 248 ASP B C   1 
ATOM   4397 C  C   D ASP B 1 248 ? 3.404   22.059  -6.048  0.25 47.24  ? 248 ASP B C   1 
ATOM   4398 O  O   A ASP B 1 248 ? 4.665   22.018  -6.293  0.25 44.86  ? 248 ASP B O   1 
ATOM   4399 O  O   B ASP B 1 248 ? 4.665   22.018  -6.293  0.25 44.86  ? 248 ASP B O   1 
ATOM   4400 O  O   C ASP B 1 248 ? 4.589   22.115  -6.443  0.25 46.51  ? 248 ASP B O   1 
ATOM   4401 O  O   D ASP B 1 248 ? 4.589   22.115  -6.443  0.25 46.51  ? 248 ASP B O   1 
ATOM   4402 C  CB  A ASP B 1 248 ? 2.788   23.671  -4.152  0.25 46.41  ? 248 ASP B CB  1 
ATOM   4403 C  CB  B ASP B 1 248 ? 2.788   23.671  -4.152  0.25 46.41  ? 248 ASP B CB  1 
ATOM   4404 C  CB  C ASP B 1 248 ? 2.586   23.241  -4.020  0.25 48.85  ? 248 ASP B CB  1 
ATOM   4405 C  CB  D ASP B 1 248 ? 2.586   23.241  -4.020  0.25 48.85  ? 248 ASP B CB  1 
ATOM   4406 C  CG  A ASP B 1 248 ? 2.205   25.036  -3.807  0.25 47.21  ? 248 ASP B CG  1 
ATOM   4407 C  CG  B ASP B 1 248 ? 2.205   25.036  -3.807  0.25 47.21  ? 248 ASP B CG  1 
ATOM   4408 C  CG  C ASP B 1 248 ? 2.239   24.549  -3.321  0.25 51.60  ? 248 ASP B CG  1 
ATOM   4409 C  CG  D ASP B 1 248 ? 2.239   24.549  -3.321  0.25 51.60  ? 248 ASP B CG  1 
ATOM   4410 O  OD1 A ASP B 1 248 ? 2.438   25.982  -4.579  0.25 46.08  ? 248 ASP B OD1 1 
ATOM   4411 O  OD1 B ASP B 1 248 ? 2.438   25.982  -4.579  0.25 46.08  ? 248 ASP B OD1 1 
ATOM   4412 O  OD1 C ASP B 1 248 ? 2.103   25.582  -4.017  0.25 50.93  ? 248 ASP B OD1 1 
ATOM   4413 O  OD1 D ASP B 1 248 ? 2.103   25.582  -4.017  0.25 50.93  ? 248 ASP B OD1 1 
ATOM   4414 O  OD2 A ASP B 1 248 ? 1.508   25.144  -2.776  0.25 45.87  ? 248 ASP B OD2 1 
ATOM   4415 O  OD2 B ASP B 1 248 ? 1.508   25.144  -2.776  0.25 45.87  ? 248 ASP B OD2 1 
ATOM   4416 O  OD2 C ASP B 1 248 ? 2.098   24.520  -2.079  0.25 52.89  ? 248 ASP B OD2 1 
ATOM   4417 O  OD2 D ASP B 1 248 ? 2.098   24.520  -2.079  0.25 52.89  ? 248 ASP B OD2 1 
ATOM   4418 N  N   . ILE B 1 249 ? 2.666   20.948  -6.001  1.00 46.27  ? 249 ILE B N   1 
ATOM   4419 C  CA  . ILE B 1 249 ? 3.168   19.577  -6.305  1.00 43.90  ? 249 ILE B CA  1 
ATOM   4420 C  C   . ILE B 1 249 ? 3.507   19.426  -7.795  1.00 41.23  ? 249 ILE B C   1 
ATOM   4421 O  O   . ILE B 1 249 ? 4.449   18.675  -8.100  1.00 46.24  ? 249 ILE B O   1 
ATOM   4422 C  CB  . ILE B 1 249 ? 2.086   18.594  -5.817  1.00 44.92  ? 249 ILE B CB  1 
ATOM   4423 C  CG1 . ILE B 1 249 ? 2.142   18.488  -4.287  1.00 50.73  ? 249 ILE B CG1 1 
ATOM   4424 C  CG2 . ILE B 1 249 ? 2.202   17.246  -6.482  1.00 42.44  ? 249 ILE B CG2 1 
ATOM   4425 C  CD1 . ILE B 1 249 ? 0.976   17.754  -3.651  1.00 45.53  ? 249 ILE B CD1 1 
ATOM   4426 N  N   . LEU B 1 250 ? 2.783   20.112  -8.687  1.00 38.88  ? 250 LEU B N   1 
ATOM   4427 C  CA  . LEU B 1 250 ? 3.097   20.173  -10.145 1.00 39.37  ? 250 LEU B CA  1 
ATOM   4428 C  C   . LEU B 1 250 ? 4.241   21.149  -10.468 1.00 43.81  ? 250 LEU B C   1 
ATOM   4429 O  O   . LEU B 1 250 ? 4.732   21.125  -11.607 1.00 41.78  ? 250 LEU B O   1 
ATOM   4430 C  CB  . LEU B 1 250 ? 1.856   20.607  -10.926 1.00 35.73  ? 250 LEU B CB  1 
ATOM   4431 C  CG  . LEU B 1 250 ? 0.716   19.601  -10.969 1.00 32.45  ? 250 LEU B CG  1 
ATOM   4432 C  CD1 . LEU B 1 250 ? -0.593  20.286  -11.324 1.00 29.57  ? 250 LEU B CD1 1 
ATOM   4433 C  CD2 . LEU B 1 250 ? 1.023   18.493  -11.965 1.00 34.23  ? 250 LEU B CD2 1 
ATOM   4434 N  N   A GLY B 1 251 ? 4.657   21.958  -9.485  0.25 46.11  ? 251 GLY B N   1 
ATOM   4435 N  N   B GLY B 1 251 ? 4.657   21.958  -9.485  0.25 46.11  ? 251 GLY B N   1 
ATOM   4436 N  N   C GLY B 1 251 ? 4.604   22.009  -9.507  0.25 46.20  ? 251 GLY B N   1 
ATOM   4437 N  N   D GLY B 1 251 ? 4.604   22.009  -9.507  0.25 46.20  ? 251 GLY B N   1 
ATOM   4438 C  CA  A GLY B 1 251 ? 5.697   22.999  -9.620  0.25 47.57  ? 251 GLY B CA  1 
ATOM   4439 C  CA  B GLY B 1 251 ? 5.697   22.999  -9.620  0.25 47.57  ? 251 GLY B CA  1 
ATOM   4440 C  CA  C GLY B 1 251 ? 5.666   23.027  -9.634  0.25 47.97  ? 251 GLY B CA  1 
ATOM   4441 C  CA  D GLY B 1 251 ? 5.666   23.027  -9.634  0.25 47.97  ? 251 GLY B CA  1 
ATOM   4442 C  C   A GLY B 1 251 ? 6.891   22.531  -10.447 0.25 48.56  ? 251 GLY B C   1 
ATOM   4443 C  C   B GLY B 1 251 ? 6.891   22.531  -10.447 0.25 48.56  ? 251 GLY B C   1 
ATOM   4444 C  C   C GLY B 1 251 ? 6.822   22.548  -10.506 0.25 49.11  ? 251 GLY B C   1 
ATOM   4445 C  C   D GLY B 1 251 ? 6.822   22.548  -10.506 0.25 49.11  ? 251 GLY B C   1 
ATOM   4446 O  O   A GLY B 1 251 ? 7.273   23.189  -11.412 0.25 50.79  ? 251 GLY B O   1 
ATOM   4447 O  O   B GLY B 1 251 ? 7.273   23.189  -11.412 0.25 50.79  ? 251 GLY B O   1 
ATOM   4448 O  O   C GLY B 1 251 ? 7.075   23.112  -11.568 0.25 51.25  ? 251 GLY B O   1 
ATOM   4449 O  O   D GLY B 1 251 ? 7.075   23.112  -11.568 0.25 51.25  ? 251 GLY B O   1 
ATOM   4450 N  N   A PRO B 1 252 ? 7.522   21.389  -10.094 0.25 49.19  ? 252 PRO B N   1 
ATOM   4451 N  N   B PRO B 1 252 ? 7.522   21.389  -10.094 0.25 49.19  ? 252 PRO B N   1 
ATOM   4452 N  N   C PRO B 1 252 ? 7.561   21.501  -10.075 0.25 50.09  ? 252 PRO B N   1 
ATOM   4453 N  N   D PRO B 1 252 ? 7.561   21.501  -10.075 0.25 50.09  ? 252 PRO B N   1 
ATOM   4454 C  CA  A PRO B 1 252 ? 8.638   20.853  -10.871 0.25 50.38  ? 252 PRO B CA  1 
ATOM   4455 C  CA  B PRO B 1 252 ? 8.638   20.853  -10.871 0.25 50.38  ? 252 PRO B CA  1 
ATOM   4456 C  CA  C PRO B 1 252 ? 8.646   20.923  -10.871 0.25 51.15  ? 252 PRO B CA  1 
ATOM   4457 C  CA  D PRO B 1 252 ? 8.646   20.923  -10.871 0.25 51.15  ? 252 PRO B CA  1 
ATOM   4458 C  C   A PRO B 1 252 ? 8.323   20.731  -12.367 0.25 53.04  ? 252 PRO B C   1 
ATOM   4459 C  C   B PRO B 1 252 ? 8.323   20.731  -12.367 0.25 53.04  ? 252 PRO B C   1 
ATOM   4460 C  C   C PRO B 1 252 ? 8.353   20.667  -12.359 0.25 53.46  ? 252 PRO B C   1 
ATOM   4461 C  C   D PRO B 1 252 ? 8.353   20.667  -12.359 0.25 53.46  ? 252 PRO B C   1 
ATOM   4462 O  O   A PRO B 1 252 ? 9.141   21.149  -13.166 0.25 58.70  ? 252 PRO B O   1 
ATOM   4463 O  O   B PRO B 1 252 ? 9.141   21.149  -13.166 0.25 58.70  ? 252 PRO B O   1 
ATOM   4464 O  O   C PRO B 1 252 ? 9.244   20.908  -13.157 0.25 58.92  ? 252 PRO B O   1 
ATOM   4465 O  O   D PRO B 1 252 ? 9.244   20.908  -13.157 0.25 58.92  ? 252 PRO B O   1 
ATOM   4466 C  CB  A PRO B 1 252 ? 8.856   19.461  -10.264 0.25 49.43  ? 252 PRO B CB  1 
ATOM   4467 C  CB  B PRO B 1 252 ? 8.856   19.461  -10.264 0.25 49.43  ? 252 PRO B CB  1 
ATOM   4468 C  CB  C PRO B 1 252 ? 8.890   19.593  -10.145 0.25 50.32  ? 252 PRO B CB  1 
ATOM   4469 C  CB  D PRO B 1 252 ? 8.890   19.593  -10.145 0.25 50.32  ? 252 PRO B CB  1 
ATOM   4470 C  CG  A PRO B 1 252 ? 8.395   19.617  -8.834  0.25 48.34  ? 252 PRO B CG  1 
ATOM   4471 C  CG  B PRO B 1 252 ? 8.395   19.617  -8.834  0.25 48.34  ? 252 PRO B CG  1 
ATOM   4472 C  CG  C PRO B 1 252 ? 8.636   19.938  -8.697  0.25 49.78  ? 252 PRO B CG  1 
ATOM   4473 C  CG  D PRO B 1 252 ? 8.636   19.938  -8.697  0.25 49.78  ? 252 PRO B CG  1 
ATOM   4474 C  CD  A PRO B 1 252 ? 7.221   20.570  -8.910  0.25 48.91  ? 252 PRO B CD  1 
ATOM   4475 C  CD  B PRO B 1 252 ? 7.221   20.570  -8.910  0.25 48.91  ? 252 PRO B CD  1 
ATOM   4476 C  CD  C PRO B 1 252 ? 7.446   20.874  -8.748  0.25 50.36  ? 252 PRO B CD  1 
ATOM   4477 C  CD  D PRO B 1 252 ? 7.446   20.874  -8.748  0.25 50.36  ? 252 PRO B CD  1 
ATOM   4478 N  N   . LEU B 1 253 ? 7.157   20.167  -12.695 1.00 53.91  ? 253 LEU B N   1 
ATOM   4479 C  CA  . LEU B 1 253 ? 6.749   19.899  -14.104 1.00 52.81  ? 253 LEU B CA  1 
ATOM   4480 C  C   . LEU B 1 253 ? 6.472   21.216  -14.842 1.00 56.23  ? 253 LEU B C   1 
ATOM   4481 O  O   . LEU B 1 253 ? 6.801   21.322  -16.056 1.00 54.00  ? 253 LEU B O   1 
ATOM   4482 C  CB  . LEU B 1 253 ? 5.516   18.988  -14.115 1.00 50.04  ? 253 LEU B CB  1 
ATOM   4483 C  CG  . LEU B 1 253 ? 5.731   17.592  -13.529 1.00 49.47  ? 253 LEU B CG  1 
ATOM   4484 C  CD1 . LEU B 1 253 ? 4.409   16.855  -13.366 1.00 48.95  ? 253 LEU B CD1 1 
ATOM   4485 C  CD2 . LEU B 1 253 ? 6.681   16.784  -14.395 1.00 48.32  ? 253 LEU B CD2 1 
ATOM   4486 N  N   A SER B 1 254 ? 5.873   22.194  -14.151 0.25 55.84  ? 254 SER B N   1 
ATOM   4487 N  N   B SER B 1 254 ? 5.873   22.194  -14.151 0.25 55.84  ? 254 SER B N   1 
ATOM   4488 N  N   C SER B 1 254 ? 5.873   22.183  -14.136 0.25 57.29  ? 254 SER B N   1 
ATOM   4489 N  N   D SER B 1 254 ? 5.873   22.183  -14.136 0.25 57.29  ? 254 SER B N   1 
ATOM   4490 C  CA  A SER B 1 254 ? 5.607   23.557  -14.685 0.25 55.37  ? 254 SER B CA  1 
ATOM   4491 C  CA  B SER B 1 254 ? 5.607   23.557  -14.685 0.25 55.37  ? 254 SER B CA  1 
ATOM   4492 C  CA  C SER B 1 254 ? 5.623   23.563  -14.629 0.25 57.89  ? 254 SER B CA  1 
ATOM   4493 C  CA  D SER B 1 254 ? 5.623   23.563  -14.629 0.25 57.89  ? 254 SER B CA  1 
ATOM   4494 C  C   A SER B 1 254 ? 6.937   24.220  -15.048 0.25 55.13  ? 254 SER B C   1 
ATOM   4495 C  C   B SER B 1 254 ? 6.937   24.220  -15.048 0.25 55.13  ? 254 SER B C   1 
ATOM   4496 C  C   C SER B 1 254 ? 6.967   24.259  -14.863 0.25 57.89  ? 254 SER B C   1 
ATOM   4497 C  C   D SER B 1 254 ? 6.967   24.259  -14.863 0.25 57.89  ? 254 SER B C   1 
ATOM   4498 O  O   A SER B 1 254 ? 7.055   24.760  -16.169 0.25 52.78  ? 254 SER B O   1 
ATOM   4499 O  O   B SER B 1 254 ? 7.055   24.760  -16.169 0.25 52.78  ? 254 SER B O   1 
ATOM   4500 O  O   C SER B 1 254 ? 7.079   25.030  -15.842 0.25 57.38  ? 254 SER B O   1 
ATOM   4501 O  O   D SER B 1 254 ? 7.079   25.030  -15.842 0.25 57.38  ? 254 SER B O   1 
ATOM   4502 C  CB  A SER B 1 254 ? 4.842   24.407  -13.712 0.25 55.50  ? 254 SER B CB  1 
ATOM   4503 C  CB  B SER B 1 254 ? 4.842   24.407  -13.712 0.25 55.50  ? 254 SER B CB  1 
ATOM   4504 C  CB  C SER B 1 254 ? 4.763   24.345  -13.677 0.25 58.49  ? 254 SER B CB  1 
ATOM   4505 C  CB  D SER B 1 254 ? 4.763   24.345  -13.677 0.25 58.49  ? 254 SER B CB  1 
ATOM   4506 O  OG  A SER B 1 254 ? 4.952   25.779  -14.066 0.25 54.00  ? 254 SER B OG  1 
ATOM   4507 O  OG  B SER B 1 254 ? 4.952   25.779  -14.066 0.25 54.00  ? 254 SER B OG  1 
ATOM   4508 O  OG  C SER B 1 254 ? 4.895   25.739  -13.927 0.25 57.84  ? 254 SER B OG  1 
ATOM   4509 O  OG  D SER B 1 254 ? 4.895   25.739  -13.927 0.25 57.84  ? 254 SER B OG  1 
ATOM   4510 N  N   A ALA B 1 255 ? 7.889   24.173  -14.114 0.25 56.22  ? 255 ALA B N   1 
ATOM   4511 N  N   B ALA B 1 255 ? 7.889   24.173  -14.114 0.25 56.22  ? 255 ALA B N   1 
ATOM   4512 N  N   C ALA B 1 255 ? 7.944   23.964  -13.999 0.25 59.48  ? 255 ALA B N   1 
ATOM   4513 N  N   D ALA B 1 255 ? 7.944   23.964  -13.999 0.25 59.48  ? 255 ALA B N   1 
ATOM   4514 C  CA  A ALA B 1 255 ? 9.300   24.558  -14.329 0.25 58.42  ? 255 ALA B CA  1 
ATOM   4515 C  CA  B ALA B 1 255 ? 9.300   24.558  -14.329 0.25 58.42  ? 255 ALA B CA  1 
ATOM   4516 C  CA  C ALA B 1 255 ? 9.351   24.407  -14.117 0.25 61.20  ? 255 ALA B CA  1 
ATOM   4517 C  CA  D ALA B 1 255 ? 9.351   24.407  -14.117 0.25 61.20  ? 255 ALA B CA  1 
ATOM   4518 C  C   A ALA B 1 255 ? 9.789   23.898  -15.618 0.25 59.90  ? 255 ALA B C   1 
ATOM   4519 C  C   B ALA B 1 255 ? 9.789   23.898  -15.618 0.25 59.90  ? 255 ALA B C   1 
ATOM   4520 C  C   C ALA B 1 255 ? 9.917   23.902  -15.451 0.25 62.24  ? 255 ALA B C   1 
ATOM   4521 C  C   D ALA B 1 255 ? 9.917   23.902  -15.451 0.25 62.24  ? 255 ALA B C   1 
ATOM   4522 O  O   A ALA B 1 255 ? 9.896   24.611  -16.633 0.25 58.41  ? 255 ALA B O   1 
ATOM   4523 O  O   B ALA B 1 255 ? 9.896   24.611  -16.633 0.25 58.41  ? 255 ALA B O   1 
ATOM   4524 O  O   C ALA B 1 255 ? 10.210  24.735  -16.328 0.25 61.92  ? 255 ALA B O   1 
ATOM   4525 O  O   D ALA B 1 255 ? 10.210  24.735  -16.328 0.25 61.92  ? 255 ALA B O   1 
ATOM   4526 C  CB  A ALA B 1 255 ? 10.146  24.152  -13.147 0.25 59.50  ? 255 ALA B CB  1 
ATOM   4527 C  CB  B ALA B 1 255 ? 10.146  24.152  -13.147 0.25 59.50  ? 255 ALA B CB  1 
ATOM   4528 C  CB  C ALA B 1 255 ? 10.151  23.897  -12.939 0.25 62.39  ? 255 ALA B CB  1 
ATOM   4529 C  CB  D ALA B 1 255 ? 10.151  23.897  -12.939 0.25 62.39  ? 255 ALA B CB  1 
ATOM   4530 N  N   . GLN B 1 256 ? 9.998   22.576  -15.595 1.00 61.55  ? 256 GLN B N   1 
ATOM   4531 C  CA  . GLN B 1 256 ? 10.748  21.869  -16.665 1.00 60.07  ? 256 GLN B CA  1 
ATOM   4532 C  C   . GLN B 1 256 ? 10.149  22.074  -18.061 1.00 58.33  ? 256 GLN B C   1 
ATOM   4533 O  O   . GLN B 1 256 ? 10.834  21.724  -19.022 1.00 67.01  ? 256 GLN B O   1 
ATOM   4534 C  CB  . GLN B 1 256 ? 10.804  20.383  -16.328 1.00 62.05  ? 256 GLN B CB  1 
ATOM   4535 C  CG  . GLN B 1 256 ? 11.886  19.628  -17.079 1.00 65.39  ? 256 GLN B CG  1 
ATOM   4536 C  CD  . GLN B 1 256 ? 11.410  18.244  -17.435 1.00 68.35  ? 256 GLN B CD  1 
ATOM   4537 O  OE1 . GLN B 1 256 ? 11.173  17.415  -16.561 1.00 73.83  ? 256 GLN B OE1 1 
ATOM   4538 N  NE2 . GLN B 1 256 ? 11.250  17.993  -18.725 1.00 70.30  ? 256 GLN B NE2 1 
ATOM   4539 N  N   . THR B 1 257 ? 8.949   22.626  -18.198 1.00 54.71  ? 257 THR B N   1 
ATOM   4540 C  CA  . THR B 1 257 ? 8.280   22.766  -19.514 1.00 57.63  ? 257 THR B CA  1 
ATOM   4541 C  C   . THR B 1 257 ? 7.982   24.231  -19.884 1.00 58.25  ? 257 THR B C   1 
ATOM   4542 O  O   . THR B 1 257 ? 7.774   24.479  -21.075 1.00 56.22  ? 257 THR B O   1 
ATOM   4543 C  CB  . THR B 1 257 ? 7.004   21.924  -19.509 1.00 57.68  ? 257 THR B CB  1 
ATOM   4544 O  OG1 . THR B 1 257 ? 6.196   22.362  -18.417 1.00 62.50  ? 257 THR B OG1 1 
ATOM   4545 C  CG2 . THR B 1 257 ? 7.298   20.445  -19.390 1.00 57.95  ? 257 THR B CG2 1 
ATOM   4546 N  N   . GLY B 1 258 ? 7.915   25.156  -18.921 1.00 57.06  ? 258 GLY B N   1 
ATOM   4547 C  CA  . GLY B 1 258 ? 7.571   26.566  -19.186 1.00 60.45  ? 258 GLY B CA  1 
ATOM   4548 C  C   . GLY B 1 258 ? 6.072   26.760  -19.354 1.00 66.51  ? 258 GLY B C   1 
ATOM   4549 O  O   . GLY B 1 258 ? 5.641   27.855  -19.818 1.00 60.97  ? 258 GLY B O   1 
ATOM   4550 N  N   . ILE B 1 259 ? 5.284   25.748  -18.986 1.00 61.67  ? 259 ILE B N   1 
ATOM   4551 C  CA  . ILE B 1 259 ? 3.809   25.891  -18.867 1.00 65.55  ? 259 ILE B CA  1 
ATOM   4552 C  C   . ILE B 1 259 ? 3.502   25.899  -17.374 1.00 67.61  ? 259 ILE B C   1 
ATOM   4553 O  O   . ILE B 1 259 ? 3.763   24.886  -16.721 1.00 58.69  ? 259 ILE B O   1 
ATOM   4554 C  CB  . ILE B 1 259 ? 3.061   24.788  -19.636 1.00 68.38  ? 259 ILE B CB  1 
ATOM   4555 C  CG1 . ILE B 1 259 ? 3.514   24.721  -21.098 1.00 69.08  ? 259 ILE B CG1 1 
ATOM   4556 C  CG2 . ILE B 1 259 ? 1.555   24.993  -19.530 1.00 70.18  ? 259 ILE B CG2 1 
ATOM   4557 C  CD1 . ILE B 1 259 ? 4.696   23.830  -21.337 1.00 67.59  ? 259 ILE B CD1 1 
ATOM   4558 N  N   . ALA B 1 260 ? 3.053   27.044  -16.860 1.00 67.05  ? 260 ALA B N   1 
ATOM   4559 C  CA  . ALA B 1 260 ? 2.658   27.220  -15.448 1.00 65.73  ? 260 ALA B CA  1 
ATOM   4560 C  C   . ALA B 1 260 ? 1.306   26.550  -15.243 1.00 54.79  ? 260 ALA B C   1 
ATOM   4561 O  O   . ALA B 1 260 ? 0.526   26.505  -16.192 1.00 56.29  ? 260 ALA B O   1 
ATOM   4562 C  CB  . ALA B 1 260 ? 2.625   28.680  -15.075 1.00 72.58  ? 260 ALA B CB  1 
ATOM   4563 N  N   . VAL B 1 261 ? 1.039   26.064  -14.039 1.00 51.59  ? 261 VAL B N   1 
ATOM   4564 C  CA  . VAL B 1 261 ? -0.119  25.154  -13.796 1.00 48.34  ? 261 VAL B CA  1 
ATOM   4565 C  C   . VAL B 1 261 ? -1.393  25.789  -14.356 1.00 47.63  ? 261 VAL B C   1 
ATOM   4566 O  O   . VAL B 1 261 ? -2.102  25.120  -15.132 1.00 44.79  ? 261 VAL B O   1 
ATOM   4567 C  CB  . VAL B 1 261 ? -0.246  24.777  -12.312 1.00 45.32  ? 261 VAL B CB  1 
ATOM   4568 C  CG1 . VAL B 1 261 ? -1.411  23.821  -12.095 1.00 50.90  ? 261 VAL B CG1 1 
ATOM   4569 C  CG2 . VAL B 1 261 ? 1.053   24.181  -11.786 1.00 46.79  ? 261 VAL B CG2 1 
ATOM   4570 N  N   . LEU B 1 262 ? -1.681  27.053  -14.036 1.00 52.07  ? 262 LEU B N   1 
ATOM   4571 C  CA  . LEU B 1 262 ? -2.948  27.685  -14.500 1.00 46.65  ? 262 LEU B CA  1 
ATOM   4572 C  C   . LEU B 1 262 ? -2.881  27.932  -16.017 1.00 41.87  ? 262 LEU B C   1 
ATOM   4573 O  O   . LEU B 1 262 ? -3.930  27.864  -16.682 1.00 42.48  ? 262 LEU B O   1 
ATOM   4574 C  CB  . LEU B 1 262 ? -3.197  28.963  -13.693 1.00 53.70  ? 262 LEU B CB  1 
ATOM   4575 C  CG  . LEU B 1 262 ? -3.544  28.742  -12.219 1.00 52.02  ? 262 LEU B CG  1 
ATOM   4576 C  CD1 . LEU B 1 262 ? -3.255  29.991  -11.410 1.00 56.58  ? 262 LEU B CD1 1 
ATOM   4577 C  CD2 . LEU B 1 262 ? -4.999  28.323  -12.057 1.00 51.71  ? 262 LEU B CD2 1 
ATOM   4578 N  N   . ASP B 1 263 ? -1.689  28.159  -16.563 1.00 44.99  ? 263 ASP B N   1 
ATOM   4579 C  CA  . ASP B 1 263 ? -1.451  28.039  -18.032 1.00 50.26  ? 263 ASP B CA  1 
ATOM   4580 C  C   . ASP B 1 263 ? -1.957  26.649  -18.466 1.00 45.86  ? 263 ASP B C   1 
ATOM   4581 O  O   . ASP B 1 263 ? -2.884  26.567  -19.300 1.00 39.96  ? 263 ASP B O   1 
ATOM   4582 C  CB  . ASP B 1 263 ? 0.026   28.310  -18.339 1.00 50.48  ? 263 ASP B CB  1 
ATOM   4583 C  CG  . ASP B 1 263 ? 0.420   28.433  -19.801 1.00 50.12  ? 263 ASP B CG  1 
ATOM   4584 O  OD1 . ASP B 1 263 ? -0.452  28.282  -20.698 1.00 41.24  ? 263 ASP B OD1 1 
ATOM   4585 O  OD2 . ASP B 1 263 ? 1.615   28.667  -20.025 1.00 54.01  ? 263 ASP B OD2 1 
ATOM   4586 N  N   . MET B 1 264 ? -1.428  25.581  -17.864 1.00 41.94  ? 264 MET B N   1 
ATOM   4587 C  CA  . MET B 1 264 ? -1.873  24.208  -18.226 1.00 42.62  ? 264 MET B CA  1 
ATOM   4588 C  C   . MET B 1 264 ? -3.356  24.047  -17.880 1.00 41.92  ? 264 MET B C   1 
ATOM   4589 O  O   . MET B 1 264 ? -4.064  23.426  -18.676 1.00 40.30  ? 264 MET B O   1 
ATOM   4590 C  CB  . MET B 1 264 ? -1.050  23.124  -17.530 1.00 38.72  ? 264 MET B CB  1 
ATOM   4591 C  CG  . MET B 1 264 ? -1.302  21.751  -18.116 1.00 38.21  ? 264 MET B CG  1 
ATOM   4592 S  SD  . MET B 1 264 ? -0.680  21.621  -19.817 1.00 37.27  ? 264 MET B SD  1 
ATOM   4593 C  CE  . MET B 1 264 ? 1.023   21.297  -19.393 1.00 37.74  ? 264 MET B CE  1 
ATOM   4594 N  N   . CYS B 1 265 ? -3.840  24.598  -16.753 1.00 43.64  ? 265 CYS B N   1 
ATOM   4595 C  CA  . CYS B 1 265 ? -5.278  24.453  -16.390 1.00 44.72  ? 265 CYS B CA  1 
ATOM   4596 C  C   . CYS B 1 265 ? -6.111  25.070  -17.506 1.00 39.67  ? 265 CYS B C   1 
ATOM   4597 O  O   . CYS B 1 265 ? -7.167  24.528  -17.820 1.00 38.64  ? 265 CYS B O   1 
ATOM   4598 C  CB  . CYS B 1 265 ? -5.659  25.087  -15.055 1.00 49.05  ? 265 CYS B CB  1 
ATOM   4599 S  SG  . CYS B 1 265 ? -4.741  24.445  -13.635 1.00 48.07  ? 265 CYS B SG  1 
ATOM   4600 N  N   . ALA B 1 266 ? -5.617  26.153  -18.120 1.00 50.29  ? 266 ALA B N   1 
ATOM   4601 C  CA  . ALA B 1 266 ? -6.291  26.838  -19.255 1.00 48.29  ? 266 ALA B CA  1 
ATOM   4602 C  C   . ALA B 1 266 ? -6.382  25.886  -20.456 1.00 41.95  ? 266 ALA B C   1 
ATOM   4603 O  O   . ALA B 1 266 ? -7.473  25.776  -21.049 1.00 36.44  ? 266 ALA B O   1 
ATOM   4604 C  CB  . ALA B 1 266 ? -5.574  28.128  -19.596 1.00 51.64  ? 266 ALA B CB  1 
ATOM   4605 N  N   . SER B 1 267 ? -5.293  25.163  -20.765 1.00 46.85  ? 267 SER B N   1 
ATOM   4606 C  CA  . SER B 1 267 ? -5.307  24.041  -21.755 1.00 42.13  ? 267 SER B CA  1 
ATOM   4607 C  C   . SER B 1 267 ? -6.414  23.052  -21.354 1.00 35.18  ? 267 SER B C   1 
ATOM   4608 O  O   . SER B 1 267 ? -7.270  22.771  -22.186 1.00 31.19  ? 267 SER B O   1 
ATOM   4609 C  CB  . SER B 1 267 ? -3.941  23.369  -21.885 1.00 43.15  ? 267 SER B CB  1 
ATOM   4610 O  OG  . SER B 1 267 ? -2.928  24.266  -22.361 1.00 46.11  ? 267 SER B OG  1 
ATOM   4611 N  N   . LEU B 1 268 ? -6.435  22.585  -20.091 1.00 38.44  ? 268 LEU B N   1 
ATOM   4612 C  CA  . LEU B 1 268 ? -7.425  21.556  -19.641 1.00 37.25  ? 268 LEU B CA  1 
ATOM   4613 C  C   . LEU B 1 268 ? -8.840  22.139  -19.612 1.00 37.78  ? 268 LEU B C   1 
ATOM   4614 O  O   . LEU B 1 268 ? -9.791  21.439  -20.043 1.00 34.18  ? 268 LEU B O   1 
ATOM   4615 C  CB  . LEU B 1 268 ? -7.031  21.015  -18.263 1.00 38.59  ? 268 LEU B CB  1 
ATOM   4616 C  CG  . LEU B 1 268 ? -8.029  20.038  -17.620 1.00 38.39  ? 268 LEU B CG  1 
ATOM   4617 C  CD1 . LEU B 1 268 ? -8.373  18.868  -18.537 1.00 38.48  ? 268 LEU B CD1 1 
ATOM   4618 C  CD2 . LEU B 1 268 ? -7.491  19.531  -16.296 1.00 37.27  ? 268 LEU B CD2 1 
ATOM   4619 N  N   . LYS B 1 269 ? -8.994  23.377  -19.125 1.00 42.96  ? 269 LYS B N   1 
ATOM   4620 C  CA  . LYS B 1 269 ? -10.295 24.090  -19.236 1.00 51.41  ? 269 LYS B CA  1 
ATOM   4621 C  C   . LYS B 1 269 ? -10.821 23.871  -20.660 1.00 45.69  ? 269 LYS B C   1 
ATOM   4622 O  O   . LYS B 1 269 ? -11.943 23.392  -20.824 1.00 44.52  ? 269 LYS B O   1 
ATOM   4623 C  CB  . LYS B 1 269 ? -10.120 25.574  -18.880 1.00 56.64  ? 269 LYS B CB  1 
ATOM   4624 C  CG  . LYS B 1 269 ? -11.353 26.457  -19.067 1.00 67.58  ? 269 LYS B CG  1 
ATOM   4625 C  CD  . LYS B 1 269 ? -11.082 27.950  -18.918 1.00 97.53  ? 269 LYS B CD  1 
ATOM   4626 C  CE  . LYS B 1 269 ? -10.789 28.360  -17.489 1.00 101.73 ? 269 LYS B CE  1 
ATOM   4627 N  NZ  . LYS B 1 269 ? -10.827 29.831  -17.307 1.00 112.29 ? 269 LYS B NZ  1 
ATOM   4628 N  N   . GLU B 1 270 ? -9.999  24.176  -21.672 1.00 50.78  ? 270 GLU B N   1 
ATOM   4629 C  CA  . GLU B 1 270 ? -10.435 24.161  -23.100 1.00 52.08  ? 270 GLU B CA  1 
ATOM   4630 C  C   . GLU B 1 270 ? -10.757 22.728  -23.533 1.00 45.82  ? 270 GLU B C   1 
ATOM   4631 O  O   . GLU B 1 270 ? -11.684 22.578  -24.344 1.00 41.26  ? 270 GLU B O   1 
ATOM   4632 C  CB  . GLU B 1 270 ? -9.383  24.777  -24.037 1.00 53.42  ? 270 GLU B CB  1 
ATOM   4633 C  CG  . GLU B 1 270 ? -9.091  26.252  -23.776 1.00 56.58  ? 270 GLU B CG  1 
ATOM   4634 C  CD  . GLU B 1 270 ? -10.307 27.176  -23.811 1.00 55.26  ? 270 GLU B CD  1 
ATOM   4635 O  OE1 . GLU B 1 270 ? -11.167 26.967  -24.687 1.00 51.65  ? 270 GLU B OE1 1 
ATOM   4636 O  OE2 . GLU B 1 270 ? -10.403 28.085  -22.939 1.00 48.41  ? 270 GLU B OE2 1 
ATOM   4637 N  N   . LEU B 1 271 ? -9.994  21.725  -23.070 1.00 41.46  ? 271 LEU B N   1 
ATOM   4638 C  CA  . LEU B 1 271 ? -10.227 20.316  -23.507 1.00 42.71  ? 271 LEU B CA  1 
ATOM   4639 C  C   . LEU B 1 271 ? -11.568 19.811  -22.980 1.00 38.11  ? 271 LEU B C   1 
ATOM   4640 O  O   . LEU B 1 271 ? -12.198 19.063  -23.701 1.00 42.51  ? 271 LEU B O   1 
ATOM   4641 C  CB  . LEU B 1 271 ? -9.085  19.394  -23.070 1.00 40.49  ? 271 LEU B CB  1 
ATOM   4642 C  CG  . LEU B 1 271 ? -7.787  19.578  -23.853 1.00 38.26  ? 271 LEU B CG  1 
ATOM   4643 C  CD1 . LEU B 1 271 ? -6.585  19.141  -23.032 1.00 38.86  ? 271 LEU B CD1 1 
ATOM   4644 C  CD2 . LEU B 1 271 ? -7.834  18.825  -25.166 1.00 40.40  ? 271 LEU B CD2 1 
ATOM   4645 N  N   . LEU B 1 272 ? -11.971 20.170  -21.760 1.00 41.62  ? 272 LEU B N   1 
ATOM   4646 C  CA  . LEU B 1 272 ? -13.281 19.729  -21.200 1.00 46.00  ? 272 LEU B CA  1 
ATOM   4647 C  C   . LEU B 1 272 ? -14.424 20.393  -21.979 1.00 52.25  ? 272 LEU B C   1 
ATOM   4648 O  O   . LEU B 1 272 ? -15.425 19.700  -22.303 1.00 51.28  ? 272 LEU B O   1 
ATOM   4649 C  CB  . LEU B 1 272 ? -13.358 20.122  -19.724 1.00 47.51  ? 272 LEU B CB  1 
ATOM   4650 C  CG  . LEU B 1 272 ? -12.293 19.514  -18.815 1.00 47.80  ? 272 LEU B CG  1 
ATOM   4651 C  CD1 . LEU B 1 272 ? -12.445 20.003  -17.383 1.00 45.92  ? 272 LEU B CD1 1 
ATOM   4652 C  CD2 . LEU B 1 272 ? -12.347 17.995  -18.866 1.00 50.17  ? 272 LEU B CD2 1 
ATOM   4653 N  N   . GLN B 1 273 ? -14.274 21.698  -22.245 1.00 58.14  ? 273 GLN B N   1 
ATOM   4654 C  CA  . GLN B 1 273 ? -15.275 22.524  -22.973 1.00 59.97  ? 273 GLN B CA  1 
ATOM   4655 C  C   . GLN B 1 273 ? -15.392 22.044  -24.431 1.00 56.75  ? 273 GLN B C   1 
ATOM   4656 O  O   . GLN B 1 273 ? -16.526 21.934  -24.889 1.00 65.63  ? 273 GLN B O   1 
ATOM   4657 C  CB  . GLN B 1 273 ? -14.932 24.013  -22.807 1.00 59.76  ? 273 GLN B CB  1 
ATOM   4658 C  CG  . GLN B 1 273 ? -15.300 24.539  -21.418 1.00 60.39  ? 273 GLN B CG  1 
ATOM   4659 C  CD  . GLN B 1 273 ? -14.698 25.869  -21.008 1.00 62.17  ? 273 GLN B CD  1 
ATOM   4660 O  OE1 . GLN B 1 273 ? -13.622 26.261  -21.448 1.00 63.90  ? 273 GLN B OE1 1 
ATOM   4661 N  NE2 . GLN B 1 273 ? -15.389 26.586  -20.133 1.00 50.99  ? 273 GLN B NE2 1 
ATOM   4662 N  N   . ASN B 1 274 ? -14.293 21.710  -25.126 1.00 55.08  ? 274 ASN B N   1 
ATOM   4663 C  CA  . ASN B 1 274 ? -14.312 21.530  -26.612 1.00 59.65  ? 274 ASN B CA  1 
ATOM   4664 C  C   . ASN B 1 274 ? -13.987 20.090  -27.054 1.00 55.91  ? 274 ASN B C   1 
ATOM   4665 O  O   . ASN B 1 274 ? -14.116 19.812  -28.263 1.00 53.01  ? 274 ASN B O   1 
ATOM   4666 C  CB  . ASN B 1 274 ? -13.366 22.519  -27.305 1.00 53.67  ? 274 ASN B CB  1 
ATOM   4667 C  CG  . ASN B 1 274 ? -13.735 23.972  -27.075 1.00 55.58  ? 274 ASN B CG  1 
ATOM   4668 O  OD1 . ASN B 1 274 ? -14.520 24.540  -27.829 1.00 61.54  ? 274 ASN B OD1 1 
ATOM   4669 N  ND2 . ASN B 1 274 ? -13.175 24.591  -26.045 1.00 54.36  ? 274 ASN B ND2 1 
ATOM   4670 N  N   . GLY B 1 275 ? -13.578 19.208  -26.139 1.00 58.44  ? 275 GLY B N   1 
ATOM   4671 C  CA  . GLY B 1 275 ? -13.050 17.873  -26.484 1.00 58.94  ? 275 GLY B CA  1 
ATOM   4672 C  C   . GLY B 1 275 ? -11.624 17.972  -27.004 1.00 55.45  ? 275 GLY B C   1 
ATOM   4673 O  O   . GLY B 1 275 ? -10.950 18.993  -26.727 1.00 43.97  ? 275 GLY B O   1 
ATOM   4674 N  N   . MET B 1 276 ? -11.181 16.946  -27.734 1.00 61.80  ? 276 MET B N   1 
ATOM   4675 C  CA  . MET B 1 276 ? -9.783  16.796  -28.221 1.00 63.00  ? 276 MET B CA  1 
ATOM   4676 C  C   . MET B 1 276 ? -9.717  17.143  -29.716 1.00 64.81  ? 276 MET B C   1 
ATOM   4677 O  O   . MET B 1 276 ? -8.613  17.045  -30.288 1.00 67.18  ? 276 MET B O   1 
ATOM   4678 C  CB  . MET B 1 276 ? -9.293  15.362  -27.981 1.00 63.83  ? 276 MET B CB  1 
ATOM   4679 C  CG  . MET B 1 276 ? -8.001  15.292  -27.173 1.00 68.12  ? 276 MET B CG  1 
ATOM   4680 S  SD  . MET B 1 276 ? -7.757  13.720  -26.290 1.00 56.26  ? 276 MET B SD  1 
ATOM   4681 C  CE  . MET B 1 276 ? -9.185  13.768  -25.211 1.00 44.13  ? 276 MET B CE  1 
ATOM   4682 N  N   . ASN B 1 277 ? -10.843 17.576  -30.303 1.00 59.90  ? 277 ASN B N   1 
ATOM   4683 C  CA  . ASN B 1 277 ? -10.992 17.899  -31.748 1.00 66.72  ? 277 ASN B CA  1 
ATOM   4684 C  C   . ASN B 1 277 ? -10.361 16.757  -32.546 1.00 60.40  ? 277 ASN B C   1 
ATOM   4685 O  O   . ASN B 1 277 ? -9.538  17.032  -33.431 1.00 59.37  ? 277 ASN B O   1 
ATOM   4686 C  CB  . ASN B 1 277 ? -10.444 19.289  -32.101 1.00 71.35  ? 277 ASN B CB  1 
ATOM   4687 C  CG  . ASN B 1 277 ? -11.387 20.403  -31.677 1.00 78.84  ? 277 ASN B CG  1 
ATOM   4688 O  OD1 . ASN B 1 277 ? -10.994 21.334  -30.971 1.00 80.50  ? 277 ASN B OD1 1 
ATOM   4689 N  ND2 . ASN B 1 277 ? -12.647 20.305  -32.080 1.00 73.41  ? 277 ASN B ND2 1 
ATOM   4690 N  N   . GLY B 1 278 ? -10.724 15.525  -32.179 1.00 60.37  ? 278 GLY B N   1 
ATOM   4691 C  CA  . GLY B 1 278 ? -10.412 14.292  -32.921 1.00 58.23  ? 278 GLY B CA  1 
ATOM   4692 C  C   . GLY B 1 278 ? -8.942  13.944  -32.873 1.00 58.28  ? 278 GLY B C   1 
ATOM   4693 O  O   . GLY B 1 278 ? -8.480  13.242  -33.783 1.00 62.47  ? 278 GLY B O   1 
ATOM   4694 N  N   . ARG B 1 279 ? -8.219  14.403  -31.854 1.00 58.15  ? 279 ARG B N   1 
ATOM   4695 C  CA  . ARG B 1 279 ? -6.774  14.090  -31.697 1.00 59.69  ? 279 ARG B CA  1 
ATOM   4696 C  C   . ARG B 1 279 ? -6.594  13.083  -30.549 1.00 51.74  ? 279 ARG B C   1 
ATOM   4697 O  O   . ARG B 1 279 ? -7.600  12.502  -30.045 1.00 48.21  ? 279 ARG B O   1 
ATOM   4698 C  CB  . ARG B 1 279 ? -5.953  15.379  -31.535 1.00 66.16  ? 279 ARG B CB  1 
ATOM   4699 C  CG  . ARG B 1 279 ? -5.564  16.019  -32.861 1.00 70.28  ? 279 ARG B CG  1 
ATOM   4700 C  CD  . ARG B 1 279 ? -4.929  17.391  -32.737 1.00 78.90  ? 279 ARG B CD  1 
ATOM   4701 N  NE  . ARG B 1 279 ? -5.926  18.458  -32.657 1.00 88.50  ? 279 ARG B NE  1 
ATOM   4702 C  CZ  . ARG B 1 279 ? -5.767  19.711  -33.100 1.00 86.33  ? 279 ARG B CZ  1 
ATOM   4703 N  NH1 . ARG B 1 279 ? -4.638  20.097  -33.680 1.00 79.16  ? 279 ARG B NH1 1 
ATOM   4704 N  NH2 . ARG B 1 279 ? -6.758  20.576  -32.965 1.00 86.94  ? 279 ARG B NH2 1 
ATOM   4705 N  N   . THR B 1 280 ? -5.334  12.797  -30.239 1.00 47.53  ? 280 THR B N   1 
ATOM   4706 C  CA  . THR B 1 280 ? -4.916  11.963  -29.094 1.00 38.84  ? 280 THR B CA  1 
ATOM   4707 C  C   . THR B 1 280 ? -3.787  12.681  -28.375 1.00 35.31  ? 280 THR B C   1 
ATOM   4708 O  O   . THR B 1 280 ? -3.091  13.528  -28.983 1.00 36.18  ? 280 THR B O   1 
ATOM   4709 C  CB  . THR B 1 280 ? -4.480  10.563  -29.527 1.00 37.46  ? 280 THR B CB  1 
ATOM   4710 O  OG1 . THR B 1 280 ? -3.335  10.692  -30.367 1.00 35.40  ? 280 THR B OG1 1 
ATOM   4711 C  CG2 . THR B 1 280 ? -5.576  9.818   -30.250 1.00 40.19  ? 280 THR B CG2 1 
ATOM   4712 N  N   . ILE B 1 281 ? -3.647  12.336  -27.107 1.00 33.15  ? 281 ILE B N   1 
ATOM   4713 C  CA  . ILE B 1 281 ? -2.559  12.794  -26.217 1.00 31.31  ? 281 ILE B CA  1 
ATOM   4714 C  C   . ILE B 1 281 ? -1.922  11.528  -25.660 1.00 28.63  ? 281 ILE B C   1 
ATOM   4715 O  O   . ILE B 1 281 ? -2.640  10.719  -25.062 1.00 28.46  ? 281 ILE B O   1 
ATOM   4716 C  CB  . ILE B 1 281 ? -3.100  13.734  -25.121 1.00 32.33  ? 281 ILE B CB  1 
ATOM   4717 C  CG1 . ILE B 1 281 ? -3.744  14.993  -25.717 1.00 36.28  ? 281 ILE B CG1 1 
ATOM   4718 C  CG2 . ILE B 1 281 ? -1.979  14.071  -24.156 1.00 34.13  ? 281 ILE B CG2 1 
ATOM   4719 C  CD1 . ILE B 1 281 ? -4.381  15.956  -24.706 1.00 34.63  ? 281 ILE B CD1 1 
ATOM   4720 N  N   . LEU B 1 282 ? -0.634  11.340  -25.922 1.00 29.21  ? 282 LEU B N   1 
ATOM   4721 C  CA  . LEU B 1 282 ? 0.104   10.113  -25.533 1.00 29.81  ? 282 LEU B CA  1 
ATOM   4722 C  C   . LEU B 1 282 ? -0.709  8.866   -25.892 1.00 27.22  ? 282 LEU B C   1 
ATOM   4723 O  O   . LEU B 1 282 ? -0.844  7.994   -25.038 1.00 26.97  ? 282 LEU B O   1 
ATOM   4724 C  CB  . LEU B 1 282 ? 0.363   10.170  -24.026 1.00 29.46  ? 282 LEU B CB  1 
ATOM   4725 C  CG  . LEU B 1 282 ? 1.459   11.131  -23.595 1.00 31.31  ? 282 LEU B CG  1 
ATOM   4726 C  CD1 . LEU B 1 282 ? 1.597   11.165  -22.085 1.00 30.35  ? 282 LEU B CD1 1 
ATOM   4727 C  CD2 . LEU B 1 282 ? 2.783   10.770  -24.255 1.00 33.03  ? 282 LEU B CD2 1 
ATOM   4728 N  N   . GLY B 1 283 ? -1.267  8.793   -27.091 1.00 30.89  ? 283 GLY B N   1 
ATOM   4729 C  CA  . GLY B 1 283 ? -2.000  7.606   -27.585 1.00 31.84  ? 283 GLY B CA  1 
ATOM   4730 C  C   . GLY B 1 283 ? -3.259  7.285   -26.777 1.00 32.75  ? 283 GLY B C   1 
ATOM   4731 O  O   . GLY B 1 283 ? -3.630  6.114   -26.704 1.00 32.45  ? 283 GLY B O   1 
ATOM   4732 N  N   . SER B 1 284 ? -3.909  8.277   -26.171 1.00 33.88  ? 284 SER B N   1 
ATOM   4733 C  CA  . SER B 1 284 ? -5.233  8.102   -25.527 1.00 33.39  ? 284 SER B CA  1 
ATOM   4734 C  C   . SER B 1 284 ? -6.217  9.101   -26.139 1.00 30.46  ? 284 SER B C   1 
ATOM   4735 O  O   . SER B 1 284 ? -5.795  10.238  -26.443 1.00 28.92  ? 284 SER B O   1 
ATOM   4736 C  CB  . SER B 1 284 ? -5.154  8.267   -24.038 1.00 34.03  ? 284 SER B CB  1 
ATOM   4737 O  OG  . SER B 1 284 ? -6.442  8.069   -23.474 1.00 36.51  ? 284 SER B OG  1 
ATOM   4738 N  N   . ALA B 1 285 ? -7.462  8.679   -26.303 1.00 32.95  ? 285 ALA B N   1 
ATOM   4739 C  CA  . ALA B 1 285 ? -8.569  9.573   -26.701 1.00 39.90  ? 285 ALA B CA  1 
ATOM   4740 C  C   . ALA B 1 285 ? -9.256  10.123  -25.438 1.00 41.47  ? 285 ALA B C   1 
ATOM   4741 O  O   . ALA B 1 285 ? -10.066 11.055  -25.588 1.00 46.80  ? 285 ALA B O   1 
ATOM   4742 C  CB  . ALA B 1 285 ? -9.535  8.849   -27.619 1.00 40.49  ? 285 ALA B CB  1 
ATOM   4743 N  N   . LEU B 1 286 ? -8.936  9.595   -24.249 1.00 34.47  ? 286 LEU B N   1 
ATOM   4744 C  CA  . LEU B 1 286 ? -9.492  10.071  -22.954 1.00 35.95  ? 286 LEU B CA  1 
ATOM   4745 C  C   . LEU B 1 286 ? -8.466  10.957  -22.256 1.00 31.34  ? 286 LEU B C   1 
ATOM   4746 O  O   . LEU B 1 286 ? -7.274  10.835  -22.563 1.00 29.39  ? 286 LEU B O   1 
ATOM   4747 C  CB  . LEU B 1 286 ? -9.795  8.876   -22.048 1.00 41.55  ? 286 LEU B CB  1 
ATOM   4748 C  CG  . LEU B 1 286 ? -10.882 7.934   -22.547 1.00 43.39  ? 286 LEU B CG  1 
ATOM   4749 C  CD1 . LEU B 1 286 ? -10.834 6.607   -21.812 1.00 43.29  ? 286 LEU B CD1 1 
ATOM   4750 C  CD2 . LEU B 1 286 ? -12.246 8.584   -22.387 1.00 50.88  ? 286 LEU B CD2 1 
ATOM   4751 N  N   . LEU B 1 287 ? -8.923  11.771  -21.309 1.00 27.55  ? 287 LEU B N   1 
ATOM   4752 C  CA  . LEU B 1 287 ? -8.040  12.503  -20.378 1.00 31.27  ? 287 LEU B CA  1 
ATOM   4753 C  C   . LEU B 1 287 ? -7.665  11.544  -19.237 1.00 31.85  ? 287 LEU B C   1 
ATOM   4754 O  O   . LEU B 1 287 ? -8.536  11.250  -18.416 1.00 32.36  ? 287 LEU B O   1 
ATOM   4755 C  CB  . LEU B 1 287 ? -8.768  13.768  -19.904 1.00 30.46  ? 287 LEU B CB  1 
ATOM   4756 C  CG  . LEU B 1 287 ? -8.964  14.827  -20.996 1.00 31.76  ? 287 LEU B CG  1 
ATOM   4757 C  CD1 . LEU B 1 287 ? -9.536  16.113  -20.425 1.00 36.71  ? 287 LEU B CD1 1 
ATOM   4758 C  CD2 . LEU B 1 287 ? -7.677  15.157  -21.716 1.00 31.94  ? 287 LEU B CD2 1 
ATOM   4759 N  N   . GLU B 1 288 ? -6.422  11.052  -19.221 1.00 30.31  ? 288 GLU B N   1 
ATOM   4760 C  CA  . GLU B 1 288 ? -5.969  9.980   -18.291 1.00 32.68  ? 288 GLU B CA  1 
ATOM   4761 C  C   . GLU B 1 288 ? -5.675  10.566  -16.904 1.00 28.67  ? 288 GLU B C   1 
ATOM   4762 O  O   . GLU B 1 288 ? -4.918  11.548  -16.805 1.00 26.32  ? 288 GLU B O   1 
ATOM   4763 C  CB  . GLU B 1 288 ? -4.722  9.274   -18.831 1.00 35.01  ? 288 GLU B CB  1 
ATOM   4764 C  CG  . GLU B 1 288 ? -4.986  8.437   -20.071 1.00 40.24  ? 288 GLU B CG  1 
ATOM   4765 C  CD  . GLU B 1 288 ? -5.732  7.133   -19.818 1.00 43.53  ? 288 GLU B CD  1 
ATOM   4766 O  OE1 . GLU B 1 288 ? -5.485  6.492   -18.780 1.00 44.01  ? 288 GLU B OE1 1 
ATOM   4767 O  OE2 . GLU B 1 288 ? -6.542  6.760   -20.679 1.00 52.22  ? 288 GLU B OE2 1 
ATOM   4768 N  N   . ASP B 1 289 ? -6.199  9.941   -15.852 1.00 27.19  ? 289 ASP B N   1 
ATOM   4769 C  CA  . ASP B 1 289 ? -6.126  10.503  -14.480 1.00 25.00  ? 289 ASP B CA  1 
ATOM   4770 C  C   . ASP B 1 289 ? -5.522  9.508   -13.498 1.00 24.56  ? 289 ASP B C   1 
ATOM   4771 O  O   . ASP B 1 289 ? -5.676  9.763   -12.292 1.00 24.10  ? 289 ASP B O   1 
ATOM   4772 C  CB  . ASP B 1 289 ? -7.502  11.005  -14.028 1.00 26.06  ? 289 ASP B CB  1 
ATOM   4773 C  CG  . ASP B 1 289 ? -8.465  9.933   -13.551 1.00 25.31  ? 289 ASP B CG  1 
ATOM   4774 O  OD1 . ASP B 1 289 ? -8.229  8.764   -13.833 1.00 23.74  ? 289 ASP B OD1 1 
ATOM   4775 O  OD2 . ASP B 1 289 ? -9.447  10.293  -12.844 1.00 27.67  ? 289 ASP B OD2 1 
ATOM   4776 N  N   . GLU B 1 290 ? -4.817  8.458   -13.966 1.00 23.35  ? 290 GLU B N   1 
ATOM   4777 C  CA  . GLU B 1 290 ? -4.176  7.484   -13.049 1.00 24.08  ? 290 GLU B CA  1 
ATOM   4778 C  C   . GLU B 1 290 ? -2.644  7.655   -13.047 1.00 23.88  ? 290 GLU B C   1 
ATOM   4779 O  O   . GLU B 1 290 ? -1.938  6.703   -12.663 1.00 27.52  ? 290 GLU B O   1 
ATOM   4780 C  CB  . GLU B 1 290 ? -4.701  6.073   -13.351 1.00 24.58  ? 290 GLU B CB  1 
ATOM   4781 C  CG  . GLU B 1 290 ? -6.205  5.951   -13.081 1.00 27.13  ? 290 GLU B CG  1 
ATOM   4782 C  CD  . GLU B 1 290 ? -6.733  4.618   -12.534 1.00 26.08  ? 290 GLU B CD  1 
ATOM   4783 O  OE1 . GLU B 1 290 ? -5.983  3.627   -12.563 1.00 25.93  ? 290 GLU B OE1 1 
ATOM   4784 O  OE2 . GLU B 1 290 ? -7.894  4.577   -12.056 1.00 25.54  ? 290 GLU B OE2 1 
ATOM   4785 N  N   . PHE B 1 291 ? -2.117  8.834   -13.390 1.00 23.09  ? 291 PHE B N   1 
ATOM   4786 C  CA  . PHE B 1 291 ? -0.679  9.144   -13.187 1.00 22.94  ? 291 PHE B CA  1 
ATOM   4787 C  C   . PHE B 1 291 ? -0.561  10.350  -12.258 1.00 24.26  ? 291 PHE B C   1 
ATOM   4788 O  O   . PHE B 1 291 ? -1.105  11.404  -12.573 1.00 22.89  ? 291 PHE B O   1 
ATOM   4789 C  CB  . PHE B 1 291 ? 0.048   9.486   -14.477 1.00 23.83  ? 291 PHE B CB  1 
ATOM   4790 C  CG  . PHE B 1 291 ? 0.076   8.393   -15.507 1.00 26.48  ? 291 PHE B CG  1 
ATOM   4791 C  CD1 . PHE B 1 291 ? -0.894  8.316   -16.493 1.00 29.55  ? 291 PHE B CD1 1 
ATOM   4792 C  CD2 . PHE B 1 291 ? 1.099   7.459   -15.495 1.00 28.63  ? 291 PHE B CD2 1 
ATOM   4793 C  CE1 . PHE B 1 291 ? -0.829  7.325   -17.466 1.00 32.93  ? 291 PHE B CE1 1 
ATOM   4794 C  CE2 . PHE B 1 291 ? 1.169   6.480   -16.473 1.00 30.08  ? 291 PHE B CE2 1 
ATOM   4795 C  CZ  . PHE B 1 291 ? 0.202   6.407   -17.447 1.00 31.26  ? 291 PHE B CZ  1 
ATOM   4796 N  N   . THR B 1 292 ? 0.147   10.195  -11.148 1.00 24.94  ? 292 THR B N   1 
ATOM   4797 C  CA  . THR B 1 292 ? 0.406   11.318  -10.218 1.00 26.57  ? 292 THR B CA  1 
ATOM   4798 C  C   . THR B 1 292 ? 1.569   12.149  -10.742 1.00 26.34  ? 292 THR B C   1 
ATOM   4799 O  O   . THR B 1 292 ? 2.291   11.728  -11.653 1.00 26.25  ? 292 THR B O   1 
ATOM   4800 C  CB  . THR B 1 292 ? 0.686   10.812  -8.808  1.00 25.17  ? 292 THR B CB  1 
ATOM   4801 O  OG1 . THR B 1 292 ? 1.995   10.242  -8.822  1.00 24.82  ? 292 THR B OG1 1 
ATOM   4802 C  CG2 . THR B 1 292 ? -0.373  9.842   -8.347  1.00 23.91  ? 292 THR B CG2 1 
ATOM   4803 N  N   . PRO B 1 293 ? 1.746   13.377  -10.207 1.00 28.24  ? 293 PRO B N   1 
ATOM   4804 C  CA  . PRO B 1 293 ? 2.930   14.182  -10.499 1.00 28.70  ? 293 PRO B CA  1 
ATOM   4805 C  C   . PRO B 1 293 ? 4.220   13.404  -10.249 1.00 27.85  ? 293 PRO B C   1 
ATOM   4806 O  O   . PRO B 1 293 ? 5.066   13.428  -11.101 1.00 29.51  ? 293 PRO B O   1 
ATOM   4807 C  CB  . PRO B 1 293 ? 2.781   15.385  -9.562  1.00 26.80  ? 293 PRO B CB  1 
ATOM   4808 C  CG  . PRO B 1 293 ? 1.291   15.534  -9.438  1.00 29.87  ? 293 PRO B CG  1 
ATOM   4809 C  CD  . PRO B 1 293 ? 0.766   14.112  -9.393  1.00 30.69  ? 293 PRO B CD  1 
ATOM   4810 N  N   . PHE B 1 294 ? 4.305   12.699  -9.123  1.00 31.92  ? 294 PHE B N   1 
ATOM   4811 C  CA  . PHE B 1 294 ? 5.486   11.873  -8.774  1.00 36.37  ? 294 PHE B CA  1 
ATOM   4812 C  C   . PHE B 1 294 ? 5.686   10.819  -9.868  1.00 33.41  ? 294 PHE B C   1 
ATOM   4813 O  O   . PHE B 1 294 ? 6.849   10.619  -10.269 1.00 32.41  ? 294 PHE B O   1 
ATOM   4814 C  CB  . PHE B 1 294 ? 5.369   11.202  -7.405  1.00 41.87  ? 294 PHE B CB  1 
ATOM   4815 C  CG  . PHE B 1 294 ? 6.600   10.397  -7.054  1.00 54.36  ? 294 PHE B CG  1 
ATOM   4816 C  CD1 . PHE B 1 294 ? 7.711   11.019  -6.501  1.00 56.92  ? 294 PHE B CD1 1 
ATOM   4817 C  CD2 . PHE B 1 294 ? 6.684   9.031   -7.344  1.00 62.40  ? 294 PHE B CD2 1 
ATOM   4818 C  CE1 . PHE B 1 294 ? 8.859   10.293  -6.211  1.00 60.14  ? 294 PHE B CE1 1 
ATOM   4819 C  CE2 . PHE B 1 294 ? 7.832   8.303   -7.048  1.00 60.97  ? 294 PHE B CE2 1 
ATOM   4820 C  CZ  . PHE B 1 294 ? 8.920   8.940   -6.484  1.00 60.30  ? 294 PHE B CZ  1 
ATOM   4821 N  N   . ASP B 1 295 ? 4.602   10.182  -10.333 1.00 28.24  ? 295 ASP B N   1 
ATOM   4822 C  CA  . ASP B 1 295 ? 4.689   9.092   -11.350 1.00 28.02  ? 295 ASP B CA  1 
ATOM   4823 C  C   . ASP B 1 295 ? 5.343   9.676   -12.598 1.00 29.45  ? 295 ASP B C   1 
ATOM   4824 O  O   . ASP B 1 295 ? 6.206   9.000   -13.205 1.00 35.04  ? 295 ASP B O   1 
ATOM   4825 C  CB  . ASP B 1 295 ? 3.333   8.472   -11.688 1.00 25.88  ? 295 ASP B CB  1 
ATOM   4826 C  CG  . ASP B 1 295 ? 2.698   7.706   -10.543 1.00 22.96  ? 295 ASP B CG  1 
ATOM   4827 O  OD1 . ASP B 1 295 ? 3.398   7.458   -9.547  1.00 27.44  ? 295 ASP B OD1 1 
ATOM   4828 O  OD2 . ASP B 1 295 ? 1.511   7.403   -10.640 1.00 21.24  ? 295 ASP B OD2 1 
ATOM   4829 N  N   . VAL B 1 296 ? 4.944   10.882  -12.979 1.00 29.35  ? 296 VAL B N   1 
ATOM   4830 C  CA  . VAL B 1 296 ? 5.429   11.499  -14.241 1.00 31.32  ? 296 VAL B CA  1 
ATOM   4831 C  C   . VAL B 1 296 ? 6.911   11.853  -14.065 1.00 34.19  ? 296 VAL B C   1 
ATOM   4832 O  O   . VAL B 1 296 ? 7.724   11.551  -14.965 1.00 34.75  ? 296 VAL B O   1 
ATOM   4833 C  CB  . VAL B 1 296 ? 4.578   12.710  -14.649 1.00 29.50  ? 296 VAL B CB  1 
ATOM   4834 C  CG1 . VAL B 1 296 ? 5.235   13.457  -15.801 1.00 29.04  ? 296 VAL B CG1 1 
ATOM   4835 C  CG2 . VAL B 1 296 ? 3.162   12.274  -15.004 1.00 28.76  ? 296 VAL B CG2 1 
ATOM   4836 N  N   . VAL B 1 297 ? 7.262   12.439  -12.930 1.00 37.56  ? 297 VAL B N   1 
ATOM   4837 C  CA  . VAL B 1 297 ? 8.660   12.869  -12.660 1.00 39.14  ? 297 VAL B CA  1 
ATOM   4838 C  C   . VAL B 1 297 ? 9.543   11.620  -12.622 1.00 39.70  ? 297 VAL B C   1 
ATOM   4839 O  O   . VAL B 1 297 ? 10.596  11.638  -13.279 1.00 45.82  ? 297 VAL B O   1 
ATOM   4840 C  CB  . VAL B 1 297 ? 8.744   13.717  -11.375 1.00 40.61  ? 297 VAL B CB  1 
ATOM   4841 C  CG1 . VAL B 1 297 ? 10.177  13.886  -10.880 1.00 42.51  ? 297 VAL B CG1 1 
ATOM   4842 C  CG2 . VAL B 1 297 ? 8.085   15.074  -11.577 1.00 40.27  ? 297 VAL B CG2 1 
ATOM   4843 N  N   . ARG B 1 298 ? 9.143   10.587  -11.870 1.00 42.78  ? 298 ARG B N   1 
ATOM   4844 C  CA  . ARG B 1 298 ? 9.922   9.326   -11.690 1.00 43.19  ? 298 ARG B CA  1 
ATOM   4845 C  C   . ARG B 1 298 ? 10.148  8.706   -13.073 1.00 42.46  ? 298 ARG B C   1 
ATOM   4846 O  O   . ARG B 1 298 ? 11.293  8.308   -13.362 1.00 42.05  ? 298 ARG B O   1 
ATOM   4847 C  CB  . ARG B 1 298 ? 9.228   8.431   -10.650 1.00 50.22  ? 298 ARG B CB  1 
ATOM   4848 C  CG  . ARG B 1 298 ? 9.292   6.919   -10.850 1.00 57.43  ? 298 ARG B CG  1 
ATOM   4849 C  CD  . ARG B 1 298 ? 7.894   6.285   -10.712 1.00 62.80  ? 298 ARG B CD  1 
ATOM   4850 N  NE  . ARG B 1 298 ? 7.844   4.825   -10.872 1.00 62.22  ? 298 ARG B NE  1 
ATOM   4851 C  CZ  . ARG B 1 298 ? 6.789   4.106   -11.255 1.00 42.89  ? 298 ARG B CZ  1 
ATOM   4852 N  NH1 . ARG B 1 298 ? 5.639   4.675   -11.525 1.00 45.44  ? 298 ARG B NH1 1 
ATOM   4853 N  NH2 . ARG B 1 298 ? 6.894   2.796   -11.332 1.00 48.50  ? 298 ARG B NH2 1 
ATOM   4854 N  N   . GLN B 1 299 ? 9.107   8.645   -13.904 1.00 38.07  ? 299 GLN B N   1 
ATOM   4855 C  CA  . GLN B 1 299 ? 9.163   7.903   -15.189 1.00 39.34  ? 299 GLN B CA  1 
ATOM   4856 C  C   . GLN B 1 299 ? 9.979   8.703   -16.205 1.00 42.68  ? 299 GLN B C   1 
ATOM   4857 O  O   . GLN B 1 299 ? 10.688  8.061   -16.985 1.00 46.69  ? 299 GLN B O   1 
ATOM   4858 C  CB  . GLN B 1 299 ? 7.778   7.579   -15.754 1.00 30.75  ? 299 GLN B CB  1 
ATOM   4859 C  CG  . GLN B 1 299 ? 7.863   6.953   -17.132 1.00 29.53  ? 299 GLN B CG  1 
ATOM   4860 C  CD  . GLN B 1 299 ? 6.656   6.163   -17.572 1.00 26.86  ? 299 GLN B CD  1 
ATOM   4861 O  OE1 . GLN B 1 299 ? 6.571   5.785   -18.738 1.00 27.60  ? 299 GLN B OE1 1 
ATOM   4862 N  NE2 . GLN B 1 299 ? 5.703   5.950   -16.682 1.00 22.12  ? 299 GLN B NE2 1 
ATOM   4863 N  N   . CYS B 1 300 ? 9.845   10.031  -16.216 1.00 43.57  ? 300 CYS B N   1 
ATOM   4864 C  CA  . CYS B 1 300 ? 10.505  10.942  -17.192 1.00 46.86  ? 300 CYS B CA  1 
ATOM   4865 C  C   . CYS B 1 300 ? 11.883  11.399  -16.662 1.00 55.36  ? 300 CYS B C   1 
ATOM   4866 O  O   . CYS B 1 300 ? 12.417  12.340  -17.255 1.00 56.19  ? 300 CYS B O   1 
ATOM   4867 C  CB  . CYS B 1 300 ? 9.613   12.139  -17.503 1.00 41.85  ? 300 CYS B CB  1 
ATOM   4868 S  SG  . CYS B 1 300 ? 8.064   11.683  -18.312 1.00 50.74  ? 300 CYS B SG  1 
ATOM   4869 N  N   . SER B 1 301 ? 12.426  10.760  -15.596 1.00 64.38  ? 301 SER B N   1 
ATOM   4870 C  CA  . SER B 1 301 ? 13.765  11.011  -14.969 1.00 61.08  ? 301 SER B CA  1 
ATOM   4871 C  C   . SER B 1 301 ? 14.488  9.723   -14.501 1.00 63.97  ? 301 SER B C   1 
ATOM   4872 O  O   . SER B 1 301 ? 15.580  9.857   -13.920 1.00 63.96  ? 301 SER B O   1 
ATOM   4873 C  CB  . SER B 1 301 ? 13.649  11.982  -13.822 1.00 62.99  ? 301 SER B CB  1 
ATOM   4874 O  OG  . SER B 1 301 ? 13.203  13.243  -14.297 1.00 66.15  ? 301 SER B OG  1 
ATOM   4875 N  N   . GLY B 1 302 ? 13.916  8.526   -14.713 1.00 61.51  ? 302 GLY B N   1 
ATOM   4876 C  CA  . GLY B 1 302 ? 14.590  7.206   -14.611 1.00 56.65  ? 302 GLY B CA  1 
ATOM   4877 C  C   . GLY B 1 302 ? 14.883  6.737   -13.185 1.00 53.29  ? 302 GLY B C   1 
ATOM   4878 O  O   . GLY B 1 302 ? 15.866  5.958   -13.022 1.00 46.28  ? 302 GLY B O   1 
ATOM   4879 N  N   . VAL B 1 303 ? 14.070  7.135   -12.189 1.00 47.32  ? 303 VAL B N   1 
ATOM   4880 C  CA  . VAL B 1 303 ? 14.277  6.754   -10.752 1.00 46.88  ? 303 VAL B CA  1 
ATOM   4881 C  C   . VAL B 1 303 ? 14.236  5.214   -10.653 1.00 47.50  ? 303 VAL B C   1 
ATOM   4882 O  O   . VAL B 1 303 ? 13.433  4.567   -11.356 1.00 45.34  ? 303 VAL B O   1 
ATOM   4883 C  CB  . VAL B 1 303 ? 13.275  7.433   -9.787  1.00 46.67  ? 303 VAL B CB  1 
ATOM   4884 C  CG1 . VAL B 1 303 ? 13.446  6.950   -8.346  1.00 44.98  ? 303 VAL B CG1 1 
ATOM   4885 C  CG2 . VAL B 1 303 ? 13.350  8.964   -9.858  1.00 49.27  ? 303 VAL B CG2 1 
ATOM   4886 N  N   . THR B 1 304 ? 15.105  4.658   -9.806  1.00 47.90  ? 304 THR B N   1 
ATOM   4887 C  CA  . THR B 1 304 ? 15.492  3.222   -9.750  1.00 48.48  ? 304 THR B CA  1 
ATOM   4888 C  C   . THR B 1 304 ? 15.318  2.746   -8.295  1.00 48.20  ? 304 THR B C   1 
ATOM   4889 O  O   . THR B 1 304 ? 15.364  3.614   -7.399  1.00 50.81  ? 304 THR B O   1 
ATOM   4890 C  CB  . THR B 1 304 ? 16.907  3.107   -10.354 1.00 47.08  ? 304 THR B CB  1 
ATOM   4891 O  OG1 . THR B 1 304 ? 16.942  2.058   -11.321 1.00 46.76  ? 304 THR B OG1 1 
ATOM   4892 C  CG2 . THR B 1 304 ? 17.989  2.932   -9.305  1.00 48.74  ? 304 THR B CG2 1 
ATOM   4893 N  N   . PHE B 1 305 ? 15.100  1.442   -8.064  1.00 51.32  ? 305 PHE B N   1 
ATOM   4894 C  CA  . PHE B 1 305 ? 14.959  0.808   -6.712  1.00 53.14  ? 305 PHE B CA  1 
ATOM   4895 C  C   . PHE B 1 305 ? 15.750  -0.512  -6.705  1.00 52.34  ? 305 PHE B C   1 
ATOM   4896 O  O   . PHE B 1 305 ? 16.963  -0.454  -7.007  1.00 54.64  ? 305 PHE B O   1 
ATOM   4897 C  CB  . PHE B 1 305 ? 13.484  0.589   -6.322  1.00 53.45  ? 305 PHE B CB  1 
ATOM   4898 C  CG  . PHE B 1 305 ? 12.527  1.582   -6.945  1.00 49.33  ? 305 PHE B CG  1 
ATOM   4899 C  CD1 . PHE B 1 305 ? 12.048  1.367   -8.231  1.00 46.82  ? 305 PHE B CD1 1 
ATOM   4900 C  CD2 . PHE B 1 305 ? 12.165  2.757   -6.292  1.00 48.59  ? 305 PHE B CD2 1 
ATOM   4901 C  CE1 . PHE B 1 305 ? 11.244  2.315   -8.859  1.00 48.70  ? 305 PHE B CE1 1 
ATOM   4902 C  CE2 . PHE B 1 305 ? 11.321  3.680   -6.901  1.00 49.34  ? 305 PHE B CE2 1 
ATOM   4903 C  CZ  . PHE B 1 305 ? 10.877  3.470   -8.196  1.00 48.97  ? 305 PHE B CZ  1 
HETATM 4904 CL CL  . CL  C 2 .   ? 5.499   -15.093 -31.293 1.00 28.67  ? 401 CL  A CL  1 
HETATM 4905 C  C4  C RD4 D 3 .   ? -9.610  -26.625 -44.972 0.26 34.96  ? 402 RD4 A C4  1 
HETATM 4906 C  C4  D RD4 D 3 .   ? -9.610  -26.625 -44.972 0.26 34.96  ? 402 RD4 A C4  1 
HETATM 4907 C  C5  C RD4 D 3 .   ? -8.623  -25.726 -45.413 0.26 35.95  ? 402 RD4 A C5  1 
HETATM 4908 C  C5  D RD4 D 3 .   ? -8.623  -25.726 -45.413 0.26 35.95  ? 402 RD4 A C5  1 
HETATM 4909 C  C6  C RD4 D 3 .   ? -8.119  -24.756 -44.495 0.26 35.98  ? 402 RD4 A C6  1 
HETATM 4910 C  C6  D RD4 D 3 .   ? -8.119  -24.756 -44.495 0.26 35.98  ? 402 RD4 A C6  1 
HETATM 4911 N  N1  C RD4 D 3 .   ? -9.201  -23.293 -41.238 0.26 35.64  ? 402 RD4 A N1  1 
HETATM 4912 N  N1  D RD4 D 3 .   ? -9.201  -23.293 -41.238 0.26 35.64  ? 402 RD4 A N1  1 
HETATM 4913 C  C7  C RD4 D 3 .   ? -6.903  -25.209 -47.087 0.26 35.96  ? 402 RD4 A C7  1 
HETATM 4914 C  C7  D RD4 D 3 .   ? -6.903  -25.209 -47.087 0.26 35.96  ? 402 RD4 A C7  1 
HETATM 4915 C  C8  C RD4 D 3 .   ? -6.394  -25.720 -48.443 0.26 36.11  ? 402 RD4 A C8  1 
HETATM 4916 C  C8  D RD4 D 3 .   ? -6.394  -25.720 -48.443 0.26 36.11  ? 402 RD4 A C8  1 
HETATM 4917 C  C   C RD4 D 3 .   ? -8.225  -23.819 -42.047 0.26 35.68  ? 402 RD4 A C   1 
HETATM 4918 C  C   D RD4 D 3 .   ? -8.225  -23.819 -42.047 0.26 35.68  ? 402 RD4 A C   1 
HETATM 4919 N  N   C RD4 D 3 .   ? -6.948  -23.502 -41.796 0.26 35.90  1 402 RD4 A N   1 
HETATM 4920 N  N   D RD4 D 3 .   ? -6.948  -23.502 -41.796 0.26 35.90  1 402 RD4 A N   1 
HETATM 4921 C  C1  C RD4 D 3 .   ? -8.603  -24.718 -43.182 0.26 35.44  ? 402 RD4 A C1  1 
HETATM 4922 C  C1  D RD4 D 3 .   ? -8.603  -24.718 -43.182 0.26 35.44  ? 402 RD4 A C1  1 
HETATM 4923 O  O   C RD4 D 3 .   ? -8.186  -25.783 -46.722 0.26 36.84  ? 402 RD4 A O   1 
HETATM 4924 O  O   D RD4 D 3 .   ? -8.186  -25.783 -46.722 0.26 36.84  ? 402 RD4 A O   1 
HETATM 4925 C  C3  C RD4 D 3 .   ? -10.089 -26.589 -43.662 0.26 34.54  ? 402 RD4 A C3  1 
HETATM 4926 C  C3  D RD4 D 3 .   ? -10.089 -26.589 -43.662 0.26 34.54  ? 402 RD4 A C3  1 
HETATM 4927 C  C2  C RD4 D 3 .   ? -9.598  -25.652 -42.759 0.26 35.46  ? 402 RD4 A C2  1 
HETATM 4928 C  C2  D RD4 D 3 .   ? -9.598  -25.652 -42.759 0.26 35.46  ? 402 RD4 A C2  1 
HETATM 4929 NA NA  . NA  E 4 .   ? -2.157  27.948  -21.774 1.00 41.33  ? 401 NA  B NA  1 
HETATM 4930 CL CL  . CL  F 2 .   ? -19.208 -8.761  13.241  1.00 42.56  ? 402 CL  B CL  1 
HETATM 4931 O  O   . HOH G 5 .   ? 12.228  3.791   -18.322 1.00 31.65  ? 501 HOH A O   1 
HETATM 4932 O  O   . HOH G 5 .   ? -11.856 4.888   -37.687 1.00 26.31  ? 502 HOH A O   1 
HETATM 4933 O  O   . HOH G 5 .   ? -1.074  -15.107 -40.093 1.00 21.99  ? 503 HOH A O   1 
HETATM 4934 O  O   . HOH G 5 .   ? -18.104 -10.203 -51.283 1.00 24.09  ? 504 HOH A O   1 
HETATM 4935 O  O   . HOH G 5 .   ? 4.657   -1.759  -28.378 1.00 19.91  ? 505 HOH A O   1 
HETATM 4936 O  O   . HOH G 5 .   ? -8.428  1.978   -34.843 1.00 30.33  ? 506 HOH A O   1 
HETATM 4937 O  O   . HOH G 5 .   ? 29.601  0.607   -42.412 1.00 26.88  ? 507 HOH A O   1 
HETATM 4938 O  O   . HOH G 5 .   ? -17.727 -4.868  -46.756 1.00 33.98  ? 508 HOH A O   1 
HETATM 4939 O  O   . HOH G 5 .   ? 24.692  -3.199  -30.159 1.00 26.00  ? 509 HOH A O   1 
HETATM 4940 O  O   . HOH G 5 .   ? 16.035  -14.106 -10.529 1.00 28.12  ? 510 HOH A O   1 
HETATM 4941 O  O   . HOH G 5 .   ? 2.670   -10.837 -22.636 1.00 23.47  ? 511 HOH A O   1 
HETATM 4942 O  O   . HOH G 5 .   ? 6.442   2.377   -34.510 1.00 35.67  ? 512 HOH A O   1 
HETATM 4943 O  O   . HOH G 5 .   ? 18.213  -6.005  -38.817 1.00 37.34  ? 513 HOH A O   1 
HETATM 4944 O  O   . HOH G 5 .   ? -15.595 0.754   -42.151 1.00 31.27  ? 514 HOH A O   1 
HETATM 4945 O  O   . HOH G 5 .   ? 1.013   -2.806  -24.200 1.00 35.43  ? 515 HOH A O   1 
HETATM 4946 O  O   . HOH G 5 .   ? 8.861   -13.159 -11.478 1.00 22.69  ? 516 HOH A O   1 
HETATM 4947 O  O   . HOH G 5 .   ? 0.123   -14.217 -27.336 1.00 29.56  ? 517 HOH A O   1 
HETATM 4948 O  O   . HOH G 5 .   ? 29.866  -1.541  -13.981 1.00 30.70  ? 518 HOH A O   1 
HETATM 4949 O  O   . HOH G 5 .   ? 21.308  -5.486  -37.723 1.00 28.66  ? 519 HOH A O   1 
HETATM 4950 O  O   . HOH G 5 .   ? 6.210   -17.694 -21.759 1.00 32.79  ? 520 HOH A O   1 
HETATM 4951 O  O   . HOH G 5 .   ? -15.726 -11.614 -50.681 1.00 24.22  ? 521 HOH A O   1 
HETATM 4952 O  O   . HOH G 5 .   ? -14.791 -15.263 -46.054 1.00 33.07  ? 522 HOH A O   1 
HETATM 4953 O  O   . HOH G 5 .   ? 13.563  -3.570  -33.167 1.00 23.07  ? 523 HOH A O   1 
HETATM 4954 O  O   . HOH G 5 .   ? -5.760  -5.851  -28.182 1.00 21.59  ? 524 HOH A O   1 
HETATM 4955 O  O   . HOH G 5 .   ? -9.270  3.416   -32.460 1.00 29.08  ? 525 HOH A O   1 
HETATM 4956 O  O   . HOH G 5 .   ? -18.858 -9.312  -47.185 1.00 23.95  ? 526 HOH A O   1 
HETATM 4957 O  O   . HOH G 5 .   ? 15.604  -5.785  -17.803 1.00 24.22  ? 527 HOH A O   1 
HETATM 4958 O  O   . HOH G 5 .   ? -0.246  -15.236 -16.419 1.00 45.24  ? 528 HOH A O   1 
HETATM 4959 O  O   . HOH G 5 .   ? 3.689   -19.757 -23.831 1.00 33.23  ? 529 HOH A O   1 
HETATM 4960 O  O   . HOH G 5 .   ? 23.772  -17.997 -19.942 1.00 40.97  ? 530 HOH A O   1 
HETATM 4961 O  O   . HOH G 5 .   ? 19.326  5.199   -28.855 1.00 29.78  ? 531 HOH A O   1 
HETATM 4962 O  O   . HOH G 5 .   ? -20.268 -4.289  -40.608 1.00 27.74  ? 532 HOH A O   1 
HETATM 4963 O  O   . HOH G 5 .   ? -1.132  -11.568 -31.992 1.00 27.96  ? 533 HOH A O   1 
HETATM 4964 O  O   . HOH G 5 .   ? 26.566  -2.151  -37.015 1.00 23.81  ? 534 HOH A O   1 
HETATM 4965 O  O   . HOH G 5 .   ? 15.493  -14.278 -27.676 1.00 21.50  ? 535 HOH A O   1 
HETATM 4966 O  O   . HOH G 5 .   ? 11.630  6.429   -36.677 1.00 28.56  ? 536 HOH A O   1 
HETATM 4967 O  O   . HOH G 5 .   ? 22.514  -16.092 -27.153 1.00 30.63  ? 537 HOH A O   1 
HETATM 4968 O  O   . HOH G 5 .   ? 20.860  -8.173  -36.415 1.00 24.48  ? 538 HOH A O   1 
HETATM 4969 O  O   . HOH G 5 .   ? -15.752 5.373   -43.158 1.00 35.05  ? 539 HOH A O   1 
HETATM 4970 O  O   . HOH G 5 .   ? 32.705  -6.808  -37.255 1.00 32.76  ? 540 HOH A O   1 
HETATM 4971 O  O   . HOH G 5 .   ? -1.680  -7.712  -20.416 1.00 24.16  ? 541 HOH A O   1 
HETATM 4972 O  O   . HOH G 5 .   ? -0.580  -7.613  -23.042 1.00 26.92  ? 542 HOH A O   1 
HETATM 4973 O  O   . HOH G 5 .   ? -8.620  -1.599  -22.641 1.00 33.14  ? 543 HOH A O   1 
HETATM 4974 O  O   . HOH G 5 .   ? 23.907  3.635   -21.820 1.00 33.37  ? 544 HOH A O   1 
HETATM 4975 O  O   . HOH G 5 .   ? -16.250 -16.749 -38.798 1.00 28.66  ? 545 HOH A O   1 
HETATM 4976 O  O   . HOH G 5 .   ? 12.916  -18.599 -31.300 1.00 27.96  ? 546 HOH A O   1 
HETATM 4977 O  O   . HOH G 5 .   ? 21.340  3.734   -28.125 1.00 30.19  ? 547 HOH A O   1 
HETATM 4978 O  O   . HOH G 5 .   ? -8.291  -11.390 -47.746 1.00 31.90  ? 548 HOH A O   1 
HETATM 4979 O  O   . HOH G 5 .   ? -13.355 -14.274 -48.125 1.00 31.37  ? 549 HOH A O   1 
HETATM 4980 O  O   . HOH G 5 .   ? -3.725  -9.030  -37.629 1.00 25.20  ? 550 HOH A O   1 
HETATM 4981 O  O   . HOH G 5 .   ? 35.780  0.726   -35.732 1.00 25.61  ? 551 HOH A O   1 
HETATM 4982 O  O   . HOH G 5 .   ? 31.047  -4.499  -37.573 1.00 33.07  ? 552 HOH A O   1 
HETATM 4983 O  O   . HOH G 5 .   ? 23.415  -4.291  -37.041 1.00 26.10  ? 553 HOH A O   1 
HETATM 4984 O  O   . HOH G 5 .   ? -8.327  5.954   -25.075 1.00 23.31  ? 554 HOH A O   1 
HETATM 4985 O  O   . HOH G 5 .   ? -19.958 -7.659  -45.473 1.00 34.11  ? 555 HOH A O   1 
HETATM 4986 O  O   . HOH G 5 .   ? -3.206  -18.007 -42.873 1.00 35.29  ? 556 HOH A O   1 
HETATM 4987 O  O   . HOH G 5 .   ? -24.489 -9.386  -43.329 1.00 36.22  ? 557 HOH A O   1 
HETATM 4988 O  O   . HOH G 5 .   ? 21.746  3.160   -22.638 1.00 28.26  ? 558 HOH A O   1 
HETATM 4989 O  O   . HOH G 5 .   ? -2.188  -15.292 -29.386 1.00 28.64  ? 559 HOH A O   1 
HETATM 4990 O  O   . HOH G 5 .   ? 25.022  -2.367  -41.562 1.00 27.24  ? 560 HOH A O   1 
HETATM 4991 O  O   . HOH G 5 .   ? 16.209  -16.319 -29.619 1.00 31.27  ? 561 HOH A O   1 
HETATM 4992 O  O   . HOH G 5 .   ? 24.055  3.309   -30.109 1.00 40.82  ? 562 HOH A O   1 
HETATM 4993 O  O   . HOH G 5 .   ? -1.164  -8.865  -37.274 1.00 29.76  ? 563 HOH A O   1 
HETATM 4994 O  O   . HOH G 5 .   ? -20.952 -10.804 -47.430 1.00 32.43  ? 564 HOH A O   1 
HETATM 4995 O  O   . HOH G 5 .   ? -2.010  -14.105 -32.224 1.00 39.11  ? 565 HOH A O   1 
HETATM 4996 O  O   . HOH G 5 .   ? -14.407 -17.954 -40.675 1.00 33.22  ? 566 HOH A O   1 
HETATM 4997 O  O   . HOH H 5 .   ? 6.499   29.283  -21.773 1.00 32.69  ? 501 HOH B O   1 
HETATM 4998 O  O   . HOH H 5 .   ? -8.547  33.343  -17.906 1.00 45.94  ? 502 HOH B O   1 
HETATM 4999 O  O   . HOH H 5 .   ? -8.064  2.523   -10.413 1.00 24.66  ? 503 HOH B O   1 
HETATM 5000 O  O   . HOH H 5 .   ? 2.694   8.465   -7.017  1.00 29.74  ? 504 HOH B O   1 
HETATM 5001 O  O   . HOH H 5 .   ? -11.965 -0.067  -1.391  1.00 23.20  ? 505 HOH B O   1 
HETATM 5002 O  O   . HOH H 5 .   ? -0.123  -9.593  -3.857  1.00 38.53  ? 506 HOH B O   1 
HETATM 5003 O  O   . HOH H 5 .   ? -20.970 -1.055  -7.952  1.00 39.00  ? 507 HOH B O   1 
HETATM 5004 O  O   . HOH H 5 .   ? -2.732  12.579  -6.989  1.00 31.21  ? 508 HOH B O   1 
HETATM 5005 O  O   . HOH H 5 .   ? -2.959  11.058  -15.018 1.00 24.87  ? 509 HOH B O   1 
HETATM 5006 O  O   . HOH H 5 .   ? -14.322 2.600   5.622   1.00 32.99  ? 510 HOH B O   1 
HETATM 5007 O  O   . HOH H 5 .   ? -3.644  2.784   -13.624 1.00 31.57  ? 511 HOH B O   1 
HETATM 5008 O  O   . HOH H 5 .   ? -19.151 -7.633  7.903   1.00 32.71  ? 512 HOH B O   1 
HETATM 5009 O  O   . HOH H 5 .   ? -1.614  -0.487  5.087   1.00 30.36  ? 513 HOH B O   1 
HETATM 5010 O  O   . HOH H 5 .   ? -12.444 -7.161  13.780  1.00 30.76  ? 514 HOH B O   1 
HETATM 5011 O  O   . HOH H 5 .   ? -12.314 5.390   3.304   1.00 25.99  ? 515 HOH B O   1 
HETATM 5012 O  O   . HOH H 5 .   ? 14.500  10.563  -23.917 1.00 34.34  ? 516 HOH B O   1 
HETATM 5013 O  O   . HOH H 5 .   ? 2.624   4.488   -7.667  1.00 25.57  ? 517 HOH B O   1 
HETATM 5014 O  O   . HOH H 5 .   ? -15.748 9.500   -1.962  1.00 31.21  ? 518 HOH B O   1 
HETATM 5015 O  O   . HOH H 5 .   ? -7.602  7.480   2.626   1.00 29.22  ? 519 HOH B O   1 
HETATM 5016 O  O   . HOH H 5 .   ? 10.902  -5.568  -6.089  1.00 31.81  ? 520 HOH B O   1 
HETATM 5017 O  O   . HOH H 5 .   ? -10.684 -14.740 -3.814  1.00 30.28  ? 521 HOH B O   1 
HETATM 5018 O  O   . HOH H 5 .   ? 5.159   6.358   -13.832 1.00 30.46  ? 522 HOH B O   1 
HETATM 5019 O  O   . HOH H 5 .   ? -12.707 -9.792  5.014   1.00 23.02  ? 523 HOH B O   1 
HETATM 5020 O  O   . HOH H 5 .   ? 0.992   7.269   -4.960  1.00 32.09  ? 524 HOH B O   1 
HETATM 5021 O  O   . HOH H 5 .   ? -15.927 3.062   -9.447  1.00 33.93  ? 525 HOH B O   1 
HETATM 5022 O  O   . HOH H 5 .   ? -10.145 6.963   4.029   1.00 33.93  ? 526 HOH B O   1 
HETATM 5023 O  O   . HOH H 5 .   ? 10.787  -4.055  7.676   1.00 27.94  ? 527 HOH B O   1 
HETATM 5024 O  O   . HOH H 5 .   ? -7.215  17.130  -8.209  1.00 31.09  ? 528 HOH B O   1 
HETATM 5025 O  O   . HOH H 5 .   ? 3.102   4.572   -13.905 1.00 21.68  ? 529 HOH B O   1 
HETATM 5026 O  O   . HOH H 5 .   ? -16.450 -4.228  7.323   1.00 27.97  ? 530 HOH B O   1 
HETATM 5027 O  O   . HOH H 5 .   ? 9.692   -14.937 -4.792  1.00 46.30  ? 531 HOH B O   1 
HETATM 5028 O  O   . HOH H 5 .   ? -20.628 -12.027 19.961  1.00 46.91  ? 532 HOH B O   1 
HETATM 5029 O  O   . HOH H 5 .   ? 3.734   7.003   -25.491 1.00 45.79  ? 533 HOH B O   1 
HETATM 5030 O  O   . HOH H 5 .   ? -1.790  0.917   7.350   1.00 32.91  ? 534 HOH B O   1 
# 
